data_8RHV
# 
_entry.id   8RHV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8RHV         pdb_00008rhv 10.2210/pdb8rhv/pdb 
WWPDB D_1292135044 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8RHV 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'Crystal Structure of Trypanosoma brucei DHFR in complex with the cofactor and inhibitor P25' 8RHT unspecified 
PDB 'Crystal Structure of Trypanosoma brucei PTR1 in complex with the cofactor and inhibitor P25' 8RHU unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              pozzi4@unisi.it 
_pdbx_contact_author.name_first         Cecilia 
_pdbx_contact_author.name_last          Pozzi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2574-3911 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pozzi, C.'   1 0000-0003-2574-3911 
'Mangani, S.' 2 0000-0003-4824-7478 
'Landi, G.'   3 0000-0001-6332-166X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Infect Dis.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2373-8227 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                2755 
_citation.page_last                 2774 
_citation.title                     
;Identification of Innovative Folate Inhibitors Leveraging the Amino Dihydrotriazine Motif from Cycloguanil for Their Potential as Anti- Trypanosoma brucei Agents.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsinfecdis.4c00113 
_citation.pdbx_database_id_PubMed   38953453 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Francesconi, V.'       1  ?                   
primary 'Rizzo, M.'             2  ?                   
primary 'Pozzi, C.'             3  0000-0003-2574-3911 
primary 'Tagliazucchi, L.'      4  0000-0002-7244-7106 
primary 'Konchie Simo, C.U.'    5  ?                   
primary 'Saporito, G.'          6  ?                   
primary 'Landi, G.'             7  ?                   
primary 'Mangani, S.'           8  0000-0003-4824-7478 
primary 'Carbone, A.'           9  0000-0002-6767-2376 
primary 'Schenone, S.'          10 ?                   
primary 'Santarem, N.'          11 ?                   
primary 'Tavares, J.'           12 ?                   
primary 'Cordeiro-da-Silva, A.' 13 0000-0003-2392-6087 
primary 'Costi, M.P.'           14 0000-0002-0443-5402 
primary 'Tonelli, M.'           15 0000-0003-1518-2890 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Pteridine reductase'                                                      30800.982 4   ? ? ? ? 
2 non-polymer syn 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'                745.421   4   ? ? ? ? 
3 non-polymer syn 'ACETATE ION'                                                              59.044    3   ? ? ? ? 
4 non-polymer syn '7-methoxy-4,4-dimethyl-10~{H}-[1,3,5]triazino[1,2-a]benzimidazol-2-amine' 245.280   3   ? ? ? ? 
5 water       nat water                                                                      18.015    564 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGSSHHHHHHSSGLVPRGSHMMEAPAAVVTGAAKRIGRAIAVKLHQTGYRVVIHYHNSAEAAVSLADELNKERSNTAVVC
QADLTNSNVLPASCEEIINSCFRAFGRCDVLVNNASAFYPTPLVQGDHEDNSNGKTVETQVAELIGTNAIAPFLLTMSFA
QRQKGTNPNCTSSNLSIVNLCDAMVDQPCMAFSLYNMGKHALVGLTQSAALELAPYGIRVNGVAPGVSLLPVAMGEEEKD
KWRRKVPLGRREASAEQIADAVIFLVSGSAQYITGSIIKVDGGLSLVHA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMMEAPAAVVTGAAKRIGRAIAVKLHQTGYRVVIHYHNSAEAAVSLADELNKERSNTAVVC
QADLTNSNVLPASCEEIINSCFRAFGRCDVLVNNASAFYPTPLVQGDHEDNSNGKTVETQVAELIGTNAIAPFLLTMSFA
QRQKGTNPNCTSSNLSIVNLCDAMVDQPCMAFSLYNMGKHALVGLTQSAALELAPYGIRVNGVAPGVSLLPVAMGEEEKD
KWRRKVPLGRREASAEQIADAVIFLVSGSAQYITGSIIKVDGGLSLVHA
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'                NDP   
3 'ACETATE ION'                                                              ACT   
4 '7-methoxy-4,4-dimethyl-10~{H}-[1,3,5]triazino[1,2-a]benzimidazol-2-amine' A1H0U 
5 water                                                                      HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  MET n 
1 23  GLU n 
1 24  ALA n 
1 25  PRO n 
1 26  ALA n 
1 27  ALA n 
1 28  VAL n 
1 29  VAL n 
1 30  THR n 
1 31  GLY n 
1 32  ALA n 
1 33  ALA n 
1 34  LYS n 
1 35  ARG n 
1 36  ILE n 
1 37  GLY n 
1 38  ARG n 
1 39  ALA n 
1 40  ILE n 
1 41  ALA n 
1 42  VAL n 
1 43  LYS n 
1 44  LEU n 
1 45  HIS n 
1 46  GLN n 
1 47  THR n 
1 48  GLY n 
1 49  TYR n 
1 50  ARG n 
1 51  VAL n 
1 52  VAL n 
1 53  ILE n 
1 54  HIS n 
1 55  TYR n 
1 56  HIS n 
1 57  ASN n 
1 58  SER n 
1 59  ALA n 
1 60  GLU n 
1 61  ALA n 
1 62  ALA n 
1 63  VAL n 
1 64  SER n 
1 65  LEU n 
1 66  ALA n 
1 67  ASP n 
1 68  GLU n 
1 69  LEU n 
1 70  ASN n 
1 71  LYS n 
1 72  GLU n 
1 73  ARG n 
1 74  SER n 
1 75  ASN n 
1 76  THR n 
1 77  ALA n 
1 78  VAL n 
1 79  VAL n 
1 80  CYS n 
1 81  GLN n 
1 82  ALA n 
1 83  ASP n 
1 84  LEU n 
1 85  THR n 
1 86  ASN n 
1 87  SER n 
1 88  ASN n 
1 89  VAL n 
1 90  LEU n 
1 91  PRO n 
1 92  ALA n 
1 93  SER n 
1 94  CYS n 
1 95  GLU n 
1 96  GLU n 
1 97  ILE n 
1 98  ILE n 
1 99  ASN n 
1 100 SER n 
1 101 CYS n 
1 102 PHE n 
1 103 ARG n 
1 104 ALA n 
1 105 PHE n 
1 106 GLY n 
1 107 ARG n 
1 108 CYS n 
1 109 ASP n 
1 110 VAL n 
1 111 LEU n 
1 112 VAL n 
1 113 ASN n 
1 114 ASN n 
1 115 ALA n 
1 116 SER n 
1 117 ALA n 
1 118 PHE n 
1 119 TYR n 
1 120 PRO n 
1 121 THR n 
1 122 PRO n 
1 123 LEU n 
1 124 VAL n 
1 125 GLN n 
1 126 GLY n 
1 127 ASP n 
1 128 HIS n 
1 129 GLU n 
1 130 ASP n 
1 131 ASN n 
1 132 SER n 
1 133 ASN n 
1 134 GLY n 
1 135 LYS n 
1 136 THR n 
1 137 VAL n 
1 138 GLU n 
1 139 THR n 
1 140 GLN n 
1 141 VAL n 
1 142 ALA n 
1 143 GLU n 
1 144 LEU n 
1 145 ILE n 
1 146 GLY n 
1 147 THR n 
1 148 ASN n 
1 149 ALA n 
1 150 ILE n 
1 151 ALA n 
1 152 PRO n 
1 153 PHE n 
1 154 LEU n 
1 155 LEU n 
1 156 THR n 
1 157 MET n 
1 158 SER n 
1 159 PHE n 
1 160 ALA n 
1 161 GLN n 
1 162 ARG n 
1 163 GLN n 
1 164 LYS n 
1 165 GLY n 
1 166 THR n 
1 167 ASN n 
1 168 PRO n 
1 169 ASN n 
1 170 CYS n 
1 171 THR n 
1 172 SER n 
1 173 SER n 
1 174 ASN n 
1 175 LEU n 
1 176 SER n 
1 177 ILE n 
1 178 VAL n 
1 179 ASN n 
1 180 LEU n 
1 181 CYS n 
1 182 ASP n 
1 183 ALA n 
1 184 MET n 
1 185 VAL n 
1 186 ASP n 
1 187 GLN n 
1 188 PRO n 
1 189 CYS n 
1 190 MET n 
1 191 ALA n 
1 192 PHE n 
1 193 SER n 
1 194 LEU n 
1 195 TYR n 
1 196 ASN n 
1 197 MET n 
1 198 GLY n 
1 199 LYS n 
1 200 HIS n 
1 201 ALA n 
1 202 LEU n 
1 203 VAL n 
1 204 GLY n 
1 205 LEU n 
1 206 THR n 
1 207 GLN n 
1 208 SER n 
1 209 ALA n 
1 210 ALA n 
1 211 LEU n 
1 212 GLU n 
1 213 LEU n 
1 214 ALA n 
1 215 PRO n 
1 216 TYR n 
1 217 GLY n 
1 218 ILE n 
1 219 ARG n 
1 220 VAL n 
1 221 ASN n 
1 222 GLY n 
1 223 VAL n 
1 224 ALA n 
1 225 PRO n 
1 226 GLY n 
1 227 VAL n 
1 228 SER n 
1 229 LEU n 
1 230 LEU n 
1 231 PRO n 
1 232 VAL n 
1 233 ALA n 
1 234 MET n 
1 235 GLY n 
1 236 GLU n 
1 237 GLU n 
1 238 GLU n 
1 239 LYS n 
1 240 ASP n 
1 241 LYS n 
1 242 TRP n 
1 243 ARG n 
1 244 ARG n 
1 245 LYS n 
1 246 VAL n 
1 247 PRO n 
1 248 LEU n 
1 249 GLY n 
1 250 ARG n 
1 251 ARG n 
1 252 GLU n 
1 253 ALA n 
1 254 SER n 
1 255 ALA n 
1 256 GLU n 
1 257 GLN n 
1 258 ILE n 
1 259 ALA n 
1 260 ASP n 
1 261 ALA n 
1 262 VAL n 
1 263 ILE n 
1 264 PHE n 
1 265 LEU n 
1 266 VAL n 
1 267 SER n 
1 268 GLY n 
1 269 SER n 
1 270 ALA n 
1 271 GLN n 
1 272 TYR n 
1 273 ILE n 
1 274 THR n 
1 275 GLY n 
1 276 SER n 
1 277 ILE n 
1 278 ILE n 
1 279 LYS n 
1 280 VAL n 
1 281 ASP n 
1 282 GLY n 
1 283 GLY n 
1 284 LEU n 
1 285 SER n 
1 286 LEU n 
1 287 VAL n 
1 288 HIS n 
1 289 ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   289 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PTR1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Trypanosoma brucei brucei' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5702 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   pET15b 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       plasmid 
_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 
A1H0U non-polymer         . '7-methoxy-4,4-dimethyl-10~{H}-[1,3,5]triazino[1,2-a]benzimidazol-2-amine' ? 'C12 H15 N5 O'      
245.280 
ACT   non-polymer         . 'ACETATE ION'                                                              ? 'C2 H3 O2 -1'       
59.044  
ALA   'L-peptide linking' y ALANINE                                                                    ? 'C3 H7 N O2'        
89.093  
ARG   'L-peptide linking' y ARGININE                                                                   ? 'C6 H15 N4 O2 1'    
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                 ? 'C4 H8 N2 O3'       
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                            ? 'C4 H7 N O4'        
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                   ? 'C3 H7 N O2 S'      
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                  ? 'C5 H10 N2 O3'      
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                            ? 'C5 H9 N O4'        
147.129 
GLY   'peptide linking'   y GLYCINE                                                                    ? 'C2 H5 N O2'        
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                  ? 'C6 H10 N3 O2 1'    
156.162 
HOH   non-polymer         . WATER                                                                      ? 'H2 O'              
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                 ? 'C6 H13 N O2'       
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                    ? 'C6 H13 N O2'       
131.173 
LYS   'L-peptide linking' y LYSINE                                                                     ? 'C6 H15 N2 O2 1'    
147.195 
MET   'L-peptide linking' y METHIONINE                                                                 ? 'C5 H11 N O2 S'     
149.211 
NDP   non-polymer         . 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'                ? 'C21 H30 N7 O17 P3' 
745.421 
PHE   'L-peptide linking' y PHENYLALANINE                                                              ? 'C9 H11 N O2'       
165.189 
PRO   'L-peptide linking' y PROLINE                                                                    ? 'C5 H9 N O2'        
115.130 
SER   'L-peptide linking' y SERINE                                                                     ? 'C3 H7 N O3'        
105.093 
THR   'L-peptide linking' y THREONINE                                                                  ? 'C4 H9 N O3'        
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                 ? 'C11 H12 N2 O2'     
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                   ? 'C9 H11 N O3'       
181.189 
VAL   'L-peptide linking' y VALINE                                                                     ? 'C5 H11 N O2'       
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -20 ?   ?   ?   A . n 
A 1 2   GLY 2   -19 ?   ?   ?   A . n 
A 1 3   SER 3   -18 ?   ?   ?   A . n 
A 1 4   SER 4   -17 ?   ?   ?   A . n 
A 1 5   HIS 5   -16 ?   ?   ?   A . n 
A 1 6   HIS 6   -15 ?   ?   ?   A . n 
A 1 7   HIS 7   -14 ?   ?   ?   A . n 
A 1 8   HIS 8   -13 ?   ?   ?   A . n 
A 1 9   HIS 9   -12 ?   ?   ?   A . n 
A 1 10  HIS 10  -11 ?   ?   ?   A . n 
A 1 11  SER 11  -10 ?   ?   ?   A . n 
A 1 12  SER 12  -9  ?   ?   ?   A . n 
A 1 13  GLY 13  -8  ?   ?   ?   A . n 
A 1 14  LEU 14  -7  ?   ?   ?   A . n 
A 1 15  VAL 15  -6  ?   ?   ?   A . n 
A 1 16  PRO 16  -5  ?   ?   ?   A . n 
A 1 17  ARG 17  -4  ?   ?   ?   A . n 
A 1 18  GLY 18  -3  ?   ?   ?   A . n 
A 1 19  SER 19  -2  ?   ?   ?   A . n 
A 1 20  HIS 20  -1  ?   ?   ?   A . n 
A 1 21  MET 21  0   ?   ?   ?   A . n 
A 1 22  MET 22  1   ?   ?   ?   A . n 
A 1 23  GLU 23  2   2   GLU GLU A . n 
A 1 24  ALA 24  3   3   ALA ALA A . n 
A 1 25  PRO 25  4   4   PRO PRO A . n 
A 1 26  ALA 26  5   5   ALA ALA A . n 
A 1 27  ALA 27  6   6   ALA ALA A . n 
A 1 28  VAL 28  7   7   VAL VAL A . n 
A 1 29  VAL 29  8   8   VAL VAL A . n 
A 1 30  THR 30  9   9   THR THR A . n 
A 1 31  GLY 31  10  10  GLY GLY A . n 
A 1 32  ALA 32  11  11  ALA ALA A . n 
A 1 33  ALA 33  12  12  ALA ALA A . n 
A 1 34  LYS 34  13  13  LYS LYS A . n 
A 1 35  ARG 35  14  14  ARG ARG A . n 
A 1 36  ILE 36  15  15  ILE ILE A . n 
A 1 37  GLY 37  16  16  GLY GLY A . n 
A 1 38  ARG 38  17  17  ARG ARG A . n 
A 1 39  ALA 39  18  18  ALA ALA A . n 
A 1 40  ILE 40  19  19  ILE ILE A . n 
A 1 41  ALA 41  20  20  ALA ALA A . n 
A 1 42  VAL 42  21  21  VAL VAL A . n 
A 1 43  LYS 43  22  22  LYS LYS A . n 
A 1 44  LEU 44  23  23  LEU LEU A . n 
A 1 45  HIS 45  24  24  HIS HIS A . n 
A 1 46  GLN 46  25  25  GLN GLN A . n 
A 1 47  THR 47  26  26  THR THR A . n 
A 1 48  GLY 48  27  27  GLY GLY A . n 
A 1 49  TYR 49  28  28  TYR TYR A . n 
A 1 50  ARG 50  29  29  ARG ARG A . n 
A 1 51  VAL 51  30  30  VAL VAL A . n 
A 1 52  VAL 52  31  31  VAL VAL A . n 
A 1 53  ILE 53  32  32  ILE ILE A . n 
A 1 54  HIS 54  33  33  HIS HIS A . n 
A 1 55  TYR 55  34  34  TYR TYR A . n 
A 1 56  HIS 56  35  35  HIS HIS A . n 
A 1 57  ASN 57  36  36  ASN ASN A . n 
A 1 58  SER 58  37  37  SER SER A . n 
A 1 59  ALA 59  38  38  ALA ALA A . n 
A 1 60  GLU 60  39  39  GLU GLU A . n 
A 1 61  ALA 61  40  40  ALA ALA A . n 
A 1 62  ALA 62  41  41  ALA ALA A . n 
A 1 63  VAL 63  42  42  VAL VAL A . n 
A 1 64  SER 64  43  43  SER SER A . n 
A 1 65  LEU 65  44  44  LEU LEU A . n 
A 1 66  ALA 66  45  45  ALA ALA A . n 
A 1 67  ASP 67  46  46  ASP ASP A . n 
A 1 68  GLU 68  47  47  GLU GLU A . n 
A 1 69  LEU 69  48  48  LEU LEU A . n 
A 1 70  ASN 70  49  49  ASN ASN A . n 
A 1 71  LYS 71  50  50  LYS LYS A . n 
A 1 72  GLU 72  51  51  GLU GLU A . n 
A 1 73  ARG 73  52  52  ARG ARG A . n 
A 1 74  SER 74  53  53  SER SER A . n 
A 1 75  ASN 75  54  54  ASN ASN A . n 
A 1 76  THR 76  55  55  THR THR A . n 
A 1 77  ALA 77  56  56  ALA ALA A . n 
A 1 78  VAL 78  57  57  VAL VAL A . n 
A 1 79  VAL 79  58  58  VAL VAL A . n 
A 1 80  CYS 80  59  59  CYS CYS A . n 
A 1 81  GLN 81  60  60  GLN GLN A . n 
A 1 82  ALA 82  61  61  ALA ALA A . n 
A 1 83  ASP 83  62  62  ASP ASP A . n 
A 1 84  LEU 84  63  63  LEU LEU A . n 
A 1 85  THR 85  64  64  THR THR A . n 
A 1 86  ASN 86  65  65  ASN ASN A . n 
A 1 87  SER 87  66  66  SER SER A . n 
A 1 88  ASN 88  67  67  ASN ASN A . n 
A 1 89  VAL 89  68  68  VAL VAL A . n 
A 1 90  LEU 90  69  69  LEU LEU A . n 
A 1 91  PRO 91  70  70  PRO PRO A . n 
A 1 92  ALA 92  71  71  ALA ALA A . n 
A 1 93  SER 93  72  72  SER SER A . n 
A 1 94  CYS 94  73  73  CYS CYS A . n 
A 1 95  GLU 95  74  74  GLU GLU A . n 
A 1 96  GLU 96  75  75  GLU GLU A . n 
A 1 97  ILE 97  76  76  ILE ILE A . n 
A 1 98  ILE 98  77  77  ILE ILE A . n 
A 1 99  ASN 99  78  78  ASN ASN A . n 
A 1 100 SER 100 79  79  SER SER A . n 
A 1 101 CYS 101 80  80  CYS CYS A . n 
A 1 102 PHE 102 81  81  PHE PHE A . n 
A 1 103 ARG 103 82  82  ARG ARG A . n 
A 1 104 ALA 104 83  83  ALA ALA A . n 
A 1 105 PHE 105 84  84  PHE PHE A . n 
A 1 106 GLY 106 85  85  GLY GLY A . n 
A 1 107 ARG 107 86  86  ARG ARG A . n 
A 1 108 CYS 108 87  87  CYS CYS A . n 
A 1 109 ASP 109 88  88  ASP ASP A . n 
A 1 110 VAL 110 89  89  VAL VAL A . n 
A 1 111 LEU 111 90  90  LEU LEU A . n 
A 1 112 VAL 112 91  91  VAL VAL A . n 
A 1 113 ASN 113 92  92  ASN ASN A . n 
A 1 114 ASN 114 93  93  ASN ASN A . n 
A 1 115 ALA 115 94  94  ALA ALA A . n 
A 1 116 SER 116 95  95  SER SER A . n 
A 1 117 ALA 117 96  96  ALA ALA A . n 
A 1 118 PHE 118 97  97  PHE PHE A . n 
A 1 119 TYR 119 98  98  TYR TYR A . n 
A 1 120 PRO 120 99  99  PRO PRO A . n 
A 1 121 THR 121 100 100 THR THR A . n 
A 1 122 PRO 122 101 101 PRO PRO A . n 
A 1 123 LEU 123 102 102 LEU LEU A . n 
A 1 124 VAL 124 103 103 VAL VAL A . n 
A 1 125 GLN 125 104 104 GLN GLN A . n 
A 1 126 GLY 126 105 ?   ?   ?   A . n 
A 1 127 ASP 127 106 ?   ?   ?   A . n 
A 1 128 HIS 128 107 ?   ?   ?   A . n 
A 1 129 GLU 129 108 ?   ?   ?   A . n 
A 1 130 ASP 130 109 ?   ?   ?   A . n 
A 1 131 ASN 131 110 ?   ?   ?   A . n 
A 1 132 SER 132 111 ?   ?   ?   A . n 
A 1 133 ASN 133 112 ?   ?   ?   A . n 
A 1 134 GLY 134 113 113 GLY GLY A . n 
A 1 135 LYS 135 114 114 LYS LYS A . n 
A 1 136 THR 136 115 115 THR THR A . n 
A 1 137 VAL 137 116 116 VAL VAL A . n 
A 1 138 GLU 138 117 117 GLU GLU A . n 
A 1 139 THR 139 118 118 THR THR A . n 
A 1 140 GLN 140 119 119 GLN GLN A . n 
A 1 141 VAL 141 120 120 VAL VAL A . n 
A 1 142 ALA 142 121 121 ALA ALA A . n 
A 1 143 GLU 143 122 122 GLU GLU A . n 
A 1 144 LEU 144 123 123 LEU LEU A . n 
A 1 145 ILE 145 124 124 ILE ILE A . n 
A 1 146 GLY 146 125 125 GLY GLY A . n 
A 1 147 THR 147 126 126 THR THR A . n 
A 1 148 ASN 148 127 127 ASN ASN A . n 
A 1 149 ALA 149 128 128 ALA ALA A . n 
A 1 150 ILE 150 129 129 ILE ILE A . n 
A 1 151 ALA 151 130 130 ALA ALA A . n 
A 1 152 PRO 152 131 131 PRO PRO A . n 
A 1 153 PHE 153 132 132 PHE PHE A . n 
A 1 154 LEU 154 133 133 LEU LEU A . n 
A 1 155 LEU 155 134 134 LEU LEU A . n 
A 1 156 THR 156 135 135 THR THR A . n 
A 1 157 MET 157 136 136 MET MET A . n 
A 1 158 SER 158 137 137 SER SER A . n 
A 1 159 PHE 159 138 138 PHE PHE A . n 
A 1 160 ALA 160 139 139 ALA ALA A . n 
A 1 161 GLN 161 140 140 GLN GLN A . n 
A 1 162 ARG 162 141 141 ARG ARG A . n 
A 1 163 GLN 163 142 142 GLN GLN A . n 
A 1 164 LYS 164 143 ?   ?   ?   A . n 
A 1 165 GLY 165 144 ?   ?   ?   A . n 
A 1 166 THR 166 145 ?   ?   ?   A . n 
A 1 167 ASN 167 146 ?   ?   ?   A . n 
A 1 168 PRO 168 147 ?   ?   ?   A . n 
A 1 169 ASN 169 148 ?   ?   ?   A . n 
A 1 170 CYS 170 149 ?   ?   ?   A . n 
A 1 171 THR 171 150 ?   ?   ?   A . n 
A 1 172 SER 172 151 ?   ?   ?   A . n 
A 1 173 SER 173 152 152 SER SER A . n 
A 1 174 ASN 174 153 153 ASN ASN A . n 
A 1 175 LEU 175 154 154 LEU LEU A . n 
A 1 176 SER 176 155 155 SER SER A . n 
A 1 177 ILE 177 156 156 ILE ILE A . n 
A 1 178 VAL 178 157 157 VAL VAL A . n 
A 1 179 ASN 179 158 158 ASN ASN A . n 
A 1 180 LEU 180 159 159 LEU LEU A . n 
A 1 181 CYS 181 160 160 CYS CYS A . n 
A 1 182 ASP 182 161 161 ASP ASP A . n 
A 1 183 ALA 183 162 162 ALA ALA A . n 
A 1 184 MET 184 163 163 MET MET A . n 
A 1 185 VAL 185 164 164 VAL VAL A . n 
A 1 186 ASP 186 165 165 ASP ASP A . n 
A 1 187 GLN 187 166 166 GLN GLN A . n 
A 1 188 PRO 188 167 167 PRO PRO A . n 
A 1 189 CYS 189 168 168 CYS CYS A . n 
A 1 190 MET 190 169 169 MET MET A . n 
A 1 191 ALA 191 170 170 ALA ALA A . n 
A 1 192 PHE 192 171 171 PHE PHE A . n 
A 1 193 SER 193 172 172 SER SER A . n 
A 1 194 LEU 194 173 173 LEU LEU A . n 
A 1 195 TYR 195 174 174 TYR TYR A . n 
A 1 196 ASN 196 175 175 ASN ASN A . n 
A 1 197 MET 197 176 176 MET MET A . n 
A 1 198 GLY 198 177 177 GLY GLY A . n 
A 1 199 LYS 199 178 178 LYS LYS A . n 
A 1 200 HIS 200 179 179 HIS HIS A . n 
A 1 201 ALA 201 180 180 ALA ALA A . n 
A 1 202 LEU 202 181 181 LEU LEU A . n 
A 1 203 VAL 203 182 182 VAL VAL A . n 
A 1 204 GLY 204 183 183 GLY GLY A . n 
A 1 205 LEU 205 184 184 LEU LEU A . n 
A 1 206 THR 206 185 185 THR THR A . n 
A 1 207 GLN 207 186 186 GLN GLN A . n 
A 1 208 SER 208 187 187 SER SER A . n 
A 1 209 ALA 209 188 188 ALA ALA A . n 
A 1 210 ALA 210 189 189 ALA ALA A . n 
A 1 211 LEU 211 190 190 LEU LEU A . n 
A 1 212 GLU 212 191 191 GLU GLU A . n 
A 1 213 LEU 213 192 192 LEU LEU A . n 
A 1 214 ALA 214 193 193 ALA ALA A . n 
A 1 215 PRO 215 194 194 PRO PRO A . n 
A 1 216 TYR 216 195 195 TYR TYR A . n 
A 1 217 GLY 217 196 196 GLY GLY A . n 
A 1 218 ILE 218 197 197 ILE ILE A . n 
A 1 219 ARG 219 198 198 ARG ARG A . n 
A 1 220 VAL 220 199 199 VAL VAL A . n 
A 1 221 ASN 221 200 200 ASN ASN A . n 
A 1 222 GLY 222 201 201 GLY GLY A . n 
A 1 223 VAL 223 202 202 VAL VAL A . n 
A 1 224 ALA 224 203 203 ALA ALA A . n 
A 1 225 PRO 225 204 204 PRO PRO A . n 
A 1 226 GLY 226 205 205 GLY GLY A . n 
A 1 227 VAL 227 206 206 VAL VAL A . n 
A 1 228 SER 228 207 207 SER SER A . n 
A 1 229 LEU 229 208 208 LEU LEU A . n 
A 1 230 LEU 230 209 209 LEU LEU A . n 
A 1 231 PRO 231 210 210 PRO PRO A . n 
A 1 232 VAL 232 211 211 VAL VAL A . n 
A 1 233 ALA 233 212 212 ALA ALA A . n 
A 1 234 MET 234 213 213 MET MET A . n 
A 1 235 GLY 235 214 214 GLY GLY A . n 
A 1 236 GLU 236 215 215 GLU GLU A . n 
A 1 237 GLU 237 216 216 GLU GLU A . n 
A 1 238 GLU 238 217 217 GLU GLU A . n 
A 1 239 LYS 239 218 218 LYS LYS A . n 
A 1 240 ASP 240 219 219 ASP ASP A . n 
A 1 241 LYS 241 220 220 LYS LYS A . n 
A 1 242 TRP 242 221 221 TRP TRP A . n 
A 1 243 ARG 243 222 222 ARG ARG A . n 
A 1 244 ARG 244 223 223 ARG ARG A . n 
A 1 245 LYS 245 224 224 LYS LYS A . n 
A 1 246 VAL 246 225 225 VAL VAL A . n 
A 1 247 PRO 247 226 226 PRO PRO A . n 
A 1 248 LEU 248 227 227 LEU LEU A . n 
A 1 249 GLY 249 228 228 GLY GLY A . n 
A 1 250 ARG 250 229 229 ARG ARG A . n 
A 1 251 ARG 251 230 230 ARG ARG A . n 
A 1 252 GLU 252 231 231 GLU GLU A . n 
A 1 253 ALA 253 232 232 ALA ALA A . n 
A 1 254 SER 254 233 233 SER SER A . n 
A 1 255 ALA 255 234 234 ALA ALA A . n 
A 1 256 GLU 256 235 235 GLU GLU A . n 
A 1 257 GLN 257 236 236 GLN GLN A . n 
A 1 258 ILE 258 237 237 ILE ILE A . n 
A 1 259 ALA 259 238 238 ALA ALA A . n 
A 1 260 ASP 260 239 239 ASP ASP A . n 
A 1 261 ALA 261 240 240 ALA ALA A . n 
A 1 262 VAL 262 241 241 VAL VAL A . n 
A 1 263 ILE 263 242 242 ILE ILE A . n 
A 1 264 PHE 264 243 243 PHE PHE A . n 
A 1 265 LEU 265 244 244 LEU LEU A . n 
A 1 266 VAL 266 245 245 VAL VAL A . n 
A 1 267 SER 267 246 246 SER SER A . n 
A 1 268 GLY 268 247 247 GLY GLY A . n 
A 1 269 SER 269 248 248 SER SER A . n 
A 1 270 ALA 270 249 249 ALA ALA A . n 
A 1 271 GLN 271 250 250 GLN GLN A . n 
A 1 272 TYR 272 251 251 TYR TYR A . n 
A 1 273 ILE 273 252 252 ILE ILE A . n 
A 1 274 THR 274 253 253 THR THR A . n 
A 1 275 GLY 275 254 254 GLY GLY A . n 
A 1 276 SER 276 255 255 SER SER A . n 
A 1 277 ILE 277 256 256 ILE ILE A . n 
A 1 278 ILE 278 257 257 ILE ILE A . n 
A 1 279 LYS 279 258 258 LYS LYS A . n 
A 1 280 VAL 280 259 259 VAL VAL A . n 
A 1 281 ASP 281 260 260 ASP ASP A . n 
A 1 282 GLY 282 261 261 GLY GLY A . n 
A 1 283 GLY 283 262 262 GLY GLY A . n 
A 1 284 LEU 284 263 263 LEU LEU A . n 
A 1 285 SER 285 264 264 SER SER A . n 
A 1 286 LEU 286 265 265 LEU LEU A . n 
A 1 287 VAL 287 266 266 VAL VAL A . n 
A 1 288 HIS 288 267 267 HIS HIS A . n 
A 1 289 ALA 289 268 268 ALA ALA A . n 
B 1 1   MET 1   -20 ?   ?   ?   B . n 
B 1 2   GLY 2   -19 ?   ?   ?   B . n 
B 1 3   SER 3   -18 ?   ?   ?   B . n 
B 1 4   SER 4   -17 ?   ?   ?   B . n 
B 1 5   HIS 5   -16 ?   ?   ?   B . n 
B 1 6   HIS 6   -15 ?   ?   ?   B . n 
B 1 7   HIS 7   -14 ?   ?   ?   B . n 
B 1 8   HIS 8   -13 ?   ?   ?   B . n 
B 1 9   HIS 9   -12 ?   ?   ?   B . n 
B 1 10  HIS 10  -11 ?   ?   ?   B . n 
B 1 11  SER 11  -10 ?   ?   ?   B . n 
B 1 12  SER 12  -9  ?   ?   ?   B . n 
B 1 13  GLY 13  -8  ?   ?   ?   B . n 
B 1 14  LEU 14  -7  ?   ?   ?   B . n 
B 1 15  VAL 15  -6  ?   ?   ?   B . n 
B 1 16  PRO 16  -5  ?   ?   ?   B . n 
B 1 17  ARG 17  -4  ?   ?   ?   B . n 
B 1 18  GLY 18  -3  ?   ?   ?   B . n 
B 1 19  SER 19  -2  ?   ?   ?   B . n 
B 1 20  HIS 20  -1  ?   ?   ?   B . n 
B 1 21  MET 21  0   ?   ?   ?   B . n 
B 1 22  MET 22  1   ?   ?   ?   B . n 
B 1 23  GLU 23  2   2   GLU GLU B . n 
B 1 24  ALA 24  3   3   ALA ALA B . n 
B 1 25  PRO 25  4   4   PRO PRO B . n 
B 1 26  ALA 26  5   5   ALA ALA B . n 
B 1 27  ALA 27  6   6   ALA ALA B . n 
B 1 28  VAL 28  7   7   VAL VAL B . n 
B 1 29  VAL 29  8   8   VAL VAL B . n 
B 1 30  THR 30  9   9   THR THR B . n 
B 1 31  GLY 31  10  10  GLY GLY B . n 
B 1 32  ALA 32  11  11  ALA ALA B . n 
B 1 33  ALA 33  12  12  ALA ALA B . n 
B 1 34  LYS 34  13  13  LYS LYS B . n 
B 1 35  ARG 35  14  14  ARG ARG B . n 
B 1 36  ILE 36  15  15  ILE ILE B . n 
B 1 37  GLY 37  16  16  GLY GLY B . n 
B 1 38  ARG 38  17  17  ARG ARG B . n 
B 1 39  ALA 39  18  18  ALA ALA B . n 
B 1 40  ILE 40  19  19  ILE ILE B . n 
B 1 41  ALA 41  20  20  ALA ALA B . n 
B 1 42  VAL 42  21  21  VAL VAL B . n 
B 1 43  LYS 43  22  22  LYS LYS B . n 
B 1 44  LEU 44  23  23  LEU LEU B . n 
B 1 45  HIS 45  24  24  HIS HIS B . n 
B 1 46  GLN 46  25  25  GLN GLN B . n 
B 1 47  THR 47  26  26  THR THR B . n 
B 1 48  GLY 48  27  27  GLY GLY B . n 
B 1 49  TYR 49  28  28  TYR TYR B . n 
B 1 50  ARG 50  29  29  ARG ARG B . n 
B 1 51  VAL 51  30  30  VAL VAL B . n 
B 1 52  VAL 52  31  31  VAL VAL B . n 
B 1 53  ILE 53  32  32  ILE ILE B . n 
B 1 54  HIS 54  33  33  HIS HIS B . n 
B 1 55  TYR 55  34  34  TYR TYR B . n 
B 1 56  HIS 56  35  35  HIS HIS B . n 
B 1 57  ASN 57  36  36  ASN ASN B . n 
B 1 58  SER 58  37  37  SER SER B . n 
B 1 59  ALA 59  38  38  ALA ALA B . n 
B 1 60  GLU 60  39  39  GLU GLU B . n 
B 1 61  ALA 61  40  40  ALA ALA B . n 
B 1 62  ALA 62  41  41  ALA ALA B . n 
B 1 63  VAL 63  42  42  VAL VAL B . n 
B 1 64  SER 64  43  43  SER SER B . n 
B 1 65  LEU 65  44  44  LEU LEU B . n 
B 1 66  ALA 66  45  45  ALA ALA B . n 
B 1 67  ASP 67  46  46  ASP ASP B . n 
B 1 68  GLU 68  47  47  GLU GLU B . n 
B 1 69  LEU 69  48  48  LEU LEU B . n 
B 1 70  ASN 70  49  49  ASN ASN B . n 
B 1 71  LYS 71  50  50  LYS LYS B . n 
B 1 72  GLU 72  51  51  GLU GLU B . n 
B 1 73  ARG 73  52  52  ARG ARG B . n 
B 1 74  SER 74  53  53  SER SER B . n 
B 1 75  ASN 75  54  54  ASN ASN B . n 
B 1 76  THR 76  55  55  THR THR B . n 
B 1 77  ALA 77  56  56  ALA ALA B . n 
B 1 78  VAL 78  57  57  VAL VAL B . n 
B 1 79  VAL 79  58  58  VAL VAL B . n 
B 1 80  CYS 80  59  59  CYS CYS B . n 
B 1 81  GLN 81  60  60  GLN GLN B . n 
B 1 82  ALA 82  61  61  ALA ALA B . n 
B 1 83  ASP 83  62  62  ASP ASP B . n 
B 1 84  LEU 84  63  63  LEU LEU B . n 
B 1 85  THR 85  64  64  THR THR B . n 
B 1 86  ASN 86  65  65  ASN ASN B . n 
B 1 87  SER 87  66  66  SER SER B . n 
B 1 88  ASN 88  67  67  ASN ASN B . n 
B 1 89  VAL 89  68  68  VAL VAL B . n 
B 1 90  LEU 90  69  69  LEU LEU B . n 
B 1 91  PRO 91  70  70  PRO PRO B . n 
B 1 92  ALA 92  71  71  ALA ALA B . n 
B 1 93  SER 93  72  72  SER SER B . n 
B 1 94  CYS 94  73  73  CYS CYS B . n 
B 1 95  GLU 95  74  74  GLU GLU B . n 
B 1 96  GLU 96  75  75  GLU GLU B . n 
B 1 97  ILE 97  76  76  ILE ILE B . n 
B 1 98  ILE 98  77  77  ILE ILE B . n 
B 1 99  ASN 99  78  78  ASN ASN B . n 
B 1 100 SER 100 79  79  SER SER B . n 
B 1 101 CYS 101 80  80  CYS CYS B . n 
B 1 102 PHE 102 81  81  PHE PHE B . n 
B 1 103 ARG 103 82  82  ARG ARG B . n 
B 1 104 ALA 104 83  83  ALA ALA B . n 
B 1 105 PHE 105 84  84  PHE PHE B . n 
B 1 106 GLY 106 85  85  GLY GLY B . n 
B 1 107 ARG 107 86  86  ARG ARG B . n 
B 1 108 CYS 108 87  87  CYS CYS B . n 
B 1 109 ASP 109 88  88  ASP ASP B . n 
B 1 110 VAL 110 89  89  VAL VAL B . n 
B 1 111 LEU 111 90  90  LEU LEU B . n 
B 1 112 VAL 112 91  91  VAL VAL B . n 
B 1 113 ASN 113 92  92  ASN ASN B . n 
B 1 114 ASN 114 93  93  ASN ASN B . n 
B 1 115 ALA 115 94  94  ALA ALA B . n 
B 1 116 SER 116 95  95  SER SER B . n 
B 1 117 ALA 117 96  96  ALA ALA B . n 
B 1 118 PHE 118 97  97  PHE PHE B . n 
B 1 119 TYR 119 98  98  TYR TYR B . n 
B 1 120 PRO 120 99  99  PRO PRO B . n 
B 1 121 THR 121 100 100 THR THR B . n 
B 1 122 PRO 122 101 101 PRO PRO B . n 
B 1 123 LEU 123 102 102 LEU LEU B . n 
B 1 124 VAL 124 103 103 VAL VAL B . n 
B 1 125 GLN 125 104 ?   ?   ?   B . n 
B 1 126 GLY 126 105 ?   ?   ?   B . n 
B 1 127 ASP 127 106 ?   ?   ?   B . n 
B 1 128 HIS 128 107 ?   ?   ?   B . n 
B 1 129 GLU 129 108 ?   ?   ?   B . n 
B 1 130 ASP 130 109 ?   ?   ?   B . n 
B 1 131 ASN 131 110 ?   ?   ?   B . n 
B 1 132 SER 132 111 ?   ?   ?   B . n 
B 1 133 ASN 133 112 ?   ?   ?   B . n 
B 1 134 GLY 134 113 113 GLY GLY B . n 
B 1 135 LYS 135 114 114 LYS LYS B . n 
B 1 136 THR 136 115 115 THR THR B . n 
B 1 137 VAL 137 116 116 VAL VAL B . n 
B 1 138 GLU 138 117 117 GLU GLU B . n 
B 1 139 THR 139 118 118 THR THR B . n 
B 1 140 GLN 140 119 119 GLN GLN B . n 
B 1 141 VAL 141 120 120 VAL VAL B . n 
B 1 142 ALA 142 121 121 ALA ALA B . n 
B 1 143 GLU 143 122 122 GLU GLU B . n 
B 1 144 LEU 144 123 123 LEU LEU B . n 
B 1 145 ILE 145 124 124 ILE ILE B . n 
B 1 146 GLY 146 125 125 GLY GLY B . n 
B 1 147 THR 147 126 126 THR THR B . n 
B 1 148 ASN 148 127 127 ASN ASN B . n 
B 1 149 ALA 149 128 128 ALA ALA B . n 
B 1 150 ILE 150 129 129 ILE ILE B . n 
B 1 151 ALA 151 130 130 ALA ALA B . n 
B 1 152 PRO 152 131 131 PRO PRO B . n 
B 1 153 PHE 153 132 132 PHE PHE B . n 
B 1 154 LEU 154 133 133 LEU LEU B . n 
B 1 155 LEU 155 134 134 LEU LEU B . n 
B 1 156 THR 156 135 135 THR THR B . n 
B 1 157 MET 157 136 136 MET MET B . n 
B 1 158 SER 158 137 137 SER SER B . n 
B 1 159 PHE 159 138 138 PHE PHE B . n 
B 1 160 ALA 160 139 139 ALA ALA B . n 
B 1 161 GLN 161 140 140 GLN GLN B . n 
B 1 162 ARG 162 141 141 ARG ARG B . n 
B 1 163 GLN 163 142 142 GLN GLN B . n 
B 1 164 LYS 164 143 143 LYS LYS B . n 
B 1 165 GLY 165 144 ?   ?   ?   B . n 
B 1 166 THR 166 145 ?   ?   ?   B . n 
B 1 167 ASN 167 146 ?   ?   ?   B . n 
B 1 168 PRO 168 147 ?   ?   ?   B . n 
B 1 169 ASN 169 148 ?   ?   ?   B . n 
B 1 170 CYS 170 149 ?   ?   ?   B . n 
B 1 171 THR 171 150 ?   ?   ?   B . n 
B 1 172 SER 172 151 ?   ?   ?   B . n 
B 1 173 SER 173 152 152 SER SER B . n 
B 1 174 ASN 174 153 153 ASN ASN B . n 
B 1 175 LEU 175 154 154 LEU LEU B . n 
B 1 176 SER 176 155 155 SER SER B . n 
B 1 177 ILE 177 156 156 ILE ILE B . n 
B 1 178 VAL 178 157 157 VAL VAL B . n 
B 1 179 ASN 179 158 158 ASN ASN B . n 
B 1 180 LEU 180 159 159 LEU LEU B . n 
B 1 181 CYS 181 160 160 CYS CYS B . n 
B 1 182 ASP 182 161 161 ASP ASP B . n 
B 1 183 ALA 183 162 162 ALA ALA B . n 
B 1 184 MET 184 163 163 MET MET B . n 
B 1 185 VAL 185 164 164 VAL VAL B . n 
B 1 186 ASP 186 165 165 ASP ASP B . n 
B 1 187 GLN 187 166 166 GLN GLN B . n 
B 1 188 PRO 188 167 167 PRO PRO B . n 
B 1 189 CYS 189 168 168 CYS CYS B . n 
B 1 190 MET 190 169 169 MET MET B . n 
B 1 191 ALA 191 170 170 ALA ALA B . n 
B 1 192 PHE 192 171 171 PHE PHE B . n 
B 1 193 SER 193 172 172 SER SER B . n 
B 1 194 LEU 194 173 173 LEU LEU B . n 
B 1 195 TYR 195 174 174 TYR TYR B . n 
B 1 196 ASN 196 175 175 ASN ASN B . n 
B 1 197 MET 197 176 176 MET MET B . n 
B 1 198 GLY 198 177 177 GLY GLY B . n 
B 1 199 LYS 199 178 178 LYS LYS B . n 
B 1 200 HIS 200 179 179 HIS HIS B . n 
B 1 201 ALA 201 180 180 ALA ALA B . n 
B 1 202 LEU 202 181 181 LEU LEU B . n 
B 1 203 VAL 203 182 182 VAL VAL B . n 
B 1 204 GLY 204 183 183 GLY GLY B . n 
B 1 205 LEU 205 184 184 LEU LEU B . n 
B 1 206 THR 206 185 185 THR THR B . n 
B 1 207 GLN 207 186 186 GLN GLN B . n 
B 1 208 SER 208 187 187 SER SER B . n 
B 1 209 ALA 209 188 188 ALA ALA B . n 
B 1 210 ALA 210 189 189 ALA ALA B . n 
B 1 211 LEU 211 190 190 LEU LEU B . n 
B 1 212 GLU 212 191 191 GLU GLU B . n 
B 1 213 LEU 213 192 192 LEU LEU B . n 
B 1 214 ALA 214 193 193 ALA ALA B . n 
B 1 215 PRO 215 194 194 PRO PRO B . n 
B 1 216 TYR 216 195 195 TYR TYR B . n 
B 1 217 GLY 217 196 196 GLY GLY B . n 
B 1 218 ILE 218 197 197 ILE ILE B . n 
B 1 219 ARG 219 198 198 ARG ARG B . n 
B 1 220 VAL 220 199 199 VAL VAL B . n 
B 1 221 ASN 221 200 200 ASN ASN B . n 
B 1 222 GLY 222 201 201 GLY GLY B . n 
B 1 223 VAL 223 202 202 VAL VAL B . n 
B 1 224 ALA 224 203 203 ALA ALA B . n 
B 1 225 PRO 225 204 204 PRO PRO B . n 
B 1 226 GLY 226 205 205 GLY GLY B . n 
B 1 227 VAL 227 206 206 VAL VAL B . n 
B 1 228 SER 228 207 207 SER SER B . n 
B 1 229 LEU 229 208 208 LEU LEU B . n 
B 1 230 LEU 230 209 209 LEU LEU B . n 
B 1 231 PRO 231 210 210 PRO PRO B . n 
B 1 232 VAL 232 211 211 VAL VAL B . n 
B 1 233 ALA 233 212 212 ALA ALA B . n 
B 1 234 MET 234 213 213 MET MET B . n 
B 1 235 GLY 235 214 214 GLY GLY B . n 
B 1 236 GLU 236 215 215 GLU GLU B . n 
B 1 237 GLU 237 216 216 GLU GLU B . n 
B 1 238 GLU 238 217 217 GLU GLU B . n 
B 1 239 LYS 239 218 218 LYS LYS B . n 
B 1 240 ASP 240 219 219 ASP ASP B . n 
B 1 241 LYS 241 220 220 LYS LYS B . n 
B 1 242 TRP 242 221 221 TRP TRP B . n 
B 1 243 ARG 243 222 222 ARG ARG B . n 
B 1 244 ARG 244 223 223 ARG ARG B . n 
B 1 245 LYS 245 224 224 LYS LYS B . n 
B 1 246 VAL 246 225 225 VAL VAL B . n 
B 1 247 PRO 247 226 226 PRO PRO B . n 
B 1 248 LEU 248 227 227 LEU LEU B . n 
B 1 249 GLY 249 228 228 GLY GLY B . n 
B 1 250 ARG 250 229 229 ARG ARG B . n 
B 1 251 ARG 251 230 230 ARG ARG B . n 
B 1 252 GLU 252 231 231 GLU GLU B . n 
B 1 253 ALA 253 232 232 ALA ALA B . n 
B 1 254 SER 254 233 233 SER SER B . n 
B 1 255 ALA 255 234 234 ALA ALA B . n 
B 1 256 GLU 256 235 235 GLU GLU B . n 
B 1 257 GLN 257 236 236 GLN GLN B . n 
B 1 258 ILE 258 237 237 ILE ILE B . n 
B 1 259 ALA 259 238 238 ALA ALA B . n 
B 1 260 ASP 260 239 239 ASP ASP B . n 
B 1 261 ALA 261 240 240 ALA ALA B . n 
B 1 262 VAL 262 241 241 VAL VAL B . n 
B 1 263 ILE 263 242 242 ILE ILE B . n 
B 1 264 PHE 264 243 243 PHE PHE B . n 
B 1 265 LEU 265 244 244 LEU LEU B . n 
B 1 266 VAL 266 245 245 VAL VAL B . n 
B 1 267 SER 267 246 246 SER SER B . n 
B 1 268 GLY 268 247 247 GLY GLY B . n 
B 1 269 SER 269 248 248 SER SER B . n 
B 1 270 ALA 270 249 249 ALA ALA B . n 
B 1 271 GLN 271 250 250 GLN GLN B . n 
B 1 272 TYR 272 251 251 TYR TYR B . n 
B 1 273 ILE 273 252 252 ILE ILE B . n 
B 1 274 THR 274 253 253 THR THR B . n 
B 1 275 GLY 275 254 254 GLY GLY B . n 
B 1 276 SER 276 255 255 SER SER B . n 
B 1 277 ILE 277 256 256 ILE ILE B . n 
B 1 278 ILE 278 257 257 ILE ILE B . n 
B 1 279 LYS 279 258 258 LYS LYS B . n 
B 1 280 VAL 280 259 259 VAL VAL B . n 
B 1 281 ASP 281 260 260 ASP ASP B . n 
B 1 282 GLY 282 261 261 GLY GLY B . n 
B 1 283 GLY 283 262 262 GLY GLY B . n 
B 1 284 LEU 284 263 263 LEU LEU B . n 
B 1 285 SER 285 264 264 SER SER B . n 
B 1 286 LEU 286 265 265 LEU LEU B . n 
B 1 287 VAL 287 266 266 VAL VAL B . n 
B 1 288 HIS 288 267 267 HIS HIS B . n 
B 1 289 ALA 289 268 268 ALA ALA B . n 
C 1 1   MET 1   -20 ?   ?   ?   C . n 
C 1 2   GLY 2   -19 ?   ?   ?   C . n 
C 1 3   SER 3   -18 ?   ?   ?   C . n 
C 1 4   SER 4   -17 ?   ?   ?   C . n 
C 1 5   HIS 5   -16 ?   ?   ?   C . n 
C 1 6   HIS 6   -15 ?   ?   ?   C . n 
C 1 7   HIS 7   -14 ?   ?   ?   C . n 
C 1 8   HIS 8   -13 ?   ?   ?   C . n 
C 1 9   HIS 9   -12 ?   ?   ?   C . n 
C 1 10  HIS 10  -11 ?   ?   ?   C . n 
C 1 11  SER 11  -10 ?   ?   ?   C . n 
C 1 12  SER 12  -9  ?   ?   ?   C . n 
C 1 13  GLY 13  -8  ?   ?   ?   C . n 
C 1 14  LEU 14  -7  ?   ?   ?   C . n 
C 1 15  VAL 15  -6  ?   ?   ?   C . n 
C 1 16  PRO 16  -5  ?   ?   ?   C . n 
C 1 17  ARG 17  -4  ?   ?   ?   C . n 
C 1 18  GLY 18  -3  ?   ?   ?   C . n 
C 1 19  SER 19  -2  ?   ?   ?   C . n 
C 1 20  HIS 20  -1  ?   ?   ?   C . n 
C 1 21  MET 21  0   ?   ?   ?   C . n 
C 1 22  MET 22  1   ?   ?   ?   C . n 
C 1 23  GLU 23  2   2   GLU GLU C . n 
C 1 24  ALA 24  3   3   ALA ALA C . n 
C 1 25  PRO 25  4   4   PRO PRO C . n 
C 1 26  ALA 26  5   5   ALA ALA C . n 
C 1 27  ALA 27  6   6   ALA ALA C . n 
C 1 28  VAL 28  7   7   VAL VAL C . n 
C 1 29  VAL 29  8   8   VAL VAL C . n 
C 1 30  THR 30  9   9   THR THR C . n 
C 1 31  GLY 31  10  10  GLY GLY C . n 
C 1 32  ALA 32  11  11  ALA ALA C . n 
C 1 33  ALA 33  12  12  ALA ALA C . n 
C 1 34  LYS 34  13  13  LYS LYS C . n 
C 1 35  ARG 35  14  14  ARG ARG C . n 
C 1 36  ILE 36  15  15  ILE ILE C . n 
C 1 37  GLY 37  16  16  GLY GLY C . n 
C 1 38  ARG 38  17  17  ARG ARG C . n 
C 1 39  ALA 39  18  18  ALA ALA C . n 
C 1 40  ILE 40  19  19  ILE ILE C . n 
C 1 41  ALA 41  20  20  ALA ALA C . n 
C 1 42  VAL 42  21  21  VAL VAL C . n 
C 1 43  LYS 43  22  22  LYS LYS C . n 
C 1 44  LEU 44  23  23  LEU LEU C . n 
C 1 45  HIS 45  24  24  HIS HIS C . n 
C 1 46  GLN 46  25  25  GLN GLN C . n 
C 1 47  THR 47  26  26  THR THR C . n 
C 1 48  GLY 48  27  27  GLY GLY C . n 
C 1 49  TYR 49  28  28  TYR TYR C . n 
C 1 50  ARG 50  29  29  ARG ARG C . n 
C 1 51  VAL 51  30  30  VAL VAL C . n 
C 1 52  VAL 52  31  31  VAL VAL C . n 
C 1 53  ILE 53  32  32  ILE ILE C . n 
C 1 54  HIS 54  33  33  HIS HIS C . n 
C 1 55  TYR 55  34  34  TYR TYR C . n 
C 1 56  HIS 56  35  35  HIS HIS C . n 
C 1 57  ASN 57  36  36  ASN ASN C . n 
C 1 58  SER 58  37  37  SER SER C . n 
C 1 59  ALA 59  38  38  ALA ALA C . n 
C 1 60  GLU 60  39  39  GLU GLU C . n 
C 1 61  ALA 61  40  40  ALA ALA C . n 
C 1 62  ALA 62  41  41  ALA ALA C . n 
C 1 63  VAL 63  42  42  VAL VAL C . n 
C 1 64  SER 64  43  43  SER SER C . n 
C 1 65  LEU 65  44  44  LEU LEU C . n 
C 1 66  ALA 66  45  45  ALA ALA C . n 
C 1 67  ASP 67  46  46  ASP ASP C . n 
C 1 68  GLU 68  47  47  GLU GLU C . n 
C 1 69  LEU 69  48  48  LEU LEU C . n 
C 1 70  ASN 70  49  49  ASN ASN C . n 
C 1 71  LYS 71  50  50  LYS LYS C . n 
C 1 72  GLU 72  51  51  GLU GLU C . n 
C 1 73  ARG 73  52  52  ARG ARG C . n 
C 1 74  SER 74  53  53  SER SER C . n 
C 1 75  ASN 75  54  54  ASN ASN C . n 
C 1 76  THR 76  55  55  THR THR C . n 
C 1 77  ALA 77  56  56  ALA ALA C . n 
C 1 78  VAL 78  57  57  VAL VAL C . n 
C 1 79  VAL 79  58  58  VAL VAL C . n 
C 1 80  CYS 80  59  59  CYS CYS C . n 
C 1 81  GLN 81  60  60  GLN GLN C . n 
C 1 82  ALA 82  61  61  ALA ALA C . n 
C 1 83  ASP 83  62  62  ASP ASP C . n 
C 1 84  LEU 84  63  63  LEU LEU C . n 
C 1 85  THR 85  64  64  THR THR C . n 
C 1 86  ASN 86  65  65  ASN ASN C . n 
C 1 87  SER 87  66  66  SER SER C . n 
C 1 88  ASN 88  67  67  ASN ASN C . n 
C 1 89  VAL 89  68  68  VAL VAL C . n 
C 1 90  LEU 90  69  69  LEU LEU C . n 
C 1 91  PRO 91  70  70  PRO PRO C . n 
C 1 92  ALA 92  71  71  ALA ALA C . n 
C 1 93  SER 93  72  72  SER SER C . n 
C 1 94  CYS 94  73  73  CYS CYS C . n 
C 1 95  GLU 95  74  74  GLU GLU C . n 
C 1 96  GLU 96  75  75  GLU GLU C . n 
C 1 97  ILE 97  76  76  ILE ILE C . n 
C 1 98  ILE 98  77  77  ILE ILE C . n 
C 1 99  ASN 99  78  78  ASN ASN C . n 
C 1 100 SER 100 79  79  SER SER C . n 
C 1 101 CYS 101 80  80  CYS CYS C . n 
C 1 102 PHE 102 81  81  PHE PHE C . n 
C 1 103 ARG 103 82  82  ARG ARG C . n 
C 1 104 ALA 104 83  83  ALA ALA C . n 
C 1 105 PHE 105 84  84  PHE PHE C . n 
C 1 106 GLY 106 85  85  GLY GLY C . n 
C 1 107 ARG 107 86  86  ARG ARG C . n 
C 1 108 CYS 108 87  87  CYS CYS C . n 
C 1 109 ASP 109 88  88  ASP ASP C . n 
C 1 110 VAL 110 89  89  VAL VAL C . n 
C 1 111 LEU 111 90  90  LEU LEU C . n 
C 1 112 VAL 112 91  91  VAL VAL C . n 
C 1 113 ASN 113 92  92  ASN ASN C . n 
C 1 114 ASN 114 93  93  ASN ASN C . n 
C 1 115 ALA 115 94  94  ALA ALA C . n 
C 1 116 SER 116 95  95  SER SER C . n 
C 1 117 ALA 117 96  96  ALA ALA C . n 
C 1 118 PHE 118 97  97  PHE PHE C . n 
C 1 119 TYR 119 98  98  TYR TYR C . n 
C 1 120 PRO 120 99  99  PRO PRO C . n 
C 1 121 THR 121 100 100 THR THR C . n 
C 1 122 PRO 122 101 101 PRO PRO C . n 
C 1 123 LEU 123 102 102 LEU LEU C . n 
C 1 124 VAL 124 103 103 VAL VAL C . n 
C 1 125 GLN 125 104 ?   ?   ?   C . n 
C 1 126 GLY 126 105 ?   ?   ?   C . n 
C 1 127 ASP 127 106 ?   ?   ?   C . n 
C 1 128 HIS 128 107 ?   ?   ?   C . n 
C 1 129 GLU 129 108 ?   ?   ?   C . n 
C 1 130 ASP 130 109 ?   ?   ?   C . n 
C 1 131 ASN 131 110 ?   ?   ?   C . n 
C 1 132 SER 132 111 ?   ?   ?   C . n 
C 1 133 ASN 133 112 ?   ?   ?   C . n 
C 1 134 GLY 134 113 ?   ?   ?   C . n 
C 1 135 LYS 135 114 114 LYS LYS C . n 
C 1 136 THR 136 115 115 THR THR C . n 
C 1 137 VAL 137 116 116 VAL VAL C . n 
C 1 138 GLU 138 117 117 GLU GLU C . n 
C 1 139 THR 139 118 118 THR THR C . n 
C 1 140 GLN 140 119 119 GLN GLN C . n 
C 1 141 VAL 141 120 120 VAL VAL C . n 
C 1 142 ALA 142 121 121 ALA ALA C . n 
C 1 143 GLU 143 122 122 GLU GLU C . n 
C 1 144 LEU 144 123 123 LEU LEU C . n 
C 1 145 ILE 145 124 124 ILE ILE C . n 
C 1 146 GLY 146 125 125 GLY GLY C . n 
C 1 147 THR 147 126 126 THR THR C . n 
C 1 148 ASN 148 127 127 ASN ASN C . n 
C 1 149 ALA 149 128 128 ALA ALA C . n 
C 1 150 ILE 150 129 129 ILE ILE C . n 
C 1 151 ALA 151 130 130 ALA ALA C . n 
C 1 152 PRO 152 131 131 PRO PRO C . n 
C 1 153 PHE 153 132 132 PHE PHE C . n 
C 1 154 LEU 154 133 133 LEU LEU C . n 
C 1 155 LEU 155 134 134 LEU LEU C . n 
C 1 156 THR 156 135 135 THR THR C . n 
C 1 157 MET 157 136 136 MET MET C . n 
C 1 158 SER 158 137 137 SER SER C . n 
C 1 159 PHE 159 138 138 PHE PHE C . n 
C 1 160 ALA 160 139 139 ALA ALA C . n 
C 1 161 GLN 161 140 140 GLN GLN C . n 
C 1 162 ARG 162 141 141 ARG ARG C . n 
C 1 163 GLN 163 142 142 GLN GLN C . n 
C 1 164 LYS 164 143 ?   ?   ?   C . n 
C 1 165 GLY 165 144 ?   ?   ?   C . n 
C 1 166 THR 166 145 ?   ?   ?   C . n 
C 1 167 ASN 167 146 ?   ?   ?   C . n 
C 1 168 PRO 168 147 ?   ?   ?   C . n 
C 1 169 ASN 169 148 ?   ?   ?   C . n 
C 1 170 CYS 170 149 ?   ?   ?   C . n 
C 1 171 THR 171 150 ?   ?   ?   C . n 
C 1 172 SER 172 151 ?   ?   ?   C . n 
C 1 173 SER 173 152 152 SER SER C . n 
C 1 174 ASN 174 153 153 ASN ASN C . n 
C 1 175 LEU 175 154 154 LEU LEU C . n 
C 1 176 SER 176 155 155 SER SER C . n 
C 1 177 ILE 177 156 156 ILE ILE C . n 
C 1 178 VAL 178 157 157 VAL VAL C . n 
C 1 179 ASN 179 158 158 ASN ASN C . n 
C 1 180 LEU 180 159 159 LEU LEU C . n 
C 1 181 CYS 181 160 160 CYS CYS C . n 
C 1 182 ASP 182 161 161 ASP ASP C . n 
C 1 183 ALA 183 162 162 ALA ALA C . n 
C 1 184 MET 184 163 163 MET MET C . n 
C 1 185 VAL 185 164 164 VAL VAL C . n 
C 1 186 ASP 186 165 165 ASP ASP C . n 
C 1 187 GLN 187 166 166 GLN GLN C . n 
C 1 188 PRO 188 167 167 PRO PRO C . n 
C 1 189 CYS 189 168 168 CYS CYS C . n 
C 1 190 MET 190 169 169 MET MET C . n 
C 1 191 ALA 191 170 170 ALA ALA C . n 
C 1 192 PHE 192 171 171 PHE PHE C . n 
C 1 193 SER 193 172 172 SER SER C . n 
C 1 194 LEU 194 173 173 LEU LEU C . n 
C 1 195 TYR 195 174 174 TYR TYR C . n 
C 1 196 ASN 196 175 175 ASN ASN C . n 
C 1 197 MET 197 176 176 MET MET C . n 
C 1 198 GLY 198 177 177 GLY GLY C . n 
C 1 199 LYS 199 178 178 LYS LYS C . n 
C 1 200 HIS 200 179 179 HIS HIS C . n 
C 1 201 ALA 201 180 180 ALA ALA C . n 
C 1 202 LEU 202 181 181 LEU LEU C . n 
C 1 203 VAL 203 182 182 VAL VAL C . n 
C 1 204 GLY 204 183 183 GLY GLY C . n 
C 1 205 LEU 205 184 184 LEU LEU C . n 
C 1 206 THR 206 185 185 THR THR C . n 
C 1 207 GLN 207 186 186 GLN GLN C . n 
C 1 208 SER 208 187 187 SER SER C . n 
C 1 209 ALA 209 188 188 ALA ALA C . n 
C 1 210 ALA 210 189 189 ALA ALA C . n 
C 1 211 LEU 211 190 190 LEU LEU C . n 
C 1 212 GLU 212 191 191 GLU GLU C . n 
C 1 213 LEU 213 192 192 LEU LEU C . n 
C 1 214 ALA 214 193 193 ALA ALA C . n 
C 1 215 PRO 215 194 194 PRO PRO C . n 
C 1 216 TYR 216 195 195 TYR TYR C . n 
C 1 217 GLY 217 196 196 GLY GLY C . n 
C 1 218 ILE 218 197 197 ILE ILE C . n 
C 1 219 ARG 219 198 198 ARG ARG C . n 
C 1 220 VAL 220 199 199 VAL VAL C . n 
C 1 221 ASN 221 200 200 ASN ASN C . n 
C 1 222 GLY 222 201 201 GLY GLY C . n 
C 1 223 VAL 223 202 202 VAL VAL C . n 
C 1 224 ALA 224 203 203 ALA ALA C . n 
C 1 225 PRO 225 204 204 PRO PRO C . n 
C 1 226 GLY 226 205 205 GLY GLY C . n 
C 1 227 VAL 227 206 206 VAL VAL C . n 
C 1 228 SER 228 207 207 SER SER C . n 
C 1 229 LEU 229 208 208 LEU LEU C . n 
C 1 230 LEU 230 209 209 LEU LEU C . n 
C 1 231 PRO 231 210 210 PRO PRO C . n 
C 1 232 VAL 232 211 211 VAL VAL C . n 
C 1 233 ALA 233 212 212 ALA ALA C . n 
C 1 234 MET 234 213 213 MET MET C . n 
C 1 235 GLY 235 214 214 GLY GLY C . n 
C 1 236 GLU 236 215 215 GLU GLU C . n 
C 1 237 GLU 237 216 216 GLU GLU C . n 
C 1 238 GLU 238 217 217 GLU GLU C . n 
C 1 239 LYS 239 218 218 LYS LYS C . n 
C 1 240 ASP 240 219 219 ASP ASP C . n 
C 1 241 LYS 241 220 220 LYS LYS C . n 
C 1 242 TRP 242 221 221 TRP TRP C . n 
C 1 243 ARG 243 222 222 ARG ARG C . n 
C 1 244 ARG 244 223 223 ARG ARG C . n 
C 1 245 LYS 245 224 224 LYS LYS C . n 
C 1 246 VAL 246 225 225 VAL VAL C . n 
C 1 247 PRO 247 226 226 PRO PRO C . n 
C 1 248 LEU 248 227 227 LEU LEU C . n 
C 1 249 GLY 249 228 228 GLY GLY C . n 
C 1 250 ARG 250 229 229 ARG ARG C . n 
C 1 251 ARG 251 230 230 ARG ARG C . n 
C 1 252 GLU 252 231 231 GLU GLU C . n 
C 1 253 ALA 253 232 232 ALA ALA C . n 
C 1 254 SER 254 233 233 SER SER C . n 
C 1 255 ALA 255 234 234 ALA ALA C . n 
C 1 256 GLU 256 235 235 GLU GLU C . n 
C 1 257 GLN 257 236 236 GLN GLN C . n 
C 1 258 ILE 258 237 237 ILE ILE C . n 
C 1 259 ALA 259 238 238 ALA ALA C . n 
C 1 260 ASP 260 239 239 ASP ASP C . n 
C 1 261 ALA 261 240 240 ALA ALA C . n 
C 1 262 VAL 262 241 241 VAL VAL C . n 
C 1 263 ILE 263 242 242 ILE ILE C . n 
C 1 264 PHE 264 243 243 PHE PHE C . n 
C 1 265 LEU 265 244 244 LEU LEU C . n 
C 1 266 VAL 266 245 245 VAL VAL C . n 
C 1 267 SER 267 246 246 SER SER C . n 
C 1 268 GLY 268 247 247 GLY GLY C . n 
C 1 269 SER 269 248 248 SER SER C . n 
C 1 270 ALA 270 249 249 ALA ALA C . n 
C 1 271 GLN 271 250 250 GLN GLN C . n 
C 1 272 TYR 272 251 251 TYR TYR C . n 
C 1 273 ILE 273 252 252 ILE ILE C . n 
C 1 274 THR 274 253 253 THR THR C . n 
C 1 275 GLY 275 254 254 GLY GLY C . n 
C 1 276 SER 276 255 255 SER SER C . n 
C 1 277 ILE 277 256 256 ILE ILE C . n 
C 1 278 ILE 278 257 257 ILE ILE C . n 
C 1 279 LYS 279 258 258 LYS LYS C . n 
C 1 280 VAL 280 259 259 VAL VAL C . n 
C 1 281 ASP 281 260 260 ASP ASP C . n 
C 1 282 GLY 282 261 261 GLY GLY C . n 
C 1 283 GLY 283 262 262 GLY GLY C . n 
C 1 284 LEU 284 263 263 LEU LEU C . n 
C 1 285 SER 285 264 264 SER SER C . n 
C 1 286 LEU 286 265 265 LEU LEU C . n 
C 1 287 VAL 287 266 266 VAL VAL C . n 
C 1 288 HIS 288 267 267 HIS HIS C . n 
C 1 289 ALA 289 268 268 ALA ALA C . n 
D 1 1   MET 1   -20 ?   ?   ?   D . n 
D 1 2   GLY 2   -19 ?   ?   ?   D . n 
D 1 3   SER 3   -18 ?   ?   ?   D . n 
D 1 4   SER 4   -17 ?   ?   ?   D . n 
D 1 5   HIS 5   -16 ?   ?   ?   D . n 
D 1 6   HIS 6   -15 ?   ?   ?   D . n 
D 1 7   HIS 7   -14 ?   ?   ?   D . n 
D 1 8   HIS 8   -13 ?   ?   ?   D . n 
D 1 9   HIS 9   -12 ?   ?   ?   D . n 
D 1 10  HIS 10  -11 ?   ?   ?   D . n 
D 1 11  SER 11  -10 ?   ?   ?   D . n 
D 1 12  SER 12  -9  ?   ?   ?   D . n 
D 1 13  GLY 13  -8  ?   ?   ?   D . n 
D 1 14  LEU 14  -7  ?   ?   ?   D . n 
D 1 15  VAL 15  -6  ?   ?   ?   D . n 
D 1 16  PRO 16  -5  ?   ?   ?   D . n 
D 1 17  ARG 17  -4  ?   ?   ?   D . n 
D 1 18  GLY 18  -3  ?   ?   ?   D . n 
D 1 19  SER 19  -2  ?   ?   ?   D . n 
D 1 20  HIS 20  -1  ?   ?   ?   D . n 
D 1 21  MET 21  0   ?   ?   ?   D . n 
D 1 22  MET 22  1   ?   ?   ?   D . n 
D 1 23  GLU 23  2   2   GLU GLU D . n 
D 1 24  ALA 24  3   3   ALA ALA D . n 
D 1 25  PRO 25  4   4   PRO PRO D . n 
D 1 26  ALA 26  5   5   ALA ALA D . n 
D 1 27  ALA 27  6   6   ALA ALA D . n 
D 1 28  VAL 28  7   7   VAL VAL D . n 
D 1 29  VAL 29  8   8   VAL VAL D . n 
D 1 30  THR 30  9   9   THR THR D . n 
D 1 31  GLY 31  10  10  GLY GLY D . n 
D 1 32  ALA 32  11  11  ALA ALA D . n 
D 1 33  ALA 33  12  12  ALA ALA D . n 
D 1 34  LYS 34  13  13  LYS LYS D . n 
D 1 35  ARG 35  14  14  ARG ARG D . n 
D 1 36  ILE 36  15  15  ILE ILE D . n 
D 1 37  GLY 37  16  16  GLY GLY D . n 
D 1 38  ARG 38  17  17  ARG ARG D . n 
D 1 39  ALA 39  18  18  ALA ALA D . n 
D 1 40  ILE 40  19  19  ILE ILE D . n 
D 1 41  ALA 41  20  20  ALA ALA D . n 
D 1 42  VAL 42  21  21  VAL VAL D . n 
D 1 43  LYS 43  22  22  LYS LYS D . n 
D 1 44  LEU 44  23  23  LEU LEU D . n 
D 1 45  HIS 45  24  24  HIS HIS D . n 
D 1 46  GLN 46  25  25  GLN GLN D . n 
D 1 47  THR 47  26  26  THR THR D . n 
D 1 48  GLY 48  27  27  GLY GLY D . n 
D 1 49  TYR 49  28  28  TYR TYR D . n 
D 1 50  ARG 50  29  29  ARG ARG D . n 
D 1 51  VAL 51  30  30  VAL VAL D . n 
D 1 52  VAL 52  31  31  VAL VAL D . n 
D 1 53  ILE 53  32  32  ILE ILE D . n 
D 1 54  HIS 54  33  33  HIS HIS D . n 
D 1 55  TYR 55  34  34  TYR TYR D . n 
D 1 56  HIS 56  35  35  HIS HIS D . n 
D 1 57  ASN 57  36  36  ASN ASN D . n 
D 1 58  SER 58  37  37  SER SER D . n 
D 1 59  ALA 59  38  38  ALA ALA D . n 
D 1 60  GLU 60  39  39  GLU GLU D . n 
D 1 61  ALA 61  40  40  ALA ALA D . n 
D 1 62  ALA 62  41  41  ALA ALA D . n 
D 1 63  VAL 63  42  42  VAL VAL D . n 
D 1 64  SER 64  43  43  SER SER D . n 
D 1 65  LEU 65  44  44  LEU LEU D . n 
D 1 66  ALA 66  45  45  ALA ALA D . n 
D 1 67  ASP 67  46  46  ASP ASP D . n 
D 1 68  GLU 68  47  47  GLU GLU D . n 
D 1 69  LEU 69  48  48  LEU LEU D . n 
D 1 70  ASN 70  49  49  ASN ASN D . n 
D 1 71  LYS 71  50  50  LYS LYS D . n 
D 1 72  GLU 72  51  51  GLU GLU D . n 
D 1 73  ARG 73  52  52  ARG ARG D . n 
D 1 74  SER 74  53  53  SER SER D . n 
D 1 75  ASN 75  54  54  ASN ASN D . n 
D 1 76  THR 76  55  55  THR THR D . n 
D 1 77  ALA 77  56  56  ALA ALA D . n 
D 1 78  VAL 78  57  57  VAL VAL D . n 
D 1 79  VAL 79  58  58  VAL VAL D . n 
D 1 80  CYS 80  59  59  CYS CYS D . n 
D 1 81  GLN 81  60  60  GLN GLN D . n 
D 1 82  ALA 82  61  61  ALA ALA D . n 
D 1 83  ASP 83  62  62  ASP ASP D . n 
D 1 84  LEU 84  63  63  LEU LEU D . n 
D 1 85  THR 85  64  64  THR THR D . n 
D 1 86  ASN 86  65  65  ASN ASN D . n 
D 1 87  SER 87  66  66  SER SER D . n 
D 1 88  ASN 88  67  67  ASN ASN D . n 
D 1 89  VAL 89  68  68  VAL VAL D . n 
D 1 90  LEU 90  69  69  LEU LEU D . n 
D 1 91  PRO 91  70  70  PRO PRO D . n 
D 1 92  ALA 92  71  71  ALA ALA D . n 
D 1 93  SER 93  72  72  SER SER D . n 
D 1 94  CYS 94  73  73  CYS CYS D . n 
D 1 95  GLU 95  74  74  GLU GLU D . n 
D 1 96  GLU 96  75  75  GLU GLU D . n 
D 1 97  ILE 97  76  76  ILE ILE D . n 
D 1 98  ILE 98  77  77  ILE ILE D . n 
D 1 99  ASN 99  78  78  ASN ASN D . n 
D 1 100 SER 100 79  79  SER SER D . n 
D 1 101 CYS 101 80  80  CYS CYS D . n 
D 1 102 PHE 102 81  81  PHE PHE D . n 
D 1 103 ARG 103 82  82  ARG ARG D . n 
D 1 104 ALA 104 83  83  ALA ALA D . n 
D 1 105 PHE 105 84  84  PHE PHE D . n 
D 1 106 GLY 106 85  85  GLY GLY D . n 
D 1 107 ARG 107 86  86  ARG ARG D . n 
D 1 108 CYS 108 87  87  CYS CYS D . n 
D 1 109 ASP 109 88  88  ASP ASP D . n 
D 1 110 VAL 110 89  89  VAL VAL D . n 
D 1 111 LEU 111 90  90  LEU LEU D . n 
D 1 112 VAL 112 91  91  VAL VAL D . n 
D 1 113 ASN 113 92  92  ASN ASN D . n 
D 1 114 ASN 114 93  93  ASN ASN D . n 
D 1 115 ALA 115 94  94  ALA ALA D . n 
D 1 116 SER 116 95  95  SER SER D . n 
D 1 117 ALA 117 96  96  ALA ALA D . n 
D 1 118 PHE 118 97  97  PHE PHE D . n 
D 1 119 TYR 119 98  98  TYR TYR D . n 
D 1 120 PRO 120 99  99  PRO PRO D . n 
D 1 121 THR 121 100 100 THR THR D . n 
D 1 122 PRO 122 101 101 PRO PRO D . n 
D 1 123 LEU 123 102 102 LEU LEU D . n 
D 1 124 VAL 124 103 103 VAL VAL D . n 
D 1 125 GLN 125 104 ?   ?   ?   D . n 
D 1 126 GLY 126 105 ?   ?   ?   D . n 
D 1 127 ASP 127 106 ?   ?   ?   D . n 
D 1 128 HIS 128 107 ?   ?   ?   D . n 
D 1 129 GLU 129 108 ?   ?   ?   D . n 
D 1 130 ASP 130 109 ?   ?   ?   D . n 
D 1 131 ASN 131 110 ?   ?   ?   D . n 
D 1 132 SER 132 111 ?   ?   ?   D . n 
D 1 133 ASN 133 112 ?   ?   ?   D . n 
D 1 134 GLY 134 113 113 GLY GLY D . n 
D 1 135 LYS 135 114 114 LYS LYS D . n 
D 1 136 THR 136 115 115 THR THR D . n 
D 1 137 VAL 137 116 116 VAL VAL D . n 
D 1 138 GLU 138 117 117 GLU GLU D . n 
D 1 139 THR 139 118 118 THR THR D . n 
D 1 140 GLN 140 119 119 GLN GLN D . n 
D 1 141 VAL 141 120 120 VAL VAL D . n 
D 1 142 ALA 142 121 121 ALA ALA D . n 
D 1 143 GLU 143 122 122 GLU GLU D . n 
D 1 144 LEU 144 123 123 LEU LEU D . n 
D 1 145 ILE 145 124 124 ILE ILE D . n 
D 1 146 GLY 146 125 125 GLY GLY D . n 
D 1 147 THR 147 126 126 THR THR D . n 
D 1 148 ASN 148 127 127 ASN ASN D . n 
D 1 149 ALA 149 128 128 ALA ALA D . n 
D 1 150 ILE 150 129 129 ILE ILE D . n 
D 1 151 ALA 151 130 130 ALA ALA D . n 
D 1 152 PRO 152 131 131 PRO PRO D . n 
D 1 153 PHE 153 132 132 PHE PHE D . n 
D 1 154 LEU 154 133 133 LEU LEU D . n 
D 1 155 LEU 155 134 134 LEU LEU D . n 
D 1 156 THR 156 135 135 THR THR D . n 
D 1 157 MET 157 136 136 MET MET D . n 
D 1 158 SER 158 137 137 SER SER D . n 
D 1 159 PHE 159 138 138 PHE PHE D . n 
D 1 160 ALA 160 139 139 ALA ALA D . n 
D 1 161 GLN 161 140 140 GLN GLN D . n 
D 1 162 ARG 162 141 141 ARG ARG D . n 
D 1 163 GLN 163 142 142 GLN GLN D . n 
D 1 164 LYS 164 143 ?   ?   ?   D . n 
D 1 165 GLY 165 144 ?   ?   ?   D . n 
D 1 166 THR 166 145 ?   ?   ?   D . n 
D 1 167 ASN 167 146 ?   ?   ?   D . n 
D 1 168 PRO 168 147 ?   ?   ?   D . n 
D 1 169 ASN 169 148 ?   ?   ?   D . n 
D 1 170 CYS 170 149 ?   ?   ?   D . n 
D 1 171 THR 171 150 ?   ?   ?   D . n 
D 1 172 SER 172 151 ?   ?   ?   D . n 
D 1 173 SER 173 152 152 SER SER D . n 
D 1 174 ASN 174 153 153 ASN ASN D . n 
D 1 175 LEU 175 154 154 LEU LEU D . n 
D 1 176 SER 176 155 155 SER SER D . n 
D 1 177 ILE 177 156 156 ILE ILE D . n 
D 1 178 VAL 178 157 157 VAL VAL D . n 
D 1 179 ASN 179 158 158 ASN ASN D . n 
D 1 180 LEU 180 159 159 LEU LEU D . n 
D 1 181 CYS 181 160 160 CYS CYS D . n 
D 1 182 ASP 182 161 161 ASP ASP D . n 
D 1 183 ALA 183 162 162 ALA ALA D . n 
D 1 184 MET 184 163 163 MET MET D . n 
D 1 185 VAL 185 164 164 VAL VAL D . n 
D 1 186 ASP 186 165 165 ASP ASP D . n 
D 1 187 GLN 187 166 166 GLN GLN D . n 
D 1 188 PRO 188 167 167 PRO PRO D . n 
D 1 189 CYS 189 168 168 CYS CYS D . n 
D 1 190 MET 190 169 169 MET MET D . n 
D 1 191 ALA 191 170 170 ALA ALA D . n 
D 1 192 PHE 192 171 171 PHE PHE D . n 
D 1 193 SER 193 172 172 SER SER D . n 
D 1 194 LEU 194 173 173 LEU LEU D . n 
D 1 195 TYR 195 174 174 TYR TYR D . n 
D 1 196 ASN 196 175 175 ASN ASN D . n 
D 1 197 MET 197 176 176 MET MET D . n 
D 1 198 GLY 198 177 177 GLY GLY D . n 
D 1 199 LYS 199 178 178 LYS LYS D . n 
D 1 200 HIS 200 179 179 HIS HIS D . n 
D 1 201 ALA 201 180 180 ALA ALA D . n 
D 1 202 LEU 202 181 181 LEU LEU D . n 
D 1 203 VAL 203 182 182 VAL VAL D . n 
D 1 204 GLY 204 183 183 GLY GLY D . n 
D 1 205 LEU 205 184 184 LEU LEU D . n 
D 1 206 THR 206 185 185 THR THR D . n 
D 1 207 GLN 207 186 186 GLN GLN D . n 
D 1 208 SER 208 187 187 SER SER D . n 
D 1 209 ALA 209 188 188 ALA ALA D . n 
D 1 210 ALA 210 189 189 ALA ALA D . n 
D 1 211 LEU 211 190 190 LEU LEU D . n 
D 1 212 GLU 212 191 191 GLU GLU D . n 
D 1 213 LEU 213 192 192 LEU LEU D . n 
D 1 214 ALA 214 193 193 ALA ALA D . n 
D 1 215 PRO 215 194 194 PRO PRO D . n 
D 1 216 TYR 216 195 195 TYR TYR D . n 
D 1 217 GLY 217 196 196 GLY GLY D . n 
D 1 218 ILE 218 197 197 ILE ILE D . n 
D 1 219 ARG 219 198 198 ARG ARG D . n 
D 1 220 VAL 220 199 199 VAL VAL D . n 
D 1 221 ASN 221 200 200 ASN ASN D . n 
D 1 222 GLY 222 201 201 GLY GLY D . n 
D 1 223 VAL 223 202 202 VAL VAL D . n 
D 1 224 ALA 224 203 203 ALA ALA D . n 
D 1 225 PRO 225 204 204 PRO PRO D . n 
D 1 226 GLY 226 205 205 GLY GLY D . n 
D 1 227 VAL 227 206 206 VAL VAL D . n 
D 1 228 SER 228 207 207 SER SER D . n 
D 1 229 LEU 229 208 208 LEU LEU D . n 
D 1 230 LEU 230 209 209 LEU LEU D . n 
D 1 231 PRO 231 210 210 PRO PRO D . n 
D 1 232 VAL 232 211 211 VAL VAL D . n 
D 1 233 ALA 233 212 212 ALA ALA D . n 
D 1 234 MET 234 213 213 MET MET D . n 
D 1 235 GLY 235 214 214 GLY GLY D . n 
D 1 236 GLU 236 215 215 GLU GLU D . n 
D 1 237 GLU 237 216 216 GLU GLU D . n 
D 1 238 GLU 238 217 217 GLU GLU D . n 
D 1 239 LYS 239 218 218 LYS LYS D . n 
D 1 240 ASP 240 219 219 ASP ASP D . n 
D 1 241 LYS 241 220 220 LYS LYS D . n 
D 1 242 TRP 242 221 221 TRP TRP D . n 
D 1 243 ARG 243 222 222 ARG ARG D . n 
D 1 244 ARG 244 223 223 ARG ARG D . n 
D 1 245 LYS 245 224 224 LYS LYS D . n 
D 1 246 VAL 246 225 225 VAL VAL D . n 
D 1 247 PRO 247 226 226 PRO PRO D . n 
D 1 248 LEU 248 227 227 LEU LEU D . n 
D 1 249 GLY 249 228 228 GLY GLY D . n 
D 1 250 ARG 250 229 229 ARG ARG D . n 
D 1 251 ARG 251 230 230 ARG ARG D . n 
D 1 252 GLU 252 231 231 GLU GLU D . n 
D 1 253 ALA 253 232 232 ALA ALA D . n 
D 1 254 SER 254 233 233 SER SER D . n 
D 1 255 ALA 255 234 234 ALA ALA D . n 
D 1 256 GLU 256 235 235 GLU GLU D . n 
D 1 257 GLN 257 236 236 GLN GLN D . n 
D 1 258 ILE 258 237 237 ILE ILE D . n 
D 1 259 ALA 259 238 238 ALA ALA D . n 
D 1 260 ASP 260 239 239 ASP ASP D . n 
D 1 261 ALA 261 240 240 ALA ALA D . n 
D 1 262 VAL 262 241 241 VAL VAL D . n 
D 1 263 ILE 263 242 242 ILE ILE D . n 
D 1 264 PHE 264 243 243 PHE PHE D . n 
D 1 265 LEU 265 244 244 LEU LEU D . n 
D 1 266 VAL 266 245 245 VAL VAL D . n 
D 1 267 SER 267 246 246 SER SER D . n 
D 1 268 GLY 268 247 247 GLY GLY D . n 
D 1 269 SER 269 248 248 SER SER D . n 
D 1 270 ALA 270 249 249 ALA ALA D . n 
D 1 271 GLN 271 250 250 GLN GLN D . n 
D 1 272 TYR 272 251 251 TYR TYR D . n 
D 1 273 ILE 273 252 252 ILE ILE D . n 
D 1 274 THR 274 253 253 THR THR D . n 
D 1 275 GLY 275 254 254 GLY GLY D . n 
D 1 276 SER 276 255 255 SER SER D . n 
D 1 277 ILE 277 256 256 ILE ILE D . n 
D 1 278 ILE 278 257 257 ILE ILE D . n 
D 1 279 LYS 279 258 258 LYS LYS D . n 
D 1 280 VAL 280 259 259 VAL VAL D . n 
D 1 281 ASP 281 260 260 ASP ASP D . n 
D 1 282 GLY 282 261 261 GLY GLY D . n 
D 1 283 GLY 283 262 262 GLY GLY D . n 
D 1 284 LEU 284 263 263 LEU LEU D . n 
D 1 285 SER 285 264 264 SER SER D . n 
D 1 286 LEU 286 265 265 LEU LEU D . n 
D 1 287 VAL 287 266 266 VAL VAL D . n 
D 1 288 HIS 288 267 267 HIS HIS D . n 
D 1 289 ALA 289 268 268 ALA ALA D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H0U 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H0U 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 NDP   1   301 269 NDP   NDP A . 
F 3 ACT   1   302 271 ACT   ACT A . 
G 3 ACT   1   303 272 ACT   ACT A . 
H 4 A1H0U 1   304 273 A1H0U DH9 A . 
I 2 NDP   1   301 269 NDP   NDP B . 
J 3 ACT   1   302 271 ACT   ACT B . 
K 4 A1H0U 1   303 272 A1H0U DH9 B . 
L 2 NDP   1   301 269 NDP   NDP C . 
M 2 NDP   1   301 269 NDP   NDP D . 
N 4 A1H0U 1   302 270 A1H0U DH9 D . 
O 5 HOH   1   401 588 HOH   HOH A . 
O 5 HOH   2   402 187 HOH   HOH A . 
O 5 HOH   3   403 35  HOH   HOH A . 
O 5 HOH   4   404 381 HOH   HOH A . 
O 5 HOH   5   405 531 HOH   HOH A . 
O 5 HOH   6   406 204 HOH   HOH A . 
O 5 HOH   7   407 113 HOH   HOH A . 
O 5 HOH   8   408 169 HOH   HOH A . 
O 5 HOH   9   409 199 HOH   HOH A . 
O 5 HOH   10  410 581 HOH   HOH A . 
O 5 HOH   11  411 208 HOH   HOH A . 
O 5 HOH   12  412 285 HOH   HOH A . 
O 5 HOH   13  413 238 HOH   HOH A . 
O 5 HOH   14  414 586 HOH   HOH A . 
O 5 HOH   15  415 65  HOH   HOH A . 
O 5 HOH   16  416 223 HOH   HOH A . 
O 5 HOH   17  417 232 HOH   HOH A . 
O 5 HOH   18  418 260 HOH   HOH A . 
O 5 HOH   19  419 186 HOH   HOH A . 
O 5 HOH   20  420 283 HOH   HOH A . 
O 5 HOH   21  421 397 HOH   HOH A . 
O 5 HOH   22  422 100 HOH   HOH A . 
O 5 HOH   23  423 3   HOH   HOH A . 
O 5 HOH   24  424 88  HOH   HOH A . 
O 5 HOH   25  425 111 HOH   HOH A . 
O 5 HOH   26  426 171 HOH   HOH A . 
O 5 HOH   27  427 10  HOH   HOH A . 
O 5 HOH   28  428 276 HOH   HOH A . 
O 5 HOH   29  429 190 HOH   HOH A . 
O 5 HOH   30  430 120 HOH   HOH A . 
O 5 HOH   31  431 50  HOH   HOH A . 
O 5 HOH   32  432 279 HOH   HOH A . 
O 5 HOH   33  433 33  HOH   HOH A . 
O 5 HOH   34  434 532 HOH   HOH A . 
O 5 HOH   35  435 84  HOH   HOH A . 
O 5 HOH   36  436 219 HOH   HOH A . 
O 5 HOH   37  437 464 HOH   HOH A . 
O 5 HOH   38  438 346 HOH   HOH A . 
O 5 HOH   39  439 304 HOH   HOH A . 
O 5 HOH   40  440 149 HOH   HOH A . 
O 5 HOH   41  441 248 HOH   HOH A . 
O 5 HOH   42  442 389 HOH   HOH A . 
O 5 HOH   43  443 22  HOH   HOH A . 
O 5 HOH   44  444 184 HOH   HOH A . 
O 5 HOH   45  445 47  HOH   HOH A . 
O 5 HOH   46  446 123 HOH   HOH A . 
O 5 HOH   47  447 160 HOH   HOH A . 
O 5 HOH   48  448 48  HOH   HOH A . 
O 5 HOH   49  449 213 HOH   HOH A . 
O 5 HOH   50  450 530 HOH   HOH A . 
O 5 HOH   51  451 252 HOH   HOH A . 
O 5 HOH   52  452 148 HOH   HOH A . 
O 5 HOH   53  453 289 HOH   HOH A . 
O 5 HOH   54  454 348 HOH   HOH A . 
O 5 HOH   55  455 5   HOH   HOH A . 
O 5 HOH   56  456 74  HOH   HOH A . 
O 5 HOH   57  457 85  HOH   HOH A . 
O 5 HOH   58  458 14  HOH   HOH A . 
O 5 HOH   59  459 143 HOH   HOH A . 
O 5 HOH   60  460 128 HOH   HOH A . 
O 5 HOH   61  461 165 HOH   HOH A . 
O 5 HOH   62  462 243 HOH   HOH A . 
O 5 HOH   63  463 60  HOH   HOH A . 
O 5 HOH   64  464 294 HOH   HOH A . 
O 5 HOH   65  465 92  HOH   HOH A . 
O 5 HOH   66  466 176 HOH   HOH A . 
O 5 HOH   67  467 306 HOH   HOH A . 
O 5 HOH   68  468 277 HOH   HOH A . 
O 5 HOH   69  469 329 HOH   HOH A . 
O 5 HOH   70  470 167 HOH   HOH A . 
O 5 HOH   71  471 315 HOH   HOH A . 
O 5 HOH   72  472 178 HOH   HOH A . 
O 5 HOH   73  473 542 HOH   HOH A . 
O 5 HOH   74  474 28  HOH   HOH A . 
O 5 HOH   75  475 25  HOH   HOH A . 
O 5 HOH   76  476 61  HOH   HOH A . 
O 5 HOH   77  477 86  HOH   HOH A . 
O 5 HOH   78  478 53  HOH   HOH A . 
O 5 HOH   79  479 131 HOH   HOH A . 
O 5 HOH   80  480 288 HOH   HOH A . 
O 5 HOH   81  481 62  HOH   HOH A . 
O 5 HOH   82  482 242 HOH   HOH A . 
O 5 HOH   83  483 300 HOH   HOH A . 
O 5 HOH   84  484 435 HOH   HOH A . 
O 5 HOH   85  485 181 HOH   HOH A . 
O 5 HOH   86  486 134 HOH   HOH A . 
O 5 HOH   87  487 497 HOH   HOH A . 
O 5 HOH   88  488 122 HOH   HOH A . 
O 5 HOH   89  489 461 HOH   HOH A . 
O 5 HOH   90  490 209 HOH   HOH A . 
O 5 HOH   91  491 492 HOH   HOH A . 
O 5 HOH   92  492 26  HOH   HOH A . 
O 5 HOH   93  493 302 HOH   HOH A . 
O 5 HOH   94  494 136 HOH   HOH A . 
O 5 HOH   95  495 292 HOH   HOH A . 
O 5 HOH   96  496 159 HOH   HOH A . 
O 5 HOH   97  497 157 HOH   HOH A . 
O 5 HOH   98  498 457 HOH   HOH A . 
O 5 HOH   99  499 604 HOH   HOH A . 
O 5 HOH   100 500 507 HOH   HOH A . 
O 5 HOH   101 501 514 HOH   HOH A . 
O 5 HOH   102 502 342 HOH   HOH A . 
O 5 HOH   103 503 107 HOH   HOH A . 
O 5 HOH   104 504 314 HOH   HOH A . 
O 5 HOH   105 505 589 HOH   HOH A . 
O 5 HOH   106 506 337 HOH   HOH A . 
O 5 HOH   107 507 398 HOH   HOH A . 
O 5 HOH   108 508 572 HOH   HOH A . 
O 5 HOH   109 509 594 HOH   HOH A . 
O 5 HOH   110 510 366 HOH   HOH A . 
O 5 HOH   111 511 265 HOH   HOH A . 
O 5 HOH   112 512 449 HOH   HOH A . 
O 5 HOH   113 513 354 HOH   HOH A . 
O 5 HOH   114 514 468 HOH   HOH A . 
O 5 HOH   115 515 571 HOH   HOH A . 
O 5 HOH   116 516 479 HOH   HOH A . 
O 5 HOH   117 517 541 HOH   HOH A . 
O 5 HOH   118 518 584 HOH   HOH A . 
O 5 HOH   119 519 427 HOH   HOH A . 
O 5 HOH   120 520 319 HOH   HOH A . 
O 5 HOH   121 521 551 HOH   HOH A . 
O 5 HOH   122 522 405 HOH   HOH A . 
O 5 HOH   123 523 559 HOH   HOH A . 
O 5 HOH   124 524 415 HOH   HOH A . 
O 5 HOH   125 525 402 HOH   HOH A . 
O 5 HOH   126 526 426 HOH   HOH A . 
O 5 HOH   127 527 307 HOH   HOH A . 
O 5 HOH   128 528 414 HOH   HOH A . 
O 5 HOH   129 529 406 HOH   HOH A . 
O 5 HOH   130 530 420 HOH   HOH A . 
O 5 HOH   131 531 409 HOH   HOH A . 
O 5 HOH   132 532 451 HOH   HOH A . 
O 5 HOH   133 533 562 HOH   HOH A . 
O 5 HOH   134 534 568 HOH   HOH A . 
O 5 HOH   135 535 471 HOH   HOH A . 
O 5 HOH   136 536 536 HOH   HOH A . 
O 5 HOH   137 537 570 HOH   HOH A . 
O 5 HOH   138 538 494 HOH   HOH A . 
O 5 HOH   139 539 218 HOH   HOH A . 
O 5 HOH   140 540 229 HOH   HOH A . 
O 5 HOH   141 541 228 HOH   HOH A . 
O 5 HOH   142 542 506 HOH   HOH A . 
O 5 HOH   143 543 333 HOH   HOH A . 
O 5 HOH   144 544 475 HOH   HOH A . 
O 5 HOH   145 545 363 HOH   HOH A . 
O 5 HOH   146 546 555 HOH   HOH A . 
O 5 HOH   147 547 403 HOH   HOH A . 
O 5 HOH   148 548 401 HOH   HOH A . 
P 5 HOH   1   401 245 HOH   HOH B . 
P 5 HOH   2   402 259 HOH   HOH B . 
P 5 HOH   3   403 295 HOH   HOH B . 
P 5 HOH   4   404 360 HOH   HOH B . 
P 5 HOH   5   405 155 HOH   HOH B . 
P 5 HOH   6   406 13  HOH   HOH B . 
P 5 HOH   7   407 152 HOH   HOH B . 
P 5 HOH   8   408 102 HOH   HOH B . 
P 5 HOH   9   409 553 HOH   HOH B . 
P 5 HOH   10  410 504 HOH   HOH B . 
P 5 HOH   11  411 18  HOH   HOH B . 
P 5 HOH   12  412 488 HOH   HOH B . 
P 5 HOH   13  413 130 HOH   HOH B . 
P 5 HOH   14  414 500 HOH   HOH B . 
P 5 HOH   15  415 63  HOH   HOH B . 
P 5 HOH   16  416 369 HOH   HOH B . 
P 5 HOH   17  417 11  HOH   HOH B . 
P 5 HOH   18  418 137 HOH   HOH B . 
P 5 HOH   19  419 462 HOH   HOH B . 
P 5 HOH   20  420 434 HOH   HOH B . 
P 5 HOH   21  421 511 HOH   HOH B . 
P 5 HOH   22  422 115 HOH   HOH B . 
P 5 HOH   23  423 73  HOH   HOH B . 
P 5 HOH   24  424 197 HOH   HOH B . 
P 5 HOH   25  425 205 HOH   HOH B . 
P 5 HOH   26  426 566 HOH   HOH B . 
P 5 HOH   27  427 117 HOH   HOH B . 
P 5 HOH   28  428 227 HOH   HOH B . 
P 5 HOH   29  429 546 HOH   HOH B . 
P 5 HOH   30  430 339 HOH   HOH B . 
P 5 HOH   31  431 446 HOH   HOH B . 
P 5 HOH   32  432 522 HOH   HOH B . 
P 5 HOH   33  433 109 HOH   HOH B . 
P 5 HOH   34  434 180 HOH   HOH B . 
P 5 HOH   35  435 575 HOH   HOH B . 
P 5 HOH   36  436 70  HOH   HOH B . 
P 5 HOH   37  437 41  HOH   HOH B . 
P 5 HOH   38  438 142 HOH   HOH B . 
P 5 HOH   39  439 7   HOH   HOH B . 
P 5 HOH   40  440 278 HOH   HOH B . 
P 5 HOH   41  441 206 HOH   HOH B . 
P 5 HOH   42  442 214 HOH   HOH B . 
P 5 HOH   43  443 80  HOH   HOH B . 
P 5 HOH   44  444 472 HOH   HOH B . 
P 5 HOH   45  445 247 HOH   HOH B . 
P 5 HOH   46  446 175 HOH   HOH B . 
P 5 HOH   47  447 561 HOH   HOH B . 
P 5 HOH   48  448 230 HOH   HOH B . 
P 5 HOH   49  449 150 HOH   HOH B . 
P 5 HOH   50  450 174 HOH   HOH B . 
P 5 HOH   51  451 299 HOH   HOH B . 
P 5 HOH   52  452 396 HOH   HOH B . 
P 5 HOH   53  453 79  HOH   HOH B . 
P 5 HOH   54  454 556 HOH   HOH B . 
P 5 HOH   55  455 90  HOH   HOH B . 
P 5 HOH   56  456 286 HOH   HOH B . 
P 5 HOH   57  457 196 HOH   HOH B . 
P 5 HOH   58  458 237 HOH   HOH B . 
P 5 HOH   59  459 552 HOH   HOH B . 
P 5 HOH   60  460 200 HOH   HOH B . 
P 5 HOH   61  461 141 HOH   HOH B . 
P 5 HOH   62  462 30  HOH   HOH B . 
P 5 HOH   63  463 221 HOH   HOH B . 
P 5 HOH   64  464 4   HOH   HOH B . 
P 5 HOH   65  465 399 HOH   HOH B . 
P 5 HOH   66  466 6   HOH   HOH B . 
P 5 HOH   67  467 17  HOH   HOH B . 
P 5 HOH   68  468 163 HOH   HOH B . 
P 5 HOH   69  469 44  HOH   HOH B . 
P 5 HOH   70  470 40  HOH   HOH B . 
P 5 HOH   71  471 103 HOH   HOH B . 
P 5 HOH   72  472 56  HOH   HOH B . 
P 5 HOH   73  473 54  HOH   HOH B . 
P 5 HOH   74  474 287 HOH   HOH B . 
P 5 HOH   75  475 182 HOH   HOH B . 
P 5 HOH   76  476 455 HOH   HOH B . 
P 5 HOH   77  477 509 HOH   HOH B . 
P 5 HOH   78  478 52  HOH   HOH B . 
P 5 HOH   79  479 602 HOH   HOH B . 
P 5 HOH   80  480 64  HOH   HOH B . 
P 5 HOH   81  481 249 HOH   HOH B . 
P 5 HOH   82  482 244 HOH   HOH B . 
P 5 HOH   83  483 379 HOH   HOH B . 
P 5 HOH   84  484 135 HOH   HOH B . 
P 5 HOH   85  485 194 HOH   HOH B . 
P 5 HOH   86  486 192 HOH   HOH B . 
P 5 HOH   87  487 1   HOH   HOH B . 
P 5 HOH   88  488 94  HOH   HOH B . 
P 5 HOH   89  489 112 HOH   HOH B . 
P 5 HOH   90  490 179 HOH   HOH B . 
P 5 HOH   91  491 78  HOH   HOH B . 
P 5 HOH   92  492 58  HOH   HOH B . 
P 5 HOH   93  493 191 HOH   HOH B . 
P 5 HOH   94  494 98  HOH   HOH B . 
P 5 HOH   95  495 151 HOH   HOH B . 
P 5 HOH   96  496 267 HOH   HOH B . 
P 5 HOH   97  497 15  HOH   HOH B . 
P 5 HOH   98  498 91  HOH   HOH B . 
P 5 HOH   99  499 271 HOH   HOH B . 
P 5 HOH   100 500 21  HOH   HOH B . 
P 5 HOH   101 501 45  HOH   HOH B . 
P 5 HOH   102 502 193 HOH   HOH B . 
P 5 HOH   103 503 432 HOH   HOH B . 
P 5 HOH   104 504 603 HOH   HOH B . 
P 5 HOH   105 505 437 HOH   HOH B . 
P 5 HOH   106 506 438 HOH   HOH B . 
P 5 HOH   107 507 254 HOH   HOH B . 
P 5 HOH   108 508 484 HOH   HOH B . 
P 5 HOH   109 509 170 HOH   HOH B . 
P 5 HOH   110 510 236 HOH   HOH B . 
P 5 HOH   111 511 114 HOH   HOH B . 
P 5 HOH   112 512 345 HOH   HOH B . 
P 5 HOH   113 513 330 HOH   HOH B . 
P 5 HOH   114 514 226 HOH   HOH B . 
P 5 HOH   115 515 388 HOH   HOH B . 
P 5 HOH   116 516 580 HOH   HOH B . 
P 5 HOH   117 517 495 HOH   HOH B . 
P 5 HOH   118 518 528 HOH   HOH B . 
P 5 HOH   119 519 436 HOH   HOH B . 
P 5 HOH   120 520 253 HOH   HOH B . 
P 5 HOH   121 521 587 HOH   HOH B . 
P 5 HOH   122 522 344 HOH   HOH B . 
P 5 HOH   123 523 266 HOH   HOH B . 
P 5 HOH   124 524 359 HOH   HOH B . 
P 5 HOH   125 525 425 HOH   HOH B . 
P 5 HOH   126 526 560 HOH   HOH B . 
P 5 HOH   127 527 444 HOH   HOH B . 
P 5 HOH   128 528 328 HOH   HOH B . 
P 5 HOH   129 529 297 HOH   HOH B . 
P 5 HOH   130 530 263 HOH   HOH B . 
P 5 HOH   131 531 108 HOH   HOH B . 
P 5 HOH   132 532 469 HOH   HOH B . 
P 5 HOH   133 533 477 HOH   HOH B . 
P 5 HOH   134 534 327 HOH   HOH B . 
P 5 HOH   135 535 443 HOH   HOH B . 
P 5 HOH   136 536 474 HOH   HOH B . 
P 5 HOH   137 537 42  HOH   HOH B . 
P 5 HOH   138 538 129 HOH   HOH B . 
P 5 HOH   139 539 548 HOH   HOH B . 
P 5 HOH   140 540 473 HOH   HOH B . 
P 5 HOH   141 541 416 HOH   HOH B . 
P 5 HOH   142 542 362 HOH   HOH B . 
P 5 HOH   143 543 273 HOH   HOH B . 
P 5 HOH   144 544 274 HOH   HOH B . 
P 5 HOH   145 545 460 HOH   HOH B . 
P 5 HOH   146 546 411 HOH   HOH B . 
P 5 HOH   147 547 518 HOH   HOH B . 
P 5 HOH   148 548 201 HOH   HOH B . 
P 5 HOH   149 549 431 HOH   HOH B . 
P 5 HOH   150 550 517 HOH   HOH B . 
P 5 HOH   151 551 391 HOH   HOH B . 
P 5 HOH   152 552 454 HOH   HOH B . 
P 5 HOH   153 553 439 HOH   HOH B . 
P 5 HOH   154 554 456 HOH   HOH B . 
P 5 HOH   155 555 256 HOH   HOH B . 
P 5 HOH   156 556 400 HOH   HOH B . 
P 5 HOH   157 557 579 HOH   HOH B . 
P 5 HOH   158 558 503 HOH   HOH B . 
P 5 HOH   159 559 558 HOH   HOH B . 
P 5 HOH   160 560 595 HOH   HOH B . 
P 5 HOH   161 561 491 HOH   HOH B . 
P 5 HOH   162 562 317 HOH   HOH B . 
P 5 HOH   163 563 512 HOH   HOH B . 
P 5 HOH   164 564 410 HOH   HOH B . 
P 5 HOH   165 565 423 HOH   HOH B . 
P 5 HOH   166 566 212 HOH   HOH B . 
P 5 HOH   167 567 513 HOH   HOH B . 
P 5 HOH   168 568 239 HOH   HOH B . 
P 5 HOH   169 569 351 HOH   HOH B . 
P 5 HOH   170 570 222 HOH   HOH B . 
P 5 HOH   171 571 234 HOH   HOH B . 
P 5 HOH   172 572 535 HOH   HOH B . 
P 5 HOH   173 573 470 HOH   HOH B . 
P 5 HOH   174 574 598 HOH   HOH B . 
Q 5 HOH   1   401 486 HOH   HOH C . 
Q 5 HOH   2   402 356 HOH   HOH C . 
Q 5 HOH   3   403 210 HOH   HOH C . 
Q 5 HOH   4   404 95  HOH   HOH C . 
Q 5 HOH   5   405 37  HOH   HOH C . 
Q 5 HOH   6   406 324 HOH   HOH C . 
Q 5 HOH   7   407 476 HOH   HOH C . 
Q 5 HOH   8   408 343 HOH   HOH C . 
Q 5 HOH   9   409 258 HOH   HOH C . 
Q 5 HOH   10  410 326 HOH   HOH C . 
Q 5 HOH   11  411 582 HOH   HOH C . 
Q 5 HOH   12  412 565 HOH   HOH C . 
Q 5 HOH   13  413 66  HOH   HOH C . 
Q 5 HOH   14  414 207 HOH   HOH C . 
Q 5 HOH   15  415 593 HOH   HOH C . 
Q 5 HOH   16  416 606 HOH   HOH C . 
Q 5 HOH   17  417 20  HOH   HOH C . 
Q 5 HOH   18  418 440 HOH   HOH C . 
Q 5 HOH   19  419 146 HOH   HOH C . 
Q 5 HOH   20  420 525 HOH   HOH C . 
Q 5 HOH   21  421 390 HOH   HOH C . 
Q 5 HOH   22  422 501 HOH   HOH C . 
Q 5 HOH   23  423 235 HOH   HOH C . 
Q 5 HOH   24  424 305 HOH   HOH C . 
Q 5 HOH   25  425 533 HOH   HOH C . 
Q 5 HOH   26  426 119 HOH   HOH C . 
Q 5 HOH   27  427 225 HOH   HOH C . 
Q 5 HOH   28  428 270 HOH   HOH C . 
Q 5 HOH   29  429 75  HOH   HOH C . 
Q 5 HOH   30  430 49  HOH   HOH C . 
Q 5 HOH   31  431 8   HOH   HOH C . 
Q 5 HOH   32  432 83  HOH   HOH C . 
Q 5 HOH   33  433 124 HOH   HOH C . 
Q 5 HOH   34  434 59  HOH   HOH C . 
Q 5 HOH   35  435 19  HOH   HOH C . 
Q 5 HOH   36  436 101 HOH   HOH C . 
Q 5 HOH   37  437 140 HOH   HOH C . 
Q 5 HOH   38  438 563 HOH   HOH C . 
Q 5 HOH   39  439 445 HOH   HOH C . 
Q 5 HOH   40  440 55  HOH   HOH C . 
Q 5 HOH   41  441 485 HOH   HOH C . 
Q 5 HOH   42  442 51  HOH   HOH C . 
Q 5 HOH   43  443 68  HOH   HOH C . 
Q 5 HOH   44  444 280 HOH   HOH C . 
Q 5 HOH   45  445 38  HOH   HOH C . 
Q 5 HOH   46  446 166 HOH   HOH C . 
Q 5 HOH   47  447 195 HOH   HOH C . 
Q 5 HOH   48  448 147 HOH   HOH C . 
Q 5 HOH   49  449 240 HOH   HOH C . 
Q 5 HOH   50  450 428 HOH   HOH C . 
Q 5 HOH   51  451 87  HOH   HOH C . 
Q 5 HOH   52  452 502 HOH   HOH C . 
Q 5 HOH   53  453 308 HOH   HOH C . 
Q 5 HOH   54  454 364 HOH   HOH C . 
Q 5 HOH   55  455 211 HOH   HOH C . 
Q 5 HOH   56  456 106 HOH   HOH C . 
Q 5 HOH   57  457 89  HOH   HOH C . 
Q 5 HOH   58  458 313 HOH   HOH C . 
Q 5 HOH   59  459 215 HOH   HOH C . 
Q 5 HOH   60  460 168 HOH   HOH C . 
Q 5 HOH   61  461 246 HOH   HOH C . 
Q 5 HOH   62  462 365 HOH   HOH C . 
Q 5 HOH   63  463 99  HOH   HOH C . 
Q 5 HOH   64  464 395 HOH   HOH C . 
Q 5 HOH   65  465 231 HOH   HOH C . 
Q 5 HOH   66  466 36  HOH   HOH C . 
Q 5 HOH   67  467 24  HOH   HOH C . 
Q 5 HOH   68  468 233 HOH   HOH C . 
Q 5 HOH   69  469 185 HOH   HOH C . 
Q 5 HOH   70  470 301 HOH   HOH C . 
Q 5 HOH   71  471 183 HOH   HOH C . 
Q 5 HOH   72  472 352 HOH   HOH C . 
Q 5 HOH   73  473 383 HOH   HOH C . 
Q 5 HOH   74  474 296 HOH   HOH C . 
Q 5 HOH   75  475 350 HOH   HOH C . 
Q 5 HOH   76  476 608 HOH   HOH C . 
Q 5 HOH   77  477 569 HOH   HOH C . 
Q 5 HOH   78  478 487 HOH   HOH C . 
Q 5 HOH   79  479 576 HOH   HOH C . 
Q 5 HOH   80  480 153 HOH   HOH C . 
Q 5 HOH   81  481 466 HOH   HOH C . 
Q 5 HOH   82  482 521 HOH   HOH C . 
Q 5 HOH   83  483 547 HOH   HOH C . 
Q 5 HOH   84  484 441 HOH   HOH C . 
Q 5 HOH   85  485 607 HOH   HOH C . 
Q 5 HOH   86  486 550 HOH   HOH C . 
Q 5 HOH   87  487 384 HOH   HOH C . 
Q 5 HOH   88  488 412 HOH   HOH C . 
Q 5 HOH   89  489 549 HOH   HOH C . 
Q 5 HOH   90  490 376 HOH   HOH C . 
Q 5 HOH   91  491 447 HOH   HOH C . 
Q 5 HOH   92  492 430 HOH   HOH C . 
Q 5 HOH   93  493 69  HOH   HOH C . 
Q 5 HOH   94  494 516 HOH   HOH C . 
Q 5 HOH   95  495 596 HOH   HOH C . 
Q 5 HOH   96  496 537 HOH   HOH C . 
Q 5 HOH   97  497 478 HOH   HOH C . 
Q 5 HOH   98  498 393 HOH   HOH C . 
Q 5 HOH   99  499 310 HOH   HOH C . 
Q 5 HOH   100 500 323 HOH   HOH C . 
Q 5 HOH   101 501 465 HOH   HOH C . 
Q 5 HOH   102 502 527 HOH   HOH C . 
Q 5 HOH   103 503 452 HOH   HOH C . 
Q 5 HOH   104 504 320 HOH   HOH C . 
Q 5 HOH   105 505 422 HOH   HOH C . 
Q 5 HOH   106 506 480 HOH   HOH C . 
Q 5 HOH   107 507 340 HOH   HOH C . 
Q 5 HOH   108 508 429 HOH   HOH C . 
Q 5 HOH   109 509 418 HOH   HOH C . 
Q 5 HOH   110 510 392 HOH   HOH C . 
Q 5 HOH   111 511 519 HOH   HOH C . 
Q 5 HOH   112 512 538 HOH   HOH C . 
Q 5 HOH   113 513 394 HOH   HOH C . 
Q 5 HOH   114 514 367 HOH   HOH C . 
R 5 HOH   1   401 375 HOH   HOH D . 
R 5 HOH   2   402 524 HOH   HOH D . 
R 5 HOH   3   403 241 HOH   HOH D . 
R 5 HOH   4   404 46  HOH   HOH D . 
R 5 HOH   5   405 543 HOH   HOH D . 
R 5 HOH   6   406 336 HOH   HOH D . 
R 5 HOH   7   407 23  HOH   HOH D . 
R 5 HOH   8   408 482 HOH   HOH D . 
R 5 HOH   9   409 220 HOH   HOH D . 
R 5 HOH   10  410 371 HOH   HOH D . 
R 5 HOH   11  411 93  HOH   HOH D . 
R 5 HOH   12  412 32  HOH   HOH D . 
R 5 HOH   13  413 77  HOH   HOH D . 
R 5 HOH   14  414 529 HOH   HOH D . 
R 5 HOH   15  415 489 HOH   HOH D . 
R 5 HOH   16  416 557 HOH   HOH D . 
R 5 HOH   17  417 272 HOH   HOH D . 
R 5 HOH   18  418 71  HOH   HOH D . 
R 5 HOH   19  419 564 HOH   HOH D . 
R 5 HOH   20  420 609 HOH   HOH D . 
R 5 HOH   21  421 224 HOH   HOH D . 
R 5 HOH   22  422 110 HOH   HOH D . 
R 5 HOH   23  423 2   HOH   HOH D . 
R 5 HOH   24  424 467 HOH   HOH D . 
R 5 HOH   25  425 144 HOH   HOH D . 
R 5 HOH   26  426 139 HOH   HOH D . 
R 5 HOH   27  427 76  HOH   HOH D . 
R 5 HOH   28  428 347 HOH   HOH D . 
R 5 HOH   29  429 29  HOH   HOH D . 
R 5 HOH   30  430 577 HOH   HOH D . 
R 5 HOH   31  431 442 HOH   HOH D . 
R 5 HOH   32  432 374 HOH   HOH D . 
R 5 HOH   33  433 298 HOH   HOH D . 
R 5 HOH   34  434 216 HOH   HOH D . 
R 5 HOH   35  435 127 HOH   HOH D . 
R 5 HOH   36  436 353 HOH   HOH D . 
R 5 HOH   37  437 496 HOH   HOH D . 
R 5 HOH   38  438 12  HOH   HOH D . 
R 5 HOH   39  439 421 HOH   HOH D . 
R 5 HOH   40  440 72  HOH   HOH D . 
R 5 HOH   41  441 39  HOH   HOH D . 
R 5 HOH   42  442 251 HOH   HOH D . 
R 5 HOH   43  443 540 HOH   HOH D . 
R 5 HOH   44  444 118 HOH   HOH D . 
R 5 HOH   45  445 291 HOH   HOH D . 
R 5 HOH   46  446 82  HOH   HOH D . 
R 5 HOH   47  447 290 HOH   HOH D . 
R 5 HOH   48  448 361 HOH   HOH D . 
R 5 HOH   49  449 105 HOH   HOH D . 
R 5 HOH   50  450 481 HOH   HOH D . 
R 5 HOH   51  451 257 HOH   HOH D . 
R 5 HOH   52  452 173 HOH   HOH D . 
R 5 HOH   53  453 523 HOH   HOH D . 
R 5 HOH   54  454 16  HOH   HOH D . 
R 5 HOH   55  455 57  HOH   HOH D . 
R 5 HOH   56  456 97  HOH   HOH D . 
R 5 HOH   57  457 133 HOH   HOH D . 
R 5 HOH   58  458 539 HOH   HOH D . 
R 5 HOH   59  459 189 HOH   HOH D . 
R 5 HOH   60  460 284 HOH   HOH D . 
R 5 HOH   61  461 43  HOH   HOH D . 
R 5 HOH   62  462 96  HOH   HOH D . 
R 5 HOH   63  463 493 HOH   HOH D . 
R 5 HOH   64  464 293 HOH   HOH D . 
R 5 HOH   65  465 605 HOH   HOH D . 
R 5 HOH   66  466 154 HOH   HOH D . 
R 5 HOH   67  467 268 HOH   HOH D . 
R 5 HOH   68  468 31  HOH   HOH D . 
R 5 HOH   69  469 483 HOH   HOH D . 
R 5 HOH   70  470 162 HOH   HOH D . 
R 5 HOH   71  471 125 HOH   HOH D . 
R 5 HOH   72  472 156 HOH   HOH D . 
R 5 HOH   73  473 177 HOH   HOH D . 
R 5 HOH   74  474 126 HOH   HOH D . 
R 5 HOH   75  475 526 HOH   HOH D . 
R 5 HOH   76  476 9   HOH   HOH D . 
R 5 HOH   77  477 544 HOH   HOH D . 
R 5 HOH   78  478 498 HOH   HOH D . 
R 5 HOH   79  479 325 HOH   HOH D . 
R 5 HOH   80  480 413 HOH   HOH D . 
R 5 HOH   81  481 145 HOH   HOH D . 
R 5 HOH   82  482 380 HOH   HOH D . 
R 5 HOH   83  483 27  HOH   HOH D . 
R 5 HOH   84  484 567 HOH   HOH D . 
R 5 HOH   85  485 158 HOH   HOH D . 
R 5 HOH   86  486 81  HOH   HOH D . 
R 5 HOH   87  487 554 HOH   HOH D . 
R 5 HOH   88  488 262 HOH   HOH D . 
R 5 HOH   89  489 116 HOH   HOH D . 
R 5 HOH   90  490 458 HOH   HOH D . 
R 5 HOH   91  491 138 HOH   HOH D . 
R 5 HOH   92  492 601 HOH   HOH D . 
R 5 HOH   93  493 545 HOH   HOH D . 
R 5 HOH   94  494 334 HOH   HOH D . 
R 5 HOH   95  495 590 HOH   HOH D . 
R 5 HOH   96  496 104 HOH   HOH D . 
R 5 HOH   97  497 459 HOH   HOH D . 
R 5 HOH   98  498 275 HOH   HOH D . 
R 5 HOH   99  499 358 HOH   HOH D . 
R 5 HOH   100 500 255 HOH   HOH D . 
R 5 HOH   101 501 463 HOH   HOH D . 
R 5 HOH   102 502 331 HOH   HOH D . 
R 5 HOH   103 503 600 HOH   HOH D . 
R 5 HOH   104 504 407 HOH   HOH D . 
R 5 HOH   105 505 417 HOH   HOH D . 
R 5 HOH   106 506 505 HOH   HOH D . 
R 5 HOH   107 507 583 HOH   HOH D . 
R 5 HOH   108 508 574 HOH   HOH D . 
R 5 HOH   109 509 282 HOH   HOH D . 
R 5 HOH   110 510 408 HOH   HOH D . 
R 5 HOH   111 511 322 HOH   HOH D . 
R 5 HOH   112 512 499 HOH   HOH D . 
R 5 HOH   113 513 424 HOH   HOH D . 
R 5 HOH   114 514 592 HOH   HOH D . 
R 5 HOH   115 515 332 HOH   HOH D . 
R 5 HOH   116 516 349 HOH   HOH D . 
R 5 HOH   117 517 573 HOH   HOH D . 
R 5 HOH   118 518 591 HOH   HOH D . 
R 5 HOH   119 519 250 HOH   HOH D . 
R 5 HOH   120 520 510 HOH   HOH D . 
R 5 HOH   121 521 281 HOH   HOH D . 
R 5 HOH   122 522 433 HOH   HOH D . 
R 5 HOH   123 523 450 HOH   HOH D . 
R 5 HOH   124 524 453 HOH   HOH D . 
R 5 HOH   125 525 419 HOH   HOH D . 
R 5 HOH   126 526 316 HOH   HOH D . 
R 5 HOH   127 527 355 HOH   HOH D . 
R 5 HOH   128 528 578 HOH   HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 2   ? CD  ? A GLU 23  CD  
2  1 Y 1 A GLU 2   ? OE1 ? A GLU 23  OE1 
3  1 Y 1 A GLU 2   ? OE2 ? A GLU 23  OE2 
4  1 Y 1 A LYS 50  ? CE  ? A LYS 71  CE  
5  1 Y 1 A LYS 50  ? NZ  ? A LYS 71  NZ  
6  1 Y 1 A VAL 103 ? CG1 ? A VAL 124 CG1 
7  1 Y 1 A VAL 103 ? CG2 ? A VAL 124 CG2 
8  1 Y 1 A GLN 104 ? CG  ? A GLN 125 CG  
9  1 Y 1 A GLN 104 ? CD  ? A GLN 125 CD  
10 1 Y 1 A GLN 104 ? OE1 ? A GLN 125 OE1 
11 1 Y 1 A GLN 104 ? NE2 ? A GLN 125 NE2 
12 1 Y 1 A VAL 211 ? CG1 ? A VAL 232 CG1 
13 1 Y 1 A VAL 211 ? CG2 ? A VAL 232 CG2 
14 1 Y 1 A GLU 216 ? CD  ? A GLU 237 CD  
15 1 Y 1 A GLU 216 ? OE1 ? A GLU 237 OE1 
16 1 Y 1 A GLU 216 ? OE2 ? A GLU 237 OE2 
17 1 Y 1 B GLU 39  ? CD  ? B GLU 60  CD  
18 1 Y 1 B GLU 39  ? OE1 ? B GLU 60  OE1 
19 1 Y 1 B GLU 39  ? OE2 ? B GLU 60  OE2 
20 1 Y 1 B LYS 50  ? CG  ? B LYS 71  CG  
21 1 Y 1 B LYS 50  ? CD  ? B LYS 71  CD  
22 1 Y 1 B LYS 50  ? CE  ? B LYS 71  CE  
23 1 Y 1 B LYS 50  ? NZ  ? B LYS 71  NZ  
24 1 Y 1 B ARG 82  ? NE  ? B ARG 103 NE  
25 1 Y 1 B ARG 82  ? CZ  ? B ARG 103 CZ  
26 1 Y 1 B ARG 82  ? NH1 ? B ARG 103 NH1 
27 1 Y 1 B ARG 82  ? NH2 ? B ARG 103 NH2 
28 1 Y 1 B LYS 143 ? CG  ? B LYS 164 CG  
29 1 Y 1 B LYS 143 ? CD  ? B LYS 164 CD  
30 1 Y 1 B LYS 143 ? CE  ? B LYS 164 CE  
31 1 Y 1 B LYS 143 ? NZ  ? B LYS 164 NZ  
32 1 Y 1 B SER 152 ? OG  ? B SER 173 OG  
33 1 Y 1 C GLU 2   ? CG  ? C GLU 23  CG  
34 1 Y 1 C GLU 2   ? CD  ? C GLU 23  CD  
35 1 Y 1 C GLU 2   ? OE1 ? C GLU 23  OE1 
36 1 Y 1 C GLU 2   ? OE2 ? C GLU 23  OE2 
37 1 Y 1 C LYS 13  ? CE  ? C LYS 34  CE  
38 1 Y 1 C LYS 13  ? NZ  ? C LYS 34  NZ  
39 1 Y 1 C LYS 50  ? CG  ? C LYS 71  CG  
40 1 Y 1 C LYS 50  ? CD  ? C LYS 71  CD  
41 1 Y 1 C LYS 50  ? CE  ? C LYS 71  CE  
42 1 Y 1 C LYS 50  ? NZ  ? C LYS 71  NZ  
43 1 Y 1 C ARG 141 ? NE  ? C ARG 162 NE  
44 1 Y 1 C ARG 141 ? CZ  ? C ARG 162 CZ  
45 1 Y 1 C ARG 141 ? NH1 ? C ARG 162 NH1 
46 1 Y 1 C ARG 141 ? NH2 ? C ARG 162 NH2 
47 1 Y 1 C SER 152 ? OG  ? C SER 173 OG  
48 1 Y 1 C VAL 211 ? CG1 ? C VAL 232 CG1 
49 1 Y 1 C VAL 211 ? CG2 ? C VAL 232 CG2 
50 1 Y 1 C GLU 216 ? CG  ? C GLU 237 CG  
51 1 Y 1 C GLU 216 ? CD  ? C GLU 237 CD  
52 1 Y 1 C GLU 216 ? OE1 ? C GLU 237 OE1 
53 1 Y 1 C GLU 216 ? OE2 ? C GLU 237 OE2 
54 1 Y 1 C GLU 217 ? CG  ? C GLU 238 CG  
55 1 Y 1 C GLU 217 ? CD  ? C GLU 238 CD  
56 1 Y 1 C GLU 217 ? OE1 ? C GLU 238 OE1 
57 1 Y 1 C GLU 217 ? OE2 ? C GLU 238 OE2 
58 1 Y 1 C LYS 220 ? CD  ? C LYS 241 CD  
59 1 Y 1 C LYS 220 ? CE  ? C LYS 241 CE  
60 1 Y 1 C LYS 220 ? NZ  ? C LYS 241 NZ  
61 1 Y 1 C ARG 223 ? CG  ? C ARG 244 CG  
62 1 Y 1 C ARG 223 ? CD  ? C ARG 244 CD  
63 1 Y 1 C ARG 223 ? NE  ? C ARG 244 NE  
64 1 Y 1 C ARG 223 ? CZ  ? C ARG 244 CZ  
65 1 Y 1 C ARG 223 ? NH1 ? C ARG 244 NH1 
66 1 Y 1 C ARG 223 ? NH2 ? C ARG 244 NH2 
67 1 Y 1 C ARG 230 ? NE  ? C ARG 251 NE  
68 1 Y 1 C ARG 230 ? CZ  ? C ARG 251 CZ  
69 1 Y 1 C ARG 230 ? NH1 ? C ARG 251 NH1 
70 1 Y 1 C ARG 230 ? NH2 ? C ARG 251 NH2 
71 1 Y 1 D GLU 2   ? CD  ? D GLU 23  CD  
72 1 Y 1 D GLU 2   ? OE1 ? D GLU 23  OE1 
73 1 Y 1 D GLU 2   ? OE2 ? D GLU 23  OE2 
74 1 Y 1 D LYS 13  ? CE  ? D LYS 34  CE  
75 1 Y 1 D LYS 13  ? NZ  ? D LYS 34  NZ  
76 1 Y 1 D LYS 50  ? CG  ? D LYS 71  CG  
77 1 Y 1 D LYS 50  ? CD  ? D LYS 71  CD  
78 1 Y 1 D LYS 50  ? CE  ? D LYS 71  CE  
79 1 Y 1 D LYS 50  ? NZ  ? D LYS 71  NZ  
80 1 Y 1 D SER 152 ? OG  ? D SER 173 OG  
81 1 Y 1 D VAL 211 ? CG1 ? D VAL 232 CG1 
82 1 Y 1 D VAL 211 ? CG2 ? D VAL 232 CG2 
83 1 Y 1 D GLU 216 ? CG  ? D GLU 237 CG  
84 1 Y 1 D GLU 216 ? CD  ? D GLU 237 CD  
85 1 Y 1 D GLU 216 ? OE1 ? D GLU 237 OE1 
86 1 Y 1 D GLU 216 ? OE2 ? D GLU 237 OE2 
87 1 Y 1 D GLU 217 ? CG  ? D GLU 238 CG  
88 1 Y 1 D GLU 217 ? CD  ? D GLU 238 CD  
89 1 Y 1 D GLU 217 ? OE1 ? D GLU 238 OE1 
90 1 Y 1 D GLU 217 ? OE2 ? D GLU 238 OE2 
91 1 Y 1 D ARG 223 ? CG  ? D ARG 244 CG  
92 1 Y 1 D ARG 223 ? CD  ? D ARG 244 CD  
93 1 Y 1 D ARG 223 ? NE  ? D ARG 244 NE  
94 1 Y 1 D ARG 223 ? CZ  ? D ARG 244 CZ  
95 1 Y 1 D ARG 223 ? NH1 ? D ARG 244 NH1 
96 1 Y 1 D ARG 223 ? NH2 ? D ARG 244 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   115.26 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RHV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.523 
_cell.length_a_esd                 ? 
_cell.length_b                     89.451 
_cell.length_b_esd                 ? 
_cell.length_c                     82.632 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8RHV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8RHV 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.92 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          36.04 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.6-2.5 M sodium acetate and 0.1 M sodium citrate, pH 5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            297 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-13 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Double Crystal' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.95374 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95374 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          27.4 
_reflns.entry_id                                       8RHV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.70 
_reflns.d_resolution_low                               89.45 
_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                                     106873 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     2.0 
_reflns.percent_possible_obs                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.2 
_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                                0.042 
_reflns.pdbx_Rpim_I_all                                0.024 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.034 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.70 
_reflns_shell.d_res_low                                     1.73 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5251 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               5.8 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.851 
_reflns_shell.pdbx_Rpim_I_all                               0.483 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.808 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.696 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.00 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.01 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.01 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               33.023 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.972 
_refine.correlation_coeff_Fo_to_Fc_free          0.960 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8RHV 
_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                            1.70 
_refine.ls_d_res_low                             74.73 
_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                     101395 
_refine.ls_number_reflns_R_free                  5445 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.19 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18361 
_refine.ls_R_factor_R_free                       0.22120 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18157 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.109 
_refine.pdbx_overall_ESU_R_Free                  0.109 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             3.058 
_refine.overall_SU_ML                            0.094 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        8RHV 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.22 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        74.73 
_refine_hist.number_atoms_solvent             564 
_refine_hist.number_atoms_total               8156 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        7334 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         258 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  0.012  7781  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.873  1.809  10644 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.419  5.000  1007  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 5.002  5.000  63    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.883 10.000 1178  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.136  0.200  1280  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  5758  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.065  3.132  4001  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.086  5.597  4982  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.587  3.368  3780  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.075  35.21  12355 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.700 
_refine_ls_shell.d_res_low                        1.744 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             383 
_refine_ls_shell.number_reflns_R_work             7444 
_refine_ls_shell.percent_reflns_obs               98.33 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.362 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.373 
# 
_struct.entry_id                     8RHV 
_struct.title                        'Crystal Structure of Trypanosoma brucei PTR1 in complex with the cofactor and inhibitor P30' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8RHV 
_struct_keywords.text            'Trypanosoma brucei, PTR1, Pteridine reductase, cofactor, NADPH, inhibitor, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
L N N 2 ? 
M N N 2 ? 
N N N 4 ? 
O N N 5 ? 
P N N 5 ? 
Q N N 5 ? 
R N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    O76290_TRYBB 
_struct_ref.pdbx_db_accession          O76290 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MEAPAAVVTGAAKRIGRAIAVKLHQTGYRVVIHYHNSAEAAVSLADELNKERSNTAVVCQADLTNSNVLPASCEEIINSC
FRAFGRCDVLVNNASAFYPTPLVQGDHEDNSNGKTVETQVAELIGTNAIAPFLLTMSFAQRQKGTNPNCTSSNLSIVNLC
DAMVDQPCMAFSLYNMGKHALVGLTQSAALELAPYGIRVNGVAPGVSLLPVAMGEEEKDKWRRKVPLGRREASAEQIADA
VIFLVSGSAQYITGSIIKVDGGLSLVHA
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8RHV A 22 ? 289 ? O76290 1 ? 268 ? 1 268 
2 1 8RHV B 22 ? 289 ? O76290 1 ? 268 ? 1 268 
3 1 8RHV C 22 ? 289 ? O76290 1 ? 268 ? 1 268 
4 1 8RHV D 22 ? 289 ? O76290 1 ? 268 ? 1 268 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8RHV MET A 1  ? UNP O76290 ? ? 'initiating methionine' -20 1  
1 8RHV GLY A 2  ? UNP O76290 ? ? 'expression tag'        -19 2  
1 8RHV SER A 3  ? UNP O76290 ? ? 'expression tag'        -18 3  
1 8RHV SER A 4  ? UNP O76290 ? ? 'expression tag'        -17 4  
1 8RHV HIS A 5  ? UNP O76290 ? ? 'expression tag'        -16 5  
1 8RHV HIS A 6  ? UNP O76290 ? ? 'expression tag'        -15 6  
1 8RHV HIS A 7  ? UNP O76290 ? ? 'expression tag'        -14 7  
1 8RHV HIS A 8  ? UNP O76290 ? ? 'expression tag'        -13 8  
1 8RHV HIS A 9  ? UNP O76290 ? ? 'expression tag'        -12 9  
1 8RHV HIS A 10 ? UNP O76290 ? ? 'expression tag'        -11 10 
1 8RHV SER A 11 ? UNP O76290 ? ? 'expression tag'        -10 11 
1 8RHV SER A 12 ? UNP O76290 ? ? 'expression tag'        -9  12 
1 8RHV GLY A 13 ? UNP O76290 ? ? 'expression tag'        -8  13 
1 8RHV LEU A 14 ? UNP O76290 ? ? 'expression tag'        -7  14 
1 8RHV VAL A 15 ? UNP O76290 ? ? 'expression tag'        -6  15 
1 8RHV PRO A 16 ? UNP O76290 ? ? 'expression tag'        -5  16 
1 8RHV ARG A 17 ? UNP O76290 ? ? 'expression tag'        -4  17 
1 8RHV GLY A 18 ? UNP O76290 ? ? 'expression tag'        -3  18 
1 8RHV SER A 19 ? UNP O76290 ? ? 'expression tag'        -2  19 
1 8RHV HIS A 20 ? UNP O76290 ? ? 'expression tag'        -1  20 
1 8RHV MET A 21 ? UNP O76290 ? ? 'expression tag'        0   21 
2 8RHV MET B 1  ? UNP O76290 ? ? 'initiating methionine' -20 22 
2 8RHV GLY B 2  ? UNP O76290 ? ? 'expression tag'        -19 23 
2 8RHV SER B 3  ? UNP O76290 ? ? 'expression tag'        -18 24 
2 8RHV SER B 4  ? UNP O76290 ? ? 'expression tag'        -17 25 
2 8RHV HIS B 5  ? UNP O76290 ? ? 'expression tag'        -16 26 
2 8RHV HIS B 6  ? UNP O76290 ? ? 'expression tag'        -15 27 
2 8RHV HIS B 7  ? UNP O76290 ? ? 'expression tag'        -14 28 
2 8RHV HIS B 8  ? UNP O76290 ? ? 'expression tag'        -13 29 
2 8RHV HIS B 9  ? UNP O76290 ? ? 'expression tag'        -12 30 
2 8RHV HIS B 10 ? UNP O76290 ? ? 'expression tag'        -11 31 
2 8RHV SER B 11 ? UNP O76290 ? ? 'expression tag'        -10 32 
2 8RHV SER B 12 ? UNP O76290 ? ? 'expression tag'        -9  33 
2 8RHV GLY B 13 ? UNP O76290 ? ? 'expression tag'        -8  34 
2 8RHV LEU B 14 ? UNP O76290 ? ? 'expression tag'        -7  35 
2 8RHV VAL B 15 ? UNP O76290 ? ? 'expression tag'        -6  36 
2 8RHV PRO B 16 ? UNP O76290 ? ? 'expression tag'        -5  37 
2 8RHV ARG B 17 ? UNP O76290 ? ? 'expression tag'        -4  38 
2 8RHV GLY B 18 ? UNP O76290 ? ? 'expression tag'        -3  39 
2 8RHV SER B 19 ? UNP O76290 ? ? 'expression tag'        -2  40 
2 8RHV HIS B 20 ? UNP O76290 ? ? 'expression tag'        -1  41 
2 8RHV MET B 21 ? UNP O76290 ? ? 'expression tag'        0   42 
3 8RHV MET C 1  ? UNP O76290 ? ? 'initiating methionine' -20 43 
3 8RHV GLY C 2  ? UNP O76290 ? ? 'expression tag'        -19 44 
3 8RHV SER C 3  ? UNP O76290 ? ? 'expression tag'        -18 45 
3 8RHV SER C 4  ? UNP O76290 ? ? 'expression tag'        -17 46 
3 8RHV HIS C 5  ? UNP O76290 ? ? 'expression tag'        -16 47 
3 8RHV HIS C 6  ? UNP O76290 ? ? 'expression tag'        -15 48 
3 8RHV HIS C 7  ? UNP O76290 ? ? 'expression tag'        -14 49 
3 8RHV HIS C 8  ? UNP O76290 ? ? 'expression tag'        -13 50 
3 8RHV HIS C 9  ? UNP O76290 ? ? 'expression tag'        -12 51 
3 8RHV HIS C 10 ? UNP O76290 ? ? 'expression tag'        -11 52 
3 8RHV SER C 11 ? UNP O76290 ? ? 'expression tag'        -10 53 
3 8RHV SER C 12 ? UNP O76290 ? ? 'expression tag'        -9  54 
3 8RHV GLY C 13 ? UNP O76290 ? ? 'expression tag'        -8  55 
3 8RHV LEU C 14 ? UNP O76290 ? ? 'expression tag'        -7  56 
3 8RHV VAL C 15 ? UNP O76290 ? ? 'expression tag'        -6  57 
3 8RHV PRO C 16 ? UNP O76290 ? ? 'expression tag'        -5  58 
3 8RHV ARG C 17 ? UNP O76290 ? ? 'expression tag'        -4  59 
3 8RHV GLY C 18 ? UNP O76290 ? ? 'expression tag'        -3  60 
3 8RHV SER C 19 ? UNP O76290 ? ? 'expression tag'        -2  61 
3 8RHV HIS C 20 ? UNP O76290 ? ? 'expression tag'        -1  62 
3 8RHV MET C 21 ? UNP O76290 ? ? 'expression tag'        0   63 
4 8RHV MET D 1  ? UNP O76290 ? ? 'initiating methionine' -20 64 
4 8RHV GLY D 2  ? UNP O76290 ? ? 'expression tag'        -19 65 
4 8RHV SER D 3  ? UNP O76290 ? ? 'expression tag'        -18 66 
4 8RHV SER D 4  ? UNP O76290 ? ? 'expression tag'        -17 67 
4 8RHV HIS D 5  ? UNP O76290 ? ? 'expression tag'        -16 68 
4 8RHV HIS D 6  ? UNP O76290 ? ? 'expression tag'        -15 69 
4 8RHV HIS D 7  ? UNP O76290 ? ? 'expression tag'        -14 70 
4 8RHV HIS D 8  ? UNP O76290 ? ? 'expression tag'        -13 71 
4 8RHV HIS D 9  ? UNP O76290 ? ? 'expression tag'        -12 72 
4 8RHV HIS D 10 ? UNP O76290 ? ? 'expression tag'        -11 73 
4 8RHV SER D 11 ? UNP O76290 ? ? 'expression tag'        -10 74 
4 8RHV SER D 12 ? UNP O76290 ? ? 'expression tag'        -9  75 
4 8RHV GLY D 13 ? UNP O76290 ? ? 'expression tag'        -8  76 
4 8RHV LEU D 14 ? UNP O76290 ? ? 'expression tag'        -7  77 
4 8RHV VAL D 15 ? UNP O76290 ? ? 'expression tag'        -6  78 
4 8RHV PRO D 16 ? UNP O76290 ? ? 'expression tag'        -5  79 
4 8RHV ARG D 17 ? UNP O76290 ? ? 'expression tag'        -4  80 
4 8RHV GLY D 18 ? UNP O76290 ? ? 'expression tag'        -3  81 
4 8RHV SER D 19 ? UNP O76290 ? ? 'expression tag'        -2  82 
4 8RHV HIS D 20 ? UNP O76290 ? ? 'expression tag'        -1  83 
4 8RHV MET D 21 ? UNP O76290 ? ? 'expression tag'        0   84 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 20200 ? 
1 MORE         -130  ? 
1 'SSA (A^2)'  31700 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LYS A 34  ? THR A 47  ? LYS A 13  THR A 26  1 ? 14 
HELX_P HELX_P2  AA2 SER A 58  ? ARG A 73  ? SER A 37  ARG A 52  1 ? 16 
HELX_P HELX_P3  AA3 VAL A 89  ? GLY A 106 ? VAL A 68  GLY A 85  1 ? 18 
HELX_P HELX_P4  AA4 THR A 136 ? ALA A 149 ? THR A 115 ALA A 128 1 ? 14 
HELX_P HELX_P5  AA5 ALA A 149 ? ARG A 162 ? ALA A 128 ARG A 141 1 ? 14 
HELX_P HELX_P6  AA6 PHE A 192 ? ALA A 214 ? PHE A 171 ALA A 193 1 ? 23 
HELX_P HELX_P7  AA7 PRO A 215 ? GLY A 217 ? PRO A 194 GLY A 196 5 ? 3  
HELX_P HELX_P8  AA8 GLY A 235 ? ARG A 244 ? GLY A 214 ARG A 223 1 ? 10 
HELX_P HELX_P9  AA9 SER A 254 ? SER A 267 ? SER A 233 SER A 246 1 ? 14 
HELX_P HELX_P10 AB1 GLY A 268 ? GLN A 271 ? GLY A 247 GLN A 250 5 ? 4  
HELX_P HELX_P11 AB2 GLY A 283 ? VAL A 287 ? GLY A 262 VAL A 266 5 ? 5  
HELX_P HELX_P12 AB3 LYS B 34  ? GLY B 48  ? LYS B 13  GLY B 27  1 ? 15 
HELX_P HELX_P13 AB4 SER B 58  ? ARG B 73  ? SER B 37  ARG B 52  1 ? 16 
HELX_P HELX_P14 AB5 VAL B 89  ? GLY B 106 ? VAL B 68  GLY B 85  1 ? 18 
HELX_P HELX_P15 AB6 THR B 136 ? ALA B 149 ? THR B 115 ALA B 128 1 ? 14 
HELX_P HELX_P16 AB7 ALA B 149 ? ARG B 162 ? ALA B 128 ARG B 141 1 ? 14 
HELX_P HELX_P17 AB8 PHE B 192 ? ALA B 214 ? PHE B 171 ALA B 193 1 ? 23 
HELX_P HELX_P18 AB9 GLY B 235 ? ARG B 244 ? GLY B 214 ARG B 223 1 ? 10 
HELX_P HELX_P19 AC1 SER B 254 ? SER B 267 ? SER B 233 SER B 246 1 ? 14 
HELX_P HELX_P20 AC2 GLY B 268 ? GLN B 271 ? GLY B 247 GLN B 250 5 ? 4  
HELX_P HELX_P21 AC3 GLY B 283 ? VAL B 287 ? GLY B 262 VAL B 266 5 ? 5  
HELX_P HELX_P22 AC4 LYS C 34  ? GLY C 48  ? LYS C 13  GLY C 27  1 ? 15 
HELX_P HELX_P23 AC5 SER C 58  ? ARG C 73  ? SER C 37  ARG C 52  1 ? 16 
HELX_P HELX_P24 AC6 VAL C 89  ? GLY C 106 ? VAL C 68  GLY C 85  1 ? 18 
HELX_P HELX_P25 AC7 THR C 136 ? ILE C 145 ? THR C 115 ILE C 124 1 ? 10 
HELX_P HELX_P26 AC8 ALA C 149 ? ARG C 162 ? ALA C 128 ARG C 141 1 ? 14 
HELX_P HELX_P27 AC9 PHE C 192 ? ALA C 214 ? PHE C 171 ALA C 193 1 ? 23 
HELX_P HELX_P28 AD1 GLY C 235 ? ARG C 244 ? GLY C 214 ARG C 223 1 ? 10 
HELX_P HELX_P29 AD2 SER C 254 ? SER C 267 ? SER C 233 SER C 246 1 ? 14 
HELX_P HELX_P30 AD3 GLY C 268 ? GLN C 271 ? GLY C 247 GLN C 250 5 ? 4  
HELX_P HELX_P31 AD4 GLY C 283 ? VAL C 287 ? GLY C 262 VAL C 266 5 ? 5  
HELX_P HELX_P32 AD5 LYS D 34  ? THR D 47  ? LYS D 13  THR D 26  1 ? 14 
HELX_P HELX_P33 AD6 SER D 58  ? ARG D 73  ? SER D 37  ARG D 52  1 ? 16 
HELX_P HELX_P34 AD7 VAL D 89  ? GLY D 106 ? VAL D 68  GLY D 85  1 ? 18 
HELX_P HELX_P35 AD8 THR D 136 ? ALA D 149 ? THR D 115 ALA D 128 1 ? 14 
HELX_P HELX_P36 AD9 ALA D 149 ? ARG D 162 ? ALA D 128 ARG D 141 1 ? 14 
HELX_P HELX_P37 AE1 PHE D 192 ? ALA D 214 ? PHE D 171 ALA D 193 1 ? 23 
HELX_P HELX_P38 AE2 GLY D 235 ? ARG D 244 ? GLY D 214 ARG D 223 1 ? 10 
HELX_P HELX_P39 AE3 SER D 254 ? SER D 267 ? SER D 233 SER D 246 1 ? 14 
HELX_P HELX_P40 AE4 GLY D 268 ? GLN D 271 ? GLY D 247 GLN D 250 5 ? 4  
HELX_P HELX_P41 AE5 GLY D 283 ? VAL D 287 ? GLY D 262 VAL D 266 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
AA3 ? 7 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? parallel 
AA2 5 6 ? parallel 
AA2 6 7 ? parallel 
AA3 1 2 ? parallel 
AA3 2 3 ? parallel 
AA3 3 4 ? parallel 
AA3 4 5 ? parallel 
AA3 5 6 ? parallel 
AA3 6 7 ? parallel 
AA4 1 2 ? parallel 
AA4 2 3 ? parallel 
AA4 3 4 ? parallel 
AA4 4 5 ? parallel 
AA4 5 6 ? parallel 
AA4 6 7 ? parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 77  ? GLN A 81  ? ALA A 56  GLN A 60  
AA1 2 ARG A 50  ? TYR A 55  ? ARG A 29  TYR A 34  
AA1 3 ALA A 26  ? VAL A 29  ? ALA A 5   VAL A 8   
AA1 4 VAL A 110 ? ASN A 113 ? VAL A 89  ASN A 92  
AA1 5 SER A 176 ? LEU A 180 ? SER A 155 LEU A 159 
AA1 6 ARG A 219 ? PRO A 225 ? ARG A 198 PRO A 204 
AA1 7 ILE A 277 ? VAL A 280 ? ILE A 256 VAL A 259 
AA2 1 ALA B 77  ? GLN B 81  ? ALA B 56  GLN B 60  
AA2 2 ARG B 50  ? TYR B 55  ? ARG B 29  TYR B 34  
AA2 3 ALA B 26  ? VAL B 29  ? ALA B 5   VAL B 8   
AA2 4 VAL B 110 ? ASN B 113 ? VAL B 89  ASN B 92  
AA2 5 LEU B 175 ? LEU B 180 ? LEU B 154 LEU B 159 
AA2 6 ILE B 218 ? PRO B 225 ? ILE B 197 PRO B 204 
AA2 7 ILE B 277 ? VAL B 280 ? ILE B 256 VAL B 259 
AA3 1 ALA C 77  ? GLN C 81  ? ALA C 56  GLN C 60  
AA3 2 ARG C 50  ? TYR C 55  ? ARG C 29  TYR C 34  
AA3 3 ALA C 26  ? VAL C 29  ? ALA C 5   VAL C 8   
AA3 4 VAL C 110 ? ASN C 113 ? VAL C 89  ASN C 92  
AA3 5 LEU C 175 ? LEU C 180 ? LEU C 154 LEU C 159 
AA3 6 ILE C 218 ? PRO C 225 ? ILE C 197 PRO C 204 
AA3 7 ILE C 277 ? VAL C 280 ? ILE C 256 VAL C 259 
AA4 1 ALA D 77  ? GLN D 81  ? ALA D 56  GLN D 60  
AA4 2 ARG D 50  ? TYR D 55  ? ARG D 29  TYR D 34  
AA4 3 ALA D 26  ? VAL D 29  ? ALA D 5   VAL D 8   
AA4 4 VAL D 110 ? ASN D 113 ? VAL D 89  ASN D 92  
AA4 5 LEU D 175 ? LEU D 180 ? LEU D 154 LEU D 159 
AA4 6 ILE D 218 ? PRO D 225 ? ILE D 197 PRO D 204 
AA4 7 ILE D 277 ? VAL D 280 ? ILE D 256 VAL D 259 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 78  ? O VAL A 57  N ILE A 53  ? N ILE A 32  
AA1 2 3 O ARG A 50  ? O ARG A 29  N ALA A 27  ? N ALA A 6   
AA1 3 4 N VAL A 28  ? N VAL A 7   O VAL A 112 ? O VAL A 91  
AA1 4 5 N ASN A 113 ? N ASN A 92  O LEU A 180 ? O LEU A 159 
AA1 5 6 N ASN A 179 ? N ASN A 158 O ASN A 221 ? O ASN A 200 
AA1 6 7 N ALA A 224 ? N ALA A 203 O ILE A 278 ? O ILE A 257 
AA2 1 2 O VAL B 78  ? O VAL B 57  N ILE B 53  ? N ILE B 32  
AA2 2 3 O VAL B 52  ? O VAL B 31  N ALA B 27  ? N ALA B 6   
AA2 3 4 N VAL B 28  ? N VAL B 7   O VAL B 112 ? O VAL B 91  
AA2 4 5 N ASN B 113 ? N ASN B 92  O LEU B 180 ? O LEU B 159 
AA2 5 6 N ASN B 179 ? N ASN B 158 O ASN B 221 ? O ASN B 200 
AA2 6 7 N ALA B 224 ? N ALA B 203 O ILE B 278 ? O ILE B 257 
AA3 1 2 O VAL C 78  ? O VAL C 57  N ILE C 53  ? N ILE C 32  
AA3 2 3 O ARG C 50  ? O ARG C 29  N ALA C 27  ? N ALA C 6   
AA3 3 4 N VAL C 28  ? N VAL C 7   O VAL C 112 ? O VAL C 91  
AA3 4 5 N LEU C 111 ? N LEU C 90  O VAL C 178 ? O VAL C 157 
AA3 5 6 N ASN C 179 ? N ASN C 158 O ASN C 221 ? O ASN C 200 
AA3 6 7 N ALA C 224 ? N ALA C 203 O VAL C 280 ? O VAL C 259 
AA4 1 2 O VAL D 78  ? O VAL D 57  N ILE D 53  ? N ILE D 32  
AA4 2 3 O VAL D 52  ? O VAL D 31  N ALA D 27  ? N ALA D 6   
AA4 3 4 N VAL D 28  ? N VAL D 7   O VAL D 112 ? O VAL D 91  
AA4 4 5 N ASN D 113 ? N ASN D 92  O LEU D 180 ? O LEU D 159 
AA4 5 6 N ILE D 177 ? N ILE D 156 O ARG D 219 ? O ARG D 198 
AA4 6 7 N GLY D 222 ? N GLY D 201 O ILE D 278 ? O ILE D 257 
# 
_pdbx_entry_details.entry_id                   8RHV 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 14  ? ? 56.43   -135.49 
2  1 HIS A 35  ? ? -115.45 -71.70  
3  1 ALA A 128 ? ? -140.05 -50.01  
4  1 ASN A 153 ? ? -151.74 79.05   
5  1 CYS A 160 ? ? -99.79  -154.63 
6  1 SER A 207 ? ? -123.10 -139.01 
7  1 ARG B 14  ? ? 54.64   -130.38 
8  1 ALA B 128 ? ? -139.85 -55.40  
9  1 CYS B 160 ? ? -101.05 -157.35 
10 1 SER B 207 ? ? -119.10 -142.01 
11 1 ARG C 14  ? ? 57.84   -129.91 
12 1 HIS C 35  ? ? -107.87 -72.47  
13 1 SER C 37  ? ? -100.98 61.61   
14 1 ALA C 128 ? ? -137.10 -47.91  
15 1 CYS C 160 ? ? -97.64  -147.36 
16 1 SER C 207 ? ? -109.11 -152.17 
17 1 LEU C 208 ? ? -36.72  120.77  
18 1 ARG D 14  ? ? 53.05   -127.45 
19 1 HIS D 35  ? ? -114.39 -73.40  
20 1 ALA D 128 ? ? -137.57 -51.89  
21 1 CYS D 160 ? ? -99.68  -150.84 
22 1 SER D 207 ? ? -121.39 -147.23 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       574 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   9.90 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET -20 ? A MET 1   
2   1 Y 1 A GLY -19 ? A GLY 2   
3   1 Y 1 A SER -18 ? A SER 3   
4   1 Y 1 A SER -17 ? A SER 4   
5   1 Y 1 A HIS -16 ? A HIS 5   
6   1 Y 1 A HIS -15 ? A HIS 6   
7   1 Y 1 A HIS -14 ? A HIS 7   
8   1 Y 1 A HIS -13 ? A HIS 8   
9   1 Y 1 A HIS -12 ? A HIS 9   
10  1 Y 1 A HIS -11 ? A HIS 10  
11  1 Y 1 A SER -10 ? A SER 11  
12  1 Y 1 A SER -9  ? A SER 12  
13  1 Y 1 A GLY -8  ? A GLY 13  
14  1 Y 1 A LEU -7  ? A LEU 14  
15  1 Y 1 A VAL -6  ? A VAL 15  
16  1 Y 1 A PRO -5  ? A PRO 16  
17  1 Y 1 A ARG -4  ? A ARG 17  
18  1 Y 1 A GLY -3  ? A GLY 18  
19  1 Y 1 A SER -2  ? A SER 19  
20  1 Y 1 A HIS -1  ? A HIS 20  
21  1 Y 1 A MET 0   ? A MET 21  
22  1 Y 1 A MET 1   ? A MET 22  
23  1 Y 1 A GLY 105 ? A GLY 126 
24  1 Y 1 A ASP 106 ? A ASP 127 
25  1 Y 1 A HIS 107 ? A HIS 128 
26  1 Y 1 A GLU 108 ? A GLU 129 
27  1 Y 1 A ASP 109 ? A ASP 130 
28  1 Y 1 A ASN 110 ? A ASN 131 
29  1 Y 1 A SER 111 ? A SER 132 
30  1 Y 1 A ASN 112 ? A ASN 133 
31  1 Y 1 A LYS 143 ? A LYS 164 
32  1 Y 1 A GLY 144 ? A GLY 165 
33  1 Y 1 A THR 145 ? A THR 166 
34  1 Y 1 A ASN 146 ? A ASN 167 
35  1 Y 1 A PRO 147 ? A PRO 168 
36  1 Y 1 A ASN 148 ? A ASN 169 
37  1 Y 1 A CYS 149 ? A CYS 170 
38  1 Y 1 A THR 150 ? A THR 171 
39  1 Y 1 A SER 151 ? A SER 172 
40  1 Y 1 B MET -20 ? B MET 1   
41  1 Y 1 B GLY -19 ? B GLY 2   
42  1 Y 1 B SER -18 ? B SER 3   
43  1 Y 1 B SER -17 ? B SER 4   
44  1 Y 1 B HIS -16 ? B HIS 5   
45  1 Y 1 B HIS -15 ? B HIS 6   
46  1 Y 1 B HIS -14 ? B HIS 7   
47  1 Y 1 B HIS -13 ? B HIS 8   
48  1 Y 1 B HIS -12 ? B HIS 9   
49  1 Y 1 B HIS -11 ? B HIS 10  
50  1 Y 1 B SER -10 ? B SER 11  
51  1 Y 1 B SER -9  ? B SER 12  
52  1 Y 1 B GLY -8  ? B GLY 13  
53  1 Y 1 B LEU -7  ? B LEU 14  
54  1 Y 1 B VAL -6  ? B VAL 15  
55  1 Y 1 B PRO -5  ? B PRO 16  
56  1 Y 1 B ARG -4  ? B ARG 17  
57  1 Y 1 B GLY -3  ? B GLY 18  
58  1 Y 1 B SER -2  ? B SER 19  
59  1 Y 1 B HIS -1  ? B HIS 20  
60  1 Y 1 B MET 0   ? B MET 21  
61  1 Y 1 B MET 1   ? B MET 22  
62  1 Y 1 B GLN 104 ? B GLN 125 
63  1 Y 1 B GLY 105 ? B GLY 126 
64  1 Y 1 B ASP 106 ? B ASP 127 
65  1 Y 1 B HIS 107 ? B HIS 128 
66  1 Y 1 B GLU 108 ? B GLU 129 
67  1 Y 1 B ASP 109 ? B ASP 130 
68  1 Y 1 B ASN 110 ? B ASN 131 
69  1 Y 1 B SER 111 ? B SER 132 
70  1 Y 1 B ASN 112 ? B ASN 133 
71  1 Y 1 B GLY 144 ? B GLY 165 
72  1 Y 1 B THR 145 ? B THR 166 
73  1 Y 1 B ASN 146 ? B ASN 167 
74  1 Y 1 B PRO 147 ? B PRO 168 
75  1 Y 1 B ASN 148 ? B ASN 169 
76  1 Y 1 B CYS 149 ? B CYS 170 
77  1 Y 1 B THR 150 ? B THR 171 
78  1 Y 1 B SER 151 ? B SER 172 
79  1 Y 1 C MET -20 ? C MET 1   
80  1 Y 1 C GLY -19 ? C GLY 2   
81  1 Y 1 C SER -18 ? C SER 3   
82  1 Y 1 C SER -17 ? C SER 4   
83  1 Y 1 C HIS -16 ? C HIS 5   
84  1 Y 1 C HIS -15 ? C HIS 6   
85  1 Y 1 C HIS -14 ? C HIS 7   
86  1 Y 1 C HIS -13 ? C HIS 8   
87  1 Y 1 C HIS -12 ? C HIS 9   
88  1 Y 1 C HIS -11 ? C HIS 10  
89  1 Y 1 C SER -10 ? C SER 11  
90  1 Y 1 C SER -9  ? C SER 12  
91  1 Y 1 C GLY -8  ? C GLY 13  
92  1 Y 1 C LEU -7  ? C LEU 14  
93  1 Y 1 C VAL -6  ? C VAL 15  
94  1 Y 1 C PRO -5  ? C PRO 16  
95  1 Y 1 C ARG -4  ? C ARG 17  
96  1 Y 1 C GLY -3  ? C GLY 18  
97  1 Y 1 C SER -2  ? C SER 19  
98  1 Y 1 C HIS -1  ? C HIS 20  
99  1 Y 1 C MET 0   ? C MET 21  
100 1 Y 1 C MET 1   ? C MET 22  
101 1 Y 1 C GLN 104 ? C GLN 125 
102 1 Y 1 C GLY 105 ? C GLY 126 
103 1 Y 1 C ASP 106 ? C ASP 127 
104 1 Y 1 C HIS 107 ? C HIS 128 
105 1 Y 1 C GLU 108 ? C GLU 129 
106 1 Y 1 C ASP 109 ? C ASP 130 
107 1 Y 1 C ASN 110 ? C ASN 131 
108 1 Y 1 C SER 111 ? C SER 132 
109 1 Y 1 C ASN 112 ? C ASN 133 
110 1 Y 1 C GLY 113 ? C GLY 134 
111 1 Y 1 C LYS 143 ? C LYS 164 
112 1 Y 1 C GLY 144 ? C GLY 165 
113 1 Y 1 C THR 145 ? C THR 166 
114 1 Y 1 C ASN 146 ? C ASN 167 
115 1 Y 1 C PRO 147 ? C PRO 168 
116 1 Y 1 C ASN 148 ? C ASN 169 
117 1 Y 1 C CYS 149 ? C CYS 170 
118 1 Y 1 C THR 150 ? C THR 171 
119 1 Y 1 C SER 151 ? C SER 172 
120 1 Y 1 D MET -20 ? D MET 1   
121 1 Y 1 D GLY -19 ? D GLY 2   
122 1 Y 1 D SER -18 ? D SER 3   
123 1 Y 1 D SER -17 ? D SER 4   
124 1 Y 1 D HIS -16 ? D HIS 5   
125 1 Y 1 D HIS -15 ? D HIS 6   
126 1 Y 1 D HIS -14 ? D HIS 7   
127 1 Y 1 D HIS -13 ? D HIS 8   
128 1 Y 1 D HIS -12 ? D HIS 9   
129 1 Y 1 D HIS -11 ? D HIS 10  
130 1 Y 1 D SER -10 ? D SER 11  
131 1 Y 1 D SER -9  ? D SER 12  
132 1 Y 1 D GLY -8  ? D GLY 13  
133 1 Y 1 D LEU -7  ? D LEU 14  
134 1 Y 1 D VAL -6  ? D VAL 15  
135 1 Y 1 D PRO -5  ? D PRO 16  
136 1 Y 1 D ARG -4  ? D ARG 17  
137 1 Y 1 D GLY -3  ? D GLY 18  
138 1 Y 1 D SER -2  ? D SER 19  
139 1 Y 1 D HIS -1  ? D HIS 20  
140 1 Y 1 D MET 0   ? D MET 21  
141 1 Y 1 D MET 1   ? D MET 22  
142 1 Y 1 D GLN 104 ? D GLN 125 
143 1 Y 1 D GLY 105 ? D GLY 126 
144 1 Y 1 D ASP 106 ? D ASP 127 
145 1 Y 1 D HIS 107 ? D HIS 128 
146 1 Y 1 D GLU 108 ? D GLU 129 
147 1 Y 1 D ASP 109 ? D ASP 130 
148 1 Y 1 D ASN 110 ? D ASN 131 
149 1 Y 1 D SER 111 ? D SER 132 
150 1 Y 1 D ASN 112 ? D ASN 133 
151 1 Y 1 D LYS 143 ? D LYS 164 
152 1 Y 1 D GLY 144 ? D GLY 165 
153 1 Y 1 D THR 145 ? D THR 166 
154 1 Y 1 D ASN 146 ? D ASN 167 
155 1 Y 1 D PRO 147 ? D PRO 168 
156 1 Y 1 D ASN 148 ? D ASN 169 
157 1 Y 1 D CYS 149 ? D CYS 170 
158 1 Y 1 D THR 150 ? D THR 171 
159 1 Y 1 D SER 151 ? D SER 172 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1H0U CAP  C N N 1   
A1H0U OAO  O N N 2   
A1H0U CAC  C Y N 3   
A1H0U CAQ  C Y N 4   
A1H0U CAD  C Y N 5   
A1H0U NAF  N N N 6   
A1H0U CAL  C N N 7   
A1H0U CAM  C N N 8   
A1H0U CAN  C N N 9   
A1H0U NAR  N N N 10  
A1H0U CAJ  C N N 11  
A1H0U NAK  N N N 12  
A1H0U NAI  N N N 13  
A1H0U CAG  C N N 14  
A1H0U NAH  N N N 15  
A1H0U CAE  C Y N 16  
A1H0U CAA  C Y N 17  
A1H0U CAB  C Y N 18  
A1H0U H1   H N N 19  
A1H0U H2   H N N 20  
A1H0U H3   H N N 21  
A1H0U H4   H N N 22  
A1H0U H5   H N N 23  
A1H0U H6   H N N 24  
A1H0U H7   H N N 25  
A1H0U H8   H N N 26  
A1H0U H9   H N N 27  
A1H0U H10  H N N 28  
A1H0U H12  H N N 29  
A1H0U H13  H N N 30  
A1H0U H15  H N N 31  
A1H0U H16  H N N 32  
A1H0U H17  H N N 33  
ACT   C    C N N 34  
ACT   O    O N N 35  
ACT   OXT  O N N 36  
ACT   CH3  C N N 37  
ACT   H1   H N N 38  
ACT   H2   H N N 39  
ACT   H3   H N N 40  
ALA   N    N N N 41  
ALA   CA   C N S 42  
ALA   C    C N N 43  
ALA   O    O N N 44  
ALA   CB   C N N 45  
ALA   OXT  O N N 46  
ALA   H    H N N 47  
ALA   H2   H N N 48  
ALA   HA   H N N 49  
ALA   HB1  H N N 50  
ALA   HB2  H N N 51  
ALA   HB3  H N N 52  
ALA   HXT  H N N 53  
ARG   N    N N N 54  
ARG   CA   C N S 55  
ARG   C    C N N 56  
ARG   O    O N N 57  
ARG   CB   C N N 58  
ARG   CG   C N N 59  
ARG   CD   C N N 60  
ARG   NE   N N N 61  
ARG   CZ   C N N 62  
ARG   NH1  N N N 63  
ARG   NH2  N N N 64  
ARG   OXT  O N N 65  
ARG   H    H N N 66  
ARG   H2   H N N 67  
ARG   HA   H N N 68  
ARG   HB2  H N N 69  
ARG   HB3  H N N 70  
ARG   HG2  H N N 71  
ARG   HG3  H N N 72  
ARG   HD2  H N N 73  
ARG   HD3  H N N 74  
ARG   HE   H N N 75  
ARG   HH11 H N N 76  
ARG   HH12 H N N 77  
ARG   HH21 H N N 78  
ARG   HH22 H N N 79  
ARG   HXT  H N N 80  
ASN   N    N N N 81  
ASN   CA   C N S 82  
ASN   C    C N N 83  
ASN   O    O N N 84  
ASN   CB   C N N 85  
ASN   CG   C N N 86  
ASN   OD1  O N N 87  
ASN   ND2  N N N 88  
ASN   OXT  O N N 89  
ASN   H    H N N 90  
ASN   H2   H N N 91  
ASN   HA   H N N 92  
ASN   HB2  H N N 93  
ASN   HB3  H N N 94  
ASN   HD21 H N N 95  
ASN   HD22 H N N 96  
ASN   HXT  H N N 97  
ASP   N    N N N 98  
ASP   CA   C N S 99  
ASP   C    C N N 100 
ASP   O    O N N 101 
ASP   CB   C N N 102 
ASP   CG   C N N 103 
ASP   OD1  O N N 104 
ASP   OD2  O N N 105 
ASP   OXT  O N N 106 
ASP   H    H N N 107 
ASP   H2   H N N 108 
ASP   HA   H N N 109 
ASP   HB2  H N N 110 
ASP   HB3  H N N 111 
ASP   HD2  H N N 112 
ASP   HXT  H N N 113 
CYS   N    N N N 114 
CYS   CA   C N R 115 
CYS   C    C N N 116 
CYS   O    O N N 117 
CYS   CB   C N N 118 
CYS   SG   S N N 119 
CYS   OXT  O N N 120 
CYS   H    H N N 121 
CYS   H2   H N N 122 
CYS   HA   H N N 123 
CYS   HB2  H N N 124 
CYS   HB3  H N N 125 
CYS   HG   H N N 126 
CYS   HXT  H N N 127 
GLN   N    N N N 128 
GLN   CA   C N S 129 
GLN   C    C N N 130 
GLN   O    O N N 131 
GLN   CB   C N N 132 
GLN   CG   C N N 133 
GLN   CD   C N N 134 
GLN   OE1  O N N 135 
GLN   NE2  N N N 136 
GLN   OXT  O N N 137 
GLN   H    H N N 138 
GLN   H2   H N N 139 
GLN   HA   H N N 140 
GLN   HB2  H N N 141 
GLN   HB3  H N N 142 
GLN   HG2  H N N 143 
GLN   HG3  H N N 144 
GLN   HE21 H N N 145 
GLN   HE22 H N N 146 
GLN   HXT  H N N 147 
GLU   N    N N N 148 
GLU   CA   C N S 149 
GLU   C    C N N 150 
GLU   O    O N N 151 
GLU   CB   C N N 152 
GLU   CG   C N N 153 
GLU   CD   C N N 154 
GLU   OE1  O N N 155 
GLU   OE2  O N N 156 
GLU   OXT  O N N 157 
GLU   H    H N N 158 
GLU   H2   H N N 159 
GLU   HA   H N N 160 
GLU   HB2  H N N 161 
GLU   HB3  H N N 162 
GLU   HG2  H N N 163 
GLU   HG3  H N N 164 
GLU   HE2  H N N 165 
GLU   HXT  H N N 166 
GLY   N    N N N 167 
GLY   CA   C N N 168 
GLY   C    C N N 169 
GLY   O    O N N 170 
GLY   OXT  O N N 171 
GLY   H    H N N 172 
GLY   H2   H N N 173 
GLY   HA2  H N N 174 
GLY   HA3  H N N 175 
GLY   HXT  H N N 176 
HIS   N    N N N 177 
HIS   CA   C N S 178 
HIS   C    C N N 179 
HIS   O    O N N 180 
HIS   CB   C N N 181 
HIS   CG   C Y N 182 
HIS   ND1  N Y N 183 
HIS   CD2  C Y N 184 
HIS   CE1  C Y N 185 
HIS   NE2  N Y N 186 
HIS   OXT  O N N 187 
HIS   H    H N N 188 
HIS   H2   H N N 189 
HIS   HA   H N N 190 
HIS   HB2  H N N 191 
HIS   HB3  H N N 192 
HIS   HD1  H N N 193 
HIS   HD2  H N N 194 
HIS   HE1  H N N 195 
HIS   HE2  H N N 196 
HIS   HXT  H N N 197 
HOH   O    O N N 198 
HOH   H1   H N N 199 
HOH   H2   H N N 200 
ILE   N    N N N 201 
ILE   CA   C N S 202 
ILE   C    C N N 203 
ILE   O    O N N 204 
ILE   CB   C N S 205 
ILE   CG1  C N N 206 
ILE   CG2  C N N 207 
ILE   CD1  C N N 208 
ILE   OXT  O N N 209 
ILE   H    H N N 210 
ILE   H2   H N N 211 
ILE   HA   H N N 212 
ILE   HB   H N N 213 
ILE   HG12 H N N 214 
ILE   HG13 H N N 215 
ILE   HG21 H N N 216 
ILE   HG22 H N N 217 
ILE   HG23 H N N 218 
ILE   HD11 H N N 219 
ILE   HD12 H N N 220 
ILE   HD13 H N N 221 
ILE   HXT  H N N 222 
LEU   N    N N N 223 
LEU   CA   C N S 224 
LEU   C    C N N 225 
LEU   O    O N N 226 
LEU   CB   C N N 227 
LEU   CG   C N N 228 
LEU   CD1  C N N 229 
LEU   CD2  C N N 230 
LEU   OXT  O N N 231 
LEU   H    H N N 232 
LEU   H2   H N N 233 
LEU   HA   H N N 234 
LEU   HB2  H N N 235 
LEU   HB3  H N N 236 
LEU   HG   H N N 237 
LEU   HD11 H N N 238 
LEU   HD12 H N N 239 
LEU   HD13 H N N 240 
LEU   HD21 H N N 241 
LEU   HD22 H N N 242 
LEU   HD23 H N N 243 
LEU   HXT  H N N 244 
LYS   N    N N N 245 
LYS   CA   C N S 246 
LYS   C    C N N 247 
LYS   O    O N N 248 
LYS   CB   C N N 249 
LYS   CG   C N N 250 
LYS   CD   C N N 251 
LYS   CE   C N N 252 
LYS   NZ   N N N 253 
LYS   OXT  O N N 254 
LYS   H    H N N 255 
LYS   H2   H N N 256 
LYS   HA   H N N 257 
LYS   HB2  H N N 258 
LYS   HB3  H N N 259 
LYS   HG2  H N N 260 
LYS   HG3  H N N 261 
LYS   HD2  H N N 262 
LYS   HD3  H N N 263 
LYS   HE2  H N N 264 
LYS   HE3  H N N 265 
LYS   HZ1  H N N 266 
LYS   HZ2  H N N 267 
LYS   HZ3  H N N 268 
LYS   HXT  H N N 269 
MET   N    N N N 270 
MET   CA   C N S 271 
MET   C    C N N 272 
MET   O    O N N 273 
MET   CB   C N N 274 
MET   CG   C N N 275 
MET   SD   S N N 276 
MET   CE   C N N 277 
MET   OXT  O N N 278 
MET   H    H N N 279 
MET   H2   H N N 280 
MET   HA   H N N 281 
MET   HB2  H N N 282 
MET   HB3  H N N 283 
MET   HG2  H N N 284 
MET   HG3  H N N 285 
MET   HE1  H N N 286 
MET   HE2  H N N 287 
MET   HE3  H N N 288 
MET   HXT  H N N 289 
NDP   PA   P N S 290 
NDP   O1A  O N N 291 
NDP   O2A  O N N 292 
NDP   O5B  O N N 293 
NDP   C5B  C N N 294 
NDP   C4B  C N R 295 
NDP   O4B  O N N 296 
NDP   C3B  C N R 297 
NDP   O3B  O N N 298 
NDP   C2B  C N R 299 
NDP   O2B  O N N 300 
NDP   C1B  C N R 301 
NDP   N9A  N Y N 302 
NDP   C8A  C Y N 303 
NDP   N7A  N Y N 304 
NDP   C5A  C Y N 305 
NDP   C6A  C Y N 306 
NDP   N6A  N N N 307 
NDP   N1A  N Y N 308 
NDP   C2A  C Y N 309 
NDP   N3A  N Y N 310 
NDP   C4A  C Y N 311 
NDP   O3   O N N 312 
NDP   PN   P N S 313 
NDP   O1N  O N N 314 
NDP   O2N  O N N 315 
NDP   O5D  O N N 316 
NDP   C5D  C N N 317 
NDP   C4D  C N R 318 
NDP   O4D  O N N 319 
NDP   C3D  C N S 320 
NDP   O3D  O N N 321 
NDP   C2D  C N R 322 
NDP   O2D  O N N 323 
NDP   C1D  C N R 324 
NDP   N1N  N N N 325 
NDP   C2N  C N N 326 
NDP   C3N  C N N 327 
NDP   C7N  C N N 328 
NDP   O7N  O N N 329 
NDP   N7N  N N N 330 
NDP   C4N  C N N 331 
NDP   C5N  C N N 332 
NDP   C6N  C N N 333 
NDP   P2B  P N N 334 
NDP   O1X  O N N 335 
NDP   O2X  O N N 336 
NDP   O3X  O N N 337 
NDP   HOA2 H N N 338 
NDP   H51A H N N 339 
NDP   H52A H N N 340 
NDP   H4B  H N N 341 
NDP   H3B  H N N 342 
NDP   HO3A H N N 343 
NDP   H2B  H N N 344 
NDP   H1B  H N N 345 
NDP   H8A  H N N 346 
NDP   H61A H N N 347 
NDP   H62A H N N 348 
NDP   H2A  H N N 349 
NDP   H21N H N N 350 
NDP   H51N H N N 351 
NDP   H52N H N N 352 
NDP   H4D  H N N 353 
NDP   H3D  H N N 354 
NDP   HO3N H N N 355 
NDP   H2D  H N N 356 
NDP   HO2N H N N 357 
NDP   H1D  H N N 358 
NDP   H2N  H N N 359 
NDP   H71N H N N 360 
NDP   H72N H N N 361 
NDP   H41N H N N 362 
NDP   H42N H N N 363 
NDP   H5N  H N N 364 
NDP   H6N  H N N 365 
NDP   HOP2 H N N 366 
NDP   HOP3 H N N 367 
PHE   N    N N N 368 
PHE   CA   C N S 369 
PHE   C    C N N 370 
PHE   O    O N N 371 
PHE   CB   C N N 372 
PHE   CG   C Y N 373 
PHE   CD1  C Y N 374 
PHE   CD2  C Y N 375 
PHE   CE1  C Y N 376 
PHE   CE2  C Y N 377 
PHE   CZ   C Y N 378 
PHE   OXT  O N N 379 
PHE   H    H N N 380 
PHE   H2   H N N 381 
PHE   HA   H N N 382 
PHE   HB2  H N N 383 
PHE   HB3  H N N 384 
PHE   HD1  H N N 385 
PHE   HD2  H N N 386 
PHE   HE1  H N N 387 
PHE   HE2  H N N 388 
PHE   HZ   H N N 389 
PHE   HXT  H N N 390 
PRO   N    N N N 391 
PRO   CA   C N S 392 
PRO   C    C N N 393 
PRO   O    O N N 394 
PRO   CB   C N N 395 
PRO   CG   C N N 396 
PRO   CD   C N N 397 
PRO   OXT  O N N 398 
PRO   H    H N N 399 
PRO   HA   H N N 400 
PRO   HB2  H N N 401 
PRO   HB3  H N N 402 
PRO   HG2  H N N 403 
PRO   HG3  H N N 404 
PRO   HD2  H N N 405 
PRO   HD3  H N N 406 
PRO   HXT  H N N 407 
SER   N    N N N 408 
SER   CA   C N S 409 
SER   C    C N N 410 
SER   O    O N N 411 
SER   CB   C N N 412 
SER   OG   O N N 413 
SER   OXT  O N N 414 
SER   H    H N N 415 
SER   H2   H N N 416 
SER   HA   H N N 417 
SER   HB2  H N N 418 
SER   HB3  H N N 419 
SER   HG   H N N 420 
SER   HXT  H N N 421 
THR   N    N N N 422 
THR   CA   C N S 423 
THR   C    C N N 424 
THR   O    O N N 425 
THR   CB   C N R 426 
THR   OG1  O N N 427 
THR   CG2  C N N 428 
THR   OXT  O N N 429 
THR   H    H N N 430 
THR   H2   H N N 431 
THR   HA   H N N 432 
THR   HB   H N N 433 
THR   HG1  H N N 434 
THR   HG21 H N N 435 
THR   HG22 H N N 436 
THR   HG23 H N N 437 
THR   HXT  H N N 438 
TRP   N    N N N 439 
TRP   CA   C N S 440 
TRP   C    C N N 441 
TRP   O    O N N 442 
TRP   CB   C N N 443 
TRP   CG   C Y N 444 
TRP   CD1  C Y N 445 
TRP   CD2  C Y N 446 
TRP   NE1  N Y N 447 
TRP   CE2  C Y N 448 
TRP   CE3  C Y N 449 
TRP   CZ2  C Y N 450 
TRP   CZ3  C Y N 451 
TRP   CH2  C Y N 452 
TRP   OXT  O N N 453 
TRP   H    H N N 454 
TRP   H2   H N N 455 
TRP   HA   H N N 456 
TRP   HB2  H N N 457 
TRP   HB3  H N N 458 
TRP   HD1  H N N 459 
TRP   HE1  H N N 460 
TRP   HE3  H N N 461 
TRP   HZ2  H N N 462 
TRP   HZ3  H N N 463 
TRP   HH2  H N N 464 
TRP   HXT  H N N 465 
TYR   N    N N N 466 
TYR   CA   C N S 467 
TYR   C    C N N 468 
TYR   O    O N N 469 
TYR   CB   C N N 470 
TYR   CG   C Y N 471 
TYR   CD1  C Y N 472 
TYR   CD2  C Y N 473 
TYR   CE1  C Y N 474 
TYR   CE2  C Y N 475 
TYR   CZ   C Y N 476 
TYR   OH   O N N 477 
TYR   OXT  O N N 478 
TYR   H    H N N 479 
TYR   H2   H N N 480 
TYR   HA   H N N 481 
TYR   HB2  H N N 482 
TYR   HB3  H N N 483 
TYR   HD1  H N N 484 
TYR   HD2  H N N 485 
TYR   HE1  H N N 486 
TYR   HE2  H N N 487 
TYR   HH   H N N 488 
TYR   HXT  H N N 489 
VAL   N    N N N 490 
VAL   CA   C N S 491 
VAL   C    C N N 492 
VAL   O    O N N 493 
VAL   CB   C N N 494 
VAL   CG1  C N N 495 
VAL   CG2  C N N 496 
VAL   OXT  O N N 497 
VAL   H    H N N 498 
VAL   H2   H N N 499 
VAL   HA   H N N 500 
VAL   HB   H N N 501 
VAL   HG11 H N N 502 
VAL   HG12 H N N 503 
VAL   HG13 H N N 504 
VAL   HG21 H N N 505 
VAL   HG22 H N N 506 
VAL   HG23 H N N 507 
VAL   HXT  H N N 508 
# 
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 
A1H0U CAN CAL  sing N N 1   
A1H0U NAR CAL  sing N N 2   
A1H0U NAR CAJ  doub N N 3   
A1H0U CAL NAF  sing N N 4   
A1H0U CAL CAM  sing N N 5   
A1H0U NAF CAD  sing N N 6   
A1H0U NAF CAG  sing N N 7   
A1H0U CAQ CAD  doub Y N 8   
A1H0U CAQ CAC  sing Y N 9   
A1H0U CAJ NAK  sing N N 10  
A1H0U CAJ NAI  sing N N 11  
A1H0U CAD CAE  sing Y N 12  
A1H0U OAO CAC  sing N N 13  
A1H0U OAO CAP  sing N N 14  
A1H0U CAC CAB  doub Y N 15  
A1H0U CAG NAI  doub N N 16  
A1H0U CAG NAH  sing N N 17  
A1H0U CAE NAH  sing N N 18  
A1H0U CAE CAA  doub Y N 19  
A1H0U CAB CAA  sing Y N 20  
A1H0U CAP H1   sing N N 21  
A1H0U CAP H2   sing N N 22  
A1H0U CAP H3   sing N N 23  
A1H0U CAQ H4   sing N N 24  
A1H0U CAM H5   sing N N 25  
A1H0U CAM H6   sing N N 26  
A1H0U CAM H7   sing N N 27  
A1H0U CAN H8   sing N N 28  
A1H0U CAN H9   sing N N 29  
A1H0U CAN H10  sing N N 30  
A1H0U NAK H12  sing N N 31  
A1H0U NAK H13  sing N N 32  
A1H0U NAH H15  sing N N 33  
A1H0U CAA H16  sing N N 34  
A1H0U CAB H17  sing N N 35  
ACT   C   O    doub N N 36  
ACT   C   OXT  sing N N 37  
ACT   C   CH3  sing N N 38  
ACT   CH3 H1   sing N N 39  
ACT   CH3 H2   sing N N 40  
ACT   CH3 H3   sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
GLN   N   CA   sing N N 124 
GLN   N   H    sing N N 125 
GLN   N   H2   sing N N 126 
GLN   CA  C    sing N N 127 
GLN   CA  CB   sing N N 128 
GLN   CA  HA   sing N N 129 
GLN   C   O    doub N N 130 
GLN   C   OXT  sing N N 131 
GLN   CB  CG   sing N N 132 
GLN   CB  HB2  sing N N 133 
GLN   CB  HB3  sing N N 134 
GLN   CG  CD   sing N N 135 
GLN   CG  HG2  sing N N 136 
GLN   CG  HG3  sing N N 137 
GLN   CD  OE1  doub N N 138 
GLN   CD  NE2  sing N N 139 
GLN   NE2 HE21 sing N N 140 
GLN   NE2 HE22 sing N N 141 
GLN   OXT HXT  sing N N 142 
GLU   N   CA   sing N N 143 
GLU   N   H    sing N N 144 
GLU   N   H2   sing N N 145 
GLU   CA  C    sing N N 146 
GLU   CA  CB   sing N N 147 
GLU   CA  HA   sing N N 148 
GLU   C   O    doub N N 149 
GLU   C   OXT  sing N N 150 
GLU   CB  CG   sing N N 151 
GLU   CB  HB2  sing N N 152 
GLU   CB  HB3  sing N N 153 
GLU   CG  CD   sing N N 154 
GLU   CG  HG2  sing N N 155 
GLU   CG  HG3  sing N N 156 
GLU   CD  OE1  doub N N 157 
GLU   CD  OE2  sing N N 158 
GLU   OE2 HE2  sing N N 159 
GLU   OXT HXT  sing N N 160 
GLY   N   CA   sing N N 161 
GLY   N   H    sing N N 162 
GLY   N   H2   sing N N 163 
GLY   CA  C    sing N N 164 
GLY   CA  HA2  sing N N 165 
GLY   CA  HA3  sing N N 166 
GLY   C   O    doub N N 167 
GLY   C   OXT  sing N N 168 
GLY   OXT HXT  sing N N 169 
HIS   N   CA   sing N N 170 
HIS   N   H    sing N N 171 
HIS   N   H2   sing N N 172 
HIS   CA  C    sing N N 173 
HIS   CA  CB   sing N N 174 
HIS   CA  HA   sing N N 175 
HIS   C   O    doub N N 176 
HIS   C   OXT  sing N N 177 
HIS   CB  CG   sing N N 178 
HIS   CB  HB2  sing N N 179 
HIS   CB  HB3  sing N N 180 
HIS   CG  ND1  sing Y N 181 
HIS   CG  CD2  doub Y N 182 
HIS   ND1 CE1  doub Y N 183 
HIS   ND1 HD1  sing N N 184 
HIS   CD2 NE2  sing Y N 185 
HIS   CD2 HD2  sing N N 186 
HIS   CE1 NE2  sing Y N 187 
HIS   CE1 HE1  sing N N 188 
HIS   NE2 HE2  sing N N 189 
HIS   OXT HXT  sing N N 190 
HOH   O   H1   sing N N 191 
HOH   O   H2   sing N N 192 
ILE   N   CA   sing N N 193 
ILE   N   H    sing N N 194 
ILE   N   H2   sing N N 195 
ILE   CA  C    sing N N 196 
ILE   CA  CB   sing N N 197 
ILE   CA  HA   sing N N 198 
ILE   C   O    doub N N 199 
ILE   C   OXT  sing N N 200 
ILE   CB  CG1  sing N N 201 
ILE   CB  CG2  sing N N 202 
ILE   CB  HB   sing N N 203 
ILE   CG1 CD1  sing N N 204 
ILE   CG1 HG12 sing N N 205 
ILE   CG1 HG13 sing N N 206 
ILE   CG2 HG21 sing N N 207 
ILE   CG2 HG22 sing N N 208 
ILE   CG2 HG23 sing N N 209 
ILE   CD1 HD11 sing N N 210 
ILE   CD1 HD12 sing N N 211 
ILE   CD1 HD13 sing N N 212 
ILE   OXT HXT  sing N N 213 
LEU   N   CA   sing N N 214 
LEU   N   H    sing N N 215 
LEU   N   H2   sing N N 216 
LEU   CA  C    sing N N 217 
LEU   CA  CB   sing N N 218 
LEU   CA  HA   sing N N 219 
LEU   C   O    doub N N 220 
LEU   C   OXT  sing N N 221 
LEU   CB  CG   sing N N 222 
LEU   CB  HB2  sing N N 223 
LEU   CB  HB3  sing N N 224 
LEU   CG  CD1  sing N N 225 
LEU   CG  CD2  sing N N 226 
LEU   CG  HG   sing N N 227 
LEU   CD1 HD11 sing N N 228 
LEU   CD1 HD12 sing N N 229 
LEU   CD1 HD13 sing N N 230 
LEU   CD2 HD21 sing N N 231 
LEU   CD2 HD22 sing N N 232 
LEU   CD2 HD23 sing N N 233 
LEU   OXT HXT  sing N N 234 
LYS   N   CA   sing N N 235 
LYS   N   H    sing N N 236 
LYS   N   H2   sing N N 237 
LYS   CA  C    sing N N 238 
LYS   CA  CB   sing N N 239 
LYS   CA  HA   sing N N 240 
LYS   C   O    doub N N 241 
LYS   C   OXT  sing N N 242 
LYS   CB  CG   sing N N 243 
LYS   CB  HB2  sing N N 244 
LYS   CB  HB3  sing N N 245 
LYS   CG  CD   sing N N 246 
LYS   CG  HG2  sing N N 247 
LYS   CG  HG3  sing N N 248 
LYS   CD  CE   sing N N 249 
LYS   CD  HD2  sing N N 250 
LYS   CD  HD3  sing N N 251 
LYS   CE  NZ   sing N N 252 
LYS   CE  HE2  sing N N 253 
LYS   CE  HE3  sing N N 254 
LYS   NZ  HZ1  sing N N 255 
LYS   NZ  HZ2  sing N N 256 
LYS   NZ  HZ3  sing N N 257 
LYS   OXT HXT  sing N N 258 
MET   N   CA   sing N N 259 
MET   N   H    sing N N 260 
MET   N   H2   sing N N 261 
MET   CA  C    sing N N 262 
MET   CA  CB   sing N N 263 
MET   CA  HA   sing N N 264 
MET   C   O    doub N N 265 
MET   C   OXT  sing N N 266 
MET   CB  CG   sing N N 267 
MET   CB  HB2  sing N N 268 
MET   CB  HB3  sing N N 269 
MET   CG  SD   sing N N 270 
MET   CG  HG2  sing N N 271 
MET   CG  HG3  sing N N 272 
MET   SD  CE   sing N N 273 
MET   CE  HE1  sing N N 274 
MET   CE  HE2  sing N N 275 
MET   CE  HE3  sing N N 276 
MET   OXT HXT  sing N N 277 
NDP   PA  O1A  doub N N 278 
NDP   PA  O2A  sing N N 279 
NDP   PA  O5B  sing N N 280 
NDP   PA  O3   sing N N 281 
NDP   O2A HOA2 sing N N 282 
NDP   O5B C5B  sing N N 283 
NDP   C5B C4B  sing N N 284 
NDP   C5B H51A sing N N 285 
NDP   C5B H52A sing N N 286 
NDP   C4B O4B  sing N N 287 
NDP   C4B C3B  sing N N 288 
NDP   C4B H4B  sing N N 289 
NDP   O4B C1B  sing N N 290 
NDP   C3B O3B  sing N N 291 
NDP   C3B C2B  sing N N 292 
NDP   C3B H3B  sing N N 293 
NDP   O3B HO3A sing N N 294 
NDP   C2B O2B  sing N N 295 
NDP   C2B C1B  sing N N 296 
NDP   C2B H2B  sing N N 297 
NDP   O2B P2B  sing N N 298 
NDP   C1B N9A  sing N N 299 
NDP   C1B H1B  sing N N 300 
NDP   N9A C8A  sing Y N 301 
NDP   N9A C4A  sing Y N 302 
NDP   C8A N7A  doub Y N 303 
NDP   C8A H8A  sing N N 304 
NDP   N7A C5A  sing Y N 305 
NDP   C5A C6A  sing Y N 306 
NDP   C5A C4A  doub Y N 307 
NDP   C6A N6A  sing N N 308 
NDP   C6A N1A  doub Y N 309 
NDP   N6A H61A sing N N 310 
NDP   N6A H62A sing N N 311 
NDP   N1A C2A  sing Y N 312 
NDP   C2A N3A  doub Y N 313 
NDP   C2A H2A  sing N N 314 
NDP   N3A C4A  sing Y N 315 
NDP   O3  PN   sing N N 316 
NDP   PN  O1N  doub N N 317 
NDP   PN  O2N  sing N N 318 
NDP   PN  O5D  sing N N 319 
NDP   O2N H21N sing N N 320 
NDP   O5D C5D  sing N N 321 
NDP   C5D C4D  sing N N 322 
NDP   C5D H51N sing N N 323 
NDP   C5D H52N sing N N 324 
NDP   C4D O4D  sing N N 325 
NDP   C4D C3D  sing N N 326 
NDP   C4D H4D  sing N N 327 
NDP   O4D C1D  sing N N 328 
NDP   C3D O3D  sing N N 329 
NDP   C3D C2D  sing N N 330 
NDP   C3D H3D  sing N N 331 
NDP   O3D HO3N sing N N 332 
NDP   C2D O2D  sing N N 333 
NDP   C2D C1D  sing N N 334 
NDP   C2D H2D  sing N N 335 
NDP   O2D HO2N sing N N 336 
NDP   C1D N1N  sing N N 337 
NDP   C1D H1D  sing N N 338 
NDP   N1N C2N  sing N N 339 
NDP   N1N C6N  sing N N 340 
NDP   C2N C3N  doub N N 341 
NDP   C2N H2N  sing N N 342 
NDP   C3N C7N  sing N N 343 
NDP   C3N C4N  sing N N 344 
NDP   C7N O7N  doub N N 345 
NDP   C7N N7N  sing N N 346 
NDP   N7N H71N sing N N 347 
NDP   N7N H72N sing N N 348 
NDP   C4N C5N  sing N N 349 
NDP   C4N H41N sing N N 350 
NDP   C4N H42N sing N N 351 
NDP   C5N C6N  doub N N 352 
NDP   C5N H5N  sing N N 353 
NDP   C6N H6N  sing N N 354 
NDP   P2B O1X  doub N N 355 
NDP   P2B O2X  sing N N 356 
NDP   P2B O3X  sing N N 357 
NDP   O2X HOP2 sing N N 358 
NDP   O3X HOP3 sing N N 359 
PHE   N   CA   sing N N 360 
PHE   N   H    sing N N 361 
PHE   N   H2   sing N N 362 
PHE   CA  C    sing N N 363 
PHE   CA  CB   sing N N 364 
PHE   CA  HA   sing N N 365 
PHE   C   O    doub N N 366 
PHE   C   OXT  sing N N 367 
PHE   CB  CG   sing N N 368 
PHE   CB  HB2  sing N N 369 
PHE   CB  HB3  sing N N 370 
PHE   CG  CD1  doub Y N 371 
PHE   CG  CD2  sing Y N 372 
PHE   CD1 CE1  sing Y N 373 
PHE   CD1 HD1  sing N N 374 
PHE   CD2 CE2  doub Y N 375 
PHE   CD2 HD2  sing N N 376 
PHE   CE1 CZ   doub Y N 377 
PHE   CE1 HE1  sing N N 378 
PHE   CE2 CZ   sing Y N 379 
PHE   CE2 HE2  sing N N 380 
PHE   CZ  HZ   sing N N 381 
PHE   OXT HXT  sing N N 382 
PRO   N   CA   sing N N 383 
PRO   N   CD   sing N N 384 
PRO   N   H    sing N N 385 
PRO   CA  C    sing N N 386 
PRO   CA  CB   sing N N 387 
PRO   CA  HA   sing N N 388 
PRO   C   O    doub N N 389 
PRO   C   OXT  sing N N 390 
PRO   CB  CG   sing N N 391 
PRO   CB  HB2  sing N N 392 
PRO   CB  HB3  sing N N 393 
PRO   CG  CD   sing N N 394 
PRO   CG  HG2  sing N N 395 
PRO   CG  HG3  sing N N 396 
PRO   CD  HD2  sing N N 397 
PRO   CD  HD3  sing N N 398 
PRO   OXT HXT  sing N N 399 
SER   N   CA   sing N N 400 
SER   N   H    sing N N 401 
SER   N   H2   sing N N 402 
SER   CA  C    sing N N 403 
SER   CA  CB   sing N N 404 
SER   CA  HA   sing N N 405 
SER   C   O    doub N N 406 
SER   C   OXT  sing N N 407 
SER   CB  OG   sing N N 408 
SER   CB  HB2  sing N N 409 
SER   CB  HB3  sing N N 410 
SER   OG  HG   sing N N 411 
SER   OXT HXT  sing N N 412 
THR   N   CA   sing N N 413 
THR   N   H    sing N N 414 
THR   N   H2   sing N N 415 
THR   CA  C    sing N N 416 
THR   CA  CB   sing N N 417 
THR   CA  HA   sing N N 418 
THR   C   O    doub N N 419 
THR   C   OXT  sing N N 420 
THR   CB  OG1  sing N N 421 
THR   CB  CG2  sing N N 422 
THR   CB  HB   sing N N 423 
THR   OG1 HG1  sing N N 424 
THR   CG2 HG21 sing N N 425 
THR   CG2 HG22 sing N N 426 
THR   CG2 HG23 sing N N 427 
THR   OXT HXT  sing N N 428 
TRP   N   CA   sing N N 429 
TRP   N   H    sing N N 430 
TRP   N   H2   sing N N 431 
TRP   CA  C    sing N N 432 
TRP   CA  CB   sing N N 433 
TRP   CA  HA   sing N N 434 
TRP   C   O    doub N N 435 
TRP   C   OXT  sing N N 436 
TRP   CB  CG   sing N N 437 
TRP   CB  HB2  sing N N 438 
TRP   CB  HB3  sing N N 439 
TRP   CG  CD1  doub Y N 440 
TRP   CG  CD2  sing Y N 441 
TRP   CD1 NE1  sing Y N 442 
TRP   CD1 HD1  sing N N 443 
TRP   CD2 CE2  doub Y N 444 
TRP   CD2 CE3  sing Y N 445 
TRP   NE1 CE2  sing Y N 446 
TRP   NE1 HE1  sing N N 447 
TRP   CE2 CZ2  sing Y N 448 
TRP   CE3 CZ3  doub Y N 449 
TRP   CE3 HE3  sing N N 450 
TRP   CZ2 CH2  doub Y N 451 
TRP   CZ2 HZ2  sing N N 452 
TRP   CZ3 CH2  sing Y N 453 
TRP   CZ3 HZ3  sing N N 454 
TRP   CH2 HH2  sing N N 455 
TRP   OXT HXT  sing N N 456 
TYR   N   CA   sing N N 457 
TYR   N   H    sing N N 458 
TYR   N   H2   sing N N 459 
TYR   CA  C    sing N N 460 
TYR   CA  CB   sing N N 461 
TYR   CA  HA   sing N N 462 
TYR   C   O    doub N N 463 
TYR   C   OXT  sing N N 464 
TYR   CB  CG   sing N N 465 
TYR   CB  HB2  sing N N 466 
TYR   CB  HB3  sing N N 467 
TYR   CG  CD1  doub Y N 468 
TYR   CG  CD2  sing Y N 469 
TYR   CD1 CE1  sing Y N 470 
TYR   CD1 HD1  sing N N 471 
TYR   CD2 CE2  doub Y N 472 
TYR   CD2 HD2  sing N N 473 
TYR   CE1 CZ   doub Y N 474 
TYR   CE1 HE1  sing N N 475 
TYR   CE2 CZ   sing Y N 476 
TYR   CE2 HE2  sing N N 477 
TYR   CZ  OH   sing N N 478 
TYR   OH  HH   sing N N 479 
TYR   OXT HXT  sing N N 480 
VAL   N   CA   sing N N 481 
VAL   N   H    sing N N 482 
VAL   N   H2   sing N N 483 
VAL   CA  C    sing N N 484 
VAL   CA  CB   sing N N 485 
VAL   CA  HA   sing N N 486 
VAL   C   O    doub N N 487 
VAL   C   OXT  sing N N 488 
VAL   CB  CG1  sing N N 489 
VAL   CB  CG2  sing N N 490 
VAL   CB  HB   sing N N 491 
VAL   CG1 HG11 sing N N 492 
VAL   CG1 HG12 sing N N 493 
VAL   CG1 HG13 sing N N 494 
VAL   CG2 HG21 sing N N 495 
VAL   CG2 HG22 sing N N 496 
VAL   CG2 HG23 sing N N 497 
VAL   OXT HXT  sing N N 498 
# 
_pdbx_audit_support.funding_organization   'European Union (EU)' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           CA21111 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6TBX 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8RHV 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.013419 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006331 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011179 
_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]   0.013381 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU   A 1 23  ? 19.257  10.273  -10.674 1.00 57.17 ? 2   GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 23  ? 19.756  8.942   -10.234 1.00 59.30 ? 2   GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 23  ? 18.621  8.123   -9.604  1.00 57.44 ? 2   GLU   A C   1 
ATOM   4    O O   . GLU   A 1 23  ? 17.477  8.565   -9.473  1.00 54.08 ? 2   GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 23  ? 21.037  9.077   -9.400  1.00 55.14 ? 2   GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 23  ? 20.873  9.834   -8.080  1.00 52.64 ? 2   GLU   A CG  1 
ATOM   7    N N   . ALA   A 1 24  ? 18.957  6.885   -9.253  1.00 49.86 ? 3   ALA   A N   1 
ATOM   8    C CA  . ALA   A 1 24  ? 18.053  5.992   -8.557  1.00 40.71 ? 3   ALA   A CA  1 
ATOM   9    C C   . ALA   A 1 24  ? 18.014  6.344   -7.068  1.00 43.57 ? 3   ALA   A C   1 
ATOM   10   O O   . ALA   A 1 24  ? 19.006  6.757   -6.480  1.00 38.74 ? 3   ALA   A O   1 
ATOM   11   C CB  . ALA   A 1 24  ? 18.505  4.569   -8.768  1.00 42.84 ? 3   ALA   A CB  1 
ATOM   12   N N   . PRO   A 1 25  ? 16.852  6.179   -6.404  1.00 38.68 ? 4   PRO   A N   1 
ATOM   13   C CA  . PRO   A 1 25  ? 16.779  6.321   -4.954  1.00 34.83 ? 4   PRO   A CA  1 
ATOM   14   C C   . PRO   A 1 25  ? 17.500  5.177   -4.236  1.00 28.46 ? 4   PRO   A C   1 
ATOM   15   O O   . PRO   A 1 25  ? 17.857  4.184   -4.869  1.00 34.40 ? 4   PRO   A O   1 
ATOM   16   C CB  . PRO   A 1 25  ? 15.218  6.308   -4.779  1.00 34.70 ? 4   PRO   A CB  1 
ATOM   17   C CG  . PRO   A 1 25  ? 14.740  5.366   -5.849  1.00 36.99 ? 4   PRO   A CG  1 
ATOM   18   C CD  . PRO   A 1 25  ? 15.564  5.834   -7.036  1.00 39.95 ? 4   PRO   A CD  1 
ATOM   19   N N   . ALA   A 1 26  ? 17.746  5.366   -2.932  1.00 31.36 ? 5   ALA   A N   1 
ATOM   20   C CA  . ALA   A 1 26  ? 18.424  4.378   -2.099  1.00 31.59 ? 5   ALA   A CA  1 
ATOM   21   C C   . ALA   A 1 26  ? 17.620  4.098   -0.827  1.00 29.08 ? 5   ALA   A C   1 
ATOM   22   O O   . ALA   A 1 26  ? 17.025  5.004   -0.273  1.00 29.92 ? 5   ALA   A O   1 
ATOM   23   C CB  . ALA   A 1 26  ? 19.807  4.879   -1.735  1.00 32.09 ? 5   ALA   A CB  1 
ATOM   24   N N   . ALA   A 1 27  ? 17.675  2.843   -0.356  1.00 32.54 ? 6   ALA   A N   1 
ATOM   25   C CA  . ALA   A 1 27  ? 16.987  2.422   0.860   1.00 31.45 ? 6   ALA   A CA  1 
ATOM   26   C C   . ALA   A 1 27  ? 17.962  1.737   1.801   1.00 30.22 ? 6   ALA   A C   1 
ATOM   27   O O   . ALA   A 1 27  ? 18.902  1.085   1.352   1.00 32.12 ? 6   ALA   A O   1 
ATOM   28   C CB  . ALA   A 1 27  ? 15.881  1.452   0.488   1.00 29.28 ? 6   ALA   A CB  1 
ATOM   29   N N   . VAL   A 1 28  ? 17.722  1.886   3.114   1.00 27.44 ? 7   VAL   A N   1 
ATOM   30   C CA  . VAL   A 1 28  ? 18.381  1.044   4.099   1.00 27.67 ? 7   VAL   A CA  1 
ATOM   31   C C   . VAL   A 1 28  ? 17.350  0.034   4.590   1.00 30.15 ? 7   VAL   A C   1 
ATOM   32   O O   . VAL   A 1 28  ? 16.267  0.459   4.999   1.00 25.03 ? 7   VAL   A O   1 
ATOM   33   C CB  . VAL   A 1 28  ? 18.822  1.923   5.284   1.00 27.27 ? 7   VAL   A CB  1 
ATOM   34   C CG1 . VAL   A 1 28  ? 19.101  1.090   6.529   1.00 27.45 ? 7   VAL   A CG1 1 
ATOM   35   C CG2 . VAL   A 1 28  ? 19.987  2.843   4.906   1.00 29.92 ? 7   VAL   A CG2 1 
ATOM   36   N N   . VAL   A 1 29  ? 17.715  -1.262  4.603   1.00 27.86 ? 8   VAL   A N   1 
ATOM   37   C CA  . VAL   A 1 29  ? 16.873  -2.313  5.164   1.00 28.28 ? 8   VAL   A CA  1 
ATOM   38   C C   . VAL   A 1 29  ? 17.673  -3.003  6.267   1.00 27.49 ? 8   VAL   A C   1 
ATOM   39   O O   . VAL   A 1 29  ? 18.736  -3.541  6.000   1.00 27.99 ? 8   VAL   A O   1 
ATOM   40   C CB  . VAL   A 1 29  ? 16.382  -3.316  4.097   1.00 27.40 ? 8   VAL   A CB  1 
ATOM   41   C CG1 . VAL   A 1 29  ? 15.476  -4.396  4.699   1.00 23.62 ? 8   VAL   A CG1 1 
ATOM   42   C CG2 . VAL   A 1 29  ? 15.675  -2.633  2.925   1.00 26.53 ? 8   VAL   A CG2 1 
ATOM   43   N N   . THR   A 1 30  ? 17.166  -2.979  7.507   1.00 26.75 ? 9   THR   A N   1 
ATOM   44   C CA  . THR   A 1 30  ? 17.853  -3.571  8.648   1.00 24.82 ? 9   THR   A CA  1 
ATOM   45   C C   . THR   A 1 30  ? 17.530  -5.060  8.696   1.00 24.97 ? 9   THR   A C   1 
ATOM   46   O O   . THR   A 1 30  ? 16.466  -5.451  8.267   1.00 25.82 ? 9   THR   A O   1 
ATOM   47   C CB  . THR   A 1 30  ? 17.565  -2.820  9.944   1.00 26.60 ? 9   THR   A CB  1 
ATOM   48   O OG1 . THR   A 1 30  ? 16.185  -2.998  10.308  1.00 26.20 ? 9   THR   A OG1 1 
ATOM   49   C CG2 . THR   A 1 30  ? 17.828  -1.337  9.743   1.00 22.46 ? 9   THR   A CG2 1 
ATOM   50   N N   . GLY   A 1 31  ? 18.488  -5.873  9.154   1.00 26.60 ? 10  GLY   A N   1 
ATOM   51   C CA  . GLY   A 1 31  ? 18.352  -7.323  9.181   1.00 25.34 ? 10  GLY   A CA  1 
ATOM   52   C C   . GLY   A 1 31  ? 17.944  -7.879  7.811   1.00 27.98 ? 10  GLY   A C   1 
ATOM   53   O O   . GLY   A 1 31  ? 17.044  -8.715  7.736   1.00 28.63 ? 10  GLY   A O   1 
ATOM   54   N N   . ALA   A 1 32  ? 18.637  -7.468  6.738   1.00 27.68 ? 11  ALA   A N   1 
ATOM   55   C CA  . ALA   A 1 32  ? 18.196  -7.790  5.382   1.00 26.23 ? 11  ALA   A CA  1 
ATOM   56   C C   . ALA   A 1 32  ? 18.921  -9.000  4.787   1.00 27.98 ? 11  ALA   A C   1 
ATOM   57   O O   . ALA   A 1 32  ? 18.761  -9.242  3.595   1.00 26.04 ? 11  ALA   A O   1 
ATOM   58   C CB  . ALA   A 1 32  ? 18.331  -6.599  4.450   1.00 26.41 ? 11  ALA   A CB  1 
ATOM   59   N N   . ALA   A 1 33  ? 19.679  -9.768  5.587   1.00 26.83 ? 12  ALA   A N   1 
ATOM   60   C CA  . ALA   A 1 33  ? 20.445  -10.841 4.954   1.00 32.63 ? 12  ALA   A CA  1 
ATOM   61   C C   . ALA   A 1 33  ? 19.548  -12.001 4.514   1.00 34.54 ? 12  ALA   A C   1 
ATOM   62   O O   . ALA   A 1 33  ? 19.873  -12.713 3.566   1.00 31.94 ? 12  ALA   A O   1 
ATOM   63   C CB  . ALA   A 1 33  ? 21.580  -11.315 5.845   1.00 31.20 ? 12  ALA   A CB  1 
ATOM   64   N N   . LYS   A 1 34  ? 18.428  -12.199 5.217   1.00 31.60 ? 13  LYS   A N   1 
ATOM   65   C CA  . LYS   A 1 34  ? 17.621  -13.397 5.021   1.00 31.64 ? 13  LYS   A CA  1 
ATOM   66   C C   . LYS   A 1 34  ? 16.140  -13.057 5.184   1.00 31.49 ? 13  LYS   A C   1 
ATOM   67   O O   . LYS   A 1 34  ? 15.791  -11.923 5.495   1.00 29.53 ? 13  LYS   A O   1 
ATOM   68   C CB  . LYS   A 1 34  ? 17.965  -14.487 6.051   1.00 36.55 ? 13  LYS   A CB  1 
ATOM   69   C CG  . LYS   A 1 34  ? 19.421  -14.902 6.008   1.00 46.79 ? 13  LYS   A CG  1 
ATOM   70   C CD  . LYS   A 1 34  ? 19.876  -15.943 7.028   1.00 51.04 ? 13  LYS   A CD  1 
ATOM   71   C CE  . LYS   A 1 34  ? 19.847  -15.475 8.419   1.00 49.07 ? 13  LYS   A CE  1 
ATOM   72   N NZ  . LYS   A 1 34  ? 20.506  -16.463 9.275   1.00 49.74 ? 13  LYS   A NZ  1 
ATOM   73   N N   . ARG   A 1 35  ? 15.286  -14.033 4.863   1.00 28.97 ? 14  ARG   A N   1 
ATOM   74   C CA  . ARG   A 1 35  ? 13.893  -14.035 5.292   1.00 28.58 ? 14  ARG   A CA  1 
ATOM   75   C C   . ARG   A 1 35  ? 13.216  -12.749 4.825   1.00 28.21 ? 14  ARG   A C   1 
ATOM   76   O O   . ARG   A 1 35  ? 13.383  -12.371 3.685   1.00 25.05 ? 14  ARG   A O   1 
ATOM   77   C CB  . ARG   A 1 35  ? 13.871  -14.370 6.792   1.00 29.70 ? 14  ARG   A CB  1 
ATOM   78   C CG  . ARG   A 1 35  ? 14.247  -15.823 7.063   1.00 28.97 ? 14  ARG   A CG  1 
ATOM   79   C CD  . ARG   A 1 35  ? 14.612  -16.102 8.513   1.00 32.21 ? 14  ARG   A CD  1 
ATOM   80   N NE  . ARG   A 1 35  ? 13.467  -15.857 9.403   1.00 32.22 ? 14  ARG   A NE  1 
ATOM   81   C CZ  . ARG   A 1 35  ? 12.417  -16.682 9.588   1.00 31.59 ? 14  ARG   A CZ  1 
ATOM   82   N NH1 . ARG   A 1 35  ? 12.443  -17.906 9.059   1.00 31.71 ? 14  ARG   A NH1 1 
ATOM   83   N NH2 . ARG   A 1 35  ? 11.378  -16.298 10.347  1.00 29.77 ? 14  ARG   A NH2 1 
ATOM   84   N N   . ILE   A 1 36  ? 12.424  -12.083 5.688   1.00 25.44 ? 15  ILE   A N   1 
ATOM   85   C CA  . ILE   A 1 36  ? 11.572  -11.007 5.184   1.00 26.46 ? 15  ILE   A CA  1 
ATOM   86   C C   . ILE   A 1 36  ? 12.421  -9.808  4.760   1.00 25.03 ? 15  ILE   A C   1 
ATOM   87   O O   . ILE   A 1 36  ? 12.108  -9.089  3.785   1.00 25.49 ? 15  ILE   A O   1 
ATOM   88   C CB  . ILE   A 1 36  ? 10.514  -10.629 6.246   1.00 25.45 ? 15  ILE   A CB  1 
ATOM   89   C CG1 . ILE   A 1 36  ? 9.431   -11.729 6.283   1.00 29.81 ? 15  ILE   A CG1 1 
ATOM   90   C CG2 . ILE   A 1 36  ? 9.854   -9.278  5.942   1.00 24.17 ? 15  ILE   A CG2 1 
ATOM   91   C CD1 . ILE   A 1 36  ? 8.538   -11.660 7.516   1.00 28.31 ? 15  ILE   A CD1 1 
ATOM   92   N N   . GLY   A 1 37  ? 13.492  -9.574  5.507   1.00 25.19 ? 16  GLY   A N   1 
ATOM   93   C CA  . GLY   A 1 37  ? 14.317  -8.414  5.176   1.00 26.83 ? 16  GLY   A CA  1 
ATOM   94   C C   . GLY   A 1 37  ? 14.972  -8.545  3.790   1.00 26.08 ? 16  GLY   A C   1 
ATOM   95   O O   . GLY   A 1 37  ? 15.050  -7.581  3.046   1.00 24.12 ? 16  GLY   A O   1 
ATOM   96   N N   . ARG   A 1 38  ? 15.428  -9.744  3.435   1.00 26.91 ? 17  ARG   A N   1 
ATOM   97   C CA  . ARG   A 1 38  ? 15.969  -9.958  2.095   1.00 25.95 ? 17  ARG   A CA  1 
ATOM   98   C C   . ARG   A 1 38  ? 14.896  -9.754  1.034   1.00 27.97 ? 17  ARG   A C   1 
ATOM   99   O O   . ARG   A 1 38  ? 15.158  -9.241  -0.044  1.00 26.82 ? 17  ARG   A O   1 
ATOM   100  C CB  . ARG   A 1 38  ? 16.496  -11.397 1.967   1.00 29.57 ? 17  ARG   A CB  1 
ATOM   101  C CG  . ARG   A 1 38  ? 16.931  -11.756 0.545   1.00 28.98 ? 17  ARG   A CG  1 
ATOM   102  C CD  . ARG   A 1 38  ? 17.716  -13.108 0.424   1.00 26.78 ? 17  ARG   A CD  1 
ATOM   103  N NE  . ARG   A 1 38  ? 17.834  -13.514 -0.987  1.00 32.06 ? 17  ARG   A NE  1 
ATOM   104  C CZ  . ARG   A 1 38  ? 18.943  -13.928 -1.630  1.00 34.04 ? 17  ARG   A CZ  1 
ATOM   105  N NH1 . ARG   A 1 38  ? 20.102  -14.054 -1.005  1.00 35.40 ? 17  ARG   A NH1 1 
ATOM   106  N NH2 . ARG   A 1 38  ? 18.853  -14.248 -2.896  1.00 33.21 ? 17  ARG   A NH2 1 
ATOM   107  N N   . ALA   A 1 39  ? 13.681  -10.246 1.312   1.00 26.51 ? 18  ALA   A N   1 
ATOM   108  C CA  . ALA   A 1 39  ? 12.601  -10.122 0.358   1.00 26.94 ? 18  ALA   A CA  1 
ATOM   109  C C   . ALA   A 1 39  ? 12.298  -8.645  0.106   1.00 27.03 ? 18  ALA   A C   1 
ATOM   110  O O   . ALA   A 1 39  ? 12.042  -8.254  -1.026  1.00 27.61 ? 18  ALA   A O   1 
ATOM   111  C CB  . ALA   A 1 39  ? 11.379  -10.866 0.913   1.00 27.03 ? 18  ALA   A CB  1 
ATOM   112  N N   . ILE   A 1 40  ? 12.327  -7.821  1.170   1.00 25.27 ? 19  ILE   A N   1 
ATOM   113  C CA  . ILE   A 1 40  ? 12.127  -6.389  1.000   1.00 24.35 ? 19  ILE   A CA  1 
ATOM   114  C C   . ILE   A 1 40  ? 13.265  -5.771  0.168   1.00 27.00 ? 19  ILE   A C   1 
ATOM   115  O O   . ILE   A 1 40  ? 13.000  -4.985  -0.753  1.00 26.65 ? 19  ILE   A O   1 
ATOM   116  C CB  . ILE   A 1 40  ? 11.959  -5.696  2.359   1.00 25.00 ? 19  ILE   A CB  1 
ATOM   117  C CG1 . ILE   A 1 40  ? 10.647  -6.191  3.011   1.00 24.34 ? 19  ILE   A CG1 1 
ATOM   118  C CG2 . ILE   A 1 40  ? 11.997  -4.171  2.207   1.00 23.71 ? 19  ILE   A CG2 1 
ATOM   119  C CD1 . ILE   A 1 40  ? 10.584  -5.961  4.528   1.00 25.91 ? 19  ILE   A CD1 1 
ATOM   120  N N   . ALA   A 1 41  ? 14.508  -6.111  0.506   1.00 25.99 ? 20  ALA   A N   1 
ATOM   121  C CA  . ALA   A 1 41  ? 15.646  -5.487  -0.179  1.00 28.25 ? 20  ALA   A CA  1 
ATOM   122  C C   . ALA   A 1 41  ? 15.599  -5.896  -1.645  1.00 25.34 ? 20  ALA   A C   1 
ATOM   123  O O   . ALA   A 1 41  ? 15.752  -5.064  -2.517  1.00 28.40 ? 20  ALA   A O   1 
ATOM   124  C CB  . ALA   A 1 41  ? 16.972  -5.899  0.472   1.00 28.80 ? 20  ALA   A CB  1 
ATOM   125  N N   . VAL   A 1 42  ? 15.316  -7.178  -1.896  1.00 24.06 ? 21  VAL   A N   1 
ATOM   126  C CA  . VAL   A 1 42  ? 15.195  -7.661  -3.265  1.00 29.21 ? 21  VAL   A CA  1 
ATOM   127  C C   . VAL   A 1 42  ? 14.117  -6.909  -4.051  1.00 33.02 ? 21  VAL   A C   1 
ATOM   128  O O   . VAL   A 1 42  ? 14.333  -6.534  -5.205  1.00 34.25 ? 21  VAL   A O   1 
ATOM   129  C CB  . VAL   A 1 42  ? 14.995  -9.192  -3.327  1.00 31.42 ? 21  VAL   A CB  1 
ATOM   130  C CG1 . VAL   A 1 42  ? 14.559  -9.667  -4.707  1.00 32.26 ? 21  VAL   A CG1 1 
ATOM   131  C CG2 . VAL   A 1 42  ? 16.263  -9.918  -2.936  1.00 31.17 ? 21  VAL   A CG2 1 
ATOM   132  N N   . LYS   A 1 43  ? 12.926  -6.738  -3.458  1.00 28.44 ? 22  LYS   A N   1 
ATOM   133  C CA  . LYS   A 1 43  ? 11.830  -6.119  -4.171  1.00 30.64 ? 22  LYS   A CA  1 
ATOM   134  C C   . LYS   A 1 43  ? 12.119  -4.620  -4.367  1.00 29.63 ? 22  LYS   A C   1 
ATOM   135  O O   . LYS   A 1 43  ? 11.814  -4.054  -5.425  1.00 29.18 ? 22  LYS   A O   1 
ATOM   136  C CB  . LYS   A 1 43  ? 10.512  -6.458  -3.457  1.00 34.86 ? 22  LYS   A CB  1 
ATOM   137  C CG  . LYS   A 1 43  ? 9.341   -6.304  -4.429  1.00 41.04 ? 22  LYS   A CG  1 
ATOM   138  C CD  . LYS   A 1 43  ? 7.964   -6.662  -3.887  1.00 44.52 ? 22  LYS   A CD  1 
ATOM   139  C CE  . LYS   A 1 43  ? 7.774   -8.130  -3.826  1.00 43.80 ? 22  LYS   A CE  1 
ATOM   140  N NZ  . LYS   A 1 43  ? 7.449   -8.688  -5.147  1.00 53.50 ? 22  LYS   A NZ  1 
ATOM   141  N N   . LEU   A 1 44  ? 12.726  -3.982  -3.365  1.00 28.24 ? 23  LEU   A N   1 
ATOM   142  C CA  . LEU   A 1 44  ? 13.107  -2.581  -3.546  1.00 30.20 ? 23  LEU   A CA  1 
ATOM   143  C C   . LEU   A 1 44  ? 14.105  -2.476  -4.717  1.00 31.57 ? 23  LEU   A C   1 
ATOM   144  O O   . LEU   A 1 44  ? 14.008  -1.580  -5.571  1.00 32.03 ? 23  LEU   A O   1 
ATOM   145  C CB  . LEU   A 1 44  ? 13.693  -1.999  -2.262  1.00 26.69 ? 23  LEU   A CB  1 
ATOM   146  C CG  . LEU   A 1 44  ? 12.684  -1.596  -1.173  1.00 29.74 ? 23  LEU   A CG  1 
ATOM   147  C CD1 . LEU   A 1 44  ? 13.419  -1.451  0.150   1.00 30.67 ? 23  LEU   A CD1 1 
ATOM   148  C CD2 . LEU   A 1 44  ? 11.926  -0.301  -1.464  1.00 25.97 ? 23  LEU   A CD2 1 
ATOM   149  N N   . HIS   A 1 45  ? 15.048  -3.418  -4.755  1.00 30.96 ? 24  HIS   A N   1 
ATOM   150  C CA  . HIS   A 1 45  ? 16.075  -3.406  -5.795  1.00 34.27 ? 24  HIS   A CA  1 
ATOM   151  C C   . HIS   A 1 45  ? 15.451  -3.608  -7.181  1.00 39.09 ? 24  HIS   A C   1 
ATOM   152  O O   . HIS   A 1 45  ? 15.803  -2.900  -8.123  1.00 36.52 ? 24  HIS   A O   1 
ATOM   153  C CB  . HIS   A 1 45  ? 17.226  -4.351  -5.439  1.00 33.05 ? 24  HIS   A CB  1 
ATOM   154  C CG  . HIS   A 1 45  ? 18.401  -4.271  -6.367  1.00 35.38 ? 24  HIS   A CG  1 
ATOM   155  N ND1 . HIS   A 1 45  ? 18.521  -5.117  -7.447  1.00 36.33 ? 24  HIS   A ND1 1 
ATOM   156  C CD2 . HIS   A 1 45  ? 19.497  -3.508  -6.366  1.00 37.38 ? 24  HIS   A CD2 1 
ATOM   157  C CE1 . HIS   A 1 45  ? 19.667  -4.869  -8.064  1.00 35.62 ? 24  HIS   A CE1 1 
ATOM   158  N NE2 . HIS   A 1 45  ? 20.280  -3.893  -7.430  1.00 39.15 ? 24  HIS   A NE2 1 
ATOM   159  N N   . GLN   A 1 46  ? 14.506  -4.550  -7.296  1.00 35.75 ? 25  GLN   A N   1 
ATOM   160  C CA  . GLN   A 1 46  ? 13.814  -4.792  -8.554  1.00 39.12 ? 25  GLN   A CA  1 
ATOM   161  C C   . GLN   A 1 46  ? 12.999  -3.580  -9.006  1.00 42.27 ? 25  GLN   A C   1 
ATOM   162  O O   . GLN   A 1 46  ? 12.780  -3.414  -10.196 1.00 42.06 ? 25  GLN   A O   1 
ATOM   163  C CB  . GLN   A 1 46  ? 12.904  -6.013  -8.500  1.00 36.38 ? 25  GLN   A CB  1 
ATOM   164  C CG  . GLN   A 1 46  ? 13.670  -7.286  -8.174  1.00 33.80 ? 25  GLN   A CG  1 
ATOM   165  C CD  . GLN   A 1 46  ? 12.757  -8.465  -7.954  1.00 42.03 ? 25  GLN   A CD  1 
ATOM   166  O OE1 . GLN   A 1 46  ? 13.150  -9.625  -8.148  1.00 45.71 ? 25  GLN   A OE1 1 
ATOM   167  N NE2 . GLN   A 1 46  ? 11.526  -8.173  -7.561  1.00 41.82 ? 25  GLN   A NE2 1 
ATOM   168  N N   . THR   A 1 47  ? 12.570  -2.729  -8.067  1.00 39.54 ? 26  THR   A N   1 
ATOM   169  C CA  . THR   A 1 47  ? 11.780  -1.543  -8.367  1.00 37.34 ? 26  THR   A CA  1 
ATOM   170  C C   . THR   A 1 47  ? 12.709  -0.416  -8.814  1.00 38.61 ? 26  THR   A C   1 
ATOM   171  O O   . THR   A 1 47  ? 12.246  0.644   -9.227  1.00 40.26 ? 26  THR   A O   1 
ATOM   172  C CB  . THR   A 1 47  ? 10.987  -1.163  -7.109  1.00 42.32 ? 26  THR   A CB  1 
ATOM   173  O OG1 . THR   A 1 47  ? 10.179  -2.302  -6.819  1.00 44.08 ? 26  THR   A OG1 1 
ATOM   174  C CG2 . THR   A 1 47  ? 10.027  -0.005  -7.298  1.00 39.09 ? 26  THR   A CG2 1 
ATOM   175  N N   . GLY   A 1 48  ? 14.021  -0.608  -8.628  1.00 38.24 ? 27  GLY   A N   1 
ATOM   176  C CA  . GLY   A 1 48  ? 14.991  0.369   -9.091  1.00 38.13 ? 27  GLY   A CA  1 
ATOM   177  C C   . GLY   A 1 48  ? 15.747  1.081   -7.967  1.00 40.96 ? 27  GLY   A C   1 
ATOM   178  O O   . GLY   A 1 48  ? 16.433  2.063   -8.246  1.00 37.88 ? 27  GLY   A O   1 
ATOM   179  N N   . TYR   A 1 49  ? 15.610  0.621   -6.707  1.00 35.83 ? 28  TYR   A N   1 
ATOM   180  C CA  . TYR   A 1 49  ? 16.316  1.249   -5.596  1.00 31.40 ? 28  TYR   A CA  1 
ATOM   181  C C   . TYR   A 1 49  ? 17.731  0.682   -5.511  1.00 29.56 ? 28  TYR   A C   1 
ATOM   182  O O   . TYR   A 1 49  ? 17.918  -0.499  -5.750  1.00 32.53 ? 28  TYR   A O   1 
ATOM   183  C CB  . TYR   A 1 49  ? 15.768  0.993   -4.176  1.00 30.32 ? 28  TYR   A CB  1 
ATOM   184  C CG  . TYR   A 1 49  ? 14.523  1.834   -3.897  1.00 29.76 ? 28  TYR   A CG  1 
ATOM   185  C CD1 . TYR   A 1 49  ? 13.291  1.469   -4.433  1.00 35.27 ? 28  TYR   A CD1 1 
ATOM   186  C CD2 . TYR   A 1 49  ? 14.603  3.016   -3.173  1.00 31.81 ? 28  TYR   A CD2 1 
ATOM   187  C CE1 . TYR   A 1 49  ? 12.166  2.250   -4.231  1.00 33.07 ? 28  TYR   A CE1 1 
ATOM   188  C CE2 . TYR   A 1 49  ? 13.484  3.803   -2.964  1.00 33.07 ? 28  TYR   A CE2 1 
ATOM   189  C CZ  . TYR   A 1 49  ? 12.267  3.408   -3.489  1.00 30.61 ? 28  TYR   A CZ  1 
ATOM   190  O OH  . TYR   A 1 49  ? 11.172  4.185   -3.281  1.00 33.77 ? 28  TYR   A OH  1 
ATOM   191  N N   . ARG   A 1 50  ? 18.673  1.523   -5.062  1.00 32.10 ? 29  ARG   A N   1 
ATOM   192  C CA  . ARG   A 1 50  ? 19.932  1.062   -4.484  1.00 33.76 ? 29  ARG   A CA  1 
ATOM   193  C C   . ARG   A 1 50  ? 19.724  0.711   -3.010  1.00 33.98 ? 29  ARG   A C   1 
ATOM   194  O O   . ARG   A 1 50  ? 18.940  1.371   -2.324  1.00 35.42 ? 29  ARG   A O   1 
ATOM   195  C CB  . ARG   A 1 50  ? 21.031  2.116   -4.664  1.00 34.56 ? 29  ARG   A CB  1 
ATOM   196  C CG  . ARG   A 1 50  ? 21.179  2.322   -6.166  1.00 39.75 ? 29  ARG   A CG  1 
ATOM   197  C CD  . ARG   A 1 50  ? 22.267  3.322   -6.481  1.00 38.68 ? 29  ARG   A CD  1 
ATOM   198  N NE  . ARG   A 1 50  ? 21.748  4.658   -6.170  1.00 38.66 ? 29  ARG   A NE  1 
ATOM   199  C CZ  . ARG   A 1 50  ? 22.521  5.738   -6.163  1.00 42.01 ? 29  ARG   A CZ  1 
ATOM   200  N NH1 . ARG   A 1 50  ? 23.817  5.627   -6.444  1.00 45.99 ? 29  ARG   A NH1 1 
ATOM   201  N NH2 . ARG   A 1 50  ? 21.997  6.914   -5.874  1.00 40.30 ? 29  ARG   A NH2 1 
ATOM   202  N N   . VAL   A 1 51  ? 20.430  -0.316  -2.522  1.00 32.64 ? 30  VAL   A N   1 
ATOM   203  C CA  . VAL   A 1 51  ? 20.128  -0.804  -1.182  1.00 32.31 ? 30  VAL   A CA  1 
ATOM   204  C C   . VAL   A 1 51  ? 21.361  -0.968  -0.293  1.00 33.76 ? 30  VAL   A C   1 
ATOM   205  O O   . VAL   A 1 51  ? 22.421  -1.451  -0.712  1.00 34.02 ? 30  VAL   A O   1 
ATOM   206  C CB  . VAL   A 1 51  ? 19.332  -2.114  -1.288  1.00 31.54 ? 30  VAL   A CB  1 
ATOM   207  C CG1 . VAL   A 1 51  ? 17.995  -1.895  -1.986  1.00 29.69 ? 30  VAL   A CG1 1 
ATOM   208  C CG2 . VAL   A 1 51  ? 20.117  -3.230  -1.969  1.00 32.38 ? 30  VAL   A CG2 1 
ATOM   209  N N   . VAL   A 1 52  ? 21.196  -0.595  0.979   1.00 30.11 ? 31  VAL   A N   1 
ATOM   210  C CA  . VAL   A 1 52  ? 22.112  -0.990  2.028   1.00 29.15 ? 31  VAL   A CA  1 
ATOM   211  C C   . VAL   A 1 52  ? 21.495  -2.192  2.719   1.00 33.44 ? 31  VAL   A C   1 
ATOM   212  O O   . VAL   A 1 52  ? 20.383  -2.084  3.254   1.00 28.89 ? 31  VAL   A O   1 
ATOM   213  C CB  . VAL   A 1 52  ? 22.285  0.155   3.046   1.00 33.87 ? 31  VAL   A CB  1 
ATOM   214  C CG1 . VAL   A 1 52  ? 23.209  -0.225  4.185   1.00 31.97 ? 31  VAL   A CG1 1 
ATOM   215  C CG2 . VAL   A 1 52  ? 22.755  1.451   2.397   1.00 32.31 ? 31  VAL   A CG2 1 
ATOM   216  N N   . ILE   A 1 53  ? 22.243  -3.298  2.726   1.00 29.08 ? 32  ILE   A N   1 
ATOM   217  C CA  . ILE   A 1 53  ? 21.877  -4.503  3.439   1.00 29.97 ? 32  ILE   A CA  1 
ATOM   218  C C   . ILE   A 1 53  ? 22.553  -4.501  4.812   1.00 29.81 ? 32  ILE   A C   1 
ATOM   219  O O   . ILE   A 1 53  ? 23.728  -4.875  4.954   1.00 27.71 ? 32  ILE   A O   1 
ATOM   220  C CB  . ILE   A 1 53  ? 22.278  -5.705  2.573   1.00 29.44 ? 32  ILE   A CB  1 
ATOM   221  C CG1 . ILE   A 1 53  ? 21.639  -5.580  1.209   1.00 36.14 ? 32  ILE   A CG1 1 
ATOM   222  C CG2 . ILE   A 1 53  ? 21.989  -7.042  3.270   1.00 31.34 ? 32  ILE   A CG2 1 
ATOM   223  C CD1 . ILE   A 1 53  ? 22.289  -6.427  0.139   1.00 38.40 ? 32  ILE   A CD1 1 
ATOM   224  N N   . HIS   A 1 54  ? 21.804  -4.083  5.844   1.00 29.24 ? 33  HIS   A N   1 
ATOM   225  C CA  . HIS   A 1 54  ? 22.297  -4.198  7.207   1.00 27.22 ? 33  HIS   A CA  1 
ATOM   226  C C   . HIS   A 1 54  ? 22.180  -5.652  7.641   1.00 27.44 ? 33  HIS   A C   1 
ATOM   227  O O   . HIS   A 1 54  ? 21.222  -6.338  7.266   1.00 28.27 ? 33  HIS   A O   1 
ATOM   228  C CB  . HIS   A 1 54  ? 21.572  -3.255  8.177   1.00 24.46 ? 33  HIS   A CB  1 
ATOM   229  C CG  . HIS   A 1 54  ? 21.718  -3.687  9.604   1.00 28.56 ? 33  HIS   A CG  1 
ATOM   230  N ND1 . HIS   A 1 54  ? 20.827  -4.550  10.214  1.00 26.42 ? 33  HIS   A ND1 1 
ATOM   231  C CD2 . HIS   A 1 54  ? 22.684  -3.450  10.512  1.00 26.09 ? 33  HIS   A CD2 1 
ATOM   232  C CE1 . HIS   A 1 54  ? 21.231  -4.783  11.454  1.00 30.06 ? 33  HIS   A CE1 1 
ATOM   233  N NE2 . HIS   A 1 54  ? 22.365  -4.127  11.650  1.00 27.06 ? 33  HIS   A NE2 1 
ATOM   234  N N   . TYR   A 1 55  ? 23.165  -6.095  8.430   1.00 26.53 ? 34  TYR   A N   1 
ATOM   235  C CA  . TYR   A 1 55  ? 23.150  -7.411  9.057   1.00 26.56 ? 34  TYR   A CA  1 
ATOM   236  C C   . TYR   A 1 55  ? 23.904  -7.334  10.382  1.00 25.72 ? 34  TYR   A C   1 
ATOM   237  O O   . TYR   A 1 55  ? 24.579  -6.339  10.673  1.00 27.94 ? 34  TYR   A O   1 
ATOM   238  C CB  . TYR   A 1 55  ? 23.656  -8.453  8.044   1.00 30.62 ? 34  TYR   A CB  1 
ATOM   239  C CG  . TYR   A 1 55  ? 25.168  -8.350  7.964   1.00 33.52 ? 34  TYR   A CG  1 
ATOM   240  C CD1 . TYR   A 1 55  ? 25.770  -7.423  7.117   1.00 32.99 ? 34  TYR   A CD1 1 
ATOM   241  C CD2 . TYR   A 1 55  ? 25.969  -9.111  8.816   1.00 36.44 ? 34  TYR   A CD2 1 
ATOM   242  C CE1 . TYR   A 1 55  ? 27.159  -7.317  7.058   1.00 38.78 ? 34  TYR   A CE1 1 
ATOM   243  C CE2 . TYR   A 1 55  ? 27.352  -9.001  8.776   1.00 39.38 ? 34  TYR   A CE2 1 
ATOM   244  C CZ  . TYR   A 1 55  ? 27.941  -8.112  7.886   1.00 39.53 ? 34  TYR   A CZ  1 
ATOM   245  O OH  . TYR   A 1 55  ? 29.308  -7.994  7.855   1.00 43.86 ? 34  TYR   A OH  1 
ATOM   246  N N   . HIS   A 1 56  ? 23.732  -8.362  11.203  1.00 27.63 ? 35  HIS   A N   1 
ATOM   247  C CA  . HIS   A 1 56  ? 24.430  -8.456  12.483  1.00 31.65 ? 35  HIS   A CA  1 
ATOM   248  C C   . HIS   A 1 56  ? 25.377  -9.660  12.463  1.00 32.24 ? 35  HIS   A C   1 
ATOM   249  O O   . HIS   A 1 56  ? 26.583  -9.455  12.377  1.00 35.57 ? 35  HIS   A O   1 
ATOM   250  C CB  . HIS   A 1 56  ? 23.450  -8.494  13.654  1.00 27.21 ? 35  HIS   A CB  1 
ATOM   251  C CG  . HIS   A 1 56  ? 24.050  -8.694  15.001  1.00 29.30 ? 35  HIS   A CG  1 
ATOM   252  N ND1 . HIS   A 1 56  ? 23.434  -9.511  15.929  1.00 33.34 ? 35  HIS   A ND1 1 
ATOM   253  C CD2 . HIS   A 1 56  ? 25.181  -8.239  15.569  1.00 32.22 ? 35  HIS   A CD2 1 
ATOM   254  C CE1 . HIS   A 1 56  ? 24.170  -9.540  17.035  1.00 40.55 ? 35  HIS   A CE1 1 
ATOM   255  N NE2 . HIS   A 1 56  ? 25.237  -8.770  16.840  1.00 39.62 ? 35  HIS   A NE2 1 
ATOM   256  N N   . ASN   A 1 57  ? 24.838  -10.890 12.508  1.00 30.54 ? 36  ASN   A N   1 
ATOM   257  C CA  . ASN   A 1 57  ? 25.685  -12.075 12.485  1.00 32.77 ? 36  ASN   A CA  1 
ATOM   258  C C   . ASN   A 1 57  ? 25.797  -12.715 11.099  1.00 38.70 ? 36  ASN   A C   1 
ATOM   259  O O   . ASN   A 1 57  ? 26.725  -13.500 10.870  1.00 40.05 ? 36  ASN   A O   1 
ATOM   260  C CB  . ASN   A 1 57  ? 25.228  -13.165 13.444  1.00 38.36 ? 36  ASN   A CB  1 
ATOM   261  C CG  . ASN   A 1 57  ? 25.243  -12.732 14.890  1.00 39.38 ? 36  ASN   A CG  1 
ATOM   262  O OD1 . ASN   A 1 57  ? 26.219  -12.125 15.360  1.00 37.88 ? 36  ASN   A OD1 1 
ATOM   263  N ND2 . ASN   A 1 57  ? 24.178  -13.063 15.601  1.00 39.04 ? 36  ASN   A ND2 1 
ATOM   264  N N   . SER   A 1 58  ? 24.862  -12.419 10.186  1.00 34.16 ? 37  SER   A N   1 
ATOM   265  C CA  . SER   A 1 58  ? 24.717  -13.202 8.962   1.00 32.50 ? 37  SER   A CA  1 
ATOM   266  C C   . SER   A 1 58  ? 25.561  -12.602 7.833   1.00 31.97 ? 37  SER   A C   1 
ATOM   267  O O   . SER   A 1 58  ? 25.051  -12.154 6.811   1.00 31.27 ? 37  SER   A O   1 
ATOM   268  C CB  . SER   A 1 58  ? 23.248  -13.353 8.567   1.00 32.00 ? 37  SER   A CB  1 
ATOM   269  O OG  . SER   A 1 58  ? 22.540  -14.084 9.566   1.00 28.97 ? 37  SER   A OG  1 
ATOM   270  N N   . ALA   A 1 59  ? 26.888  -12.630 8.015   1.00 33.48 ? 38  ALA   A N   1 
ATOM   271  C CA  . ALA   A 1 59  ? 27.807  -11.943 7.120   1.00 33.29 ? 38  ALA   A CA  1 
ATOM   272  C C   . ALA   A 1 59  ? 27.823  -12.622 5.754   1.00 32.02 ? 38  ALA   A C   1 
ATOM   273  O O   . ALA   A 1 59  ? 27.774  -11.962 4.715   1.00 31.25 ? 38  ALA   A O   1 
ATOM   274  C CB  . ALA   A 1 59  ? 29.210  -11.929 7.735   1.00 37.69 ? 38  ALA   A CB  1 
ATOM   275  N N   . GLU   A 1 60  ? 27.892  -13.959 5.766   1.00 32.86 ? 39  GLU   A N   1 
ATOM   276  C CA  . GLU   A 1 60  ? 27.960  -14.694 4.508   1.00 36.36 ? 39  GLU   A CA  1 
ATOM   277  C C   . GLU   A 1 60  ? 26.708  -14.426 3.661   1.00 39.31 ? 39  GLU   A C   1 
ATOM   278  O O   . GLU   A 1 60  ? 26.798  -14.150 2.456   1.00 37.75 ? 39  GLU   A O   1 
ATOM   279  C CB  . GLU   A 1 60  ? 28.212  -16.171 4.826   1.00 35.78 ? 39  GLU   A CB  1 
ATOM   280  C CG  . GLU   A 1 60  ? 28.079  -17.099 3.616   0.60 37.78 ? 39  GLU   A CG  1 
ATOM   281  C CD  . GLU   A 1 60  ? 28.682  -18.487 3.803   0.60 43.74 ? 39  GLU   A CD  1 
ATOM   282  O OE1 . GLU   A 1 60  ? 28.290  -19.430 3.079   0.60 42.07 ? 39  GLU   A OE1 1 
ATOM   283  O OE2 . GLU   A 1 60  ? 29.573  -18.624 4.670   0.60 45.21 ? 39  GLU   A OE2 1 
ATOM   284  N N   . ALA   A 1 61  ? 25.526  -14.484 4.303   1.00 36.19 ? 40  ALA   A N   1 
ATOM   285  C CA  . ALA   A 1 61  ? 24.279  -14.367 3.559   1.00 30.47 ? 40  ALA   A CA  1 
ATOM   286  C C   . ALA   A 1 61  ? 24.115  -12.946 3.020   1.00 30.74 ? 40  ALA   A C   1 
ATOM   287  O O   . ALA   A 1 61  ? 23.633  -12.765 1.904   1.00 31.40 ? 40  ALA   A O   1 
ATOM   288  C CB  . ALA   A 1 61  ? 23.115  -14.797 4.445   1.00 30.07 ? 40  ALA   A CB  1 
ATOM   289  N N   . ALA   A 1 62  ? 24.521  -11.945 3.822   1.00 29.86 ? 41  ALA   A N   1 
ATOM   290  C CA  . ALA   A 1 62  ? 24.445  -10.554 3.405   1.00 29.31 ? 41  ALA   A CA  1 
ATOM   291  C C   . ALA   A 1 62  ? 25.304  -10.302 2.163   1.00 32.95 ? 41  ALA   A C   1 
ATOM   292  O O   . ALA   A 1 62  ? 24.892  -9.595  1.256   1.00 32.15 ? 41  ALA   A O   1 
ATOM   293  C CB  . ALA   A 1 62  ? 24.868  -9.649  4.545   1.00 28.10 ? 41  ALA   A CB  1 
ATOM   294  N N   . VAL   A 1 63  ? 26.540  -10.822 2.158   1.00 36.95 ? 42  VAL   A N   1 
ATOM   295  C CA  . VAL   A 1 63  ? 27.464  -10.526 1.072   1.00 35.02 ? 42  VAL   A CA  1 
ATOM   296  C C   . VAL   A 1 63  ? 26.974  -11.229 -0.192  1.00 34.21 ? 42  VAL   A C   1 
ATOM   297  O O   . VAL   A 1 63  ? 26.971  -10.643 -1.274  1.00 38.83 ? 42  VAL   A O   1 
ATOM   298  C CB  . VAL   A 1 63  ? 28.898  -10.925 1.455   1.00 37.27 ? 42  VAL   A CB  1 
ATOM   299  C CG1 . VAL   A 1 63  ? 29.826  -10.935 0.237   1.00 37.75 ? 42  VAL   A CG1 1 
ATOM   300  C CG2 . VAL   A 1 63  ? 29.438  -10.037 2.581   1.00 36.44 ? 42  VAL   A CG2 1 
ATOM   301  N N   . SER   A 1 64  ? 26.484  -12.461 -0.016  1.00 34.36 ? 43  SER   A N   1 
ATOM   302  C CA  . SER   A 1 64  ? 25.878  -13.238 -1.092  1.00 32.82 ? 43  SER   A CA  1 
ATOM   303  C C   . SER   A 1 64  ? 24.738  -12.473 -1.769  1.00 35.55 ? 43  SER   A C   1 
ATOM   304  O O   . SER   A 1 64  ? 24.631  -12.440 -2.996  1.00 32.67 ? 43  SER   A O   1 
ATOM   305  C CB  . SER   A 1 64  ? 25.408  -14.571 -0.544  1.00 35.14 ? 43  SER   A CB  1 
ATOM   306  O OG  . SER   A 1 64  ? 24.990  -15.417 -1.602  1.00 38.20 ? 43  SER   A OG  1 
ATOM   307  N N   . LEU   A 1 65  ? 23.860  -11.859 -0.958  1.00 32.60 ? 44  LEU   A N   1 
ATOM   308  C CA  . LEU   A 1 65  ? 22.759  -11.077 -1.501  1.00 30.13 ? 44  LEU   A CA  1 
ATOM   309  C C   . LEU   A 1 65  ? 23.287  -9.863  -2.258  1.00 31.29 ? 44  LEU   A C   1 
ATOM   310  O O   . LEU   A 1 65  ? 22.840  -9.598  -3.372  1.00 34.67 ? 44  LEU   A O   1 
ATOM   311  C CB  . LEU   A 1 65  ? 21.857  -10.616 -0.350  1.00 34.81 ? 44  LEU   A CB  1 
ATOM   312  C CG  . LEU   A 1 65  ? 20.718  -9.678  -0.755  1.00 29.24 ? 44  LEU   A CG  1 
ATOM   313  C CD1 . LEU   A 1 65  ? 19.859  -10.319 -1.824  1.00 28.96 ? 44  LEU   A CD1 1 
ATOM   314  C CD2 . LEU   A 1 65  ? 19.937  -9.389  0.539   1.00 29.92 ? 44  LEU   A CD2 1 
ATOM   315  N N   . ALA   A 1 66  ? 24.207  -9.107  -1.647  1.00 33.42 ? 45  ALA   A N   1 
ATOM   316  C CA  . ALA   A 1 66  ? 24.732  -7.930  -2.331  1.00 35.40 ? 45  ALA   A CA  1 
ATOM   317  C C   . ALA   A 1 66  ? 25.424  -8.342  -3.632  1.00 37.08 ? 45  ALA   A C   1 
ATOM   318  O O   . ALA   A 1 66  ? 25.315  -7.643  -4.629  1.00 35.89 ? 45  ALA   A O   1 
ATOM   319  C CB  . ALA   A 1 66  ? 25.666  -7.135  -1.441  1.00 36.85 ? 45  ALA   A CB  1 
ATOM   320  N N   . ASP   A 1 67  ? 26.093  -9.506  -3.622  1.00 39.07 ? 46  ASP   A N   1 
ATOM   321  C CA  . ASP   A 1 67  ? 26.712  -10.033 -4.832  1.00 42.52 ? 46  ASP   A CA  1 
ATOM   322  C C   . ASP   A 1 67  ? 25.660  -10.254 -5.921  1.00 45.52 ? 46  ASP   A C   1 
ATOM   323  O O   . ASP   A 1 67  ? 25.845  -9.813  -7.054  1.00 48.83 ? 46  ASP   A O   1 
ATOM   324  C CB  . ASP   A 1 67  ? 27.528  -11.295 -4.558  1.00 47.50 ? 46  ASP   A CB  1 
ATOM   325  C CG  . ASP   A 1 67  ? 28.842  -11.117 -3.802  1.00 52.13 ? 46  ASP   A CG  1 
ATOM   326  O OD1 . ASP   A 1 67  ? 29.293  -9.960  -3.680  1.00 48.16 ? 46  ASP   A OD1 1 
ATOM   327  O OD2 . ASP   A 1 67  ? 29.407  -12.138 -3.319  1.00 51.05 ? 46  ASP   A OD2 1 
ATOM   328  N N   . GLU   A 1 68  ? 24.555  -10.939 -5.582  1.00 43.83 ? 47  GLU   A N   1 
ATOM   329  C CA  . GLU   A 1 68  ? 23.470  -11.161 -6.529  1.00 42.47 ? 47  GLU   A CA  1 
ATOM   330  C C   . GLU   A 1 68  ? 22.928  -9.837  -7.071  1.00 41.12 ? 47  GLU   A C   1 
ATOM   331  O O   . GLU   A 1 68  ? 22.713  -9.701  -8.279  1.00 37.24 ? 47  GLU   A O   1 
ATOM   332  C CB  . GLU   A 1 68  ? 22.323  -11.979 -5.948  1.00 47.46 ? 47  GLU   A CB  1 
ATOM   333  C CG  . GLU   A 1 68  ? 22.643  -13.459 -5.756  1.00 46.79 ? 47  GLU   A CG  1 
ATOM   334  C CD  . GLU   A 1 68  ? 21.401  -14.298 -5.487  1.00 50.67 ? 47  GLU   A CD  1 
ATOM   335  O OE1 . GLU   A 1 68  ? 21.313  -14.938 -4.410  1.00 48.61 ? 47  GLU   A OE1 1 
ATOM   336  O OE2 . GLU   A 1 68  ? 20.515  -14.315 -6.373  1.00 54.52 ? 47  GLU   A OE2 1 
ATOM   337  N N   . LEU   A 1 69  ? 22.726  -8.846  -6.184  1.00 37.41 ? 48  LEU   A N   1 
ATOM   338  C CA  . LEU   A 1 69  ? 22.110  -7.609  -6.644  1.00 39.20 ? 48  LEU   A CA  1 
ATOM   339  C C   . LEU   A 1 69  ? 23.073  -6.800  -7.518  1.00 40.54 ? 48  LEU   A C   1 
ATOM   340  O O   . LEU   A 1 69  ? 22.645  -6.236  -8.525  1.00 39.35 ? 48  LEU   A O   1 
ATOM   341  C CB  . LEU   A 1 69  ? 21.517  -6.789  -5.491  1.00 36.97 ? 48  LEU   A CB  1 
ATOM   342  C CG  . LEU   A 1 69  ? 20.548  -7.550  -4.575  1.00 33.83 ? 48  LEU   A CG  1 
ATOM   343  C CD1 . LEU   A 1 69  ? 20.019  -6.630  -3.485  1.00 33.99 ? 48  LEU   A CD1 1 
ATOM   344  C CD2 . LEU   A 1 69  ? 19.394  -8.137  -5.377  1.00 37.52 ? 48  LEU   A CD2 1 
ATOM   345  N N   . ASN   A 1 70  ? 24.363  -6.767  -7.143  1.00 38.68 ? 49  ASN   A N   1 
ATOM   346  C CA  . ASN   A 1 70  ? 25.372  -6.044  -7.915  1.00 43.63 ? 49  ASN   A CA  1 
ATOM   347  C C   . ASN   A 1 70  ? 25.570  -6.669  -9.300  1.00 41.90 ? 49  ASN   A C   1 
ATOM   348  O O   . ASN   A 1 70  ? 25.903  -5.975  -10.263 1.00 42.26 ? 49  ASN   A O   1 
ATOM   349  C CB  . ASN   A 1 70  ? 26.670  -5.876  -7.129  1.00 41.07 ? 49  ASN   A CB  1 
ATOM   350  C CG  . ASN   A 1 70  ? 26.543  -4.816  -6.058  1.00 38.84 ? 49  ASN   A CG  1 
ATOM   351  O OD1 . ASN   A 1 70  ? 25.983  -3.743  -6.308  1.00 40.35 ? 49  ASN   A OD1 1 
ATOM   352  N ND2 . ASN   A 1 70  ? 27.027  -5.102  -4.855  1.00 38.72 ? 49  ASN   A ND2 1 
ATOM   353  N N   . LYS   A 1 71  ? 25.341  -7.984  -9.389  1.00 37.35 ? 50  LYS   A N   1 
ATOM   354  C CA  . LYS   A 1 71  ? 25.494  -8.751  -10.617 1.00 45.25 ? 50  LYS   A CA  1 
ATOM   355  C C   . LYS   A 1 71  ? 24.345  -8.407  -11.554 1.00 48.85 ? 50  LYS   A C   1 
ATOM   356  O O   . LYS   A 1 71  ? 24.456  -8.554  -12.769 1.00 52.64 ? 50  LYS   A O   1 
ATOM   357  C CB  . LYS   A 1 71  ? 25.597  -10.248 -10.294 1.00 42.87 ? 50  LYS   A CB  1 
ATOM   358  C CG  . LYS   A 1 71  ? 25.134  -11.215 -11.385 1.00 57.04 ? 50  LYS   A CG  1 
ATOM   359  C CD  . LYS   A 1 71  ? 25.161  -12.688 -10.981 1.00 58.25 ? 50  LYS   A CD  1 
ATOM   360  N N   . GLU   A 1 72  ? 23.234  -7.964  -10.953 1.00 44.58 ? 51  GLU   A N   1 
ATOM   361  C CA  . GLU   A 1 72  ? 22.061  -7.508  -11.671 1.00 42.01 ? 51  GLU   A CA  1 
ATOM   362  C C   . GLU   A 1 72  ? 22.315  -6.072  -12.156 1.00 41.41 ? 51  GLU   A C   1 
ATOM   363  O O   . GLU   A 1 72  ? 22.073  -5.752  -13.324 1.00 45.59 ? 51  GLU   A O   1 
ATOM   364  C CB  . GLU   A 1 72  ? 20.881  -7.808  -10.731 1.00 41.96 ? 51  GLU   A CB  1 
ATOM   365  C CG  . GLU   A 1 72  ? 19.509  -7.605  -11.361 0.60 45.76 ? 51  GLU   A CG  1 
ATOM   366  C CD  . GLU   A 1 72  ? 19.247  -8.453  -12.583 0.60 51.40 ? 51  GLU   A CD  1 
ATOM   367  O OE1 . GLU   A 1 72  ? 19.524  -9.677  -12.563 0.60 49.41 ? 51  GLU   A OE1 1 
ATOM   368  O OE2 . GLU   A 1 72  ? 18.727  -7.857  -13.546 0.60 50.04 ? 51  GLU   A OE2 1 
ATOM   369  N N   . ARG   A 1 73  ? 22.857  -5.209  -11.282 1.00 36.67 ? 52  ARG   A N   1 
ATOM   370  C CA  . ARG   A 1 73  ? 23.166  -3.829  -11.641 1.00 39.02 ? 52  ARG   A CA  1 
ATOM   371  C C   . ARG   A 1 73  ? 24.365  -3.399  -10.812 1.00 45.43 ? 52  ARG   A C   1 
ATOM   372  O O   . ARG   A 1 73  ? 24.344  -3.512  -9.580  1.00 43.15 ? 52  ARG   A O   1 
ATOM   373  C CB  . ARG   A 1 73  ? 21.974  -2.877  -11.448 1.00 41.36 ? 52  ARG   A CB  1 
ATOM   374  C CG  . ARG   A 1 73  ? 20.705  -3.018  -12.283 1.00 41.90 ? 52  ARG   A CG  1 
ATOM   375  C CD  . ARG   A 1 73  ? 19.841  -1.742  -12.307 1.00 44.77 ? 52  ARG   A CD  1 
ATOM   376  N NE  . ARG   A 1 73  ? 19.469  -1.189  -10.994 1.00 50.95 ? 52  ARG   A NE  1 
ATOM   377  C CZ  . ARG   A 1 73  ? 18.616  -1.725  -10.106 1.00 56.56 ? 52  ARG   A CZ  1 
ATOM   378  N NH1 . ARG   A 1 73  ? 17.922  -2.802  -10.429 1.00 48.60 ? 52  ARG   A NH1 1 
ATOM   379  N NH2 . ARG   A 1 73  ? 18.439  -1.169  -8.911  1.00 48.86 ? 52  ARG   A NH2 1 
ATOM   380  N N   . SER   A 1 74  ? 25.454  -2.961  -11.456 1.00 41.75 ? 53  SER   A N   1 
ATOM   381  C CA  . SER   A 1 74  ? 26.649  -2.876  -10.636 1.00 42.86 ? 53  SER   A CA  1 
ATOM   382  C C   . SER   A 1 74  ? 26.574  -1.627  -9.772  1.00 40.25 ? 53  SER   A C   1 
ATOM   383  O O   . SER   A 1 74  ? 25.877  -0.683  -10.140 1.00 43.33 ? 53  SER   A O   1 
ATOM   384  C CB  . SER   A 1 74  ? 27.922  -2.983  -11.446 1.00 53.45 ? 53  SER   A CB  1 
ATOM   385  O OG  . SER   A 1 74  ? 27.889  -2.022  -12.485 1.00 47.08 ? 53  SER   A OG  1 
ATOM   386  N N   . ASN   A 1 75  ? 27.213  -1.683  -8.590  1.00 38.64 ? 54  ASN   A N   1 
ATOM   387  C CA  . ASN   A 1 75  ? 27.227  -0.575  -7.646  1.00 44.15 ? 54  ASN   A CA  1 
ATOM   388  C C   . ASN   A 1 75  ? 25.801  -0.187  -7.222  1.00 42.36 ? 54  ASN   A C   1 
ATOM   389  O O   . ASN   A 1 75  ? 25.479  1.002   -7.141  1.00 43.46 ? 54  ASN   A O   1 
ATOM   390  C CB  . ASN   A 1 75  ? 27.882  0.678   -8.224  1.00 45.67 ? 54  ASN   A CB  1 
ATOM   391  C CG  . ASN   A 1 75  ? 29.204  0.404   -8.899  1.00 56.78 ? 54  ASN   A CG  1 
ATOM   392  O OD1 . ASN   A 1 75  ? 30.082  -0.225  -8.296  1.00 56.17 ? 54  ASN   A OD1 1 
ATOM   393  N ND2 . ASN   A 1 75  ? 29.356  0.859   -10.140 1.00 56.30 ? 54  ASN   A ND2 1 
ATOM   394  N N   . THR   A 1 76  ? 24.936  -1.176  -6.975  1.00 39.59 ? 55  THR   A N   1 
ATOM   395  C CA  . THR   A 1 76  ? 23.616  -0.823  -6.460  1.00 36.52 ? 55  THR   A CA  1 
ATOM   396  C C   . THR   A 1 76  ? 23.383  -1.399  -5.054  1.00 38.29 ? 55  THR   A C   1 
ATOM   397  O O   . THR   A 1 76  ? 22.380  -1.076  -4.435  1.00 41.67 ? 55  THR   A O   1 
ATOM   398  C CB  . THR   A 1 76  ? 22.507  -1.231  -7.428  1.00 34.23 ? 55  THR   A CB  1 
ATOM   399  O OG1 . THR   A 1 76  ? 22.767  -2.617  -7.584  1.00 36.96 ? 55  THR   A OG1 1 
ATOM   400  C CG2 . THR   A 1 76  ? 22.516  -0.471  -8.746  1.00 35.49 ? 55  THR   A CG2 1 
ATOM   401  N N   . ALA   A 1 77  ? 24.258  -2.278  -4.560  1.00 34.79 ? 56  ALA   A N   1 
ATOM   402  C CA  . ALA   A 1 77  ? 24.065  -2.863  -3.236  1.00 35.11 ? 56  ALA   A CA  1 
ATOM   403  C C   . ALA   A 1 77  ? 25.357  -2.828  -2.428  1.00 38.84 ? 56  ALA   A C   1 
ATOM   404  O O   . ALA   A 1 77  ? 26.426  -3.136  -2.959  1.00 40.79 ? 56  ALA   A O   1 
ATOM   405  C CB  . ALA   A 1 77  ? 23.562  -4.281  -3.367  1.00 29.92 ? 56  ALA   A CB  1 
ATOM   406  N N   . VAL   A 1 78  ? 25.246  -2.492  -1.136  1.00 34.91 ? 57  VAL   A N   1 
ATOM   407  C CA  . VAL   A 1 78  ? 26.332  -2.599  -0.168  1.00 35.73 ? 57  VAL   A CA  1 
ATOM   408  C C   . VAL   A 1 78  ? 25.806  -3.259  1.103   1.00 36.42 ? 57  VAL   A C   1 
ATOM   409  O O   . VAL   A 1 78  ? 24.593  -3.311  1.325   1.00 34.37 ? 57  VAL   A O   1 
ATOM   410  C CB  . VAL   A 1 78  ? 27.006  -1.251  0.163   1.00 37.99 ? 57  VAL   A CB  1 
ATOM   411  C CG1 . VAL   A 1 78  ? 27.651  -0.616  -1.064  1.00 41.32 ? 57  VAL   A CG1 1 
ATOM   412  C CG2 . VAL   A 1 78  ? 26.047  -0.255  0.811   1.00 38.31 ? 57  VAL   A CG2 1 
ATOM   413  N N   . VAL   A 1 79  ? 26.728  -3.776  1.917   1.00 32.44 ? 58  VAL   A N   1 
ATOM   414  C CA  . VAL   A 1 79  ? 26.407  -4.360  3.221   1.00 33.30 ? 58  VAL   A CA  1 
ATOM   415  C C   . VAL   A 1 79  ? 26.881  -3.416  4.321   1.00 35.49 ? 58  VAL   A C   1 
ATOM   416  O O   . VAL   A 1 79  ? 27.734  -2.574  4.066   1.00 36.94 ? 58  VAL   A O   1 
ATOM   417  C CB  . VAL   A 1 79  ? 26.935  -5.797  3.427   1.00 38.55 ? 58  VAL   A CB  1 
ATOM   418  C CG1 . VAL   A 1 79  ? 26.474  -6.703  2.294   1.00 31.93 ? 58  VAL   A CG1 1 
ATOM   419  C CG2 . VAL   A 1 79  ? 28.454  -5.860  3.622   1.00 35.24 ? 58  VAL   A CG2 1 
ATOM   420  N N   . CYS   A 1 80  ? 26.328  -3.561  5.542   1.00 32.88 ? 59  CYS   A N   1 
ATOM   421  C CA  . CYS   A 1 80  ? 26.665  -2.711  6.671   1.00 32.38 ? 59  CYS   A CA  1 
ATOM   422  C C   . CYS   A 1 80  ? 26.379  -3.472  7.957   1.00 37.59 ? 59  CYS   A C   1 
ATOM   423  O O   . CYS   A 1 80  ? 25.214  -3.757  8.248   1.00 35.64 ? 59  CYS   A O   1 
ATOM   424  C CB  . CYS   A 1 80  ? 25.870  -1.410  6.613   1.00 32.97 ? 59  CYS   A CB  1 
ATOM   425  S SG  . CYS   A 1 80  ? 26.240  -0.293  7.991   1.00 39.36 ? 59  CYS   A SG  1 
ATOM   426  N N   . GLN   A 1 81  ? 27.436  -3.814  8.714   1.00 33.06 ? 60  GLN   A N   1 
ATOM   427  C CA  . GLN   A 1 81  ? 27.285  -4.606  9.922   1.00 35.09 ? 60  GLN   A CA  1 
ATOM   428  C C   . GLN   A 1 81  ? 27.000  -3.687  11.104  1.00 33.97 ? 60  GLN   A C   1 
ATOM   429  O O   . GLN   A 1 81  ? 27.636  -2.647  11.258  1.00 35.37 ? 60  GLN   A O   1 
ATOM   430  C CB  . GLN   A 1 81  ? 28.544  -5.453  10.180  1.00 38.97 ? 60  GLN   A CB  1 
ATOM   431  C CG  . GLN   A 1 81  ? 28.411  -6.553  11.233  1.00 33.18 ? 60  GLN   A CG  1 
ATOM   432  C CD  . GLN   A 1 81  ? 28.513  -6.098  12.680  1.00 40.37 ? 60  GLN   A CD  1 
ATOM   433  O OE1 . GLN   A 1 81  ? 29.070  -5.046  13.004  1.00 46.85 ? 60  GLN   A OE1 1 
ATOM   434  N NE2 . GLN   A 1 81  ? 27.989  -6.899  13.598  1.00 40.49 ? 60  GLN   A NE2 1 
ATOM   435  N N   . ALA   A 1 82  ? 26.051  -4.095  11.964  1.00 34.96 ? 61  ALA   A N   1 
ATOM   436  C CA  . ALA   A 1 82  ? 25.863  -3.408  13.230  1.00 31.76 ? 61  ALA   A CA  1 
ATOM   437  C C   . ALA   A 1 82  ? 25.058  -4.269  14.191  1.00 31.18 ? 61  ALA   A C   1 
ATOM   438  O O   . ALA   A 1 82  ? 24.097  -4.915  13.783  1.00 32.84 ? 61  ALA   A O   1 
ATOM   439  C CB  . ALA   A 1 82  ? 25.203  -2.063  13.002  1.00 32.83 ? 61  ALA   A CB  1 
ATOM   440  N N   . ASP   A 1 83  ? 25.408  -4.211  15.476  1.00 31.14 ? 62  ASP   A N   1 
ATOM   441  C CA  . ASP   A 1 83  ? 24.575  -4.754  16.532  1.00 31.42 ? 62  ASP   A CA  1 
ATOM   442  C C   . ASP   A 1 83  ? 23.532  -3.694  16.881  1.00 32.68 ? 62  ASP   A C   1 
ATOM   443  O O   . ASP   A 1 83  ? 23.897  -2.542  17.101  1.00 31.24 ? 62  ASP   A O   1 
ATOM   444  C CB  . ASP   A 1 83  ? 25.431  -5.132  17.729  1.00 37.73 ? 62  ASP   A CB  1 
ATOM   445  C CG  . ASP   A 1 83  ? 24.741  -5.816  18.898  1.00 40.31 ? 62  ASP   A CG  1 
ATOM   446  O OD1 . ASP   A 1 83  ? 23.518  -6.103  18.808  1.00 35.97 ? 62  ASP   A OD1 1 
ATOM   447  O OD2 . ASP   A 1 83  ? 25.447  -6.094  19.902  1.00 37.94 ? 62  ASP   A OD2 1 
ATOM   448  N N   . LEU   A 1 84  ? 22.249  -4.086  16.965  1.00 28.68 ? 63  LEU   A N   1 
ATOM   449  C CA  . LEU   A 1 84  ? 21.184  -3.128  17.248  1.00 28.45 ? 63  LEU   A CA  1 
ATOM   450  C C   . LEU   A 1 84  ? 20.660  -3.279  18.671  1.00 31.73 ? 63  LEU   A C   1 
ATOM   451  O O   . LEU   A 1 84  ? 19.623  -2.692  19.014  1.00 27.29 ? 63  LEU   A O   1 
ATOM   452  C CB  . LEU   A 1 84  ? 20.093  -3.192  16.172  1.00 28.10 ? 63  LEU   A CB  1 
ATOM   453  C CG  . LEU   A 1 84  ? 20.504  -2.725  14.764  1.00 27.36 ? 63  LEU   A CG  1 
ATOM   454  C CD1 . LEU   A 1 84  ? 19.360  -2.845  13.741  1.00 33.30 ? 63  LEU   A CD1 1 
ATOM   455  C CD2 . LEU   A 1 84  ? 21.101  -1.331  14.697  1.00 29.26 ? 63  LEU   A CD2 1 
ATOM   456  N N   . THR   A 1 85  ? 21.381  -4.057  19.496  1.00 26.69 ? 64  THR   A N   1 
ATOM   457  C CA  . THR   A 1 85  ? 21.139  -4.137  20.928  1.00 27.66 ? 64  THR   A CA  1 
ATOM   458  C C   . THR   A 1 85  ? 21.269  -2.733  21.519  1.00 28.57 ? 64  THR   A C   1 
ATOM   459  O O   . THR   A 1 85  ? 22.174  -1.990  21.122  1.00 30.40 ? 64  THR   A O   1 
ATOM   460  C CB  . THR   A 1 85  ? 22.165  -5.095  21.548  1.00 32.28 ? 64  THR   A CB  1 
ATOM   461  O OG1 . THR   A 1 85  ? 21.925  -6.396  21.024  1.00 33.33 ? 64  THR   A OG1 1 
ATOM   462  C CG2 . THR   A 1 85  ? 22.058  -5.200  23.058  1.00 33.27 ? 64  THR   A CG2 1 
ATOM   463  N N   . ASN   A 1 86  ? 20.401  -2.371  22.476  1.00 27.72 ? 65  ASN   A N   1 
ATOM   464  C CA  . ASN   A 1 86  ? 20.557  -1.063  23.111  1.00 28.49 ? 65  ASN   A CA  1 
ATOM   465  C C   . ASN   A 1 86  ? 21.893  -1.006  23.878  1.00 30.72 ? 65  ASN   A C   1 
ATOM   466  O O   . ASN   A 1 86  ? 22.272  -1.963  24.555  1.00 31.02 ? 65  ASN   A O   1 
ATOM   467  C CB  . ASN   A 1 86  ? 19.382  -0.717  24.024  1.00 27.00 ? 65  ASN   A CB  1 
ATOM   468  C CG  . ASN   A 1 86  ? 19.350  0.760   24.350  1.00 28.45 ? 65  ASN   A CG  1 
ATOM   469  O OD1 . ASN   A 1 86  ? 19.572  1.594   23.466  1.00 30.00 ? 65  ASN   A OD1 1 
ATOM   470  N ND2 . ASN   A 1 86  ? 19.154  1.108   25.603  1.00 30.75 ? 65  ASN   A ND2 1 
ATOM   471  N N   . SER   A 1 87  ? 22.529  0.174   23.857  1.00 32.50 ? 66  SER   A N   1 
ATOM   472  C CA  . SER   A 1 87  ? 23.685  0.515   24.685  1.00 32.57 ? 66  SER   A CA  1 
ATOM   473  C C   . SER   A 1 87  ? 24.030  1.976   24.408  1.00 31.86 ? 66  SER   A C   1 
ATOM   474  O O   . SER   A 1 87  ? 23.417  2.613   23.548  1.00 30.15 ? 66  SER   A O   1 
ATOM   475  C CB  . SER   A 1 87  ? 24.863  -0.349  24.353  1.00 35.67 ? 66  SER   A CB  1 
ATOM   476  O OG  . SER   A 1 87  ? 25.351  0.037   23.078  1.00 32.27 ? 66  SER   A OG  1 
ATOM   477  N N   . ASN   A 1 88  ? 25.052  2.488   25.106  1.00 33.64 ? 67  ASN   A N   1 
ATOM   478  C CA  . ASN   A 1 88  ? 25.443  3.880   24.950  1.00 33.99 ? 67  ASN   A CA  1 
ATOM   479  C C   . ASN   A 1 88  ? 25.997  4.145   23.551  1.00 32.55 ? 67  ASN   A C   1 
ATOM   480  O O   . ASN   A 1 88  ? 26.066  5.292   23.127  1.00 34.66 ? 67  ASN   A O   1 
ATOM   481  C CB  . ASN   A 1 88  ? 26.356  4.339   26.089  1.00 31.31 ? 67  ASN   A CB  1 
ATOM   482  C CG  . ASN   A 1 88  ? 25.595  4.570   27.377  1.00 38.14 ? 67  ASN   A CG  1 
ATOM   483  O OD1 . ASN   A 1 88  ? 24.360  4.661   27.366  1.00 44.16 ? 67  ASN   A OD1 1 
ATOM   484  N ND2 . ASN   A 1 88  ? 26.306  4.668   28.493  1.00 39.27 ? 67  ASN   A ND2 1 
ATOM   485  N N   . VAL   A 1 89  ? 26.396  3.105   22.821  1.00 31.11 ? 68  VAL   A N   1 
ATOM   486  C CA  . VAL   A 1 89  ? 26.895  3.372   21.476  1.00 34.33 ? 68  VAL   A CA  1 
ATOM   487  C C   . VAL   A 1 89  ? 25.845  3.081   20.400  1.00 34.13 ? 68  VAL   A C   1 
ATOM   488  O O   . VAL   A 1 89  ? 26.067  3.306   19.204  1.00 30.20 ? 68  VAL   A O   1 
ATOM   489  C CB  . VAL   A 1 89  ? 28.231  2.658   21.170  1.00 35.05 ? 68  VAL   A CB  1 
ATOM   490  C CG1 . VAL   A 1 89  ? 29.170  2.800   22.359  1.00 36.71 ? 68  VAL   A CG1 1 
ATOM   491  C CG2 . VAL   A 1 89  ? 28.045  1.182   20.827  1.00 30.69 ? 68  VAL   A CG2 1 
ATOM   492  N N   . LEU   A 1 90  ? 24.674  2.613   20.818  1.00 32.39 ? 69  LEU   A N   1 
ATOM   493  C CA  . LEU   A 1 90  ? 23.677  2.368   19.781  1.00 27.28 ? 69  LEU   A CA  1 
ATOM   494  C C   . LEU   A 1 90  ? 23.430  3.636   18.960  1.00 23.98 ? 69  LEU   A C   1 
ATOM   495  O O   . LEU   A 1 90  ? 23.286  3.531   17.760  1.00 24.80 ? 69  LEU   A O   1 
ATOM   496  C CB  . LEU   A 1 90  ? 22.386  1.791   20.369  1.00 23.60 ? 69  LEU   A CB  1 
ATOM   497  C CG  . LEU   A 1 90  ? 21.353  1.344   19.333  1.00 28.10 ? 69  LEU   A CG  1 
ATOM   498  C CD1 . LEU   A 1 90  ? 21.794  0.217   18.380  1.00 27.09 ? 69  LEU   A CD1 1 
ATOM   499  C CD2 . LEU   A 1 90  ? 20.017  0.979   20.019  1.00 26.49 ? 69  LEU   A CD2 1 
ATOM   500  N N   . PRO   A 1 91  ? 23.330  4.869   19.522  1.00 24.09 ? 70  PRO   A N   1 
ATOM   501  C CA  . PRO   A 1 91  ? 23.132  6.028   18.667  1.00 24.67 ? 70  PRO   A CA  1 
ATOM   502  C C   . PRO   A 1 91  ? 24.175  6.182   17.559  1.00 28.03 ? 70  PRO   A C   1 
ATOM   503  O O   . PRO   A 1 91  ? 23.819  6.447   16.408  1.00 26.91 ? 70  PRO   A O   1 
ATOM   504  C CB  . PRO   A 1 91  ? 23.004  7.230   19.594  1.00 23.20 ? 70  PRO   A CB  1 
ATOM   505  C CG  . PRO   A 1 91  ? 22.745  6.607   20.965  1.00 25.79 ? 70  PRO   A CG  1 
ATOM   506  C CD  . PRO   A 1 91  ? 23.367  5.220   20.945  1.00 25.80 ? 70  PRO   A CD  1 
ATOM   507  N N   . ALA   A 1 92  ? 25.453  5.933   17.895  1.00 28.33 ? 71  ALA   A N   1 
ATOM   508  C CA  . ALA   A 1 92  ? 26.502  6.001   16.885  1.00 30.76 ? 71  ALA   A CA  1 
ATOM   509  C C   . ALA   A 1 92  ? 26.338  4.928   15.812  1.00 26.02 ? 71  ALA   A C   1 
ATOM   510  O O   . ALA   A 1 92  ? 26.533  5.218   14.653  1.00 25.56 ? 71  ALA   A O   1 
ATOM   511  C CB  . ALA   A 1 92  ? 27.873  5.910   17.522  1.00 31.53 ? 71  ALA   A CB  1 
ATOM   512  N N   . SER   A 1 93  ? 26.027  3.691   16.211  1.00 26.92 ? 72  SER   A N   1 
ATOM   513  C CA  . SER   A 1 93  ? 25.839  2.620   15.256  1.00 26.15 ? 72  SER   A CA  1 
ATOM   514  C C   . SER   A 1 93  ? 24.704  2.974   14.296  1.00 28.13 ? 72  SER   A C   1 
ATOM   515  O O   . SER   A 1 93  ? 24.815  2.740   13.095  1.00 26.99 ? 72  SER   A O   1 
ATOM   516  C CB  . SER   A 1 93  ? 25.531  1.342   15.935  1.00 32.77 ? 72  SER   A CB  1 
ATOM   517  O OG  . SER   A 1 93  ? 26.568  0.934   16.812  1.00 33.06 ? 72  SER   A OG  1 
ATOM   518  N N   . CYS   A 1 94  ? 23.604  3.528   14.834  1.00 28.34 ? 73  CYS   A N   1 
ATOM   519  C CA  . CYS   A 1 94  ? 22.488  3.910   13.970  1.00 25.72 ? 73  CYS   A CA  1 
ATOM   520  C C   . CYS   A 1 94  ? 22.866  5.039   13.012  1.00 26.65 ? 73  CYS   A C   1 
ATOM   521  O O   . CYS   A 1 94  ? 22.517  5.015   11.840  1.00 26.23 ? 73  CYS   A O   1 
ATOM   522  C CB  . CYS   A 1 94  ? 21.243  4.188   14.795  1.00 23.71 ? 73  CYS   A CB  1 
ATOM   523  S SG  . CYS   A 1 94  ? 20.642  2.706   15.639  1.00 28.72 ? 73  CYS   A SG  1 
ATOM   524  N N   . GLU   A 1 95  ? 23.552  6.071   13.528  1.00 29.37 ? 74  GLU   A N   1 
ATOM   525  C CA  . GLU   A 1 95  ? 24.041  7.135   12.667  1.00 30.35 ? 74  GLU   A CA  1 
ATOM   526  C C   . GLU   A 1 95  ? 24.889  6.563   11.528  1.00 30.26 ? 74  GLU   A C   1 
ATOM   527  O O   . GLU   A 1 95  ? 24.800  7.041   10.397  1.00 31.81 ? 74  GLU   A O   1 
ATOM   528  C CB  . GLU   A 1 95  ? 24.802  8.167   13.503  1.00 30.92 ? 74  GLU   A CB  1 
ATOM   529  C CG  . GLU   A 1 95  ? 25.296  9.371   12.711  1.00 40.70 ? 74  GLU   A CG  1 
ATOM   530  C CD  . GLU   A 1 95  ? 25.788  10.451  13.654  0.70 48.80 ? 74  GLU   A CD  1 
ATOM   531  O OE1 . GLU   A 1 95  ? 26.942  10.883  13.470  0.70 62.91 ? 74  GLU   A OE1 1 
ATOM   532  O OE2 . GLU   A 1 95  ? 25.052  10.845  14.581  0.70 45.65 ? 74  GLU   A OE2 1 
ATOM   533  N N   . GLU   A 1 96  ? 25.716  5.558   11.842  1.00 31.92 ? 75  GLU   A N   1 
ATOM   534  C CA  . GLU   A 1 96  ? 26.675  5.019   10.884  1.00 30.51 ? 75  GLU   A CA  1 
ATOM   535  C C   . GLU   A 1 96  ? 25.948  4.232   9.797   1.00 30.85 ? 75  GLU   A C   1 
ATOM   536  O O   . GLU   A 1 96  ? 26.329  4.294   8.632   1.00 30.82 ? 75  GLU   A O   1 
ATOM   537  C CB  . GLU   A 1 96  ? 27.739  4.215   11.646  1.00 36.57 ? 75  GLU   A CB  1 
ATOM   538  C CG  . GLU   A 1 96  ? 28.618  3.364   10.734  1.00 36.99 ? 75  GLU   A CG  1 
ATOM   539  C CD  . GLU   A 1 96  ? 29.368  4.154   9.683   1.00 32.38 ? 75  GLU   A CD  1 
ATOM   540  O OE1 . GLU   A 1 96  ? 29.476  5.415   9.803   1.00 35.14 ? 75  GLU   A OE1 1 
ATOM   541  O OE2 . GLU   A 1 96  ? 29.840  3.467   8.734   1.00 35.62 ? 75  GLU   A OE2 1 
ATOM   542  N N   . ILE   A 1 97  ? 24.886  3.487   10.177  1.00 28.73 ? 76  ILE   A N   1 
ATOM   543  C CA  . ILE   A 1 97  ? 24.052  2.818   9.186   1.00 27.61 ? 76  ILE   A CA  1 
ATOM   544  C C   . ILE   A 1 97  ? 23.545  3.836   8.155   1.00 28.89 ? 76  ILE   A C   1 
ATOM   545  O O   . ILE   A 1 97  ? 23.617  3.641   6.939   1.00 28.89 ? 76  ILE   A O   1 
ATOM   546  C CB  . ILE   A 1 97  ? 22.899  2.058   9.880   1.00 29.19 ? 76  ILE   A CB  1 
ATOM   547  C CG1 . ILE   A 1 97  ? 23.452  0.911   10.737  1.00 33.72 ? 76  ILE   A CG1 1 
ATOM   548  C CG2 . ILE   A 1 97  ? 21.931  1.543   8.827   1.00 31.68 ? 76  ILE   A CG2 1 
ATOM   549  C CD1 . ILE   A 1 97  ? 22.443  0.129   11.560  1.00 28.97 ? 76  ILE   A CD1 1 
ATOM   550  N N   . ILE   A 1 98  ? 22.948  4.922   8.641   1.00 29.75 ? 77  ILE   A N   1 
ATOM   551  C CA  . ILE   A 1 98  ? 22.461  5.911   7.701   1.00 29.59 ? 77  ILE   A CA  1 
ATOM   552  C C   . ILE   A 1 98  ? 23.646  6.498   6.908   1.00 33.53 ? 77  ILE   A C   1 
ATOM   553  O O   . ILE   A 1 98  ? 23.550  6.695   5.702   1.00 30.96 ? 77  ILE   A O   1 
ATOM   554  C CB  . ILE   A 1 98  ? 21.651  6.970   8.472   1.00 30.43 ? 77  ILE   A CB  1 
ATOM   555  C CG1 . ILE   A 1 98  ? 20.407  6.304   9.150   1.00 28.45 ? 77  ILE   A CG1 1 
ATOM   556  C CG2 . ILE   A 1 98  ? 21.230  8.121   7.552   1.00 27.73 ? 77  ILE   A CG2 1 
ATOM   557  C CD1 . ILE   A 1 98  ? 19.508  5.553   8.156   1.00 28.54 ? 77  ILE   A CD1 1 
ATOM   558  N N   . ASN   A 1 99  ? 24.775  6.762   7.584   1.00 33.75 ? 78  ASN   A N   1 
ATOM   559  C CA  . ASN   A 1 99  ? 25.926  7.351   6.889   1.00 34.73 ? 78  ASN   A CA  1 
ATOM   560  C C   . ASN   A 1 99  ? 26.408  6.470   5.745   1.00 33.65 ? 78  ASN   A C   1 
ATOM   561  O O   . ASN   A 1 99  ? 26.860  6.978   4.724   1.00 34.92 ? 78  ASN   A O   1 
ATOM   562  C CB  . ASN   A 1 99  ? 27.054  7.656   7.867   1.00 36.07 ? 78  ASN   A CB  1 
ATOM   563  C CG  . ASN   A 1 99  ? 26.752  8.910   8.647   1.00 38.70 ? 78  ASN   A CG  1 
ATOM   564  O OD1 . ASN   A 1 99  ? 26.051  9.805   8.157   1.00 45.28 ? 78  ASN   A OD1 1 
ATOM   565  N ND2 . ASN   A 1 99  ? 27.287  9.005   9.854   1.00 40.30 ? 78  ASN   A ND2 1 
ATOM   566  N N   . SER   A 1 100 ? 26.293  5.154   5.921   1.00 33.29 ? 79  SER   A N   1 
ATOM   567  C CA  . SER   A 1 100 ? 26.750  4.168   4.957   1.00 36.38 ? 79  SER   A CA  1 
ATOM   568  C C   . SER   A 1 100 ? 25.986  4.295   3.651   1.00 38.46 ? 79  SER   A C   1 
ATOM   569  O O   . SER   A 1 100 ? 26.527  4.037   2.583   1.00 34.78 ? 79  SER   A O   1 
ATOM   570  C CB  . SER   A 1 100 ? 26.595  2.766   5.494   1.00 40.47 ? 79  SER   A CB  1 
ATOM   571  O OG  . SER   A 1 100 ? 27.438  2.604   6.619   1.00 46.76 ? 79  SER   A OG  1 
ATOM   572  N N   . CYS   A 1 101 ? 24.701  4.657   3.762   1.00 33.98 ? 80  CYS   A N   1 
ATOM   573  C CA  . CYS   A 1 101 ? 23.862  4.824   2.599   1.00 31.14 ? 80  CYS   A CA  1 
ATOM   574  C C   . CYS   A 1 101 ? 24.305  6.077   1.846   1.00 30.43 ? 80  CYS   A C   1 
ATOM   575  O O   . CYS   A 1 101 ? 24.394  6.058   0.618   1.00 33.13 ? 80  CYS   A O   1 
ATOM   576  C CB  . CYS   A 1 101 ? 22.388  4.864   3.028   1.00 30.27 ? 80  CYS   A CB  1 
ATOM   577  S SG  . CYS   A 1 101 ? 21.230  4.736   1.654   1.00 32.15 ? 80  CYS   A SG  1 
ATOM   578  N N   . PHE   A 1 102 ? 24.526  7.167   2.596   1.00 31.69 ? 81  PHE   A N   1 
ATOM   579  C CA  . PHE   A 1 102 ? 24.960  8.415   1.986   1.00 35.78 ? 81  PHE   A CA  1 
ATOM   580  C C   . PHE   A 1 102 ? 26.356  8.259   1.382   1.00 40.06 ? 81  PHE   A C   1 
ATOM   581  O O   . PHE   A 1 102 ? 26.603  8.800   0.309   1.00 40.17 ? 81  PHE   A O   1 
ATOM   582  C CB  . PHE   A 1 102 ? 24.988  9.580   2.976   1.00 34.32 ? 81  PHE   A CB  1 
ATOM   583  C CG  . PHE   A 1 102 ? 23.619  10.227  3.114   1.00 42.12 ? 81  PHE   A CG  1 
ATOM   584  C CD1 . PHE   A 1 102 ? 23.197  11.214  2.224   1.00 39.58 ? 81  PHE   A CD1 1 
ATOM   585  C CD2 . PHE   A 1 102 ? 22.749  9.836   4.136   1.00 38.85 ? 81  PHE   A CD2 1 
ATOM   586  C CE1 . PHE   A 1 102 ? 21.943  11.806  2.365   1.00 42.69 ? 81  PHE   A CE1 1 
ATOM   587  C CE2 . PHE   A 1 102 ? 21.489  10.414  4.252   1.00 41.43 ? 81  PHE   A CE2 1 
ATOM   588  C CZ  . PHE   A 1 102 ? 21.091  11.399  3.377   1.00 39.65 ? 81  PHE   A CZ  1 
ATOM   589  N N   . ARG   A 1 103 ? 27.239  7.511   2.066   1.00 39.55 ? 82  ARG   A N   1 
ATOM   590  C CA  . ARG   A 1 103 ? 28.596  7.277   1.588   1.00 40.54 ? 82  ARG   A CA  1 
ATOM   591  C C   . ARG   A 1 103 ? 28.548  6.482   0.292   1.00 40.55 ? 82  ARG   A C   1 
ATOM   592  O O   . ARG   A 1 103 ? 29.249  6.816   -0.654  1.00 40.94 ? 82  ARG   A O   1 
ATOM   593  C CB  . ARG   A 1 103 ? 29.485  6.470   2.540   1.00 38.67 ? 82  ARG   A CB  1 
ATOM   594  C CG  . ARG   A 1 103 ? 30.141  7.275   3.651   1.00 46.88 ? 82  ARG   A CG  1 
ATOM   595  C CD  . ARG   A 1 103 ? 31.401  6.534   4.088   1.00 44.72 ? 82  ARG   A CD  1 
ATOM   596  N NE  . ARG   A 1 103 ? 31.154  5.140   4.476   1.00 45.60 ? 82  ARG   A NE  1 
ATOM   597  C CZ  . ARG   A 1 103 ? 30.625  4.751   5.641   1.00 35.96 ? 82  ARG   A CZ  1 
ATOM   598  N NH1 . ARG   A 1 103 ? 30.316  3.482   5.812   1.00 35.25 ? 82  ARG   A NH1 1 
ATOM   599  N NH2 . ARG   A 1 103 ? 30.383  5.630   6.596   1.00 37.46 ? 82  ARG   A NH2 1 
ATOM   600  N N   . ALA   A 1 104 ? 27.704  5.443   0.234   1.00 36.12 ? 83  ALA   A N   1 
ATOM   601  C CA  . ALA   A 1 104 ? 27.682  4.622   -0.959  1.00 37.55 ? 83  ALA   A CA  1 
ATOM   602  C C   . ALA   A 1 104 ? 26.938  5.288   -2.112  1.00 39.04 ? 83  ALA   A C   1 
ATOM   603  O O   . ALA   A 1 104 ? 27.360  5.141   -3.253  1.00 33.64 ? 83  ALA   A O   1 
ATOM   604  C CB  . ALA   A 1 104 ? 27.174  3.225   -0.690  1.00 33.92 ? 83  ALA   A CB  1 
ATOM   605  N N   . PHE   A 1 105 ? 25.833  5.988   -1.832  1.00 37.37 ? 84  PHE   A N   1 
ATOM   606  C CA  . PHE   A 1 105 ? 24.891  6.316   -2.892  1.00 34.14 ? 84  PHE   A CA  1 
ATOM   607  C C   . PHE   A 1 105 ? 24.550  7.799   -2.937  1.00 31.42 ? 84  PHE   A C   1 
ATOM   608  O O   . PHE   A 1 105 ? 23.864  8.236   -3.857  1.00 38.03 ? 84  PHE   A O   1 
ATOM   609  C CB  . PHE   A 1 105 ? 23.579  5.555   -2.673  1.00 33.67 ? 84  PHE   A CB  1 
ATOM   610  C CG  . PHE   A 1 105 ? 23.778  4.051   -2.675  1.00 32.17 ? 84  PHE   A CG  1 
ATOM   611  C CD1 . PHE   A 1 105 ? 24.424  3.424   -3.730  1.00 32.72 ? 84  PHE   A CD1 1 
ATOM   612  C CD2 . PHE   A 1 105 ? 23.273  3.264   -1.646  1.00 33.80 ? 84  PHE   A CD2 1 
ATOM   613  C CE1 . PHE   A 1 105 ? 24.590  2.042   -3.747  1.00 33.88 ? 84  PHE   A CE1 1 
ATOM   614  C CE2 . PHE   A 1 105 ? 23.413  1.877   -1.678  1.00 36.04 ? 84  PHE   A CE2 1 
ATOM   615  C CZ  . PHE   A 1 105 ? 24.098  1.271   -2.715  1.00 39.75 ? 84  PHE   A CZ  1 
ATOM   616  N N   . GLY   A 1 106 ? 24.960  8.556   -1.925  1.00 32.51 ? 85  GLY   A N   1 
ATOM   617  C CA  . GLY   A 1 106 ? 24.804  9.997   -2.005  1.00 34.65 ? 85  GLY   A CA  1 
ATOM   618  C C   . GLY   A 1 106 ? 23.400  10.472  -1.619  1.00 36.88 ? 85  GLY   A C   1 
ATOM   619  O O   . GLY   A 1 106 ? 23.094  11.661  -1.708  1.00 36.87 ? 85  GLY   A O   1 
ATOM   620  N N   . ARG   A 1 107 ? 22.567  9.552   -1.125  1.00 36.66 ? 86  ARG   A N   1 
ATOM   621  C CA  . ARG   A 1 107 ? 21.239  9.934   -0.656  1.00 36.33 ? 86  ARG   A CA  1 
ATOM   622  C C   . ARG   A 1 107 ? 20.642  8.771   0.139   1.00 36.85 ? 86  ARG   A C   1 
ATOM   623  O O   . ARG   A 1 107 ? 21.191  7.681   0.122   1.00 33.88 ? 86  ARG   A O   1 
ATOM   624  C CB  . ARG   A 1 107 ? 20.351  10.251  -1.865  1.00 34.19 ? 86  ARG   A CB  1 
ATOM   625  C CG  . ARG   A 1 107 ? 20.211  9.028   -2.758  1.00 31.63 ? 86  ARG   A CG  1 
ATOM   626  C CD  . ARG   A 1 107 ? 19.586  9.331   -4.125  1.00 38.83 ? 86  ARG   A CD  1 
ATOM   627  N NE  . ARG   A 1 107 ? 18.181  9.757   -4.062  1.00 40.65 ? 86  ARG   A NE  1 
ATOM   628  C CZ  . ARG   A 1 107 ? 17.459  10.282  -5.059  1.00 46.09 ? 86  ARG   A CZ  1 
ATOM   629  N NH1 . ARG   A 1 107 ? 18.007  10.541  -6.234  1.00 40.07 ? 86  ARG   A NH1 1 
ATOM   630  N NH2 . ARG   A 1 107 ? 16.178  10.550  -4.875  1.00 38.77 ? 86  ARG   A NH2 1 
ATOM   631  N N   . CYS   A 1 108 ? 19.535  9.021   0.863   1.00 36.13 ? 87  CYS   A N   1 
ATOM   632  C CA  . CYS   A 1 108 ? 18.839  7.949   1.557   1.00 31.94 ? 87  CYS   A CA  1 
ATOM   633  C C   . CYS   A 1 108 ? 17.351  8.295   1.556   1.00 28.97 ? 87  CYS   A C   1 
ATOM   634  O O   . CYS   A 1 108 ? 16.946  9.236   2.249   1.00 31.88 ? 87  CYS   A O   1 
ATOM   635  C CB  . CYS   A 1 108 ? 19.337  7.826   2.993   1.00 34.48 ? 87  CYS   A CB  1 
ATOM   636  S SG  . CYS   A 1 108 ? 18.629  6.417   3.906   1.00 33.01 ? 87  CYS   A SG  1 
ATOM   637  N N   . ASP   A 1 109 ? 16.558  7.519   0.796   1.00 29.67 ? 88  ASP   A N   1 
ATOM   638  C CA  . ASP   A 1 109 ? 15.178  7.905   0.529   1.00 29.16 ? 88  ASP   A CA  1 
ATOM   639  C C   . ASP   A 1 109 ? 14.199  7.105   1.390   1.00 29.54 ? 88  ASP   A C   1 
ATOM   640  O O   . ASP   A 1 109 ? 13.126  7.624   1.703   1.00 27.58 ? 88  ASP   A O   1 
ATOM   641  C CB  . ASP   A 1 109 ? 14.840  7.709   -0.932  1.00 30.70 ? 88  ASP   A CB  1 
ATOM   642  C CG  . ASP   A 1 109 ? 15.701  8.590   -1.831  1.00 36.84 ? 88  ASP   A CG  1 
ATOM   643  O OD1 . ASP   A 1 109 ? 15.293  9.745   -2.079  1.00 35.04 ? 88  ASP   A OD1 1 
ATOM   644  O OD2 . ASP   A 1 109 ? 16.795  8.136   -2.196  1.00 33.45 ? 88  ASP   A OD2 1 
ATOM   645  N N   . VAL   A 1 110 ? 14.587  5.864   1.724   1.00 29.72 ? 89  VAL   A N   1 
ATOM   646  C CA  . VAL   A 1 110 ? 13.736  4.908   2.445   1.00 28.05 ? 89  VAL   A CA  1 
ATOM   647  C C   . VAL   A 1 110 ? 14.526  4.201   3.552   1.00 29.16 ? 89  VAL   A C   1 
ATOM   648  O O   . VAL   A 1 110 ? 15.675  3.775   3.367   1.00 27.28 ? 89  VAL   A O   1 
ATOM   649  C CB  . VAL   A 1 110 ? 13.203  3.904   1.402   1.00 30.27 ? 89  VAL   A CB  1 
ATOM   650  C CG1 . VAL   A 1 110 ? 12.561  2.684   2.061   1.00 32.20 ? 89  VAL   A CG1 1 
ATOM   651  C CG2 . VAL   A 1 110 ? 12.228  4.543   0.418   1.00 28.95 ? 89  VAL   A CG2 1 
ATOM   652  N N   . LEU   A 1 111 ? 13.900  4.057   4.730   1.00 25.12 ? 90  LEU   A N   1 
ATOM   653  C CA  . LEU   A 1 111 ? 14.427  3.288   5.840   1.00 24.54 ? 90  LEU   A CA  1 
ATOM   654  C C   . LEU   A 1 111 ? 13.372  2.228   6.142   1.00 24.67 ? 90  LEU   A C   1 
ATOM   655  O O   . LEU   A 1 111 ? 12.232  2.612   6.405   1.00 23.31 ? 90  LEU   A O   1 
ATOM   656  C CB  . LEU   A 1 111 ? 14.663  4.177   7.074   1.00 23.20 ? 90  LEU   A CB  1 
ATOM   657  C CG  . LEU   A 1 111 ? 14.838  3.459   8.423   1.00 23.72 ? 90  LEU   A CG  1 
ATOM   658  C CD1 . LEU   A 1 111 ? 16.105  2.566   8.447   1.00 26.64 ? 90  LEU   A CD1 1 
ATOM   659  C CD2 . LEU   A 1 111 ? 14.873  4.554   9.492   1.00 25.58 ? 90  LEU   A CD2 1 
ATOM   660  N N   . VAL   A 1 112 ? 13.758  0.946   6.114   1.00 24.66 ? 91  VAL   A N   1 
ATOM   661  C CA  . VAL   A 1 112 ? 12.879  -0.142  6.531   1.00 24.62 ? 91  VAL   A CA  1 
ATOM   662  C C   . VAL   A 1 112 ? 13.430  -0.727  7.836   1.00 27.20 ? 91  VAL   A C   1 
ATOM   663  O O   . VAL   A 1 112 ? 14.524  -1.320  7.845   1.00 23.09 ? 91  VAL   A O   1 
ATOM   664  C CB  . VAL   A 1 112 ? 12.685  -1.219  5.435   1.00 23.33 ? 91  VAL   A CB  1 
ATOM   665  C CG1 . VAL   A 1 112 ? 11.756  -2.333  5.949   1.00 25.57 ? 91  VAL   A CG1 1 
ATOM   666  C CG2 . VAL   A 1 112 ? 12.125  -0.639  4.135   1.00 24.09 ? 91  VAL   A CG2 1 
ATOM   667  N N   . ASN   A 1 113 ? 12.689  -0.530  8.964   1.00 23.94 ? 92  ASN   A N   1 
ATOM   668  C CA  . ASN   A 1 113 ? 13.078  -1.074  10.255  1.00 22.52 ? 92  ASN   A CA  1 
ATOM   669  C C   . ASN   A 1 113 ? 12.535  -2.507  10.385  1.00 25.50 ? 92  ASN   A C   1 
ATOM   670  O O   . ASN   A 1 113 ? 11.387  -2.693  10.828  1.00 24.65 ? 92  ASN   A O   1 
ATOM   671  C CB  . ASN   A 1 113 ? 12.601  -0.216  11.425  1.00 22.65 ? 92  ASN   A CB  1 
ATOM   672  C CG  . ASN   A 1 113 ? 13.421  1.045   11.504  1.00 23.92 ? 92  ASN   A CG  1 
ATOM   673  O OD1 . ASN   A 1 113 ? 14.647  0.956   11.629  1.00 24.55 ? 92  ASN   A OD1 1 
ATOM   674  N ND2 . ASN   A 1 113 ? 12.798  2.217   11.426  1.00 22.74 ? 92  ASN   A ND2 1 
ATOM   675  N N   . ASN   A 1 114 ? 13.360  -3.504  9.980   1.00 23.12 ? 93  ASN   A N   1 
ATOM   676  C CA  . ASN   A 1 114 ? 12.983  -4.920  9.860   1.00 22.91 ? 93  ASN   A CA  1 
ATOM   677  C C   . ASN   A 1 114 ? 13.654  -5.791  10.938  1.00 25.00 ? 93  ASN   A C   1 
ATOM   678  O O   . ASN   A 1 114 ? 13.048  -6.741  11.436  1.00 22.91 ? 93  ASN   A O   1 
ATOM   679  C CB  . ASN   A 1 114 ? 13.278  -5.457  8.448   1.00 23.57 ? 93  ASN   A CB  1 
ATOM   680  C CG  . ASN   A 1 114 ? 13.095  -6.964  8.352   1.00 27.47 ? 93  ASN   A CG  1 
ATOM   681  O OD1 . ASN   A 1 114 ? 11.969  -7.467  8.177   1.00 23.18 ? 93  ASN   A OD1 1 
ATOM   682  N ND2 . ASN   A 1 114 ? 14.191  -7.726  8.431   1.00 24.54 ? 93  ASN   A ND2 1 
ATOM   683  N N   . ALA   A 1 115 ? 14.917  -5.474  11.326  1.00 25.72 ? 94  ALA   A N   1 
ATOM   684  C CA  . ALA   A 1 115 ? 15.695  -6.304  12.254  1.00 25.09 ? 94  ALA   A CA  1 
ATOM   685  C C   . ALA   A 1 115 ? 14.926  -6.512  13.564  1.00 26.38 ? 94  ALA   A C   1 
ATOM   686  O O   . ALA   A 1 115 ? 14.331  -5.578  14.066  1.00 26.06 ? 94  ALA   A O   1 
ATOM   687  C CB  . ALA   A 1 115 ? 17.016  -5.607  12.557  1.00 25.55 ? 94  ALA   A CB  1 
ATOM   688  N N   . SER   A 1 116 ? 14.968  -7.714  14.147  1.00 23.75 ? 95  SER   A N   1 
ATOM   689  C CA  . SER   A 1 116 ? 14.174  -7.952  15.341  1.00 25.40 ? 95  SER   A CA  1 
ATOM   690  C C   . SER   A 1 116 ? 14.749  -9.132  16.114  1.00 28.08 ? 95  SER   A C   1 
ATOM   691  O O   . SER   A 1 116 ? 14.959  -10.186 15.509  1.00 27.92 ? 95  SER   A O   1 
ATOM   692  C CB  . SER   A 1 116 ? 12.716  -8.261  14.885  1.00 27.22 ? 95  SER   A CB  1 
ATOM   693  O OG  . SER   A 1 116 ? 11.905  -8.674  15.975  1.00 28.06 ? 95  SER   A OG  1 
ATOM   694  N N   . ALA   A 1 117 ? 14.945  -8.973  17.437  1.00 28.16 ? 96  ALA   A N   1 
ATOM   695  C CA  . ALA   A 1 117 ? 15.169  -10.111 18.331  1.00 28.49 ? 96  ALA   A CA  1 
ATOM   696  C C   . ALA   A 1 117 ? 13.813  -10.646 18.782  1.00 32.58 ? 96  ALA   A C   1 
ATOM   697  O O   . ALA   A 1 117 ? 12.893  -9.868  19.022  1.00 30.48 ? 96  ALA   A O   1 
ATOM   698  C CB  . ALA   A 1 117 ? 15.989  -9.678  19.522  1.00 26.64 ? 96  ALA   A CB  1 
ATOM   699  N N   . PHE   A 1 118 ? 13.691  -11.972 18.939  1.00 31.58 ? 97  PHE   A N   1 
ATOM   700  C CA  . PHE   A 1 118 ? 12.429  -12.548 19.357  1.00 31.47 ? 97  PHE   A CA  1 
ATOM   701  C C   . PHE   A 1 118 ? 12.723  -13.793 20.187  1.00 33.52 ? 97  PHE   A C   1 
ATOM   702  O O   . PHE   A 1 118 ? 13.283  -14.721 19.629  1.00 32.33 ? 97  PHE   A O   1 
ATOM   703  C CB  . PHE   A 1 118 ? 11.659  -12.967 18.096  1.00 32.87 ? 97  PHE   A CB  1 
ATOM   704  C CG  . PHE   A 1 118 ? 10.372  -13.738 18.386  1.00 37.50 ? 97  PHE   A CG  1 
ATOM   705  C CD1 . PHE   A 1 118 ? 10.367  -15.132 18.495  1.00 42.31 ? 97  PHE   A CD1 1 
ATOM   706  C CD2 . PHE   A 1 118 ? 9.156   -13.074 18.540  1.00 34.31 ? 97  PHE   A CD2 1 
ATOM   707  C CE1 . PHE   A 1 118 ? 9.183   -15.828 18.746  1.00 41.20 ? 97  PHE   A CE1 1 
ATOM   708  C CE2 . PHE   A 1 118 ? 7.985   -13.769 18.780  1.00 30.75 ? 97  PHE   A CE2 1 
ATOM   709  C CZ  . PHE   A 1 118 ? 7.985   -15.144 18.867  1.00 36.35 ? 97  PHE   A CZ  1 
ATOM   710  N N   . TYR   A 1 119 ? 12.316  -13.809 21.465  1.00 28.96 ? 98  TYR   A N   1 
ATOM   711  C CA  . TYR   A 1 119 ? 12.426  -14.980 22.315  1.00 29.79 ? 98  TYR   A CA  1 
ATOM   712  C C   . TYR   A 1 119 ? 11.642  -14.724 23.595  1.00 29.72 ? 98  TYR   A C   1 
ATOM   713  O O   . TYR   A 1 119 ? 11.348  -13.582 23.945  1.00 28.25 ? 98  TYR   A O   1 
ATOM   714  C CB  . TYR   A 1 119 ? 13.889  -15.372 22.597  1.00 31.17 ? 98  TYR   A CB  1 
ATOM   715  C CG  . TYR   A 1 119 ? 14.784  -14.263 23.141  1.00 29.68 ? 98  TYR   A CG  1 
ATOM   716  C CD1 . TYR   A 1 119 ? 14.746  -13.886 24.482  1.00 31.92 ? 98  TYR   A CD1 1 
ATOM   717  C CD2 . TYR   A 1 119 ? 15.648  -13.565 22.294  1.00 28.70 ? 98  TYR   A CD2 1 
ATOM   718  C CE1 . TYR   A 1 119 ? 15.558  -12.868 24.972  1.00 31.70 ? 98  TYR   A CE1 1 
ATOM   719  C CE2 . TYR   A 1 119 ? 16.482  -12.574 22.780  1.00 28.30 ? 98  TYR   A CE2 1 
ATOM   720  C CZ  . TYR   A 1 119 ? 16.434  -12.213 24.116  1.00 33.50 ? 98  TYR   A CZ  1 
ATOM   721  O OH  . TYR   A 1 119 ? 17.291  -11.232 24.578  1.00 34.45 ? 98  TYR   A OH  1 
ATOM   722  N N   . PRO   A 1 120 ? 11.228  -15.800 24.290  1.00 30.10 ? 99  PRO   A N   1 
ATOM   723  C CA  . PRO   A 1 120 ? 10.521  -15.694 25.569  1.00 33.44 ? 99  PRO   A CA  1 
ATOM   724  C C   . PRO   A 1 120 ? 11.280  -15.003 26.700  1.00 32.09 ? 99  PRO   A C   1 
ATOM   725  O O   . PRO   A 1 120 ? 12.493  -15.184 26.846  1.00 33.36 ? 99  PRO   A O   1 
ATOM   726  C CB  . PRO   A 1 120 ? 10.176  -17.147 25.931  1.00 36.80 ? 99  PRO   A CB  1 
ATOM   727  C CG  . PRO   A 1 120 ? 11.083  -18.004 25.050  1.00 34.44 ? 99  PRO   A CG  1 
ATOM   728  C CD  . PRO   A 1 120 ? 11.349  -17.190 23.800  1.00 35.57 ? 99  PRO   A CD  1 
ATOM   729  N N   . THR   A 1 121 ? 10.542  -14.240 27.506  1.00 33.26 ? 100 THR   A N   1 
ATOM   730  C CA  . THR   A 1 121 ? 11.040  -13.641 28.743  1.00 28.69 ? 100 THR   A CA  1 
ATOM   731  C C   . THR   A 1 121 ? 9.993   -13.837 29.831  1.00 30.07 ? 100 THR   A C   1 
ATOM   732  O O   . THR   A 1 121 ? 9.265   -12.910 30.177  1.00 29.99 ? 100 THR   A O   1 
ATOM   733  C CB  . THR   A 1 121 ? 11.379  -12.170 28.527  1.00 32.83 ? 100 THR   A CB  1 
ATOM   734  O OG1 . THR   A 1 121 ? 10.129  -11.575 28.145  1.00 32.22 ? 100 THR   A OG1 1 
ATOM   735  C CG2 . THR   A 1 121 ? 12.516  -12.020 27.530  1.00 28.45 ? 100 THR   A CG2 1 
ATOM   736  N N   . PRO   A 1 122 ? 9.844   -15.068 30.377  1.00 29.28 ? 101 PRO   A N   1 
ATOM   737  C CA  . PRO   A 1 122 ? 8.770   -15.338 31.342  1.00 34.10 ? 101 PRO   A CA  1 
ATOM   738  C C   . PRO   A 1 122 ? 8.831   -14.428 32.572  1.00 33.03 ? 101 PRO   A C   1 
ATOM   739  O O   . PRO   A 1 122 ? 9.919   -14.102 33.047  1.00 35.65 ? 101 PRO   A O   1 
ATOM   740  C CB  . PRO   A 1 122 ? 8.888   -16.826 31.717  1.00 35.44 ? 101 PRO   A CB  1 
ATOM   741  C CG  . PRO   A 1 122 ? 10.176  -17.283 31.033  1.00 35.08 ? 101 PRO   A CG  1 
ATOM   742  C CD  . PRO   A 1 122 ? 10.668  -16.239 30.041  1.00 33.32 ? 101 PRO   A CD  1 
ATOM   743  N N   . LEU   A 1 123 ? 7.658   -14.039 33.089  1.00 32.21 ? 102 LEU   A N   1 
ATOM   744  C CA  . LEU   A 1 123 ? 7.602   -13.154 34.255  1.00 36.94 ? 102 LEU   A CA  1 
ATOM   745  C C   . LEU   A 1 123 ? 7.851   -13.907 35.565  1.00 44.11 ? 102 LEU   A C   1 
ATOM   746  O O   . LEU   A 1 123 ? 8.413   -13.336 36.502  1.00 46.92 ? 102 LEU   A O   1 
ATOM   747  C CB  . LEU   A 1 123 ? 6.278   -12.398 34.347  1.00 33.22 ? 102 LEU   A CB  1 
ATOM   748  C CG  . LEU   A 1 123 ? 5.982   -11.388 33.231  1.00 32.12 ? 102 LEU   A CG  1 
ATOM   749  C CD1 . LEU   A 1 123 ? 4.479   -11.092 33.206  1.00 30.30 ? 102 LEU   A CD1 1 
ATOM   750  C CD2 . LEU   A 1 123 ? 6.779   -10.133 33.422  1.00 33.57 ? 102 LEU   A CD2 1 
ATOM   751  N N   . VAL   A 1 124 ? 7.350   -15.146 35.645  1.00 44.27 ? 103 VAL   A N   1 
ATOM   752  C CA  . VAL   A 1 124 ? 7.597   -16.037 36.773  1.00 45.14 ? 103 VAL   A CA  1 
ATOM   753  C C   . VAL   A 1 124 ? 8.546   -17.114 36.257  1.00 59.64 ? 103 VAL   A C   1 
ATOM   754  O O   . VAL   A 1 124 ? 8.254   -17.775 35.253  1.00 54.67 ? 103 VAL   A O   1 
ATOM   755  C CB  . VAL   A 1 124 ? 6.283   -16.655 37.296  1.00 45.63 ? 103 VAL   A CB  1 
ATOM   756  N N   . GLN   A 1 125 ? 9.697   -17.237 36.929  1.00 70.98 ? 104 GLN   A N   1 
ATOM   757  C CA  . GLN   A 1 125 ? 10.836  -17.968 36.396  1.00 84.48 ? 104 GLN   A CA  1 
ATOM   758  C C   . GLN   A 1 125 ? 11.455  -18.835 37.509  1.00 79.94 ? 104 GLN   A C   1 
ATOM   759  O O   . GLN   A 1 125 ? 12.267  -19.716 37.153  1.00 75.85 ? 104 GLN   A O   1 
ATOM   760  C CB  . GLN   A 1 125 ? 11.832  -17.000 35.747  1.00 87.72 ? 104 GLN   A CB  1 
ATOM   761  N N   . GLY   A 1 134 ? 21.980  -18.741 30.470  1.00 84.44 ? 113 GLY   A N   1 
ATOM   762  C CA  . GLY   A 1 134 ? 21.220  -17.867 29.553  1.00 78.93 ? 113 GLY   A CA  1 
ATOM   763  C C   . GLY   A 1 134 ? 21.611  -16.404 29.738  1.00 70.70 ? 113 GLY   A C   1 
ATOM   764  O O   . GLY   A 1 134 ? 22.702  -16.100 30.214  1.00 65.27 ? 113 GLY   A O   1 
ATOM   765  N N   . LYS   A 1 135 ? 20.697  -15.505 29.361  1.00 65.43 ? 114 LYS   A N   1 
ATOM   766  C CA  . LYS   A 1 135 ? 20.945  -14.074 29.423  1.00 48.47 ? 114 LYS   A CA  1 
ATOM   767  C C   . LYS   A 1 135 ? 20.400  -13.501 30.727  1.00 41.30 ? 114 LYS   A C   1 
ATOM   768  O O   . LYS   A 1 135 ? 19.406  -13.997 31.252  1.00 46.06 ? 114 LYS   A O   1 
ATOM   769  C CB  . LYS   A 1 135 ? 20.264  -13.471 28.198  1.00 47.75 ? 114 LYS   A CB  1 
ATOM   770  C CG  . LYS   A 1 135 ? 21.020  -13.746 26.913  1.00 48.26 ? 114 LYS   A CG  1 
ATOM   771  C CD  . LYS   A 1 135 ? 20.121  -13.639 25.692  1.00 45.79 ? 114 LYS   A CD  1 
ATOM   772  C CE  . LYS   A 1 135 ? 20.899  -13.375 24.445  1.00 42.66 ? 114 LYS   A CE  1 
ATOM   773  N NZ  . LYS   A 1 135 ? 20.136  -13.849 23.298  1.00 45.79 ? 114 LYS   A NZ  1 
ATOM   774  N N   . THR   A 1 136 ? 21.092  -12.472 31.244  1.00 34.99 ? 115 THR   A N   1 
ATOM   775  C CA  . THR   A 1 136 ? 20.607  -11.639 32.328  1.00 36.56 ? 115 THR   A CA  1 
ATOM   776  C C   . THR   A 1 136 ? 19.410  -10.836 31.791  1.00 32.96 ? 115 THR   A C   1 
ATOM   777  O O   . THR   A 1 136 ? 19.294  -10.616 30.582  1.00 36.03 ? 115 THR   A O   1 
ATOM   778  C CB  . THR   A 1 136 ? 21.710  -10.711 32.837  1.00 37.20 ? 115 THR   A CB  1 
ATOM   779  O OG1 . THR   A 1 136 ? 21.784  -9.594  31.955  1.00 42.63 ? 115 THR   A OG1 1 
ATOM   780  C CG2 . THR   A 1 136 ? 23.093  -11.339 32.840  1.00 41.85 ? 115 THR   A CG2 1 
ATOM   781  N N   . VAL   A 1 137 ? 18.519  -10.457 32.704  1.00 36.81 ? 116 VAL   A N   1 
ATOM   782  C CA  . VAL   A 1 137 ? 17.314  -9.733  32.337  1.00 36.79 ? 116 VAL   A CA  1 
ATOM   783  C C   . VAL   A 1 137 ? 17.737  -8.440  31.646  1.00 37.59 ? 116 VAL   A C   1 
ATOM   784  O O   . VAL   A 1 137 ? 17.078  -7.990  30.711  1.00 38.35 ? 116 VAL   A O   1 
ATOM   785  C CB  . VAL   A 1 137 ? 16.396  -9.477  33.550  1.00 40.49 ? 116 VAL   A CB  1 
ATOM   786  C CG1 . VAL   A 1 137 ? 17.034  -8.539  34.565  1.00 42.70 ? 116 VAL   A CG1 1 
ATOM   787  C CG2 . VAL   A 1 137 ? 15.039  -8.923  33.122  1.00 42.76 ? 116 VAL   A CG2 1 
ATOM   788  N N   . GLU   A 1 138 ? 18.854  -7.853  32.101  1.00 41.60 ? 117 GLU   A N   1 
ATOM   789  C CA  . GLU   A 1 138 ? 19.336  -6.584  31.569  1.00 41.53 ? 117 GLU   A CA  1 
ATOM   790  C C   . GLU   A 1 138 ? 19.714  -6.762  30.105  1.00 34.66 ? 117 GLU   A C   1 
ATOM   791  O O   . GLU   A 1 138 ? 19.485  -5.856  29.304  1.00 33.74 ? 117 GLU   A O   1 
ATOM   792  C CB  . GLU   A 1 138 ? 20.596  -5.993  32.220  1.00 50.98 ? 117 GLU   A CB  1 
ATOM   793  C CG  . GLU   A 1 138 ? 20.516  -5.770  33.727  0.70 52.92 ? 117 GLU   A CG  1 
ATOM   794  C CD  . GLU   A 1 138 ? 20.981  -6.888  34.654  0.70 51.22 ? 117 GLU   A CD  1 
ATOM   795  O OE1 . GLU   A 1 138 ? 20.337  -7.958  34.744  0.70 42.30 ? 117 GLU   A OE1 1 
ATOM   796  O OE2 . GLU   A 1 138 ? 22.012  -6.653  35.318  0.70 51.58 ? 117 GLU   A OE2 1 
ATOM   797  N N   . THR   A 1 139 ? 20.239  -7.939  29.741  1.00 34.31 ? 118 THR   A N   1 
ATOM   798  C CA  . THR   A 1 139 ? 20.578  -8.237  28.351  1.00 31.85 ? 118 THR   A CA  1 
ATOM   799  C C   . THR   A 1 139 ? 19.301  -8.434  27.512  1.00 28.47 ? 118 THR   A C   1 
ATOM   800  O O   . THR   A 1 139 ? 19.252  -8.048  26.347  1.00 28.76 ? 118 THR   A O   1 
ATOM   801  C CB  . THR   A 1 139 ? 21.428  -9.507  28.287  1.00 38.89 ? 118 THR   A CB  1 
ATOM   802  O OG1 . THR   A 1 139 ? 22.677  -9.260  28.937  1.00 41.79 ? 118 THR   A OG1 1 
ATOM   803  C CG2 . THR   A 1 139 ? 21.635  -9.999  26.869  1.00 35.01 ? 118 THR   A CG2 1 
ATOM   804  N N   . GLN   A 1 140 ? 18.324  -9.171  28.062  1.00 28.98 ? 119 GLN   A N   1 
ATOM   805  C CA  . GLN   A 1 140 ? 17.041  -9.357  27.389  1.00 27.93 ? 119 GLN   A CA  1 
ATOM   806  C C   . GLN   A 1 140 ? 16.416  -7.999  27.052  1.00 27.41 ? 119 GLN   A C   1 
ATOM   807  O O   . GLN   A 1 140 ? 15.917  -7.775  25.946  1.00 29.49 ? 119 GLN   A O   1 
ATOM   808  C CB  . GLN   A 1 140 ? 16.128  -10.259 28.214  1.00 30.57 ? 119 GLN   A CB  1 
ATOM   809  C CG  . GLN   A 1 140 ? 16.700  -11.669 28.362  1.00 34.35 ? 119 GLN   A CG  1 
ATOM   810  C CD  . GLN   A 1 140 ? 15.988  -12.470 29.422  1.00 38.27 ? 119 GLN   A CD  1 
ATOM   811  O OE1 . GLN   A 1 140 ? 15.098  -11.976 30.114  1.00 44.34 ? 119 GLN   A OE1 1 
ATOM   812  N NE2 . GLN   A 1 140 ? 16.374  -13.724 29.563  1.00 48.65 ? 119 GLN   A NE2 1 
ATOM   813  N N   . VAL   A 1 141 ? 16.378  -7.113  28.041  1.00 27.57 ? 120 VAL   A N   1 
ATOM   814  C CA  . VAL   A 1 141 ? 15.804  -5.791  27.799  1.00 25.54 ? 120 VAL   A CA  1 
ATOM   815  C C   . VAL   A 1 141 ? 16.564  -5.114  26.658  1.00 27.05 ? 120 VAL   A C   1 
ATOM   816  O O   . VAL   A 1 141 ? 15.988  -4.591  25.709  1.00 25.63 ? 120 VAL   A O   1 
ATOM   817  C CB  . VAL   A 1 141 ? 15.854  -4.965  29.096  1.00 25.40 ? 120 VAL   A CB  1 
ATOM   818  C CG1 . VAL   A 1 141 ? 15.568  -3.483  28.851  1.00 26.82 ? 120 VAL   A CG1 1 
ATOM   819  C CG2 . VAL   A 1 141 ? 14.891  -5.513  30.142  1.00 27.43 ? 120 VAL   A CG2 1 
ATOM   820  N N   . ALA   A 1 142 ? 17.896  -5.087  26.744  1.00 24.91 ? 121 ALA   A N   1 
ATOM   821  C CA  . ALA   A 1 142 ? 18.734  -4.460  25.737  1.00 27.45 ? 121 ALA   A CA  1 
ATOM   822  C C   . ALA   A 1 142 ? 18.441  -4.955  24.316  1.00 27.10 ? 121 ALA   A C   1 
ATOM   823  O O   . ALA   A 1 142 ? 18.350  -4.163  23.380  1.00 25.15 ? 121 ALA   A O   1 
ATOM   824  C CB  . ALA   A 1 142 ? 20.208  -4.666  26.112  1.00 26.06 ? 121 ALA   A CB  1 
ATOM   825  N N   . GLU   A 1 143 ? 18.318  -6.280  24.153  1.00 27.35 ? 122 GLU   A N   1 
ATOM   826  C CA  . GLU   A 1 143 ? 18.177  -6.879  22.837  1.00 30.02 ? 122 GLU   A CA  1 
ATOM   827  C C   . GLU   A 1 143 ? 16.746  -6.714  22.309  1.00 27.99 ? 122 GLU   A C   1 
ATOM   828  O O   . GLU   A 1 143 ? 16.557  -6.222  21.209  1.00 26.81 ? 122 GLU   A O   1 
ATOM   829  C CB  . GLU   A 1 143 ? 18.514  -8.374  22.838  1.00 35.58 ? 122 GLU   A CB  1 
ATOM   830  C CG  . GLU   A 1 143 ? 20.003  -8.657  23.066  1.00 39.19 ? 122 GLU   A CG  1 
ATOM   831  C CD  . GLU   A 1 143 ? 20.439  -10.124 23.034  1.00 48.63 ? 122 GLU   A CD  1 
ATOM   832  O OE1 . GLU   A 1 143 ? 19.572  -11.020 23.196  1.00 38.30 ? 122 GLU   A OE1 1 
ATOM   833  O OE2 . GLU   A 1 143 ? 21.668  -10.369 22.848  1.00 48.00 ? 122 GLU   A OE2 1 
ATOM   834  N N   . LEU   A 1 144 ? 15.758  -7.051  23.142  1.00 26.69 ? 123 LEU   A N   1 
ATOM   835  C CA  . LEU   A 1 144 ? 14.373  -7.076  22.691  1.00 24.80 ? 123 LEU   A CA  1 
ATOM   836  C C   . LEU   A 1 144 ? 13.849  -5.655  22.518  1.00 26.81 ? 123 LEU   A C   1 
ATOM   837  O O   . LEU   A 1 144 ? 13.232  -5.386  21.485  1.00 29.55 ? 123 LEU   A O   1 
ATOM   838  C CB  . LEU   A 1 144 ? 13.549  -7.946  23.639  1.00 27.41 ? 123 LEU   A CB  1 
ATOM   839  C CG  . LEU   A 1 144 ? 13.836  -9.451  23.523  1.00 29.68 ? 123 LEU   A CG  1 
ATOM   840  C CD1 . LEU   A 1 144 ? 13.182  -10.162 24.710  1.00 27.09 ? 123 LEU   A CD1 1 
ATOM   841  C CD2 . LEU   A 1 144 ? 13.274  -9.981  22.191  1.00 29.73 ? 123 LEU   A CD2 1 
ATOM   842  N N   . ILE   A 1 145 ? 14.134  -4.760  23.482  1.00 25.20 ? 124 ILE   A N   1 
ATOM   843  C CA  . ILE   A 1 145 ? 13.664  -3.379  23.373  1.00 27.38 ? 124 ILE   A CA  1 
ATOM   844  C C   . ILE   A 1 145 ? 14.576  -2.611  22.417  1.00 23.86 ? 124 ILE   A C   1 
ATOM   845  O O   . ILE   A 1 145 ? 14.143  -1.759  21.626  1.00 23.88 ? 124 ILE   A O   1 
ATOM   846  C CB  . ILE   A 1 145 ? 13.488  -2.701  24.754  1.00 23.95 ? 124 ILE   A CB  1 
ATOM   847  C CG1 . ILE   A 1 145 ? 12.675  -3.565  25.729  1.00 24.69 ? 124 ILE   A CG1 1 
ATOM   848  C CG2 . ILE   A 1 145 ? 12.908  -1.286  24.591  1.00 24.95 ? 124 ILE   A CG2 1 
ATOM   849  C CD1 . ILE   A 1 145 ? 11.265  -3.908  25.272  1.00 24.18 ? 124 ILE   A CD1 1 
ATOM   850  N N   . GLY   A 1 146 ? 15.889  -2.895  22.472  1.00 23.30 ? 125 GLY   A N   1 
ATOM   851  C CA  . GLY   A 1 146 ? 16.794  -2.233  21.538  1.00 22.69 ? 125 GLY   A CA  1 
ATOM   852  C C   . GLY   A 1 146 ? 16.520  -2.534  20.069  1.00 23.83 ? 125 GLY   A C   1 
ATOM   853  O O   . GLY   A 1 146 ? 16.377  -1.630  19.256  1.00 24.48 ? 125 GLY   A O   1 
ATOM   854  N N   . THR   A 1 147 ? 16.403  -3.814  19.679  1.00 23.62 ? 126 THR   A N   1 
ATOM   855  C CA  . THR   A 1 147 ? 16.241  -4.060  18.254  1.00 23.78 ? 126 THR   A CA  1 
ATOM   856  C C   . THR   A 1 147 ? 14.845  -3.633  17.797  1.00 24.63 ? 126 THR   A C   1 
ATOM   857  O O   . THR   A 1 147 ? 14.717  -3.079  16.719  1.00 25.66 ? 126 THR   A O   1 
ATOM   858  C CB  . THR   A 1 147 ? 16.443  -5.529  17.919  1.00 27.40 ? 126 THR   A CB  1 
ATOM   859  O OG1 . THR   A 1 147 ? 15.483  -6.234  18.700  1.00 28.56 ? 126 THR   A OG1 1 
ATOM   860  C CG2 . THR   A 1 147 ? 17.827  -6.013  18.306  1.00 29.43 ? 126 THR   A CG2 1 
ATOM   861  N N   . ASN   A 1 148 ? 13.818  -3.851  18.634  1.00 24.43 ? 127 ASN   A N   1 
ATOM   862  C CA  . ASN   A 1 148 ? 12.439  -3.703  18.174  1.00 26.29 ? 127 ASN   A CA  1 
ATOM   863  C C   . ASN   A 1 148 ? 11.948  -2.260  18.257  1.00 26.95 ? 127 ASN   A C   1 
ATOM   864  O O   . ASN   A 1 148 ? 10.934  -1.912  17.618  1.00 25.44 ? 127 ASN   A O   1 
ATOM   865  C CB  . ASN   A 1 148 ? 11.494  -4.638  18.929  1.00 25.35 ? 127 ASN   A CB  1 
ATOM   866  C CG  . ASN   A 1 148 ? 11.711  -6.081  18.520  1.00 28.32 ? 127 ASN   A CG  1 
ATOM   867  O OD1 . ASN   A 1 148 ? 11.415  -6.404  17.362  1.00 31.93 ? 127 ASN   A OD1 1 
ATOM   868  N ND2 . ASN   A 1 148 ? 12.133  -6.951  19.443  1.00 25.15 ? 127 ASN   A ND2 1 
ATOM   869  N N   . ALA   A 1 149 ? 12.615  -1.432  19.078  1.00 23.57 ? 128 ALA   A N   1 
ATOM   870  C CA  . ALA   A 1 149 ? 12.061  -0.099  19.299  1.00 22.30 ? 128 ALA   A CA  1 
ATOM   871  C C   . ALA   A 1 149 ? 13.139  0.992   19.346  1.00 24.38 ? 128 ALA   A C   1 
ATOM   872  O O   . ALA   A 1 149 ? 12.975  2.032   18.707  1.00 24.11 ? 128 ALA   A O   1 
ATOM   873  C CB  . ALA   A 1 149 ? 11.273  -0.068  20.596  1.00 23.33 ? 128 ALA   A CB  1 
ATOM   874  N N   . ILE   A 1 150 ? 14.192  0.786   20.150  1.00 21.76 ? 129 ILE   A N   1 
ATOM   875  C CA  . ILE   A 1 150 ? 15.131  1.883   20.387  1.00 23.43 ? 129 ILE   A CA  1 
ATOM   876  C C   . ILE   A 1 150 ? 15.922  2.116   19.091  1.00 22.00 ? 129 ILE   A C   1 
ATOM   877  O O   . ILE   A 1 150 ? 16.122  3.249   18.660  1.00 24.30 ? 129 ILE   A O   1 
ATOM   878  C CB  . ILE   A 1 150 ? 16.068  1.671   21.592  1.00 23.91 ? 129 ILE   A CB  1 
ATOM   879  C CG1 . ILE   A 1 150 ? 15.354  1.402   22.981  1.00 24.72 ? 129 ILE   A CG1 1 
ATOM   880  C CG2 . ILE   A 1 150 ? 17.022  2.874   21.712  1.00 26.49 ? 129 ILE   A CG2 1 
ATOM   881  C CD1 . ILE   A 1 150 ? 14.120  2.248   23.233  1.00 28.95 ? 129 ILE   A CD1 1 
ATOM   882  N N   . ALA   A 1 151 ? 16.438  1.042   18.502  1.00 20.83 ? 130 ALA   A N   1 
ATOM   883  C CA  . ALA   A 1 151 ? 17.142  1.219   17.225  1.00 22.83 ? 130 ALA   A CA  1 
ATOM   884  C C   . ALA   A 1 151 ? 16.269  1.853   16.152  1.00 24.89 ? 130 ALA   A C   1 
ATOM   885  O O   . ALA   A 1 151 ? 16.697  2.803   15.506  1.00 20.57 ? 130 ALA   A O   1 
ATOM   886  C CB  . ALA   A 1 151 ? 17.839  -0.042  16.751  1.00 22.25 ? 130 ALA   A CB  1 
ATOM   887  N N   . PRO   A 1 152 ? 14.998  1.405   15.921  1.00 23.20 ? 131 PRO   A N   1 
ATOM   888  C CA  . PRO   A 1 152 ? 14.128  2.137   15.012  1.00 24.96 ? 131 PRO   A CA  1 
ATOM   889  C C   . PRO   A 1 152 ? 14.051  3.640   15.321  1.00 22.58 ? 131 PRO   A C   1 
ATOM   890  O O   . PRO   A 1 152 ? 14.069  4.438   14.392  1.00 25.66 ? 131 PRO   A O   1 
ATOM   891  C CB  . PRO   A 1 152 ? 12.790  1.359   15.208  1.00 23.22 ? 131 PRO   A CB  1 
ATOM   892  C CG  . PRO   A 1 152 ? 13.283  -0.080  15.335  1.00 25.79 ? 131 PRO   A CG  1 
ATOM   893  C CD  . PRO   A 1 152 ? 14.421  0.127   16.380  1.00 23.42 ? 131 PRO   A CD  1 
ATOM   894  N N   . PHE   A 1 153 ? 13.971  4.005   16.608  1.00 23.95 ? 132 PHE   A N   1 
ATOM   895  C CA  . PHE   A 1 153 ? 13.866  5.428   16.986  1.00 22.71 ? 132 PHE   A CA  1 
ATOM   896  C C   . PHE   A 1 153 ? 15.140  6.183   16.591  1.00 26.44 ? 132 PHE   A C   1 
ATOM   897  O O   . PHE   A 1 153 ? 15.097  7.263   15.975  1.00 24.28 ? 132 PHE   A O   1 
ATOM   898  C CB  . PHE   A 1 153 ? 13.605  5.528   18.492  1.00 24.44 ? 132 PHE   A CB  1 
ATOM   899  C CG  . PHE   A 1 153 ? 13.893  6.874   19.168  1.00 26.90 ? 132 PHE   A CG  1 
ATOM   900  C CD1 . PHE   A 1 153 ? 12.997  7.925   19.076  1.00 26.79 ? 132 PHE   A CD1 1 
ATOM   901  C CD2 . PHE   A 1 153 ? 15.049  7.057   19.922  1.00 30.03 ? 132 PHE   A CD2 1 
ATOM   902  C CE1 . PHE   A 1 153 ? 13.235  9.146   19.703  1.00 31.17 ? 132 PHE   A CE1 1 
ATOM   903  C CE2 . PHE   A 1 153 ? 15.299  8.286   20.545  1.00 29.62 ? 132 PHE   A CE2 1 
ATOM   904  C CZ  . PHE   A 1 153 ? 14.387  9.320   20.459  1.00 26.94 ? 132 PHE   A CZ  1 
ATOM   905  N N   . LEU   A 1 154 ? 16.295  5.580   16.910  1.00 25.80 ? 133 LEU   A N   1 
ATOM   906  C CA  . LEU   A 1 154 ? 17.574  6.270   16.677  1.00 26.01 ? 133 LEU   A CA  1 
ATOM   907  C C   . LEU   A 1 154 ? 17.833  6.353   15.181  1.00 24.06 ? 133 LEU   A C   1 
ATOM   908  O O   . LEU   A 1 154 ? 18.236  7.396   14.665  1.00 24.84 ? 133 LEU   A O   1 
ATOM   909  C CB  . LEU   A 1 154 ? 18.710  5.533   17.393  1.00 22.52 ? 133 LEU   A CB  1 
ATOM   910  C CG  . LEU   A 1 154 ? 18.673  5.675   18.913  1.00 25.71 ? 133 LEU   A CG  1 
ATOM   911  C CD1 . LEU   A 1 154 ? 19.643  4.693   19.568  1.00 26.58 ? 133 LEU   A CD1 1 
ATOM   912  C CD2 . LEU   A 1 154 ? 18.916  7.115   19.330  1.00 28.08 ? 133 LEU   A CD2 1 
ATOM   913  N N   . LEU   A 1 155 ? 17.476  5.274   14.466  1.00 26.08 ? 134 LEU   A N   1 
ATOM   914  C CA  . LEU   A 1 155 ? 17.603  5.275   13.014  1.00 25.81 ? 134 LEU   A CA  1 
ATOM   915  C C   . LEU   A 1 155 ? 16.677  6.302   12.369  1.00 27.24 ? 134 LEU   A C   1 
ATOM   916  O O   . LEU   A 1 155 ? 17.018  6.907   11.344  1.00 27.36 ? 134 LEU   A O   1 
ATOM   917  C CB  . LEU   A 1 155 ? 17.325  3.898   12.418  1.00 25.71 ? 134 LEU   A CB  1 
ATOM   918  C CG  . LEU   A 1 155 ? 18.424  2.868   12.688  1.00 25.85 ? 134 LEU   A CG  1 
ATOM   919  C CD1 . LEU   A 1 155 ? 17.850  1.455   12.538  1.00 26.97 ? 134 LEU   A CD1 1 
ATOM   920  C CD2 . LEU   A 1 155 ? 19.605  3.148   11.728  1.00 26.32 ? 134 LEU   A CD2 1 
ATOM   921  N N   . THR   A 1 156 ? 15.500  6.493   12.964  1.00 24.56 ? 135 THR   A N   1 
ATOM   922  C CA  . THR   A 1 156 ? 14.555  7.479   12.441  1.00 24.27 ? 135 THR   A CA  1 
ATOM   923  C C   . THR   A 1 156 ? 15.147  8.882   12.611  1.00 25.66 ? 135 THR   A C   1 
ATOM   924  O O   . THR   A 1 156 ? 15.062  9.685   11.690  1.00 27.65 ? 135 THR   A O   1 
ATOM   925  C CB  . THR   A 1 156 ? 13.204  7.370   13.170  1.00 24.61 ? 135 THR   A CB  1 
ATOM   926  O OG1 . THR   A 1 156 ? 12.589  6.151   12.753  1.00 24.94 ? 135 THR   A OG1 1 
ATOM   927  C CG2 . THR   A 1 156 ? 12.255  8.492   12.790  1.00 25.14 ? 135 THR   A CG2 1 
ATOM   928  N N   . MET   A 1 157 ? 15.661  9.158   13.809  1.00 28.42 ? 136 MET   A N   1 
ATOM   929  C CA  . MET   A 1 157 ? 16.338  10.407  14.151  1.00 30.48 ? 136 MET   A CA  1 
ATOM   930  C C   . MET   A 1 157 ? 17.462  10.687  13.145  1.00 28.32 ? 136 MET   A C   1 
ATOM   931  O O   . MET   A 1 157 ? 17.504  11.759  12.509  1.00 31.65 ? 136 MET   A O   1 
ATOM   932  C CB  . MET   A 1 157 ? 16.974  10.293  15.540  1.00 31.59 ? 136 MET   A CB  1 
ATOM   933  C CG  . MET   A 1 157 ? 16.037  10.366  16.723  1.00 41.23 ? 136 MET   A CG  1 
ATOM   934  S SD  . MET   A 1 157 ? 16.982  10.699  18.232  1.00 48.06 ? 136 MET   A SD  1 
ATOM   935  C CE  . MET   A 1 157 ? 17.729  12.211  17.606  1.00 38.04 ? 136 MET   A CE  1 
ATOM   936  N N   . SER   A 1 158 ? 18.352  9.709   12.936  1.00 28.73 ? 137 SER   A N   1 
ATOM   937  C CA  . SER   A 1 158 ? 19.441  9.909   11.978  1.00 31.60 ? 137 SER   A CA  1 
ATOM   938  C C   . SER   A 1 158 ? 18.940  10.098  10.546  1.00 30.70 ? 137 SER   A C   1 
ATOM   939  O O   . SER   A 1 158 ? 19.485  10.886  9.787   1.00 30.50 ? 137 SER   A O   1 
ATOM   940  C CB  . SER   A 1 158 ? 20.488  8.803   12.015  1.00 29.34 ? 137 SER   A CB  1 
ATOM   941  O OG  . SER   A 1 158 ? 21.183  8.797   13.246  1.00 32.24 ? 137 SER   A OG  1 
ATOM   942  N N   . PHE   A 1 159 ? 17.913  9.355   10.131  1.00 31.27 ? 138 PHE   A N   1 
ATOM   943  C CA  . PHE   A 1 159 ? 17.465  9.438   8.746   1.00 27.57 ? 138 PHE   A CA  1 
ATOM   944  C C   . PHE   A 1 159 ? 16.909  10.832  8.493   1.00 28.55 ? 138 PHE   A C   1 
ATOM   945  O O   . PHE   A 1 159 ? 17.189  11.445  7.459   1.00 29.33 ? 138 PHE   A O   1 
ATOM   946  C CB  . PHE   A 1 159 ? 16.361  8.383   8.570   1.00 28.32 ? 138 PHE   A CB  1 
ATOM   947  C CG  . PHE   A 1 159 ? 15.640  8.468   7.230   1.00 25.65 ? 138 PHE   A CG  1 
ATOM   948  C CD1 . PHE   A 1 159 ? 14.518  9.290   7.075   1.00 27.66 ? 138 PHE   A CD1 1 
ATOM   949  C CD2 . PHE   A 1 159 ? 16.038  7.687   6.147   1.00 25.39 ? 138 PHE   A CD2 1 
ATOM   950  C CE1 . PHE   A 1 159 ? 13.850  9.344   5.857   1.00 29.09 ? 138 PHE   A CE1 1 
ATOM   951  C CE2 . PHE   A 1 159 ? 15.359  7.727   4.924   1.00 25.27 ? 138 PHE   A CE2 1 
ATOM   952  C CZ  . PHE   A 1 159 ? 14.267  8.558   4.779   1.00 27.71 ? 138 PHE   A CZ  1 
ATOM   953  N N   . ALA   A 1 160 ? 16.171  11.356  9.483   1.00 28.00 ? 139 ALA   A N   1 
ATOM   954  C CA  . ALA   A 1 160 ? 15.538  12.656  9.298   1.00 31.47 ? 139 ALA   A CA  1 
ATOM   955  C C   . ALA   A 1 160 ? 16.599  13.765  9.386   1.00 34.04 ? 139 ALA   A C   1 
ATOM   956  O O   . ALA   A 1 160 ? 16.560  14.739  8.621   1.00 32.49 ? 139 ALA   A O   1 
ATOM   957  C CB  . ALA   A 1 160 ? 14.434  12.855  10.301  1.00 34.12 ? 139 ALA   A CB  1 
ATOM   958  N N   . GLN   A 1 161 ? 17.571  13.579  10.286  1.00 33.87 ? 140 GLN   A N   1 
ATOM   959  C CA  . GLN   A 1 161 ? 18.541  14.651  10.490  1.00 40.40 ? 140 GLN   A CA  1 
ATOM   960  C C   . GLN   A 1 161 ? 19.438  14.791  9.264   1.00 42.08 ? 140 GLN   A C   1 
ATOM   961  O O   . GLN   A 1 161 ? 19.822  15.902  8.906   1.00 44.70 ? 140 GLN   A O   1 
ATOM   962  C CB  . GLN   A 1 161 ? 19.245  14.576  11.840  1.00 38.98 ? 140 GLN   A CB  1 
ATOM   963  C CG  . GLN   A 1 161 ? 18.287  14.934  12.970  0.70 46.76 ? 140 GLN   A CG  1 
ATOM   964  C CD  . GLN   A 1 161 ? 18.945  14.988  14.324  0.70 52.40 ? 140 GLN   A CD  1 
ATOM   965  O OE1 . GLN   A 1 161 ? 18.486  14.355  15.284  0.70 44.65 ? 140 GLN   A OE1 1 
ATOM   966  N NE2 . GLN   A 1 161 ? 20.015  15.769  14.407  0.70 53.83 ? 140 GLN   A NE2 1 
ATOM   967  N N   . ARG   A 1 162 ? 19.704  13.667  8.591   1.00 38.40 ? 141 ARG   A N   1 
ATOM   968  C CA  . ARG   A 1 162 ? 20.635  13.617  7.475   1.00 45.83 ? 141 ARG   A CA  1 
ATOM   969  C C   . ARG   A 1 162 ? 20.040  14.165  6.180   1.00 48.82 ? 141 ARG   A C   1 
ATOM   970  O O   . ARG   A 1 162 ? 20.765  14.274  5.193   1.00 51.32 ? 141 ARG   A O   1 
ATOM   971  C CB  . ARG   A 1 162 ? 21.112  12.192  7.180   1.00 44.69 ? 141 ARG   A CB  1 
ATOM   972  C CG  . ARG   A 1 162 ? 22.457  11.834  7.784   0.80 51.09 ? 141 ARG   A CG  1 
ATOM   973  C CD  . ARG   A 1 162 ? 23.509  12.671  7.075   0.80 50.09 ? 141 ARG   A CD  1 
ATOM   974  N NE  . ARG   A 1 162 ? 24.733  11.892  6.880   0.80 56.56 ? 141 ARG   A NE  1 
ATOM   975  C CZ  . ARG   A 1 162 ? 25.410  11.864  5.746   0.80 56.25 ? 141 ARG   A CZ  1 
ATOM   976  N NH1 . ARG   A 1 162 ? 25.161  12.739  4.786   0.80 55.59 ? 141 ARG   A NH1 1 
ATOM   977  N NH2 . ARG   A 1 162 ? 26.367  10.974  5.597   0.80 59.40 ? 141 ARG   A NH2 1 
ATOM   978  N N   . GLN   A 1 163 ? 18.753  14.529  6.175   1.00 50.57 ? 142 GLN   A N   1 
ATOM   979  C CA  . GLN   A 1 163 ? 18.089  14.888  4.923   1.00 57.11 ? 142 GLN   A CA  1 
ATOM   980  C C   . GLN   A 1 163 ? 18.650  16.205  4.340   1.00 67.78 ? 142 GLN   A C   1 
ATOM   981  O O   . GLN   A 1 163 ? 19.139  17.037  5.132   1.00 76.21 ? 142 GLN   A O   1 
ATOM   982  C CB  . GLN   A 1 163 ? 16.558  14.838  4.974   1.00 49.14 ? 142 GLN   A CB  1 
ATOM   983  C CG  . GLN   A 1 163 ? 15.994  13.423  5.101   1.00 38.47 ? 142 GLN   A CG  1 
ATOM   984  C CD  . GLN   A 1 163 ? 16.548  12.417  4.115   1.00 43.11 ? 142 GLN   A CD  1 
ATOM   985  O OE1 . GLN   A 1 163 ? 16.785  12.724  2.944   1.00 39.37 ? 142 GLN   A OE1 1 
ATOM   986  N NE2 . GLN   A 1 163 ? 16.780  11.196  4.579   1.00 42.86 ? 142 GLN   A NE2 1 
ATOM   987  N N   . SER   A 1 173 ? 10.617  14.216  -4.839  1.00 58.49 ? 152 SER   A N   1 
ATOM   988  C CA  . SER   A 1 173 ? 11.135  13.020  -4.111  1.00 60.06 ? 152 SER   A CA  1 
ATOM   989  C C   . SER   A 1 173 ? 10.042  12.371  -3.249  1.00 53.73 ? 152 SER   A C   1 
ATOM   990  O O   . SER   A 1 173 ? 8.902   12.851  -3.190  1.00 49.82 ? 152 SER   A O   1 
ATOM   991  C CB  . SER   A 1 173 ? 12.358  13.364  -3.298  1.00 60.04 ? 152 SER   A CB  1 
ATOM   992  O OG  . SER   A 1 173 ? 11.990  14.177  -2.192  1.00 60.76 ? 152 SER   A OG  1 
ATOM   993  N N   . ASN   A 1 174 ? 10.399  11.256  -2.595  1.00 44.28 ? 153 ASN   A N   1 
ATOM   994  C CA  . ASN   A 1 174 ? 9.421   10.430  -1.897  1.00 38.72 ? 153 ASN   A CA  1 
ATOM   995  C C   . ASN   A 1 174 ? 10.114  9.717   -0.737  1.00 30.19 ? 153 ASN   A C   1 
ATOM   996  O O   . ASN   A 1 174 ? 10.440  8.526   -0.842  1.00 33.75 ? 153 ASN   A O   1 
ATOM   997  C CB  . ASN   A 1 174 ? 8.698   9.545   -2.917  1.00 39.74 ? 153 ASN   A CB  1 
ATOM   998  C CG  . ASN   A 1 174 ? 7.638   8.646   -2.318  1.00 41.87 ? 153 ASN   A CG  1 
ATOM   999  O OD1 . ASN   A 1 174 ? 7.049   8.965   -1.275  1.00 39.39 ? 153 ASN   A OD1 1 
ATOM   1000 N ND2 . ASN   A 1 174 ? 7.347   7.545   -3.001  1.00 47.40 ? 153 ASN   A ND2 1 
ATOM   1001 N N   . LEU   A 1 175 ? 10.317  10.452  0.359   1.00 28.08 ? 154 LEU   A N   1 
ATOM   1002 C CA  . LEU   A 1 175 ? 10.959  9.922   1.552   1.00 28.83 ? 154 LEU   A CA  1 
ATOM   1003 C C   . LEU   A 1 175 ? 9.939   9.169   2.413   1.00 30.21 ? 154 LEU   A C   1 
ATOM   1004 O O   . LEU   A 1 175 ? 8.901   9.734   2.765   1.00 28.27 ? 154 LEU   A O   1 
ATOM   1005 C CB  . LEU   A 1 175 ? 11.534  11.096  2.344   1.00 28.34 ? 154 LEU   A CB  1 
ATOM   1006 C CG  . LEU   A 1 175 ? 12.558  11.977  1.609   1.00 37.30 ? 154 LEU   A CG  1 
ATOM   1007 C CD1 . LEU   A 1 175 ? 12.945  13.199  2.416   1.00 36.23 ? 154 LEU   A CD1 1 
ATOM   1008 C CD2 . LEU   A 1 175 ? 13.803  11.184  1.231   1.00 36.58 ? 154 LEU   A CD2 1 
ATOM   1009 N N   . SER   A 1 176 ? 10.263  7.927   2.811   1.00 28.97 ? 155 SER   A N   1 
ATOM   1010 C CA  . SER   A 1 176 ? 9.431   7.300   3.834   1.00 28.59 ? 155 SER   A CA  1 
ATOM   1011 C C   . SER   A 1 176 ? 10.200  6.257   4.637   1.00 27.21 ? 155 SER   A C   1 
ATOM   1012 O O   . SER   A 1 176 ? 11.289  5.809   4.264   1.00 28.04 ? 155 SER   A O   1 
ATOM   1013 C CB  . SER   A 1 176 ? 8.149   6.726   3.265   1.00 30.41 ? 155 SER   A CB  1 
ATOM   1014 O OG  . SER   A 1 176 ? 8.445   5.541   2.543   1.00 32.45 ? 155 SER   A OG  1 
ATOM   1015 N N   . ILE   A 1 177 ? 9.589   5.900   5.780   1.00 25.41 ? 156 ILE   A N   1 
ATOM   1016 C CA  . ILE   A 1 177 ? 10.070  4.914   6.722   1.00 23.46 ? 156 ILE   A CA  1 
ATOM   1017 C C   . ILE   A 1 177 ? 8.951   3.889   6.845   1.00 22.63 ? 156 ILE   A C   1 
ATOM   1018 O O   . ILE   A 1 177 ? 7.788   4.261   7.000   1.00 22.45 ? 156 ILE   A O   1 
ATOM   1019 C CB  . ILE   A 1 177 ? 10.361  5.560   8.083   1.00 24.21 ? 156 ILE   A CB  1 
ATOM   1020 C CG1 . ILE   A 1 177 ? 11.406  6.768   7.934   1.00 25.46 ? 156 ILE   A CG1 1 
ATOM   1021 C CG2 . ILE   A 1 177 ? 10.787  4.503   9.116   1.00 23.91 ? 156 ILE   A CG2 1 
ATOM   1022 C CD1 . ILE   A 1 177 ? 11.771  7.455   9.241   1.00 25.48 ? 156 ILE   A CD1 1 
ATOM   1023 N N   . VAL   A 1 178 ? 9.351   2.617   6.851   1.00 24.34 ? 157 VAL   A N   1 
ATOM   1024 C CA  . VAL   A 1 178 ? 8.391   1.537   7.035   1.00 21.81 ? 157 VAL   A CA  1 
ATOM   1025 C C   . VAL   A 1 178 ? 8.899   0.663   8.183   1.00 22.34 ? 157 VAL   A C   1 
ATOM   1026 O O   . VAL   A 1 178 ? 10.015  0.154   8.134   1.00 22.73 ? 157 VAL   A O   1 
ATOM   1027 C CB  . VAL   A 1 178 ? 8.177   0.680   5.775   1.00 21.21 ? 157 VAL   A CB  1 
ATOM   1028 C CG1 . VAL   A 1 178 ? 7.172   -0.442  6.085   1.00 27.04 ? 157 VAL   A CG1 1 
ATOM   1029 C CG2 . VAL   A 1 178 ? 7.694   1.484   4.589   1.00 24.33 ? 157 VAL   A CG2 1 
ATOM   1030 N N   . ASN   A 1 179 ? 8.088   0.545   9.251   1.00 20.74 ? 158 ASN   A N   1 
ATOM   1031 C CA  . ASN   A 1 179 ? 8.434   -0.252  10.421  1.00 21.31 ? 158 ASN   A CA  1 
ATOM   1032 C C   . ASN   A 1 179 ? 7.756   -1.612  10.326  1.00 21.41 ? 158 ASN   A C   1 
ATOM   1033 O O   . ASN   A 1 179 ? 6.566   -1.672  10.089  1.00 21.63 ? 158 ASN   A O   1 
ATOM   1034 C CB  . ASN   A 1 179 ? 8.019   0.459   11.709  1.00 21.94 ? 158 ASN   A CB  1 
ATOM   1035 C CG  . ASN   A 1 179 ? 8.827   1.729   11.876  1.00 23.36 ? 158 ASN   A CG  1 
ATOM   1036 O OD1 . ASN   A 1 179 ? 10.000  1.754   11.469  1.00 25.14 ? 158 ASN   A OD1 1 
ATOM   1037 N ND2 . ASN   A 1 179 ? 8.229   2.780   12.397  1.00 24.27 ? 158 ASN   A ND2 1 
ATOM   1038 N N   . LEU   A 1 180 ? 8.491   -2.694  10.624  1.00 20.56 ? 159 LEU   A N   1 
ATOM   1039 C CA  . LEU   A 1 180 ? 7.856   -4.007  10.651  1.00 20.27 ? 159 LEU   A CA  1 
ATOM   1040 C C   . LEU   A 1 180 ? 7.313   -4.291  12.054  1.00 22.87 ? 159 LEU   A C   1 
ATOM   1041 O O   . LEU   A 1 180 ? 8.060   -4.420  13.052  1.00 22.53 ? 159 LEU   A O   1 
ATOM   1042 C CB  . LEU   A 1 180 ? 8.835   -5.104  10.196  1.00 18.20 ? 159 LEU   A CB  1 
ATOM   1043 C CG  . LEU   A 1 180 ? 9.014   -5.299  8.690   1.00 20.47 ? 159 LEU   A CG  1 
ATOM   1044 C CD1 . LEU   A 1 180 ? 7.831   -6.173  8.214   1.00 22.68 ? 159 LEU   A CD1 1 
ATOM   1045 C CD2 . LEU   A 1 180 ? 9.127   -4.034  7.820   1.00 21.05 ? 159 LEU   A CD2 1 
ATOM   1046 N N   . CYS   A 1 181 ? 5.965   -4.300  12.103  1.00 22.30 ? 160 CYS   A N   1 
ATOM   1047 C CA  . CYS   A 1 181 ? 5.210   -4.377  13.334  1.00 22.48 ? 160 CYS   A CA  1 
ATOM   1048 C C   . CYS   A 1 181 ? 4.746   -5.821  13.545  1.00 24.10 ? 160 CYS   A C   1 
ATOM   1049 O O   . CYS   A 1 181 ? 5.424   -6.751  13.143  1.00 28.06 ? 160 CYS   A O   1 
ATOM   1050 C CB  . CYS   A 1 181 ? 4.061   -3.383  13.275  1.00 22.52 ? 160 CYS   A CB  1 
ATOM   1051 S SG  . CYS   A 1 181 ? 4.674   -1.677  13.284  1.00 27.51 ? 160 CYS   A SG  1 
ATOM   1052 N N   . ASP   A 1 182 ? 3.652   -6.051  14.285  1.00 21.24 ? 161 ASP   A N   1 
ATOM   1053 C CA  . ASP   A 1 182 ? 3.241   -7.422  14.513  1.00 22.21 ? 161 ASP   A CA  1 
ATOM   1054 C C   . ASP   A 1 182 ? 1.718   -7.396  14.688  1.00 25.06 ? 161 ASP   A C   1 
ATOM   1055 O O   . ASP   A 1 182 ? 1.228   -6.711  15.587  1.00 24.48 ? 161 ASP   A O   1 
ATOM   1056 C CB  . ASP   A 1 182 ? 3.965   -7.995  15.729  1.00 25.87 ? 161 ASP   A CB  1 
ATOM   1057 C CG  . ASP   A 1 182 ? 3.642   -9.449  16.066  1.00 36.28 ? 161 ASP   A CG  1 
ATOM   1058 O OD1 . ASP   A 1 182 ? 2.537   -9.878  15.722  1.00 28.11 ? 161 ASP   A OD1 1 
ATOM   1059 O OD2 . ASP   A 1 182 ? 4.534   -10.193 16.597  1.00 32.30 ? 161 ASP   A OD2 1 
ATOM   1060 N N   . ALA   A 1 183 ? 0.970   -8.070  13.801  1.00 22.63 ? 162 ALA   A N   1 
ATOM   1061 C CA  . ALA   A 1 183 ? -0.491  -7.992  13.838  1.00 21.64 ? 162 ALA   A CA  1 
ATOM   1062 C C   . ALA   A 1 183 ? -1.071  -8.555  15.128  1.00 22.76 ? 162 ALA   A C   1 
ATOM   1063 O O   . ALA   A 1 183 ? -2.263  -8.313  15.413  1.00 22.67 ? 162 ALA   A O   1 
ATOM   1064 C CB  . ALA   A 1 183 ? -1.091  -8.739  12.656  1.00 23.80 ? 162 ALA   A CB  1 
ATOM   1065 N N   . MET   A 1 184 ? -0.265  -9.330  15.866  1.00 21.31 ? 163 MET   A N   1 
ATOM   1066 C CA  . MET   A 1 184 ? -0.806  -10.061 17.001  1.00 22.71 ? 163 MET   A CA  1 
ATOM   1067 C C   . MET   A 1 184 ? -0.433  -9.412  18.340  1.00 24.62 ? 163 MET   A C   1 
ATOM   1068 O O   . MET   A 1 184 ? -0.599  -10.055 19.373  1.00 26.93 ? 163 MET   A O   1 
ATOM   1069 C CB  . MET   A 1 184 ? -0.386  -11.546 16.943  1.00 27.20 ? 163 MET   A CB  1 
ATOM   1070 C CG  . MET   A 1 184 ? -0.889  -12.266 15.649  1.00 27.88 ? 163 MET   A CG  1 
ATOM   1071 S SD  . MET   A 1 184 ? -2.686  -12.402 15.757  1.00 30.03 ? 163 MET   A SD  1 
ATOM   1072 C CE  . MET   A 1 184 ? -2.919  -13.825 16.840  1.00 33.83 ? 163 MET   A CE  1 
ATOM   1073 N N   . VAL   A 1 185 ? -0.017  -8.134  18.328  1.00 25.12 ? 164 VAL   A N   1 
ATOM   1074 C CA  . VAL   A 1 185 ? 0.432   -7.484  19.561  1.00 29.78 ? 164 VAL   A CA  1 
ATOM   1075 C C   . VAL   A 1 185 ? -0.667  -7.367  20.615  1.00 27.16 ? 164 VAL   A C   1 
ATOM   1076 O O   . VAL   A 1 185 ? -0.352  -7.277  21.807  1.00 29.19 ? 164 VAL   A O   1 
ATOM   1077 C CB  . VAL   A 1 185 ? 1.113   -6.115  19.362  1.00 32.91 ? 164 VAL   A CB  1 
ATOM   1078 C CG1 . VAL   A 1 185 ? 2.447   -6.270  18.634  1.00 38.71 ? 164 VAL   A CG1 1 
ATOM   1079 C CG2 . VAL   A 1 185 ? 0.208   -5.117  18.680  1.00 28.98 ? 164 VAL   A CG2 1 
ATOM   1080 N N   . ASP   A 1 186 ? -1.942  -7.371  20.218  1.00 27.89 ? 165 ASP   A N   1 
ATOM   1081 C CA  . ASP   A 1 186 ? -2.994  -7.328  21.236  1.00 26.97 ? 165 ASP   A CA  1 
ATOM   1082 C C   . ASP   A 1 186 ? -3.512  -8.705  21.668  1.00 25.39 ? 165 ASP   A C   1 
ATOM   1083 O O   . ASP   A 1 186 ? -4.377  -8.793  22.552  1.00 25.55 ? 165 ASP   A O   1 
ATOM   1084 C CB  . ASP   A 1 186 ? -4.123  -6.387  20.848  1.00 25.80 ? 165 ASP   A CB  1 
ATOM   1085 C CG  . ASP   A 1 186 ? -3.675  -4.958  20.641  1.00 27.33 ? 165 ASP   A CG  1 
ATOM   1086 O OD1 . ASP   A 1 186 ? -2.888  -4.457  21.447  1.00 28.49 ? 165 ASP   A OD1 1 
ATOM   1087 O OD2 . ASP   A 1 186 ? -4.118  -4.358  19.670  1.00 31.88 ? 165 ASP   A OD2 1 
ATOM   1088 N N   . GLN   A 1 187 ? -2.984  -9.773  21.070  1.00 23.26 ? 166 GLN   A N   1 
ATOM   1089 C CA  . GLN   A 1 187 ? -3.323  -11.136 21.446  1.00 22.84 ? 166 GLN   A CA  1 
ATOM   1090 C C   . GLN   A 1 187 ? -2.005  -11.907 21.495  1.00 26.64 ? 166 GLN   A C   1 
ATOM   1091 O O   . GLN   A 1 187 ? -1.764  -12.811 20.703  1.00 25.64 ? 166 GLN   A O   1 
ATOM   1092 C CB  . GLN   A 1 187 ? -4.245  -11.778 20.399  1.00 28.04 ? 166 GLN   A CB  1 
ATOM   1093 C CG  . GLN   A 1 187 ? -5.593  -11.069 20.265  1.00 29.09 ? 166 GLN   A CG  1 
ATOM   1094 C CD  . GLN   A 1 187 ? -5.928  -10.751 18.820  1.00 33.73 ? 166 GLN   A CD  1 
ATOM   1095 O OE1 . GLN   A 1 187 ? -5.490  -9.740  18.268  1.00 39.95 ? 166 GLN   A OE1 1 
ATOM   1096 N NE2 . GLN   A 1 187 ? -6.727  -11.588 18.186  1.00 36.76 ? 166 GLN   A NE2 1 
ATOM   1097 N N   . PRO   A 1 188 ? -1.109  -11.544 22.435  1.00 24.66 ? 167 PRO   A N   1 
ATOM   1098 C CA  . PRO   A 1 188 ? 0.298   -11.944 22.328  1.00 26.70 ? 167 PRO   A CA  1 
ATOM   1099 C C   . PRO   A 1 188 ? 0.526   -13.403 22.737  1.00 25.72 ? 167 PRO   A C   1 
ATOM   1100 O O   . PRO   A 1 188 ? -0.336  -14.003 23.380  1.00 28.55 ? 167 PRO   A O   1 
ATOM   1101 C CB  . PRO   A 1 188 ? 0.909   -10.915 23.285  1.00 25.93 ? 167 PRO   A CB  1 
ATOM   1102 C CG  . PRO   A 1 188 ? -0.098  -10.803 24.397  1.00 26.55 ? 167 PRO   A CG  1 
ATOM   1103 C CD  . PRO   A 1 188 ? -1.422  -10.694 23.608  1.00 24.93 ? 167 PRO   A CD  1 
ATOM   1104 N N   . CYS   A 1 189 ? 1.686   -13.942 22.368  1.00 28.14 ? 168 CYS   A N   1 
ATOM   1105 C CA  . CYS   A 1 189 ? 2.090   -15.252 22.862  1.00 32.05 ? 168 CYS   A CA  1 
ATOM   1106 C C   . CYS   A 1 189 ? 2.425   -15.140 24.344  1.00 29.54 ? 168 CYS   A C   1 
ATOM   1107 O O   . CYS   A 1 189 ? 2.995   -14.149 24.810  1.00 29.12 ? 168 CYS   A O   1 
ATOM   1108 C CB  . CYS   A 1 189 ? 3.275   -15.821 22.100  1.00 40.19 ? 168 CYS   A CB  1 
ATOM   1109 S SG  . CYS   A 1 189 ? 2.829   -16.437 20.452  1.00 48.30 ? 168 CYS   A SG  1 
ATOM   1110 N N   . MET   A 1 190 ? 2.059   -16.191 25.058  1.00 33.17 ? 169 MET   A N   1 
ATOM   1111 C CA  . MET   A 1 190 ? 2.354   -16.339 26.472  1.00 37.36 ? 169 MET   A CA  1 
ATOM   1112 C C   . MET   A 1 190 ? 3.868   -16.227 26.668  1.00 29.68 ? 169 MET   A C   1 
ATOM   1113 O O   . MET   A 1 190 ? 4.608   -16.836 25.922  1.00 30.78 ? 169 MET   A O   1 
ATOM   1114 C CB  . MET   A 1 190 ? 1.906   -17.755 26.879  1.00 46.09 ? 169 MET   A CB  1 
ATOM   1115 C CG  . MET   A 1 190 ? 2.137   -18.137 28.327  1.00 54.77 ? 169 MET   A CG  1 
ATOM   1116 S SD  . MET   A 1 190 ? 1.003   -17.085 29.243  1.00 56.23 ? 169 MET   A SD  1 
ATOM   1117 C CE  . MET   A 1 190 ? -0.607  -17.882 29.144  1.00 45.69 ? 169 MET   A CE  1 
ATOM   1118 N N   . ALA   A 1 191 ? 4.299   -15.445 27.669  1.00 30.28 ? 170 ALA   A N   1 
ATOM   1119 C CA  . ALA   A 1 191 ? 5.669   -15.352 28.147  1.00 29.55 ? 170 ALA   A CA  1 
ATOM   1120 C C   . ALA   A 1 191 ? 6.556   -14.503 27.237  1.00 29.01 ? 170 ALA   A C   1 
ATOM   1121 O O   . ALA   A 1 191 ? 7.786   -14.595 27.315  1.00 29.19 ? 170 ALA   A O   1 
ATOM   1122 C CB  . ALA   A 1 191 ? 6.254   -16.758 28.369  1.00 30.80 ? 170 ALA   A CB  1 
ATOM   1123 N N   . PHE   A 1 192 ? 5.954   -13.653 26.385  1.00 28.23 ? 171 PHE   A N   1 
ATOM   1124 C CA  . PHE   A 1 192 ? 6.753   -12.812 25.503  1.00 25.47 ? 171 PHE   A CA  1 
ATOM   1125 C C   . PHE   A 1 192 ? 6.597   -11.317 25.819  1.00 26.78 ? 171 PHE   A C   1 
ATOM   1126 O O   . PHE   A 1 192 ? 6.570   -10.520 24.886  1.00 25.68 ? 171 PHE   A O   1 
ATOM   1127 C CB  . PHE   A 1 192 ? 6.458   -12.986 24.002  1.00 25.19 ? 171 PHE   A CB  1 
ATOM   1128 C CG  . PHE   A 1 192 ? 7.060   -14.261 23.418  1.00 28.17 ? 171 PHE   A CG  1 
ATOM   1129 C CD1 . PHE   A 1 192 ? 6.508   -15.505 23.719  1.00 29.72 ? 171 PHE   A CD1 1 
ATOM   1130 C CD2 . PHE   A 1 192 ? 8.204   -14.198 22.612  1.00 31.00 ? 171 PHE   A CD2 1 
ATOM   1131 C CE1 . PHE   A 1 192 ? 7.069   -16.674 23.210  1.00 29.56 ? 171 PHE   A CE1 1 
ATOM   1132 C CE2 . PHE   A 1 192 ? 8.771   -15.375 22.108  1.00 33.66 ? 171 PHE   A CE2 1 
ATOM   1133 C CZ  . PHE   A 1 192 ? 8.191   -16.601 22.395  1.00 32.89 ? 171 PHE   A CZ  1 
ATOM   1134 N N   . SER   A 1 193 ? 6.539   -10.948 27.111  1.00 26.12 ? 172 SER   A N   1 
ATOM   1135 C CA  . SER   A 1 193 ? 6.311   -9.567  27.570  1.00 28.61 ? 172 SER   A CA  1 
ATOM   1136 C C   . SER   A 1 193 ? 7.238   -8.555  26.904  1.00 29.79 ? 172 SER   A C   1 
ATOM   1137 O O   . SER   A 1 193 ? 6.784   -7.510  26.432  1.00 25.72 ? 172 SER   A O   1 
ATOM   1138 C CB  . SER   A 1 193 ? 6.523   -9.465  29.051  1.00 32.83 ? 172 SER   A CB  1 
ATOM   1139 O OG  . SER   A 1 193 ? 5.365   -9.928  29.724  1.00 38.47 ? 172 SER   A OG  1 
ATOM   1140 N N   . LEU   A 1 194 ? 8.555   -8.820  26.931  1.00 28.57 ? 173 LEU   A N   1 
ATOM   1141 C CA  . LEU   A 1 194 ? 9.530   -7.842  26.464  1.00 27.48 ? 173 LEU   A CA  1 
ATOM   1142 C C   . LEU   A 1 194 ? 9.445   -7.667  24.951  1.00 25.02 ? 173 LEU   A C   1 
ATOM   1143 O O   . LEU   A 1 194 ? 9.445   -6.543  24.443  1.00 24.31 ? 173 LEU   A O   1 
ATOM   1144 C CB  . LEU   A 1 194 ? 10.980  -8.090  26.935  1.00 24.31 ? 173 LEU   A CB  1 
ATOM   1145 C CG  . LEU   A 1 194 ? 11.294  -7.723  28.388  1.00 26.63 ? 173 LEU   A CG  1 
ATOM   1146 C CD1 . LEU   A 1 194 ? 12.677  -8.286  28.820  1.00 25.22 ? 173 LEU   A CD1 1 
ATOM   1147 C CD2 . LEU   A 1 194 ? 11.268  -6.206  28.631  1.00 27.45 ? 173 LEU   A CD2 1 
ATOM   1148 N N   . TYR   A 1 195 ? 9.339   -8.766  24.202  1.00 24.69 ? 174 TYR   A N   1 
ATOM   1149 C CA  . TYR   A 1 195 ? 9.115   -8.633  22.777  1.00 23.28 ? 174 TYR   A CA  1 
ATOM   1150 C C   . TYR   A 1 195 ? 7.820   -7.834  22.511  1.00 21.88 ? 174 TYR   A C   1 
ATOM   1151 O O   . TYR   A 1 195 ? 7.825   -6.950  21.647  1.00 24.10 ? 174 TYR   A O   1 
ATOM   1152 C CB  . TYR   A 1 195 ? 8.954   -10.017 22.137  1.00 25.04 ? 174 TYR   A CB  1 
ATOM   1153 C CG  . TYR   A 1 195 ? 8.498   -9.925  20.691  1.00 24.10 ? 174 TYR   A CG  1 
ATOM   1154 C CD1 . TYR   A 1 195 ? 9.384   -9.617  19.660  1.00 22.01 ? 174 TYR   A CD1 1 
ATOM   1155 C CD2 . TYR   A 1 195 ? 7.167   -10.159 20.367  1.00 22.32 ? 174 TYR   A CD2 1 
ATOM   1156 C CE1 . TYR   A 1 195 ? 8.949   -9.533  18.350  1.00 25.63 ? 174 TYR   A CE1 1 
ATOM   1157 C CE2 . TYR   A 1 195 ? 6.710   -10.084 19.058  1.00 24.48 ? 174 TYR   A CE2 1 
ATOM   1158 C CZ  . TYR   A 1 195 ? 7.607   -9.774  18.053  1.00 25.54 ? 174 TYR   A CZ  1 
ATOM   1159 O OH  . TYR   A 1 195 ? 7.164   -9.719  16.774  1.00 27.64 ? 174 TYR   A OH  1 
ATOM   1160 N N   . ASN   A 1 196 ? 6.723   -8.147  23.218  1.00 20.96 ? 175 ASN   A N   1 
ATOM   1161 C CA  A ASN   A 1 196 ? 5.444   -7.472  22.994  0.50 22.27 ? 175 ASN   A CA  1 
ATOM   1162 C CA  B ASN   A 1 196 ? 5.481   -7.451  22.912  0.50 22.55 ? 175 ASN   A CA  1 
ATOM   1163 C C   . ASN   A 1 196 ? 5.593   -5.978  23.303  1.00 23.77 ? 175 ASN   A C   1 
ATOM   1164 O O   . ASN   A 1 196 ? 5.035   -5.091  22.617  1.00 22.78 ? 175 ASN   A O   1 
ATOM   1165 C CB  A ASN   A 1 196 ? 4.322   -8.099  23.816  0.50 23.85 ? 175 ASN   A CB  1 
ATOM   1166 C CB  B ASN   A 1 196 ? 4.257   -8.216  23.388  0.50 24.31 ? 175 ASN   A CB  1 
ATOM   1167 C CG  A ASN   A 1 196 ? 2.954   -7.629  23.363  0.50 24.53 ? 175 ASN   A CG  1 
ATOM   1168 C CG  B ASN   A 1 196 ? 3.976   -9.376  22.467  0.50 23.85 ? 175 ASN   A CG  1 
ATOM   1169 O OD1 A ASN   A 1 196 ? 2.191   -7.039  24.142  0.50 32.13 ? 175 ASN   A OD1 1 
ATOM   1170 O OD1 B ASN   A 1 196 ? 3.617   -9.180  21.299  0.50 29.39 ? 175 ASN   A OD1 1 
ATOM   1171 N ND2 A ASN   A 1 196 ? 2.640   -7.852  22.099  0.50 22.01 ? 175 ASN   A ND2 1 
ATOM   1172 N ND2 B ASN   A 1 196 ? 4.160   -10.589 22.960  0.50 24.33 ? 175 ASN   A ND2 1 
ATOM   1173 N N   . MET   A 1 197 ? 6.332   -5.704  24.375  1.00 24.49 ? 176 MET   A N   1 
ATOM   1174 C CA  . MET   A 1 197 ? 6.537   -4.323  24.780  1.00 25.95 ? 176 MET   A CA  1 
ATOM   1175 C C   . MET   A 1 197 ? 7.233   -3.555  23.667  1.00 23.26 ? 176 MET   A C   1 
ATOM   1176 O O   . MET   A 1 197 ? 6.924   -2.385  23.416  1.00 22.95 ? 176 MET   A O   1 
ATOM   1177 C CB  . MET   A 1 197 ? 7.318   -4.251  26.104  1.00 20.47 ? 176 MET   A CB  1 
ATOM   1178 C CG  . MET   A 1 197 ? 6.476   -4.644  27.308  1.00 25.98 ? 176 MET   A CG  1 
ATOM   1179 S SD  . MET   A 1 197 ? 7.457   -4.885  28.810  1.00 26.56 ? 176 MET   A SD  1 
ATOM   1180 C CE  . MET   A 1 197 ? 7.810   -3.155  29.179  1.00 26.16 ? 176 MET   A CE  1 
ATOM   1181 N N   . GLY   A 1 198 ? 8.260   -4.178  23.071  1.00 22.78 ? 177 GLY   A N   1 
ATOM   1182 C CA  . GLY   A 1 198 ? 9.012   -3.520  22.025  1.00 20.96 ? 177 GLY   A CA  1 
ATOM   1183 C C   . GLY   A 1 198 ? 8.151   -3.255  20.783  1.00 21.26 ? 177 GLY   A C   1 
ATOM   1184 O O   . GLY   A 1 198 ? 8.258   -2.205  20.130  1.00 20.66 ? 177 GLY   A O   1 
ATOM   1185 N N   . LYS   A 1 199 ? 7.360   -4.252  20.365  1.00 19.28 ? 178 LYS   A N   1 
ATOM   1186 C CA  . LYS   A 1 199 ? 6.518   -4.029  19.189  1.00 21.25 ? 178 LYS   A CA  1 
ATOM   1187 C C   . LYS   A 1 199 ? 5.428   -2.981  19.472  1.00 19.16 ? 178 LYS   A C   1 
ATOM   1188 O O   . LYS   A 1 199 ? 5.098   -2.223  18.577  1.00 22.08 ? 178 LYS   A O   1 
ATOM   1189 C CB  . LYS   A 1 199 ? 5.879   -5.335  18.693  1.00 19.04 ? 178 LYS   A CB  1 
ATOM   1190 C CG  . LYS   A 1 199 ? 6.934   -6.259  18.045  1.00 20.93 ? 178 LYS   A CG  1 
ATOM   1191 C CD  . LYS   A 1 199 ? 7.679   -5.667  16.851  1.00 22.35 ? 178 LYS   A CD  1 
ATOM   1192 C CE  . LYS   A 1 199 ? 8.310   -6.725  15.983  1.00 23.27 ? 178 LYS   A CE  1 
ATOM   1193 N NZ  . LYS   A 1 199 ? 9.292   -6.111  15.073  1.00 24.35 ? 178 LYS   A NZ  1 
ATOM   1194 N N   . HIS   A 1 200 ? 4.912   -2.893  20.702  1.00 22.80 ? 179 HIS   A N   1 
ATOM   1195 C CA  . HIS   A 1 200 ? 3.957   -1.815  21.022  1.00 21.15 ? 179 HIS   A CA  1 
ATOM   1196 C C   . HIS   A 1 200 ? 4.661   -0.466  20.976  1.00 23.17 ? 179 HIS   A C   1 
ATOM   1197 O O   . HIS   A 1 200 ? 4.098   0.520   20.465  1.00 21.50 ? 179 HIS   A O   1 
ATOM   1198 C CB  . HIS   A 1 200 ? 3.362   -2.018  22.413  1.00 21.37 ? 179 HIS   A CB  1 
ATOM   1199 C CG  . HIS   A 1 200 ? 2.105   -2.805  22.417  1.00 24.74 ? 179 HIS   A CG  1 
ATOM   1200 N ND1 . HIS   A 1 200 ? 0.882   -2.201  22.253  1.00 26.23 ? 179 HIS   A ND1 1 
ATOM   1201 C CD2 . HIS   A 1 200 ? 1.864   -4.134  22.536  1.00 27.30 ? 179 HIS   A CD2 1 
ATOM   1202 C CE1 . HIS   A 1 200 ? -0.071  -3.116  22.322  1.00 26.93 ? 179 HIS   A CE1 1 
ATOM   1203 N NE2 . HIS   A 1 200 ? 0.504   -4.304  22.473  1.00 27.98 ? 179 HIS   A NE2 1 
ATOM   1204 N N   . ALA   A 1 201 ? 5.903   -0.419  21.494  1.00 22.54 ? 180 ALA   A N   1 
ATOM   1205 C CA  . ALA   A 1 201 ? 6.629   0.857   21.395  1.00 23.92 ? 180 ALA   A CA  1 
ATOM   1206 C C   . ALA   A 1 201 ? 6.850   1.253   19.942  1.00 22.07 ? 180 ALA   A C   1 
ATOM   1207 O O   . ALA   A 1 201 ? 6.831   2.425   19.575  1.00 21.90 ? 180 ALA   A O   1 
ATOM   1208 C CB  . ALA   A 1 201 ? 7.956   0.780   22.165  1.00 24.27 ? 180 ALA   A CB  1 
ATOM   1209 N N   . LEU   A 1 202 ? 7.080   0.263   19.065  1.00 20.04 ? 181 LEU   A N   1 
ATOM   1210 C CA  . LEU   A 1 202 ? 7.265   0.544   17.655  1.00 19.78 ? 181 LEU   A CA  1 
ATOM   1211 C C   . LEU   A 1 202 ? 5.979   1.120   17.017  1.00 21.41 ? 181 LEU   A C   1 
ATOM   1212 O O   . LEU   A 1 202 ? 6.056   2.009   16.173  1.00 21.77 ? 181 LEU   A O   1 
ATOM   1213 C CB  . LEU   A 1 202 ? 7.720   -0.737  16.930  1.00 18.97 ? 181 LEU   A CB  1 
ATOM   1214 C CG  . LEU   A 1 202 ? 8.114   -0.561  15.452  1.00 22.68 ? 181 LEU   A CG  1 
ATOM   1215 C CD1 . LEU   A 1 202 ? 9.267   0.434   15.204  1.00 24.28 ? 181 LEU   A CD1 1 
ATOM   1216 C CD2 . LEU   A 1 202 ? 8.455   -1.966  14.942  1.00 21.22 ? 181 LEU   A CD2 1 
ATOM   1217 N N   . VAL   A 1 203 ? 4.789   0.659   17.443  1.00 22.38 ? 182 VAL   A N   1 
ATOM   1218 C CA  . VAL   A 1 203 ? 3.564   1.341   16.977  1.00 22.04 ? 182 VAL   A CA  1 
ATOM   1219 C C   . VAL   A 1 203 ? 3.591   2.804   17.416  1.00 20.08 ? 182 VAL   A C   1 
ATOM   1220 O O   . VAL   A 1 203 ? 3.238   3.700   16.651  1.00 23.31 ? 182 VAL   A O   1 
ATOM   1221 C CB  . VAL   A 1 203 ? 2.322   0.641   17.534  1.00 22.77 ? 182 VAL   A CB  1 
ATOM   1222 C CG1 . VAL   A 1 203 ? 1.016   1.386   17.201  1.00 21.27 ? 182 VAL   A CG1 1 
ATOM   1223 C CG2 . VAL   A 1 203 ? 2.302   -0.775  16.994  1.00 24.65 ? 182 VAL   A CG2 1 
ATOM   1224 N N   . GLY   A 1 204 ? 3.956   3.010   18.677  1.00 20.67 ? 183 GLY   A N   1 
ATOM   1225 C CA  . GLY   A 1 204 ? 3.990   4.378   19.193  1.00 22.49 ? 183 GLY   A CA  1 
ATOM   1226 C C   . GLY   A 1 204 ? 4.929   5.226   18.353  1.00 22.86 ? 183 GLY   A C   1 
ATOM   1227 O O   . GLY   A 1 204 ? 4.634   6.382   18.037  1.00 24.16 ? 183 GLY   A O   1 
ATOM   1228 N N   . LEU   A 1 205 ? 6.129   4.670   18.056  1.00 22.50 ? 184 LEU   A N   1 
ATOM   1229 C CA  . LEU   A 1 205 ? 7.090   5.370   17.208  1.00 23.04 ? 184 LEU   A CA  1 
ATOM   1230 C C   . LEU   A 1 205 ? 6.478   5.690   15.858  1.00 22.00 ? 184 LEU   A C   1 
ATOM   1231 O O   . LEU   A 1 205 ? 6.631   6.796   15.347  1.00 22.92 ? 184 LEU   A O   1 
ATOM   1232 C CB  . LEU   A 1 205 ? 8.382   4.549   16.995  1.00 23.93 ? 184 LEU   A CB  1 
ATOM   1233 C CG  . LEU   A 1 205 ? 9.377   5.163   15.990  1.00 23.08 ? 184 LEU   A CG  1 
ATOM   1234 C CD1 . LEU   A 1 205 ? 9.801   6.499   16.587  1.00 23.40 ? 184 LEU   A CD1 1 
ATOM   1235 C CD2 . LEU   A 1 205 ? 10.587  4.218   15.941  1.00 21.50 ? 184 LEU   A CD2 1 
ATOM   1236 N N   . THR   A 1 206 ? 5.832   4.699   15.221  1.00 20.57 ? 185 THR   A N   1 
ATOM   1237 C CA  . THR   A 1 206 ? 5.274   4.936   13.905  1.00 22.43 ? 185 THR   A CA  1 
ATOM   1238 C C   . THR   A 1 206 ? 4.331   6.136   13.957  1.00 21.56 ? 185 THR   A C   1 
ATOM   1239 O O   . THR   A 1 206 ? 4.420   6.945   13.058  1.00 23.26 ? 185 THR   A O   1 
ATOM   1240 C CB  . THR   A 1 206 ? 4.545   3.705   13.359  1.00 22.72 ? 185 THR   A CB  1 
ATOM   1241 O OG1 . THR   A 1 206 ? 5.449   2.599   13.471  1.00 22.30 ? 185 THR   A OG1 1 
ATOM   1242 C CG2 . THR   A 1 206 ? 4.108   3.919   11.919  1.00 22.79 ? 185 THR   A CG2 1 
ATOM   1243 N N   . GLN   A 1 207 ? 3.488   6.245   15.014  1.00 22.73 ? 186 GLN   A N   1 
ATOM   1244 C CA  . GLN   A 1 207 ? 2.490   7.306   15.092  1.00 21.13 ? 186 GLN   A CA  1 
ATOM   1245 C C   . GLN   A 1 207 ? 3.151   8.650   15.372  1.00 22.42 ? 186 GLN   A C   1 
ATOM   1246 O O   . GLN   A 1 207 ? 2.892   9.638   14.665  1.00 22.41 ? 186 GLN   A O   1 
ATOM   1247 C CB  . GLN   A 1 207 ? 1.360   6.986   16.074  1.00 23.82 ? 186 GLN   A CB  1 
ATOM   1248 C CG  . GLN   A 1 207 ? 0.663   5.690   15.684  1.00 24.09 ? 186 GLN   A CG  1 
ATOM   1249 C CD  . GLN   A 1 207 ? -0.476  5.256   16.589  1.00 30.82 ? 186 GLN   A CD  1 
ATOM   1250 O OE1 . GLN   A 1 207 ? -1.362  4.513   16.154  1.00 37.13 ? 186 GLN   A OE1 1 
ATOM   1251 N NE2 . GLN   A 1 207 ? -0.471  5.677   17.842  1.00 32.91 ? 186 GLN   A NE2 1 
ATOM   1252 N N   . SER   A 1 208 ? 4.019   8.645   16.378  1.00 22.17 ? 187 SER   A N   1 
ATOM   1253 C CA  . SER   A 1 208 ? 4.707   9.855   16.828  1.00 23.27 ? 187 SER   A CA  1 
ATOM   1254 C C   . SER   A 1 208 ? 5.601   10.390  15.720  1.00 23.20 ? 187 SER   A C   1 
ATOM   1255 O O   . SER   A 1 208 ? 5.622   11.607  15.459  1.00 23.94 ? 187 SER   A O   1 
ATOM   1256 C CB  . SER   A 1 208 ? 5.527   9.616   18.048  1.00 23.22 ? 187 SER   A CB  1 
ATOM   1257 O OG  . SER   A 1 208 ? 4.730   9.542   19.199  1.00 24.50 ? 187 SER   A OG  1 
ATOM   1258 N N   . ALA   A 1 209 ? 6.317   9.482   15.049  1.00 22.20 ? 188 ALA   A N   1 
ATOM   1259 C CA  . ALA   A 1 209 ? 7.199   9.949   13.981  1.00 25.17 ? 188 ALA   A CA  1 
ATOM   1260 C C   . ALA   A 1 209 ? 6.393   10.426  12.779  1.00 25.53 ? 188 ALA   A C   1 
ATOM   1261 O O   . ALA   A 1 209 ? 6.787   11.392  12.129  1.00 25.92 ? 188 ALA   A O   1 
ATOM   1262 C CB  . ALA   A 1 209 ? 8.224   8.909   13.613  1.00 25.65 ? 188 ALA   A CB  1 
ATOM   1263 N N   . ALA   A 1 210 ? 5.253   9.757   12.464  1.00 24.12 ? 189 ALA   A N   1 
ATOM   1264 C CA  . ALA   A 1 210 ? 4.473   10.220  11.311  1.00 23.36 ? 189 ALA   A CA  1 
ATOM   1265 C C   . ALA   A 1 210 ? 4.040   11.669  11.535  1.00 23.39 ? 189 ALA   A C   1 
ATOM   1266 O O   . ALA   A 1 210 ? 4.139   12.489  10.624  1.00 26.67 ? 189 ALA   A O   1 
ATOM   1267 C CB  . ALA   A 1 210 ? 3.278   9.308   11.108  1.00 23.55 ? 189 ALA   A CB  1 
ATOM   1268 N N   . LEU   A 1 211 ? 3.566   11.959  12.747  1.00 24.53 ? 190 LEU   A N   1 
ATOM   1269 C CA  . LEU   A 1 211 ? 3.096   13.290  13.129  1.00 25.11 ? 190 LEU   A CA  1 
ATOM   1270 C C   . LEU   A 1 211 ? 4.214   14.326  13.001  1.00 26.81 ? 190 LEU   A C   1 
ATOM   1271 O O   . LEU   A 1 211 ? 4.031   15.401  12.421  1.00 28.50 ? 190 LEU   A O   1 
ATOM   1272 C CB  . LEU   A 1 211 ? 2.576   13.221  14.568  1.00 25.72 ? 190 LEU   A CB  1 
ATOM   1273 C CG  . LEU   A 1 211 ? 2.071   14.553  15.136  1.00 28.76 ? 190 LEU   A CG  1 
ATOM   1274 C CD1 . LEU   A 1 211 ? 0.736   14.857  14.410  1.00 30.26 ? 190 LEU   A CD1 1 
ATOM   1275 C CD2 . LEU   A 1 211 ? 1.874   14.529  16.649  1.00 28.94 ? 190 LEU   A CD2 1 
ATOM   1276 N N   . GLU   A 1 212 ? 5.363   14.008  13.588  1.00 28.24 ? 191 GLU   A N   1 
ATOM   1277 C CA  . GLU   A 1 212 ? 6.424   15.004  13.744  1.00 28.76 ? 191 GLU   A CA  1 
ATOM   1278 C C   . GLU   A 1 212 ? 7.166   15.189  12.423  1.00 30.79 ? 191 GLU   A C   1 
ATOM   1279 O O   . GLU   A 1 212 ? 7.577   16.293  12.107  1.00 33.35 ? 191 GLU   A O   1 
ATOM   1280 C CB  . GLU   A 1 212 ? 7.348   14.502  14.855  1.00 27.85 ? 191 GLU   A CB  1 
ATOM   1281 C CG  . GLU   A 1 212 ? 8.565   15.405  15.058  1.00 30.51 ? 191 GLU   A CG  1 
ATOM   1282 C CD  . GLU   A 1 212 ? 9.350   15.084  16.315  1.00 35.19 ? 191 GLU   A CD  1 
ATOM   1283 O OE1 . GLU   A 1 212 ? 10.408  15.747  16.494  1.00 35.36 ? 191 GLU   A OE1 1 
ATOM   1284 O OE2 . GLU   A 1 212 ? 8.945   14.185  17.099  1.00 35.44 ? 191 GLU   A OE2 1 
ATOM   1285 N N   . LEU   A 1 213 ? 7.296   14.133  11.615  1.00 27.44 ? 192 LEU   A N   1 
ATOM   1286 C CA  . LEU   A 1 213 ? 8.028   14.239  10.352  1.00 27.42 ? 192 LEU   A CA  1 
ATOM   1287 C C   . LEU   A 1 213 ? 7.177   14.654  9.149   1.00 26.99 ? 192 LEU   A C   1 
ATOM   1288 O O   . LEU   A 1 213 ? 7.721   14.870  8.068   1.00 26.84 ? 192 LEU   A O   1 
ATOM   1289 C CB  . LEU   A 1 213 ? 8.862   12.995  10.029  1.00 25.16 ? 192 LEU   A CB  1 
ATOM   1290 C CG  . LEU   A 1 213 ? 9.849   12.592  11.139  1.00 27.71 ? 192 LEU   A CG  1 
ATOM   1291 C CD1 . LEU   A 1 213 ? 10.635  11.340  10.780  1.00 26.33 ? 192 LEU   A CD1 1 
ATOM   1292 C CD2 . LEU   A 1 213 ? 10.818  13.715  11.533  1.00 26.70 ? 192 LEU   A CD2 1 
ATOM   1293 N N   . ALA   A 1 214 ? 5.844   14.672  9.286   1.00 27.26 ? 193 ALA   A N   1 
ATOM   1294 C CA  . ALA   A 1 214 ? 4.971   15.017  8.165   1.00 30.29 ? 193 ALA   A CA  1 
ATOM   1295 C C   . ALA   A 1 214 ? 5.346   16.385  7.578   1.00 34.69 ? 193 ALA   A C   1 
ATOM   1296 O O   . ALA   A 1 214 ? 5.448   16.518  6.359   1.00 30.20 ? 193 ALA   A O   1 
ATOM   1297 C CB  . ALA   A 1 214 ? 3.511   14.979  8.596   1.00 29.47 ? 193 ALA   A CB  1 
ATOM   1298 N N   . PRO   A 1 215 ? 5.576   17.434  8.402   1.00 37.48 ? 194 PRO   A N   1 
ATOM   1299 C CA  . PRO   A 1 215 ? 6.032   18.726  7.879   1.00 38.66 ? 194 PRO   A CA  1 
ATOM   1300 C C   . PRO   A 1 215 ? 7.298   18.656  7.012   1.00 41.61 ? 194 PRO   A C   1 
ATOM   1301 O O   . PRO   A 1 215 ? 7.481   19.488  6.125   1.00 39.29 ? 194 PRO   A O   1 
ATOM   1302 C CB  . PRO   A 1 215 ? 6.137   19.666  9.099   1.00 40.47 ? 194 PRO   A CB  1 
ATOM   1303 C CG  . PRO   A 1 215 ? 5.320   18.972  10.176  1.00 45.20 ? 194 PRO   A CG  1 
ATOM   1304 C CD  . PRO   A 1 215 ? 5.367   17.466  9.861   1.00 41.64 ? 194 PRO   A CD  1 
ATOM   1305 N N   . TYR   A 1 216 ? 8.101   17.591  7.153   1.00 35.86 ? 195 TYR   A N   1 
ATOM   1306 C CA  . TYR   A 1 216 ? 9.298   17.462  6.335   1.00 34.77 ? 195 TYR   A CA  1 
ATOM   1307 C C   . TYR   A 1 216 ? 9.021   16.622  5.094   1.00 37.69 ? 195 TYR   A C   1 
ATOM   1308 O O   . TYR   A 1 216 ? 9.928   16.401  4.295   1.00 42.09 ? 195 TYR   A O   1 
ATOM   1309 C CB  . TYR   A 1 216 ? 10.439  16.883  7.178   1.00 40.26 ? 195 TYR   A CB  1 
ATOM   1310 C CG  . TYR   A 1 216 ? 10.723  17.733  8.406   1.00 46.99 ? 195 TYR   A CG  1 
ATOM   1311 C CD1 . TYR   A 1 216 ? 9.838   17.751  9.481   1.00 54.15 ? 195 TYR   A CD1 1 
ATOM   1312 C CD2 . TYR   A 1 216 ? 11.864  18.530  8.490   1.00 60.34 ? 195 TYR   A CD2 1 
ATOM   1313 C CE1 . TYR   A 1 216 ? 10.068  18.531  10.604  1.00 60.40 ? 195 TYR   A CE1 1 
ATOM   1314 C CE2 . TYR   A 1 216 ? 12.106  19.318  9.608   1.00 62.74 ? 195 TYR   A CE2 1 
ATOM   1315 C CZ  . TYR   A 1 216 ? 11.210  19.314  10.667  1.00 66.61 ? 195 TYR   A CZ  1 
ATOM   1316 O OH  . TYR   A 1 216 ? 11.428  20.070  11.784  1.00 71.81 ? 195 TYR   A OH  1 
ATOM   1317 N N   . GLY   A 1 217 ? 7.783   16.121  4.938   1.00 31.61 ? 196 GLY   A N   1 
ATOM   1318 C CA  . GLY   A 1 217 ? 7.451   15.317  3.776   1.00 30.34 ? 196 GLY   A CA  1 
ATOM   1319 C C   . GLY   A 1 217 ? 7.937   13.879  3.962   1.00 28.51 ? 196 GLY   A C   1 
ATOM   1320 O O   . GLY   A 1 217 ? 7.955   13.101  3.015   1.00 33.18 ? 196 GLY   A O   1 
ATOM   1321 N N   . ILE   A 1 218 ? 8.312   13.525  5.200   1.00 28.04 ? 197 ILE   A N   1 
ATOM   1322 C CA  . ILE   A 1 218 ? 8.666   12.139  5.462   1.00 24.03 ? 197 ILE   A CA  1 
ATOM   1323 C C   . ILE   A 1 218 ? 7.438   11.381  5.976   1.00 23.69 ? 197 ILE   A C   1 
ATOM   1324 O O   . ILE   A 1 218 ? 6.957   11.682  7.082   1.00 24.84 ? 197 ILE   A O   1 
ATOM   1325 C CB  . ILE   A 1 218 ? 9.848   12.038  6.439   1.00 28.73 ? 197 ILE   A CB  1 
ATOM   1326 C CG1 . ILE   A 1 218 ? 11.085  12.790  5.879   1.00 33.32 ? 197 ILE   A CG1 1 
ATOM   1327 C CG2 . ILE   A 1 218 ? 10.210  10.579  6.750   1.00 25.76 ? 197 ILE   A CG2 1 
ATOM   1328 C CD1 . ILE   A 1 218 ? 12.105  13.078  6.967   1.00 32.99 ? 197 ILE   A CD1 1 
ATOM   1329 N N   . ARG   A 1 219 ? 7.061   10.326  5.248   1.00 23.44 ? 198 ARG   A N   1 
ATOM   1330 C CA  . ARG   A 1 219 ? 5.922   9.478   5.659   1.00 23.32 ? 198 ARG   A CA  1 
ATOM   1331 C C   . ARG   A 1 219 ? 6.452   8.327   6.511   1.00 27.02 ? 198 ARG   A C   1 
ATOM   1332 O O   . ARG   A 1 219 ? 7.545   7.845   6.257   1.00 27.51 ? 198 ARG   A O   1 
ATOM   1333 C CB  . ARG   A 1 219 ? 5.177   8.934   4.426   1.00 22.40 ? 198 ARG   A CB  1 
ATOM   1334 C CG  . ARG   A 1 219 ? 4.391   10.006  3.670   1.00 21.17 ? 198 ARG   A CG  1 
ATOM   1335 C CD  . ARG   A 1 219 ? 3.691   9.568   2.362   1.00 21.33 ? 198 ARG   A CD  1 
ATOM   1336 N NE  . ARG   A 1 219 ? 4.604   8.800   1.503   1.00 25.04 ? 198 ARG   A NE  1 
ATOM   1337 C CZ  . ARG   A 1 219 ? 4.676   7.473   1.427   1.00 25.57 ? 198 ARG   A CZ  1 
ATOM   1338 N NH1 . ARG   A 1 219 ? 3.866   6.668   2.135   1.00 23.14 ? 198 ARG   A NH1 1 
ATOM   1339 N NH2 . ARG   A 1 219 ? 5.579   6.934   0.639   1.00 26.58 ? 198 ARG   A NH2 1 
ATOM   1340 N N   . VAL   A 1 220 ? 5.690   7.918   7.538   1.00 22.34 ? 199 VAL   A N   1 
ATOM   1341 C CA  . VAL   A 1 220 ? 6.105   6.847   8.437   1.00 22.51 ? 199 VAL   A CA  1 
ATOM   1342 C C   . VAL   A 1 220 ? 4.891   5.917   8.565   1.00 22.23 ? 199 VAL   A C   1 
ATOM   1343 O O   . VAL   A 1 220 ? 3.863   6.308   9.142   1.00 21.17 ? 199 VAL   A O   1 
ATOM   1344 C CB  . VAL   A 1 220 ? 6.550   7.345   9.828   1.00 23.19 ? 199 VAL   A CB  1 
ATOM   1345 C CG1 . VAL   A 1 220 ? 7.113   6.181   10.635  1.00 22.85 ? 199 VAL   A CG1 1 
ATOM   1346 C CG2 . VAL   A 1 220 ? 7.617   8.487   9.768   1.00 23.82 ? 199 VAL   A CG2 1 
ATOM   1347 N N   . ASN   A 1 221 ? 5.062   4.661   8.146   1.00 20.39 ? 200 ASN   A N   1 
ATOM   1348 C CA  . ASN   A 1 221 ? 3.981   3.668   8.186   1.00 19.30 ? 200 ASN   A CA  1 
ATOM   1349 C C   . ASN   A 1 221 ? 4.551   2.349   8.711   1.00 22.29 ? 200 ASN   A C   1 
ATOM   1350 O O   . ASN   A 1 221 ? 5.752   2.232   8.990   1.00 21.98 ? 200 ASN   A O   1 
ATOM   1351 C CB  . ASN   A 1 221 ? 3.373   3.501   6.800   1.00 20.14 ? 200 ASN   A CB  1 
ATOM   1352 C CG  . ASN   A 1 221 ? 2.742   4.790   6.303   1.00 20.42 ? 200 ASN   A CG  1 
ATOM   1353 O OD1 . ASN   A 1 221 ? 1.749   5.211   6.883   1.00 21.84 ? 200 ASN   A OD1 1 
ATOM   1354 N ND2 . ASN   A 1 221 ? 3.286   5.424   5.262   1.00 21.56 ? 200 ASN   A ND2 1 
ATOM   1355 N N   . GLY   A 1 222 ? 3.660   1.371   8.919   1.00 22.39 ? 201 GLY   A N   1 
ATOM   1356 C CA  . GLY   A 1 222 ? 4.068   0.045   9.377   1.00 20.92 ? 201 GLY   A CA  1 
ATOM   1357 C C   . GLY   A 1 222 ? 3.372   -1.042  8.568   1.00 21.00 ? 201 GLY   A C   1 
ATOM   1358 O O   . GLY   A 1 222 ? 2.387   -0.808  7.857   1.00 21.40 ? 201 GLY   A O   1 
ATOM   1359 N N   . VAL   A 1 223 ? 4.011   -2.219  8.584   1.00 21.02 ? 202 VAL   A N   1 
ATOM   1360 C CA  . VAL   A 1 223 ? 3.481   -3.436  7.995   1.00 23.34 ? 202 VAL   A CA  1 
ATOM   1361 C C   . VAL   A 1 223 ? 3.481   -4.443  9.121   1.00 20.43 ? 202 VAL   A C   1 
ATOM   1362 O O   . VAL   A 1 223 ? 4.492   -4.579  9.832   1.00 21.24 ? 202 VAL   A O   1 
ATOM   1363 C CB  . VAL   A 1 223 ? 4.300   -3.963  6.794   1.00 19.85 ? 202 VAL   A CB  1 
ATOM   1364 C CG1 . VAL   A 1 223 ? 3.801   -5.341  6.352   1.00 21.33 ? 202 VAL   A CG1 1 
ATOM   1365 C CG2 . VAL   A 1 223 ? 4.162   -3.062  5.562   1.00 20.86 ? 202 VAL   A CG2 1 
ATOM   1366 N N   . ALA   A 1 224 ? 2.318   -5.082  9.340   1.00 19.13 ? 203 ALA   A N   1 
ATOM   1367 C CA  . ALA   A 1 224 ? 2.173   -5.934  10.509  1.00 21.43 ? 203 ALA   A CA  1 
ATOM   1368 C C   . ALA   A 1 224 ? 1.873   -7.352  10.041  1.00 22.58 ? 203 ALA   A C   1 
ATOM   1369 O O   . ALA   A 1 224 ? 0.700   -7.647  9.830   1.00 21.72 ? 203 ALA   A O   1 
ATOM   1370 C CB  . ALA   A 1 224 ? 1.089   -5.436  11.466  1.00 19.74 ? 203 ALA   A CB  1 
ATOM   1371 N N   . PRO   A 1 225 ? 2.890   -8.262  9.920   1.00 21.19 ? 204 PRO   A N   1 
ATOM   1372 C CA  . PRO   A 1 225 ? 2.604   -9.675  9.626   1.00 23.64 ? 204 PRO   A CA  1 
ATOM   1373 C C   . PRO   A 1 225 ? 1.860   -10.287 10.798  1.00 25.22 ? 204 PRO   A C   1 
ATOM   1374 O O   . PRO   A 1 225 ? 1.988   -9.794  11.930  1.00 23.93 ? 204 PRO   A O   1 
ATOM   1375 C CB  . PRO   A 1 225 ? 3.979   -10.311 9.539   1.00 22.29 ? 204 PRO   A CB  1 
ATOM   1376 C CG  . PRO   A 1 225 ? 4.879   -9.147  9.250   1.00 23.43 ? 204 PRO   A CG  1 
ATOM   1377 C CD  . PRO   A 1 225 ? 4.327   -7.995  10.082  1.00 20.13 ? 204 PRO   A CD  1 
ATOM   1378 N N   . GLY   A 1 226 ? 1.143   -11.392 10.497  1.00 23.78 ? 205 GLY   A N   1 
ATOM   1379 C CA  . GLY   A 1 226 ? 0.689   -12.278 11.547  1.00 23.59 ? 205 GLY   A CA  1 
ATOM   1380 C C   . GLY   A 1 226 ? 1.651   -13.451 11.661  1.00 24.74 ? 205 GLY   A C   1 
ATOM   1381 O O   . GLY   A 1 226 ? 2.575   -13.416 12.476  1.00 28.85 ? 205 GLY   A O   1 
ATOM   1382 N N   . VAL   A 1 227 ? 1.376   -14.504 10.890  1.00 23.58 ? 206 VAL   A N   1 
ATOM   1383 C CA  . VAL   A 1 227 ? 2.385   -15.539 10.729  1.00 26.26 ? 206 VAL   A CA  1 
ATOM   1384 C C   . VAL   A 1 227 ? 2.873   -15.452 9.285   1.00 21.88 ? 206 VAL   A C   1 
ATOM   1385 O O   . VAL   A 1 227 ? 2.114   -15.489 8.328   1.00 25.40 ? 206 VAL   A O   1 
ATOM   1386 C CB  . VAL   A 1 227 ? 2.002   -16.977 11.142  1.00 33.42 ? 206 VAL   A CB  1 
ATOM   1387 C CG1 . VAL   A 1 227 ? 1.588   -17.039 12.608  1.00 39.65 ? 206 VAL   A CG1 1 
ATOM   1388 C CG2 . VAL   A 1 227 ? 0.886   -17.541 10.290  1.00 32.75 ? 206 VAL   A CG2 1 
ATOM   1389 N N   . SER   A 1 228 ? 4.183   -15.304 9.157   1.00 25.85 ? 207 SER   A N   1 
ATOM   1390 C CA  . SER   A 1 228 ? 4.823   -15.324 7.860   1.00 26.23 ? 207 SER   A CA  1 
ATOM   1391 C C   . SER   A 1 228 ? 5.843   -16.439 7.983   1.00 27.54 ? 207 SER   A C   1 
ATOM   1392 O O   . SER   A 1 228 ? 5.560   -17.413 8.657   1.00 29.06 ? 207 SER   A O   1 
ATOM   1393 C CB  . SER   A 1 228 ? 5.457   -14.002 7.523   1.00 23.86 ? 207 SER   A CB  1 
ATOM   1394 O OG  . SER   A 1 228 ? 5.997   -14.003 6.202   1.00 28.05 ? 207 SER   A OG  1 
ATOM   1395 N N   . LEU   A 1 229 ? 7.047   -16.243 7.447   1.00 31.88 ? 208 LEU   A N   1 
ATOM   1396 C CA  . LEU   A 1 229 ? 8.046   -17.313 7.552   1.00 30.23 ? 208 LEU   A CA  1 
ATOM   1397 C C   . LEU   A 1 229 ? 8.223   -17.697 9.010   1.00 35.57 ? 208 LEU   A C   1 
ATOM   1398 O O   . LEU   A 1 229 ? 8.536   -16.855 9.866   1.00 33.48 ? 208 LEU   A O   1 
ATOM   1399 C CB  . LEU   A 1 229 ? 9.372   -16.876 6.927   1.00 33.73 ? 208 LEU   A CB  1 
ATOM   1400 C CG  . LEU   A 1 229 ? 9.401   -16.746 5.406   1.00 38.79 ? 208 LEU   A CG  1 
ATOM   1401 C CD1 . LEU   A 1 229 ? 10.765  -16.139 5.027   1.00 37.22 ? 208 LEU   A CD1 1 
ATOM   1402 C CD2 . LEU   A 1 229 ? 9.198   -18.124 4.756   1.00 40.48 ? 208 LEU   A CD2 1 
ATOM   1403 N N   . LEU   A 1 230 ? 8.005   -18.994 9.271   1.00 30.21 ? 209 LEU   A N   1 
ATOM   1404 C CA  . LEU   A 1 230 ? 8.180   -19.526 10.597  1.00 33.06 ? 209 LEU   A CA  1 
ATOM   1405 C C   . LEU   A 1 230 ? 9.677   -19.653 10.876  1.00 35.57 ? 209 LEU   A C   1 
ATOM   1406 O O   . LEU   A 1 230 ? 10.496  -19.711 9.938   1.00 34.39 ? 209 LEU   A O   1 
ATOM   1407 C CB  . LEU   A 1 230 ? 7.439   -20.860 10.738  1.00 36.60 ? 209 LEU   A CB  1 
ATOM   1408 C CG  . LEU   A 1 230 ? 5.912   -20.814 10.925  1.00 41.10 ? 209 LEU   A CG  1 
ATOM   1409 C CD1 . LEU   A 1 230 ? 5.384   -19.583 11.666  1.00 42.15 ? 209 LEU   A CD1 1 
ATOM   1410 C CD2 . LEU   A 1 230 ? 5.068   -21.117 9.703   1.00 37.72 ? 209 LEU   A CD2 1 
ATOM   1411 N N   . PRO   A 1 231 ? 10.052  -19.660 12.174  1.00 37.99 ? 210 PRO   A N   1 
ATOM   1412 C CA  . PRO   A 1 231 ? 11.452  -19.696 12.577  1.00 40.02 ? 210 PRO   A CA  1 
ATOM   1413 C C   . PRO   A 1 231 ? 12.099  -20.953 11.992  1.00 40.65 ? 210 PRO   A C   1 
ATOM   1414 O O   . PRO   A 1 231 ? 11.455  -22.003 11.889  1.00 36.92 ? 210 PRO   A O   1 
ATOM   1415 C CB  . PRO   A 1 231 ? 11.447  -19.681 14.128  1.00 39.02 ? 210 PRO   A CB  1 
ATOM   1416 C CG  . PRO   A 1 231 ? 10.023  -19.321 14.533  1.00 41.64 ? 210 PRO   A CG  1 
ATOM   1417 C CD  . PRO   A 1 231 ? 9.133   -19.629 13.332  1.00 38.65 ? 210 PRO   A CD  1 
ATOM   1418 N N   . VAL   A 1 232 ? 13.368  -20.805 11.584  1.00 38.96 ? 211 VAL   A N   1 
ATOM   1419 C CA  . VAL   A 1 232 ? 14.154  -21.902 11.032  1.00 46.88 ? 211 VAL   A CA  1 
ATOM   1420 C C   . VAL   A 1 232 ? 14.153  -23.086 12.004  1.00 48.44 ? 211 VAL   A C   1 
ATOM   1421 O O   . VAL   A 1 232 ? 14.178  -24.229 11.554  1.00 53.17 ? 211 VAL   A O   1 
ATOM   1422 C CB  . VAL   A 1 232 ? 15.583  -21.487 10.620  1.00 44.63 ? 211 VAL   A CB  1 
ATOM   1423 N N   . ALA   A 1 233 ? 14.071  -22.808 13.319  1.00 48.28 ? 212 ALA   A N   1 
ATOM   1424 C CA  . ALA   A 1 233 ? 14.187  -23.816 14.368  1.00 51.93 ? 212 ALA   A CA  1 
ATOM   1425 C C   . ALA   A 1 233 ? 12.885  -24.573 14.630  1.00 48.93 ? 212 ALA   A C   1 
ATOM   1426 O O   . ALA   A 1 233 ? 12.922  -25.644 15.230  1.00 44.43 ? 212 ALA   A O   1 
ATOM   1427 C CB  . ALA   A 1 233 ? 14.708  -23.199 15.661  1.00 50.32 ? 212 ALA   A CB  1 
ATOM   1428 N N   . MET   A 1 234 ? 11.736  -24.042 14.196  1.00 43.42 ? 213 MET   A N   1 
ATOM   1429 C CA  . MET   A 1 234 ? 10.447  -24.642 14.546  1.00 41.95 ? 213 MET   A CA  1 
ATOM   1430 C C   . MET   A 1 234 ? 10.242  -25.955 13.777  1.00 42.39 ? 213 MET   A C   1 
ATOM   1431 O O   . MET   A 1 234 ? 10.546  -26.002 12.586  1.00 38.97 ? 213 MET   A O   1 
ATOM   1432 C CB  . MET   A 1 234 ? 9.315   -23.654 14.213  1.00 39.19 ? 213 MET   A CB  1 
ATOM   1433 C CG  . MET   A 1 234 ? 7.936   -24.088 14.657  1.00 38.54 ? 213 MET   A CG  1 
ATOM   1434 S SD  . MET   A 1 234 ? 6.721   -22.775 14.380  1.00 40.68 ? 213 MET   A SD  1 
ATOM   1435 C CE  . MET   A 1 234 ? 7.033   -21.667 15.765  1.00 44.79 ? 213 MET   A CE  1 
ATOM   1436 N N   . GLY   A 1 235 ? 9.705   -27.000 14.443  1.00 42.55 ? 214 GLY   A N   1 
ATOM   1437 C CA  . GLY   A 1 235 ? 9.355   -28.262 13.781  1.00 39.30 ? 214 GLY   A CA  1 
ATOM   1438 C C   . GLY   A 1 235 ? 8.122   -28.095 12.889  1.00 40.58 ? 214 GLY   A C   1 
ATOM   1439 O O   . GLY   A 1 235 ? 7.319   -27.183 13.109  1.00 34.13 ? 214 GLY   A O   1 
ATOM   1440 N N   . GLU   A 1 236 ? 7.989   -28.951 11.865  1.00 36.62 ? 215 GLU   A N   1 
ATOM   1441 C CA  . GLU   A 1 236 ? 6.885   -28.855 10.927  1.00 34.61 ? 215 GLU   A CA  1 
ATOM   1442 C C   . GLU   A 1 236 ? 5.538   -28.984 11.641  1.00 38.50 ? 215 GLU   A C   1 
ATOM   1443 O O   . GLU   A 1 236 ? 4.556   -28.391 11.222  1.00 38.17 ? 215 GLU   A O   1 
ATOM   1444 C CB  . GLU   A 1 236 ? 6.951   -29.966 9.882   1.00 36.92 ? 215 GLU   A CB  1 
ATOM   1445 C CG  . GLU   A 1 236 ? 6.002   -29.732 8.712   1.00 42.97 ? 215 GLU   A CG  1 
ATOM   1446 C CD  . GLU   A 1 236 ? 6.415   -28.543 7.848   1.00 45.81 ? 215 GLU   A CD  1 
ATOM   1447 O OE1 . GLU   A 1 236 ? 7.507   -27.986 8.085   1.00 50.85 ? 215 GLU   A OE1 1 
ATOM   1448 O OE2 . GLU   A 1 236 ? 5.648   -28.167 6.928   1.00 51.63 ? 215 GLU   A OE2 1 
ATOM   1449 N N   . GLU   A 1 237 ? 5.461   -29.826 12.672  1.00 36.65 ? 216 GLU   A N   1 
ATOM   1450 C CA  . GLU   A 1 237 ? 4.205   -30.054 13.366  1.00 39.67 ? 216 GLU   A CA  1 
ATOM   1451 C C   . GLU   A 1 237 ? 3.696   -28.740 13.974  1.00 41.89 ? 216 GLU   A C   1 
ATOM   1452 O O   . GLU   A 1 237 ? 2.508   -28.403 13.896  1.00 38.31 ? 216 GLU   A O   1 
ATOM   1453 C CB  . GLU   A 1 237 ? 4.462   -31.100 14.460  1.00 45.83 ? 216 GLU   A CB  1 
ATOM   1454 C CG  . GLU   A 1 237 ? 3.193   -31.672 15.090  1.00 44.91 ? 216 GLU   A CG  1 
ATOM   1455 N N   . GLU   A 1 238 ? 4.622   -28.001 14.591  1.00 39.21 ? 217 GLU   A N   1 
ATOM   1456 C CA  . GLU   A 1 238 ? 4.285   -26.767 15.285  1.00 40.13 ? 217 GLU   A CA  1 
ATOM   1457 C C   . GLU   A 1 238 ? 3.976   -25.691 14.242  1.00 36.08 ? 217 GLU   A C   1 
ATOM   1458 O O   . GLU   A 1 238 ? 3.049   -24.925 14.434  1.00 35.48 ? 217 GLU   A O   1 
ATOM   1459 C CB  . GLU   A 1 238 ? 5.391   -26.413 16.287  1.00 42.54 ? 217 GLU   A CB  1 
ATOM   1460 C CG  . GLU   A 1 238 ? 5.041   -25.254 17.218  0.70 42.57 ? 217 GLU   A CG  1 
ATOM   1461 C CD  . GLU   A 1 238 ? 6.205   -24.672 18.012  0.70 49.82 ? 217 GLU   A CD  1 
ATOM   1462 O OE1 . GLU   A 1 238 ? 5.986   -23.680 18.741  0.70 43.80 ? 217 GLU   A OE1 1 
ATOM   1463 O OE2 . GLU   A 1 238 ? 7.338   -25.190 17.904  0.70 54.18 ? 217 GLU   A OE2 1 
ATOM   1464 N N   . LYS   A 1 239 ? 4.760   -25.636 13.151  1.00 34.39 ? 218 LYS   A N   1 
ATOM   1465 C CA  . LYS   A 1 239 ? 4.424   -24.793 12.008  1.00 33.36 ? 218 LYS   A CA  1 
ATOM   1466 C C   . LYS   A 1 239 ? 2.992   -25.054 11.512  1.00 30.40 ? 218 LYS   A C   1 
ATOM   1467 O O   . LYS   A 1 239 ? 2.243   -24.113 11.237  1.00 28.59 ? 218 LYS   A O   1 
ATOM   1468 C CB  . LYS   A 1 239 ? 5.404   -24.977 10.841  1.00 33.51 ? 218 LYS   A CB  1 
ATOM   1469 C CG  . LYS   A 1 239 ? 6.844   -24.531 11.108  1.00 33.34 ? 218 LYS   A CG  1 
ATOM   1470 C CD  . LYS   A 1 239 ? 7.771   -24.667 9.896   1.00 38.45 ? 218 LYS   A CD  1 
ATOM   1471 C CE  . LYS   A 1 239 ? 9.155   -24.212 10.256  1.00 49.04 ? 218 LYS   A CE  1 
ATOM   1472 N NZ  . LYS   A 1 239 ? 10.200  -24.572 9.295   1.00 49.45 ? 218 LYS   A NZ  1 
ATOM   1473 N N   . ASP   A 1 240 ? 2.564   -26.321 11.405  1.00 30.46 ? 219 ASP   A N   1 
ATOM   1474 C CA  . ASP   A 1 240 ? 1.224   -26.579 10.880  1.00 31.63 ? 219 ASP   A CA  1 
ATOM   1475 C C   . ASP   A 1 240 ? 0.125   -26.155 11.855  1.00 30.99 ? 219 ASP   A C   1 
ATOM   1476 O O   . ASP   A 1 240 ? -0.993  -25.837 11.424  1.00 31.86 ? 219 ASP   A O   1 
ATOM   1477 C CB  . ASP   A 1 240 ? 1.006   -28.050 10.566  1.00 36.19 ? 219 ASP   A CB  1 
ATOM   1478 C CG  . ASP   A 1 240 ? 1.687   -28.531 9.293   1.00 42.26 ? 219 ASP   A CG  1 
ATOM   1479 O OD1 . ASP   A 1 240 ? 2.056   -27.685 8.431   1.00 43.56 ? 219 ASP   A OD1 1 
ATOM   1480 O OD2 . ASP   A 1 240 ? 1.830   -29.749 9.173   1.00 42.93 ? 219 ASP   A OD2 1 
ATOM   1481 N N   . LYS   A 1 241 ? 0.415   -26.231 13.161  1.00 30.13 ? 220 LYS   A N   1 
ATOM   1482 C CA  . LYS   A 1 241 ? -0.504  -25.723 14.168  1.00 33.39 ? 220 LYS   A CA  1 
ATOM   1483 C C   . LYS   A 1 241 ? -0.755  -24.236 13.894  1.00 27.90 ? 220 LYS   A C   1 
ATOM   1484 O O   . LYS   A 1 241 ? -1.916  -23.821 13.843  1.00 33.63 ? 220 LYS   A O   1 
ATOM   1485 C CB  . LYS   A 1 241 ? -0.004  -25.949 15.600  1.00 35.42 ? 220 LYS   A CB  1 
ATOM   1486 C CG  . LYS   A 1 241 ? -0.912  -25.462 16.739  0.60 39.01 ? 220 LYS   A CG  1 
ATOM   1487 C CD  . LYS   A 1 241 ? -0.195  -25.367 18.086  0.60 40.20 ? 220 LYS   A CD  1 
ATOM   1488 C CE  . LYS   A 1 241 ? 0.849   -24.296 18.168  0.60 42.73 ? 220 LYS   A CE  1 
ATOM   1489 N NZ  . LYS   A 1 241 ? 0.278   -22.949 18.312  0.60 43.33 ? 220 LYS   A NZ  1 
ATOM   1490 N N   . TRP   A 1 242 ? 0.308   -23.459 13.673  1.00 28.47 ? 221 TRP   A N   1 
ATOM   1491 C CA  . TRP   A 1 242 ? 0.088   -22.052 13.321  1.00 28.15 ? 221 TRP   A CA  1 
ATOM   1492 C C   . TRP   A 1 242 ? -0.655  -21.876 11.993  1.00 32.98 ? 221 TRP   A C   1 
ATOM   1493 O O   . TRP   A 1 242 ? -1.592  -21.074 11.890  1.00 30.23 ? 221 TRP   A O   1 
ATOM   1494 C CB  . TRP   A 1 242 ? 1.399   -21.267 13.341  1.00 29.86 ? 221 TRP   A CB  1 
ATOM   1495 C CG  . TRP   A 1 242 ? 1.817   -20.957 14.745  1.00 37.49 ? 221 TRP   A CG  1 
ATOM   1496 C CD1 . TRP   A 1 242 ? 2.698   -21.644 15.529  1.00 42.22 ? 221 TRP   A CD1 1 
ATOM   1497 C CD2 . TRP   A 1 242 ? 1.264   -19.903 15.567  1.00 41.28 ? 221 TRP   A CD2 1 
ATOM   1498 N NE1 . TRP   A 1 242 ? 2.753   -21.076 16.777  1.00 44.18 ? 221 TRP   A NE1 1 
ATOM   1499 C CE2 . TRP   A 1 242 ? 1.888   -20.011 16.831  1.00 44.81 ? 221 TRP   A CE2 1 
ATOM   1500 C CE3 . TRP   A 1 242 ? 0.326   -18.884 15.347  1.00 40.78 ? 221 TRP   A CE3 1 
ATOM   1501 C CZ2 . TRP   A 1 242 ? 1.590   -19.137 17.876  1.00 44.26 ? 221 TRP   A CZ2 1 
ATOM   1502 C CZ3 . TRP   A 1 242 ? 0.033   -18.020 16.383  1.00 43.80 ? 221 TRP   A CZ3 1 
ATOM   1503 C CH2 . TRP   A 1 242 ? 0.637   -18.171 17.631  1.00 42.07 ? 221 TRP   A CH2 1 
ATOM   1504 N N   . ARG   A 1 243 ? -0.193  -22.565 10.929  1.00 27.97 ? 222 ARG   A N   1 
ATOM   1505 C CA  . ARG   A 1 243 ? -0.861  -22.482 9.636   1.00 28.94 ? 222 ARG   A CA  1 
ATOM   1506 C C   . ARG   A 1 243 ? -2.383  -22.673 9.739   1.00 28.24 ? 222 ARG   A C   1 
ATOM   1507 O O   . ARG   A 1 243 ? -3.158  -21.945 9.115   1.00 29.22 ? 222 ARG   A O   1 
ATOM   1508 C CB  . ARG   A 1 243 ? -0.283  -23.569 8.713   1.00 24.98 ? 222 ARG   A CB  1 
ATOM   1509 C CG  . ARG   A 1 243 ? 1.119   -23.157 8.305   1.00 28.91 ? 222 ARG   A CG  1 
ATOM   1510 C CD  . ARG   A 1 243 ? 1.810   -24.258 7.509   1.00 29.67 ? 222 ARG   A CD  1 
ATOM   1511 N NE  . ARG   A 1 243 ? 3.139   -23.832 7.053   1.00 30.93 ? 222 ARG   A NE  1 
ATOM   1512 C CZ  . ARG   A 1 243 ? 4.226   -24.593 7.058   1.00 29.22 ? 222 ARG   A CZ  1 
ATOM   1513 N NH1 . ARG   A 1 243 ? 4.127   -25.861 7.400   1.00 29.98 ? 222 ARG   A NH1 1 
ATOM   1514 N NH2 . ARG   A 1 243 ? 5.389   -24.076 6.682   1.00 29.23 ? 222 ARG   A NH2 1 
ATOM   1515 N N   . ARG   A 1 244 ? -2.822  -23.680 10.501  1.00 28.48 ? 223 ARG   A N   1 
ATOM   1516 C CA  . ARG   A 1 244 ? -4.219  -24.074 10.547  1.00 29.93 ? 223 ARG   A CA  1 
ATOM   1517 C C   . ARG   A 1 244 ? -5.111  -22.992 11.165  1.00 31.29 ? 223 ARG   A C   1 
ATOM   1518 O O   . ARG   A 1 244 ? -6.312  -23.092 11.008  1.00 32.42 ? 223 ARG   A O   1 
ATOM   1519 C CB  . ARG   A 1 244 ? -4.494  -25.387 11.310  1.00 34.80 ? 223 ARG   A CB  1 
ATOM   1520 C CG  . ARG   A 1 244 ? -4.352  -26.589 10.389  1.00 49.67 ? 223 ARG   A CG  1 
ATOM   1521 C CD  . ARG   A 1 244 ? -4.563  -27.937 11.068  1.00 53.77 ? 223 ARG   A CD  1 
ATOM   1522 N NE  . ARG   A 1 244 ? -3.825  -28.060 12.331  1.00 58.84 ? 223 ARG   A NE  1 
ATOM   1523 C CZ  . ARG   A 1 244 ? -2.795  -28.875 12.583  1.00 57.55 ? 223 ARG   A CZ  1 
ATOM   1524 N NH1 . ARG   A 1 244 ? -2.276  -29.628 11.629  1.00 51.07 ? 223 ARG   A NH1 1 
ATOM   1525 N NH2 . ARG   A 1 244 ? -2.274  -28.913 13.798  1.00 50.65 ? 223 ARG   A NH2 1 
ATOM   1526 N N   . LYS   A 1 245 ? -4.525  -22.001 11.857  1.00 28.02 ? 224 LYS   A N   1 
ATOM   1527 C CA  . LYS   A 1 245 ? -5.276  -20.916 12.486  1.00 28.15 ? 224 LYS   A CA  1 
ATOM   1528 C C   . LYS   A 1 245 ? -5.625  -19.819 11.474  1.00 28.25 ? 224 LYS   A C   1 
ATOM   1529 O O   . LYS   A 1 245 ? -6.511  -19.003 11.744  1.00 25.38 ? 224 LYS   A O   1 
ATOM   1530 C CB  . LYS   A 1 245 ? -4.429  -20.292 13.604  1.00 27.41 ? 224 LYS   A CB  1 
ATOM   1531 C CG  . LYS   A 1 245 ? -3.985  -21.204 14.800  1.00 28.90 ? 224 LYS   A CG  1 
ATOM   1532 C CD  . LYS   A 1 245 ? -2.954  -20.507 15.692  1.00 34.46 ? 224 LYS   A CD  1 
ATOM   1533 C CE  . LYS   A 1 245 ? -2.279  -21.321 16.806  1.00 36.41 ? 224 LYS   A CE  1 
ATOM   1534 N NZ  . LYS   A 1 245 ? -3.272  -22.067 17.595  1.00 38.30 ? 224 LYS   A NZ  1 
ATOM   1535 N N   . VAL   A 1 246 ? -4.924  -19.747 10.335  1.00 23.78 ? 225 VAL   A N   1 
ATOM   1536 C CA  . VAL   A 1 246 ? -5.105  -18.632 9.390   1.00 21.25 ? 225 VAL   A CA  1 
ATOM   1537 C C   . VAL   A 1 246 ? -6.360  -18.826 8.535   1.00 22.78 ? 225 VAL   A C   1 
ATOM   1538 O O   . VAL   A 1 246 ? -6.427  -19.747 7.709   1.00 25.73 ? 225 VAL   A O   1 
ATOM   1539 C CB  . VAL   A 1 246 ? -3.853  -18.463 8.491   1.00 24.03 ? 225 VAL   A CB  1 
ATOM   1540 C CG1 . VAL   A 1 246 ? -4.021  -17.308 7.484   1.00 22.41 ? 225 VAL   A CG1 1 
ATOM   1541 C CG2 . VAL   A 1 246 ? -2.555  -18.312 9.317   1.00 20.95 ? 225 VAL   A CG2 1 
ATOM   1542 N N   . PRO   A 1 247 ? -7.391  -17.944 8.633   1.00 23.13 ? 226 PRO   A N   1 
ATOM   1543 C CA  . PRO   A 1 247 ? -8.593  -18.062 7.807   1.00 25.05 ? 226 PRO   A CA  1 
ATOM   1544 C C   . PRO   A 1 247 ? -8.357  -18.109 6.298   1.00 24.37 ? 226 PRO   A C   1 
ATOM   1545 O O   . PRO   A 1 247 ? -8.941  -18.931 5.604   1.00 23.37 ? 226 PRO   A O   1 
ATOM   1546 C CB  . PRO   A 1 247 ? -9.446  -16.820 8.199   1.00 26.31 ? 226 PRO   A CB  1 
ATOM   1547 C CG  . PRO   A 1 247 ? -8.972  -16.519 9.616   1.00 23.82 ? 226 PRO   A CG  1 
ATOM   1548 C CD  . PRO   A 1 247 ? -7.467  -16.822 9.603   1.00 24.38 ? 226 PRO   A CD  1 
ATOM   1549 N N   . LEU   A 1 248 ? -7.460  -17.249 5.800   1.00 23.00 ? 227 LEU   A N   1 
ATOM   1550 C CA  . LEU   A 1 248 ? -7.321  -17.091 4.360   1.00 25.27 ? 227 LEU   A CA  1 
ATOM   1551 C C   . LEU   A 1 248 ? -6.256  -18.076 3.887   1.00 24.07 ? 227 LEU   A C   1 
ATOM   1552 O O   . LEU   A 1 248 ? -5.088  -17.723 3.777   1.00 27.48 ? 227 LEU   A O   1 
ATOM   1553 C CB  . LEU   A 1 248 ? -6.893  -15.640 4.068   1.00 23.87 ? 227 LEU   A CB  1 
ATOM   1554 C CG  . LEU   A 1 248 ? -6.905  -15.221 2.593   1.00 25.85 ? 227 LEU   A CG  1 
ATOM   1555 C CD1 . LEU   A 1 248 ? -8.372  -15.215 2.106   1.00 27.74 ? 227 LEU   A CD1 1 
ATOM   1556 C CD2 . LEU   A 1 248 ? -6.308  -13.836 2.480   1.00 24.78 ? 227 LEU   A CD2 1 
ATOM   1557 N N   . GLY   A 1 249 ? -6.655  -19.338 3.715   1.00 25.81 ? 228 GLY   A N   1 
ATOM   1558 C CA  . GLY   A 1 249 ? -5.775  -20.258 3.029   1.00 28.69 ? 228 GLY   A CA  1 
ATOM   1559 C C   . GLY   A 1 249 ? -5.103  -21.252 3.961   1.00 28.70 ? 228 GLY   A C   1 
ATOM   1560 O O   . GLY   A 1 249 ? -4.389  -22.127 3.452   1.00 26.66 ? 228 GLY   A O   1 
ATOM   1561 N N   . ARG   A 1 250 ? -5.234  -21.049 5.295   1.00 27.12 ? 229 ARG   A N   1 
ATOM   1562 C CA  . ARG   A 1 250 ? -4.569  -21.923 6.257   1.00 25.87 ? 229 ARG   A CA  1 
ATOM   1563 C C   . ARG   A 1 250 ? -3.084  -22.066 5.940   1.00 28.90 ? 229 ARG   A C   1 
ATOM   1564 O O   . ARG   A 1 250 ? -2.526  -23.182 5.915   1.00 25.61 ? 229 ARG   A O   1 
ATOM   1565 C CB  . ARG   A 1 250 ? -5.157  -23.344 6.249   1.00 30.19 ? 229 ARG   A CB  1 
ATOM   1566 C CG  . ARG   A 1 250 ? -6.663  -23.383 6.466   1.00 36.46 ? 229 ARG   A CG  1 
ATOM   1567 C CD  . ARG   A 1 250 ? -7.025  -22.844 7.814   1.00 38.70 ? 229 ARG   A CD  1 
ATOM   1568 N NE  . ARG   A 1 250 ? -8.443  -22.464 7.842   1.00 39.60 ? 229 ARG   A NE  1 
ATOM   1569 C CZ  . ARG   A 1 250 ? -9.097  -21.956 8.888   1.00 41.56 ? 229 ARG   A CZ  1 
ATOM   1570 N NH1 . ARG   A 1 250 ? -8.468  -21.657 10.013  1.00 40.52 ? 229 ARG   A NH1 1 
ATOM   1571 N NH2 . ARG   A 1 250 ? -10.393 -21.743 8.792   1.00 43.19 ? 229 ARG   A NH2 1 
ATOM   1572 N N   . ARG   A 1 251 ? -2.437  -20.935 5.673   1.00 25.60 ? 230 ARG   A N   1 
ATOM   1573 C CA  . ARG   A 1 251 ? -1.013  -20.941 5.407   1.00 23.69 ? 230 ARG   A CA  1 
ATOM   1574 C C   . ARG   A 1 251 ? -0.420  -19.611 5.857   1.00 28.09 ? 230 ARG   A C   1 
ATOM   1575 O O   . ARG   A 1 251 ? -1.153  -18.610 6.001   1.00 25.60 ? 230 ARG   A O   1 
ATOM   1576 C CB  . ARG   A 1 251 ? -0.741  -21.255 3.928   1.00 32.40 ? 230 ARG   A CB  1 
ATOM   1577 C CG  . ARG   A 1 251 ? -1.275  -20.251 2.911   1.00 38.73 ? 230 ARG   A CG  1 
ATOM   1578 C CD  . ARG   A 1 251 ? -1.029  -20.615 1.432   1.00 45.87 ? 230 ARG   A CD  1 
ATOM   1579 N NE  . ARG   A 1 251 ? 0.368   -21.017 1.217   0.70 49.99 ? 230 ARG   A NE  1 
ATOM   1580 C CZ  . ARG   A 1 251 ? 0.963   -21.529 0.131   0.70 49.59 ? 230 ARG   A CZ  1 
ATOM   1581 N NH1 . ARG   A 1 251 ? 0.311   -21.699 -1.009  0.70 44.67 ? 230 ARG   A NH1 1 
ATOM   1582 N NH2 . ARG   A 1 251 ? 2.237   -21.864 0.206   0.70 47.37 ? 230 ARG   A NH2 1 
ATOM   1583 N N   . GLU   A 1 252 ? 0.905   -19.632 6.090   1.00 24.87 ? 231 GLU   A N   1 
ATOM   1584 C CA  . GLU   A 1 252 ? 1.629   -18.428 6.486   1.00 25.61 ? 231 GLU   A CA  1 
ATOM   1585 C C   . GLU   A 1 252 ? 1.807   -17.536 5.268   1.00 27.41 ? 231 GLU   A C   1 
ATOM   1586 O O   . GLU   A 1 252 ? 1.787   -18.017 4.136   1.00 26.76 ? 231 GLU   A O   1 
ATOM   1587 C CB  . GLU   A 1 252 ? 2.962   -18.770 7.166   1.00 25.71 ? 231 GLU   A CB  1 
ATOM   1588 C CG  . GLU   A 1 252 ? 4.027   -19.317 6.204   1.00 28.79 ? 231 GLU   A CG  1 
ATOM   1589 C CD  . GLU   A 1 252 ? 4.018   -20.828 5.951   1.00 33.83 ? 231 GLU   A CD  1 
ATOM   1590 O OE1 . GLU   A 1 252 ? 5.128   -21.446 5.861   1.00 32.38 ? 231 GLU   A OE1 1 
ATOM   1591 O OE2 . GLU   A 1 252 ? 2.886   -21.383 5.854   1.00 29.50 ? 231 GLU   A OE2 1 
ATOM   1592 N N   . ALA   A 1 253 ? 2.039   -16.224 5.500   1.00 26.61 ? 232 ALA   A N   1 
ATOM   1593 C CA  . ALA   A 1 253 ? 2.391   -15.318 4.420   1.00 27.16 ? 232 ALA   A CA  1 
ATOM   1594 C C   . ALA   A 1 253 ? 3.796   -15.643 3.906   1.00 25.49 ? 232 ALA   A C   1 
ATOM   1595 O O   . ALA   A 1 253 ? 4.720   -15.873 4.705   1.00 27.32 ? 232 ALA   A O   1 
ATOM   1596 C CB  . ALA   A 1 253 ? 2.468   -13.904 4.947   1.00 25.59 ? 232 ALA   A CB  1 
ATOM   1597 N N   . SER   A 1 254 ? 3.946   -15.532 2.584   1.00 24.59 ? 233 SER   A N   1 
ATOM   1598 C CA  . SER   A 1 254 ? 5.268   -15.604 1.986   1.00 23.93 ? 233 SER   A CA  1 
ATOM   1599 C C   . SER   A 1 254 ? 6.003   -14.313 2.311   1.00 29.68 ? 233 SER   A C   1 
ATOM   1600 O O   . SER   A 1 254 ? 5.385   -13.278 2.580   1.00 26.56 ? 233 SER   A O   1 
ATOM   1601 C CB  . SER   A 1 254 ? 5.233   -15.839 0.514   1.00 23.93 ? 233 SER   A CB  1 
ATOM   1602 O OG  . SER   A 1 254 ? 4.685   -14.737 -0.192  1.00 27.98 ? 233 SER   A OG  1 
ATOM   1603 N N   . ALA   A 1 255 ? 7.339   -14.381 2.264   1.00 26.70 ? 234 ALA   A N   1 
ATOM   1604 C CA  . ALA   A 1 255 ? 8.135   -13.187 2.488   1.00 27.96 ? 234 ALA   A CA  1 
ATOM   1605 C C   . ALA   A 1 255 ? 7.779   -12.162 1.424   1.00 26.13 ? 234 ALA   A C   1 
ATOM   1606 O O   . ALA   A 1 255 ? 7.779   -10.945 1.671   1.00 24.88 ? 234 ALA   A O   1 
ATOM   1607 C CB  . ALA   A 1 255 ? 9.630   -13.549 2.491   1.00 26.68 ? 234 ALA   A CB  1 
ATOM   1608 N N   . GLU   A 1 256 ? 7.471   -12.643 0.208   1.00 23.12 ? 235 GLU   A N   1 
ATOM   1609 C CA  . GLU   A 1 256 ? 7.161   -11.709 -0.857  1.00 26.03 ? 235 GLU   A CA  1 
ATOM   1610 C C   . GLU   A 1 256 ? 5.883   -10.920 -0.575  1.00 24.07 ? 235 GLU   A C   1 
ATOM   1611 O O   . GLU   A 1 256 ? 5.762   -9.775  -1.001  1.00 26.15 ? 235 GLU   A O   1 
ATOM   1612 C CB  . GLU   A 1 256 ? 6.971   -12.462 -2.174  1.00 32.16 ? 235 GLU   A CB  1 
ATOM   1613 C CG  . GLU   A 1 256 ? 6.885   -11.518 -3.369  1.00 43.29 ? 235 GLU   A CG  1 
ATOM   1614 C CD  . GLU   A 1 256 ? 6.825   -12.111 -4.777  1.00 57.48 ? 235 GLU   A CD  1 
ATOM   1615 O OE1 . GLU   A 1 256 ? 6.734   -11.302 -5.730  1.00 61.71 ? 235 GLU   A OE1 1 
ATOM   1616 O OE2 . GLU   A 1 256 ? 6.878   -13.354 -4.933  1.00 66.42 ? 235 GLU   A OE2 1 
ATOM   1617 N N   . GLN   A 1 257 ? 4.878   -11.597 -0.010  1.00 23.73 ? 236 GLN   A N   1 
ATOM   1618 C CA  . GLN   A 1 257 ? 3.598   -10.958 0.326   1.00 24.43 ? 236 GLN   A CA  1 
ATOM   1619 C C   . GLN   A 1 257 ? 3.805   -9.834  1.357   1.00 24.03 ? 236 GLN   A C   1 
ATOM   1620 O O   . GLN   A 1 257 ? 3.166   -8.779  1.242   1.00 23.66 ? 236 GLN   A O   1 
ATOM   1621 C CB  . GLN   A 1 257 ? 2.618   -12.031 0.811   1.00 24.77 ? 236 GLN   A CB  1 
ATOM   1622 C CG  . GLN   A 1 257 ? 2.073   -12.888 -0.335  1.00 25.62 ? 236 GLN   A CG  1 
ATOM   1623 C CD  . GLN   A 1 257 ? 1.266   -14.085 0.104   1.00 25.01 ? 236 GLN   A CD  1 
ATOM   1624 O OE1 . GLN   A 1 257 ? 1.494   -14.673 1.172   1.00 27.68 ? 236 GLN   A OE1 1 
ATOM   1625 N NE2 . GLN   A 1 257 ? 0.280   -14.428 -0.720  1.00 29.24 ? 236 GLN   A NE2 1 
ATOM   1626 N N   . ILE   A 1 258 ? 4.694   -10.052 2.328   1.00 22.32 ? 237 ILE   A N   1 
ATOM   1627 C CA  . ILE   A 1 258 ? 5.047   -8.981  3.292   1.00 22.65 ? 237 ILE   A CA  1 
ATOM   1628 C C   . ILE   A 1 258 ? 5.734   -7.845  2.548   1.00 24.64 ? 237 ILE   A C   1 
ATOM   1629 O O   . ILE   A 1 258 ? 5.357   -6.679  2.679   1.00 22.23 ? 237 ILE   A O   1 
ATOM   1630 C CB  . ILE   A 1 258 ? 5.880   -9.490  4.484   1.00 23.39 ? 237 ILE   A CB  1 
ATOM   1631 C CG1 . ILE   A 1 258 ? 5.210   -10.674 5.226   1.00 24.42 ? 237 ILE   A CG1 1 
ATOM   1632 C CG2 . ILE   A 1 258 ? 6.284   -8.358  5.450   1.00 22.00 ? 237 ILE   A CG2 1 
ATOM   1633 C CD1 . ILE   A 1 258 ? 3.752   -10.405 5.599   1.00 24.17 ? 237 ILE   A CD1 1 
ATOM   1634 N N   . ALA   A 1 259 ? 6.705   -8.182  1.676   1.00 22.31 ? 238 ALA   A N   1 
ATOM   1635 C CA  . ALA   A 1 259 ? 7.404   -7.161  0.895   1.00 25.88 ? 238 ALA   A CA  1 
ATOM   1636 C C   . ALA   A 1 259 ? 6.448   -6.362  0.008   1.00 26.47 ? 238 ALA   A C   1 
ATOM   1637 O O   . ALA   A 1 259 ? 6.642   -5.158  -0.211  1.00 27.13 ? 238 ALA   A O   1 
ATOM   1638 C CB  . ALA   A 1 259 ? 8.494   -7.813  0.029   1.00 25.58 ? 238 ALA   A CB  1 
ATOM   1639 N N   . ASP   A 1 260 ? 5.434   -7.024  -0.570  1.00 26.89 ? 239 ASP   A N   1 
ATOM   1640 C CA  . ASP   A 1 260 ? 4.480   -6.329  -1.435  1.00 25.19 ? 239 ASP   A CA  1 
ATOM   1641 C C   . ASP   A 1 260 ? 3.844   -5.135  -0.721  1.00 25.70 ? 239 ASP   A C   1 
ATOM   1642 O O   . ASP   A 1 260 ? 3.619   -4.074  -1.312  1.00 24.42 ? 239 ASP   A O   1 
ATOM   1643 C CB  . ASP   A 1 260 ? 3.355   -7.256  -1.890  1.00 26.80 ? 239 ASP   A CB  1 
ATOM   1644 C CG  . ASP   A 1 260 ? 3.668   -8.158  -3.083  1.00 32.24 ? 239 ASP   A CG  1 
ATOM   1645 O OD1 . ASP   A 1 260 ? 4.528   -7.777  -3.883  1.00 32.79 ? 239 ASP   A OD1 1 
ATOM   1646 O OD2 . ASP   A 1 260 ? 3.068   -9.255  -3.190  1.00 32.20 ? 239 ASP   A OD2 1 
ATOM   1647 N N   . ALA   A 1 261 ? 3.580   -5.273  0.584   1.00 24.16 ? 240 ALA   A N   1 
ATOM   1648 C CA  . ALA   A 1 261 ? 2.889   -4.200  1.288   1.00 23.26 ? 240 ALA   A CA  1 
ATOM   1649 C C   . ALA   A 1 261 ? 3.887   -3.084  1.596   1.00 24.80 ? 240 ALA   A C   1 
ATOM   1650 O O   . ALA   A 1 261 ? 3.549   -1.899  1.592   1.00 22.65 ? 240 ALA   A O   1 
ATOM   1651 C CB  . ALA   A 1 261 ? 2.292   -4.785  2.556   1.00 26.43 ? 240 ALA   A CB  1 
ATOM   1652 N N   . VAL   A 1 262 ? 5.147   -3.478  1.802   1.00 23.91 ? 241 VAL   A N   1 
ATOM   1653 C CA  . VAL   A 1 262 ? 6.192   -2.497  2.027   1.00 25.74 ? 241 VAL   A CA  1 
ATOM   1654 C C   . VAL   A 1 262 ? 6.357   -1.652  0.766   1.00 25.47 ? 241 VAL   A C   1 
ATOM   1655 O O   . VAL   A 1 262 ? 6.451   -0.416  0.824   1.00 24.05 ? 241 VAL   A O   1 
ATOM   1656 C CB  . VAL   A 1 262 ? 7.543   -3.104  2.475   1.00 26.92 ? 241 VAL   A CB  1 
ATOM   1657 C CG1 . VAL   A 1 262 ? 8.595   -1.995  2.592   1.00 25.20 ? 241 VAL   A CG1 1 
ATOM   1658 C CG2 . VAL   A 1 262 ? 7.421   -3.862  3.793   1.00 24.31 ? 241 VAL   A CG2 1 
ATOM   1659 N N   . ILE   A 1 263 ? 6.463   -2.340  -0.375  1.00 25.49 ? 242 ILE   A N   1 
ATOM   1660 C CA  . ILE   A 1 263 ? 6.596   -1.702  -1.676  1.00 27.14 ? 242 ILE   A CA  1 
ATOM   1661 C C   . ILE   A 1 263 ? 5.447   -0.720  -1.924  1.00 25.88 ? 242 ILE   A C   1 
ATOM   1662 O O   . ILE   A 1 263 ? 5.649   0.395   -2.422  1.00 25.59 ? 242 ILE   A O   1 
ATOM   1663 C CB  . ILE   A 1 263 ? 6.687   -2.781  -2.769  1.00 31.81 ? 242 ILE   A CB  1 
ATOM   1664 C CG1 . ILE   A 1 263 ? 8.066   -3.473  -2.727  1.00 35.70 ? 242 ILE   A CG1 1 
ATOM   1665 C CG2 . ILE   A 1 263 ? 6.377   -2.236  -4.164  1.00 33.44 ? 242 ILE   A CG2 1 
ATOM   1666 C CD1 . ILE   A 1 263 ? 9.217   -2.543  -2.414  1.00 38.33 ? 242 ILE   A CD1 1 
ATOM   1667 N N   . PHE   A 1 264 ? 4.232   -1.142  -1.575  1.00 25.97 ? 243 PHE   A N   1 
ATOM   1668 C CA  . PHE   A 1 264 ? 3.089   -0.244  -1.702  1.00 24.07 ? 243 PHE   A CA  1 
ATOM   1669 C C   . PHE   A 1 264 ? 3.291   1.036   -0.892  1.00 23.81 ? 243 PHE   A C   1 
ATOM   1670 O O   . PHE   A 1 264 ? 3.131   2.128   -1.424  1.00 24.54 ? 243 PHE   A O   1 
ATOM   1671 C CB  . PHE   A 1 264 ? 1.779   -0.971  -1.384  1.00 24.50 ? 243 PHE   A CB  1 
ATOM   1672 C CG  . PHE   A 1 264 ? 0.641   0.033   -1.227  1.00 25.01 ? 243 PHE   A CG  1 
ATOM   1673 C CD1 . PHE   A 1 264 ? 0.128   0.711   -2.332  1.00 27.15 ? 243 PHE   A CD1 1 
ATOM   1674 C CD2 . PHE   A 1 264 ? 0.114   0.305   0.044   1.00 26.82 ? 243 PHE   A CD2 1 
ATOM   1675 C CE1 . PHE   A 1 264 ? -0.915  1.622   -2.183  1.00 28.50 ? 243 PHE   A CE1 1 
ATOM   1676 C CE2 . PHE   A 1 264 ? -0.936  1.211   0.185   1.00 25.66 ? 243 PHE   A CE2 1 
ATOM   1677 C CZ  . PHE   A 1 264 ? -1.429  1.880   -0.922  1.00 26.85 ? 243 PHE   A CZ  1 
ATOM   1678 N N   . LEU   A 1 265 ? 3.610   0.912   0.400   1.00 23.35 ? 244 LEU   A N   1 
ATOM   1679 C CA  . LEU   A 1 265 ? 3.768   2.061   1.287   1.00 21.77 ? 244 LEU   A CA  1 
ATOM   1680 C C   . LEU   A 1 265 ? 4.879   3.015   0.833   1.00 28.42 ? 244 LEU   A C   1 
ATOM   1681 O O   . LEU   A 1 265 ? 4.787   4.229   1.065   1.00 25.29 ? 244 LEU   A O   1 
ATOM   1682 C CB  . LEU   A 1 265 ? 4.001   1.589   2.717   1.00 24.35 ? 244 LEU   A CB  1 
ATOM   1683 C CG  . LEU   A 1 265 ? 2.748   1.007   3.394   1.00 22.42 ? 244 LEU   A CG  1 
ATOM   1684 C CD1 . LEU   A 1 265 ? 3.094   0.340   4.702   1.00 22.09 ? 244 LEU   A CD1 1 
ATOM   1685 C CD2 . LEU   A 1 265 ? 1.881   2.221   3.610   1.00 20.97 ? 244 LEU   A CD2 1 
ATOM   1686 N N   . VAL   A 1 266 ? 5.912   2.487   0.171   1.00 25.38 ? 245 VAL   A N   1 
ATOM   1687 C CA  . VAL   A 1 266 ? 6.956   3.426   -0.231  1.00 27.59 ? 245 VAL   A CA  1 
ATOM   1688 C C   . VAL   A 1 266 ? 6.620   4.085   -1.566  1.00 28.92 ? 245 VAL   A C   1 
ATOM   1689 O O   . VAL   A 1 266 ? 7.211   5.122   -1.906  1.00 30.72 ? 245 VAL   A O   1 
ATOM   1690 C CB  . VAL   A 1 266 ? 8.379   2.830   -0.228  1.00 29.81 ? 245 VAL   A CB  1 
ATOM   1691 C CG1 . VAL   A 1 266 ? 8.687   2.059   1.065   1.00 29.63 ? 245 VAL   A CG1 1 
ATOM   1692 C CG2 . VAL   A 1 266 ? 8.632   1.954   -1.440  1.00 30.40 ? 245 VAL   A CG2 1 
ATOM   1693 N N   . SER   A 1 267 ? 5.720   3.461   -2.343  1.00 29.06 ? 246 SER   A N   1 
ATOM   1694 C CA  . SER   A 1 267 ? 5.384   3.874   -3.702  1.00 28.06 ? 246 SER   A CA  1 
ATOM   1695 C C   . SER   A 1 267 ? 4.611   5.187   -3.728  1.00 30.21 ? 246 SER   A C   1 
ATOM   1696 O O   . SER   A 1 267 ? 4.084   5.641   -2.705  1.00 31.01 ? 246 SER   A O   1 
ATOM   1697 C CB  . SER   A 1 267 ? 4.583   2.815   -4.423  1.00 29.52 ? 246 SER   A CB  1 
ATOM   1698 O OG  . SER   A 1 267 ? 3.222   2.871   -4.022  1.00 29.72 ? 246 SER   A OG  1 
ATOM   1699 N N   . GLY   A 1 268 ? 4.561   5.804   -4.914  1.00 30.92 ? 247 GLY   A N   1 
ATOM   1700 C CA  . GLY   A 1 268 ? 3.734   6.988   -5.119  1.00 32.03 ? 247 GLY   A CA  1 
ATOM   1701 C C   . GLY   A 1 268 ? 2.228   6.684   -5.030  1.00 32.12 ? 247 GLY   A C   1 
ATOM   1702 O O   . GLY   A 1 268 ? 1.425   7.608   -4.979  1.00 36.89 ? 247 GLY   A O   1 
ATOM   1703 N N   . SER   A 1 269 ? 1.841   5.400   -4.955  1.00 27.61 ? 248 SER   A N   1 
ATOM   1704 C CA  . SER   A 1 269 ? 0.444   5.030   -4.738  1.00 29.15 ? 248 SER   A CA  1 
ATOM   1705 C C   . SER   A 1 269 ? 0.017   5.232   -3.288  1.00 27.90 ? 248 SER   A C   1 
ATOM   1706 O O   . SER   A 1 269 ? -1.185  5.074   -3.008  1.00 28.55 ? 248 SER   A O   1 
ATOM   1707 C CB  . SER   A 1 269 ? 0.137   3.589   -5.188  1.00 28.93 ? 248 SER   A CB  1 
ATOM   1708 O OG  . SER   A 1 269 ? 0.235   3.514   -6.608  1.00 36.28 ? 248 SER   A OG  1 
ATOM   1709 N N   . ALA   A 1 270 ? 0.967   5.632   -2.410  1.00 23.12 ? 249 ALA   A N   1 
ATOM   1710 C CA  . ALA   A 1 270 ? 0.676   5.811   -0.992  1.00 22.54 ? 249 ALA   A CA  1 
ATOM   1711 C C   . ALA   A 1 270 ? 1.097   7.200   -0.539  1.00 23.79 ? 249 ALA   A C   1 
ATOM   1712 O O   . ALA   A 1 270 ? 1.397   7.405   0.648   1.00 24.78 ? 249 ALA   A O   1 
ATOM   1713 C CB  . ALA   A 1 270 ? 1.394   4.751   -0.181  1.00 23.18 ? 249 ALA   A CB  1 
ATOM   1714 N N   . GLN   A 1 271 ? 1.142   8.154   -1.494  1.00 25.54 ? 250 GLN   A N   1 
ATOM   1715 C CA  . GLN   A 1 271 ? 1.669   9.476   -1.181  1.00 27.72 ? 250 GLN   A CA  1 
ATOM   1716 C C   . GLN   A 1 271 ? 0.904   10.200  -0.074  1.00 29.21 ? 250 GLN   A C   1 
ATOM   1717 O O   . GLN   A 1 271 ? 1.427   11.188  0.452   1.00 26.25 ? 250 GLN   A O   1 
ATOM   1718 C CB  . GLN   A 1 271 ? 1.639   10.421  -2.390  1.00 32.69 ? 250 GLN   A CB  1 
ATOM   1719 C CG  . GLN   A 1 271 ? 0.301   10.466  -3.122  0.70 43.59 ? 250 GLN   A CG  1 
ATOM   1720 C CD  . GLN   A 1 271 ? 0.337   11.223  -4.435  0.70 44.40 ? 250 GLN   A CD  1 
ATOM   1721 O OE1 . GLN   A 1 271 ? -0.527  11.038  -5.305  0.70 38.77 ? 250 GLN   A OE1 1 
ATOM   1722 N NE2 . GLN   A 1 271 ? 1.362   12.053  -4.592  0.70 41.48 ? 250 GLN   A NE2 1 
ATOM   1723 N N   . TYR   A 1 272 ? -0.358  9.822   0.210   1.00 25.69 ? 251 TYR   A N   1 
ATOM   1724 C CA  . TYR   A 1 272 ? -1.085  10.534  1.265   1.00 24.22 ? 251 TYR   A CA  1 
ATOM   1725 C C   . TYR   A 1 272 ? -1.158  9.686   2.536   1.00 23.24 ? 251 TYR   A C   1 
ATOM   1726 O O   . TYR   A 1 272 ? -1.762  10.083  3.522   1.00 22.66 ? 251 TYR   A O   1 
ATOM   1727 C CB  . TYR   A 1 272 ? -2.492  10.923  0.779   1.00 25.11 ? 251 TYR   A CB  1 
ATOM   1728 C CG  . TYR   A 1 272 ? -3.263  11.951  1.596   1.00 26.15 ? 251 TYR   A CG  1 
ATOM   1729 C CD1 . TYR   A 1 272 ? -2.953  13.304  1.487   1.00 24.38 ? 251 TYR   A CD1 1 
ATOM   1730 C CD2 . TYR   A 1 272 ? -4.326  11.600  2.431   1.00 23.03 ? 251 TYR   A CD2 1 
ATOM   1731 C CE1 . TYR   A 1 272 ? -3.628  14.255  2.218   1.00 24.68 ? 251 TYR   A CE1 1 
ATOM   1732 C CE2 . TYR   A 1 272 ? -5.033  12.562  3.148   1.00 22.45 ? 251 TYR   A CE2 1 
ATOM   1733 C CZ  . TYR   A 1 272 ? -4.710  13.899  3.010   1.00 22.57 ? 251 TYR   A CZ  1 
ATOM   1734 O OH  . TYR   A 1 272 ? -5.412  14.875  3.648   1.00 22.41 ? 251 TYR   A OH  1 
ATOM   1735 N N   . ILE   A 1 273 ? -0.534  8.511   2.511   1.00 19.98 ? 252 ILE   A N   1 
ATOM   1736 C CA  . ILE   A 1 273 ? -0.641  7.624   3.669   1.00 21.61 ? 252 ILE   A CA  1 
ATOM   1737 C C   . ILE   A 1 273 ? 0.529   7.887   4.620   1.00 23.54 ? 252 ILE   A C   1 
ATOM   1738 O O   . ILE   A 1 273 ? 1.693   7.760   4.222   1.00 23.28 ? 252 ILE   A O   1 
ATOM   1739 C CB  . ILE   A 1 273 ? -0.665  6.161   3.179   1.00 22.05 ? 252 ILE   A CB  1 
ATOM   1740 C CG1 . ILE   A 1 273 ? -1.780  5.923   2.106   1.00 23.41 ? 252 ILE   A CG1 1 
ATOM   1741 C CG2 . ILE   A 1 273 ? -0.767  5.205   4.378   1.00 21.67 ? 252 ILE   A CG2 1 
ATOM   1742 C CD1 . ILE   A 1 273 ? -1.875  4.471   1.603   1.00 21.06 ? 252 ILE   A CD1 1 
ATOM   1743 N N   . THR   A 1 274 ? 0.224   8.229   5.878   1.00 21.09 ? 253 THR   A N   1 
ATOM   1744 C CA  . THR   A 1 274 ? 1.253   8.311   6.924   1.00 23.36 ? 253 THR   A CA  1 
ATOM   1745 C C   . THR   A 1 274 ? 0.601   7.971   8.256   1.00 22.55 ? 253 THR   A C   1 
ATOM   1746 O O   . THR   A 1 274 ? -0.557  8.288   8.514   1.00 22.65 ? 253 THR   A O   1 
ATOM   1747 C CB  . THR   A 1 274 ? 1.992   9.664   6.956   1.00 24.54 ? 253 THR   A CB  1 
ATOM   1748 O OG1 . THR   A 1 274 ? 3.181   9.458   7.718   1.00 24.63 ? 253 THR   A OG1 1 
ATOM   1749 C CG2 . THR   A 1 274 ? 1.141   10.786  7.540   1.00 22.19 ? 253 THR   A CG2 1 
ATOM   1750 N N   . GLY   A 1 275 ? 1.368   7.265   9.085   1.00 24.90 ? 254 GLY   A N   1 
ATOM   1751 C CA  . GLY   A 1 275 ? 0.821   6.850   10.356  1.00 22.45 ? 254 GLY   A CA  1 
ATOM   1752 C C   . GLY   A 1 275 ? -0.085  5.617   10.271  1.00 24.35 ? 254 GLY   A C   1 
ATOM   1753 O O   . GLY   A 1 275 ? -0.757  5.348   11.264  1.00 24.86 ? 254 GLY   A O   1 
ATOM   1754 N N   . SER   A 1 276 ? -0.043  4.850   9.171   1.00 23.79 ? 255 SER   A N   1 
ATOM   1755 C CA  . SER   A 1 276 ? -0.974  3.734   8.960   1.00 20.95 ? 255 SER   A CA  1 
ATOM   1756 C C   . SER   A 1 276 ? -0.188  2.454   9.156   1.00 23.40 ? 255 SER   A C   1 
ATOM   1757 O O   . SER   A 1 276 ? 0.947   2.411   8.734   1.00 23.95 ? 255 SER   A O   1 
ATOM   1758 C CB  . SER   A 1 276 ? -1.552  3.727   7.579   1.00 23.34 ? 255 SER   A CB  1 
ATOM   1759 O OG  . SER   A 1 276 ? -2.305  4.928   7.466   1.00 28.63 ? 255 SER   A OG  1 
ATOM   1760 N N   . ILE   A 1 277 ? -0.808  1.449   9.772   1.00 20.57 ? 256 ILE   A N   1 
ATOM   1761 C CA  . ILE   A 1 277 ? -0.133  0.160   9.861   1.00 22.47 ? 256 ILE   A CA  1 
ATOM   1762 C C   . ILE   A 1 277 ? -1.032  -0.850  9.176   1.00 25.06 ? 256 ILE   A C   1 
ATOM   1763 O O   . ILE   A 1 277 ? -2.182  -1.027  9.570   1.00 25.45 ? 256 ILE   A O   1 
ATOM   1764 C CB  . ILE   A 1 277 ? 0.082   -0.203  11.332  1.00 24.22 ? 256 ILE   A CB  1 
ATOM   1765 C CG1 . ILE   A 1 277 ? 1.039   0.809   12.009  1.00 24.66 ? 256 ILE   A CG1 1 
ATOM   1766 C CG2 . ILE   A 1 277 ? 0.569   -1.657  11.467  1.00 26.06 ? 256 ILE   A CG2 1 
ATOM   1767 C CD1 . ILE   A 1 277 ? 0.970   0.736   13.530  1.00 32.17 ? 256 ILE   A CD1 1 
ATOM   1768 N N   . ILE   A 1 278 ? -0.499  -1.446  8.116   1.00 21.03 ? 257 ILE   A N   1 
ATOM   1769 C CA  . ILE   A 1 278 ? -1.297  -2.352  7.309   1.00 20.99 ? 257 ILE   A CA  1 
ATOM   1770 C C   . ILE   A 1 278 ? -1.026  -3.757  7.826   1.00 22.30 ? 257 ILE   A C   1 
ATOM   1771 O O   . ILE   A 1 278 ? 0.126   -4.226  7.746   1.00 22.11 ? 257 ILE   A O   1 
ATOM   1772 C CB  . ILE   A 1 278 ? -0.854  -2.238  5.841   1.00 22.82 ? 257 ILE   A CB  1 
ATOM   1773 C CG1 . ILE   A 1 278 ? -1.078  -0.834  5.251   1.00 25.43 ? 257 ILE   A CG1 1 
ATOM   1774 C CG2 . ILE   A 1 278 ? -1.535  -3.297  4.972   1.00 24.51 ? 257 ILE   A CG2 1 
ATOM   1775 C CD1 . ILE   A 1 278 ? -0.577  -0.737  3.824   1.00 26.77 ? 257 ILE   A CD1 1 
ATOM   1776 N N   . LYS   A 1 279 ? -2.095  -4.432  8.283   1.00 22.36 ? 258 LYS   A N   1 
ATOM   1777 C CA  . LYS   A 1 279 ? -1.965  -5.820  8.684   1.00 22.75 ? 258 LYS   A CA  1 
ATOM   1778 C C   . LYS   A 1 279 ? -1.863  -6.641  7.414   1.00 20.26 ? 258 LYS   A C   1 
ATOM   1779 O O   . LYS   A 1 279 ? -2.618  -6.427  6.464   1.00 22.89 ? 258 LYS   A O   1 
ATOM   1780 C CB  . LYS   A 1 279 ? -3.138  -6.438  9.468   1.00 24.48 ? 258 LYS   A CB  1 
ATOM   1781 C CG  . LYS   A 1 279 ? -3.470  -5.819  10.793  1.00 28.47 ? 258 LYS   A CG  1 
ATOM   1782 C CD  . LYS   A 1 279 ? -4.681  -6.524  11.424  1.00 25.61 ? 258 LYS   A CD  1 
ATOM   1783 C CE  . LYS   A 1 279 ? -6.017  -6.058  10.881  1.00 28.79 ? 258 LYS   A CE  1 
ATOM   1784 N NZ  . LYS   A 1 279 ? -7.170  -6.928  11.220  1.00 24.39 ? 258 LYS   A NZ  1 
ATOM   1785 N N   . VAL   A 1 280 ? -0.972  -7.644  7.437   1.00 22.58 ? 259 VAL   A N   1 
ATOM   1786 C CA  . VAL   A 1 280 ? -0.883  -8.589  6.323   1.00 21.61 ? 259 VAL   A CA  1 
ATOM   1787 C C   . VAL   A 1 280 ? -0.894  -9.958  6.970   1.00 20.53 ? 259 VAL   A C   1 
ATOM   1788 O O   . VAL   A 1 280 ? 0.171   -10.532 7.207   1.00 23.32 ? 259 VAL   A O   1 
ATOM   1789 C CB  . VAL   A 1 280 ? 0.396   -8.379  5.475   1.00 21.82 ? 259 VAL   A CB  1 
ATOM   1790 C CG1 . VAL   A 1 280 ? 0.478   -9.330  4.269   1.00 20.81 ? 259 VAL   A CG1 1 
ATOM   1791 C CG2 . VAL   A 1 280 ? 0.478   -6.926  5.004   1.00 23.45 ? 259 VAL   A CG2 1 
ATOM   1792 N N   . ASP   A 1 281 ? -2.097  -10.399 7.364   1.00 20.70 ? 260 ASP   A N   1 
ATOM   1793 C CA  . ASP   A 1 281 ? -2.172  -11.498 8.315   1.00 21.15 ? 260 ASP   A CA  1 
ATOM   1794 C C   . ASP   A 1 281 ? -3.198  -12.575 7.935   1.00 20.09 ? 260 ASP   A C   1 
ATOM   1795 O O   . ASP   A 1 281 ? -3.432  -13.481 8.735   1.00 22.09 ? 260 ASP   A O   1 
ATOM   1796 C CB  . ASP   A 1 281 ? -2.437  -10.962 9.706   1.00 23.58 ? 260 ASP   A CB  1 
ATOM   1797 C CG  . ASP   A 1 281 ? -3.879  -10.549 9.998   1.00 24.48 ? 260 ASP   A CG  1 
ATOM   1798 O OD1 . ASP   A 1 281 ? -4.686  -10.379 9.050   1.00 23.34 ? 260 ASP   A OD1 1 
ATOM   1799 O OD2 . ASP   A 1 281 ? -4.193  -10.454 11.189  1.00 22.65 ? 260 ASP   A OD2 1 
ATOM   1800 N N   . GLY   A 1 282 ? -3.779  -12.473 6.739   1.00 21.43 ? 261 GLY   A N   1 
ATOM   1801 C CA  . GLY   A 1 282 ? -4.737  -13.465 6.240   1.00 21.76 ? 261 GLY   A CA  1 
ATOM   1802 C C   . GLY   A 1 282 ? -5.901  -13.671 7.205   1.00 21.64 ? 261 GLY   A C   1 
ATOM   1803 O O   . GLY   A 1 282 ? -6.515  -14.733 7.238   1.00 21.01 ? 261 GLY   A O   1 
ATOM   1804 N N   . GLY   A 1 283 ? -6.216  -12.631 7.990   1.00 20.00 ? 262 GLY   A N   1 
ATOM   1805 C CA  . GLY   A 1 283 ? -7.298  -12.652 8.975   1.00 20.36 ? 262 GLY   A CA  1 
ATOM   1806 C C   . GLY   A 1 283 ? -6.975  -13.258 10.344  1.00 22.07 ? 262 GLY   A C   1 
ATOM   1807 O O   . GLY   A 1 283 ? -7.892  -13.380 11.163  1.00 23.02 ? 262 GLY   A O   1 
ATOM   1808 N N   . LEU   A 1 284 ? -5.716  -13.656 10.601  1.00 20.25 ? 263 LEU   A N   1 
ATOM   1809 C CA  . LEU   A 1 284 ? -5.344  -14.304 11.860  1.00 20.10 ? 263 LEU   A CA  1 
ATOM   1810 C C   . LEU   A 1 284 ? -5.821  -13.547 13.102  1.00 22.99 ? 263 LEU   A C   1 
ATOM   1811 O O   . LEU   A 1 284 ? -6.358  -14.164 14.023  1.00 23.38 ? 263 LEU   A O   1 
ATOM   1812 C CB  . LEU   A 1 284 ? -3.835  -14.582 11.935  1.00 20.28 ? 263 LEU   A CB  1 
ATOM   1813 C CG  . LEU   A 1 284 ? -3.369  -15.286 13.225  1.00 22.58 ? 263 LEU   A CG  1 
ATOM   1814 C CD1 . LEU   A 1 284 ? -3.921  -16.717 13.264  1.00 25.04 ? 263 LEU   A CD1 1 
ATOM   1815 C CD2 . LEU   A 1 284 ? -1.853  -15.307 13.241  1.00 26.84 ? 263 LEU   A CD2 1 
ATOM   1816 N N   . SER   A 1 285 ? -5.621  -12.226 13.129  1.00 21.09 ? 264 SER   A N   1 
ATOM   1817 C CA  . SER   A 1 285 ? -5.933  -11.441 14.311  1.00 23.30 ? 264 SER   A CA  1 
ATOM   1818 C C   . SER   A 1 285 ? -7.443  -11.353 14.576  1.00 23.05 ? 264 SER   A C   1 
ATOM   1819 O O   . SER   A 1 285 ? -7.835  -10.852 15.618  1.00 24.14 ? 264 SER   A O   1 
ATOM   1820 C CB  . SER   A 1 285 ? -5.320  -10.077 14.217  1.00 23.67 ? 264 SER   A CB  1 
ATOM   1821 O OG  . SER   A 1 285 ? -5.827  -9.407  13.080  1.00 26.13 ? 264 SER   A OG  1 
ATOM   1822 N N   . LEU   A 1 286 ? -8.296  -11.807 13.650  1.00 21.45 ? 265 LEU   A N   1 
ATOM   1823 C CA  . LEU   A 1 286 ? -9.748  -11.733 13.792  1.00 20.66 ? 265 LEU   A CA  1 
ATOM   1824 C C   . LEU   A 1 286 ? -10.285 -13.008 14.453  1.00 20.99 ? 265 LEU   A C   1 
ATOM   1825 O O   . LEU   A 1 286 ? -11.482 -13.087 14.768  1.00 23.57 ? 265 LEU   A O   1 
ATOM   1826 C CB  . LEU   A 1 286 ? -10.359 -11.580 12.394  1.00 18.82 ? 265 LEU   A CB  1 
ATOM   1827 C CG  . LEU   A 1 286 ? -9.944  -10.348 11.595  1.00 25.16 ? 265 LEU   A CG  1 
ATOM   1828 C CD1 . LEU   A 1 286 ? -10.714 -10.452 10.270  1.00 25.37 ? 265 LEU   A CD1 1 
ATOM   1829 C CD2 . LEU   A 1 286 ? -10.284 -9.145  12.415  1.00 27.78 ? 265 LEU   A CD2 1 
ATOM   1830 N N   . VAL   A 1 287 ? -9.397  -14.004 14.636  1.00 22.87 ? 266 VAL   A N   1 
ATOM   1831 C CA  . VAL   A 1 287 ? -9.834  -15.325 15.084  1.00 24.22 ? 266 VAL   A CA  1 
ATOM   1832 C C   . VAL   A 1 287 ? -9.833  -15.360 16.618  1.00 25.22 ? 266 VAL   A C   1 
ATOM   1833 O O   . VAL   A 1 287 ? -8.772  -15.231 17.219  1.00 27.88 ? 266 VAL   A O   1 
ATOM   1834 C CB  . VAL   A 1 287 ? -8.950  -16.478 14.571  1.00 23.22 ? 266 VAL   A CB  1 
ATOM   1835 C CG1 . VAL   A 1 287 ? -9.515  -17.806 15.072  1.00 26.68 ? 266 VAL   A CG1 1 
ATOM   1836 C CG2 . VAL   A 1 287 ? -8.879  -16.516 13.039  1.00 25.18 ? 266 VAL   A CG2 1 
ATOM   1837 N N   . HIS   A 1 288 ? -10.997 -15.621 17.233  1.00 25.04 ? 267 HIS   A N   1 
ATOM   1838 C CA  . HIS   A 1 288 ? -11.064 -15.771 18.697  1.00 28.53 ? 267 HIS   A CA  1 
ATOM   1839 C C   . HIS   A 1 288 ? -10.386 -17.056 19.190  1.00 29.86 ? 267 HIS   A C   1 
ATOM   1840 O O   . HIS   A 1 288 ? -10.128 -17.974 18.416  1.00 27.64 ? 267 HIS   A O   1 
ATOM   1841 C CB  . HIS   A 1 288 ? -12.510 -15.718 19.215  1.00 30.62 ? 267 HIS   A CB  1 
ATOM   1842 C CG  . HIS   A 1 288 ? -13.383 -16.806 18.724  1.00 28.85 ? 267 HIS   A CG  1 
ATOM   1843 N ND1 . HIS   A 1 288 ? -13.208 -18.127 19.122  1.00 30.78 ? 267 HIS   A ND1 1 
ATOM   1844 C CD2 . HIS   A 1 288 ? -14.395 -16.799 17.852  1.00 30.16 ? 267 HIS   A CD2 1 
ATOM   1845 C CE1 . HIS   A 1 288 ? -14.120 -18.876 18.522  1.00 30.93 ? 267 HIS   A CE1 1 
ATOM   1846 N NE2 . HIS   A 1 288 ? -14.866 -18.100 17.753  1.00 33.29 ? 267 HIS   A NE2 1 
ATOM   1847 N N   . ALA   A 1 289 ? -10.150 -17.141 20.516  1.00 28.46 ? 268 ALA   A N   1 
ATOM   1848 C CA  . ALA   A 1 289 ? -9.465  -18.283 21.114  1.00 31.23 ? 268 ALA   A CA  1 
ATOM   1849 C C   . ALA   A 1 289 ? -10.288 -19.562 20.929  1.00 33.78 ? 268 ALA   A C   1 
ATOM   1850 O O   . ALA   A 1 289 ? -9.697  -20.680 21.064  1.00 36.81 ? 268 ALA   A O   1 
ATOM   1851 C CB  . ALA   A 1 289 ? -9.266  -18.008 22.594  1.00 37.10 ? 268 ALA   A CB  1 
ATOM   1852 O OXT . ALA   A 1 289 ? -11.504 -19.415 20.750  1.00 32.63 ? 268 ALA   A OXT 1 
ATOM   1853 N N   . GLU   B 1 23  ? -11.620 -14.008 -19.245 0.70 51.70 ? 2   GLU   B N   1 
ATOM   1854 C CA  . GLU   B 1 23  ? -11.709 -12.657 -19.848 0.70 51.68 ? 2   GLU   B CA  1 
ATOM   1855 C C   . GLU   B 1 23  ? -11.375 -11.604 -18.789 0.70 47.23 ? 2   GLU   B C   1 
ATOM   1856 O O   . GLU   B 1 23  ? -10.637 -11.864 -17.841 0.70 49.33 ? 2   GLU   B O   1 
ATOM   1857 C CB  . GLU   B 1 23  ? -13.120 -12.507 -20.411 0.70 54.97 ? 2   GLU   B CB  1 
ATOM   1858 C CG  . GLU   B 1 23  ? -13.149 -11.743 -21.731 0.70 58.92 ? 2   GLU   B CG  1 
ATOM   1859 C CD  . GLU   B 1 23  ? -14.574 -11.514 -22.185 0.70 60.33 ? 2   GLU   B CD  1 
ATOM   1860 O OE1 . GLU   B 1 23  ? -15.387 -12.454 -22.061 0.70 64.55 ? 2   GLU   B OE1 1 
ATOM   1861 O OE2 . GLU   B 1 23  ? -14.867 -10.399 -22.660 0.70 59.51 ? 2   GLU   B OE2 1 
ATOM   1862 N N   . ALA   B 1 24  ? -11.912 -10.400 -18.981 1.00 43.68 ? 3   ALA   B N   1 
ATOM   1863 C CA  . ALA   B 1 24  ? -11.646 -9.257  -18.118 1.00 40.93 ? 3   ALA   B CA  1 
ATOM   1864 C C   . ALA   B 1 24  ? -12.465 -9.390  -16.825 1.00 38.61 ? 3   ALA   B C   1 
ATOM   1865 O O   . ALA   B 1 24  ? -13.637 -9.751  -16.871 1.00 31.77 ? 3   ALA   B O   1 
ATOM   1866 C CB  . ALA   B 1 24  ? -12.016 -8.003  -18.881 1.00 35.92 ? 3   ALA   B CB  1 
ATOM   1867 N N   . PRO   B 1 25  ? -11.913 -9.073  -15.624 1.00 35.14 ? 4   PRO   B N   1 
ATOM   1868 C CA  . PRO   B 1 25  ? -12.722 -9.116  -14.391 1.00 33.28 ? 4   PRO   B CA  1 
ATOM   1869 C C   . PRO   B 1 25  ? -13.777 -8.009  -14.388 1.00 31.28 ? 4   PRO   B C   1 
ATOM   1870 O O   . PRO   B 1 25  ? -13.678 -7.072  -15.182 1.00 34.15 ? 4   PRO   B O   1 
ATOM   1871 C CB  . PRO   B 1 25  ? -11.656 -8.981  -13.286 1.00 33.95 ? 4   PRO   B CB  1 
ATOM   1872 C CG  . PRO   B 1 25  ? -10.531 -8.158  -13.920 1.00 32.93 ? 4   PRO   B CG  1 
ATOM   1873 C CD  . PRO   B 1 25  ? -10.537 -8.587  -15.402 1.00 33.79 ? 4   PRO   B CD  1 
ATOM   1874 N N   . ALA   B 1 26  ? -14.798 -8.128  -13.520 1.00 27.68 ? 5   ALA   B N   1 
ATOM   1875 C CA  . ALA   B 1 26  ? -15.821 -7.095  -13.350 1.00 31.26 ? 5   ALA   B CA  1 
ATOM   1876 C C   . ALA   B 1 26  ? -15.963 -6.666  -11.880 1.00 30.08 ? 5   ALA   B C   1 
ATOM   1877 O O   . ALA   B 1 26  ? -15.832 -7.489  -10.972 1.00 29.57 ? 5   ALA   B O   1 
ATOM   1878 C CB  . ALA   B 1 26  ? -17.161 -7.565  -13.861 1.00 28.98 ? 5   ALA   B CB  1 
ATOM   1879 N N   . ALA   B 1 27  ? -16.256 -5.374  -11.691 1.00 27.50 ? 6   ALA   B N   1 
ATOM   1880 C CA  . ALA   B 1 27  ? -16.399 -4.759  -10.376 1.00 28.15 ? 6   ALA   B CA  1 
ATOM   1881 C C   . ALA   B 1 27  ? -17.696 -3.971  -10.323 1.00 27.56 ? 6   ALA   B C   1 
ATOM   1882 O O   . ALA   B 1 27  ? -18.099 -3.326  -11.298 1.00 27.37 ? 6   ALA   B O   1 
ATOM   1883 C CB  . ALA   B 1 27  ? -15.240 -3.836  -10.110 1.00 23.78 ? 6   ALA   B CB  1 
ATOM   1884 N N   . VAL   B 1 28  ? -18.357 -4.023  -9.159  1.00 24.38 ? 7   VAL   B N   1 
ATOM   1885 C CA  . VAL   B 1 28  ? -19.446 -3.106  -8.862  1.00 21.66 ? 7   VAL   B CA  1 
ATOM   1886 C C   . VAL   B 1 28  ? -18.888 -2.018  -7.939  1.00 23.32 ? 7   VAL   B C   1 
ATOM   1887 O O   . VAL   B 1 28  ? -18.241 -2.341  -6.946  1.00 24.96 ? 7   VAL   B O   1 
ATOM   1888 C CB  . VAL   B 1 28  ? -20.543 -3.909  -8.144  1.00 24.69 ? 7   VAL   B CB  1 
ATOM   1889 C CG1 . VAL   B 1 28  ? -21.580 -2.996  -7.511  1.00 23.76 ? 7   VAL   B CG1 1 
ATOM   1890 C CG2 . VAL   B 1 28  ? -21.232 -4.918  -9.075  1.00 25.37 ? 7   VAL   B CG2 1 
ATOM   1891 N N   . VAL   B 1 29  ? -19.194 -0.757  -8.233  1.00 20.91 ? 8   VAL   B N   1 
ATOM   1892 C CA  . VAL   B 1 29  ? -18.841 0.368   -7.358  1.00 23.51 ? 8   VAL   B CA  1 
ATOM   1893 C C   . VAL   B 1 29  ? -20.121 1.108   -7.007  1.00 23.20 ? 8   VAL   B C   1 
ATOM   1894 O O   . VAL   B 1 29  ? -20.777 1.615   -7.918  1.00 23.39 ? 8   VAL   B O   1 
ATOM   1895 C CB  . VAL   B 1 29  ? -17.845 1.345   -8.010  1.00 22.78 ? 8   VAL   B CB  1 
ATOM   1896 C CG1 . VAL   B 1 29  ? -17.409 2.458   -7.050  1.00 22.31 ? 8   VAL   B CG1 1 
ATOM   1897 C CG2 . VAL   B 1 29  ? -16.610 0.632   -8.529  1.00 22.39 ? 8   VAL   B CG2 1 
ATOM   1898 N N   . THR   B 1 30  ? -20.479 1.214   -5.688  1.00 22.69 ? 9   THR   B N   1 
ATOM   1899 C CA  . THR   B 1 30  ? -21.713 1.916   -5.372  1.00 23.16 ? 9   THR   B CA  1 
ATOM   1900 C C   . THR   B 1 30  ? -21.437 3.417   -5.276  1.00 23.72 ? 9   THR   B C   1 
ATOM   1901 O O   . THR   B 1 30  ? -20.342 3.807   -4.920  1.00 24.51 ? 9   THR   B O   1 
ATOM   1902 C CB  . THR   B 1 30  ? -22.377 1.407   -4.092  1.00 22.31 ? 9   THR   B CB  1 
ATOM   1903 O OG1 . THR   B 1 30  ? -21.485 1.548   -2.970  1.00 23.20 ? 9   THR   B OG1 1 
ATOM   1904 C CG2 . THR   B 1 30  ? -22.716 -0.070  -4.193  1.00 21.14 ? 9   THR   B CG2 1 
ATOM   1905 N N   . GLY   B 1 31  ? -22.428 4.255   -5.609  1.00 23.91 ? 10  GLY   B N   1 
ATOM   1906 C CA  . GLY   B 1 31  ? -22.251 5.698   -5.541  1.00 23.97 ? 10  GLY   B CA  1 
ATOM   1907 C C   . GLY   B 1 31  ? -21.106 6.160   -6.447  1.00 27.67 ? 10  GLY   B C   1 
ATOM   1908 O O   . GLY   B 1 31  ? -20.297 6.996   -6.033  1.00 25.97 ? 10  GLY   B O   1 
ATOM   1909 N N   . ALA   B 1 32  ? -21.053 5.636   -7.688  1.00 21.94 ? 11  ALA   B N   1 
ATOM   1910 C CA  . ALA   B 1 32  ? -19.867 5.776   -8.530  1.00 24.29 ? 11  ALA   B CA  1 
ATOM   1911 C C   . ALA   B 1 32  ? -19.972 6.924   -9.535  1.00 22.85 ? 11  ALA   B C   1 
ATOM   1912 O O   . ALA   B 1 32  ? -19.065 7.120   -10.343 1.00 28.05 ? 11  ALA   B O   1 
ATOM   1913 C CB  . ALA   B 1 32  ? -19.597 4.489   -9.247  1.00 26.42 ? 11  ALA   B CB  1 
ATOM   1914 N N   . ALA   B 1 33  ? -21.053 7.694   -9.438  1.00 23.29 ? 12  ALA   B N   1 
ATOM   1915 C CA  . ALA   B 1 33  ? -21.292 8.736   -10.444 1.00 28.37 ? 12  ALA   B CA  1 
ATOM   1916 C C   . ALA   B 1 33  ? -20.327 9.899   -10.303 1.00 30.68 ? 12  ALA   B C   1 
ATOM   1917 O O   . ALA   B 1 33  ? -19.950 10.524  -11.300 1.00 29.96 ? 12  ALA   B O   1 
ATOM   1918 C CB  . ALA   B 1 33  ? -22.707 9.235   -10.350 1.00 27.44 ? 12  ALA   B CB  1 
ATOM   1919 N N   . LYS   B 1 34  ? -19.924 10.186  -9.058  1.00 26.88 ? 13  LYS   B N   1 
ATOM   1920 C CA  . LYS   B 1 34  ? -19.196 11.414  -8.771  1.00 28.51 ? 13  LYS   B CA  1 
ATOM   1921 C C   . LYS   B 1 34  ? -18.096 11.164  -7.726  1.00 31.84 ? 13  LYS   B C   1 
ATOM   1922 O O   . LYS   B 1 34  ? -18.060 10.116  -7.092  1.00 25.87 ? 13  LYS   B O   1 
ATOM   1923 C CB  . LYS   B 1 34  ? -20.187 12.403  -8.137  1.00 34.82 ? 13  LYS   B CB  1 
ATOM   1924 C CG  . LYS   B 1 34  ? -21.203 13.067  -9.054  1.00 37.30 ? 13  LYS   B CG  1 
ATOM   1925 C CD  . LYS   B 1 34  ? -22.154 13.987  -8.303  1.00 40.88 ? 13  LYS   B CD  1 
ATOM   1926 C CE  . LYS   B 1 34  ? -23.205 14.504  -9.227  1.00 45.83 ? 13  LYS   B CE  1 
ATOM   1927 N NZ  . LYS   B 1 34  ? -24.005 15.560  -8.602  1.00 51.58 ? 13  LYS   B NZ  1 
ATOM   1928 N N   . ARG   B 1 35  ? -17.170 12.118  -7.601  1.00 26.99 ? 14  ARG   B N   1 
ATOM   1929 C CA  . ARG   B 1 35  ? -16.213 12.194  -6.499  1.00 27.54 ? 14  ARG   B CA  1 
ATOM   1930 C C   . ARG   B 1 35  ? -15.425 10.888  -6.361  1.00 25.28 ? 14  ARG   B C   1 
ATOM   1931 O O   . ARG   B 1 35  ? -14.744 10.462  -7.311  1.00 24.74 ? 14  ARG   B O   1 
ATOM   1932 C CB  . ARG   B 1 35  ? -16.945 12.734  -5.262  1.00 29.05 ? 14  ARG   B CB  1 
ATOM   1933 C CG  . ARG   B 1 35  ? -17.511 14.129  -5.501  1.00 28.83 ? 14  ARG   B CG  1 
ATOM   1934 C CD  . ARG   B 1 35  ? -18.641 14.550  -4.567  1.00 33.10 ? 14  ARG   B CD  1 
ATOM   1935 N NE  . ARG   B 1 35  ? -18.251 14.360  -3.167  1.00 34.40 ? 14  ARG   B NE  1 
ATOM   1936 C CZ  . ARG   B 1 35  ? -17.475 15.186  -2.445  1.00 37.97 ? 14  ARG   B CZ  1 
ATOM   1937 N NH1 . ARG   B 1 35  ? -17.098 16.368  -2.930  1.00 31.72 ? 14  ARG   B NH1 1 
ATOM   1938 N NH2 . ARG   B 1 35  ? -17.112 14.816  -1.220  1.00 32.33 ? 14  ARG   B NH2 1 
ATOM   1939 N N   . ILE   B 1 36  ? -15.367 10.363  -5.126  1.00 21.52 ? 15  ILE   B N   1 
ATOM   1940 C CA  . ILE   B 1 36  ? -14.460 9.245   -4.854  1.00 22.05 ? 15  ILE   B CA  1 
ATOM   1941 C C   . ILE   B 1 36  ? -14.911 7.975   -5.597  1.00 21.59 ? 15  ILE   B C   1 
ATOM   1942 O O   . ILE   B 1 36  ? -14.079 7.221   -6.129  1.00 23.25 ? 15  ILE   B O   1 
ATOM   1943 C CB  . ILE   B 1 36  ? -14.324 9.034   -3.326  1.00 22.68 ? 15  ILE   B CB  1 
ATOM   1944 C CG1 . ILE   B 1 36  ? -13.461 10.164  -2.692  1.00 27.30 ? 15  ILE   B CG1 1 
ATOM   1945 C CG2 . ILE   B 1 36  ? -13.752 7.635   -3.047  1.00 19.73 ? 15  ILE   B CG2 1 
ATOM   1946 C CD1 . ILE   B 1 36  ? -13.508 10.247  -1.163  1.00 25.32 ? 15  ILE   B CD1 1 
ATOM   1947 N N   . GLY   B 1 37  ? -16.211 7.706   -5.599  1.00 21.86 ? 16  GLY   B N   1 
ATOM   1948 C CA  . GLY   B 1 37  ? -16.686 6.499   -6.276  1.00 23.95 ? 16  GLY   B CA  1 
ATOM   1949 C C   . GLY   B 1 37  ? -16.349 6.556   -7.779  1.00 24.38 ? 16  GLY   B C   1 
ATOM   1950 O O   . GLY   B 1 37  ? -15.949 5.573   -8.401  1.00 22.90 ? 16  GLY   B O   1 
ATOM   1951 N N   . ARG   B 1 38  ? -16.498 7.754   -8.358  1.00 24.61 ? 17  ARG   B N   1 
ATOM   1952 C CA  . ARG   B 1 38  ? -16.126 7.936   -9.754  1.00 24.44 ? 17  ARG   B CA  1 
ATOM   1953 C C   . ARG   B 1 38  ? -14.654 7.585   -9.958  1.00 25.29 ? 17  ARG   B C   1 
ATOM   1954 O O   . ARG   B 1 38  ? -14.322 6.895   -10.904 1.00 26.16 ? 17  ARG   B O   1 
ATOM   1955 C CB  . ARG   B 1 38  ? -16.529 9.342   -10.212 1.00 23.94 ? 17  ARG   B CB  1 
ATOM   1956 C CG  . ARG   B 1 38  ? -16.143 9.558   -11.669 1.00 30.82 ? 17  ARG   B CG  1 
ATOM   1957 C CD  . ARG   B 1 38  ? -16.476 11.003  -12.065 1.00 34.44 ? 17  ARG   B CD  1 
ATOM   1958 N NE  . ARG   B 1 38  ? -16.704 11.130  -13.511 1.00 37.41 ? 17  ARG   B NE  1 
ATOM   1959 C CZ  . ARG   B 1 38  ? -15.782 11.166  -14.473 1.00 43.42 ? 17  ARG   B CZ  1 
ATOM   1960 N NH1 . ARG   B 1 38  ? -14.505 10.967  -14.210 1.00 38.18 ? 17  ARG   B NH1 1 
ATOM   1961 N NH2 . ARG   B 1 38  ? -16.154 11.366  -15.726 1.00 45.43 ? 17  ARG   B NH2 1 
ATOM   1962 N N   . ALA   B 1 39  ? -13.754 8.073   -9.070  1.00 22.15 ? 18  ALA   B N   1 
ATOM   1963 C CA  . ALA   B 1 39  ? -12.322 7.899   -9.263  1.00 20.95 ? 18  ALA   B CA  1 
ATOM   1964 C C   . ALA   B 1 39  ? -11.991 6.422   -9.133  1.00 22.97 ? 18  ALA   B C   1 
ATOM   1965 O O   . ALA   B 1 39  ? -11.118 5.915   -9.826  1.00 24.79 ? 18  ALA   B O   1 
ATOM   1966 C CB  . ALA   B 1 39  ? -11.547 8.731   -8.237  1.00 22.91 ? 18  ALA   B CB  1 
ATOM   1967 N N   . ILE   B 1 40  ? -12.697 5.724   -8.239  1.00 22.13 ? 19  ILE   B N   1 
ATOM   1968 C CA  . ILE   B 1 40  ? -12.516 4.283   -8.085  1.00 21.22 ? 19  ILE   B CA  1 
ATOM   1969 C C   . ILE   B 1 40  ? -12.939 3.514   -9.348  1.00 23.42 ? 19  ILE   B C   1 
ATOM   1970 O O   . ILE   B 1 40  ? -12.207 2.635   -9.820  1.00 23.72 ? 19  ILE   B O   1 
ATOM   1971 C CB  . ILE   B 1 40  ? -13.282 3.786   -6.840  1.00 22.83 ? 19  ILE   B CB  1 
ATOM   1972 C CG1 . ILE   B 1 40  ? -12.643 4.397   -5.553  1.00 22.60 ? 19  ILE   B CG1 1 
ATOM   1973 C CG2 . ILE   B 1 40  ? -13.303 2.245   -6.825  1.00 22.01 ? 19  ILE   B CG2 1 
ATOM   1974 C CD1 . ILE   B 1 40  ? -13.471 4.216   -4.287  1.00 23.20 ? 19  ILE   B CD1 1 
ATOM   1975 N N   . ALA   B 1 41  ? -14.095 3.855   -9.917  1.00 26.31 ? 20  ALA   B N   1 
ATOM   1976 C CA  . ALA   B 1 41  ? -14.558 3.169   -11.126 1.00 26.79 ? 20  ALA   B CA  1 
ATOM   1977 C C   . ALA   B 1 41  ? -13.563 3.396   -12.272 1.00 28.79 ? 20  ALA   B C   1 
ATOM   1978 O O   . ALA   B 1 41  ? -13.202 2.471   -12.983 1.00 28.16 ? 20  ALA   B O   1 
ATOM   1979 C CB  . ALA   B 1 41  ? -15.956 3.620   -11.491 1.00 25.10 ? 20  ALA   B CB  1 
ATOM   1980 N N   . VAL   B 1 42  ? -13.098 4.636   -12.424 1.00 27.31 ? 21  VAL   B N   1 
ATOM   1981 C CA  . VAL   B 1 42  ? -12.135 4.950   -13.471 1.00 28.50 ? 21  VAL   B CA  1 
ATOM   1982 C C   . VAL   B 1 42  ? -10.847 4.153   -13.325 1.00 32.54 ? 21  VAL   B C   1 
ATOM   1983 O O   . VAL   B 1 42  ? -10.332 3.599   -14.306 1.00 31.07 ? 21  VAL   B O   1 
ATOM   1984 C CB  . VAL   B 1 42  ? -11.869 6.466   -13.441 1.00 24.33 ? 21  VAL   B CB  1 
ATOM   1985 C CG1 . VAL   B 1 42  ? -10.648 6.858   -14.288 1.00 25.88 ? 21  VAL   B CG1 1 
ATOM   1986 C CG2 . VAL   B 1 42  ? -13.121 7.232   -13.824 1.00 26.01 ? 21  VAL   B CG2 1 
ATOM   1987 N N   . LYS   B 1 43  ? -10.315 4.085   -12.091 1.00 26.09 ? 22  LYS   B N   1 
ATOM   1988 C CA  . LYS   B 1 43  ? -9.032  3.469   -11.890 1.00 28.08 ? 22  LYS   B CA  1 
ATOM   1989 C C   . LYS   B 1 43  ? -9.186  1.966   -12.061 1.00 29.23 ? 22  LYS   B C   1 
ATOM   1990 O O   . LYS   B 1 43  ? -8.269  1.322   -12.571 1.00 27.56 ? 22  LYS   B O   1 
ATOM   1991 C CB  . LYS   B 1 43  ? -8.389  3.727   -10.519 1.00 33.05 ? 22  LYS   B CB  1 
ATOM   1992 C CG  . LYS   B 1 43  ? -7.703  5.049   -10.338 1.00 33.30 ? 22  LYS   B CG  1 
ATOM   1993 C CD  . LYS   B 1 43  ? -6.457  4.896   -9.470  1.00 29.92 ? 22  LYS   B CD  1 
ATOM   1994 C CE  . LYS   B 1 43  ? -6.119  6.314   -9.162  1.00 35.28 ? 22  LYS   B CE  1 
ATOM   1995 N NZ  . LYS   B 1 43  ? -5.232  6.726   -10.244 1.00 38.84 ? 22  LYS   B NZ  1 
ATOM   1996 N N   . LEU   B 1 44  ? -10.323 1.407   -11.619 1.00 24.51 ? 23  LEU   B N   1 
ATOM   1997 C CA  . LEU   B 1 44  ? -10.524 -0.021  -11.863 1.00 23.87 ? 23  LEU   B CA  1 
ATOM   1998 C C   . LEU   B 1 44  ? -10.542 -0.299  -13.380 1.00 27.24 ? 23  LEU   B C   1 
ATOM   1999 O O   . LEU   B 1 44  ? -9.973  -1.288  -13.857 1.00 27.96 ? 23  LEU   B O   1 
ATOM   2000 C CB  . LEU   B 1 44  ? -11.858 -0.420  -11.236 1.00 25.65 ? 23  LEU   B CB  1 
ATOM   2001 C CG  . LEU   B 1 44  ? -11.844 -0.589  -9.700  1.00 22.37 ? 23  LEU   B CG  1 
ATOM   2002 C CD1 . LEU   B 1 44  ? -13.283 -0.724  -9.150  1.00 25.01 ? 23  LEU   B CD1 1 
ATOM   2003 C CD2 . LEU   B 1 44  ? -10.981 -1.804  -9.395  1.00 22.43 ? 23  LEU   B CD2 1 
ATOM   2004 N N   . HIS   B 1 45  ? -11.248 0.559   -14.115 1.00 29.26 ? 24  HIS   B N   1 
ATOM   2005 C CA  . HIS   B 1 45  ? -11.417 0.379   -15.559 1.00 31.10 ? 24  HIS   B CA  1 
ATOM   2006 C C   . HIS   B 1 45  ? -10.055 0.466   -16.244 1.00 34.39 ? 24  HIS   B C   1 
ATOM   2007 O O   . HIS   B 1 45  ? -9.748  -0.334  -17.126 1.00 32.62 ? 24  HIS   B O   1 
ATOM   2008 C CB  . HIS   B 1 45  ? -12.381 1.445   -16.095 1.00 29.07 ? 24  HIS   B CB  1 
ATOM   2009 C CG  . HIS   B 1 45  ? -12.810 1.263   -17.532 1.00 35.28 ? 24  HIS   B CG  1 
ATOM   2010 N ND1 . HIS   B 1 45  ? -12.224 1.950   -18.581 1.00 35.76 ? 24  HIS   B ND1 1 
ATOM   2011 C CD2 . HIS   B 1 45  ? -13.739 0.456   -18.083 1.00 34.36 ? 24  HIS   B CD2 1 
ATOM   2012 C CE1 . HIS   B 1 45  ? -12.819 1.606   -19.724 1.00 36.19 ? 24  HIS   B CE1 1 
ATOM   2013 N NE2 . HIS   B 1 45  ? -13.745 0.697   -19.458 1.00 36.69 ? 24  HIS   B NE2 1 
ATOM   2014 N N   . GLN   B 1 46  ? -9.263  1.462   -15.854 1.00 31.81 ? 25  GLN   B N   1 
ATOM   2015 C CA  . GLN   B 1 46  ? -7.925  1.639   -16.401 1.00 38.52 ? 25  GLN   B CA  1 
ATOM   2016 C C   . GLN   B 1 46  ? -7.049  0.429   -16.088 1.00 44.56 ? 25  GLN   B C   1 
ATOM   2017 O O   . GLN   B 1 46  ? -6.135  0.121   -16.851 1.00 46.80 ? 25  GLN   B O   1 
ATOM   2018 C CB  . GLN   B 1 46  ? -7.275  2.913   -15.874 1.00 39.69 ? 25  GLN   B CB  1 
ATOM   2019 C CG  . GLN   B 1 46  ? -8.052  4.164   -16.253 1.00 36.83 ? 25  GLN   B CG  1 
ATOM   2020 C CD  . GLN   B 1 46  ? -7.520  5.424   -15.604 1.00 44.81 ? 25  GLN   B CD  1 
ATOM   2021 O OE1 . GLN   B 1 46  ? -6.856  5.394   -14.553 1.00 45.27 ? 25  GLN   B OE1 1 
ATOM   2022 N NE2 . GLN   B 1 46  ? -7.878  6.557   -16.201 1.00 44.51 ? 25  GLN   B NE2 1 
ATOM   2023 N N   . THR   B 1 47  ? -7.338  -0.268  -14.981 1.00 35.68 ? 26  THR   B N   1 
ATOM   2024 C CA  . THR   B 1 47  ? -6.561  -1.432  -14.582 1.00 35.71 ? 26  THR   B CA  1 
ATOM   2025 C C   . THR   B 1 47  ? -6.998  -2.650  -15.389 1.00 37.96 ? 26  THR   B C   1 
ATOM   2026 O O   . THR   B 1 47  ? -6.343  -3.689  -15.327 1.00 39.56 ? 26  THR   B O   1 
ATOM   2027 C CB  . THR   B 1 47  ? -6.788  -1.698  -13.091 1.00 38.70 ? 26  THR   B CB  1 
ATOM   2028 O OG1 . THR   B 1 47  ? -6.292  -0.543  -12.427 1.00 45.40 ? 26  THR   B OG1 1 
ATOM   2029 C CG2 . THR   B 1 47  ? -6.055  -2.921  -12.586 1.00 41.89 ? 26  THR   B CG2 1 
ATOM   2030 N N   . GLY   B 1 48  ? -8.154  -2.555  -16.044 1.00 35.12 ? 27  GLY   B N   1 
ATOM   2031 C CA  . GLY   B 1 48  ? -8.634  -3.606  -16.931 1.00 34.81 ? 27  GLY   B CA  1 
ATOM   2032 C C   . GLY   B 1 48  ? -9.981  -4.190  -16.514 1.00 37.60 ? 27  GLY   B C   1 
ATOM   2033 O O   . GLY   B 1 48  ? -10.419 -5.179  -17.099 1.00 37.78 ? 27  GLY   B O   1 
ATOM   2034 N N   . TYR   B 1 49  ? -10.643 -3.577  -15.512 1.00 32.25 ? 28  TYR   B N   1 
ATOM   2035 C CA  . TYR   B 1 49  ? -11.927 -4.079  -15.052 1.00 29.78 ? 28  TYR   B CA  1 
ATOM   2036 C C   . TYR   B 1 49  ? -13.060 -3.556  -15.924 1.00 27.91 ? 28  TYR   B C   1 
ATOM   2037 O O   . TYR   B 1 49  ? -13.062 -2.396  -16.337 1.00 29.34 ? 28  TYR   B O   1 
ATOM   2038 C CB  . TYR   B 1 49  ? -12.283 -3.623  -13.617 1.00 31.64 ? 28  TYR   B CB  1 
ATOM   2039 C CG  . TYR   B 1 49  ? -11.510 -4.420  -12.586 1.00 29.71 ? 28  TYR   B CG  1 
ATOM   2040 C CD1 . TYR   B 1 49  ? -10.192 -4.099  -12.250 1.00 30.65 ? 28  TYR   B CD1 1 
ATOM   2041 C CD2 . TYR   B 1 49  ? -12.118 -5.486  -11.923 1.00 33.18 ? 28  TYR   B CD2 1 
ATOM   2042 C CE1 . TYR   B 1 49  ? -9.484  -4.849  -11.316 1.00 29.50 ? 28  TYR   B CE1 1 
ATOM   2043 C CE2 . TYR   B 1 49  ? -11.402 -6.247  -11.007 1.00 30.30 ? 28  TYR   B CE2 1 
ATOM   2044 C CZ  . TYR   B 1 49  ? -10.097 -5.913  -10.681 1.00 33.37 ? 28  TYR   B CZ  1 
ATOM   2045 O OH  . TYR   B 1 49  ? -9.393  -6.702  -9.795  1.00 34.92 ? 28  TYR   B OH  1 
ATOM   2046 N N   . ARG   B 1 50  ? -14.067 -4.418  -16.117 1.00 27.47 ? 29  ARG   B N   1 
ATOM   2047 C CA  . ARG   B 1 50  ? -15.376 -3.962  -16.560 1.00 27.98 ? 29  ARG   B CA  1 
ATOM   2048 C C   . ARG   B 1 50  ? -16.136 -3.501  -15.321 1.00 28.53 ? 29  ARG   B C   1 
ATOM   2049 O O   . ARG   B 1 50  ? -15.873 -4.037  -14.250 1.00 29.95 ? 29  ARG   B O   1 
ATOM   2050 C CB  . ARG   B 1 50  ? -16.081 -5.123  -17.267 1.00 33.55 ? 29  ARG   B CB  1 
ATOM   2051 C CG  . ARG   B 1 50  ? -15.347 -5.343  -18.584 1.00 35.43 ? 29  ARG   B CG  1 
ATOM   2052 C CD  . ARG   B 1 50  ? -16.012 -6.486  -19.315 1.00 36.33 ? 29  ARG   B CD  1 
ATOM   2053 N NE  . ARG   B 1 50  ? -15.681 -7.734  -18.623 1.00 40.64 ? 29  ARG   B NE  1 
ATOM   2054 C CZ  . ARG   B 1 50  ? -16.269 -8.879  -18.913 1.00 42.11 ? 29  ARG   B CZ  1 
ATOM   2055 N NH1 . ARG   B 1 50  ? -17.203 -8.929  -19.855 1.00 44.11 ? 29  ARG   B NH1 1 
ATOM   2056 N NH2 . ARG   B 1 50  ? -15.909 -9.968  -18.268 1.00 44.69 ? 29  ARG   B NH2 1 
ATOM   2057 N N   . VAL   B 1 51  ? -17.001 -2.480  -15.449 1.00 27.89 ? 30  VAL   B N   1 
ATOM   2058 C CA  . VAL   B 1 51  ? -17.491 -1.835  -14.231 1.00 30.96 ? 30  VAL   B CA  1 
ATOM   2059 C C   . VAL   B 1 51  ? -19.005 -1.679  -14.255 1.00 29.77 ? 30  VAL   B C   1 
ATOM   2060 O O   . VAL   B 1 51  ? -19.565 -1.245  -15.269 1.00 29.94 ? 30  VAL   B O   1 
ATOM   2061 C CB  . VAL   B 1 51  ? -16.838 -0.483  -13.870 1.00 28.29 ? 30  VAL   B CB  1 
ATOM   2062 C CG1 . VAL   B 1 51  ? -15.371 -0.611  -13.494 1.00 29.72 ? 30  VAL   B CG1 1 
ATOM   2063 C CG2 . VAL   B 1 51  ? -17.035 0.571   -14.955 1.00 32.46 ? 30  VAL   B CG2 1 
ATOM   2064 N N   . VAL   B 1 52  ? -19.668 -1.970  -13.115 1.00 25.14 ? 31  VAL   B N   1 
ATOM   2065 C CA  . VAL   B 1 52  ? -21.010 -1.461  -12.881 1.00 23.80 ? 31  VAL   B CA  1 
ATOM   2066 C C   . VAL   B 1 52  ? -20.939 -0.165  -12.090 1.00 28.63 ? 31  VAL   B C   1 
ATOM   2067 O O   . VAL   B 1 52  ? -20.460 -0.182  -10.956 1.00 27.92 ? 31  VAL   B O   1 
ATOM   2068 C CB  . VAL   B 1 52  ? -21.933 -2.445  -12.151 1.00 26.92 ? 31  VAL   B CB  1 
ATOM   2069 C CG1 . VAL   B 1 52  ? -23.288 -1.808  -11.845 1.00 23.92 ? 31  VAL   B CG1 1 
ATOM   2070 C CG2 . VAL   B 1 52  ? -22.092 -3.749  -12.927 1.00 27.04 ? 31  VAL   B CG2 1 
ATOM   2071 N N   . ILE   B 1 53  ? -21.469 0.926   -12.667 1.00 24.50 ? 32  ILE   B N   1 
ATOM   2072 C CA  . ILE   B 1 53  ? -21.577 2.227   -12.012 1.00 26.86 ? 32  ILE   B CA  1 
ATOM   2073 C C   . ILE   B 1 53  ? -22.949 2.343   -11.359 1.00 27.39 ? 32  ILE   B C   1 
ATOM   2074 O O   . ILE   B 1 53  ? -23.950 2.564   -12.045 1.00 28.65 ? 32  ILE   B O   1 
ATOM   2075 C CB  . ILE   B 1 53  ? -21.373 3.330   -13.065 1.00 27.74 ? 32  ILE   B CB  1 
ATOM   2076 C CG1 . ILE   B 1 53  ? -20.054 3.139   -13.762 1.00 29.84 ? 32  ILE   B CG1 1 
ATOM   2077 C CG2 . ILE   B 1 53  ? -21.569 4.740   -12.481 1.00 28.29 ? 32  ILE   B CG2 1 
ATOM   2078 C CD1 . ILE   B 1 53  ? -19.973 3.845   -15.103 1.00 35.60 ? 32  ILE   B CD1 1 
ATOM   2079 N N   . HIS   B 1 54  ? -23.024 2.124   -10.033 1.00 25.21 ? 33  HIS   B N   1 
ATOM   2080 C CA  . HIS   B 1 54  ? -24.283 2.282   -9.315  1.00 24.35 ? 33  HIS   B CA  1 
ATOM   2081 C C   . HIS   B 1 54  ? -24.429 3.769   -8.965  1.00 26.04 ? 33  HIS   B C   1 
ATOM   2082 O O   . HIS   B 1 54  ? -23.434 4.465   -8.738  1.00 25.69 ? 33  HIS   B O   1 
ATOM   2083 C CB  . HIS   B 1 54  ? -24.327 1.404   -8.044  1.00 26.53 ? 33  HIS   B CB  1 
ATOM   2084 C CG  . HIS   B 1 54  ? -25.311 1.949   -7.059  1.00 25.26 ? 33  HIS   B CG  1 
ATOM   2085 N ND1 . HIS   B 1 54  ? -24.938 2.906   -6.139  1.00 23.51 ? 33  HIS   B ND1 1 
ATOM   2086 C CD2 . HIS   B 1 54  ? -26.633 1.776   -6.891  1.00 26.47 ? 33  HIS   B CD2 1 
ATOM   2087 C CE1 . HIS   B 1 54  ? -25.994 3.294   -5.443  1.00 23.96 ? 33  HIS   B CE1 1 
ATOM   2088 N NE2 . HIS   B 1 54  ? -27.041 2.615   -5.896  1.00 23.55 ? 33  HIS   B NE2 1 
ATOM   2089 N N   . TYR   B 1 55  ? -25.669 4.267   -8.996  1.00 24.47 ? 34  TYR   B N   1 
ATOM   2090 C CA  . TYR   B 1 55  ? -25.969 5.646   -8.638  1.00 27.79 ? 34  TYR   B CA  1 
ATOM   2091 C C   . TYR   B 1 55  ? -27.364 5.703   -8.018  1.00 28.72 ? 34  TYR   B C   1 
ATOM   2092 O O   . TYR   B 1 55  ? -28.135 4.751   -8.071  1.00 27.44 ? 34  TYR   B O   1 
ATOM   2093 C CB  . TYR   B 1 55  ? -25.784 6.592   -9.836  1.00 27.11 ? 34  TYR   B CB  1 
ATOM   2094 C CG  . TYR   B 1 55  ? -26.906 6.423   -10.853 1.00 28.01 ? 34  TYR   B CG  1 
ATOM   2095 C CD1 . TYR   B 1 55  ? -26.832 5.442   -11.840 1.00 29.32 ? 34  TYR   B CD1 1 
ATOM   2096 C CD2 . TYR   B 1 55  ? -28.060 7.210   -10.780 1.00 32.32 ? 34  TYR   B CD2 1 
ATOM   2097 C CE1 . TYR   B 1 55  ? -27.878 5.270   -12.742 1.00 31.05 ? 34  TYR   B CE1 1 
ATOM   2098 C CE2 . TYR   B 1 55  ? -29.108 7.045   -11.678 1.00 26.04 ? 34  TYR   B CE2 1 
ATOM   2099 C CZ  . TYR   B 1 55  ? -29.009 6.079   -12.665 1.00 32.16 ? 34  TYR   B CZ  1 
ATOM   2100 O OH  . TYR   B 1 55  ? -30.039 5.923   -13.572 1.00 32.41 ? 34  TYR   B OH  1 
ATOM   2101 N N   . HIS   B 1 56  ? -27.679 6.823   -7.379  1.00 27.35 ? 35  HIS   B N   1 
ATOM   2102 C CA  . HIS   B 1 56  ? -29.005 6.987   -6.818  1.00 29.17 ? 35  HIS   B CA  1 
ATOM   2103 C C   . HIS   B 1 56  ? -29.722 8.105   -7.585  1.00 32.98 ? 35  HIS   B C   1 
ATOM   2104 O O   . HIS   B 1 56  ? -30.619 7.835   -8.385  1.00 32.16 ? 35  HIS   B O   1 
ATOM   2105 C CB  . HIS   B 1 56  ? -28.891 7.245   -5.314  1.00 27.38 ? 35  HIS   B CB  1 
ATOM   2106 C CG  . HIS   B 1 56  ? -30.185 7.562   -4.654  1.00 30.39 ? 35  HIS   B CG  1 
ATOM   2107 N ND1 . HIS   B 1 56  ? -30.299 8.494   -3.647  1.00 30.76 ? 35  HIS   B ND1 1 
ATOM   2108 C CD2 . HIS   B 1 56  ? -31.427 7.112   -4.912  1.00 32.33 ? 35  HIS   B CD2 1 
ATOM   2109 C CE1 . HIS   B 1 56  ? -31.572 8.562   -3.285  1.00 33.00 ? 35  HIS   B CE1 1 
ATOM   2110 N NE2 . HIS   B 1 56  ? -32.272 7.738   -4.044  1.00 33.54 ? 35  HIS   B NE2 1 
ATOM   2111 N N   . ASN   B 1 57  ? -29.245 9.339   -7.419  1.00 33.17 ? 36  ASN   B N   1 
ATOM   2112 C CA  . ASN   B 1 57  ? -29.832 10.516  -8.044  1.00 33.30 ? 36  ASN   B CA  1 
ATOM   2113 C C   . ASN   B 1 57  ? -29.012 11.022  -9.236  1.00 38.88 ? 36  ASN   B C   1 
ATOM   2114 O O   . ASN   B 1 57  ? -29.512 11.798  -10.058 1.00 39.79 ? 36  ASN   B O   1 
ATOM   2115 C CB  . ASN   B 1 57  ? -29.895 11.685  -7.065  1.00 33.43 ? 36  ASN   B CB  1 
ATOM   2116 C CG  . ASN   B 1 57  ? -30.897 11.453  -5.960  1.00 42.96 ? 36  ASN   B CG  1 
ATOM   2117 O OD1 . ASN   B 1 57  ? -31.921 10.801  -6.194  1.00 39.09 ? 36  ASN   B OD1 1 
ATOM   2118 N ND2 . ASN   B 1 57  ? -30.617 11.945  -4.752  1.00 39.83 ? 36  ASN   B ND2 1 
ATOM   2119 N N   . SER   B 1 58  ? -27.746 10.632  -9.356  1.00 32.59 ? 37  SER   B N   1 
ATOM   2120 C CA  . SER   B 1 58  ? -26.943 11.362  -10.317 1.00 30.96 ? 37  SER   B CA  1 
ATOM   2121 C C   . SER   B 1 58  ? -26.901 10.604  -11.648 1.00 27.56 ? 37  SER   B C   1 
ATOM   2122 O O   . SER   B 1 58  ? -25.832 10.175  -12.064 1.00 28.55 ? 37  SER   B O   1 
ATOM   2123 C CB  . SER   B 1 58  ? -25.546 11.661  -9.756  1.00 36.75 ? 37  SER   B CB  1 
ATOM   2124 O OG  . SER   B 1 58  ? -25.563 12.498  -8.602  1.00 36.33 ? 37  SER   B OG  1 
ATOM   2125 N N   . ALA   B 1 59  ? -28.052 10.522  -12.353 1.00 29.71 ? 38  ALA   B N   1 
ATOM   2126 C CA  . ALA   B 1 59  ? -28.161 9.710   -13.569 1.00 31.33 ? 38  ALA   B CA  1 
ATOM   2127 C C   . ALA   B 1 59  ? -27.269 10.269  -14.681 1.00 30.79 ? 38  ALA   B C   1 
ATOM   2128 O O   . ALA   B 1 59  ? -26.584 9.531   -15.379 1.00 30.72 ? 38  ALA   B O   1 
ATOM   2129 C CB  . ALA   B 1 59  ? -29.601 9.583   -14.009 1.00 34.82 ? 38  ALA   B CB  1 
ATOM   2130 N N   . GLU   B 1 60  ? -27.268 11.600  -14.823 1.00 36.02 ? 39  GLU   B N   1 
ATOM   2131 C CA  . GLU   B 1 60  ? -26.566 12.248  -15.917 1.00 36.00 ? 39  GLU   B CA  1 
ATOM   2132 C C   . GLU   B 1 60  ? -25.058 12.020  -15.776 1.00 32.29 ? 39  GLU   B C   1 
ATOM   2133 O O   . GLU   B 1 60  ? -24.386 11.686  -16.752 1.00 31.63 ? 39  GLU   B O   1 
ATOM   2134 C CB  . GLU   B 1 60  ? -27.029 13.706  -16.006 1.00 38.46 ? 39  GLU   B CB  1 
ATOM   2135 C CG  . GLU   B 1 60  ? -26.469 14.460  -17.213 1.00 50.29 ? 39  GLU   B CG  1 
ATOM   2136 N N   . ALA   B 1 61  ? -24.523 12.209  -14.555 1.00 29.98 ? 40  ALA   B N   1 
ATOM   2137 C CA  . ALA   B 1 61  ? -23.127 11.924  -14.304 1.00 24.66 ? 40  ALA   B CA  1 
ATOM   2138 C C   . ALA   B 1 61  ? -22.808 10.442  -14.496 1.00 23.71 ? 40  ALA   B C   1 
ATOM   2139 O O   . ALA   B 1 61  ? -21.742 10.128  -15.015 1.00 27.88 ? 40  ALA   B O   1 
ATOM   2140 C CB  . ALA   B 1 61  ? -22.685 12.456  -12.927 1.00 29.51 ? 40  ALA   B CB  1 
ATOM   2141 N N   . ALA   B 1 62  ? -23.714 9.550   -14.076 1.00 25.85 ? 41  ALA   B N   1 
ATOM   2142 C CA  . ALA   B 1 62  ? -23.469 8.114   -14.183 1.00 28.17 ? 41  ALA   B CA  1 
ATOM   2143 C C   . ALA   B 1 62  ? -23.320 7.704   -15.657 1.00 31.57 ? 41  ALA   B C   1 
ATOM   2144 O O   . ALA   B 1 62  ? -22.385 6.991   -16.055 1.00 30.06 ? 41  ALA   B O   1 
ATOM   2145 C CB  . ALA   B 1 62  ? -24.589 7.355   -13.502 1.00 30.54 ? 41  ALA   B CB  1 
ATOM   2146 N N   . VAL   B 1 63  ? -24.234 8.210   -16.492 1.00 34.04 ? 42  VAL   B N   1 
ATOM   2147 C CA  . VAL   B 1 63  ? -24.255 7.820   -17.899 1.00 30.44 ? 42  VAL   B CA  1 
ATOM   2148 C C   . VAL   B 1 63  ? -23.064 8.415   -18.641 1.00 33.75 ? 42  VAL   B C   1 
ATOM   2149 O O   . VAL   B 1 63  ? -22.469 7.760   -19.493 1.00 35.78 ? 42  VAL   B O   1 
ATOM   2150 C CB  . VAL   B 1 63  ? -25.595 8.334   -18.456 1.00 33.45 ? 42  VAL   B CB  1 
ATOM   2151 C CG1 . VAL   B 1 63  ? -25.607 8.317   -19.986 1.00 34.70 ? 42  VAL   B CG1 1 
ATOM   2152 C CG2 . VAL   B 1 63  ? -26.749 7.520   -17.883 1.00 30.54 ? 42  VAL   B CG2 1 
ATOM   2153 N N   . SER   B 1 64  ? -22.732 9.666   -18.302 1.00 34.99 ? 43  SER   B N   1 
ATOM   2154 C CA  . SER   B 1 64  ? -21.588 10.354  -18.872 1.00 35.39 ? 43  SER   B CA  1 
ATOM   2155 C C   . SER   B 1 64  ? -20.321 9.552   -18.607 1.00 40.46 ? 43  SER   B C   1 
ATOM   2156 O O   . SER   B 1 64  ? -19.433 9.429   -19.469 1.00 36.09 ? 43  SER   B O   1 
ATOM   2157 C CB  . SER   B 1 64  ? -21.491 11.738  -18.264 1.00 40.75 ? 43  SER   B CB  1 
ATOM   2158 O OG  . SER   B 1 64  ? -20.282 12.360  -18.675 1.00 49.01 ? 43  SER   B OG  1 
ATOM   2159 N N   . LEU   B 1 65  ? -20.205 9.051   -17.365 1.00 31.56 ? 44  LEU   B N   1 
ATOM   2160 C CA  . LEU   B 1 65  ? -19.040 8.247   -17.061 1.00 28.22 ? 44  LEU   B CA  1 
ATOM   2161 C C   . LEU   B 1 65  ? -19.063 6.955   -17.891 1.00 25.17 ? 44  LEU   B C   1 
ATOM   2162 O O   . LEU   B 1 65  ? -18.041 6.560   -18.464 1.00 29.14 ? 44  LEU   B O   1 
ATOM   2163 C CB  . LEU   B 1 65  ? -18.990 7.989   -15.550 1.00 24.95 ? 44  LEU   B CB  1 
ATOM   2164 C CG  . LEU   B 1 65  ? -17.905 7.005   -15.127 1.00 28.14 ? 44  LEU   B CG  1 
ATOM   2165 C CD1 . LEU   B 1 65  ? -16.539 7.584   -15.364 1.00 30.27 ? 44  LEU   B CD1 1 
ATOM   2166 C CD2 . LEU   B 1 65  ? -18.180 6.717   -13.623 1.00 31.19 ? 44  LEU   B CD2 1 
ATOM   2167 N N   . ALA   B 1 66  ? -20.205 6.279   -17.915 1.00 27.27 ? 45  ALA   B N   1 
ATOM   2168 C CA  . ALA   B 1 66  ? -20.316 5.027   -18.674 1.00 33.24 ? 45  ALA   B CA  1 
ATOM   2169 C C   . ALA   B 1 66  ? -19.925 5.228   -20.150 1.00 33.64 ? 45  ALA   B C   1 
ATOM   2170 O O   . ALA   B 1 66  ? -19.182 4.430   -20.719 1.00 33.95 ? 45  ALA   B O   1 
ATOM   2171 C CB  . ALA   B 1 66  ? -21.698 4.429   -18.512 1.00 35.50 ? 45  ALA   B CB  1 
ATOM   2172 N N   . ASP   B 1 67  ? -20.351 6.355   -20.734 1.00 36.50 ? 46  ASP   B N   1 
ATOM   2173 C CA  . ASP   B 1 67  ? -20.076 6.687   -22.134 1.00 32.87 ? 46  ASP   B CA  1 
ATOM   2174 C C   . ASP   B 1 67  ? -18.569 6.888   -22.343 1.00 43.51 ? 46  ASP   B C   1 
ATOM   2175 O O   . ASP   B 1 67  ? -17.980 6.351   -23.290 1.00 41.82 ? 46  ASP   B O   1 
ATOM   2176 C CB  . ASP   B 1 67  ? -20.908 7.898   -22.537 1.00 37.86 ? 46  ASP   B CB  1 
ATOM   2177 C CG  . ASP   B 1 67  ? -22.390 7.623   -22.781 1.00 37.12 ? 46  ASP   B CG  1 
ATOM   2178 O OD1 . ASP   B 1 67  ? -22.808 6.462   -22.544 1.00 37.67 ? 46  ASP   B OD1 1 
ATOM   2179 O OD2 . ASP   B 1 67  ? -23.113 8.564   -23.216 1.00 33.68 ? 46  ASP   B OD2 1 
ATOM   2180 N N   . GLU   B 1 68  ? -17.947 7.656   -21.440 1.00 36.43 ? 47  GLU   B N   1 
ATOM   2181 C CA  . GLU   B 1 68  ? -16.505 7.855   -21.463 1.00 39.55 ? 47  GLU   B CA  1 
ATOM   2182 C C   . GLU   B 1 68  ? -15.740 6.526   -21.421 1.00 40.33 ? 47  GLU   B C   1 
ATOM   2183 O O   . GLU   B 1 68  ? -14.789 6.330   -22.184 1.00 38.01 ? 47  GLU   B O   1 
ATOM   2184 C CB  . GLU   B 1 68  ? -16.129 8.881   -20.398 1.00 38.16 ? 47  GLU   B CB  1 
ATOM   2185 C CG  . GLU   B 1 68  ? -14.625 8.942   -20.134 1.00 46.15 ? 47  GLU   B CG  1 
ATOM   2186 C CD  . GLU   B 1 68  ? -14.164 9.806   -18.963 1.00 54.18 ? 47  GLU   B CD  1 
ATOM   2187 O OE1 . GLU   B 1 68  ? -13.276 9.326   -18.206 1.00 55.38 ? 47  GLU   B OE1 1 
ATOM   2188 O OE2 . GLU   B 1 68  ? -14.707 10.939  -18.799 1.00 49.72 ? 47  GLU   B OE2 1 
ATOM   2189 N N   . LEU   B 1 69  ? -16.128 5.608   -20.514 1.00 34.57 ? 48  LEU   B N   1 
ATOM   2190 C CA  . LEU   B 1 69  ? -15.354 4.392   -20.330 1.00 30.17 ? 48  LEU   B CA  1 
ATOM   2191 C C   . LEU   B 1 69  ? -15.540 3.480   -21.546 1.00 33.80 ? 48  LEU   B C   1 
ATOM   2192 O O   . LEU   B 1 69  ? -14.600 2.813   -21.994 1.00 39.91 ? 48  LEU   B O   1 
ATOM   2193 C CB  . LEU   B 1 69  ? -15.714 3.705   -19.009 1.00 27.60 ? 48  LEU   B CB  1 
ATOM   2194 C CG  . LEU   B 1 69  ? -15.394 4.508   -17.737 1.00 27.90 ? 48  LEU   B CG  1 
ATOM   2195 C CD1 . LEU   B 1 69  ? -15.828 3.615   -16.540 1.00 29.80 ? 48  LEU   B CD1 1 
ATOM   2196 C CD2 . LEU   B 1 69  ? -13.920 4.878   -17.655 1.00 31.67 ? 48  LEU   B CD2 1 
ATOM   2197 N N   . ASN   B 1 70  ? -16.767 3.470   -22.077 1.00 31.76 ? 49  ASN   B N   1 
ATOM   2198 C CA  . ASN   B 1 70  ? -17.093 2.656   -23.237 1.00 34.81 ? 49  ASN   B CA  1 
ATOM   2199 C C   . ASN   B 1 70  ? -16.422 3.196   -24.505 1.00 36.22 ? 49  ASN   B C   1 
ATOM   2200 O O   . ASN   B 1 70  ? -16.257 2.451   -25.469 1.00 35.62 ? 49  ASN   B O   1 
ATOM   2201 C CB  . ASN   B 1 70  ? -18.599 2.509   -23.412 1.00 30.04 ? 49  ASN   B CB  1 
ATOM   2202 C CG  . ASN   B 1 70  ? -19.184 1.535   -22.416 1.00 37.55 ? 49  ASN   B CG  1 
ATOM   2203 O OD1 . ASN   B 1 70  ? -18.554 0.518   -22.090 1.00 37.82 ? 49  ASN   B OD1 1 
ATOM   2204 N ND2 . ASN   B 1 70  ? -20.387 1.815   -21.937 1.00 32.94 ? 49  ASN   B ND2 1 
ATOM   2205 N N   . LYS   B 1 71  ? -16.048 4.483   -24.507 1.00 32.25 ? 50  LYS   B N   1 
ATOM   2206 C CA  . LYS   B 1 71  ? -15.308 5.029   -25.629 1.00 40.49 ? 50  LYS   B CA  1 
ATOM   2207 C C   . LYS   B 1 71  ? -13.889 4.485   -25.539 1.00 44.97 ? 50  LYS   B C   1 
ATOM   2208 O O   . LYS   B 1 71  ? -13.263 4.208   -26.561 1.00 43.83 ? 50  LYS   B O   1 
ATOM   2209 C CB  . LYS   B 1 71  ? -15.326 6.563   -25.652 1.00 39.92 ? 50  LYS   B CB  1 
ATOM   2210 N N   . GLU   B 1 72  ? -13.391 4.320   -24.308 1.00 40.93 ? 51  GLU   B N   1 
ATOM   2211 C CA  . GLU   B 1 72  ? -12.044 3.804   -24.114 1.00 42.02 ? 51  GLU   B CA  1 
ATOM   2212 C C   . GLU   B 1 72  ? -11.998 2.331   -24.531 1.00 38.91 ? 51  GLU   B C   1 
ATOM   2213 O O   . GLU   B 1 72  ? -11.110 1.930   -25.274 1.00 43.79 ? 51  GLU   B O   1 
ATOM   2214 C CB  . GLU   B 1 72  ? -11.497 4.182   -22.728 1.00 42.42 ? 51  GLU   B CB  1 
ATOM   2215 C CG  . GLU   B 1 72  ? -10.012 4.535   -22.740 1.00 48.48 ? 51  GLU   B CG  1 
ATOM   2216 C CD  . GLU   B 1 72  ? -9.698  5.755   -23.594 0.50 51.50 ? 51  GLU   B CD  1 
ATOM   2217 O OE1 . GLU   B 1 72  ? -9.195  5.566   -24.726 0.50 58.99 ? 51  GLU   B OE1 1 
ATOM   2218 O OE2 . GLU   B 1 72  ? -9.971  6.893   -23.146 0.50 49.65 ? 51  GLU   B OE2 1 
ATOM   2219 N N   . ARG   B 1 73  ? -12.980 1.535   -24.091 1.00 38.78 ? 52  ARG   B N   1 
ATOM   2220 C CA  . ARG   B 1 73  ? -13.098 0.122   -24.412 1.00 36.94 ? 52  ARG   B CA  1 
ATOM   2221 C C   . ARG   B 1 73  ? -14.578 -0.231  -24.508 1.00 39.69 ? 52  ARG   B C   1 
ATOM   2222 O O   . ARG   B 1 73  ? -15.351 -0.007  -23.582 1.00 38.29 ? 52  ARG   B O   1 
ATOM   2223 C CB  . ARG   B 1 73  ? -12.440 -0.848  -23.414 1.00 36.44 ? 52  ARG   B CB  1 
ATOM   2224 C CG  . ARG   B 1 73  ? -10.941 -0.842  -23.169 0.70 44.43 ? 52  ARG   B CG  1 
ATOM   2225 C CD  . ARG   B 1 73  ? -10.503 -2.133  -22.485 0.70 42.74 ? 52  ARG   B CD  1 
ATOM   2226 N NE  . ARG   B 1 73  ? -11.183 -2.353  -21.198 0.70 40.91 ? 52  ARG   B NE  1 
ATOM   2227 C CZ  . ARG   B 1 73  ? -11.056 -1.655  -20.065 0.70 42.06 ? 52  ARG   B CZ  1 
ATOM   2228 N NH1 . ARG   B 1 73  ? -10.302 -0.572  -20.007 0.70 36.96 ? 52  ARG   B NH1 1 
ATOM   2229 N NH2 . ARG   B 1 73  ? -11.716 -2.043  -18.986 0.70 42.11 ? 52  ARG   B NH2 1 
ATOM   2230 N N   . SER   B 1 74  ? -14.998 -0.802  -25.637 1.00 38.29 ? 53  SER   B N   1 
ATOM   2231 C CA  . SER   B 1 74  ? -16.421 -1.013  -25.856 1.00 35.92 ? 53  SER   B CA  1 
ATOM   2232 C C   . SER   B 1 74  ? -16.958 -2.145  -24.986 1.00 34.77 ? 53  SER   B C   1 
ATOM   2233 O O   . SER   B 1 74  ? -16.293 -3.169  -24.763 1.00 36.78 ? 53  SER   B O   1 
ATOM   2234 C CB  . SER   B 1 74  ? -16.704 -1.287  -27.328 1.00 50.11 ? 53  SER   B CB  1 
ATOM   2235 O OG  . SER   B 1 74  ? -16.704 -0.082  -28.084 1.00 46.11 ? 53  SER   B OG  1 
ATOM   2236 N N   . ASN   B 1 75  ? -18.188 -1.928  -24.505 1.00 31.95 ? 54  ASN   B N   1 
ATOM   2237 C CA  . ASN   B 1 75  ? -18.905 -2.897  -23.702 1.00 40.06 ? 54  ASN   B CA  1 
ATOM   2238 C C   . ASN   B 1 75  ? -18.145 -3.199  -22.406 1.00 38.81 ? 54  ASN   B C   1 
ATOM   2239 O O   . ASN   B 1 75  ? -18.043 -4.359  -22.003 1.00 37.29 ? 54  ASN   B O   1 
ATOM   2240 C CB  . ASN   B 1 75  ? -19.103 -4.219  -24.440 1.00 46.04 ? 54  ASN   B CB  1 
ATOM   2241 C CG  . ASN   B 1 75  ? -20.087 -4.133  -25.582 1.00 53.94 ? 54  ASN   B CG  1 
ATOM   2242 O OD1 . ASN   B 1 75  ? -20.393 -5.163  -26.196 1.00 58.95 ? 54  ASN   B OD1 1 
ATOM   2243 N ND2 . ASN   B 1 75  ? -20.603 -2.944  -25.871 1.00 49.50 ? 54  ASN   B ND2 1 
ATOM   2244 N N   . THR   B 1 76  ? -17.649 -2.161  -21.726 1.00 37.48 ? 55  THR   B N   1 
ATOM   2245 C CA  . THR   B 1 76  ? -16.944 -2.450  -20.492 1.00 34.27 ? 55  THR   B CA  1 
ATOM   2246 C C   . THR   B 1 76  ? -17.586 -1.746  -19.291 1.00 36.53 ? 55  THR   B C   1 
ATOM   2247 O O   . THR   B 1 76  ? -17.064 -1.843  -18.181 1.00 31.88 ? 55  THR   B O   1 
ATOM   2248 C CB  . THR   B 1 76  ? -15.457 -2.108  -20.621 1.00 32.86 ? 55  THR   B CB  1 
ATOM   2249 O OG1 . THR   B 1 76  ? -15.386 -0.740  -21.003 1.00 30.92 ? 55  THR   B OG1 1 
ATOM   2250 C CG2 . THR   B 1 76  ? -14.706 -3.038  -21.561 1.00 32.00 ? 55  THR   B CG2 1 
ATOM   2251 N N   . ALA   B 1 77  ? -18.674 -0.994  -19.504 1.00 31.84 ? 56  ALA   B N   1 
ATOM   2252 C CA  . ALA   B 1 77  ? -19.256 -0.206  -18.420 1.00 31.14 ? 56  ALA   B CA  1 
ATOM   2253 C C   . ALA   B 1 77  ? -20.766 -0.136  -18.603 1.00 30.32 ? 56  ALA   B C   1 
ATOM   2254 O O   . ALA   B 1 77  ? -21.242 0.137   -19.711 1.00 31.41 ? 56  ALA   B O   1 
ATOM   2255 C CB  . ALA   B 1 77  ? -18.678 1.206   -18.347 1.00 28.35 ? 56  ALA   B CB  1 
ATOM   2256 N N   . VAL   B 1 78  ? -21.508 -0.381  -17.507 1.00 28.78 ? 57  VAL   B N   1 
ATOM   2257 C CA  . VAL   B 1 78  ? -22.965 -0.262  -17.420 1.00 27.98 ? 57  VAL   B CA  1 
ATOM   2258 C C   . VAL   B 1 78  ? -23.318 0.562   -16.175 1.00 34.62 ? 57  VAL   B C   1 
ATOM   2259 O O   . VAL   B 1 78  ? -22.485 0.728   -15.271 1.00 32.66 ? 57  VAL   B O   1 
ATOM   2260 C CB  . VAL   B 1 78  ? -23.707 -1.624  -17.433 1.00 35.41 ? 57  VAL   B CB  1 
ATOM   2261 C CG1 . VAL   B 1 78  ? -23.451 -2.391  -18.729 1.00 28.86 ? 57  VAL   B CG1 1 
ATOM   2262 C CG2 . VAL   B 1 78  ? -23.371 -2.514  -16.218 1.00 28.80 ? 57  VAL   B CG2 1 
ATOM   2263 N N   . VAL   B 1 79  ? -24.526 1.144   -16.162 1.00 32.20 ? 58  VAL   B N   1 
ATOM   2264 C CA  . VAL   B 1 79  ? -25.053 1.847   -14.996 1.00 32.17 ? 58  VAL   B CA  1 
ATOM   2265 C C   . VAL   B 1 79  ? -26.137 0.998   -14.349 1.00 35.12 ? 58  VAL   B C   1 
ATOM   2266 O O   . VAL   B 1 79  ? -26.704 0.109   -14.989 1.00 36.01 ? 58  VAL   B O   1 
ATOM   2267 C CB  . VAL   B 1 79  ? -25.555 3.298   -15.176 1.00 29.36 ? 58  VAL   B CB  1 
ATOM   2268 C CG1 . VAL   B 1 79  ? -24.480 4.198   -15.765 1.00 29.26 ? 58  VAL   B CG1 1 
ATOM   2269 C CG2 . VAL   B 1 79  ? -26.855 3.344   -15.980 1.00 31.54 ? 58  VAL   B CG2 1 
ATOM   2270 N N   . CYS   B 1 80  ? -26.392 1.261   -13.052 1.00 29.70 ? 59  CYS   B N   1 
ATOM   2271 C CA  . CYS   B 1 80  ? -27.442 0.557   -12.326 1.00 30.84 ? 59  CYS   B CA  1 
ATOM   2272 C C   . CYS   B 1 80  ? -27.975 1.457   -11.210 1.00 32.50 ? 59  CYS   B C   1 
ATOM   2273 O O   . CYS   B 1 80  ? -27.241 1.776   -10.257 1.00 36.61 ? 59  CYS   B O   1 
ATOM   2274 C CB  . CYS   B 1 80  ? -26.861 -0.722  -11.734 1.00 32.78 ? 59  CYS   B CB  1 
ATOM   2275 S SG  . CYS   B 1 80  ? -28.055 -1.657  -10.750 1.00 41.76 ? 59  CYS   B SG  1 
ATOM   2276 N N   . GLN   B 1 81  ? -29.245 1.865   -11.302 1.00 26.62 ? 60  GLN   B N   1 
ATOM   2277 C CA  . GLN   B 1 81  ? -29.815 2.819   -10.347 1.00 29.99 ? 60  GLN   B CA  1 
ATOM   2278 C C   . GLN   B 1 81  ? -30.401 2.090   -9.139  1.00 33.88 ? 60  GLN   B C   1 
ATOM   2279 O O   . GLN   B 1 81  ? -31.036 1.051   -9.314  1.00 32.04 ? 60  GLN   B O   1 
ATOM   2280 C CB  . GLN   B 1 81  ? -30.852 3.712   -11.029 1.00 31.37 ? 60  GLN   B CB  1 
ATOM   2281 C CG  . GLN   B 1 81  ? -31.300 4.920   -10.218 1.00 30.75 ? 60  GLN   B CG  1 
ATOM   2282 C CD  . GLN   B 1 81  ? -32.286 4.613   -9.106  1.00 33.06 ? 60  GLN   B CD  1 
ATOM   2283 O OE1 . GLN   B 1 81  ? -32.981 3.580   -9.083  1.00 33.62 ? 60  GLN   B OE1 1 
ATOM   2284 N NE2 . GLN   B 1 81  ? -32.363 5.549   -8.174  1.00 31.79 ? 60  GLN   B NE2 1 
ATOM   2285 N N   . ALA   B 1 82  ? -30.142 2.585   -7.903  1.00 30.52 ? 61  ALA   B N   1 
ATOM   2286 C CA  . ALA   B 1 82  ? -30.860 2.078   -6.732  1.00 28.46 ? 61  ALA   B CA  1 
ATOM   2287 C C   . ALA   B 1 82  ? -30.737 3.021   -5.548  1.00 29.97 ? 61  ALA   B C   1 
ATOM   2288 O O   . ALA   B 1 82  ? -29.673 3.581   -5.303  1.00 27.72 ? 61  ALA   B O   1 
ATOM   2289 C CB  . ALA   B 1 82  ? -30.374 0.707   -6.311  1.00 27.84 ? 61  ALA   B CB  1 
ATOM   2290 N N   . ASP   B 1 83  ? -31.816 3.123   -4.769  1.00 28.04 ? 62  ASP   B N   1 
ATOM   2291 C CA  . ASP   B 1 83  ? -31.767 3.729   -3.458  1.00 29.06 ? 62  ASP   B CA  1 
ATOM   2292 C C   . ASP   B 1 83  ? -31.239 2.690   -2.464  1.00 29.57 ? 62  ASP   B C   1 
ATOM   2293 O O   . ASP   B 1 83  ? -31.720 1.554   -2.460  1.00 31.78 ? 62  ASP   B O   1 
ATOM   2294 C CB  . ASP   B 1 83  ? -33.177 4.148   -3.050  1.00 33.78 ? 62  ASP   B CB  1 
ATOM   2295 C CG  . ASP   B 1 83  ? -33.313 5.083   -1.860  1.00 37.57 ? 62  ASP   B CG  1 
ATOM   2296 O OD1 . ASP   B 1 83  ? -32.291 5.388   -1.205  1.00 37.27 ? 62  ASP   B OD1 1 
ATOM   2297 O OD2 . ASP   B 1 83  ? -34.464 5.495   -1.574  1.00 40.94 ? 62  ASP   B OD2 1 
ATOM   2298 N N   . LEU   B 1 84  ? -30.290 3.092   -1.587  1.00 27.57 ? 63  LEU   B N   1 
ATOM   2299 C CA  . LEU   B 1 84  ? -29.681 2.174   -0.618  1.00 25.44 ? 63  LEU   B CA  1 
ATOM   2300 C C   . LEU   B 1 84  ? -30.149 2.497   0.801   1.00 27.15 ? 63  LEU   B C   1 
ATOM   2301 O O   . LEU   B 1 84  ? -29.597 1.967   1.784   1.00 27.37 ? 63  LEU   B O   1 
ATOM   2302 C CB  . LEU   B 1 84  ? -28.154 2.163   -0.760  1.00 25.07 ? 63  LEU   B CB  1 
ATOM   2303 C CG  . LEU   B 1 84  ? -27.623 1.685   -2.113  1.00 25.87 ? 63  LEU   B CG  1 
ATOM   2304 C CD1 . LEU   B 1 84  ? -26.103 1.671   -2.160  1.00 29.03 ? 63  LEU   B CD1 1 
ATOM   2305 C CD2 . LEU   B 1 84  ? -28.147 0.280   -2.409  1.00 27.80 ? 63  LEU   B CD2 1 
ATOM   2306 N N   . THR   B 1 85  ? -31.218 3.299   0.904   1.00 26.70 ? 64  THR   B N   1 
ATOM   2307 C CA  . THR   B 1 85  ? -31.898 3.541   2.172   1.00 26.13 ? 64  THR   B CA  1 
ATOM   2308 C C   . THR   B 1 85  ? -32.465 2.224   2.714   1.00 31.37 ? 64  THR   B C   1 
ATOM   2309 O O   . THR   B 1 85  ? -32.971 1.402   1.946   1.00 29.11 ? 64  THR   B O   1 
ATOM   2310 C CB  . THR   B 1 85  ? -33.009 4.582   2.008   1.00 30.20 ? 64  THR   B CB  1 
ATOM   2311 O OG1 . THR   B 1 85  ? -32.433 5.719   1.372   1.00 36.56 ? 64  THR   B OG1 1 
ATOM   2312 C CG2 . THR   B 1 85  ? -33.581 5.070   3.328   1.00 26.82 ? 64  THR   B CG2 1 
ATOM   2313 N N   . ASN   B 1 86  ? -32.387 2.040   4.043   1.00 28.22 ? 65  ASN   B N   1 
ATOM   2314 C CA  . ASN   B 1 86  ? -32.921 0.843   4.681   1.00 31.39 ? 65  ASN   B CA  1 
ATOM   2315 C C   . ASN   B 1 86  ? -34.443 0.789   4.469   1.00 37.13 ? 65  ASN   B C   1 
ATOM   2316 O O   . ASN   B 1 86  ? -35.138 1.761   4.734   1.00 31.14 ? 65  ASN   B O   1 
ATOM   2317 C CB  . ASN   B 1 86  ? -32.672 0.854   6.178   1.00 31.92 ? 65  ASN   B CB  1 
ATOM   2318 C CG  . ASN   B 1 86  ? -33.036 -0.455  6.838   1.00 38.77 ? 65  ASN   B CG  1 
ATOM   2319 O OD1 . ASN   B 1 86  ? -33.502 -0.475  7.993   1.00 39.87 ? 65  ASN   B OD1 1 
ATOM   2320 N ND2 . ASN   B 1 86  ? -32.764 -1.542  6.138   1.00 31.99 ? 65  ASN   B ND2 1 
ATOM   2321 N N   . SER   B 1 87  ? -34.932 -0.353  3.961   1.00 36.48 ? 66  SER   B N   1 
ATOM   2322 C CA  . SER   B 1 87  ? -36.364 -0.628  3.874   1.00 38.73 ? 66  SER   B CA  1 
ATOM   2323 C C   . SER   B 1 87  ? -36.567 -2.126  3.674   1.00 39.96 ? 66  SER   B C   1 
ATOM   2324 O O   . SER   B 1 87  ? -35.594 -2.895  3.553   1.00 36.02 ? 66  SER   B O   1 
ATOM   2325 C CB  . SER   B 1 87  ? -37.018 0.125   2.758   1.00 32.15 ? 66  SER   B CB  1 
ATOM   2326 O OG  . SER   B 1 87  ? -36.672 -0.464  1.513   1.00 36.82 ? 66  SER   B OG  1 
ATOM   2327 N N   . ASN   B 1 88  ? -37.850 -2.509  3.579   1.00 36.40 ? 67  ASN   B N   1 
ATOM   2328 C CA  . ASN   B 1 88  ? -38.212 -3.896  3.327   1.00 43.27 ? 67  ASN   B CA  1 
ATOM   2329 C C   . ASN   B 1 88  ? -37.810 -4.350  1.920   1.00 33.97 ? 67  ASN   B C   1 
ATOM   2330 O O   . ASN   B 1 88  ? -37.647 -5.558  1.706   1.00 41.93 ? 67  ASN   B O   1 
ATOM   2331 C CB  . ASN   B 1 88  ? -39.606 -4.248  3.864   1.00 46.01 ? 67  ASN   B CB  1 
ATOM   2332 C CG  . ASN   B 1 88  ? -39.534 -4.885  5.236   0.70 48.92 ? 67  ASN   B CG  1 
ATOM   2333 O OD1 . ASN   B 1 88  ? -38.950 -4.317  6.166   0.70 41.97 ? 67  ASN   B OD1 1 
ATOM   2334 N ND2 . ASN   B 1 88  ? -40.078 -6.088  5.375   0.70 52.29 ? 67  ASN   B ND2 1 
ATOM   2335 N N   . VAL   B 1 89  ? -37.563 -3.409  0.989   1.00 35.11 ? 68  VAL   B N   1 
ATOM   2336 C CA  . VAL   B 1 89  ? -37.148 -3.774  -0.370  1.00 37.17 ? 68  VAL   B CA  1 
ATOM   2337 C C   . VAL   B 1 89  ? -35.629 -3.643  -0.568  1.00 32.55 ? 68  VAL   B C   1 
ATOM   2338 O O   . VAL   B 1 89  ? -35.126 -3.936  -1.650  1.00 33.03 ? 68  VAL   B O   1 
ATOM   2339 C CB  . VAL   B 1 89  ? -37.891 -3.079  -1.537  1.00 42.37 ? 68  VAL   B CB  1 
ATOM   2340 C CG1 . VAL   B 1 89  ? -39.412 -3.133  -1.360  1.00 44.18 ? 68  VAL   B CG1 1 
ATOM   2341 C CG2 . VAL   B 1 89  ? -37.435 -1.638  -1.774  1.00 37.08 ? 68  VAL   B CG2 1 
ATOM   2342 N N   . LEU   B 1 90  ? -34.887 -3.209  0.471   1.00 32.68 ? 69  LEU   B N   1 
ATOM   2343 C CA  . LEU   B 1 90  ? -33.440 -3.038  0.305   1.00 26.63 ? 69  LEU   B CA  1 
ATOM   2344 C C   . LEU   B 1 90  ? -32.781 -4.349  -0.121  1.00 25.07 ? 69  LEU   B C   1 
ATOM   2345 O O   . LEU   B 1 90  ? -31.951 -4.356  -1.025  1.00 30.60 ? 69  LEU   B O   1 
ATOM   2346 C CB  . LEU   B 1 90  ? -32.746 -2.355  1.494   1.00 25.85 ? 69  LEU   B CB  1 
ATOM   2347 C CG  . LEU   B 1 90  ? -31.237 -2.110  1.314   1.00 26.60 ? 69  LEU   B CG  1 
ATOM   2348 C CD1 . LEU   B 1 90  ? -30.990 -1.170  0.134   1.00 27.28 ? 69  LEU   B CD1 1 
ATOM   2349 C CD2 . LEU   B 1 90  ? -30.672 -1.539  2.629   1.00 29.68 ? 69  LEU   B CD2 1 
ATOM   2350 N N   . PRO   B 1 91  ? -33.107 -5.508  0.487   1.00 27.90 ? 70  PRO   B N   1 
ATOM   2351 C CA  . PRO   B 1 91  ? -32.453 -6.748  0.078   1.00 29.04 ? 70  PRO   B CA  1 
ATOM   2352 C C   . PRO   B 1 91  ? -32.604 -7.045  -1.402  1.00 31.24 ? 70  PRO   B C   1 
ATOM   2353 O O   . PRO   B 1 91  ? -31.624 -7.400  -2.070  1.00 30.02 ? 70  PRO   B O   1 
ATOM   2354 C CB  . PRO   B 1 91  ? -33.090 -7.802  1.011   1.00 29.14 ? 70  PRO   B CB  1 
ATOM   2355 C CG  . PRO   B 1 91  ? -33.431 -6.979  2.220   1.00 27.16 ? 70  PRO   B CG  1 
ATOM   2356 C CD  . PRO   B 1 91  ? -33.968 -5.672  1.674   1.00 27.82 ? 70  PRO   B CD  1 
ATOM   2357 N N   . ALA   B 1 92  ? -33.826 -6.846  -1.925  1.00 33.85 ? 71  ALA   B N   1 
ATOM   2358 C CA  . ALA   B 1 92  ? -34.050 -7.142  -3.331  1.00 30.60 ? 71  ALA   B CA  1 
ATOM   2359 C C   . ALA   B 1 92  ? -33.237 -6.182  -4.207  1.00 30.51 ? 71  ALA   B C   1 
ATOM   2360 O O   . ALA   B 1 92  ? -32.662 -6.611  -5.215  1.00 32.36 ? 71  ALA   B O   1 
ATOM   2361 C CB  . ALA   B 1 92  ? -35.540 -7.079  -3.653  1.00 30.61 ? 71  ALA   B CB  1 
ATOM   2362 N N   . SER   B 1 93  ? -33.187 -4.894  -3.821  1.00 32.90 ? 72  SER   B N   1 
ATOM   2363 C CA  . SER   B 1 93  ? -32.364 -3.899  -4.504  1.00 31.37 ? 72  SER   B CA  1 
ATOM   2364 C C   . SER   B 1 93  ? -30.910 -4.354  -4.580  1.00 29.16 ? 72  SER   B C   1 
ATOM   2365 O O   . SER   B 1 93  ? -30.253 -4.233  -5.627  1.00 29.11 ? 72  SER   B O   1 
ATOM   2366 C CB  . SER   B 1 93  ? -32.442 -2.548  -3.861  1.00 31.85 ? 72  SER   B CB  1 
ATOM   2367 O OG  . SER   B 1 93  ? -33.749 -2.014  -3.985  1.00 35.29 ? 72  SER   B OG  1 
ATOM   2368 N N   . CYS   B 1 94  ? -30.379 -4.819  -3.445  1.00 30.98 ? 73  CYS   B N   1 
ATOM   2369 C CA  . CYS   B 1 94  ? -28.959 -5.188  -3.400  1.00 27.86 ? 73  CYS   B CA  1 
ATOM   2370 C C   . CYS   B 1 94  ? -28.716 -6.416  -4.275  1.00 26.32 ? 73  CYS   B C   1 
ATOM   2371 O O   . CYS   B 1 94  ? -27.752 -6.485  -5.030  1.00 28.17 ? 73  CYS   B O   1 
ATOM   2372 C CB  . CYS   B 1 94  ? -28.481 -5.319  -1.952  1.00 25.05 ? 73  CYS   B CB  1 
ATOM   2373 S SG  . CYS   B 1 94  ? -28.496 -3.708  -1.121  1.00 28.79 ? 73  CYS   B SG  1 
ATOM   2374 N N   . GLU   B 1 95  ? -29.603 -7.391  -4.195  1.00 30.04 ? 74  GLU   B N   1 
ATOM   2375 C CA  . GLU   B 1 95  ? -29.493 -8.558  -5.060  1.00 33.22 ? 74  GLU   B CA  1 
ATOM   2376 C C   . GLU   B 1 95  ? -29.463 -8.161  -6.536  1.00 28.78 ? 74  GLU   B C   1 
ATOM   2377 O O   . GLU   B 1 95  ? -28.693 -8.726  -7.320  1.00 33.78 ? 74  GLU   B O   1 
ATOM   2378 C CB  . GLU   B 1 95  ? -30.622 -9.531  -4.720  1.00 36.66 ? 74  GLU   B CB  1 
ATOM   2379 C CG  . GLU   B 1 95  ? -30.442 -10.901 -5.383  1.00 42.41 ? 74  GLU   B CG  1 
ATOM   2380 C CD  . GLU   B 1 95  ? -31.614 -11.787 -4.998  0.70 47.27 ? 74  GLU   B CD  1 
ATOM   2381 O OE1 . GLU   B 1 95  ? -32.763 -11.404 -5.296  0.70 50.83 ? 74  GLU   B OE1 1 
ATOM   2382 O OE2 . GLU   B 1 95  ? -31.395 -12.834 -4.361  0.70 50.25 ? 74  GLU   B OE2 1 
ATOM   2383 N N   . GLU   B 1 96  ? -30.308 -7.203  -6.908  1.00 32.19 ? 75  GLU   B N   1 
ATOM   2384 C CA  . GLU   B 1 96  ? -30.414 -6.712  -8.276  1.00 36.78 ? 75  GLU   B CA  1 
ATOM   2385 C C   . GLU   B 1 96  ? -29.130 -6.013  -8.717  1.00 38.76 ? 75  GLU   B C   1 
ATOM   2386 O O   . GLU   B 1 96  ? -28.713 -6.127  -9.872  1.00 32.15 ? 75  GLU   B O   1 
ATOM   2387 C CB  . GLU   B 1 96  ? -31.622 -5.789  -8.450  1.00 37.21 ? 75  GLU   B CB  1 
ATOM   2388 C CG  . GLU   B 1 96  ? -32.729 -6.462  -9.250  0.70 44.34 ? 75  GLU   B CG  1 
ATOM   2389 C CD  . GLU   B 1 96  ? -32.162 -6.754  -10.630 0.70 43.29 ? 75  GLU   B CD  1 
ATOM   2390 O OE1 . GLU   B 1 96  ? -32.045 -7.947  -10.961 0.70 38.23 ? 75  GLU   B OE1 1 
ATOM   2391 O OE2 . GLU   B 1 96  ? -31.777 -5.797  -11.345 0.70 47.30 ? 75  GLU   B OE2 1 
ATOM   2392 N N   . ILE   B 1 97  ? -28.502 -5.283  -7.793  1.00 29.70 ? 76  ILE   B N   1 
ATOM   2393 C CA  . ILE   B 1 97  ? -27.261 -4.619  -8.145  1.00 27.57 ? 76  ILE   B CA  1 
ATOM   2394 C C   . ILE   B 1 97  ? -26.207 -5.640  -8.549  1.00 25.64 ? 76  ILE   B C   1 
ATOM   2395 O O   . ILE   B 1 97  ? -25.502 -5.439  -9.555  1.00 31.08 ? 76  ILE   B O   1 
ATOM   2396 C CB  . ILE   B 1 97  ? -26.755 -3.708  -7.006  1.00 26.03 ? 76  ILE   B CB  1 
ATOM   2397 C CG1 . ILE   B 1 97  ? -27.665 -2.509  -6.852  1.00 27.93 ? 76  ILE   B CG1 1 
ATOM   2398 C CG2 . ILE   B 1 97  ? -25.309 -3.300  -7.291  1.00 27.05 ? 76  ILE   B CG2 1 
ATOM   2399 C CD1 . ILE   B 1 97  ? -27.517 -1.770  -5.530  1.00 28.15 ? 76  ILE   B CD1 1 
ATOM   2400 N N   . ILE   B 1 98  ? -26.043 -6.689  -7.717  1.00 28.66 ? 77  ILE   B N   1 
ATOM   2401 C CA  . ILE   B 1 98  ? -25.086 -7.748  -7.985  1.00 29.20 ? 77  ILE   B CA  1 
ATOM   2402 C C   . ILE   B 1 98  ? -25.463 -8.495  -9.280  1.00 29.53 ? 77  ILE   B C   1 
ATOM   2403 O O   . ILE   B 1 98  ? -24.603 -8.729  -10.127 1.00 27.96 ? 77  ILE   B O   1 
ATOM   2404 C CB  . ILE   B 1 98  ? -24.900 -8.684  -6.770  1.00 28.13 ? 77  ILE   B CB  1 
ATOM   2405 C CG1 . ILE   B 1 98  ? -24.359 -7.901  -5.510  1.00 29.27 ? 77  ILE   B CG1 1 
ATOM   2406 C CG2 . ILE   B 1 98  ? -24.051 -9.903  -7.142  1.00 27.16 ? 77  ILE   B CG2 1 
ATOM   2407 C CD1 . ILE   B 1 98  ? -23.112 -7.057  -5.749  1.00 27.27 ? 77  ILE   B CD1 1 
ATOM   2408 N N   . ASN   B 1 99  ? -26.732 -8.896  -9.384  1.00 30.91 ? 78  ASN   B N   1 
ATOM   2409 C CA  . ASN   B 1 99  ? -27.281 -9.525  -10.579 1.00 34.08 ? 78  ASN   B CA  1 
ATOM   2410 C C   . ASN   B 1 99  ? -26.930 -8.713  -11.831 1.00 33.49 ? 78  ASN   B C   1 
ATOM   2411 O O   . ASN   B 1 99  ? -26.550 -9.317  -12.831 1.00 34.24 ? 78  ASN   B O   1 
ATOM   2412 C CB  . ASN   B 1 99  ? -28.780 -9.787  -10.452 1.00 35.65 ? 78  ASN   B CB  1 
ATOM   2413 C CG  . ASN   B 1 99  ? -29.085 -11.049 -9.677  1.00 47.00 ? 78  ASN   B CG  1 
ATOM   2414 O OD1 . ASN   B 1 99  ? -28.216 -11.922 -9.500  1.00 48.28 ? 78  ASN   B OD1 1 
ATOM   2415 N ND2 . ASN   B 1 99  ? -30.323 -11.165 -9.215  1.00 48.96 ? 78  ASN   B ND2 1 
ATOM   2416 N N   . SER   B 1 100 ? -26.977 -7.363  -11.754 1.00 31.88 ? 79  SER   B N   1 
ATOM   2417 C CA  A SER   B 1 100 ? -26.713 -6.503  -12.898 0.70 33.05 ? 79  SER   B CA  1 
ATOM   2418 C CA  B SER   B 1 100 ? -26.725 -6.525  -12.913 0.30 31.89 ? 79  SER   B CA  1 
ATOM   2419 C C   . SER   B 1 100 ? -25.305 -6.727  -13.435 1.00 36.98 ? 79  SER   B C   1 
ATOM   2420 O O   . SER   B 1 100 ? -25.083 -6.642  -14.645 1.00 35.37 ? 79  SER   B O   1 
ATOM   2421 C CB  A SER   B 1 100 ? -26.926 -5.048  -12.595 0.70 36.78 ? 79  SER   B CB  1 
ATOM   2422 C CB  B SER   B 1 100 ? -27.033 -5.076  -12.649 0.30 30.91 ? 79  SER   B CB  1 
ATOM   2423 O OG  A SER   B 1 100 ? -25.735 -4.473  -12.070 0.70 37.88 ? 79  SER   B OG  1 
ATOM   2424 O OG  B SER   B 1 100 ? -28.423 -4.894  -12.413 0.30 26.56 ? 79  SER   B OG  1 
ATOM   2425 N N   . CYS   B 1 101 ? -24.338 -6.977  -12.526 1.00 29.67 ? 80  CYS   B N   1 
ATOM   2426 C CA  . CYS   B 1 101 ? -22.964 -7.195  -12.951 1.00 29.31 ? 80  CYS   B CA  1 
ATOM   2427 C C   . CYS   B 1 101 ? -22.908 -8.539  -13.684 1.00 30.28 ? 80  CYS   B C   1 
ATOM   2428 O O   . CYS   B 1 101 ? -22.202 -8.677  -14.693 1.00 32.95 ? 80  CYS   B O   1 
ATOM   2429 C CB  . CYS   B 1 101 ? -22.020 -7.182  -11.728 1.00 23.82 ? 80  CYS   B CB  1 
ATOM   2430 S SG  . CYS   B 1 101 ? -20.280 -7.095  -12.166 1.00 29.88 ? 80  CYS   B SG  1 
ATOM   2431 N N   . PHE   B 1 102 ? -23.637 -9.538  -13.153 1.00 33.79 ? 81  PHE   B N   1 
ATOM   2432 C CA  . PHE   B 1 102 ? -23.563 -10.872 -13.738 1.00 38.56 ? 81  PHE   B CA  1 
ATOM   2433 C C   . PHE   B 1 102 ? -24.213 -10.855 -15.126 1.00 43.66 ? 81  PHE   B C   1 
ATOM   2434 O O   . PHE   B 1 102 ? -23.638 -11.408 -16.062 1.00 40.94 ? 81  PHE   B O   1 
ATOM   2435 C CB  . PHE   B 1 102 ? -24.194 -11.984 -12.898 1.00 34.36 ? 81  PHE   B CB  1 
ATOM   2436 C CG  . PHE   B 1 102 ? -23.250 -12.451 -11.800 1.00 37.04 ? 81  PHE   B CG  1 
ATOM   2437 C CD1 . PHE   B 1 102 ? -22.289 -13.431 -12.056 1.00 37.40 ? 81  PHE   B CD1 1 
ATOM   2438 C CD2 . PHE   B 1 102 ? -23.288 -11.864 -10.535 1.00 39.39 ? 81  PHE   B CD2 1 
ATOM   2439 C CE1 . PHE   B 1 102 ? -21.428 -13.874 -11.046 1.00 40.14 ? 81  PHE   B CE1 1 
ATOM   2440 C CE2 . PHE   B 1 102 ? -22.419 -12.297 -9.533  1.00 39.65 ? 81  PHE   B CE2 1 
ATOM   2441 C CZ  . PHE   B 1 102 ? -21.475 -13.288 -9.790  1.00 39.62 ? 81  PHE   B CZ  1 
ATOM   2442 N N   . ARG   B 1 103 ? -25.373 -10.184 -15.232 1.00 36.94 ? 82  ARG   B N   1 
ATOM   2443 C CA  . ARG   B 1 103 ? -26.101 -10.054 -16.496 1.00 40.57 ? 82  ARG   B CA  1 
ATOM   2444 C C   . ARG   B 1 103 ? -25.219 -9.381  -17.544 1.00 44.28 ? 82  ARG   B C   1 
ATOM   2445 O O   . ARG   B 1 103 ? -25.160 -9.834  -18.688 1.00 45.90 ? 82  ARG   B O   1 
ATOM   2446 C CB  . ARG   B 1 103 ? -27.449 -9.338  -16.366 1.00 35.75 ? 82  ARG   B CB  1 
ATOM   2447 C CG  . ARG   B 1 103 ? -28.463 -10.172 -15.595 1.00 39.96 ? 82  ARG   B CG  1 
ATOM   2448 C CD  . ARG   B 1 103 ? -29.891 -9.595  -15.600 1.00 44.42 ? 82  ARG   B CD  1 
ATOM   2449 N N   . ALA   B 1 104 ? -24.495 -8.328  -17.147 1.00 35.96 ? 83  ALA   B N   1 
ATOM   2450 C CA  . ALA   B 1 104 ? -23.672 -7.617  -18.112 1.00 32.55 ? 83  ALA   B CA  1 
ATOM   2451 C C   . ALA   B 1 104 ? -22.381 -8.353  -18.451 1.00 38.49 ? 83  ALA   B C   1 
ATOM   2452 O O   . ALA   B 1 104 ? -21.960 -8.303  -19.605 1.00 34.84 ? 83  ALA   B O   1 
ATOM   2453 C CB  . ALA   B 1 104 ? -23.403 -6.198  -17.664 1.00 34.93 ? 83  ALA   B CB  1 
ATOM   2454 N N   . PHE   B 1 105 ? -21.712 -9.005  -17.481 1.00 30.10 ? 84  PHE   B N   1 
ATOM   2455 C CA  . PHE   B 1 105 ? -20.304 -9.311  -17.707 1.00 30.80 ? 84  PHE   B CA  1 
ATOM   2456 C C   . PHE   B 1 105 ? -20.021 -10.785 -17.445 1.00 24.47 ? 84  PHE   B C   1 
ATOM   2457 O O   . PHE   B 1 105 ? -18.916 -11.239 -17.700 1.00 35.57 ? 84  PHE   B O   1 
ATOM   2458 C CB  . PHE   B 1 105 ? -19.382 -8.400  -16.872 1.00 32.46 ? 84  PHE   B CB  1 
ATOM   2459 C CG  . PHE   B 1 105 ? -19.554 -6.902  -17.106 1.00 36.68 ? 84  PHE   B CG  1 
ATOM   2460 C CD1 . PHE   B 1 105 ? -19.494 -6.359  -18.395 1.00 31.38 ? 84  PHE   B CD1 1 
ATOM   2461 C CD2 . PHE   B 1 105 ? -19.786 -6.035  -16.035 1.00 38.45 ? 84  PHE   B CD2 1 
ATOM   2462 C CE1 . PHE   B 1 105 ? -19.649 -4.994  -18.604 1.00 36.70 ? 84  PHE   B CE1 1 
ATOM   2463 C CE2 . PHE   B 1 105 ? -19.945 -4.670  -16.246 1.00 35.32 ? 84  PHE   B CE2 1 
ATOM   2464 C CZ  . PHE   B 1 105 ? -19.894 -4.152  -17.526 1.00 37.58 ? 84  PHE   B CZ  1 
ATOM   2465 N N   . GLY   B 1 106 ? -20.999 -11.490 -16.875 1.00 27.86 ? 85  GLY   B N   1 
ATOM   2466 C CA  . GLY   B 1 106 ? -20.880 -12.930 -16.704 1.00 29.87 ? 85  GLY   B CA  1 
ATOM   2467 C C   . GLY   B 1 106 ? -20.134 -13.305 -15.423 1.00 31.74 ? 85  GLY   B C   1 
ATOM   2468 O O   . GLY   B 1 106 ? -19.876 -14.473 -15.184 1.00 33.13 ? 85  GLY   B O   1 
ATOM   2469 N N   . ARG   B 1 107 ? -19.823 -12.320 -14.568 1.00 35.61 ? 86  ARG   B N   1 
ATOM   2470 C CA  . ARG   B 1 107 ? -18.998 -12.568 -13.382 1.00 28.52 ? 86  ARG   B CA  1 
ATOM   2471 C C   . ARG   B 1 107 ? -19.015 -11.296 -12.531 1.00 34.12 ? 86  ARG   B C   1 
ATOM   2472 O O   . ARG   B 1 107 ? -19.390 -10.227 -13.036 1.00 28.63 ? 86  ARG   B O   1 
ATOM   2473 C CB  . ARG   B 1 107 ? -17.553 -12.832 -13.824 1.00 31.45 ? 86  ARG   B CB  1 
ATOM   2474 C CG  . ARG   B 1 107 ? -16.939 -11.758 -14.714 1.00 30.76 ? 86  ARG   B CG  1 
ATOM   2475 C CD  . ARG   B 1 107 ? -15.562 -12.150 -15.191 1.00 33.94 ? 86  ARG   B CD  1 
ATOM   2476 N NE  . ARG   B 1 107 ? -14.574 -12.565 -14.188 1.00 33.93 ? 86  ARG   B NE  1 
ATOM   2477 C CZ  . ARG   B 1 107 ? -13.385 -13.053 -14.476 1.00 39.99 ? 86  ARG   B CZ  1 
ATOM   2478 N NH1 . ARG   B 1 107 ? -13.128 -13.467 -15.718 1.00 41.24 ? 86  ARG   B NH1 1 
ATOM   2479 N NH2 . ARG   B 1 107 ? -12.468 -13.161 -13.528 1.00 33.77 ? 86  ARG   B NH2 1 
ATOM   2480 N N   . CYS   B 1 108 ? -18.658 -11.426 -11.237 1.00 31.33 ? 87  CYS   B N   1 
ATOM   2481 C CA  . CYS   B 1 108 ? -18.508 -10.255 -10.364 1.00 29.96 ? 87  CYS   B CA  1 
ATOM   2482 C C   . CYS   B 1 108 ? -17.342 -10.524 -9.410  1.00 25.58 ? 87  CYS   B C   1 
ATOM   2483 O O   . CYS   B 1 108 ? -17.472 -11.369 -8.525  1.00 29.72 ? 87  CYS   B O   1 
ATOM   2484 C CB  . CYS   B 1 108 ? -19.793 -9.969  -9.597  1.00 29.84 ? 87  CYS   B CB  1 
ATOM   2485 S SG  . CYS   B 1 108 ? -19.693 -8.469  -8.568  1.00 30.81 ? 87  CYS   B SG  1 
ATOM   2486 N N   . ASP   B 1 109 ? -16.193 -9.880  -9.674  1.00 23.97 ? 88  ASP   B N   1 
ATOM   2487 C CA  . ASP   B 1 109 ? -14.928 -10.179 -9.026  1.00 24.76 ? 88  ASP   B CA  1 
ATOM   2488 C C   . ASP   B 1 109 ? -14.747 -9.260  -7.813  1.00 24.92 ? 88  ASP   B C   1 
ATOM   2489 O O   . ASP   B 1 109 ? -14.127 -9.659  -6.836  1.00 25.06 ? 88  ASP   B O   1 
ATOM   2490 C CB  . ASP   B 1 109 ? -13.760 -10.053 -9.984  1.00 28.15 ? 88  ASP   B CB  1 
ATOM   2491 C CG  . ASP   B 1 109 ? -13.934 -10.955 -11.195 1.00 33.48 ? 88  ASP   B CG  1 
ATOM   2492 O OD1 . ASP   B 1 109 ? -13.601 -12.134 -11.068 1.00 32.05 ? 88  ASP   B OD1 1 
ATOM   2493 O OD2 . ASP   B 1 109 ? -14.538 -10.500 -12.187 1.00 32.79 ? 88  ASP   B OD2 1 
ATOM   2494 N N   . VAL   B 1 110 ? -15.240 -8.028  -7.931  1.00 23.48 ? 89  VAL   B N   1 
ATOM   2495 C CA  . VAL   B 1 110 ? -14.916 -6.981  -6.952  1.00 26.51 ? 89  VAL   B CA  1 
ATOM   2496 C C   . VAL   B 1 110 ? -16.201 -6.230  -6.608  1.00 25.20 ? 89  VAL   B C   1 
ATOM   2497 O O   . VAL   B 1 110 ? -16.981 -5.888  -7.501  1.00 23.96 ? 89  VAL   B O   1 
ATOM   2498 C CB  . VAL   B 1 110 ? -13.842 -5.996  -7.456  1.00 22.10 ? 89  VAL   B CB  1 
ATOM   2499 C CG1 . VAL   B 1 110 ? -13.778 -4.685  -6.627  1.00 23.34 ? 89  VAL   B CG1 1 
ATOM   2500 C CG2 . VAL   B 1 110 ? -12.469 -6.646  -7.607  1.00 22.62 ? 89  VAL   B CG2 1 
ATOM   2501 N N   . LEU   B 1 111 ? -16.381 -5.926  -5.308  1.00 22.53 ? 90  LEU   B N   1 
ATOM   2502 C CA  . LEU   B 1 111 ? -17.458 -5.077  -4.831  1.00 20.62 ? 90  LEU   B CA  1 
ATOM   2503 C C   . LEU   B 1 111 ? -16.820 -3.941  -4.021  1.00 22.54 ? 90  LEU   B C   1 
ATOM   2504 O O   . LEU   B 1 111 ? -16.058 -4.206  -3.093  1.00 20.75 ? 90  LEU   B O   1 
ATOM   2505 C CB  . LEU   B 1 111 ? -18.443 -5.873  -3.973  1.00 21.24 ? 90  LEU   B CB  1 
ATOM   2506 C CG  . LEU   B 1 111 ? -19.425 -5.015  -3.154  1.00 20.75 ? 90  LEU   B CG  1 
ATOM   2507 C CD1 . LEU   B 1 111 ? -20.392 -4.217  -4.020  1.00 21.38 ? 90  LEU   B CD1 1 
ATOM   2508 C CD2 . LEU   B 1 111 ? -20.184 -5.984  -2.225  1.00 22.36 ? 90  LEU   B CD2 1 
ATOM   2509 N N   . VAL   B 1 112 ? -17.163 -2.706  -4.380  1.00 19.73 ? 91  VAL   B N   1 
ATOM   2510 C CA  . VAL   B 1 112 ? -16.701 -1.528  -3.653  1.00 20.38 ? 91  VAL   B CA  1 
ATOM   2511 C C   . VAL   B 1 112 ? -17.908 -0.832  -3.045  1.00 20.20 ? 91  VAL   B C   1 
ATOM   2512 O O   . VAL   B 1 112 ? -18.748 -0.230  -3.750  1.00 21.18 ? 91  VAL   B O   1 
ATOM   2513 C CB  . VAL   B 1 112 ? -15.862 -0.553  -4.505  1.00 21.55 ? 91  VAL   B CB  1 
ATOM   2514 C CG1 . VAL   B 1 112 ? -15.406 0.629   -3.654  1.00 21.92 ? 91  VAL   B CG1 1 
ATOM   2515 C CG2 . VAL   B 1 112 ? -14.657 -1.220  -5.173  1.00 19.60 ? 91  VAL   B CG2 1 
ATOM   2516 N N   . ASN   B 1 113 ? -18.000 -0.921  -1.699  1.00 20.36 ? 92  ASN   B N   1 
ATOM   2517 C CA  . ASN   B 1 113 ? -19.076 -0.282  -0.964  1.00 20.20 ? 92  ASN   B CA  1 
ATOM   2518 C C   . ASN   B 1 113 ? -18.665 1.157   -0.652  1.00 21.97 ? 92  ASN   B C   1 
ATOM   2519 O O   . ASN   B 1 113 ? -18.010 1.411   0.369   1.00 19.65 ? 92  ASN   B O   1 
ATOM   2520 C CB  . ASN   B 1 113 ? -19.422 -1.065  0.302   1.00 21.25 ? 92  ASN   B CB  1 
ATOM   2521 C CG  . ASN   B 1 113 ? -20.153 -2.355  0.007   1.00 23.65 ? 92  ASN   B CG  1 
ATOM   2522 O OD1 . ASN   B 1 113 ? -21.146 -2.307  -0.720  1.00 23.38 ? 92  ASN   B OD1 1 
ATOM   2523 N ND2 . ASN   B 1 113 ? -19.706 -3.498  0.515   1.00 22.02 ? 92  ASN   B ND2 1 
ATOM   2524 N N   . ASN   B 1 114 ? -19.042 2.089   -1.542  1.00 24.28 ? 93  ASN   B N   1 
ATOM   2525 C CA  . ASN   B 1 114 ? -18.620 3.488   -1.520  1.00 23.12 ? 93  ASN   B CA  1 
ATOM   2526 C C   . ASN   B 1 114 ? -19.786 4.428   -1.180  1.00 22.96 ? 93  ASN   B C   1 
ATOM   2527 O O   . ASN   B 1 114 ? -19.567 5.435   -0.498  1.00 23.84 ? 93  ASN   B O   1 
ATOM   2528 C CB  . ASN   B 1 114 ? -17.892 3.893   -2.820  1.00 25.03 ? 93  ASN   B CB  1 
ATOM   2529 C CG  . ASN   B 1 114 ? -17.705 5.392   -2.959  1.00 24.63 ? 93  ASN   B CG  1 
ATOM   2530 O OD1 . ASN   B 1 114 ? -16.733 5.963   -2.428  1.00 22.83 ? 93  ASN   B OD1 1 
ATOM   2531 N ND2 . ASN   B 1 114 ? -18.630 6.065   -3.634  1.00 21.18 ? 93  ASN   B ND2 1 
ATOM   2532 N N   . ALA   B 1 115 ? -21.026 4.154   -1.650  1.00 22.00 ? 94  ALA   B N   1 
ATOM   2533 C CA  . ALA   B 1 115 ? -22.148 5.054   -1.461  1.00 22.11 ? 94  ALA   B CA  1 
ATOM   2534 C C   . ALA   B 1 115 ? -22.324 5.360   0.031   1.00 22.24 ? 94  ALA   B C   1 
ATOM   2535 O O   . ALA   B 1 115 ? -22.215 4.459   0.874   1.00 24.35 ? 94  ALA   B O   1 
ATOM   2536 C CB  . ALA   B 1 115 ? -23.433 4.463   -2.019  1.00 22.53 ? 94  ALA   B CB  1 
ATOM   2537 N N   . SER   B 1 116 ? -22.654 6.611   0.360   1.00 22.34 ? 95  SER   B N   1 
ATOM   2538 C CA  . SER   B 1 116 ? -22.746 6.999   1.767   1.00 21.97 ? 95  SER   B CA  1 
ATOM   2539 C C   . SER   B 1 116 ? -23.608 8.246   1.921   1.00 25.59 ? 95  SER   B C   1 
ATOM   2540 O O   . SER   B 1 116 ? -23.339 9.232   1.245   1.00 28.07 ? 95  SER   B O   1 
ATOM   2541 C CB  . SER   B 1 116 ? -21.341 7.336   2.292   1.00 22.89 ? 95  SER   B CB  1 
ATOM   2542 O OG  . SER   B 1 116 ? -21.401 7.839   3.634   1.00 25.81 ? 95  SER   B OG  1 
ATOM   2543 N N   . ALA   B 1 117 ? -24.560 8.237   2.873   1.00 25.30 ? 96  ALA   B N   1 
ATOM   2544 C CA  . ALA   B 1 117 ? -25.272 9.449   3.277   1.00 22.60 ? 96  ALA   B CA  1 
ATOM   2545 C C   . ALA   B 1 117 ? -24.488 10.075  4.429   1.00 23.26 ? 96  ALA   B C   1 
ATOM   2546 O O   . ALA   B 1 117 ? -23.920 9.367   5.246   1.00 23.31 ? 96  ALA   B O   1 
ATOM   2547 C CB  . ALA   B 1 117 ? -26.710 9.107   3.730   1.00 21.87 ? 96  ALA   B CB  1 
ATOM   2548 N N   . PHE   B 1 118 ? -24.485 11.409  4.531   1.00 21.43 ? 97  PHE   B N   1 
ATOM   2549 C CA  . PHE   B 1 118 ? -23.694 12.080  5.539   1.00 22.25 ? 97  PHE   B CA  1 
ATOM   2550 C C   . PHE   B 1 118 ? -24.386 13.406  5.846   1.00 24.61 ? 97  PHE   B C   1 
ATOM   2551 O O   . PHE   B 1 118 ? -24.432 14.275  4.988   1.00 26.54 ? 97  PHE   B O   1 
ATOM   2552 C CB  . PHE   B 1 118 ? -22.270 12.370  5.049   1.00 28.82 ? 97  PHE   B CB  1 
ATOM   2553 C CG  . PHE   B 1 118 ? -21.402 13.206  5.983   1.00 27.44 ? 97  PHE   B CG  1 
ATOM   2554 C CD1 . PHE   B 1 118 ? -20.692 12.612  7.040   1.00 27.03 ? 97  PHE   B CD1 1 
ATOM   2555 C CD2 . PHE   B 1 118 ? -21.308 14.587  5.806   1.00 33.71 ? 97  PHE   B CD2 1 
ATOM   2556 C CE1 . PHE   B 1 118 ? -19.896 13.370  7.892   1.00 26.92 ? 97  PHE   B CE1 1 
ATOM   2557 C CE2 . PHE   B 1 118 ? -20.505 15.353  6.646   1.00 33.37 ? 97  PHE   B CE2 1 
ATOM   2558 C CZ  . PHE   B 1 118 ? -19.807 14.742  7.689   1.00 32.15 ? 97  PHE   B CZ  1 
ATOM   2559 N N   . TYR   B 1 119 ? -24.870 13.551  7.077   1.00 23.69 ? 98  TYR   B N   1 
ATOM   2560 C CA  . TYR   B 1 119 ? -25.435 14.810  7.540   1.00 24.70 ? 98  TYR   B CA  1 
ATOM   2561 C C   . TYR   B 1 119 ? -25.658 14.669  9.039   1.00 25.49 ? 98  TYR   B C   1 
ATOM   2562 O O   . TYR   B 1 119 ? -25.638 13.562  9.547   1.00 24.23 ? 98  TYR   B O   1 
ATOM   2563 C CB  . TYR   B 1 119 ? -26.746 15.196  6.829   1.00 27.37 ? 98  TYR   B CB  1 
ATOM   2564 C CG  . TYR   B 1 119 ? -27.807 14.095  6.798   1.00 28.06 ? 98  TYR   B CG  1 
ATOM   2565 C CD1 . TYR   B 1 119 ? -28.625 13.864  7.896   1.00 25.06 ? 98  TYR   B CD1 1 
ATOM   2566 C CD2 . TYR   B 1 119 ? -27.947 13.263  5.683   1.00 27.50 ? 98  TYR   B CD2 1 
ATOM   2567 C CE1 . TYR   B 1 119 ? -29.588 12.863  7.853   1.00 29.38 ? 98  TYR   B CE1 1 
ATOM   2568 C CE2 . TYR   B 1 119 ? -28.921 12.277  5.626   1.00 25.42 ? 98  TYR   B CE2 1 
ATOM   2569 C CZ  . TYR   B 1 119 ? -29.732 12.068  6.730   1.00 24.22 ? 98  TYR   B CZ  1 
ATOM   2570 O OH  . TYR   B 1 119 ? -30.723 11.117  6.703   1.00 27.97 ? 98  TYR   B OH  1 
ATOM   2571 N N   . PRO   B 1 120 ? -25.790 15.788  9.786   1.00 27.85 ? 99  PRO   B N   1 
ATOM   2572 C CA  . PRO   B 1 120 ? -25.877 15.751  11.247  1.00 27.01 ? 99  PRO   B CA  1 
ATOM   2573 C C   . PRO   B 1 120 ? -27.239 15.227  11.680  1.00 26.98 ? 99  PRO   B C   1 
ATOM   2574 O O   . PRO   B 1 120 ? -28.224 15.371  10.935  1.00 28.08 ? 99  PRO   B O   1 
ATOM   2575 C CB  . PRO   B 1 120 ? -25.645 17.191  11.711  1.00 32.56 ? 99  PRO   B CB  1 
ATOM   2576 C CG  . PRO   B 1 120 ? -25.824 18.042  10.474  1.00 31.46 ? 99  PRO   B CG  1 
ATOM   2577 C CD  . PRO   B 1 120 ? -25.783 17.162  9.241   1.00 29.55 ? 99  PRO   B CD  1 
ATOM   2578 N N   . THR   B 1 121 ? -27.244 14.533  12.827  1.00 24.78 ? 100 THR   B N   1 
ATOM   2579 C CA  . THR   B 1 121 ? -28.417 13.959  13.460  1.00 23.77 ? 100 THR   B CA  1 
ATOM   2580 C C   . THR   B 1 121 ? -28.310 14.231  14.965  1.00 22.19 ? 100 THR   B C   1 
ATOM   2581 O O   . THR   B 1 121 ? -27.981 13.339  15.733  1.00 22.91 ? 100 THR   B O   1 
ATOM   2582 C CB  . THR   B 1 121 ? -28.526 12.453  13.168  1.00 27.52 ? 100 THR   B CB  1 
ATOM   2583 O OG1 . THR   B 1 121 ? -27.359 11.821  13.704  1.00 25.51 ? 100 THR   B OG1 1 
ATOM   2584 C CG2 . THR   B 1 121 ? -28.664 12.133  11.692  1.00 24.36 ? 100 THR   B CG2 1 
ATOM   2585 N N   . PRO   B 1 122 ? -28.512 15.483  15.417  1.00 24.66 ? 101 PRO   B N   1 
ATOM   2586 C CA  . PRO   B 1 122 ? -28.262 15.869  16.811  1.00 26.57 ? 101 PRO   B CA  1 
ATOM   2587 C C   . PRO   B 1 122 ? -29.139 15.090  17.773  1.00 24.28 ? 101 PRO   B C   1 
ATOM   2588 O O   . PRO   B 1 122 ? -30.284 14.760  17.449  1.00 26.35 ? 101 PRO   B O   1 
ATOM   2589 C CB  . PRO   B 1 122 ? -28.537 17.396  16.905  1.00 29.10 ? 101 PRO   B CB  1 
ATOM   2590 C CG  . PRO   B 1 122 ? -29.010 17.781  15.537  1.00 30.55 ? 101 PRO   B CG  1 
ATOM   2591 C CD  . PRO   B 1 122 ? -28.928 16.619  14.585  1.00 26.34 ? 101 PRO   B CD  1 
ATOM   2592 N N   . LEU   B 1 123 ? -28.584 14.797  18.949  1.00 24.82 ? 102 LEU   B N   1 
ATOM   2593 C CA  . LEU   B 1 123 ? -29.322 14.031  19.939  1.00 28.68 ? 102 LEU   B CA  1 
ATOM   2594 C C   . LEU   B 1 123 ? -30.362 14.922  20.606  1.00 36.05 ? 102 LEU   B C   1 
ATOM   2595 O O   . LEU   B 1 123 ? -31.422 14.428  20.987  1.00 34.47 ? 102 LEU   B O   1 
ATOM   2596 C CB  . LEU   B 1 123 ? -28.377 13.416  20.962  1.00 27.26 ? 102 LEU   B CB  1 
ATOM   2597 C CG  . LEU   B 1 123 ? -27.515 12.268  20.425  1.00 26.48 ? 102 LEU   B CG  1 
ATOM   2598 C CD1 . LEU   B 1 123 ? -26.435 12.036  21.484  1.00 27.95 ? 102 LEU   B CD1 1 
ATOM   2599 C CD2 . LEU   B 1 123 ? -28.333 11.024  20.184  1.00 28.06 ? 102 LEU   B CD2 1 
ATOM   2600 N N   . VAL   B 1 124 ? -30.029 16.212  20.744  1.00 34.88 ? 103 VAL   B N   1 
ATOM   2601 C CA  . VAL   B 1 124 ? -30.891 17.127  21.483  1.00 47.84 ? 103 VAL   B CA  1 
ATOM   2602 C C   . VAL   B 1 124 ? -31.436 18.246  20.574  1.00 49.23 ? 103 VAL   B C   1 
ATOM   2603 O O   . VAL   B 1 124 ? -30.676 18.697  19.692  1.00 50.94 ? 103 VAL   B O   1 
ATOM   2604 C CB  . VAL   B 1 124 ? -30.100 17.660  22.695  1.00 49.77 ? 103 VAL   B CB  1 
ATOM   2605 C CG1 . VAL   B 1 124 ? -30.761 18.869  23.341  1.00 62.52 ? 103 VAL   B CG1 1 
ATOM   2606 C CG2 . VAL   B 1 124 ? -29.880 16.559  23.725  1.00 51.97 ? 103 VAL   B CG2 1 
ATOM   2607 N N   . GLY   B 1 134 ? -35.268 18.370  6.578   1.00 73.02 ? 113 GLY   B N   1 
ATOM   2608 C CA  . GLY   B 1 134 ? -36.190 18.278  7.732   1.00 68.28 ? 113 GLY   B CA  1 
ATOM   2609 C C   . GLY   B 1 134 ? -36.848 16.900  7.820   1.00 63.82 ? 113 GLY   B C   1 
ATOM   2610 O O   . GLY   B 1 134 ? -38.073 16.786  7.813   1.00 65.57 ? 113 GLY   B O   1 
ATOM   2611 N N   . LYS   B 1 135 ? -36.009 15.863  7.937   1.00 55.83 ? 114 LYS   B N   1 
ATOM   2612 C CA  . LYS   B 1 135 ? -36.402 14.462  7.869   1.00 44.32 ? 114 LYS   B CA  1 
ATOM   2613 C C   . LYS   B 1 135 ? -36.865 13.974  9.236   1.00 35.40 ? 114 LYS   B C   1 
ATOM   2614 O O   . LYS   B 1 135 ? -36.446 14.499  10.263  1.00 40.85 ? 114 LYS   B O   1 
ATOM   2615 C CB  . LYS   B 1 135 ? -35.153 13.653  7.490   1.00 40.14 ? 114 LYS   B CB  1 
ATOM   2616 C CG  . LYS   B 1 135 ? -34.578 14.110  6.157   1.00 46.65 ? 114 LYS   B CG  1 
ATOM   2617 C CD  . LYS   B 1 135 ? -33.397 13.329  5.612   1.00 45.93 ? 114 LYS   B CD  1 
ATOM   2618 C CE  . LYS   B 1 135 ? -33.245 13.657  4.160   1.00 47.89 ? 114 LYS   B CE  1 
ATOM   2619 N NZ  . LYS   B 1 135 ? -32.096 12.975  3.572   1.00 52.50 ? 114 LYS   B NZ  1 
ATOM   2620 N N   . THR   B 1 136 ? -37.715 12.940  9.249   1.00 34.66 ? 115 THR   B N   1 
ATOM   2621 C CA  . THR   B 1 136 ? -38.019 12.310  10.518  1.00 34.88 ? 115 THR   B CA  1 
ATOM   2622 C C   . THR   B 1 136 ? -36.809 11.486  10.964  1.00 34.66 ? 115 THR   B C   1 
ATOM   2623 O O   . THR   B 1 136 ? -36.006 11.021  10.138  1.00 32.42 ? 115 THR   B O   1 
ATOM   2624 C CB  . THR   B 1 136 ? -39.257 11.424  10.422  1.00 37.88 ? 115 THR   B CB  1 
ATOM   2625 O OG1 . THR   B 1 136 ? -38.863 10.294  9.655   1.00 37.71 ? 115 THR   B OG1 1 
ATOM   2626 C CG2 . THR   B 1 136 ? -40.433 12.127  9.773   1.00 44.92 ? 115 THR   B CG2 1 
ATOM   2627 N N   . VAL   B 1 137 ? -36.735 11.271  12.272  1.00 30.39 ? 116 VAL   B N   1 
ATOM   2628 C CA  . VAL   B 1 137 ? -35.649 10.477  12.836  1.00 31.58 ? 116 VAL   B CA  1 
ATOM   2629 C C   . VAL   B 1 137 ? -35.626 9.088   12.182  1.00 30.95 ? 116 VAL   B C   1 
ATOM   2630 O O   . VAL   B 1 137 ? -34.562 8.556   11.876  1.00 28.67 ? 116 VAL   B O   1 
ATOM   2631 C CB  . VAL   B 1 137 ? -35.648 10.425  14.383  1.00 32.97 ? 116 VAL   B CB  1 
ATOM   2632 C CG1 . VAL   B 1 137 ? -36.853 9.688   14.926  1.00 41.63 ? 116 VAL   B CG1 1 
ATOM   2633 C CG2 . VAL   B 1 137 ? -34.398 9.739   14.922  1.00 30.32 ? 116 VAL   B CG2 1 
ATOM   2634 N N   . GLU   B 1 138 ? -36.797 8.488   11.906  1.00 32.66 ? 117 GLU   B N   1 
ATOM   2635 C CA  . GLU   B 1 138 ? -36.751 7.146   11.354  1.00 31.40 ? 117 GLU   B CA  1 
ATOM   2636 C C   . GLU   B 1 138 ? -36.169 7.190   9.935   1.00 34.05 ? 117 GLU   B C   1 
ATOM   2637 O O   . GLU   B 1 138 ? -35.513 6.241   9.503   1.00 28.77 ? 117 GLU   B O   1 
ATOM   2638 C CB  . GLU   B 1 138 ? -38.067 6.376   11.502  1.00 38.72 ? 117 GLU   B CB  1 
ATOM   2639 C CG  . GLU   B 1 138 ? -39.259 7.157   10.960  1.00 40.63 ? 117 GLU   B CG  1 
ATOM   2640 C CD  . GLU   B 1 138 ? -40.059 8.154   11.796  0.70 44.25 ? 117 GLU   B CD  1 
ATOM   2641 O OE1 . GLU   B 1 138 ? -39.518 8.815   12.696  0.70 32.07 ? 117 GLU   B OE1 1 
ATOM   2642 O OE2 . GLU   B 1 138 ? -41.262 8.308   11.485  0.70 43.82 ? 117 GLU   B OE2 1 
ATOM   2643 N N   . THR   B 1 139 ? -36.382 8.307   9.221   1.00 27.73 ? 118 THR   B N   1 
ATOM   2644 C CA  . THR   B 1 139 ? -35.808 8.487   7.891   1.00 30.69 ? 118 THR   B CA  1 
ATOM   2645 C C   . THR   B 1 139 ? -34.277 8.591   8.007   1.00 26.97 ? 118 THR   B C   1 
ATOM   2646 O O   . THR   B 1 139 ? -33.545 8.032   7.173   1.00 27.38 ? 118 THR   B O   1 
ATOM   2647 C CB  . THR   B 1 139 ? -36.385 9.764   7.262   1.00 33.94 ? 118 THR   B CB  1 
ATOM   2648 O OG1 . THR   B 1 139 ? -37.707 9.362   6.938   1.00 35.91 ? 118 THR   B OG1 1 
ATOM   2649 C CG2 . THR   B 1 139 ? -35.740 10.124  5.937   1.00 35.19 ? 118 THR   B CG2 1 
ATOM   2650 N N   . GLN   B 1 140 ? -33.835 9.387   8.986   1.00 26.76 ? 119 GLN   B N   1 
ATOM   2651 C CA  . GLN   B 1 140 ? -32.410 9.620   9.249   1.00 26.85 ? 119 GLN   B CA  1 
ATOM   2652 C C   . GLN   B 1 140 ? -31.711 8.284   9.540   1.00 26.24 ? 119 GLN   B C   1 
ATOM   2653 O O   . GLN   B 1 140 ? -30.683 7.952   8.932   1.00 24.07 ? 119 GLN   B O   1 
ATOM   2654 C CB  . GLN   B 1 140 ? -32.189 10.614  10.374  1.00 29.64 ? 119 GLN   B CB  1 
ATOM   2655 C CG  . GLN   B 1 140 ? -32.696 12.035  10.131  1.00 32.04 ? 119 GLN   B CG  1 
ATOM   2656 C CD  . GLN   B 1 140 ? -32.926 12.737  11.454  1.00 36.53 ? 119 GLN   B CD  1 
ATOM   2657 O OE1 . GLN   B 1 140 ? -32.241 12.488  12.447  1.00 46.88 ? 119 GLN   B OE1 1 
ATOM   2658 N NE2 . GLN   B 1 140 ? -33.965 13.556  11.539  1.00 49.01 ? 119 GLN   B NE2 1 
ATOM   2659 N N   . VAL   B 1 141 ? -32.326 7.492   10.407  1.00 22.63 ? 120 VAL   B N   1 
ATOM   2660 C CA  . VAL   B 1 141 ? -31.890 6.114   10.656  1.00 25.60 ? 120 VAL   B CA  1 
ATOM   2661 C C   . VAL   B 1 141 ? -31.796 5.309   9.360   1.00 28.06 ? 120 VAL   B C   1 
ATOM   2662 O O   . VAL   B 1 141 ? -30.748 4.702   9.054   1.00 25.33 ? 120 VAL   B O   1 
ATOM   2663 C CB  . VAL   B 1 141 ? -32.786 5.404   11.672  1.00 25.39 ? 120 VAL   B CB  1 
ATOM   2664 C CG1 . VAL   B 1 141 ? -32.467 3.915   11.732  1.00 26.60 ? 120 VAL   B CG1 1 
ATOM   2665 C CG2 . VAL   B 1 141 ? -32.703 6.041   13.057  1.00 28.01 ? 120 VAL   B CG2 1 
ATOM   2666 N N   . ALA   B 1 142 ? -32.904 5.267   8.585   1.00 24.97 ? 121 ALA   B N   1 
ATOM   2667 C CA  . ALA   B 1 142 ? -32.916 4.400   7.419   1.00 25.98 ? 121 ALA   B CA  1 
ATOM   2668 C C   . ALA   B 1 142 ? -31.834 4.819   6.431   1.00 23.73 ? 121 ALA   B C   1 
ATOM   2669 O O   . ALA   B 1 142 ? -31.263 3.995   5.759   1.00 25.10 ? 121 ALA   B O   1 
ATOM   2670 C CB  . ALA   B 1 142 ? -34.285 4.447   6.751   1.00 27.93 ? 121 ALA   B CB  1 
ATOM   2671 N N   . GLU   B 1 143 ? -31.659 6.124   6.246   1.00 23.35 ? 122 GLU   B N   1 
ATOM   2672 C CA  . GLU   B 1 143 ? -30.733 6.593   5.245   1.00 25.06 ? 122 GLU   B CA  1 
ATOM   2673 C C   . GLU   B 1 143 ? -29.281 6.427   5.712   1.00 25.53 ? 122 GLU   B C   1 
ATOM   2674 O O   . GLU   B 1 143 ? -28.458 5.964   4.945   1.00 23.29 ? 122 GLU   B O   1 
ATOM   2675 C CB  . GLU   B 1 143 ? -30.938 8.083   4.993   1.00 26.57 ? 122 GLU   B CB  1 
ATOM   2676 C CG  . GLU   B 1 143 ? -32.177 8.324   4.137   1.00 30.46 ? 122 GLU   B CG  1 
ATOM   2677 C CD  . GLU   B 1 143 ? -32.418 9.775   3.779   1.00 34.39 ? 122 GLU   B CD  1 
ATOM   2678 O OE1 . GLU   B 1 143 ? -31.655 10.687  4.190   1.00 32.33 ? 122 GLU   B OE1 1 
ATOM   2679 O OE2 . GLU   B 1 143 ? -33.429 9.971   3.058   1.00 37.76 ? 122 GLU   B OE2 1 
ATOM   2680 N N   . LEU   B 1 144 ? -28.956 6.860   6.932   1.00 24.54 ? 123 LEU   B N   1 
ATOM   2681 C CA  . LEU   B 1 144 ? -27.559 6.809   7.354   1.00 21.99 ? 123 LEU   B CA  1 
ATOM   2682 C C   . LEU   B 1 144 ? -27.102 5.394   7.709   1.00 22.70 ? 123 LEU   B C   1 
ATOM   2683 O O   . LEU   B 1 144 ? -25.969 5.064   7.393   1.00 25.48 ? 123 LEU   B O   1 
ATOM   2684 C CB  . LEU   B 1 144 ? -27.353 7.792   8.508   1.00 25.27 ? 123 LEU   B CB  1 
ATOM   2685 C CG  . LEU   B 1 144 ? -27.582 9.253   8.110   1.00 23.47 ? 123 LEU   B CG  1 
ATOM   2686 C CD1 . LEU   B 1 144 ? -27.672 10.066  9.340   1.00 24.19 ? 123 LEU   B CD1 1 
ATOM   2687 C CD2 . LEU   B 1 144 ? -26.332 9.675   7.343   1.00 25.88 ? 123 LEU   B CD2 1 
ATOM   2688 N N   . ILE   B 1 145 ? -27.947 4.588   8.366   1.00 20.01 ? 124 ILE   B N   1 
ATOM   2689 C CA  . ILE   B 1 145 ? -27.566 3.221   8.671   1.00 21.12 ? 124 ILE   B CA  1 
ATOM   2690 C C   . ILE   B 1 145 ? -27.734 2.340   7.425   1.00 24.24 ? 124 ILE   B C   1 
ATOM   2691 O O   . ILE   B 1 145 ? -26.924 1.455   7.204   1.00 22.91 ? 124 ILE   B O   1 
ATOM   2692 C CB  . ILE   B 1 145 ? -28.355 2.699   9.885   1.00 20.94 ? 124 ILE   B CB  1 
ATOM   2693 C CG1 . ILE   B 1 145 ? -28.207 3.657   11.103  1.00 24.47 ? 124 ILE   B CG1 1 
ATOM   2694 C CG2 . ILE   B 1 145 ? -28.014 1.236   10.219  1.00 24.26 ? 124 ILE   B CG2 1 
ATOM   2695 C CD1 . ILE   B 1 145 ? -26.766 3.853   11.573  1.00 22.02 ? 124 ILE   B CD1 1 
ATOM   2696 N N   . GLY   B 1 146 ? -28.770 2.563   6.599   1.00 25.50 ? 125 GLY   B N   1 
ATOM   2697 C CA  . GLY   B 1 146 ? -28.949 1.801   5.358   1.00 26.35 ? 125 GLY   B CA  1 
ATOM   2698 C C   . GLY   B 1 146 ? -27.754 1.944   4.398   1.00 23.00 ? 125 GLY   B C   1 
ATOM   2699 O O   . GLY   B 1 146 ? -27.142 0.952   4.020   1.00 25.33 ? 125 GLY   B O   1 
ATOM   2700 N N   . THR   B 1 147 ? -27.400 3.198   4.036   1.00 21.30 ? 126 THR   B N   1 
ATOM   2701 C CA  . THR   B 1 147 ? -26.348 3.428   3.055   1.00 22.55 ? 126 THR   B CA  1 
ATOM   2702 C C   . THR   B 1 147 ? -25.010 2.962   3.608   1.00 23.65 ? 126 THR   B C   1 
ATOM   2703 O O   . THR   B 1 147 ? -24.272 2.330   2.882   1.00 24.76 ? 126 THR   B O   1 
ATOM   2704 C CB  . THR   B 1 147 ? -26.251 4.880   2.547   1.00 25.93 ? 126 THR   B CB  1 
ATOM   2705 O OG1 . THR   B 1 147 ? -25.876 5.639   3.696   1.00 24.70 ? 126 THR   B OG1 1 
ATOM   2706 C CG2 . THR   B 1 147 ? -27.554 5.399   1.952   1.00 27.42 ? 126 THR   B CG2 1 
ATOM   2707 N N   . ASN   B 1 148 ? -24.713 3.269   4.885   1.00 22.89 ? 127 ASN   B N   1 
ATOM   2708 C CA  . ASN   B 1 148 ? -23.361 3.097   5.386   1.00 21.95 ? 127 ASN   B CA  1 
ATOM   2709 C C   . ASN   B 1 148 ? -23.111 1.679   5.887   1.00 21.99 ? 127 ASN   B C   1 
ATOM   2710 O O   . ASN   B 1 148 ? -21.949 1.314   6.032   1.00 25.13 ? 127 ASN   B O   1 
ATOM   2711 C CB  . ASN   B 1 148 ? -23.042 4.107   6.481   1.00 23.22 ? 127 ASN   B CB  1 
ATOM   2712 C CG  . ASN   B 1 148 ? -22.836 5.483   5.900   1.00 22.86 ? 127 ASN   B CG  1 
ATOM   2713 O OD1 . ASN   B 1 148 ? -21.891 5.674   5.128   1.00 28.20 ? 127 ASN   B OD1 1 
ATOM   2714 N ND2 . ASN   B 1 148 ? -23.639 6.461   6.284   1.00 24.80 ? 127 ASN   B ND2 1 
ATOM   2715 N N   . ALA   B 1 149 ? -24.161 0.897   6.165   1.00 21.91 ? 128 ALA   B N   1 
ATOM   2716 C CA  . ALA   B 1 149 ? -23.941 -0.369  6.869   1.00 20.47 ? 128 ALA   B CA  1 
ATOM   2717 C C   . ALA   B 1 149 ? -24.806 -1.510  6.324   1.00 20.93 ? 128 ALA   B C   1 
ATOM   2718 O O   . ALA   B 1 149 ? -24.301 -2.554  5.902   1.00 23.33 ? 128 ALA   B O   1 
ATOM   2719 C CB  . ALA   B 1 149 ? -24.137 -0.182  8.361   1.00 22.66 ? 128 ALA   B CB  1 
ATOM   2720 N N   . ILE   B 1 150 ? -26.116 -1.294  6.299   1.00 22.36 ? 129 ILE   B N   1 
ATOM   2721 C CA  . ILE   B 1 150 ? -27.028 -2.362  5.894   1.00 20.31 ? 129 ILE   B CA  1 
ATOM   2722 C C   . ILE   B 1 150 ? -26.917 -2.727  4.419   1.00 21.02 ? 129 ILE   B C   1 
ATOM   2723 O O   . ILE   B 1 150 ? -26.825 -3.905  4.089   1.00 21.17 ? 129 ILE   B O   1 
ATOM   2724 C CB  . ILE   B 1 150 ? -28.478 -2.053  6.279   1.00 21.63 ? 129 ILE   B CB  1 
ATOM   2725 C CG1 . ILE   B 1 150 ? -28.606 -1.872  7.815   1.00 21.93 ? 129 ILE   B CG1 1 
ATOM   2726 C CG2 . ILE   B 1 150 ? -29.306 -3.233  5.750   1.00 22.09 ? 129 ILE   B CG2 1 
ATOM   2727 C CD1 . ILE   B 1 150 ? -29.981 -1.348  8.247   1.00 28.48 ? 129 ILE   B CD1 1 
ATOM   2728 N N   . ALA   B 1 151 ? -26.904 -1.728  3.546   1.00 21.57 ? 130 ALA   B N   1 
ATOM   2729 C CA  . ALA   B 1 151 ? -26.760 -2.033  2.132   1.00 25.09 ? 130 ALA   B CA  1 
ATOM   2730 C C   . ALA   B 1 151 ? -25.423 -2.735  1.892   1.00 21.93 ? 130 ALA   B C   1 
ATOM   2731 O O   . ALA   B 1 151 ? -25.369 -3.783  1.247   1.00 21.55 ? 130 ALA   B O   1 
ATOM   2732 C CB  . ALA   B 1 151 ? -26.948 -0.762  1.304   1.00 20.54 ? 130 ALA   B CB  1 
ATOM   2733 N N   . PRO   B 1 152 ? -24.272 -2.240  2.441   1.00 20.98 ? 131 PRO   B N   1 
ATOM   2734 C CA  . PRO   B 1 152 ? -23.041 -3.039  2.373   1.00 20.90 ? 131 PRO   B CA  1 
ATOM   2735 C C   . PRO   B 1 152 ? -23.184 -4.501  2.811   1.00 21.16 ? 131 PRO   B C   1 
ATOM   2736 O O   . PRO   B 1 152 ? -22.586 -5.388  2.191   1.00 22.90 ? 131 PRO   B O   1 
ATOM   2737 C CB  . PRO   B 1 152 ? -21.988 -2.226  3.222   1.00 21.49 ? 131 PRO   B CB  1 
ATOM   2738 C CG  . PRO   B 1 152 ? -22.495 -0.772  3.077   1.00 21.39 ? 131 PRO   B CG  1 
ATOM   2739 C CD  . PRO   B 1 152 ? -24.049 -0.868  2.984   1.00 20.94 ? 131 PRO   B CD  1 
ATOM   2740 N N   . PHE   B 1 153 ? -23.883 -4.735  3.944   1.00 19.87 ? 132 PHE   B N   1 
ATOM   2741 C CA  . PHE   B 1 153 ? -24.067 -6.114  4.391   1.00 21.83 ? 132 PHE   B CA  1 
ATOM   2742 C C   . PHE   B 1 153 ? -24.816 -6.903  3.294   1.00 21.31 ? 132 PHE   B C   1 
ATOM   2743 O O   . PHE   B 1 153 ? -24.488 -8.060  3.022   1.00 23.24 ? 132 PHE   B O   1 
ATOM   2744 C CB  . PHE   B 1 153 ? -24.814 -6.083  5.730   1.00 20.81 ? 132 PHE   B CB  1 
ATOM   2745 C CG  . PHE   B 1 153 ? -25.490 -7.397  6.110   1.00 21.80 ? 132 PHE   B CG  1 
ATOM   2746 C CD1 . PHE   B 1 153 ? -24.742 -8.404  6.706   1.00 22.39 ? 132 PHE   B CD1 1 
ATOM   2747 C CD2 . PHE   B 1 153 ? -26.855 -7.587  5.896   1.00 24.35 ? 132 PHE   B CD2 1 
ATOM   2748 C CE1 . PHE   B 1 153 ? -25.342 -9.632  7.042   1.00 23.37 ? 132 PHE   B CE1 1 
ATOM   2749 C CE2 . PHE   B 1 153 ? -27.455 -8.788  6.243   1.00 22.73 ? 132 PHE   B CE2 1 
ATOM   2750 C CZ  . PHE   B 1 153 ? -26.695 -9.814  6.795   1.00 23.45 ? 132 PHE   B CZ  1 
ATOM   2751 N N   . LEU   B 1 154 ? -25.913 -6.340  2.791   1.00 23.13 ? 133 LEU   B N   1 
ATOM   2752 C CA  . LEU   B 1 154 ? -26.794 -7.077  1.872   1.00 23.36 ? 133 LEU   B CA  1 
ATOM   2753 C C   . LEU   B 1 154 ? -26.097 -7.271  0.525   1.00 23.64 ? 133 LEU   B C   1 
ATOM   2754 O O   . LEU   B 1 154 ? -26.198 -8.337  -0.093  1.00 21.76 ? 133 LEU   B O   1 
ATOM   2755 C CB  . LEU   B 1 154 ? -28.121 -6.339  1.692   1.00 21.15 ? 133 LEU   B CB  1 
ATOM   2756 C CG  . LEU   B 1 154 ? -28.985 -6.213  2.947   1.00 25.13 ? 133 LEU   B CG  1 
ATOM   2757 C CD1 . LEU   B 1 154 ? -30.022 -5.147  2.761   1.00 27.00 ? 133 LEU   B CD1 1 
ATOM   2758 C CD2 . LEU   B 1 154 ? -29.610 -7.530  3.344   1.00 26.96 ? 133 LEU   B CD2 1 
ATOM   2759 N N   . LEU   B 1 155 ? -25.348 -6.250  0.086   1.00 22.05 ? 134 LEU   B N   1 
ATOM   2760 C CA  . LEU   B 1 155 ? -24.459 -6.411  -1.069  1.00 23.82 ? 134 LEU   B CA  1 
ATOM   2761 C C   . LEU   B 1 155 ? -23.401 -7.515  -0.885  1.00 26.33 ? 134 LEU   B C   1 
ATOM   2762 O O   . LEU   B 1 155 ? -23.146 -8.314  -1.788  1.00 24.85 ? 134 LEU   B O   1 
ATOM   2763 C CB  . LEU   B 1 155 ? -23.841 -5.079  -1.478  1.00 23.14 ? 134 LEU   B CB  1 
ATOM   2764 C CG  . LEU   B 1 155 ? -24.810 -4.037  -2.050  1.00 24.80 ? 134 LEU   B CG  1 
ATOM   2765 C CD1 . LEU   B 1 155 ? -24.224 -2.651  -1.934  1.00 22.23 ? 134 LEU   B CD1 1 
ATOM   2766 C CD2 . LEU   B 1 155 ? -25.281 -4.250  -3.508  1.00 30.26 ? 134 LEU   B CD2 1 
ATOM   2767 N N   . THR   B 1 156 ? -22.831 -7.625  0.323   1.00 23.96 ? 135 THR   B N   1 
ATOM   2768 C CA  . THR   B 1 156 ? -21.796 -8.607  0.586   1.00 20.27 ? 135 THR   B CA  1 
ATOM   2769 C C   . THR   B 1 156 ? -22.462 -9.986  0.515   1.00 21.74 ? 135 THR   B C   1 
ATOM   2770 O O   . THR   B 1 156 ? -21.871 -10.926 -0.001  1.00 23.24 ? 135 THR   B O   1 
ATOM   2771 C CB  . THR   B 1 156 ? -21.224 -8.366  1.978   1.00 21.49 ? 135 THR   B CB  1 
ATOM   2772 O OG1 . THR   B 1 156 ? -20.547 -7.099  1.893   1.00 22.17 ? 135 THR   B OG1 1 
ATOM   2773 C CG2 . THR   B 1 156 ? -20.218 -9.436  2.400   1.00 20.61 ? 135 THR   B CG2 1 
ATOM   2774 N N   . MET   B 1 157 ? -23.671 -10.094 1.055   1.00 20.38 ? 136 MET   B N   1 
ATOM   2775 C CA  . MET   B 1 157 ? -24.345 -11.406 1.051   1.00 24.99 ? 136 MET   B CA  1 
ATOM   2776 C C   . MET   B 1 157 ? -24.625 -11.863 -0.387  1.00 26.47 ? 136 MET   B C   1 
ATOM   2777 O O   . MET   B 1 157 ? -24.374 -13.027 -0.734  1.00 24.69 ? 136 MET   B O   1 
ATOM   2778 C CB  . MET   B 1 157 ? -25.738 -11.392 1.704   1.00 24.20 ? 136 MET   B CB  1 
ATOM   2779 C CG  . MET   B 1 157 ? -25.878 -11.349 3.205   1.00 35.57 ? 136 MET   B CG  1 
ATOM   2780 S SD  . MET   B 1 157 ? -27.645 -11.487 3.619   1.00 42.89 ? 136 MET   B SD  1 
ATOM   2781 C CE  . MET   B 1 157 ? -27.915 -13.063 2.827   1.00 34.15 ? 136 MET   B CE  1 
ATOM   2782 N N   . SER   B 1 158 ? -25.189 -10.955 -1.201  1.00 25.53 ? 137 SER   B N   1 
ATOM   2783 C CA  . SER   B 1 158 ? -25.533 -11.251 -2.591  1.00 24.84 ? 137 SER   B CA  1 
ATOM   2784 C C   . SER   B 1 158 ? -24.258 -11.542 -3.388  1.00 26.31 ? 137 SER   B C   1 
ATOM   2785 O O   . SER   B 1 158 ? -24.185 -12.517 -4.122  1.00 25.08 ? 137 SER   B O   1 
ATOM   2786 C CB  . SER   B 1 158 ? -26.333 -10.122 -3.210  1.00 24.08 ? 137 SER   B CB  1 
ATOM   2787 O OG  . SER   B 1 158 ? -27.657 -10.095 -2.668  1.00 29.38 ? 137 SER   B OG  1 
ATOM   2788 N N   . PHE   B 1 159 ? -23.195 -10.760 -3.155  1.00 24.17 ? 138 PHE   B N   1 
ATOM   2789 C CA  . PHE   B 1 159 ? -21.910 -10.996 -3.801  1.00 22.39 ? 138 PHE   B CA  1 
ATOM   2790 C C   . PHE   B 1 159 ? -21.400 -12.405 -3.513  1.00 25.48 ? 138 PHE   B C   1 
ATOM   2791 O O   . PHE   B 1 159 ? -20.986 -13.119 -4.421  1.00 28.81 ? 138 PHE   B O   1 
ATOM   2792 C CB  . PHE   B 1 159 ? -20.886 -9.909  -3.403  1.00 22.56 ? 138 PHE   B CB  1 
ATOM   2793 C CG  . PHE   B 1 159 ? -19.462 -10.077 -3.929  1.00 23.41 ? 138 PHE   B CG  1 
ATOM   2794 C CD1 . PHE   B 1 159 ? -18.518 -10.882 -3.270  1.00 22.33 ? 138 PHE   B CD1 1 
ATOM   2795 C CD2 . PHE   B 1 159 ? -19.094 -9.510  -5.143  1.00 23.19 ? 138 PHE   B CD2 1 
ATOM   2796 C CE1 . PHE   B 1 159 ? -17.213 -11.010 -3.773  1.00 25.34 ? 138 PHE   B CE1 1 
ATOM   2797 C CE2 . PHE   B 1 159 ? -17.808 -9.637  -5.644  1.00 22.79 ? 138 PHE   B CE2 1 
ATOM   2798 C CZ  . PHE   B 1 159 ? -16.875 -10.399 -4.977  1.00 25.71 ? 138 PHE   B CZ  1 
ATOM   2799 N N   . ALA   B 1 160 ? -21.398 -12.811 -2.242  1.00 27.74 ? 139 ALA   B N   1 
ATOM   2800 C CA  . ALA   B 1 160 ? -20.830 -14.107 -1.897  1.00 28.17 ? 139 ALA   B CA  1 
ATOM   2801 C C   . ALA   B 1 160 ? -21.741 -15.236 -2.395  1.00 29.99 ? 139 ALA   B C   1 
ATOM   2802 O O   . ALA   B 1 160 ? -21.232 -16.266 -2.828  1.00 27.04 ? 139 ALA   B O   1 
ATOM   2803 C CB  . ALA   B 1 160 ? -20.663 -14.216 -0.400  1.00 34.84 ? 139 ALA   B CB  1 
ATOM   2804 N N   . GLN   B 1 161 ? -23.061 -15.041 -2.302  1.00 24.92 ? 140 GLN   B N   1 
ATOM   2805 C CA  . GLN   B 1 161 ? -23.996 -16.102 -2.682  1.00 31.14 ? 140 GLN   B CA  1 
ATOM   2806 C C   . GLN   B 1 161 ? -23.899 -16.423 -4.171  1.00 35.52 ? 140 GLN   B C   1 
ATOM   2807 O O   . GLN   B 1 161 ? -24.144 -17.565 -4.571  1.00 36.24 ? 140 GLN   B O   1 
ATOM   2808 C CB  . GLN   B 1 161 ? -25.421 -15.824 -2.217  1.00 32.54 ? 140 GLN   B CB  1 
ATOM   2809 C CG  . GLN   B 1 161 ? -25.546 -16.022 -0.710  0.70 40.49 ? 140 GLN   B CG  1 
ATOM   2810 C CD  . GLN   B 1 161 ? -26.876 -15.607 -0.129  0.70 44.35 ? 140 GLN   B CD  1 
ATOM   2811 O OE1 . GLN   B 1 161 ? -27.011 -15.407 1.084   0.70 37.63 ? 140 GLN   B OE1 1 
ATOM   2812 N NE2 . GLN   B 1 161 ? -27.870 -15.460 -0.996  0.70 44.81 ? 140 GLN   B NE2 1 
ATOM   2813 N N   . ARG   B 1 162 ? -23.569 -15.420 -4.988  1.00 34.40 ? 141 ARG   B N   1 
ATOM   2814 C CA  . ARG   B 1 162 ? -23.635 -15.568 -6.431  1.00 39.81 ? 141 ARG   B CA  1 
ATOM   2815 C C   . ARG   B 1 162 ? -22.338 -16.125 -6.998  1.00 41.86 ? 141 ARG   B C   1 
ATOM   2816 O O   . ARG   B 1 162 ? -22.267 -16.309 -8.204  1.00 47.74 ? 141 ARG   B O   1 
ATOM   2817 C CB  . ARG   B 1 162 ? -23.936 -14.281 -7.208  1.00 37.52 ? 141 ARG   B CB  1 
ATOM   2818 C CG  . ARG   B 1 162 ? -25.360 -13.775 -7.042  1.00 41.97 ? 141 ARG   B CG  1 
ATOM   2819 C CD  . ARG   B 1 162 ? -26.473 -14.698 -7.517  0.60 43.45 ? 141 ARG   B CD  1 
ATOM   2820 N NE  . ARG   B 1 162 ? -26.875 -14.202 -8.832  0.60 46.01 ? 141 ARG   B NE  1 
ATOM   2821 C CZ  . ARG   B 1 162 ? -26.199 -14.320 -9.966  0.60 46.82 ? 141 ARG   B CZ  1 
ATOM   2822 N NH1 . ARG   B 1 162 ? -25.197 -15.180 -10.078 0.60 44.73 ? 141 ARG   B NH1 1 
ATOM   2823 N NH2 . ARG   B 1 162 ? -26.598 -13.614 -11.010 0.60 45.53 ? 141 ARG   B NH2 1 
ATOM   2824 N N   . GLN   B 1 163 ? -21.320 -16.365 -6.164  1.00 42.67 ? 142 GLN   B N   1 
ATOM   2825 C CA  . GLN   B 1 163 ? -20.063 -16.878 -6.699  1.00 51.68 ? 142 GLN   B CA  1 
ATOM   2826 C C   . GLN   B 1 163 ? -20.275 -18.308 -7.212  1.00 65.95 ? 142 GLN   B C   1 
ATOM   2827 O O   . GLN   B 1 163 ? -20.705 -19.166 -6.445  1.00 71.51 ? 142 GLN   B O   1 
ATOM   2828 C CB  . GLN   B 1 163 ? -18.873 -16.712 -5.749  1.00 39.61 ? 142 GLN   B CB  1 
ATOM   2829 C CG  . GLN   B 1 163 ? -18.521 -15.251 -5.447  1.00 37.73 ? 142 GLN   B CG  1 
ATOM   2830 C CD  . GLN   B 1 163 ? -18.333 -14.401 -6.694  1.00 41.23 ? 142 GLN   B CD  1 
ATOM   2831 O OE1 . GLN   B 1 163 ? -17.646 -14.801 -7.648  1.00 33.06 ? 142 GLN   B OE1 1 
ATOM   2832 N NE2 . GLN   B 1 163 ? -18.929 -13.212 -6.693  1.00 36.75 ? 142 GLN   B NE2 1 
ATOM   2833 N N   . LYS   B 1 164 ? -19.985 -18.544 -8.507  1.00 72.45 ? 143 LYS   B N   1 
ATOM   2834 C CA  . LYS   B 1 164 ? -20.194 -19.836 -9.156  1.00 79.10 ? 143 LYS   B CA  1 
ATOM   2835 C C   . LYS   B 1 164 ? -18.981 -20.202 -10.034 1.00 75.07 ? 143 LYS   B C   1 
ATOM   2836 O O   . LYS   B 1 164 ? -17.946 -20.620 -9.459  1.00 74.42 ? 143 LYS   B O   1 
ATOM   2837 C CB  . LYS   B 1 164 ? -21.470 -19.828 -10.009 1.00 80.04 ? 143 LYS   B CB  1 
ATOM   2838 N N   . SER   B 1 173 ? -10.791 -16.612 -8.637  1.00 57.02 ? 152 SER   B N   1 
ATOM   2839 C CA  . SER   B 1 173 ? -9.516  -15.877 -8.856  1.00 64.20 ? 152 SER   B CA  1 
ATOM   2840 C C   . SER   B 1 173 ? -9.704  -14.401 -8.520  1.00 63.43 ? 152 SER   B C   1 
ATOM   2841 O O   . SER   B 1 173 ? -10.438 -13.676 -9.205  1.00 70.04 ? 152 SER   B O   1 
ATOM   2842 C CB  . SER   B 1 173 ? -8.967  -16.056 -10.258 1.00 62.57 ? 152 SER   B CB  1 
ATOM   2843 N N   . ASN   B 1 174 ? -9.045  -14.013 -7.426  1.00 48.20 ? 153 ASN   B N   1 
ATOM   2844 C CA  . ASN   B 1 174 ? -8.886  -12.652 -6.936  1.00 39.37 ? 153 ASN   B CA  1 
ATOM   2845 C C   . ASN   B 1 174 ? -10.217 -11.957 -6.651  1.00 29.77 ? 153 ASN   B C   1 
ATOM   2846 O O   . ASN   B 1 174 ? -10.461 -10.866 -7.163  1.00 31.75 ? 153 ASN   B O   1 
ATOM   2847 C CB  . ASN   B 1 174 ? -7.944  -11.821 -7.800  1.00 44.31 ? 153 ASN   B CB  1 
ATOM   2848 C CG  . ASN   B 1 174 ? -7.316  -10.706 -6.998  1.00 47.97 ? 153 ASN   B CG  1 
ATOM   2849 O OD1 . ASN   B 1 174 ? -7.242  -10.793 -5.765  1.00 48.67 ? 153 ASN   B OD1 1 
ATOM   2850 N ND2 . ASN   B 1 174 ? -6.845  -9.669  -7.679  1.00 48.54 ? 153 ASN   B ND2 1 
ATOM   2851 N N   . LEU   B 1 175 ? -11.063 -12.582 -5.824  1.00 25.04 ? 154 LEU   B N   1 
ATOM   2852 C CA  . LEU   B 1 175 ? -12.325 -11.968 -5.415  1.00 22.20 ? 154 LEU   B CA  1 
ATOM   2853 C C   . LEU   B 1 175 ? -12.083 -11.103 -4.173  1.00 23.99 ? 154 LEU   B C   1 
ATOM   2854 O O   . LEU   B 1 175 ? -11.464 -11.536 -3.218  1.00 25.15 ? 154 LEU   B O   1 
ATOM   2855 C CB  . LEU   B 1 175 ? -13.350 -13.043 -5.054  1.00 25.92 ? 154 LEU   B CB  1 
ATOM   2856 C CG  . LEU   B 1 175 ? -13.633 -14.080 -6.155  1.00 30.10 ? 154 LEU   B CG  1 
ATOM   2857 C CD1 . LEU   B 1 175 ? -14.543 -15.211 -5.708  1.00 31.37 ? 154 LEU   B CD1 1 
ATOM   2858 C CD2 . LEU   B 1 175 ? -14.255 -13.347 -7.327  1.00 28.70 ? 154 LEU   B CD2 1 
ATOM   2859 N N   . SER   B 1 176 ? -12.565 -9.861  -4.178  1.00 25.28 ? 155 SER   B N   1 
ATOM   2860 C CA  . SER   B 1 176 ? -12.475 -9.122  -2.921  1.00 25.11 ? 155 SER   B CA  1 
ATOM   2861 C C   . SER   B 1 176 ? -13.543 -8.037  -2.836  1.00 23.32 ? 155 SER   B C   1 
ATOM   2862 O O   . SER   B 1 176 ? -14.159 -7.625  -3.843  1.00 21.94 ? 155 SER   B O   1 
ATOM   2863 C CB  . SER   B 1 176 ? -11.093 -8.595  -2.711  1.00 26.73 ? 155 SER   B CB  1 
ATOM   2864 O OG  . SER   B 1 176 ? -10.894 -7.461  -3.537  1.00 28.29 ? 155 SER   B OG  1 
ATOM   2865 N N   . ILE   B 1 177 ? -13.743 -7.559  -1.594  1.00 21.35 ? 156 ILE   B N   1 
ATOM   2866 C CA  . ILE   B 1 177 ? -14.673 -6.478  -1.307  1.00 20.33 ? 156 ILE   B CA  1 
ATOM   2867 C C   . ILE   B 1 177 ? -13.831 -5.384  -0.647  1.00 20.61 ? 156 ILE   B C   1 
ATOM   2868 O O   . ILE   B 1 177 ? -12.956 -5.690  0.159   1.00 21.57 ? 156 ILE   B O   1 
ATOM   2869 C CB  . ILE   B 1 177 ? -15.774 -6.983  -0.348  1.00 20.96 ? 156 ILE   B CB  1 
ATOM   2870 C CG1 . ILE   B 1 177 ? -16.503 -8.168  -0.976  1.00 22.02 ? 156 ILE   B CG1 1 
ATOM   2871 C CG2 . ILE   B 1 177 ? -16.746 -5.857  0.020   1.00 20.92 ? 156 ILE   B CG2 1 
ATOM   2872 C CD1 . ILE   B 1 177 ? -17.654 -8.712  -0.151  1.00 22.79 ? 156 ILE   B CD1 1 
ATOM   2873 N N   . VAL   B 1 178 ? -14.146 -4.116  -0.944  1.00 19.22 ? 157 VAL   B N   1 
ATOM   2874 C CA  . VAL   B 1 178 ? -13.495 -2.996  -0.284  1.00 18.69 ? 157 VAL   B CA  1 
ATOM   2875 C C   . VAL   B 1 178 ? -14.578 -2.057  0.218   1.00 19.04 ? 157 VAL   B C   1 
ATOM   2876 O O   . VAL   B 1 178 ? -15.413 -1.564  -0.568  1.00 21.34 ? 157 VAL   B O   1 
ATOM   2877 C CB  . VAL   B 1 178 ? -12.508 -2.241  -1.185  1.00 22.96 ? 157 VAL   B CB  1 
ATOM   2878 C CG1 . VAL   B 1 178 ? -11.923 -1.047  -0.442  1.00 21.13 ? 157 VAL   B CG1 1 
ATOM   2879 C CG2 . VAL   B 1 178 ? -11.418 -3.155  -1.744  1.00 24.05 ? 157 VAL   B CG2 1 
ATOM   2880 N N   . ASN   B 1 179 ? -14.559 -1.793  1.543   1.00 19.04 ? 158 ASN   B N   1 
ATOM   2881 C CA  . ASN   B 1 179 ? -15.553 -0.907  2.147   1.00 17.66 ? 158 ASN   B CA  1 
ATOM   2882 C C   . ASN   B 1 179 ? -14.917 0.453   2.422   1.00 19.98 ? 158 ASN   B C   1 
ATOM   2883 O O   . ASN   B 1 179 ? -13.848 0.483   2.997   1.00 19.67 ? 158 ASN   B O   1 
ATOM   2884 C CB  . ASN   B 1 179 ? -16.024 -1.518  3.462   1.00 17.82 ? 158 ASN   B CB  1 
ATOM   2885 C CG  . ASN   B 1 179 ? -16.814 -2.778  3.197   1.00 19.57 ? 158 ASN   B CG  1 
ATOM   2886 O OD1 . ASN   B 1 179 ? -17.471 -2.889  2.154   1.00 18.82 ? 158 ASN   B OD1 1 
ATOM   2887 N ND2 . ASN   B 1 179 ? -16.668 -3.767  4.058   1.00 21.10 ? 158 ASN   B ND2 1 
ATOM   2888 N N   . LEU   B 1 180 ? -15.586 1.562   2.035   1.00 17.28 ? 159 LEU   B N   1 
ATOM   2889 C CA  . LEU   B 1 180 ? -15.074 2.895   2.350   1.00 18.90 ? 159 LEU   B CA  1 
ATOM   2890 C C   . LEU   B 1 180 ? -15.522 3.255   3.773   1.00 21.22 ? 159 LEU   B C   1 
ATOM   2891 O O   . LEU   B 1 180 ? -16.699 3.481   4.033   1.00 21.17 ? 159 LEU   B O   1 
ATOM   2892 C CB  . LEU   B 1 180 ? -15.589 3.914   1.336   1.00 16.99 ? 159 LEU   B CB  1 
ATOM   2893 C CG  . LEU   B 1 180 ? -14.764 4.022   0.032   1.00 19.43 ? 159 LEU   B CG  1 
ATOM   2894 C CD1 . LEU   B 1 180 ? -13.447 4.728   0.341   1.00 20.93 ? 159 LEU   B CD1 1 
ATOM   2895 C CD2 . LEU   B 1 180 ? -14.447 2.633   -0.628  1.00 20.29 ? 159 LEU   B CD2 1 
ATOM   2896 N N   . CYS   B 1 181 ? -14.531 3.315   4.656   1.00 21.30 ? 160 CYS   B N   1 
ATOM   2897 C CA  . CYS   B 1 181 ? -14.691 3.526   6.085   1.00 19.43 ? 160 CYS   B CA  1 
ATOM   2898 C C   . CYS   B 1 181 ? -14.367 5.004   6.347   1.00 23.19 ? 160 CYS   B C   1 
ATOM   2899 O O   . CYS   B 1 181 ? -14.592 5.839   5.480   1.00 22.99 ? 160 CYS   B O   1 
ATOM   2900 C CB  . CYS   B 1 181 ? -13.804 2.554   6.854   1.00 19.30 ? 160 CYS   B CB  1 
ATOM   2901 S SG  . CYS   B 1 181 ? -14.291 0.828   6.549   1.00 24.41 ? 160 CYS   B SG  1 
ATOM   2902 N N   . ASP   B 1 182 ? -13.993 5.344   7.580   1.00 19.30 ? 161 ASP   B N   1 
ATOM   2903 C CA  . ASP   B 1 182 ? -13.765 6.749   7.910   1.00 18.53 ? 161 ASP   B CA  1 
ATOM   2904 C C   . ASP   B 1 182 ? -12.705 6.781   9.016   1.00 21.38 ? 161 ASP   B C   1 
ATOM   2905 O O   . ASP   B 1 182 ? -12.858 6.147   10.064  1.00 20.77 ? 161 ASP   B O   1 
ATOM   2906 C CB  . ASP   B 1 182 ? -15.046 7.470   8.324   1.00 21.31 ? 161 ASP   B CB  1 
ATOM   2907 C CG  . ASP   B 1 182 ? -14.917 8.963   8.630   1.00 26.13 ? 161 ASP   B CG  1 
ATOM   2908 O OD1 . ASP   B 1 182 ? -13.845 9.378   9.149   1.00 25.73 ? 161 ASP   B OD1 1 
ATOM   2909 O OD2 . ASP   B 1 182 ? -15.890 9.749   8.328   1.00 28.14 ? 161 ASP   B OD2 1 
ATOM   2910 N N   . ALA   B 1 183 ? -11.569 7.461   8.759   1.00 18.94 ? 162 ALA   B N   1 
ATOM   2911 C CA  . ALA   B 1 183 ? -10.429 7.362   9.670   1.00 19.24 ? 162 ALA   B CA  1 
ATOM   2912 C C   . ALA   B 1 183 ? -10.743 8.068   10.992  1.00 20.29 ? 162 ALA   B C   1 
ATOM   2913 O O   . ALA   B 1 183 ? -9.995  7.925   11.959  1.00 21.08 ? 162 ALA   B O   1 
ATOM   2914 C CB  . ALA   B 1 183 ? -9.208  8.032   9.000   1.00 18.57 ? 162 ALA   B CB  1 
ATOM   2915 N N   . MET   B 1 184 ? -11.798 8.911   11.006  1.00 22.44 ? 163 MET   B N   1 
ATOM   2916 C CA  . MET   B 1 184 ? -12.025 9.750   12.178  1.00 22.17 ? 163 MET   B CA  1 
ATOM   2917 C C   . MET   B 1 184 ? -13.155 9.209   13.054  1.00 20.78 ? 163 MET   B C   1 
ATOM   2918 O O   . MET   B 1 184 ? -13.701 9.939   13.865  1.00 25.42 ? 163 MET   B O   1 
ATOM   2919 C CB  . MET   B 1 184 ? -12.319 11.179  11.716  1.00 23.10 ? 163 MET   B CB  1 
ATOM   2920 C CG  . MET   B 1 184 ? -11.143 11.788  10.949  1.00 27.39 ? 163 MET   B CG  1 
ATOM   2921 S SD  . MET   B 1 184 ? -9.725  12.011  12.058  1.00 28.55 ? 163 MET   B SD  1 
ATOM   2922 C CE  . MET   B 1 184 ? -10.218 13.548  12.851  1.00 31.45 ? 163 MET   B CE  1 
ATOM   2923 N N   . VAL   B 1 185 ? -13.473 7.915   12.939  1.00 22.85 ? 164 VAL   B N   1 
ATOM   2924 C CA  . VAL   B 1 185 ? -14.648 7.405   13.643  1.00 27.81 ? 164 VAL   B CA  1 
ATOM   2925 C C   . VAL   B 1 185 ? -14.476 7.359   15.162  1.00 26.09 ? 164 VAL   B C   1 
ATOM   2926 O O   . VAL   B 1 185 ? -15.463 7.280   15.885  1.00 25.51 ? 164 VAL   B O   1 
ATOM   2927 C CB  . VAL   B 1 185 ? -15.189 6.068   13.139  1.00 30.45 ? 164 VAL   B CB  1 
ATOM   2928 C CG1 . VAL   B 1 185 ? -15.820 6.226   11.761  1.00 31.62 ? 164 VAL   B CG1 1 
ATOM   2929 C CG2 . VAL   B 1 185 ? -14.143 4.988   13.215  1.00 28.88 ? 164 VAL   B CG2 1 
ATOM   2930 N N   . ASP   B 1 186 ? -13.234 7.366   15.660  1.00 24.67 ? 165 ASP   B N   1 
ATOM   2931 C CA  . ASP   B 1 186 ? -13.033 7.394   17.101  1.00 24.65 ? 165 ASP   B CA  1 
ATOM   2932 C C   . ASP   B 1 186 ? -12.806 8.826   17.588  1.00 24.13 ? 165 ASP   B C   1 
ATOM   2933 O O   . ASP   B 1 186 ? -12.631 9.041   18.795  1.00 25.40 ? 165 ASP   B O   1 
ATOM   2934 C CB  . ASP   B 1 186 ? -11.892 6.475   17.504  1.00 24.76 ? 165 ASP   B CB  1 
ATOM   2935 C CG  . ASP   B 1 186 ? -12.155 5.013   17.177  1.00 27.99 ? 165 ASP   B CG  1 
ATOM   2936 O OD1 . ASP   B 1 186 ? -13.278 4.540   17.401  1.00 28.00 ? 165 ASP   B OD1 1 
ATOM   2937 O OD2 . ASP   B 1 186 ? -11.201 4.321   16.792  1.00 30.99 ? 165 ASP   B OD2 1 
ATOM   2938 N N   . GLN   B 1 187 ? -12.829 9.782   16.655  1.00 22.31 ? 166 GLN   B N   1 
ATOM   2939 C CA  . GLN   B 1 187 ? -12.762 11.195  17.002  1.00 23.59 ? 166 GLN   B CA  1 
ATOM   2940 C C   . GLN   B 1 187 ? -13.824 11.922  16.187  1.00 24.55 ? 166 GLN   B C   1 
ATOM   2941 O O   . GLN   B 1 187 ? -13.510 12.763  15.348  1.00 23.35 ? 166 GLN   B O   1 
ATOM   2942 C CB  . GLN   B 1 187 ? -11.416 11.887  16.771  1.00 27.81 ? 166 GLN   B CB  1 
ATOM   2943 C CG  . GLN   B 1 187 ? -10.280 11.287  17.588  1.00 35.99 ? 166 GLN   B CG  1 
ATOM   2944 C CD  . GLN   B 1 187 ? -9.148  10.837  16.694  1.00 38.61 ? 166 GLN   B CD  1 
ATOM   2945 O OE1 . GLN   B 1 187 ? -9.136  9.702   16.207  1.00 37.47 ? 166 GLN   B OE1 1 
ATOM   2946 N NE2 . GLN   B 1 187 ? -8.201  11.734  16.469  1.00 35.27 ? 166 GLN   B NE2 1 
ATOM   2947 N N   . PRO   B 1 188 ? -15.110 11.610  16.455  1.00 23.35 ? 167 PRO   B N   1 
ATOM   2948 C CA  . PRO   B 1 188 ? -16.196 11.989  15.549  1.00 26.18 ? 167 PRO   B CA  1 
ATOM   2949 C C   . PRO   B 1 188 ? -16.538 13.476  15.545  1.00 26.02 ? 167 PRO   B C   1 
ATOM   2950 O O   . PRO   B 1 188 ? -16.348 14.163  16.552  1.00 29.26 ? 167 PRO   B O   1 
ATOM   2951 C CB  . PRO   B 1 188 ? -17.343 11.164  16.126  1.00 24.87 ? 167 PRO   B CB  1 
ATOM   2952 C CG  . PRO   B 1 188 ? -17.085 11.115  17.590  1.00 27.00 ? 167 PRO   B CG  1 
ATOM   2953 C CD  . PRO   B 1 188 ? -15.556 10.863  17.634  1.00 22.00 ? 167 PRO   B CD  1 
ATOM   2954 N N   . CYS   B 1 189 ? -17.168 13.942  14.455  1.00 27.94 ? 168 CYS   B N   1 
ATOM   2955 C CA  . CYS   B 1 189 ? -17.755 15.281  14.454  1.00 28.94 ? 168 CYS   B CA  1 
ATOM   2956 C C   . CYS   B 1 189 ? -18.940 15.313  15.418  1.00 28.73 ? 168 CYS   B C   1 
ATOM   2957 O O   . CYS   B 1 189 ? -19.717 14.374  15.510  1.00 26.33 ? 168 CYS   B O   1 
ATOM   2958 C CB  . CYS   B 1 189 ? -18.243 15.676  13.068  1.00 30.43 ? 168 CYS   B CB  1 
ATOM   2959 S SG  . CYS   B 1 189 ? -16.879 15.999  11.901  1.00 43.23 ? 168 CYS   B SG  1 
ATOM   2960 N N   . MET   B 1 190 ? -19.080 16.429  16.125  1.00 30.88 ? 169 MET   B N   1 
ATOM   2961 C CA  . MET   B 1 190 ? -20.198 16.680  17.009  1.00 32.05 ? 169 MET   B CA  1 
ATOM   2962 C C   . MET   B 1 190 ? -21.518 16.505  16.245  1.00 27.56 ? 169 MET   B C   1 
ATOM   2963 O O   . MET   B 1 190 ? -21.651 17.046  15.154  1.00 25.85 ? 169 MET   B O   1 
ATOM   2964 C CB  . MET   B 1 190 ? -20.104 18.150  17.449  1.00 35.82 ? 169 MET   B CB  1 
ATOM   2965 C CG  . MET   B 1 190 ? -21.227 18.612  18.335  1.00 40.64 ? 169 MET   B CG  1 
ATOM   2966 S SD  . MET   B 1 190 ? -21.147 17.643  19.852  1.00 47.28 ? 169 MET   B SD  1 
ATOM   2967 C CE  . MET   B 1 190 ? -19.712 18.322  20.707  1.00 35.05 ? 169 MET   B CE  1 
ATOM   2968 N N   . ALA   B 1 191 ? -22.490 15.797  16.851  1.00 24.82 ? 170 ALA   B N   1 
ATOM   2969 C CA  . ALA   B 1 191 ? -23.861 15.674  16.357  1.00 25.08 ? 170 ALA   B CA  1 
ATOM   2970 C C   . ALA   B 1 191 ? -23.967 14.785  15.119  1.00 23.58 ? 170 ALA   B C   1 
ATOM   2971 O O   . ALA   B 1 191 ? -24.943 14.897  14.378  1.00 24.82 ? 170 ALA   B O   1 
ATOM   2972 C CB  . ALA   B 1 191 ? -24.500 17.049  16.058  1.00 27.41 ? 170 ALA   B CB  1 
ATOM   2973 N N   . PHE   B 1 192 ? -23.003 13.867  14.922  1.00 22.16 ? 171 PHE   B N   1 
ATOM   2974 C CA  . PHE   B 1 192 ? -23.043 12.938  13.795  1.00 21.11 ? 171 PHE   B CA  1 
ATOM   2975 C C   . PHE   B 1 192 ? -23.163 11.501  14.293  1.00 21.78 ? 171 PHE   B C   1 
ATOM   2976 O O   . PHE   B 1 192 ? -22.595 10.584  13.702  1.00 20.07 ? 171 PHE   B O   1 
ATOM   2977 C CB  . PHE   B 1 192 ? -21.856 13.107  12.849  1.00 20.50 ? 171 PHE   B CB  1 
ATOM   2978 C CG  . PHE   B 1 192 ? -21.998 14.275  11.885  1.00 22.59 ? 171 PHE   B CG  1 
ATOM   2979 C CD1 . PHE   B 1 192 ? -21.724 15.580  12.294  1.00 26.61 ? 171 PHE   B CD1 1 
ATOM   2980 C CD2 . PHE   B 1 192 ? -22.356 14.049  10.547  1.00 25.99 ? 171 PHE   B CD2 1 
ATOM   2981 C CE1 . PHE   B 1 192 ? -21.836 16.653  11.403  1.00 27.96 ? 171 PHE   B CE1 1 
ATOM   2982 C CE2 . PHE   B 1 192 ? -22.475 15.121  9.674   1.00 25.89 ? 171 PHE   B CE2 1 
ATOM   2983 C CZ  . PHE   B 1 192 ? -22.234 16.424  10.112  1.00 28.58 ? 171 PHE   B CZ  1 
ATOM   2984 N N   . SER   B 1 193 ? -23.984 11.287  15.328  1.00 20.12 ? 172 SER   B N   1 
ATOM   2985 C CA  A SER   B 1 193 ? -23.979 9.960   15.929  0.60 22.37 ? 172 SER   B CA  1 
ATOM   2986 C CA  B SER   B 1 193 ? -24.092 9.968   15.953  0.40 21.15 ? 172 SER   B CA  1 
ATOM   2987 C C   . SER   B 1 193 ? -24.428 8.882   14.929  1.00 20.33 ? 172 SER   B C   1 
ATOM   2988 O O   . SER   B 1 193 ? -23.816 7.807   14.891  1.00 19.64 ? 172 SER   B O   1 
ATOM   2989 C CB  A SER   B 1 193 ? -24.765 9.918   17.230  0.60 24.35 ? 172 SER   B CB  1 
ATOM   2990 C CB  B SER   B 1 193 ? -25.129 9.937   17.069  0.40 20.81 ? 172 SER   B CB  1 
ATOM   2991 O OG  A SER   B 1 193 ? -26.079 10.383  16.985  0.60 25.26 ? 172 SER   B OG  1 
ATOM   2992 O OG  B SER   B 1 193 ? -24.658 10.598  18.229  0.40 17.78 ? 172 SER   B OG  1 
ATOM   2993 N N   . LEU   B 1 194 ? -25.493 9.116   14.123  1.00 20.98 ? 173 LEU   B N   1 
ATOM   2994 C CA  . LEU   B 1 194 ? -25.992 8.022   13.281  1.00 21.04 ? 173 LEU   B CA  1 
ATOM   2995 C C   . LEU   B 1 194 ? -24.976 7.703   12.180  1.00 18.90 ? 173 LEU   B C   1 
ATOM   2996 O O   . LEU   B 1 194 ? -24.748 6.533   11.824  1.00 20.11 ? 173 LEU   B O   1 
ATOM   2997 C CB  . LEU   B 1 194 ? -27.385 8.313   12.678  1.00 19.62 ? 173 LEU   B CB  1 
ATOM   2998 C CG  . LEU   B 1 194 ? -28.538 8.065   13.659  1.00 18.97 ? 173 LEU   B CG  1 
ATOM   2999 C CD1 . LEU   B 1 194 ? -29.786 8.667   13.001  1.00 20.90 ? 173 LEU   B CD1 1 
ATOM   3000 C CD2 . LEU   B 1 194 ? -28.746 6.559   13.862  1.00 21.49 ? 173 LEU   B CD2 1 
ATOM   3001 N N   . TYR   B 1 195 ? -24.355 8.755   11.638  1.00 20.52 ? 174 TYR   B N   1 
ATOM   3002 C CA  . TYR   B 1 195 ? -23.304 8.555   10.649  1.00 21.87 ? 174 TYR   B CA  1 
ATOM   3003 C C   . TYR   B 1 195 ? -22.185 7.708   11.261  1.00 19.71 ? 174 TYR   B C   1 
ATOM   3004 O O   . TYR   B 1 195 ? -21.751 6.718   10.665  1.00 19.94 ? 174 TYR   B O   1 
ATOM   3005 C CB  . TYR   B 1 195 ? -22.792 9.899   10.096  1.00 18.02 ? 174 TYR   B CB  1 
ATOM   3006 C CG  . TYR   B 1 195 ? -21.537 9.681   9.253   1.00 19.93 ? 174 TYR   B CG  1 
ATOM   3007 C CD1 . TYR   B 1 195 ? -21.638 9.289   7.925   1.00 21.19 ? 174 TYR   B CD1 1 
ATOM   3008 C CD2 . TYR   B 1 195 ? -20.258 9.899   9.782   1.00 19.28 ? 174 TYR   B CD2 1 
ATOM   3009 C CE1 . TYR   B 1 195 ? -20.500 9.063   7.160   1.00 21.47 ? 174 TYR   B CE1 1 
ATOM   3010 C CE2 . TYR   B 1 195 ? -19.112 9.730   9.016   1.00 22.21 ? 174 TYR   B CE2 1 
ATOM   3011 C CZ  . TYR   B 1 195 ? -19.243 9.318   7.696   1.00 22.72 ? 174 TYR   B CZ  1 
ATOM   3012 O OH  . TYR   B 1 195 ? -18.173 9.109   6.886   1.00 25.01 ? 174 TYR   B OH  1 
ATOM   3013 N N   . ASN   B 1 196 ? -21.791 8.056   12.488  1.00 19.18 ? 175 ASN   B N   1 
ATOM   3014 C CA  A ASN   B 1 196 ? -20.660 7.426   13.165  0.60 19.15 ? 175 ASN   B CA  1 
ATOM   3015 C CA  B ASN   B 1 196 ? -20.659 7.411   13.134  0.40 18.99 ? 175 ASN   B CA  1 
ATOM   3016 C C   . ASN   B 1 196 ? -21.035 5.981   13.498  1.00 20.02 ? 175 ASN   B C   1 
ATOM   3017 O O   . ASN   B 1 196 ? -20.239 5.063   13.319  1.00 19.42 ? 175 ASN   B O   1 
ATOM   3018 C CB  A ASN   B 1 196 ? -20.253 8.233   14.401  0.60 22.41 ? 175 ASN   B CB  1 
ATOM   3019 C CB  B ASN   B 1 196 ? -20.109 8.262   14.272  0.40 20.66 ? 175 ASN   B CB  1 
ATOM   3020 C CG  A ASN   B 1 196 ? -18.966 7.771   15.045  0.60 24.01 ? 175 ASN   B CG  1 
ATOM   3021 C CG  B ASN   B 1 196 ? -19.202 9.318   13.700  0.40 20.51 ? 175 ASN   B CG  1 
ATOM   3022 O OD1 A ASN   B 1 196 ? -18.951 7.431   16.239  0.60 27.43 ? 175 ASN   B OD1 1 
ATOM   3023 O OD1 B ASN   B 1 196 ? -18.133 8.979   13.172  0.40 25.67 ? 175 ASN   B OD1 1 
ATOM   3024 N ND2 A ASN   B 1 196 ? -17.874 7.790   14.293  0.60 21.52 ? 175 ASN   B ND2 1 
ATOM   3025 N ND2 B ASN   B 1 196 ? -19.624 10.572  13.723  0.40 18.85 ? 175 ASN   B ND2 1 
ATOM   3026 N N   . MET   B 1 197 ? -22.274 5.781   13.960  1.00 19.09 ? 176 MET   B N   1 
ATOM   3027 C CA  . MET   B 1 197 ? -22.735 4.413   14.180  1.00 17.99 ? 176 MET   B CA  1 
ATOM   3028 C C   . MET   B 1 197 ? -22.650 3.590   12.893  1.00 18.71 ? 176 MET   B C   1 
ATOM   3029 O O   . MET   B 1 197 ? -22.273 2.407   12.957  1.00 17.40 ? 176 MET   B O   1 
ATOM   3030 C CB  . MET   B 1 197 ? -24.173 4.436   14.715  1.00 18.82 ? 176 MET   B CB  1 
ATOM   3031 C CG  . MET   B 1 197 ? -24.259 4.962   16.134  1.00 19.46 ? 176 MET   B CG  1 
ATOM   3032 S SD  . MET   B 1 197 ? -25.992 5.317   16.542  1.00 22.63 ? 176 MET   B SD  1 
ATOM   3033 C CE  . MET   B 1 197 ? -26.611 3.629   16.616  1.00 21.30 ? 176 MET   B CE  1 
ATOM   3034 N N   . GLY   B 1 198 ? -23.104 4.162   11.766  1.00 17.31 ? 177 GLY   B N   1 
ATOM   3035 C CA  . GLY   B 1 198 ? -23.095 3.400   10.514  1.00 19.70 ? 177 GLY   B CA  1 
ATOM   3036 C C   . GLY   B 1 198 ? -21.661 3.042   10.117  1.00 19.72 ? 177 GLY   B C   1 
ATOM   3037 O O   . GLY   B 1 198 ? -21.371 1.936   9.694   1.00 17.13 ? 177 GLY   B O   1 
ATOM   3038 N N   . LYS   B 1 199 ? -20.724 3.991   10.226  1.00 17.74 ? 178 LYS   B N   1 
ATOM   3039 C CA  . LYS   B 1 199 ? -19.348 3.664   9.833   1.00 18.12 ? 178 LYS   B CA  1 
ATOM   3040 C C   . LYS   B 1 199 ? -18.665 2.715   10.821  1.00 18.95 ? 178 LYS   B C   1 
ATOM   3041 O O   . LYS   B 1 199 ? -17.847 1.918   10.421  1.00 18.51 ? 178 LYS   B O   1 
ATOM   3042 C CB  . LYS   B 1 199 ? -18.513 4.946   9.732   1.00 18.43 ? 178 LYS   B CB  1 
ATOM   3043 C CG  . LYS   B 1 199 ? -18.930 5.789   8.490   1.00 19.74 ? 178 LYS   B CG  1 
ATOM   3044 C CD  . LYS   B 1 199 ? -18.753 5.076   7.139   1.00 19.40 ? 178 LYS   B CD  1 
ATOM   3045 C CE  . LYS   B 1 199 ? -18.809 5.951   5.899   1.00 21.63 ? 178 LYS   B CE  1 
ATOM   3046 N NZ  . LYS   B 1 199 ? -18.768 5.257   4.602   1.00 20.98 ? 178 LYS   B NZ  1 
ATOM   3047 N N   . HIS   B 1 200 ? -19.039 2.731   12.108  1.00 18.44 ? 179 HIS   B N   1 
ATOM   3048 C CA  . HIS   B 1 200 ? -18.466 1.725   12.998  1.00 19.74 ? 179 HIS   B CA  1 
ATOM   3049 C C   . HIS   B 1 200 ? -19.029 0.356   12.618  1.00 18.01 ? 179 HIS   B C   1 
ATOM   3050 O O   . HIS   B 1 200 ? -18.324 -0.674  12.681  1.00 17.80 ? 179 HIS   B O   1 
ATOM   3051 C CB  . HIS   B 1 200 ? -18.890 1.984   14.451  1.00 17.57 ? 179 HIS   B CB  1 
ATOM   3052 C CG  . HIS   B 1 200 ? -17.900 2.851   15.151  1.00 20.64 ? 179 HIS   B CG  1 
ATOM   3053 N ND1 . HIS   B 1 200 ? -16.841 2.287   15.832  1.00 23.77 ? 179 HIS   B ND1 1 
ATOM   3054 C CD2 . HIS   B 1 200 ? -17.752 4.181   15.237  1.00 23.36 ? 179 HIS   B CD2 1 
ATOM   3055 C CE1 . HIS   B 1 200 ? -16.091 3.264   16.361  1.00 22.28 ? 179 HIS   B CE1 1 
ATOM   3056 N NE2 . HIS   B 1 200 ? -16.653 4.424   16.033  1.00 25.81 ? 179 HIS   B NE2 1 
ATOM   3057 N N   . ALA   B 1 201 ? -20.326 0.340   12.304  1.00 18.15 ? 180 ALA   B N   1 
ATOM   3058 C CA  . ALA   B 1 201 ? -20.935 -0.936  11.905  1.00 17.67 ? 180 ALA   B CA  1 
ATOM   3059 C C   . ALA   B 1 201 ? -20.213 -1.506  10.688  1.00 17.17 ? 180 ALA   B C   1 
ATOM   3060 O O   . ALA   B 1 201 ? -20.072 -2.722  10.533  1.00 18.67 ? 180 ALA   B O   1 
ATOM   3061 C CB  . ALA   B 1 201 ? -22.419 -0.763  11.575  1.00 18.82 ? 180 ALA   B CB  1 
ATOM   3062 N N   . LEU   B 1 202 ? -19.812 -0.625  9.779   1.00 16.18 ? 181 LEU   B N   1 
ATOM   3063 C CA  . LEU   B 1 202 ? -19.108 -1.030  8.567   1.00 18.35 ? 181 LEU   B CA  1 
ATOM   3064 C C   . LEU   B 1 202 ? -17.750 -1.650  8.905   1.00 18.76 ? 181 LEU   B C   1 
ATOM   3065 O O   . LEU   B 1 202 ? -17.330 -2.606  8.246   1.00 19.46 ? 181 LEU   B O   1 
ATOM   3066 C CB  . LEU   B 1 202 ? -18.952 0.202   7.638   1.00 15.93 ? 181 LEU   B CB  1 
ATOM   3067 C CG  . LEU   B 1 202 ? -18.468 -0.159  6.219   1.00 18.09 ? 181 LEU   B CG  1 
ATOM   3068 C CD1 . LEU   B 1 202 ? -19.297 -1.249  5.489   1.00 18.83 ? 181 LEU   B CD1 1 
ATOM   3069 C CD2 . LEU   B 1 202 ? -18.308 1.129   5.378   1.00 20.01 ? 181 LEU   B CD2 1 
ATOM   3070 N N   . VAL   B 1 203 ? -17.062 -1.116  9.943   1.00 17.73 ? 182 VAL   B N   1 
ATOM   3071 C CA  . VAL   B 1 203 ? -15.848 -1.783  10.429  1.00 17.53 ? 182 VAL   B CA  1 
ATOM   3072 C C   . VAL   B 1 203 ? -16.184 -3.210  10.867  1.00 18.36 ? 182 VAL   B C   1 
ATOM   3073 O O   . VAL   B 1 203 ? -15.450 -4.143  10.550  1.00 18.98 ? 182 VAL   B O   1 
ATOM   3074 C CB  . VAL   B 1 203 ? -15.174 -1.013  11.594  1.00 19.08 ? 182 VAL   B CB  1 
ATOM   3075 C CG1 . VAL   B 1 203 ? -13.994 -1.799  12.180  1.00 18.20 ? 182 VAL   B CG1 1 
ATOM   3076 C CG2 . VAL   B 1 203 ? -14.696 0.366   11.115  1.00 22.04 ? 182 VAL   B CG2 1 
ATOM   3077 N N   . GLY   B 1 204 ? -17.268 -3.355  11.648  1.00 18.45 ? 183 GLY   B N   1 
ATOM   3078 C CA  . GLY   B 1 204 ? -17.618 -4.691  12.125  1.00 19.54 ? 183 GLY   B CA  1 
ATOM   3079 C C   . GLY   B 1 204 ? -17.919 -5.605  10.948  1.00 18.13 ? 183 GLY   B C   1 
ATOM   3080 O O   . GLY   B 1 204 ? -17.499 -6.759  10.947  1.00 19.76 ? 183 GLY   B O   1 
ATOM   3081 N N   . LEU   B 1 205 ? -18.620 -5.086  9.923   1.00 19.14 ? 184 LEU   B N   1 
ATOM   3082 C CA  . LEU   B 1 205 ? -18.929 -5.901  8.749   1.00 21.04 ? 184 LEU   B CA  1 
ATOM   3083 C C   . LEU   B 1 205 ? -17.624 -6.337  8.074   1.00 20.06 ? 184 LEU   B C   1 
ATOM   3084 O O   . LEU   B 1 205 ? -17.492 -7.506  7.694   1.00 20.58 ? 184 LEU   B O   1 
ATOM   3085 C CB  . LEU   B 1 205 ? -19.797 -5.167  7.728   1.00 19.38 ? 184 LEU   B CB  1 
ATOM   3086 C CG  . LEU   B 1 205 ? -19.985 -5.896  6.387   1.00 17.86 ? 184 LEU   B CG  1 
ATOM   3087 C CD1 . LEU   B 1 205 ? -20.636 -7.245  6.613   1.00 19.26 ? 184 LEU   B CD1 1 
ATOM   3088 C CD2 . LEU   B 1 205 ? -20.830 -4.939  5.524   1.00 19.88 ? 184 LEU   B CD2 1 
ATOM   3089 N N   . THR   B 1 206 ? -16.698 -5.382  7.900   1.00 17.05 ? 185 THR   B N   1 
ATOM   3090 C CA  . THR   B 1 206 ? -15.415 -5.683  7.276   1.00 18.11 ? 185 THR   B CA  1 
ATOM   3091 C C   . THR   B 1 206 ? -14.733 -6.867  7.962   1.00 20.15 ? 185 THR   B C   1 
ATOM   3092 O O   . THR   B 1 206 ? -14.282 -7.815  7.292   1.00 20.62 ? 185 THR   B O   1 
ATOM   3093 C CB  . THR   B 1 206 ? -14.512 -4.445  7.249   1.00 19.65 ? 185 THR   B CB  1 
ATOM   3094 O OG1 . THR   B 1 206 ? -15.208 -3.416  6.545   1.00 18.08 ? 185 THR   B OG1 1 
ATOM   3095 C CG2 . THR   B 1 206 ? -13.251 -4.705  6.422   1.00 20.20 ? 185 THR   B CG2 1 
ATOM   3096 N N   . GLN   B 1 207 ? -14.676 -6.802  9.307   1.00 19.42 ? 186 GLN   B N   1 
ATOM   3097 C CA  . GLN   B 1 207 ? -14.008 -7.857  10.048  1.00 19.56 ? 186 GLN   B CA  1 
ATOM   3098 C C   . GLN   B 1 207 ? -14.813 -9.148  9.978   1.00 20.02 ? 186 GLN   B C   1 
ATOM   3099 O O   . GLN   B 1 207 ? -14.224 -10.209 9.767   1.00 19.15 ? 186 GLN   B O   1 
ATOM   3100 C CB  . GLN   B 1 207 ? -13.836 -7.449  11.511  1.00 19.81 ? 186 GLN   B CB  1 
ATOM   3101 C CG  . GLN   B 1 207 ? -12.885 -6.263  11.599  1.00 21.43 ? 186 GLN   B CG  1 
ATOM   3102 C CD  . GLN   B 1 207 ? -12.613 -5.662  12.959  1.00 26.42 ? 186 GLN   B CD  1 
ATOM   3103 O OE1 . GLN   B 1 207 ? -11.622 -4.926  13.121  1.00 36.12 ? 186 GLN   B OE1 1 
ATOM   3104 N NE2 . GLN   B 1 207 ? -13.497 -5.863  13.900  1.00 25.07 ? 186 GLN   B NE2 1 
ATOM   3105 N N   . SER   B 1 208 ? -16.131 -9.054  10.236  1.00 20.65 ? 187 SER   B N   1 
ATOM   3106 C CA  . SER   B 1 208 ? -16.947 -10.272 10.291  1.00 21.19 ? 187 SER   B CA  1 
ATOM   3107 C C   . SER   B 1 208 ? -16.949 -10.959 8.926   1.00 21.34 ? 187 SER   B C   1 
ATOM   3108 O O   . SER   B 1 208 ? -16.848 -12.180 8.836   1.00 21.52 ? 187 SER   B O   1 
ATOM   3109 C CB  . SER   B 1 208 ? -18.359 -10.020 10.769  1.00 22.01 ? 187 SER   B CB  1 
ATOM   3110 O OG  . SER   B 1 208 ? -18.382 -9.781  12.169  1.00 19.99 ? 187 SER   B OG  1 
ATOM   3111 N N   . ALA   B 1 209 ? -17.075 -10.180 7.847   1.00 19.29 ? 188 ALA   B N   1 
ATOM   3112 C CA  . ALA   B 1 209 ? -17.178 -10.842 6.547   1.00 22.15 ? 188 ALA   B CA  1 
ATOM   3113 C C   . ALA   B 1 209 ? -15.809 -11.366 6.115   1.00 20.89 ? 188 ALA   B C   1 
ATOM   3114 O O   . ALA   B 1 209 ? -15.703 -12.386 5.421   1.00 20.14 ? 188 ALA   B O   1 
ATOM   3115 C CB  . ALA   B 1 209 ? -17.749 -9.853  5.555   1.00 21.87 ? 188 ALA   B CB  1 
ATOM   3116 N N   . ALA   B 1 210 ? -14.735 -10.650 6.479   1.00 19.92 ? 189 ALA   B N   1 
ATOM   3117 C CA  . ALA   B 1 210 ? -13.397 -11.180 6.181   1.00 19.25 ? 189 ALA   B CA  1 
ATOM   3118 C C   . ALA   B 1 210 ? -13.228 -12.565 6.815   1.00 19.87 ? 189 ALA   B C   1 
ATOM   3119 O O   . ALA   B 1 210 ? -12.705 -13.474 6.169   1.00 22.01 ? 189 ALA   B O   1 
ATOM   3120 C CB  . ALA   B 1 210 ? -12.309 -10.245 6.697   1.00 19.55 ? 189 ALA   B CB  1 
ATOM   3121 N N   . LEU   B 1 211 ? -13.662 -12.731 8.079   1.00 22.18 ? 190 LEU   B N   1 
ATOM   3122 C CA  . LEU   B 1 211 ? -13.474 -14.033 8.720   1.00 25.49 ? 190 LEU   B CA  1 
ATOM   3123 C C   . LEU   B 1 211 ? -14.344 -15.086 8.020   1.00 25.74 ? 190 LEU   B C   1 
ATOM   3124 O O   . LEU   B 1 211 ? -13.905 -16.216 7.740   1.00 24.67 ? 190 LEU   B O   1 
ATOM   3125 C CB  . LEU   B 1 211 ? -13.908 -13.865 10.180  1.00 26.89 ? 190 LEU   B CB  1 
ATOM   3126 C CG  . LEU   B 1 211 ? -13.906 -15.129 11.045  1.00 30.78 ? 190 LEU   B CG  1 
ATOM   3127 C CD1 . LEU   B 1 211 ? -12.473 -15.523 11.368  1.00 28.86 ? 190 LEU   B CD1 1 
ATOM   3128 C CD2 . LEU   B 1 211 ? -14.691 -14.832 12.336  1.00 30.78 ? 190 LEU   B CD2 1 
ATOM   3129 N N   . GLU   B 1 212 ? -15.588 -14.709 7.726   1.00 23.30 ? 191 GLU   B N   1 
ATOM   3130 C CA  . GLU   B 1 212 ? -16.560 -15.684 7.222   1.00 25.80 ? 191 GLU   B CA  1 
ATOM   3131 C C   . GLU   B 1 212 ? -16.324 -16.033 5.752   1.00 26.54 ? 191 GLU   B C   1 
ATOM   3132 O O   . GLU   B 1 212 ? -16.551 -17.186 5.357   1.00 28.01 ? 191 GLU   B O   1 
ATOM   3133 C CB  . GLU   B 1 212 ? -17.985 -15.170 7.419   1.00 25.33 ? 191 GLU   B CB  1 
ATOM   3134 C CG  . GLU   B 1 212 ? -19.068 -16.164 7.003   1.00 26.45 ? 191 GLU   B CG  1 
ATOM   3135 C CD  . GLU   B 1 212 ? -20.435 -15.670 7.448   1.00 29.30 ? 191 GLU   B CD  1 
ATOM   3136 O OE1 . GLU   B 1 212 ? -21.412 -16.328 7.045   1.00 27.89 ? 191 GLU   B OE1 1 
ATOM   3137 O OE2 . GLU   B 1 212 ? -20.523 -14.606 8.133   1.00 28.08 ? 191 GLU   B OE2 1 
ATOM   3138 N N   . LEU   B 1 213 ? -15.865 -15.070 4.940   1.00 22.18 ? 192 LEU   B N   1 
ATOM   3139 C CA  . LEU   B 1 213 ? -15.665 -15.351 3.514   1.00 22.79 ? 192 LEU   B CA  1 
ATOM   3140 C C   . LEU   B 1 213 ? -14.251 -15.852 3.176   1.00 25.93 ? 192 LEU   B C   1 
ATOM   3141 O O   . LEU   B 1 213 ? -13.983 -16.299 2.045   1.00 24.58 ? 192 LEU   B O   1 
ATOM   3142 C CB  . LEU   B 1 213 ? -16.093 -14.153 2.654   1.00 22.89 ? 192 LEU   B CB  1 
ATOM   3143 C CG  . LEU   B 1 213 ? -17.520 -13.667 2.956   1.00 22.31 ? 192 LEU   B CG  1 
ATOM   3144 C CD1 . LEU   B 1 213 ? -17.796 -12.418 2.108   1.00 21.78 ? 192 LEU   B CD1 1 
ATOM   3145 C CD2 . LEU   B 1 213 ? -18.586 -14.741 2.656   1.00 23.17 ? 192 LEU   B CD2 1 
ATOM   3146 N N   . ALA   B 1 214 ? -13.338 -15.814 4.152   1.00 23.79 ? 193 ALA   B N   1 
ATOM   3147 C CA  . ALA   B 1 214 ? -11.967 -16.241 3.902   1.00 27.38 ? 193 ALA   B CA  1 
ATOM   3148 C C   . ALA   B 1 214 ? -11.933 -17.664 3.321   1.00 31.20 ? 193 ALA   B C   1 
ATOM   3149 O O   . ALA   B 1 214 ? -11.171 -17.913 2.393   1.00 29.66 ? 193 ALA   B O   1 
ATOM   3150 C CB  . ALA   B 1 214 ? -11.102 -16.114 5.139   1.00 30.44 ? 193 ALA   B CB  1 
ATOM   3151 N N   . PRO   B 1 215 ? -12.728 -18.643 3.822   1.00 31.15 ? 194 PRO   B N   1 
ATOM   3152 C CA  . PRO   B 1 215 ? -12.696 -20.001 3.264   1.00 34.85 ? 194 PRO   B CA  1 
ATOM   3153 C C   . PRO   B 1 215 ? -13.150 -20.075 1.802   1.00 37.04 ? 194 PRO   B C   1 
ATOM   3154 O O   . PRO   B 1 215 ? -12.817 -21.023 1.097   1.00 39.97 ? 194 PRO   B O   1 
ATOM   3155 C CB  . PRO   B 1 215 ? -13.554 -20.847 4.229   1.00 34.31 ? 194 PRO   B CB  1 
ATOM   3156 C CG  . PRO   B 1 215 ? -13.759 -19.983 5.482   1.00 36.87 ? 194 PRO   B CG  1 
ATOM   3157 C CD  . PRO   B 1 215 ? -13.638 -18.541 4.980   1.00 31.39 ? 194 PRO   B CD  1 
ATOM   3158 N N   . TYR   B 1 216 ? -13.858 -19.049 1.312   1.00 32.73 ? 195 TYR   B N   1 
ATOM   3159 C CA  . TYR   B 1 216 ? -14.241 -19.014 -0.088  1.00 31.05 ? 195 TYR   B CA  1 
ATOM   3160 C C   . TYR   B 1 216 ? -13.201 -18.245 -0.907  1.00 29.85 ? 195 TYR   B C   1 
ATOM   3161 O O   . TYR   B 1 216 ? -13.347 -18.097 -2.106  1.00 34.18 ? 195 TYR   B O   1 
ATOM   3162 C CB  . TYR   B 1 216 ? -15.586 -18.326 -0.294  1.00 36.55 ? 195 TYR   B CB  1 
ATOM   3163 C CG  . TYR   B 1 216 ? -16.695 -18.998 0.491   1.00 39.86 ? 195 TYR   B CG  1 
ATOM   3164 C CD1 . TYR   B 1 216 ? -16.988 -18.610 1.788   1.00 38.40 ? 195 TYR   B CD1 1 
ATOM   3165 C CD2 . TYR   B 1 216 ? -17.432 -20.046 -0.058  1.00 49.10 ? 195 TYR   B CD2 1 
ATOM   3166 C CE1 . TYR   B 1 216 ? -17.999 -19.218 2.514   1.00 41.52 ? 195 TYR   B CE1 1 
ATOM   3167 C CE2 . TYR   B 1 216 ? -18.452 -20.659 0.655   1.00 46.94 ? 195 TYR   B CE2 1 
ATOM   3168 C CZ  . TYR   B 1 216 ? -18.742 -20.235 1.940   1.00 51.88 ? 195 TYR   B CZ  1 
ATOM   3169 O OH  . TYR   B 1 216 ? -19.739 -20.828 2.665   1.00 62.31 ? 195 TYR   B OH  1 
ATOM   3170 N N   . GLY   B 1 217 ? -12.161 -17.734 -0.261  1.00 27.98 ? 196 GLY   B N   1 
ATOM   3171 C CA  . GLY   B 1 217 ? -11.135 -17.053 -1.037  1.00 31.80 ? 196 GLY   B CA  1 
ATOM   3172 C C   . GLY   B 1 217 ? -11.518 -15.603 -1.350  1.00 33.80 ? 196 GLY   B C   1 
ATOM   3173 O O   . GLY   B 1 217 ? -10.906 -14.974 -2.224  1.00 31.09 ? 196 GLY   B O   1 
ATOM   3174 N N   . ILE   B 1 218 ? -12.546 -15.093 -0.661  1.00 22.89 ? 197 ILE   B N   1 
ATOM   3175 C CA  . ILE   B 1 218 ? -12.949 -13.702 -0.879  1.00 21.27 ? 197 ILE   B CA  1 
ATOM   3176 C C   . ILE   B 1 218 ? -12.339 -12.866 0.248   1.00 22.41 ? 197 ILE   B C   1 
ATOM   3177 O O   . ILE   B 1 218 ? -12.645 -13.107 1.420   1.00 23.59 ? 197 ILE   B O   1 
ATOM   3178 C CB  . ILE   B 1 218 ? -14.488 -13.574 -0.842  1.00 21.75 ? 197 ILE   B CB  1 
ATOM   3179 C CG1 . ILE   B 1 218 ? -15.195 -14.504 -1.867  1.00 24.06 ? 197 ILE   B CG1 1 
ATOM   3180 C CG2 . ILE   B 1 218 ? -14.955 -12.125 -1.016  1.00 21.73 ? 197 ILE   B CG2 1 
ATOM   3181 C CD1 . ILE   B 1 218 ? -16.680 -14.689 -1.588  1.00 27.65 ? 197 ILE   B CD1 1 
ATOM   3182 N N   . ARG   B 1 219 ? -11.542 -11.876 -0.131  1.00 21.69 ? 198 ARG   B N   1 
ATOM   3183 C CA  . ARG   B 1 219 ? -10.914 -10.982 0.863   1.00 21.64 ? 198 ARG   B CA  1 
ATOM   3184 C C   . ARG   B 1 219 ? -11.841 -9.778  1.083   1.00 19.14 ? 198 ARG   B C   1 
ATOM   3185 O O   . ARG   B 1 219 ? -12.580 -9.418  0.176   1.00 22.08 ? 198 ARG   B O   1 
ATOM   3186 C CB  . ARG   B 1 219 ? -9.514  -10.583 0.390   1.00 20.66 ? 198 ARG   B CB  1 
ATOM   3187 C CG  . ARG   B 1 219 ? -8.524  -11.724 0.226   1.00 20.58 ? 198 ARG   B CG  1 
ATOM   3188 C CD  . ARG   B 1 219 ? -7.210  -11.242 -0.364  1.00 23.33 ? 198 ARG   B CD  1 
ATOM   3189 N NE  . ARG   B 1 219 ? -7.380  -10.579 -1.659  1.00 20.71 ? 198 ARG   B NE  1 
ATOM   3190 C CZ  . ARG   B 1 219 ? -7.237  -9.283  -1.885  1.00 26.65 ? 198 ARG   B CZ  1 
ATOM   3191 N NH1 . ARG   B 1 219 ? -6.941  -8.458  -0.899  1.00 23.27 ? 198 ARG   B NH1 1 
ATOM   3192 N NH2 . ARG   B 1 219 ? -7.399  -8.814  -3.105  1.00 23.53 ? 198 ARG   B NH2 1 
ATOM   3193 N N   . VAL   B 1 220 ? -11.775 -9.197  2.276   1.00 20.56 ? 199 VAL   B N   1 
ATOM   3194 C CA  . VAL   B 1 220 ? -12.683 -8.085  2.564   1.00 19.09 ? 199 VAL   B CA  1 
ATOM   3195 C C   . VAL   B 1 220 ? -11.865 -7.081  3.382   1.00 18.94 ? 199 VAL   B C   1 
ATOM   3196 O O   . VAL   B 1 220 ? -11.437 -7.429  4.475   1.00 19.22 ? 199 VAL   B O   1 
ATOM   3197 C CB  . VAL   B 1 220 ? -13.907 -8.560  3.373   1.00 20.28 ? 199 VAL   B CB  1 
ATOM   3198 C CG1 . VAL   B 1 220 ? -14.874 -7.397  3.699   1.00 21.08 ? 199 VAL   B CG1 1 
ATOM   3199 C CG2 . VAL   B 1 220 ? -14.661 -9.738  2.730   1.00 21.80 ? 199 VAL   B CG2 1 
ATOM   3200 N N   . ASN   B 1 221 ? -11.742 -5.837  2.886   1.00 19.11 ? 200 ASN   B N   1 
ATOM   3201 C CA  . ASN   B 1 221 ? -10.838 -4.869  3.479   1.00 17.08 ? 200 ASN   B CA  1 
ATOM   3202 C C   . ASN   B 1 221 ? -11.557 -3.534  3.460   1.00 15.42 ? 200 ASN   B C   1 
ATOM   3203 O O   . ASN   B 1 221 ? -12.600 -3.409  2.836   1.00 21.30 ? 200 ASN   B O   1 
ATOM   3204 C CB  . ASN   B 1 221 ? -9.522  -4.776  2.703   1.00 17.74 ? 200 ASN   B CB  1 
ATOM   3205 C CG  . ASN   B 1 221 ? -8.723  -6.062  2.848   1.00 20.49 ? 200 ASN   B CG  1 
ATOM   3206 O OD1 . ASN   B 1 221 ? -8.271  -6.353  3.956   1.00 20.15 ? 200 ASN   B OD1 1 
ATOM   3207 N ND2 . ASN   B 1 221 ? -8.598  -6.847  1.772   1.00 20.71 ? 200 ASN   B ND2 1 
ATOM   3208 N N   . GLY   B 1 222 ? -10.914 -2.529  4.066   1.00 17.86 ? 201 GLY   B N   1 
ATOM   3209 C CA  . GLY   B 1 222 ? -11.480 -1.198  3.994   1.00 18.78 ? 201 GLY   B CA  1 
ATOM   3210 C C   . GLY   B 1 222 ? -10.417 -0.157  3.665   1.00 17.15 ? 201 GLY   B C   1 
ATOM   3211 O O   . GLY   B 1 222 ? -9.232  -0.375  3.848   1.00 19.08 ? 201 GLY   B O   1 
ATOM   3212 N N   . VAL   B 1 223 ? -10.884 1.009   3.236   1.00 18.41 ? 202 VAL   B N   1 
ATOM   3213 C CA  . VAL   B 1 223 ? -10.033 2.174   3.064   1.00 18.36 ? 202 VAL   B CA  1 
ATOM   3214 C C   . VAL   B 1 223 ? -10.722 3.273   3.843   1.00 17.22 ? 202 VAL   B C   1 
ATOM   3215 O O   . VAL   B 1 223 ? -11.938 3.459   3.683   1.00 20.53 ? 202 VAL   B O   1 
ATOM   3216 C CB  . VAL   B 1 223 ? -9.997  2.527   1.562   1.00 18.26 ? 202 VAL   B CB  1 
ATOM   3217 C CG1 . VAL   B 1 223 ? -9.353  3.881   1.304   1.00 21.31 ? 202 VAL   B CG1 1 
ATOM   3218 C CG2 . VAL   B 1 223 ? -9.229  1.446   0.815   1.00 20.62 ? 202 VAL   B CG2 1 
ATOM   3219 N N   . ALA   B 1 224 ? -9.952  3.979   4.670   1.00 17.70 ? 203 ALA   B N   1 
ATOM   3220 C CA  . ALA   B 1 224 ? -10.553 4.963   5.562   1.00 19.38 ? 203 ALA   B CA  1 
ATOM   3221 C C   . ALA   B 1 224 ? -9.948  6.340   5.281   1.00 19.69 ? 203 ALA   B C   1 
ATOM   3222 O O   . ALA   B 1 224 ? -8.923  6.683   5.876   1.00 20.85 ? 203 ALA   B O   1 
ATOM   3223 C CB  . ALA   B 1 224 ? -10.269 4.547   7.001   1.00 19.87 ? 203 ALA   B CB  1 
ATOM   3224 N N   . PRO   B 1 225 ? -10.630 7.200   4.477   1.00 20.26 ? 204 PRO   B N   1 
ATOM   3225 C CA  . PRO   B 1 225 ? -10.197 8.570   4.254   1.00 20.67 ? 204 PRO   B CA  1 
ATOM   3226 C C   . PRO   B 1 225 ? -10.307 9.343   5.557   1.00 21.71 ? 204 PRO   B C   1 
ATOM   3227 O O   . PRO   B 1 225 ? -11.117 9.017   6.421   1.00 20.27 ? 204 PRO   B O   1 
ATOM   3228 C CB  . PRO   B 1 225 ? -11.227 9.102   3.242   1.00 19.93 ? 204 PRO   B CB  1 
ATOM   3229 C CG  . PRO   B 1 225 ? -11.800 7.866   2.599   1.00 22.28 ? 204 PRO   B CG  1 
ATOM   3230 C CD  . PRO   B 1 225 ? -11.913 6.916   3.799   1.00 22.96 ? 204 PRO   B CD  1 
ATOM   3231 N N   . GLY   B 1 226 ? -9.523  10.430  5.643   1.00 21.14 ? 205 GLY   B N   1 
ATOM   3232 C CA  . GLY   B 1 226 ? -9.721  11.405  6.707   1.00 22.52 ? 205 GLY   B CA  1 
ATOM   3233 C C   . GLY   B 1 226 ? -10.523 12.582  6.140   1.00 25.79 ? 205 GLY   B C   1 
ATOM   3234 O O   . GLY   B 1 226 ? -11.760 12.629  6.233   1.00 26.68 ? 205 GLY   B O   1 
ATOM   3235 N N   . VAL   B 1 227 ? -9.815  13.573  5.608   1.00 24.34 ? 206 VAL   B N   1 
ATOM   3236 C CA  A VAL   B 1 227 ? -10.410 14.630  4.784   0.60 25.51 ? 206 VAL   B CA  1 
ATOM   3237 C CA  B VAL   B 1 227 ? -10.495 14.550  4.775   0.40 24.78 ? 206 VAL   B CA  1 
ATOM   3238 C C   . VAL   B 1 227 ? -10.018 14.359  3.336   1.00 24.91 ? 206 VAL   B C   1 
ATOM   3239 O O   . VAL   B 1 227 ? -8.822  14.329  3.033   1.00 30.21 ? 206 VAL   B O   1 
ATOM   3240 C CB  A VAL   B 1 227 ? -9.908  16.044  5.155   0.60 28.25 ? 206 VAL   B CB  1 
ATOM   3241 C CB  B VAL   B 1 227 ? -10.370 15.989  5.311   0.40 26.42 ? 206 VAL   B CB  1 
ATOM   3242 C CG1 A VAL   B 1 227 ? -10.459 17.091  4.204   0.60 31.50 ? 206 VAL   B CG1 1 
ATOM   3243 C CG1 B VAL   B 1 227 ? -8.938  16.495  5.289   0.40 24.53 ? 206 VAL   B CG1 1 
ATOM   3244 C CG2 A VAL   B 1 227 ? -10.264 16.442  6.576   0.60 29.02 ? 206 VAL   B CG2 1 
ATOM   3245 C CG2 B VAL   B 1 227 ? -11.322 16.948  4.610   0.40 26.45 ? 206 VAL   B CG2 1 
ATOM   3246 N N   . SER   B 1 228 ? -10.999 14.129  2.472   1.00 26.14 ? 207 SER   B N   1 
ATOM   3247 C CA  . SER   B 1 228 ? -10.770 13.999  1.046   1.00 26.26 ? 207 SER   B CA  1 
ATOM   3248 C C   . SER   B 1 228 ? -11.569 15.114  0.386   1.00 29.49 ? 207 SER   B C   1 
ATOM   3249 O O   . SER   B 1 228 ? -11.601 16.235  0.914   1.00 32.40 ? 207 SER   B O   1 
ATOM   3250 C CB  . SER   B 1 228 ? -11.069 12.584  0.512   1.00 27.28 ? 207 SER   B CB  1 
ATOM   3251 O OG  . SER   B 1 228 ? -10.697 12.469  -0.864  1.00 28.17 ? 207 SER   B OG  1 
ATOM   3252 N N   . LEU   B 1 229 ? -12.173 14.837  -0.771  1.00 30.00 ? 208 LEU   B N   1 
ATOM   3253 C CA  . LEU   B 1 229 ? -12.916 15.884  -1.469  1.00 34.93 ? 208 LEU   B CA  1 
ATOM   3254 C C   . LEU   B 1 229 ? -13.966 16.487  -0.547  1.00 34.94 ? 208 LEU   B C   1 
ATOM   3255 O O   . LEU   B 1 229 ? -14.826 15.777  -0.022  1.00 33.86 ? 208 LEU   B O   1 
ATOM   3256 C CB  . LEU   B 1 229 ? -13.571 15.313  -2.720  1.00 38.93 ? 208 LEU   B CB  1 
ATOM   3257 C CG  . LEU   B 1 229 ? -12.580 14.859  -3.788  1.00 40.50 ? 208 LEU   B CG  1 
ATOM   3258 C CD1 . LEU   B 1 229 ? -13.346 14.619  -5.080  1.00 41.06 ? 208 LEU   B CD1 1 
ATOM   3259 C CD2 . LEU   B 1 229 ? -11.502 15.925  -3.951  1.00 43.63 ? 208 LEU   B CD2 1 
ATOM   3260 N N   . LEU   B 1 230 ? -13.869 17.797  -0.316  1.00 32.15 ? 209 LEU   B N   1 
ATOM   3261 C CA  . LEU   B 1 230 ? -14.879 18.435  0.526   1.00 36.68 ? 209 LEU   B CA  1 
ATOM   3262 C C   . LEU   B 1 230 ? -16.062 18.825  -0.363  1.00 38.12 ? 209 LEU   B C   1 
ATOM   3263 O O   . LEU   B 1 230 ? -15.886 18.881  -1.579  1.00 37.42 ? 209 LEU   B O   1 
ATOM   3264 C CB  . LEU   B 1 230 ? -14.247 19.640  1.222   1.00 38.45 ? 209 LEU   B CB  1 
ATOM   3265 C CG  . LEU   B 1 230 ? -13.157 19.266  2.232   1.00 41.01 ? 209 LEU   B CG  1 
ATOM   3266 C CD1 . LEU   B 1 230 ? -12.069 20.306  2.400   1.00 40.36 ? 209 LEU   B CD1 1 
ATOM   3267 C CD2 . LEU   B 1 230 ? -13.810 18.891  3.556   1.00 41.74 ? 209 LEU   B CD2 1 
ATOM   3268 N N   . PRO   B 1 231 ? -17.285 19.115  0.163   1.00 40.97 ? 210 PRO   B N   1 
ATOM   3269 C CA  . PRO   B 1 231 ? -18.401 19.559  -0.699  1.00 43.64 ? 210 PRO   B CA  1 
ATOM   3270 C C   . PRO   B 1 231 ? -18.038 20.793  -1.523  1.00 45.36 ? 210 PRO   B C   1 
ATOM   3271 O O   . PRO   B 1 231 ? -17.380 21.704  -1.011  1.00 40.77 ? 210 PRO   B O   1 
ATOM   3272 C CB  . PRO   B 1 231 ? -19.557 19.860  0.248   1.00 43.16 ? 210 PRO   B CB  1 
ATOM   3273 C CG  . PRO   B 1 231 ? -19.197 19.097  1.501   1.00 38.16 ? 210 PRO   B CG  1 
ATOM   3274 C CD  . PRO   B 1 231 ? -17.673 19.008  1.580   1.00 43.56 ? 210 PRO   B CD  1 
ATOM   3275 N N   . VAL   B 1 232 ? -18.462 20.837  -2.799  1.00 46.55 ? 211 VAL   B N   1 
ATOM   3276 C CA  . VAL   B 1 232 ? -17.936 21.880  -3.671  1.00 45.49 ? 211 VAL   B CA  1 
ATOM   3277 C C   . VAL   B 1 232 ? -18.476 23.241  -3.211  1.00 44.85 ? 211 VAL   B C   1 
ATOM   3278 O O   . VAL   B 1 232 ? -17.771 24.258  -3.299  1.00 48.23 ? 211 VAL   B O   1 
ATOM   3279 C CB  . VAL   B 1 232 ? -18.037 21.639  -5.195  1.00 52.91 ? 211 VAL   B CB  1 
ATOM   3280 C CG1 . VAL   B 1 232 ? -19.435 21.187  -5.615  1.00 53.65 ? 211 VAL   B CG1 1 
ATOM   3281 C CG2 . VAL   B 1 232 ? -17.553 22.835  -6.014  1.00 52.88 ? 211 VAL   B CG2 1 
ATOM   3282 N N   . ALA   B 1 233 ? -19.664 23.216  -2.587  1.00 37.71 ? 212 ALA   B N   1 
ATOM   3283 C CA  . ALA   B 1 233 ? -20.343 24.431  -2.155  1.00 41.56 ? 212 ALA   B CA  1 
ATOM   3284 C C   . ALA   B 1 233 ? -19.905 24.909  -0.765  1.00 37.37 ? 212 ALA   B C   1 
ATOM   3285 O O   . ALA   B 1 233 ? -20.226 26.039  -0.387  1.00 37.66 ? 212 ALA   B O   1 
ATOM   3286 C CB  . ALA   B 1 233 ? -21.849 24.255  -2.239  1.00 38.16 ? 212 ALA   B CB  1 
ATOM   3287 N N   . MET   B 1 234 ? -19.189 24.065  -0.004  1.00 35.30 ? 213 MET   B N   1 
ATOM   3288 C CA  . MET   B 1 234 ? -18.591 24.477  1.265   1.00 34.10 ? 213 MET   B CA  1 
ATOM   3289 C C   . MET   B 1 234 ? -17.597 25.610  0.986   1.00 33.09 ? 213 MET   B C   1 
ATOM   3290 O O   . MET   B 1 234 ? -16.788 25.490  0.074   1.00 33.27 ? 213 MET   B O   1 
ATOM   3291 C CB  . MET   B 1 234 ? -17.830 23.307  1.918   1.00 32.60 ? 213 MET   B CB  1 
ATOM   3292 C CG  . MET   B 1 234 ? -17.073 23.683  3.202   1.00 39.95 ? 213 MET   B CG  1 
ATOM   3293 S SD  . MET   B 1 234 ? -16.078 22.366  3.942   1.00 39.56 ? 213 MET   B SD  1 
ATOM   3294 C CE  . MET   B 1 234 ? -17.409 21.458  4.749   1.00 43.17 ? 213 MET   B CE  1 
ATOM   3295 N N   . GLY   B 1 235 ? -17.650 26.701  1.764   1.00 32.85 ? 214 GLY   B N   1 
ATOM   3296 C CA  . GLY   B 1 235 ? -16.797 27.864  1.535   1.00 35.43 ? 214 GLY   B CA  1 
ATOM   3297 C C   . GLY   B 1 235 ? -15.321 27.496  1.637   1.00 33.49 ? 214 GLY   B C   1 
ATOM   3298 O O   . GLY   B 1 235 ? -14.957 26.684  2.474   1.00 27.92 ? 214 GLY   B O   1 
ATOM   3299 N N   . GLU   B 1 236 ? -14.472 28.048  0.751   1.00 31.74 ? 215 GLU   B N   1 
ATOM   3300 C CA  . GLU   B 1 236 ? -13.054 27.720  0.821   1.00 32.34 ? 215 GLU   B CA  1 
ATOM   3301 C C   . GLU   B 1 236 ? -12.497 28.021  2.215   1.00 29.94 ? 215 GLU   B C   1 
ATOM   3302 O O   . GLU   B 1 236 ? -11.580 27.335  2.693   1.00 30.77 ? 215 GLU   B O   1 
ATOM   3303 C CB  . GLU   B 1 236 ? -12.224 28.459  -0.230  1.00 28.63 ? 215 GLU   B CB  1 
ATOM   3304 C CG  . GLU   B 1 236 ? -12.445 27.976  -1.657  1.00 27.48 ? 215 GLU   B CG  1 
ATOM   3305 C CD  . GLU   B 1 236 ? -11.950 26.564  -1.861  1.00 32.91 ? 215 GLU   B CD  1 
ATOM   3306 O OE1 . GLU   B 1 236 ? -12.672 25.761  -2.505  1.00 34.38 ? 215 GLU   B OE1 1 
ATOM   3307 O OE2 . GLU   B 1 236 ? -10.841 26.270  -1.361  1.00 33.14 ? 215 GLU   B OE2 1 
ATOM   3308 N N   . GLU   B 1 237 ? -13.026 29.057  2.877   1.00 30.49 ? 216 GLU   B N   1 
ATOM   3309 C CA  . GLU   B 1 237 ? -12.484 29.427  4.177   1.00 32.46 ? 216 GLU   B CA  1 
ATOM   3310 C C   . GLU   B 1 237 ? -12.785 28.324  5.204   1.00 32.71 ? 216 GLU   B C   1 
ATOM   3311 O O   . GLU   B 1 237 ? -11.987 28.109  6.098   1.00 33.47 ? 216 GLU   B O   1 
ATOM   3312 C CB  . GLU   B 1 237 ? -12.897 30.831  4.641   1.00 38.09 ? 216 GLU   B CB  1 
ATOM   3313 C CG  . GLU   B 1 237 ? -14.348 30.926  5.116   1.00 39.52 ? 216 GLU   B CG  1 
ATOM   3314 C CD  . GLU   B 1 237 ? -15.493 30.821  4.109   1.00 43.66 ? 216 GLU   B CD  1 
ATOM   3315 O OE1 . GLU   B 1 237 ? -16.638 30.697  4.605   1.00 39.51 ? 216 GLU   B OE1 1 
ATOM   3316 O OE2 . GLU   B 1 237 ? -15.288 30.863  2.863   1.00 33.57 ? 216 GLU   B OE2 1 
ATOM   3317 N N   . GLU   B 1 238 ? -13.912 27.614  5.044   1.00 31.91 ? 217 GLU   B N   1 
ATOM   3318 C CA  . GLU   B 1 238 ? -14.240 26.458  5.871   1.00 32.08 ? 217 GLU   B CA  1 
ATOM   3319 C C   . GLU   B 1 238 ? -13.390 25.251  5.460   1.00 30.56 ? 217 GLU   B C   1 
ATOM   3320 O O   . GLU   B 1 238 ? -12.882 24.540  6.343   1.00 28.80 ? 217 GLU   B O   1 
ATOM   3321 C CB  . GLU   B 1 238 ? -15.749 26.180  5.859   1.00 32.81 ? 217 GLU   B CB  1 
ATOM   3322 C CG  . GLU   B 1 238 ? -16.177 25.164  6.918   1.00 41.53 ? 217 GLU   B CG  1 
ATOM   3323 C CD  . GLU   B 1 238 ? -16.212 25.679  8.353   0.70 50.05 ? 217 GLU   B CD  1 
ATOM   3324 O OE1 . GLU   B 1 238 ? -16.483 24.855  9.259   0.70 57.08 ? 217 GLU   B OE1 1 
ATOM   3325 O OE2 . GLU   B 1 238 ? -15.972 26.889  8.585   0.70 51.25 ? 217 GLU   B OE2 1 
ATOM   3326 N N   . LYS   B 1 239 ? -13.218 25.035  4.136   1.00 28.21 ? 218 LYS   B N   1 
ATOM   3327 C CA  . LYS   B 1 239 ? -12.353 23.969  3.625   1.00 30.89 ? 218 LYS   B CA  1 
ATOM   3328 C C   . LYS   B 1 239 ? -10.937 24.075  4.199   1.00 32.23 ? 218 LYS   B C   1 
ATOM   3329 O O   . LYS   B 1 239 ? -10.325 23.074  4.599   1.00 29.54 ? 218 LYS   B O   1 
ATOM   3330 C CB  . LYS   B 1 239 ? -12.253 23.967  2.092   1.00 31.15 ? 218 LYS   B CB  1 
ATOM   3331 C CG  . LYS   B 1 239 ? -13.490 23.539  1.325   1.00 34.96 ? 218 LYS   B CG  1 
ATOM   3332 C CD  . LYS   B 1 239 ? -13.147 23.116  -0.104  1.00 35.04 ? 218 LYS   B CD  1 
ATOM   3333 C CE  . LYS   B 1 239 ? -14.328 22.846  -0.993  1.00 36.97 ? 218 LYS   B CE  1 
ATOM   3334 N NZ  . LYS   B 1 239 ? -14.985 24.075  -1.462  1.00 38.18 ? 218 LYS   B NZ  1 
ATOM   3335 N N   . ASP   B 1 240 ? -10.426 25.313  4.276   1.00 29.61 ? 219 ASP   B N   1 
ATOM   3336 C CA  . ASP   B 1 240 ? -9.114  25.612  4.833   1.00 30.82 ? 219 ASP   B CA  1 
ATOM   3337 C C   . ASP   B 1 240 ? -8.978  25.272  6.315   1.00 29.89 ? 219 ASP   B C   1 
ATOM   3338 O O   . ASP   B 1 240 ? -7.880  24.894  6.741   1.00 33.25 ? 219 ASP   B O   1 
ATOM   3339 C CB  . ASP   B 1 240 ? -8.758  27.075  4.604   1.00 31.37 ? 219 ASP   B CB  1 
ATOM   3340 C CG  . ASP   B 1 240 ? -8.279  27.384  3.203   1.00 37.49 ? 219 ASP   B CG  1 
ATOM   3341 O OD1 . ASP   B 1 240 ? -8.097  26.405  2.393   1.00 35.01 ? 219 ASP   B OD1 1 
ATOM   3342 O OD2 . ASP   B 1 240 ? -8.132  28.600  2.924   1.00 36.93 ? 219 ASP   B OD2 1 
ATOM   3343 N N   . LYS   B 1 241 ? -10.061 25.387  7.104   1.00 33.00 ? 220 LYS   B N   1 
ATOM   3344 C CA  . LYS   B 1 241 ? -10.003 24.983  8.511   1.00 32.89 ? 220 LYS   B CA  1 
ATOM   3345 C C   . LYS   B 1 241 ? -9.625  23.502  8.611   1.00 34.47 ? 220 LYS   B C   1 
ATOM   3346 O O   . LYS   B 1 241 ? -8.825  23.132  9.475   1.00 36.02 ? 220 LYS   B O   1 
ATOM   3347 C CB  . LYS   B 1 241 ? -11.246 25.295  9.347   1.00 33.79 ? 220 LYS   B CB  1 
ATOM   3348 C CG  . LYS   B 1 241 ? -11.463 26.800  9.420   1.00 43.32 ? 220 LYS   B CG  1 
ATOM   3349 C CD  . LYS   B 1 241 ? -12.630 27.317  10.245  1.00 43.61 ? 220 LYS   B CD  1 
ATOM   3350 C CE  . LYS   B 1 241 ? -12.713 28.802  10.055  0.50 44.50 ? 220 LYS   B CE  1 
ATOM   3351 N NZ  . LYS   B 1 241 ? -13.849 29.413  10.755  0.50 48.68 ? 220 LYS   B NZ  1 
ATOM   3352 N N   . TRP   B 1 242 ? -10.187 22.684  7.711   1.00 30.52 ? 221 TRP   B N   1 
ATOM   3353 C CA  . TRP   B 1 242 ? -9.897  21.252  7.652   1.00 32.04 ? 221 TRP   B CA  1 
ATOM   3354 C C   . TRP   B 1 242 ? -8.502  20.960  7.090   1.00 31.89 ? 221 TRP   B C   1 
ATOM   3355 O O   . TRP   B 1 242 ? -7.716  20.189  7.653   1.00 28.58 ? 221 TRP   B O   1 
ATOM   3356 C CB  . TRP   B 1 242 ? -11.002 20.505  6.886   1.00 30.37 ? 221 TRP   B CB  1 
ATOM   3357 C CG  . TRP   B 1 242 ? -12.235 20.410  7.737   1.00 35.88 ? 221 TRP   B CG  1 
ATOM   3358 C CD1 . TRP   B 1 242 ? -13.313 21.241  7.691   1.00 40.74 ? 221 TRP   B CD1 1 
ATOM   3359 C CD2 . TRP   B 1 242 ? -12.454 19.520  8.860   1.00 45.03 ? 221 TRP   B CD2 1 
ATOM   3360 N NE1 . TRP   B 1 242 ? -14.205 20.907  8.679   1.00 47.87 ? 221 TRP   B NE1 1 
ATOM   3361 C CE2 . TRP   B 1 242 ? -13.709 19.860  9.412   1.00 46.26 ? 221 TRP   B CE2 1 
ATOM   3362 C CE3 . TRP   B 1 242 ? -11.732 18.465  9.440   1.00 48.54 ? 221 TRP   B CE3 1 
ATOM   3363 C CZ2 . TRP   B 1 242 ? -14.245 19.186  10.513  1.00 48.52 ? 221 TRP   B CZ2 1 
ATOM   3364 C CZ3 . TRP   B 1 242 ? -12.259 17.796  10.533  1.00 47.60 ? 221 TRP   B CZ3 1 
ATOM   3365 C CH2 . TRP   B 1 242 ? -13.492 18.172  11.074  1.00 47.91 ? 221 TRP   B CH2 1 
ATOM   3366 N N   . ARG   B 1 243 ? -8.208  21.566  5.954   1.00 27.30 ? 222 ARG   B N   1 
ATOM   3367 C CA  . ARG   B 1 243 ? -6.880  21.373  5.334   1.00 29.50 ? 222 ARG   B CA  1 
ATOM   3368 C C   . ARG   B 1 243 ? -5.759  21.699  6.328   1.00 29.95 ? 222 ARG   B C   1 
ATOM   3369 O O   . ARG   B 1 243 ? -4.780  20.957  6.353   1.00 31.97 ? 222 ARG   B O   1 
ATOM   3370 C CB  . ARG   B 1 243 ? -6.832  22.283  4.106   1.00 29.59 ? 222 ARG   B CB  1 
ATOM   3371 C CG  . ARG   B 1 243 ? -7.787  21.881  2.995   1.00 29.51 ? 222 ARG   B CG  1 
ATOM   3372 C CD  . ARG   B 1 243 ? -7.778  22.934  1.907   1.00 31.71 ? 222 ARG   B CD  1 
ATOM   3373 N NE  . ARG   B 1 243 ? -8.553  22.501  0.744   1.00 30.31 ? 222 ARG   B NE  1 
ATOM   3374 C CZ  . ARG   B 1 243 ? -9.200  23.321  -0.063  1.00 31.11 ? 222 ARG   B CZ  1 
ATOM   3375 N NH1 . ARG   B 1 243 ? -9.347  24.590  0.266   1.00 28.63 ? 222 ARG   B NH1 1 
ATOM   3376 N NH2 . ARG   B 1 243 ? -9.693  22.864  -1.196  1.00 28.72 ? 222 ARG   B NH2 1 
ATOM   3377 N N   . ARG   B 1 244 ? -5.935  22.724  7.160   1.00 28.53 ? 223 ARG   B N   1 
ATOM   3378 C CA  . ARG   B 1 244 ? -4.834  23.148  8.005   1.00 30.78 ? 223 ARG   B CA  1 
ATOM   3379 C C   . ARG   B 1 244 ? -4.566  22.117  9.108   1.00 33.03 ? 223 ARG   B C   1 
ATOM   3380 O O   . ARG   B 1 244 ? -3.471  22.093  9.647   1.00 34.43 ? 223 ARG   B O   1 
ATOM   3381 C CB  . ARG   B 1 244 ? -5.078  24.532  8.613   1.00 37.93 ? 223 ARG   B CB  1 
ATOM   3382 C CG  . ARG   B 1 244 ? -4.841  25.685  7.644   0.60 39.97 ? 223 ARG   B CG  1 
ATOM   3383 C CD  . ARG   B 1 244 ? -4.791  27.042  8.357   0.60 39.63 ? 223 ARG   B CD  1 
ATOM   3384 N NE  . ARG   B 1 244 ? -5.957  27.210  9.233   0.60 43.94 ? 223 ARG   B NE  1 
ATOM   3385 C CZ  . ARG   B 1 244 ? -7.018  27.946  8.911   0.60 42.59 ? 223 ARG   B CZ  1 
ATOM   3386 N NH1 . ARG   B 1 244 ? -7.007  28.656  7.807   0.60 37.31 ? 223 ARG   B NH1 1 
ATOM   3387 N NH2 . ARG   B 1 244 ? -8.077  27.972  9.703   0.60 47.46 ? 223 ARG   B NH2 1 
ATOM   3388 N N   . LYS   B 1 245 ? -5.529  21.236  9.390   1.00 28.64 ? 224 LYS   B N   1 
ATOM   3389 C CA  . LYS   B 1 245 ? -5.348  20.262  10.460  1.00 30.36 ? 224 LYS   B CA  1 
ATOM   3390 C C   . LYS   B 1 245 ? -4.519  19.053  9.987   1.00 29.53 ? 224 LYS   B C   1 
ATOM   3391 O O   . LYS   B 1 245 ? -4.109  18.257  10.827  1.00 31.70 ? 224 LYS   B O   1 
ATOM   3392 C CB  . LYS   B 1 245 ? -6.727  19.741  10.899  1.00 28.98 ? 224 LYS   B CB  1 
ATOM   3393 C CG  . LYS   B 1 245 ? -7.755  20.765  11.419  1.00 34.18 ? 224 LYS   B CG  1 
ATOM   3394 C CD  . LYS   B 1 245 ? -9.112  20.096  11.622  1.00 36.47 ? 224 LYS   B CD  1 
ATOM   3395 C CE  . LYS   B 1 245 ? -10.307 20.996  11.861  1.00 41.30 ? 224 LYS   B CE  1 
ATOM   3396 N NZ  . LYS   B 1 245 ? -10.196 21.734  13.124  1.00 37.74 ? 224 LYS   B NZ  1 
ATOM   3397 N N   . VAL   B 1 246 ? -4.300  18.885  8.671   1.00 26.86 ? 225 VAL   B N   1 
ATOM   3398 C CA  . VAL   B 1 246 ? -3.692  17.680  8.119   1.00 25.89 ? 225 VAL   B CA  1 
ATOM   3399 C C   . VAL   B 1 246 ? -2.172  17.814  8.174   1.00 27.00 ? 225 VAL   B C   1 
ATOM   3400 O O   . VAL   B 1 246 ? -1.629  18.670  7.481   1.00 26.96 ? 225 VAL   B O   1 
ATOM   3401 C CB  . VAL   B 1 246 ? -4.149  17.379  6.676   1.00 25.99 ? 225 VAL   B CB  1 
ATOM   3402 C CG1 . VAL   B 1 246 ? -3.477  16.136  6.091   1.00 24.45 ? 225 VAL   B CG1 1 
ATOM   3403 C CG2 . VAL   B 1 246 ? -5.680  17.295  6.570   1.00 26.28 ? 225 VAL   B CG2 1 
ATOM   3404 N N   . PRO   B 1 247 ? -1.453  16.947  8.944   1.00 26.18 ? 226 PRO   B N   1 
ATOM   3405 C CA  . PRO   B 1 247 ? 0.010   17.014  9.042   1.00 25.79 ? 226 PRO   B CA  1 
ATOM   3406 C C   . PRO   B 1 247 ? 0.730   16.996  7.715   1.00 26.63 ? 226 PRO   B C   1 
ATOM   3407 O O   . PRO   B 1 247 ? 1.637   17.792  7.507   1.00 29.45 ? 226 PRO   B O   1 
ATOM   3408 C CB  . PRO   B 1 247 ? 0.330   15.750  9.890   1.00 26.64 ? 226 PRO   B CB  1 
ATOM   3409 C CG  . PRO   B 1 247 ? -0.828  15.680  10.861  1.00 26.87 ? 226 PRO   B CG  1 
ATOM   3410 C CD  . PRO   B 1 247 ? -2.001  15.964  9.895   1.00 26.32 ? 226 PRO   B CD  1 
ATOM   3411 N N   . LEU   B 1 248 ? 0.370   16.037  6.859   1.00 24.87 ? 227 LEU   B N   1 
ATOM   3412 C CA  . LEU   B 1 248 ? 1.084   15.777  5.621   1.00 27.26 ? 227 LEU   B CA  1 
ATOM   3413 C C   . LEU   B 1 248 ? 0.576   16.681  4.494   1.00 30.13 ? 227 LEU   B C   1 
ATOM   3414 O O   . LEU   B 1 248 ? -0.289  16.266  3.709   1.00 30.44 ? 227 LEU   B O   1 
ATOM   3415 C CB  . LEU   B 1 248 ? 0.904   14.299  5.264   1.00 24.94 ? 227 LEU   B CB  1 
ATOM   3416 C CG  . LEU   B 1 248 ? 1.795   13.798  4.121   1.00 23.86 ? 227 LEU   B CG  1 
ATOM   3417 C CD1 . LEU   B 1 248 ? 3.229   13.752  4.621   1.00 26.70 ? 227 LEU   B CD1 1 
ATOM   3418 C CD2 . LEU   B 1 248 ? 1.340   12.422  3.605   1.00 26.80 ? 227 LEU   B CD2 1 
ATOM   3419 N N   . GLY   B 1 249 ? 1.133   17.906  4.429   1.00 30.34 ? 228 GLY   B N   1 
ATOM   3420 C CA  . GLY   B 1 249 ? 0.947   18.800  3.295   1.00 34.40 ? 228 GLY   B CA  1 
ATOM   3421 C C   . GLY   B 1 249 ? -0.222  19.774  3.471   1.00 32.13 ? 228 GLY   B C   1 
ATOM   3422 O O   . GLY   B 1 249 ? -0.511  20.542  2.558   1.00 30.71 ? 228 GLY   B O   1 
ATOM   3423 N N   . ARG   B 1 250 ? -0.912  19.724  4.624   1.00 30.35 ? 229 ARG   B N   1 
ATOM   3424 C CA  . ARG   B 1 250 ? -1.991  20.662  4.923   1.00 30.09 ? 229 ARG   B CA  1 
ATOM   3425 C C   . ARG   B 1 250 ? -2.997  20.759  3.770   1.00 31.57 ? 229 ARG   B C   1 
ATOM   3426 O O   . ARG   B 1 250 ? -3.404  21.849  3.344   1.00 28.54 ? 229 ARG   B O   1 
ATOM   3427 C CB  . ARG   B 1 250 ? -1.361  22.022  5.286   1.00 30.86 ? 229 ARG   B CB  1 
ATOM   3428 C CG  . ARG   B 1 250 ? -0.267  22.034  6.349   1.00 37.73 ? 229 ARG   B CG  1 
ATOM   3429 C CD  . ARG   B 1 250 ? -0.888  21.952  7.737   0.70 37.25 ? 229 ARG   B CD  1 
ATOM   3430 N NE  . ARG   B 1 250 ? 0.137   21.653  8.746   0.70 41.06 ? 229 ARG   B NE  1 
ATOM   3431 C CZ  . ARG   B 1 250 ? -0.068  21.041  9.911   0.70 38.43 ? 229 ARG   B CZ  1 
ATOM   3432 N NH1 . ARG   B 1 250 ? -1.285  20.691  10.284  0.70 38.15 ? 229 ARG   B NH1 1 
ATOM   3433 N NH2 . ARG   B 1 250 ? 0.955   20.786  10.709  0.70 41.36 ? 229 ARG   B NH2 1 
ATOM   3434 N N   . ARG   B 1 251 ? -3.442  19.604  3.264   1.00 25.63 ? 230 ARG   B N   1 
ATOM   3435 C CA  . ARG   B 1 251 ? -4.387  19.555  2.164   1.00 27.69 ? 230 ARG   B CA  1 
ATOM   3436 C C   . ARG   B 1 251 ? -5.173  18.242  2.306   1.00 30.09 ? 230 ARG   B C   1 
ATOM   3437 O O   . ARG   B 1 251 ? -4.717  17.302  2.984   1.00 25.40 ? 230 ARG   B O   1 
ATOM   3438 C CB  . ARG   B 1 251 ? -3.655  19.554  0.809   1.00 28.88 ? 230 ARG   B CB  1 
ATOM   3439 C CG  . ARG   B 1 251 ? -2.873  18.290  0.484   1.00 30.24 ? 230 ARG   B CG  1 
ATOM   3440 C CD  . ARG   B 1 251 ? -1.851  18.364  -0.644  0.70 35.02 ? 230 ARG   B CD  1 
ATOM   3441 N NE  . ARG   B 1 251 ? -0.868  19.386  -0.266  0.70 35.91 ? 230 ARG   B NE  1 
ATOM   3442 C CZ  . ARG   B 1 251 ? 0.272   19.713  -0.867  0.70 39.57 ? 230 ARG   B CZ  1 
ATOM   3443 N NH1 . ARG   B 1 251 ? 0.596   19.209  -2.040  0.70 40.40 ? 230 ARG   B NH1 1 
ATOM   3444 N NH2 . ARG   B 1 251 ? 1.073   20.586  -0.287  0.70 48.10 ? 230 ARG   B NH2 1 
ATOM   3445 N N   . GLU   B 1 252 ? -6.365  18.211  1.690   1.00 26.63 ? 231 GLU   B N   1 
ATOM   3446 C CA  . GLU   B 1 252 ? -7.217  17.032  1.676   1.00 25.89 ? 231 GLU   B CA  1 
ATOM   3447 C C   . GLU   B 1 252 ? -6.671  16.027  0.661   1.00 24.74 ? 231 GLU   B C   1 
ATOM   3448 O O   . GLU   B 1 252 ? -5.920  16.375  -0.249  1.00 27.71 ? 231 GLU   B O   1 
ATOM   3449 C CB  . GLU   B 1 252 ? -8.671  17.430  1.402   1.00 25.75 ? 231 GLU   B CB  1 
ATOM   3450 C CG  . GLU   B 1 252 ? -8.909  17.921  -0.027  1.00 30.50 ? 231 GLU   B CG  1 
ATOM   3451 C CD  . GLU   B 1 252 ? -8.618  19.394  -0.332  1.00 33.18 ? 231 GLU   B CD  1 
ATOM   3452 O OE1 . GLU   B 1 252 ? -9.450  19.951  -1.097  1.00 32.79 ? 231 GLU   B OE1 1 
ATOM   3453 O OE2 . GLU   B 1 252 ? -7.636  19.998  0.186   1.00 30.60 ? 231 GLU   B OE2 1 
ATOM   3454 N N   . ALA   B 1 253 ? -7.010  14.734  0.819   1.00 24.14 ? 232 ALA   B N   1 
ATOM   3455 C CA  . ALA   B 1 253 ? -6.684  13.781  -0.226  1.00 24.12 ? 232 ALA   B CA  1 
ATOM   3456 C C   . ALA   B 1 253 ? -7.512  14.054  -1.487  1.00 23.93 ? 232 ALA   B C   1 
ATOM   3457 O O   . ALA   B 1 253 ? -8.697  14.393  -1.435  1.00 25.43 ? 232 ALA   B O   1 
ATOM   3458 C CB  . ALA   B 1 253 ? -6.923  12.346  0.236   1.00 27.91 ? 232 ALA   B CB  1 
ATOM   3459 N N   . SER   B 1 254 ? -6.895  13.827  -2.653  1.00 24.58 ? 233 SER   B N   1 
ATOM   3460 C CA  . SER   B 1 254 ? -7.684  13.764  -3.869  1.00 23.54 ? 233 SER   B CA  1 
ATOM   3461 C C   . SER   B 1 254 ? -8.462  12.454  -3.888  1.00 26.34 ? 233 SER   B C   1 
ATOM   3462 O O   . SER   B 1 254 ? -8.110  11.531  -3.153  1.00 27.03 ? 233 SER   B O   1 
ATOM   3463 C CB  . SER   B 1 254 ? -6.815  13.833  -5.090  1.00 27.76 ? 233 SER   B CB  1 
ATOM   3464 O OG  . SER   B 1 254 ? -6.050  12.636  -5.215  1.00 27.01 ? 233 SER   B OG  1 
ATOM   3465 N N   . ALA   B 1 255 ? -9.465  12.396  -4.767  1.00 25.01 ? 234 ALA   B N   1 
ATOM   3466 C CA  . ALA   B 1 255 ? -10.257 11.187  -4.960  1.00 25.06 ? 234 ALA   B CA  1 
ATOM   3467 C C   . ALA   B 1 255 ? -9.331  10.086  -5.448  1.00 24.94 ? 234 ALA   B C   1 
ATOM   3468 O O   . ALA   B 1 255 ? -9.530  8.897   -5.135  1.00 25.45 ? 234 ALA   B O   1 
ATOM   3469 C CB  . ALA   B 1 255 ? -11.372 11.465  -5.954  1.00 23.78 ? 234 ALA   B CB  1 
ATOM   3470 N N   . GLU   B 1 256 ? -8.372  10.468  -6.309  1.00 24.05 ? 235 GLU   B N   1 
ATOM   3471 C CA  . GLU   B 1 256 ? -7.483  9.489   -6.917  1.00 28.07 ? 235 GLU   B CA  1 
ATOM   3472 C C   . GLU   B 1 256 ? -6.597  8.812   -5.858  1.00 26.26 ? 235 GLU   B C   1 
ATOM   3473 O O   . GLU   B 1 256 ? -6.227  7.650   -6.004  1.00 24.99 ? 235 GLU   B O   1 
ATOM   3474 C CB  . GLU   B 1 256 ? -6.604  10.119  -8.010  1.00 28.36 ? 235 GLU   B CB  1 
ATOM   3475 C CG  . GLU   B 1 256 ? -7.403  10.495  -9.267  1.00 29.64 ? 235 GLU   B CG  1 
ATOM   3476 C CD  . GLU   B 1 256 ? -8.344  11.701  -9.165  1.00 36.13 ? 235 GLU   B CD  1 
ATOM   3477 O OE1 . GLU   B 1 256 ? -8.388  12.487  -8.159  1.00 32.86 ? 235 GLU   B OE1 1 
ATOM   3478 O OE2 . GLU   B 1 256 ? -9.067  11.857  -10.184 1.00 34.97 ? 235 GLU   B OE2 1 
ATOM   3479 N N   . GLN   B 1 257 ? -6.178  9.573   -4.844  1.00 23.26 ? 236 GLN   B N   1 
ATOM   3480 C CA  . GLN   B 1 257 ? -5.319  9.035   -3.789  1.00 26.26 ? 236 GLN   B CA  1 
ATOM   3481 C C   . GLN   B 1 257 ? -6.081  7.981   -2.972  1.00 25.32 ? 236 GLN   B C   1 
ATOM   3482 O O   . GLN   B 1 257 ? -5.508  6.953   -2.598  1.00 22.89 ? 236 GLN   B O   1 
ATOM   3483 C CB  . GLN   B 1 257 ? -4.819  10.199  -2.944  1.00 24.26 ? 236 GLN   B CB  1 
ATOM   3484 C CG  . GLN   B 1 257 ? -3.660  10.926  -3.628  1.00 26.46 ? 236 GLN   B CG  1 
ATOM   3485 C CD  . GLN   B 1 257 ? -3.221  12.148  -2.860  1.00 26.19 ? 236 GLN   B CD  1 
ATOM   3486 O OE1 . GLN   B 1 257 ? -4.014  12.795  -2.181  1.00 27.01 ? 236 GLN   B OE1 1 
ATOM   3487 N NE2 . GLN   B 1 257 ? -1.953  12.501  -3.002  1.00 31.10 ? 236 GLN   B NE2 1 
ATOM   3488 N N   . ILE   B 1 258 ? -7.380  8.213   -2.809  1.00 22.22 ? 237 ILE   B N   1 
ATOM   3489 C CA  . ILE   B 1 258 ? -8.225  7.228   -2.138  1.00 22.38 ? 237 ILE   B CA  1 
ATOM   3490 C C   . ILE   B 1 258 ? -8.342  6.025   -3.064  1.00 24.33 ? 237 ILE   B C   1 
ATOM   3491 O O   . ILE   B 1 258 ? -8.174  4.875   -2.640  1.00 22.59 ? 237 ILE   B O   1 
ATOM   3492 C CB  . ILE   B 1 258 ? -9.596  7.802   -1.741  1.00 22.01 ? 237 ILE   B CB  1 
ATOM   3493 C CG1 . ILE   B 1 258 ? -9.478  9.069   -0.869  1.00 20.78 ? 237 ILE   B CG1 1 
ATOM   3494 C CG2 . ILE   B 1 258 ? -10.481 6.731   -1.063  1.00 26.06 ? 237 ILE   B CG2 1 
ATOM   3495 C CD1 . ILE   B 1 258 ? -8.685  8.887   0.422   1.00 21.00 ? 237 ILE   B CD1 1 
ATOM   3496 N N   . ALA   B 1 259 ? -8.554  6.291   -4.366  1.00 21.76 ? 238 ALA   B N   1 
ATOM   3497 C CA  . ALA   B 1 259 ? -8.719  5.165   -5.275  1.00 24.65 ? 238 ALA   B CA  1 
ATOM   3498 C C   . ALA   B 1 259 ? -7.455  4.298   -5.322  1.00 22.69 ? 238 ALA   B C   1 
ATOM   3499 O O   . ALA   B 1 259 ? -7.536  3.085   -5.516  1.00 22.61 ? 238 ALA   B O   1 
ATOM   3500 C CB  . ALA   B 1 259 ? -9.140  5.667   -6.676  1.00 25.01 ? 238 ALA   B CB  1 
ATOM   3501 N N   . ASP   B 1 260 ? -6.268  4.920   -5.198  1.00 24.44 ? 239 ASP   B N   1 
ATOM   3502 C CA  . ASP   B 1 260 ? -5.005  4.194   -5.246  1.00 24.98 ? 239 ASP   B CA  1 
ATOM   3503 C C   . ASP   B 1 260 ? -4.969  3.069   -4.200  1.00 22.82 ? 239 ASP   B C   1 
ATOM   3504 O O   . ASP   B 1 260 ? -4.472  1.979   -4.478  1.00 23.34 ? 239 ASP   B O   1 
ATOM   3505 C CB  . ASP   B 1 260 ? -3.831  5.136   -5.034  1.00 25.27 ? 239 ASP   B CB  1 
ATOM   3506 C CG  . ASP   B 1 260 ? -3.361  5.883   -6.279  1.00 29.90 ? 239 ASP   B CG  1 
ATOM   3507 O OD1 . ASP   B 1 260 ? -3.607  5.380   -7.395  1.00 27.69 ? 239 ASP   B OD1 1 
ATOM   3508 O OD2 . ASP   B 1 260 ? -2.805  6.982   -6.117  1.00 28.57 ? 239 ASP   B OD2 1 
ATOM   3509 N N   . ALA   B 1 261 ? -5.520  3.340   -3.004  1.00 21.87 ? 240 ALA   B N   1 
ATOM   3510 C CA  . ALA   B 1 261 ? -5.505  2.338   -1.939  1.00 21.98 ? 240 ALA   B CA  1 
ATOM   3511 C C   . ALA   B 1 261 ? -6.485  1.215   -2.267  1.00 21.32 ? 240 ALA   B C   1 
ATOM   3512 O O   . ALA   B 1 261 ? -6.229  0.065   -1.899  1.00 22.47 ? 240 ALA   B O   1 
ATOM   3513 C CB  . ALA   B 1 261 ? -5.837  2.989   -0.595  1.00 24.59 ? 240 ALA   B CB  1 
ATOM   3514 N N   . VAL   B 1 262 ? -7.651  1.586   -2.832  1.00 21.14 ? 241 VAL   B N   1 
ATOM   3515 C CA  . VAL   B 1 262 ? -8.608  0.579   -3.293  1.00 23.73 ? 241 VAL   B CA  1 
ATOM   3516 C C   . VAL   B 1 262 ? -7.931  -0.338  -4.305  1.00 24.10 ? 241 VAL   B C   1 
ATOM   3517 O O   . VAL   B 1 262 ? -8.050  -1.556  -4.233  1.00 24.64 ? 241 VAL   B O   1 
ATOM   3518 C CB  . VAL   B 1 262 ? -9.928  1.177   -3.839  1.00 25.44 ? 241 VAL   B CB  1 
ATOM   3519 C CG1 . VAL   B 1 262 ? -10.910 0.122   -4.386  1.00 25.24 ? 241 VAL   B CG1 1 
ATOM   3520 C CG2 . VAL   B 1 262 ? -10.615 2.099   -2.822  1.00 24.02 ? 241 VAL   B CG2 1 
ATOM   3521 N N   . ILE   B 1 263 ? -7.297  0.247   -5.338  1.00 28.14 ? 242 ILE   B N   1 
ATOM   3522 C CA  . ILE   B 1 263 ? -6.619  -0.561  -6.350  1.00 25.50 ? 242 ILE   B CA  1 
ATOM   3523 C C   . ILE   B 1 263 ? -5.598  -1.534  -5.739  1.00 23.01 ? 242 ILE   B C   1 
ATOM   3524 O O   . ILE   B 1 263 ? -5.508  -2.703  -6.148  1.00 24.34 ? 242 ILE   B O   1 
ATOM   3525 C CB  . ILE   B 1 263 ? -5.927  0.392   -7.345  1.00 25.58 ? 242 ILE   B CB  1 
ATOM   3526 C CG1 . ILE   B 1 263 ? -6.937  1.144   -8.184  1.00 31.22 ? 242 ILE   B CG1 1 
ATOM   3527 C CG2 . ILE   B 1 263 ? -4.924  -0.387  -8.191  1.00 29.26 ? 242 ILE   B CG2 1 
ATOM   3528 C CD1 . ILE   B 1 263 ? -7.970  0.287   -8.904  1.00 34.04 ? 242 ILE   B CD1 1 
ATOM   3529 N N   . PHE   B 1 264 ? -4.806  -1.051  -4.766  1.00 23.76 ? 243 PHE   B N   1 
ATOM   3530 C CA  . PHE   B 1 264 ? -3.853  -1.921  -4.085  1.00 21.74 ? 243 PHE   B CA  1 
ATOM   3531 C C   . PHE   B 1 264 ? -4.588  -3.118  -3.487  1.00 23.24 ? 243 PHE   B C   1 
ATOM   3532 O O   . PHE   B 1 264 ? -4.137  -4.259  -3.627  1.00 23.25 ? 243 PHE   B O   1 
ATOM   3533 C CB  . PHE   B 1 264 ? -3.045  -1.144  -3.025  1.00 26.06 ? 243 PHE   B CB  1 
ATOM   3534 C CG  . PHE   B 1 264 ? -2.265  -2.066  -2.097  1.00 28.04 ? 243 PHE   B CG  1 
ATOM   3535 C CD1 . PHE   B 1 264 ? -1.206  -2.832  -2.582  1.00 25.51 ? 243 PHE   B CD1 1 
ATOM   3536 C CD2 . PHE   B 1 264 ? -2.612  -2.177  -0.741  1.00 25.14 ? 243 PHE   B CD2 1 
ATOM   3537 C CE1 . PHE   B 1 264 ? -0.502  -3.681  -1.733  1.00 25.50 ? 243 PHE   B CE1 1 
ATOM   3538 C CE2 . PHE   B 1 264 ? -1.896  -3.025  0.091   1.00 23.21 ? 243 PHE   B CE2 1 
ATOM   3539 C CZ  . PHE   B 1 264 ? -0.863  -3.779  -0.404  1.00 25.98 ? 243 PHE   B CZ  1 
ATOM   3540 N N   . LEU   B 1 265 ? -5.686  -2.851  -2.747  1.00 22.79 ? 244 LEU   B N   1 
ATOM   3541 C CA  . LEU   B 1 265 ? -6.356  -3.919  -2.009  1.00 19.79 ? 244 LEU   B CA  1 
ATOM   3542 C C   . LEU   B 1 265 ? -6.966  -4.980  -2.910  1.00 21.18 ? 244 LEU   B C   1 
ATOM   3543 O O   . LEU   B 1 265 ? -7.096  -6.146  -2.504  1.00 23.50 ? 244 LEU   B O   1 
ATOM   3544 C CB  . LEU   B 1 265 ? -7.406  -3.391  -1.028  1.00 22.36 ? 244 LEU   B CB  1 
ATOM   3545 C CG  . LEU   B 1 265 ? -6.775  -2.672  0.183   1.00 19.87 ? 244 LEU   B CG  1 
ATOM   3546 C CD1 . LEU   B 1 265 ? -7.851  -1.850  0.908   1.00 22.15 ? 244 LEU   B CD1 1 
ATOM   3547 C CD2 . LEU   B 1 265 ? -6.213  -3.754  1.105   1.00 22.03 ? 244 LEU   B CD2 1 
ATOM   3548 N N   . VAL   B 1 266 ? -7.403  -4.581  -4.103  1.00 22.70 ? 245 VAL   B N   1 
ATOM   3549 C CA  . VAL   B 1 266 ? -8.024  -5.546  -5.014  1.00 22.97 ? 245 VAL   B CA  1 
ATOM   3550 C C   . VAL   B 1 266 ? -6.939  -6.263  -5.816  1.00 24.32 ? 245 VAL   B C   1 
ATOM   3551 O O   . VAL   B 1 266 ? -7.235  -7.236  -6.510  1.00 26.92 ? 245 VAL   B O   1 
ATOM   3552 C CB  . VAL   B 1 266 ? -9.092  -4.954  -5.951  1.00 26.87 ? 245 VAL   B CB  1 
ATOM   3553 C CG1 . VAL   B 1 266 ? -10.188 -4.235  -5.156  1.00 27.10 ? 245 VAL   B CG1 1 
ATOM   3554 C CG2 . VAL   B 1 266 ? -8.481  -4.030  -7.007  1.00 28.15 ? 245 VAL   B CG2 1 
ATOM   3555 N N   . SER   B 1 267 ? -5.707  -5.757  -5.736  1.00 26.04 ? 246 SER   B N   1 
ATOM   3556 C CA  . SER   B 1 267 ? -4.630  -6.237  -6.602  1.00 27.09 ? 246 SER   B CA  1 
ATOM   3557 C C   . SER   B 1 267 ? -4.020  -7.537  -6.098  1.00 29.50 ? 246 SER   B C   1 
ATOM   3558 O O   . SER   B 1 267 ? -4.210  -7.928  -4.943  1.00 28.12 ? 246 SER   B O   1 
ATOM   3559 C CB  . SER   B 1 267 ? -3.572  -5.160  -6.785  1.00 24.81 ? 246 SER   B CB  1 
ATOM   3560 O OG  . SER   B 1 267 ? -2.714  -5.126  -5.642  1.00 27.83 ? 246 SER   B OG  1 
ATOM   3561 N N   . GLY   B 1 268 ? -3.219  -8.161  -6.977  1.00 30.78 ? 247 GLY   B N   1 
ATOM   3562 C CA  . GLY   B 1 268 ? -2.401  -9.316  -6.648  1.00 28.48 ? 247 GLY   B CA  1 
ATOM   3563 C C   . GLY   B 1 268 ? -1.331  -9.059  -5.580  1.00 29.44 ? 247 GLY   B C   1 
ATOM   3564 O O   . GLY   B 1 268 ? -0.771  -10.013 -5.071  1.00 36.06 ? 247 GLY   B O   1 
ATOM   3565 N N   . SER   B 1 269 ? -1.015  -7.792  -5.277  1.00 23.98 ? 248 SER   B N   1 
ATOM   3566 C CA  . SER   B 1 269 ? -0.032  -7.402  -4.276  1.00 25.94 ? 248 SER   B CA  1 
ATOM   3567 C C   . SER   B 1 269 ? -0.628  -7.431  -2.873  1.00 27.01 ? 248 SER   B C   1 
ATOM   3568 O O   . SER   B 1 269 ? 0.097   -7.136  -1.939  1.00 27.04 ? 248 SER   B O   1 
ATOM   3569 C CB  . SER   B 1 269 ? 0.489   -6.025  -4.592  1.00 30.26 ? 248 SER   B CB  1 
ATOM   3570 O OG  . SER   B 1 269 ? 1.253   -6.174  -5.778  1.00 32.73 ? 248 SER   B OG  1 
ATOM   3571 N N   . ALA   B 1 270 ? -1.928  -7.738  -2.765  1.00 24.28 ? 249 ALA   B N   1 
ATOM   3572 C CA  . ALA   B 1 270 ? -2.642  -7.724  -1.482  1.00 24.18 ? 249 ALA   B CA  1 
ATOM   3573 C C   . ALA   B 1 270 ? -3.336  -9.056  -1.238  1.00 25.28 ? 249 ALA   B C   1 
ATOM   3574 O O   . ALA   B 1 270 ? -4.254  -9.151  -0.415  1.00 23.95 ? 249 ALA   B O   1 
ATOM   3575 C CB  . ALA   B 1 270 ? -3.640  -6.581  -1.445  1.00 23.15 ? 249 ALA   B CB  1 
ATOM   3576 N N   . GLN   B 1 271 ? -2.809  -10.123 -1.857  1.00 25.51 ? 250 GLN   B N   1 
ATOM   3577 C CA  . GLN   B 1 271 ? -3.507  -11.394 -1.831  1.00 25.09 ? 250 GLN   B CA  1 
ATOM   3578 C C   . GLN   B 1 271 ? -3.549  -12.076 -0.456  1.00 24.98 ? 250 GLN   B C   1 
ATOM   3579 O O   . GLN   B 1 271 ? -4.301  -13.036 -0.290  1.00 24.45 ? 250 GLN   B O   1 
ATOM   3580 C CB  . GLN   B 1 271 ? -2.838  -12.337 -2.835  1.00 31.40 ? 250 GLN   B CB  1 
ATOM   3581 C CG  . GLN   B 1 271 ? -2.989  -11.782 -4.242  0.50 36.21 ? 250 GLN   B CG  1 
ATOM   3582 C CD  . GLN   B 1 271 ? -3.080  -12.843 -5.309  0.50 40.42 ? 250 GLN   B CD  1 
ATOM   3583 O OE1 . GLN   B 1 271 ? -4.177  -13.193 -5.755  0.50 43.98 ? 250 GLN   B OE1 1 
ATOM   3584 N NE2 . GLN   B 1 271 ? -1.930  -13.372 -5.704  0.50 43.07 ? 250 GLN   B NE2 1 
ATOM   3585 N N   . TYR   B 1 272 ? -2.761  -11.616 0.521   1.00 22.51 ? 251 TYR   B N   1 
ATOM   3586 C CA  . TYR   B 1 272 ? -2.837  -12.199 1.859   1.00 20.27 ? 251 TYR   B CA  1 
ATOM   3587 C C   . TYR   B 1 272 ? -3.540  -11.257 2.831   1.00 20.73 ? 251 TYR   B C   1 
ATOM   3588 O O   . TYR   B 1 272 ? -3.582  -11.526 4.023   1.00 21.72 ? 251 TYR   B O   1 
ATOM   3589 C CB  . TYR   B 1 272 ? -1.454  -12.528 2.397   1.00 21.10 ? 251 TYR   B CB  1 
ATOM   3590 C CG  . TYR   B 1 272 ? -1.333  -13.474 3.585   1.00 21.85 ? 251 TYR   B CG  1 
ATOM   3591 C CD1 . TYR   B 1 272 ? -1.556  -14.831 3.415   1.00 21.50 ? 251 TYR   B CD1 1 
ATOM   3592 C CD2 . TYR   B 1 272 ? -0.996  -13.026 4.866   1.00 22.29 ? 251 TYR   B CD2 1 
ATOM   3593 C CE1 . TYR   B 1 272 ? -1.442  -15.720 4.464   1.00 22.28 ? 251 TYR   B CE1 1 
ATOM   3594 C CE2 . TYR   B 1 272 ? -0.863  -13.914 5.922   1.00 18.59 ? 251 TYR   B CE2 1 
ATOM   3595 C CZ  . TYR   B 1 272 ? -1.105  -15.260 5.718   1.00 21.69 ? 251 TYR   B CZ  1 
ATOM   3596 O OH  . TYR   B 1 272 ? -0.951  -16.135 6.743   1.00 21.95 ? 251 TYR   B OH  1 
ATOM   3597 N N   . ILE   B 1 273 ? -3.976  -10.102 2.331   1.00 21.19 ? 252 ILE   B N   1 
ATOM   3598 C CA  . ILE   B 1 273 ? -4.542  -9.091  3.219   1.00 21.09 ? 252 ILE   B CA  1 
ATOM   3599 C C   . ILE   B 1 273 ? -6.067  -9.275  3.268   1.00 20.51 ? 252 ILE   B C   1 
ATOM   3600 O O   . ILE   B 1 273 ? -6.725  -9.175  2.242   1.00 20.13 ? 252 ILE   B O   1 
ATOM   3601 C CB  . ILE   B 1 273 ? -4.192  -7.684  2.691   1.00 22.24 ? 252 ILE   B CB  1 
ATOM   3602 C CG1 . ILE   B 1 273 ? -2.658  -7.508  2.537   1.00 21.70 ? 252 ILE   B CG1 1 
ATOM   3603 C CG2 . ILE   B 1 273 ? -4.798  -6.645  3.663   1.00 21.84 ? 252 ILE   B CG2 1 
ATOM   3604 C CD1 . ILE   B 1 273 ? -2.212  -6.095  2.136   1.00 21.38 ? 252 ILE   B CD1 1 
ATOM   3605 N N   . THR   B 1 274 ? -6.617  -9.521  4.466   1.00 19.08 ? 253 THR   B N   1 
ATOM   3606 C CA  . THR   B 1 274 ? -8.057  -9.547  4.620   1.00 20.51 ? 253 THR   B CA  1 
ATOM   3607 C C   . THR   B 1 274 ? -8.358  -9.038  6.030   1.00 22.51 ? 253 THR   B C   1 
ATOM   3608 O O   . THR   B 1 274 ? -7.573  -9.309  6.944   1.00 20.39 ? 253 THR   B O   1 
ATOM   3609 C CB  . THR   B 1 274 ? -8.690  -10.910 4.310   1.00 20.61 ? 253 THR   B CB  1 
ATOM   3610 O OG1 . THR   B 1 274 ? -10.099 -10.676 4.183   1.00 21.16 ? 253 THR   B OG1 1 
ATOM   3611 C CG2 . THR   B 1 274 ? -8.404  -11.989 5.354   1.00 20.62 ? 253 THR   B CG2 1 
ATOM   3612 N N   . GLY   B 1 275 ? -9.462  -8.276  6.149   1.00 20.68 ? 254 GLY   B N   1 
ATOM   3613 C CA  . GLY   B 1 275 ? -9.832  -7.752  7.452   1.00 21.38 ? 254 GLY   B CA  1 
ATOM   3614 C C   . GLY   B 1 275 ? -9.006  -6.525  7.841   1.00 20.61 ? 254 GLY   B C   1 
ATOM   3615 O O   . GLY   B 1 275 ? -9.049  -6.128  8.995   1.00 23.10 ? 254 GLY   B O   1 
ATOM   3616 N N   . SER   B 1 276 ? -8.318  -5.902  6.883   1.00 21.14 ? 255 SER   B N   1 
ATOM   3617 C CA  . SER   B 1 276 ? -7.447  -4.775  7.185   1.00 20.89 ? 255 SER   B CA  1 
ATOM   3618 C C   . SER   B 1 276 ? -8.158  -3.520  6.730   1.00 22.01 ? 255 SER   B C   1 
ATOM   3619 O O   . SER   B 1 276 ? -8.797  -3.572  5.688   1.00 21.20 ? 255 SER   B O   1 
ATOM   3620 C CB  . SER   B 1 276 ? -6.120  -4.900  6.454   1.00 22.91 ? 255 SER   B CB  1 
ATOM   3621 O OG  . SER   B 1 276 ? -5.387  -6.014  6.964   1.00 29.16 ? 255 SER   B OG  1 
ATOM   3622 N N   . ILE   B 1 277 ? -7.979  -2.406  7.463   1.00 20.79 ? 256 ILE   B N   1 
ATOM   3623 C CA  . ILE   B 1 277 ? -8.538  -1.123  7.035   1.00 20.44 ? 256 ILE   B CA  1 
ATOM   3624 C C   . ILE   B 1 277 ? -7.369  -0.153  6.914   1.00 20.09 ? 256 ILE   B C   1 
ATOM   3625 O O   . ILE   B 1 277 ? -6.648  0.057   7.882   1.00 24.13 ? 256 ILE   B O   1 
ATOM   3626 C CB  . ILE   B 1 277 ? -9.607  -0.614  8.025   1.00 21.54 ? 256 ILE   B CB  1 
ATOM   3627 C CG1 . ILE   B 1 277 ? -10.827 -1.590  8.034   1.00 25.60 ? 256 ILE   B CG1 1 
ATOM   3628 C CG2 . ILE   B 1 277 ? -10.072 0.812   7.663   1.00 20.49 ? 256 ILE   B CG2 1 
ATOM   3629 C CD1 . ILE   B 1 277 ? -11.788 -1.355  9.180   1.00 31.21 ? 256 ILE   B CD1 1 
ATOM   3630 N N   . ILE   B 1 278 ? -7.100  0.327   5.693   1.00 21.43 ? 257 ILE   B N   1 
ATOM   3631 C CA  . ILE   B 1 278 ? -5.953  1.198   5.479   1.00 20.86 ? 257 ILE   B CA  1 
ATOM   3632 C C   . ILE   B 1 278 ? -6.426  2.641   5.626   1.00 22.06 ? 257 ILE   B C   1 
ATOM   3633 O O   . ILE   B 1 278 ? -7.265  3.063   4.842   1.00 19.87 ? 257 ILE   B O   1 
ATOM   3634 C CB  . ILE   B 1 278 ? -5.409  0.953   4.068   1.00 22.42 ? 257 ILE   B CB  1 
ATOM   3635 C CG1 . ILE   B 1 278 ? -4.928  -0.484  3.939   1.00 24.36 ? 257 ILE   B CG1 1 
ATOM   3636 C CG2 . ILE   B 1 278 ? -4.292  1.970   3.727   1.00 24.23 ? 257 ILE   B CG2 1 
ATOM   3637 C CD1 . ILE   B 1 278 ? -4.471  -0.853  2.531   1.00 25.43 ? 257 ILE   B CD1 1 
ATOM   3638 N N   . LYS   B 1 279 ? -5.838  3.364   6.576   1.00 20.47 ? 258 LYS   B N   1 
ATOM   3639 C CA  . LYS   B 1 279 ? -6.140  4.802   6.696   1.00 22.03 ? 258 LYS   B CA  1 
ATOM   3640 C C   . LYS   B 1 279 ? -5.416  5.529   5.569   1.00 21.34 ? 258 LYS   B C   1 
ATOM   3641 O O   . LYS   B 1 279 ? -4.258  5.221   5.324   1.00 21.66 ? 258 LYS   B O   1 
ATOM   3642 C CB  . LYS   B 1 279 ? -5.641  5.488   7.971   1.00 21.23 ? 258 LYS   B CB  1 
ATOM   3643 C CG  . LYS   B 1 279 ? -6.355  5.158   9.259   1.00 24.60 ? 258 LYS   B CG  1 
ATOM   3644 C CD  . LYS   B 1 279 ? -5.745  5.918   10.427  1.00 21.84 ? 258 LYS   B CD  1 
ATOM   3645 C CE  . LYS   B 1 279 ? -4.369  5.440   10.739  1.00 25.63 ? 258 LYS   B CE  1 
ATOM   3646 N NZ  . LYS   B 1 279 ? -3.719  6.249   11.772  1.00 27.78 ? 258 LYS   B NZ  1 
ATOM   3647 N N   . VAL   B 1 280 ? -6.120  6.446   4.922   1.00 24.10 ? 259 VAL   B N   1 
ATOM   3648 C CA  . VAL   B 1 280 ? -5.482  7.264   3.903   1.00 23.20 ? 259 VAL   B CA  1 
ATOM   3649 C C   . VAL   B 1 280 ? -5.821  8.687   4.313   1.00 22.42 ? 259 VAL   B C   1 
ATOM   3650 O O   . VAL   B 1 280 ? -6.746  9.287   3.765   1.00 23.54 ? 259 VAL   B O   1 
ATOM   3651 C CB  . VAL   B 1 280 ? -5.948  6.897   2.488   1.00 25.22 ? 259 VAL   B CB  1 
ATOM   3652 C CG1 . VAL   B 1 280 ? -5.159  7.649   1.414   1.00 23.27 ? 259 VAL   B CG1 1 
ATOM   3653 C CG2 . VAL   B 1 280 ? -5.816  5.395   2.231   1.00 20.74 ? 259 VAL   B CG2 1 
ATOM   3654 N N   . ASP   B 1 281 ? -5.103  9.179   5.330   1.00 22.77 ? 260 ASP   B N   1 
ATOM   3655 C CA  . ASP   B 1 281 ? -5.592  10.374  5.986   1.00 21.11 ? 260 ASP   B CA  1 
ATOM   3656 C C   . ASP   B 1 281 ? -4.516  11.435  6.232   1.00 23.43 ? 260 ASP   B C   1 
ATOM   3657 O O   . ASP   B 1 281 ? -4.834  12.426  6.897   1.00 22.78 ? 260 ASP   B O   1 
ATOM   3658 C CB  . ASP   B 1 281 ? -6.307  10.051  7.299   1.00 22.09 ? 260 ASP   B CB  1 
ATOM   3659 C CG  . ASP   B 1 281 ? -5.388  9.683   8.463   1.00 23.83 ? 260 ASP   B CG  1 
ATOM   3660 O OD1 . ASP   B 1 281 ? -4.173  9.442   8.225   1.00 23.72 ? 260 ASP   B OD1 1 
ATOM   3661 O OD2 . ASP   B 1 281 ? -5.889  9.672   9.607   1.00 20.53 ? 260 ASP   B OD2 1 
ATOM   3662 N N   . GLY   B 1 282 ? -3.314  11.270  5.669   1.00 21.44 ? 261 GLY   B N   1 
ATOM   3663 C CA  . GLY   B 1 282 ? -2.284  12.299  5.825   1.00 22.22 ? 261 GLY   B CA  1 
ATOM   3664 C C   . GLY   B 1 282 ? -1.918  12.570  7.298   1.00 24.66 ? 261 GLY   B C   1 
ATOM   3665 O O   . GLY   B 1 282 ? -1.358  13.624  7.617   1.00 22.44 ? 261 GLY   B O   1 
ATOM   3666 N N   . GLY   B 1 283 ? -2.208  11.619  8.212   1.00 21.51 ? 262 GLY   B N   1 
ATOM   3667 C CA  . GLY   B 1 283 ? -1.934  11.752  9.623   1.00 21.13 ? 262 GLY   B CA  1 
ATOM   3668 C C   . GLY   B 1 283 ? -3.004  12.509  10.418  1.00 24.21 ? 262 GLY   B C   1 
ATOM   3669 O O   . GLY   B 1 283 ? -2.822  12.750  11.603  1.00 23.04 ? 262 GLY   B O   1 
ATOM   3670 N N   . LEU   B 1 284 ? -4.144  12.844  9.801   1.00 24.78 ? 263 LEU   B N   1 
ATOM   3671 C CA  . LEU   B 1 284 ? -5.177  13.628  10.476  1.00 24.64 ? 263 LEU   B CA  1 
ATOM   3672 C C   . LEU   B 1 284 ? -5.618  13.008  11.809  1.00 23.11 ? 263 LEU   B C   1 
ATOM   3673 O O   . LEU   B 1 284 ? -5.791  13.717  12.807  1.00 22.83 ? 263 LEU   B O   1 
ATOM   3674 C CB  . LEU   B 1 284 ? -6.377  13.832  9.551   1.00 22.80 ? 263 LEU   B CB  1 
ATOM   3675 C CG  . LEU   B 1 284 ? -7.531  14.635  10.150  1.00 24.33 ? 263 LEU   B CG  1 
ATOM   3676 C CD1 . LEU   B 1 284 ? -7.051  16.063  10.455  1.00 24.40 ? 263 LEU   B CD1 1 
ATOM   3677 C CD2 . LEU   B 1 284 ? -8.611  14.630  9.088   1.00 25.62 ? 263 LEU   B CD2 1 
ATOM   3678 N N   . SER   B 1 285 ? -5.821  11.680  11.808  1.00 21.91 ? 264 SER   B N   1 
ATOM   3679 C CA  . SER   B 1 285 ? -6.333  10.962  12.971  1.00 23.82 ? 264 SER   B CA  1 
ATOM   3680 C C   . SER   B 1 285 ? -5.324  10.929  14.129  1.00 23.94 ? 264 SER   B C   1 
ATOM   3681 O O   . SER   B 1 285 ? -5.706  10.584  15.244  1.00 23.91 ? 264 SER   B O   1 
ATOM   3682 C CB  . SER   B 1 285 ? -6.756  9.575   12.563  1.00 22.16 ? 264 SER   B CB  1 
ATOM   3683 O OG  . SER   B 1 285 ? -5.656  8.774   12.153  1.00 25.31 ? 264 SER   B OG  1 
ATOM   3684 N N   . LEU   B 1 286 ? -4.079  11.387  13.894  1.00 24.00 ? 265 LEU   B N   1 
ATOM   3685 C CA  . LEU   B 1 286 ? -3.020  11.376  14.908  1.00 24.75 ? 265 LEU   B CA  1 
ATOM   3686 C C   . LEU   B 1 286 ? -2.958  12.691  15.694  1.00 24.90 ? 265 LEU   B C   1 
ATOM   3687 O O   . LEU   B 1 286 ? -2.248  12.750  16.693  1.00 25.22 ? 265 LEU   B O   1 
ATOM   3688 C CB  . LEU   B 1 286 ? -1.682  11.165  14.194  1.00 25.26 ? 265 LEU   B CB  1 
ATOM   3689 C CG  . LEU   B 1 286 ? -1.565  9.839   13.439  1.00 29.71 ? 265 LEU   B CG  1 
ATOM   3690 C CD1 . LEU   B 1 286 ? -0.186  9.798   12.789  1.00 34.37 ? 265 LEU   B CD1 1 
ATOM   3691 C CD2 . LEU   B 1 286 ? -1.860  8.667   14.369  1.00 27.52 ? 265 LEU   B CD2 1 
ATOM   3692 N N   . VAL   B 1 287 ? -3.698  13.718  15.241  1.00 25.90 ? 266 VAL   B N   1 
ATOM   3693 C CA  . VAL   B 1 287 ? -3.597  15.082  15.773  1.00 25.12 ? 266 VAL   B CA  1 
ATOM   3694 C C   . VAL   B 1 287 ? -4.603  15.252  16.920  1.00 27.16 ? 266 VAL   B C   1 
ATOM   3695 O O   . VAL   B 1 287 ? -5.797  15.029  16.729  1.00 28.09 ? 266 VAL   B O   1 
ATOM   3696 C CB  . VAL   B 1 287 ? -3.919  16.064  14.628  1.00 24.28 ? 266 VAL   B CB  1 
ATOM   3697 C CG1 . VAL   B 1 287 ? -3.798  17.546  15.046  1.00 29.12 ? 266 VAL   B CG1 1 
ATOM   3698 C CG2 . VAL   B 1 287 ? -3.042  15.808  13.410  1.00 29.08 ? 266 VAL   B CG2 1 
ATOM   3699 N N   . HIS   B 1 288 ? -4.134  15.705  18.090  1.00 27.26 ? 267 HIS   B N   1 
ATOM   3700 C CA  . HIS   B 1 288 ? -4.981  15.871  19.266  1.00 28.79 ? 267 HIS   B CA  1 
ATOM   3701 C C   . HIS   B 1 288 ? -5.764  17.177  19.144  1.00 30.92 ? 267 HIS   B C   1 
ATOM   3702 O O   . HIS   B 1 288 ? -5.424  18.034  18.335  1.00 29.60 ? 267 HIS   B O   1 
ATOM   3703 C CB  . HIS   B 1 288 ? -4.166  15.799  20.573  1.00 32.55 ? 267 HIS   B CB  1 
ATOM   3704 C CG  . HIS   B 1 288 ? -3.106  16.847  20.713  1.00 35.34 ? 267 HIS   B CG  1 
ATOM   3705 N ND1 . HIS   B 1 288 ? -3.384  18.197  20.837  1.00 36.25 ? 267 HIS   B ND1 1 
ATOM   3706 C CD2 . HIS   B 1 288 ? -1.753  16.742  20.691  1.00 34.31 ? 267 HIS   B CD2 1 
ATOM   3707 C CE1 . HIS   B 1 288 ? -2.242  18.884  20.896  1.00 37.53 ? 267 HIS   B CE1 1 
ATOM   3708 N NE2 . HIS   B 1 288 ? -1.228  18.020  20.822  1.00 36.08 ? 267 HIS   B NE2 1 
ATOM   3709 N N   . ALA   B 1 289 ? -6.826  17.310  19.955  1.00 30.56 ? 268 ALA   B N   1 
ATOM   3710 C CA  . ALA   B 1 289 ? -7.661  18.507  19.980  1.00 33.77 ? 268 ALA   B CA  1 
ATOM   3711 C C   . ALA   B 1 289 ? -6.808  19.760  20.233  1.00 38.21 ? 268 ALA   B C   1 
ATOM   3712 O O   . ALA   B 1 289 ? -7.259  20.847  19.777  1.00 39.20 ? 268 ALA   B O   1 
ATOM   3713 C CB  . ALA   B 1 289 ? -8.700  18.362  21.068  1.00 34.28 ? 268 ALA   B CB  1 
ATOM   3714 O OXT . ALA   B 1 289 ? -5.746  19.626  20.904  1.00 36.06 ? 268 ALA   B OXT 1 
ATOM   3715 N N   . GLU   C 1 23  ? -3.454  -9.591  58.463  1.00 75.12 ? 2   GLU   C N   1 
ATOM   3716 C CA  . GLU   C 1 23  ? -4.693  -8.896  58.906  1.00 74.94 ? 2   GLU   C CA  1 
ATOM   3717 C C   . GLU   C 1 23  ? -5.269  -8.068  57.748  1.00 73.51 ? 2   GLU   C C   1 
ATOM   3718 O O   . GLU   C 1 23  ? -6.238  -8.483  57.108  1.00 75.05 ? 2   GLU   C O   1 
ATOM   3719 C CB  . GLU   C 1 23  ? -4.397  -8.141  60.206  1.00 72.05 ? 2   GLU   C CB  1 
ATOM   3720 N N   . ALA   C 1 24  ? -4.661  -6.903  57.477  1.00 61.23 ? 3   ALA   C N   1 
ATOM   3721 C CA  . ALA   C 1 24  ? -5.095  -6.003  56.417  1.00 52.23 ? 3   ALA   C CA  1 
ATOM   3722 C C   . ALA   C 1 24  ? -4.191  -6.146  55.184  1.00 55.74 ? 3   ALA   C C   1 
ATOM   3723 O O   . ALA   C 1 24  ? -2.989  -6.394  55.326  1.00 47.14 ? 3   ALA   C O   1 
ATOM   3724 C CB  . ALA   C 1 24  ? -5.060  -4.592  56.937  1.00 47.89 ? 3   ALA   C CB  1 
ATOM   3725 N N   . PRO   C 1 25  ? -4.688  -5.884  53.939  1.00 49.69 ? 4   PRO   C N   1 
ATOM   3726 C CA  . PRO   C 1 25  ? -3.892  -6.155  52.736  1.00 47.05 ? 4   PRO   C CA  1 
ATOM   3727 C C   . PRO   C 1 25  ? -2.851  -5.042  52.621  1.00 42.66 ? 4   PRO   C C   1 
ATOM   3728 O O   . PRO   C 1 25  ? -2.987  -4.022  53.289  1.00 41.37 ? 4   PRO   C O   1 
ATOM   3729 C CB  . PRO   C 1 25  ? -4.960  -6.098  51.616  1.00 45.27 ? 4   PRO   C CB  1 
ATOM   3730 C CG  . PRO   C 1 25  ? -5.969  -5.064  52.101  1.00 46.73 ? 4   PRO   C CG  1 
ATOM   3731 C CD  . PRO   C 1 25  ? -5.933  -5.146  53.633  1.00 42.19 ? 4   PRO   C CD  1 
ATOM   3732 N N   . ALA   C 1 26  ? -1.850  -5.193  51.734  1.00 36.52 ? 5   ALA   C N   1 
ATOM   3733 C CA  . ALA   C 1 26  ? -0.815  -4.156  51.629  1.00 37.06 ? 5   ALA   C CA  1 
ATOM   3734 C C   . ALA   C 1 26  ? -0.570  -3.763  50.167  1.00 33.34 ? 5   ALA   C C   1 
ATOM   3735 O O   . ALA   C 1 26  ? -0.634  -4.623  49.305  1.00 32.45 ? 5   ALA   C O   1 
ATOM   3736 C CB  . ALA   C 1 26  ? 0.450   -4.689  52.210  1.00 33.72 ? 5   ALA   C CB  1 
ATOM   3737 N N   . ALA   C 1 27  ? -0.255  -2.483  49.912  1.00 32.50 ? 6   ALA   C N   1 
ATOM   3738 C CA  . ALA   C 1 27  ? -0.059  -2.015  48.541  1.00 36.53 ? 6   ALA   C CA  1 
ATOM   3739 C C   . ALA   C 1 27  ? 1.275   -1.267  48.419  1.00 35.86 ? 6   ALA   C C   1 
ATOM   3740 O O   . ALA   C 1 27  ? 1.634   -0.517  49.321  1.00 35.02 ? 6   ALA   C O   1 
ATOM   3741 C CB  . ALA   C 1 27  ? -1.223  -1.114  48.133  1.00 31.88 ? 6   ALA   C CB  1 
ATOM   3742 N N   . VAL   C 1 28  ? 1.968   -1.423  47.276  1.00 26.93 ? 7   VAL   C N   1 
ATOM   3743 C CA  . VAL   C 1 28  ? 3.093   -0.560  46.930  1.00 27.77 ? 7   VAL   C CA  1 
ATOM   3744 C C   . VAL   C 1 28  ? 2.591   0.457   45.905  1.00 29.39 ? 7   VAL   C C   1 
ATOM   3745 O O   . VAL   C 1 28  ? 1.940   0.078   44.931  1.00 30.03 ? 7   VAL   C O   1 
ATOM   3746 C CB  . VAL   C 1 28  ? 4.183   -1.386  46.250  1.00 27.23 ? 7   VAL   C CB  1 
ATOM   3747 C CG1 . VAL   C 1 28  ? 5.253   -0.482  45.642  1.00 29.47 ? 7   VAL   C CG1 1 
ATOM   3748 C CG2 . VAL   C 1 28  ? 4.814   -2.382  47.224  1.00 30.83 ? 7   VAL   C CG2 1 
ATOM   3749 N N   . VAL   C 1 29  ? 2.930   1.734   46.095  1.00 27.12 ? 8   VAL   C N   1 
ATOM   3750 C CA  . VAL   C 1 29  ? 2.629   2.732   45.072  1.00 27.69 ? 8   VAL   C CA  1 
ATOM   3751 C C   . VAL   C 1 29  ? 3.942   3.404   44.705  1.00 28.74 ? 8   VAL   C C   1 
ATOM   3752 O O   . VAL   C 1 29  ? 4.584   4.000   45.580  1.00 29.20 ? 8   VAL   C O   1 
ATOM   3753 C CB  . VAL   C 1 29  ? 1.595   3.788   45.508  1.00 29.84 ? 8   VAL   C CB  1 
ATOM   3754 C CG1 . VAL   C 1 29  ? 1.260   4.770   44.375  1.00 29.02 ? 8   VAL   C CG1 1 
ATOM   3755 C CG2 . VAL   C 1 29  ? 0.324   3.123   46.036  1.00 31.00 ? 8   VAL   C CG2 1 
ATOM   3756 N N   . THR   C 1 30  ? 4.325   3.365   43.409  1.00 24.73 ? 9   THR   C N   1 
ATOM   3757 C CA  . THR   C 1 30  ? 5.564   4.034   43.017  1.00 25.98 ? 9   THR   C CA  1 
ATOM   3758 C C   . THR   C 1 30  ? 5.291   5.513   42.762  1.00 32.43 ? 9   THR   C C   1 
ATOM   3759 O O   . THR   C 1 30  ? 4.181   5.844   42.368  1.00 30.80 ? 9   THR   C O   1 
ATOM   3760 C CB  . THR   C 1 30  ? 6.224   3.379   41.802  1.00 25.99 ? 9   THR   C CB  1 
ATOM   3761 O OG1 . THR   C 1 30  ? 5.376   3.438   40.648  1.00 27.45 ? 9   THR   C OG1 1 
ATOM   3762 C CG2 . THR   C 1 30  ? 6.478   1.900   42.039  1.00 27.72 ? 9   THR   C CG2 1 
ATOM   3763 N N   . GLY   C 1 31  ? 6.310   6.360   43.007  1.00 30.13 ? 10  GLY   C N   1 
ATOM   3764 C CA  . GLY   C 1 31  ? 6.247   7.816   42.917  1.00 29.35 ? 10  GLY   C CA  1 
ATOM   3765 C C   . GLY   C 1 31  ? 5.090   8.367   43.751  1.00 34.94 ? 10  GLY   C C   1 
ATOM   3766 O O   . GLY   C 1 31  ? 4.273   9.113   43.219  1.00 34.36 ? 10  GLY   C O   1 
ATOM   3767 N N   . ALA   C 1 32  ? 4.992   7.946   45.031  1.00 27.55 ? 11  ALA   C N   1 
ATOM   3768 C CA  . ALA   C 1 32  ? 3.762   8.125   45.786  1.00 28.74 ? 11  ALA   C CA  1 
ATOM   3769 C C   . ALA   C 1 32  ? 3.782   9.414   46.619  1.00 30.52 ? 11  ALA   C C   1 
ATOM   3770 O O   . ALA   C 1 32  ? 2.850   9.671   47.361  1.00 34.61 ? 11  ALA   C O   1 
ATOM   3771 C CB  . ALA   C 1 32  ? 3.485   6.902   46.629  1.00 33.09 ? 11  ALA   C CB  1 
ATOM   3772 N N   . ALA   C 1 33  ? 4.810   10.248  46.471  1.00 29.05 ? 12  ALA   C N   1 
ATOM   3773 C CA  . ALA   C 1 33  ? 5.028   11.292  47.464  1.00 35.44 ? 12  ALA   C CA  1 
ATOM   3774 C C   . ALA   C 1 33  ? 4.185   12.501  47.111  1.00 44.36 ? 12  ALA   C C   1 
ATOM   3775 O O   . ALA   C 1 33  ? 3.860   13.303  47.995  1.00 37.09 ? 12  ALA   C O   1 
ATOM   3776 C CB  . ALA   C 1 33  ? 6.493   11.683  47.543  1.00 36.07 ? 12  ALA   C CB  1 
ATOM   3777 N N   . LYS   C 1 34  ? 3.873   12.622  45.807  1.00 38.44 ? 13  LYS   C N   1 
ATOM   3778 C CA  . LYS   C 1 34  ? 3.223   13.828  45.315  1.00 37.08 ? 13  LYS   C CA  1 
ATOM   3779 C C   . LYS   C 1 34  ? 2.122   13.459  44.318  1.00 42.09 ? 13  LYS   C C   1 
ATOM   3780 O O   . LYS   C 1 34  ? 2.076   12.327  43.809  1.00 36.39 ? 13  LYS   C O   1 
ATOM   3781 C CB  . LYS   C 1 34  ? 4.265   14.736  44.646  1.00 37.64 ? 13  LYS   C CB  1 
ATOM   3782 C CG  . LYS   C 1 34  ? 5.128   15.539  45.646  0.60 36.53 ? 13  LYS   C CG  1 
ATOM   3783 C CD  . LYS   C 1 34  ? 6.210   16.453  45.090  0.60 35.91 ? 13  LYS   C CD  1 
ATOM   3784 N N   . ARG   C 1 35  ? 1.214   14.425  44.100  1.00 40.19 ? 14  ARG   C N   1 
ATOM   3785 C CA  . ARG   C 1 35  ? 0.332   14.442  42.943  1.00 38.56 ? 14  ARG   C CA  1 
ATOM   3786 C C   . ARG   C 1 35  ? -0.508  13.167  42.881  1.00 33.17 ? 14  ARG   C C   1 
ATOM   3787 O O   . ARG   C 1 35  ? -1.198  12.815  43.843  1.00 37.10 ? 14  ARG   C O   1 
ATOM   3788 C CB  . ARG   C 1 35  ? 1.195   14.757  41.712  1.00 39.10 ? 14  ARG   C CB  1 
ATOM   3789 C CG  . ARG   C 1 35  ? 1.731   16.182  41.659  1.00 43.13 ? 14  ARG   C CG  1 
ATOM   3790 C CD  . ARG   C 1 35  ? 2.884   16.326  40.674  1.00 40.31 ? 14  ARG   C CD  1 
ATOM   3791 N NE  . ARG   C 1 35  ? 2.504   16.124  39.270  0.70 47.50 ? 14  ARG   C NE  1 
ATOM   3792 C CZ  . ARG   C 1 35  ? 1.916   17.004  38.460  0.70 48.61 ? 14  ARG   C CZ  1 
ATOM   3793 N NH1 . ARG   C 1 35  ? 1.730   18.261  38.841  0.70 45.07 ? 14  ARG   C NH1 1 
ATOM   3794 N NH2 . ARG   C 1 35  ? 1.549   16.624  37.242  0.70 42.19 ? 14  ARG   C NH2 1 
ATOM   3795 N N   . ILE   C 1 36  ? -0.521  12.512  41.702  1.00 37.53 ? 15  ILE   C N   1 
ATOM   3796 C CA  . ILE   C 1 36  ? -1.409  11.379  41.482  1.00 30.38 ? 15  ILE   C CA  1 
ATOM   3797 C C   . ILE   C 1 36  ? -1.064  10.211  42.416  1.00 26.42 ? 15  ILE   C C   1 
ATOM   3798 O O   . ILE   C 1 36  ? -1.946  9.614   43.037  1.00 31.50 ? 15  ILE   C O   1 
ATOM   3799 C CB  . ILE   C 1 36  ? -1.466  10.978  39.986  1.00 31.05 ? 15  ILE   C CB  1 
ATOM   3800 C CG1 . ILE   C 1 36  ? -2.165  12.098  39.167  1.00 37.33 ? 15  ILE   C CG1 1 
ATOM   3801 C CG2 . ILE   C 1 36  ? -2.187  9.628   39.849  1.00 27.83 ? 15  ILE   C CG2 1 
ATOM   3802 C CD1 . ILE   C 1 36  ? -2.079  11.933  37.651  1.00 37.02 ? 15  ILE   C CD1 1 
ATOM   3803 N N   . GLY   C 1 37  ? 0.217   9.868   42.528  1.00 28.26 ? 16  GLY   C N   1 
ATOM   3804 C CA  . GLY   C 1 37  ? 0.607   8.746   43.387  1.00 30.85 ? 16  GLY   C CA  1 
ATOM   3805 C C   . GLY   C 1 37  ? 0.264   8.954   44.874  1.00 28.61 ? 16  GLY   C C   1 
ATOM   3806 O O   . GLY   C 1 37  ? -0.125  8.020   45.586  1.00 30.88 ? 16  GLY   C O   1 
ATOM   3807 N N   . ARG   C 1 38  ? 0.375   10.202  45.347  1.00 33.17 ? 17  ARG   C N   1 
ATOM   3808 C CA  . ARG   C 1 38  ? -0.036  10.489  46.708  1.00 29.95 ? 17  ARG   C CA  1 
ATOM   3809 C C   . ARG   C 1 38  ? -1.532  10.252  46.887  1.00 34.11 ? 17  ARG   C C   1 
ATOM   3810 O O   . ARG   C 1 38  ? -1.963  9.656   47.887  1.00 30.15 ? 17  ARG   C O   1 
ATOM   3811 C CB  . ARG   C 1 38  ? 0.285   11.976  46.928  1.00 35.20 ? 17  ARG   C CB  1 
ATOM   3812 C CG  . ARG   C 1 38  ? 0.024   12.504  48.326  1.00 34.55 ? 17  ARG   C CG  1 
ATOM   3813 C CD  . ARG   C 1 38  ? 0.608   13.916  48.437  0.80 40.81 ? 17  ARG   C CD  1 
ATOM   3814 N NE  . ARG   C 1 38  ? 0.841   14.331  49.826  0.80 44.02 ? 17  ARG   C NE  1 
ATOM   3815 C CZ  . ARG   C 1 38  ? -0.063  14.443  50.814  0.80 49.32 ? 17  ARG   C CZ  1 
ATOM   3816 N NH1 . ARG   C 1 38  ? 0.340   14.793  52.016  0.80 44.13 ? 17  ARG   C NH1 1 
ATOM   3817 N NH2 . ARG   C 1 38  ? -1.356  14.218  50.621  0.80 48.20 ? 17  ARG   C NH2 1 
ATOM   3818 N N   . ALA   C 1 39  ? -2.339  10.726  45.908  1.00 30.70 ? 18  ALA   C N   1 
ATOM   3819 C CA  . ALA   C 1 39  ? -3.778  10.580  46.008  1.00 33.37 ? 18  ALA   C CA  1 
ATOM   3820 C C   . ALA   C 1 39  ? -4.113  9.094   46.026  1.00 29.83 ? 18  ALA   C C   1 
ATOM   3821 O O   . ALA   C 1 39  ? -5.031  8.648   46.719  1.00 28.72 ? 18  ALA   C O   1 
ATOM   3822 C CB  . ALA   C 1 39  ? -4.491  11.311  44.867  1.00 32.39 ? 18  ALA   C CB  1 
ATOM   3823 N N   . ILE   C 1 40  ? -3.385  8.331   45.204  1.00 31.55 ? 19  ILE   C N   1 
ATOM   3824 C CA  . ILE   C 1 40  ? -3.626  6.897   45.132  1.00 25.49 ? 19  ILE   C CA  1 
ATOM   3825 C C   . ILE   C 1 40  ? -3.284  6.217   46.468  1.00 27.97 ? 19  ILE   C C   1 
ATOM   3826 O O   . ILE   C 1 40  ? -4.059  5.426   47.018  1.00 28.66 ? 19  ILE   C O   1 
ATOM   3827 C CB  . ILE   C 1 40  ? -2.835  6.302   43.957  1.00 28.50 ? 19  ILE   C CB  1 
ATOM   3828 C CG1 . ILE   C 1 40  ? -3.366  6.822   42.556  1.00 25.23 ? 19  ILE   C CG1 1 
ATOM   3829 C CG2 . ILE   C 1 40  ? -2.903  4.782   44.031  1.00 22.60 ? 19  ILE   C CG2 1 
ATOM   3830 C CD1 . ILE   C 1 40  ? -2.448  6.436   41.402  1.00 28.27 ? 19  ILE   C CD1 1 
ATOM   3831 N N   . ALA   C 1 41  ? -2.090  6.482   46.979  1.00 31.93 ? 20  ALA   C N   1 
ATOM   3832 C CA  . ALA   C 1 41  ? -1.714  6.016   48.321  1.00 34.52 ? 20  ALA   C CA  1 
ATOM   3833 C C   . ALA   C 1 41  ? -2.740  6.357   49.420  1.00 30.41 ? 20  ALA   C C   1 
ATOM   3834 O O   . ALA   C 1 41  ? -3.134  5.475   50.199  1.00 31.69 ? 20  ALA   C O   1 
ATOM   3835 C CB  . ALA   C 1 41  ? -0.329  6.501   48.634  1.00 31.07 ? 20  ALA   C CB  1 
ATOM   3836 N N   . VAL   C 1 42  ? -3.168  7.626   49.503  1.00 31.27 ? 21  VAL   C N   1 
ATOM   3837 C CA  . VAL   C 1 42  ? -4.107  8.047   50.540  1.00 32.84 ? 21  VAL   C CA  1 
ATOM   3838 C C   . VAL   C 1 42  ? -5.401  7.253   50.414  1.00 36.76 ? 21  VAL   C C   1 
ATOM   3839 O O   . VAL   C 1 42  ? -5.970  6.760   51.391  1.00 33.41 ? 21  VAL   C O   1 
ATOM   3840 C CB  . VAL   C 1 42  ? -4.381  9.560   50.371  1.00 31.53 ? 21  VAL   C CB  1 
ATOM   3841 C CG1 . VAL   C 1 42  ? -5.547  10.061  51.230  1.00 35.08 ? 21  VAL   C CG1 1 
ATOM   3842 C CG2 . VAL   C 1 42  ? -3.140  10.384  50.655  1.00 29.33 ? 21  VAL   C CG2 1 
ATOM   3843 N N   . LYS   C 1 43  ? -5.890  7.149   49.168  1.00 35.05 ? 22  LYS   C N   1 
ATOM   3844 C CA  . LYS   C 1 43  ? -7.199  6.567   48.967  1.00 37.51 ? 22  LYS   C CA  1 
ATOM   3845 C C   . LYS   C 1 43  ? -7.085  5.084   49.307  1.00 35.74 ? 22  LYS   C C   1 
ATOM   3846 O O   . LYS   C 1 43  ? -7.998  4.515   49.904  1.00 36.97 ? 22  LYS   C O   1 
ATOM   3847 C CB  . LYS   C 1 43  ? -7.753  6.971   47.586  1.00 38.75 ? 22  LYS   C CB  1 
ATOM   3848 C CG  . LYS   C 1 43  ? -9.237  6.641   47.420  1.00 45.61 ? 22  LYS   C CG  1 
ATOM   3849 C CD  . LYS   C 1 43  ? -9.855  7.304   46.194  1.00 39.40 ? 22  LYS   C CD  1 
ATOM   3850 C CE  . LYS   C 1 43  ? -9.862  8.801   46.240  1.00 39.23 ? 22  LYS   C CE  1 
ATOM   3851 N NZ  . LYS   C 1 43  ? -11.112 9.168   46.908  1.00 42.21 ? 22  LYS   C NZ  1 
ATOM   3852 N N   . LEU   C 1 44  ? -5.941  4.472   48.949  1.00 29.24 ? 23  LEU   C N   1 
ATOM   3853 C CA  . LEU   C 1 44  ? -5.736  3.067   49.273  1.00 30.91 ? 23  LEU   C CA  1 
ATOM   3854 C C   . LEU   C 1 44  ? -5.791  2.889   50.802  1.00 35.69 ? 23  LEU   C C   1 
ATOM   3855 O O   . LEU   C 1 44  ? -6.475  2.002   51.323  1.00 39.95 ? 23  LEU   C O   1 
ATOM   3856 C CB  . LEU   C 1 44  ? -4.378  2.641   48.713  1.00 32.10 ? 23  LEU   C CB  1 
ATOM   3857 C CG  . LEU   C 1 44  ? -4.371  2.176   47.240  1.00 41.00 ? 23  LEU   C CG  1 
ATOM   3858 C CD1 . LEU   C 1 44  ? -2.978  1.877   46.691  1.00 31.29 ? 23  LEU   C CD1 1 
ATOM   3859 C CD2 . LEU   C 1 44  ? -5.314  1.004   46.996  1.00 34.32 ? 23  LEU   C CD2 1 
ATOM   3860 N N   . HIS   C 1 45  ? -5.064  3.770   51.494  1.00 38.32 ? 24  HIS   C N   1 
ATOM   3861 C CA  . HIS   C 1 45  ? -4.984  3.775   52.950  1.00 39.60 ? 24  HIS   C CA  1 
ATOM   3862 C C   . HIS   C 1 45  ? -6.388  3.875   53.561  1.00 42.61 ? 24  HIS   C C   1 
ATOM   3863 O O   . HIS   C 1 45  ? -6.787  3.040   54.387  1.00 41.34 ? 24  HIS   C O   1 
ATOM   3864 C CB  . HIS   C 1 45  ? -4.003  4.849   53.417  1.00 38.87 ? 24  HIS   C CB  1 
ATOM   3865 C CG  . HIS   C 1 45  ? -3.690  4.636   54.858  1.00 45.37 ? 24  HIS   C CG  1 
ATOM   3866 N ND1 . HIS   C 1 45  ? -4.217  5.416   55.866  1.00 47.21 ? 24  HIS   C ND1 1 
ATOM   3867 C CD2 . HIS   C 1 45  ? -2.943  3.694   55.457  1.00 46.60 ? 24  HIS   C CD2 1 
ATOM   3868 C CE1 . HIS   C 1 45  ? -3.773  4.959   57.036  1.00 49.40 ? 24  HIS   C CE1 1 
ATOM   3869 N NE2 . HIS   C 1 45  ? -3.007  3.913   56.814  1.00 46.62 ? 24  HIS   C NE2 1 
ATOM   3870 N N   . GLN   C 1 46  ? -7.142  4.879   53.112  1.00 38.37 ? 25  GLN   C N   1 
ATOM   3871 C CA  . GLN   C 1 46  ? -8.499  5.119   53.586  1.00 42.53 ? 25  GLN   C CA  1 
ATOM   3872 C C   . GLN   C 1 46  ? -9.419  3.934   53.303  1.00 45.40 ? 25  GLN   C C   1 
ATOM   3873 O O   . GLN   C 1 46  ? -10.457 3.786   53.958  1.00 40.33 ? 25  GLN   C O   1 
ATOM   3874 C CB  . GLN   C 1 46  ? -9.082  6.376   52.951  1.00 40.80 ? 25  GLN   C CB  1 
ATOM   3875 C CG  . GLN   C 1 46  ? -8.460  7.674   53.455  1.00 42.50 ? 25  GLN   C CG  1 
ATOM   3876 C CD  . GLN   C 1 46  ? -8.746  8.848   52.545  1.00 51.17 ? 25  GLN   C CD  1 
ATOM   3877 O OE1 . GLN   C 1 46  ? -9.112  8.670   51.374  1.00 49.03 ? 25  GLN   C OE1 1 
ATOM   3878 N NE2 . GLN   C 1 46  ? -8.538  10.058  53.058  1.00 46.32 ? 25  GLN   C NE2 1 
ATOM   3879 N N   . THR   C 1 47  ? -9.044  3.092   52.326  1.00 42.58 ? 26  THR   C N   1 
ATOM   3880 C CA  . THR   C 1 47  ? -9.845  1.925   52.001  1.00 43.19 ? 26  THR   C CA  1 
ATOM   3881 C C   . THR   C 1 47  ? -9.416  0.792   52.924  1.00 45.41 ? 26  THR   C C   1 
ATOM   3882 O O   . THR   C 1 47  ? -10.082 -0.241  53.013  1.00 43.40 ? 26  THR   C O   1 
ATOM   3883 C CB  . THR   C 1 47  ? -9.699  1.571   50.510  1.00 42.08 ? 26  THR   C CB  1 
ATOM   3884 O OG1 . THR   C 1 47  ? -10.218 2.682   49.773  1.00 41.19 ? 26  THR   C OG1 1 
ATOM   3885 C CG2 . THR   C 1 47  ? -10.471 0.324   50.124  1.00 41.70 ? 26  THR   C CG2 1 
ATOM   3886 N N   . GLY   C 1 48  ? -8.248  0.967   53.547  1.00 46.81 ? 27  GLY   C N   1 
ATOM   3887 C CA  . GLY   C 1 48  ? -7.842  0.074   54.619  1.00 47.09 ? 27  GLY   C CA  1 
ATOM   3888 C C   . GLY   C 1 48  ? -6.560  -0.696  54.308  1.00 47.23 ? 27  GLY   C C   1 
ATOM   3889 O O   . GLY   C 1 48  ? -6.208  -1.603  55.065  1.00 43.02 ? 27  GLY   C O   1 
ATOM   3890 N N   . TYR   C 1 49  ? -5.896  -0.358  53.188  1.00 40.06 ? 28  TYR   C N   1 
ATOM   3891 C CA  . TYR   C 1 49  ? -4.601  -0.958  52.870  1.00 38.40 ? 28  TYR   C CA  1 
ATOM   3892 C C   . TYR   C 1 49  ? -3.506  -0.353  53.742  1.00 33.65 ? 28  TYR   C C   1 
ATOM   3893 O O   . TYR   C 1 49  ? -3.535  0.833   54.047  1.00 35.76 ? 28  TYR   C O   1 
ATOM   3894 C CB  . TYR   C 1 49  ? -4.086  -0.693  51.444  1.00 36.72 ? 28  TYR   C CB  1 
ATOM   3895 C CG  . TYR   C 1 49  ? -4.837  -1.523  50.409  1.00 40.94 ? 28  TYR   C CG  1 
ATOM   3896 C CD1 . TYR   C 1 49  ? -6.100  -1.124  49.964  1.00 38.81 ? 28  TYR   C CD1 1 
ATOM   3897 C CD2 . TYR   C 1 49  ? -4.325  -2.726  49.930  1.00 41.80 ? 28  TYR   C CD2 1 
ATOM   3898 C CE1 . TYR   C 1 49  ? -6.829  -1.902  49.072  1.00 38.16 ? 28  TYR   C CE1 1 
ATOM   3899 C CE2 . TYR   C 1 49  ? -5.042  -3.506  49.034  1.00 42.65 ? 28  TYR   C CE2 1 
ATOM   3900 C CZ  . TYR   C 1 49  ? -6.300  -3.099  48.613  1.00 40.55 ? 28  TYR   C CZ  1 
ATOM   3901 O OH  . TYR   C 1 49  ? -7.009  -3.859  47.717  1.00 35.25 ? 28  TYR   C OH  1 
ATOM   3902 N N   . ARG   C 1 50  ? -2.508  -1.174  54.075  1.00 38.27 ? 29  ARG   C N   1 
ATOM   3903 C CA  . ARG   C 1 50  ? -1.205  -0.674  54.519  1.00 39.17 ? 29  ARG   C CA  1 
ATOM   3904 C C   . ARG   C 1 50  ? -0.392  -0.338  53.268  1.00 35.97 ? 29  ARG   C C   1 
ATOM   3905 O O   . ARG   C 1 50  ? -0.595  -0.975  52.236  1.00 38.42 ? 29  ARG   C O   1 
ATOM   3906 C CB  . ARG   C 1 50  ? -0.543  -1.756  55.388  1.00 41.24 ? 29  ARG   C CB  1 
ATOM   3907 C CG  . ARG   C 1 50  ? -1.337  -2.005  56.670  0.70 37.12 ? 29  ARG   C CG  1 
ATOM   3908 C CD  . ARG   C 1 50  ? -1.584  -3.505  56.819  0.70 39.18 ? 29  ARG   C CD  1 
ATOM   3909 N NE  . ARG   C 1 50  ? -0.368  -4.161  57.298  0.70 37.94 ? 29  ARG   C NE  1 
ATOM   3910 C CZ  . ARG   C 1 50  ? -0.186  -5.476  57.424  0.70 38.93 ? 29  ARG   C CZ  1 
ATOM   3911 N NH1 . ARG   C 1 50  ? -1.029  -6.347  56.930  0.70 35.11 ? 29  ARG   C NH1 1 
ATOM   3912 N NH2 . ARG   C 1 50  ? 0.879   -5.917  58.042  0.70 47.62 ? 29  ARG   C NH2 1 
ATOM   3913 N N   . VAL   C 1 51  ? 0.452   0.696   53.313  1.00 36.07 ? 30  VAL   C N   1 
ATOM   3914 C CA  . VAL   C 1 51  ? 1.039   1.150   52.050  1.00 34.34 ? 30  VAL   C CA  1 
ATOM   3915 C C   . VAL   C 1 51  ? 2.555   1.350   52.147  1.00 30.82 ? 30  VAL   C C   1 
ATOM   3916 O O   . VAL   C 1 51  ? 3.082   1.798   53.152  1.00 33.70 ? 30  VAL   C O   1 
ATOM   3917 C CB  . VAL   C 1 51  ? 0.396   2.433   51.488  1.00 32.97 ? 30  VAL   C CB  1 
ATOM   3918 C CG1 . VAL   C 1 51  ? -1.093  2.250   51.197  1.00 33.28 ? 30  VAL   C CG1 1 
ATOM   3919 C CG2 . VAL   C 1 51  ? 0.622   3.633   52.408  1.00 40.29 ? 30  VAL   C CG2 1 
ATOM   3920 N N   . VAL   C 1 52  ? 3.224   1.146   51.014  1.00 27.03 ? 31  VAL   C N   1 
ATOM   3921 C CA  . VAL   C 1 52  ? 4.607   1.524   50.813  1.00 30.30 ? 31  VAL   C CA  1 
ATOM   3922 C C   . VAL   C 1 52  ? 4.592   2.696   49.860  1.00 36.52 ? 31  VAL   C C   1 
ATOM   3923 O O   . VAL   C 1 52  ? 4.063   2.586   48.742  1.00 35.77 ? 31  VAL   C O   1 
ATOM   3924 C CB  . VAL   C 1 52  ? 5.478   0.418   50.198  1.00 32.62 ? 31  VAL   C CB  1 
ATOM   3925 C CG1 . VAL   C 1 52  ? 6.862   0.951   49.806  1.00 34.58 ? 31  VAL   C CG1 1 
ATOM   3926 C CG2 . VAL   C 1 52  ? 5.560   -0.804  51.114  1.00 37.57 ? 31  VAL   C CG2 1 
ATOM   3927 N N   . ILE   C 1 53  ? 5.156   3.803   50.342  1.00 30.54 ? 32  ILE   C N   1 
ATOM   3928 C CA  . ILE   C 1 53  ? 5.279   5.026   49.576  1.00 33.45 ? 32  ILE   C CA  1 
ATOM   3929 C C   . ILE   C 1 53  ? 6.678   5.012   48.961  1.00 31.53 ? 32  ILE   C C   1 
ATOM   3930 O O   . ILE   C 1 53  ? 7.655   5.107   49.683  1.00 33.96 ? 32  ILE   C O   1 
ATOM   3931 C CB  . ILE   C 1 53  ? 5.053   6.199   50.555  1.00 31.93 ? 32  ILE   C CB  1 
ATOM   3932 C CG1 . ILE   C 1 53  ? 3.615   6.165   51.092  1.00 38.92 ? 32  ILE   C CG1 1 
ATOM   3933 C CG2 . ILE   C 1 53  ? 5.427   7.539   49.941  1.00 29.83 ? 32  ILE   C CG2 1 
ATOM   3934 C CD1 . ILE   C 1 53  ? 3.437   6.738   52.488  1.00 44.21 ? 32  ILE   C CD1 1 
ATOM   3935 N N   . HIS   C 1 54  ? 6.767   4.771   47.644  1.00 32.98 ? 33  HIS   C N   1 
ATOM   3936 C CA  . HIS   C 1 54  ? 8.034   4.802   46.931  1.00 29.09 ? 33  HIS   C CA  1 
ATOM   3937 C C   . HIS   C 1 54  ? 8.294   6.236   46.511  1.00 33.09 ? 33  HIS   C C   1 
ATOM   3938 O O   . HIS   C 1 54  ? 7.367   6.990   46.195  1.00 31.54 ? 33  HIS   C O   1 
ATOM   3939 C CB  . HIS   C 1 54  ? 8.123   3.798   45.771  1.00 28.99 ? 33  HIS   C CB  1 
ATOM   3940 C CG  . HIS   C 1 54  ? 9.151   4.241   44.775  1.00 29.84 ? 33  HIS   C CG  1 
ATOM   3941 N ND1 . HIS   C 1 54  ? 8.827   5.161   43.811  1.00 29.41 ? 33  HIS   C ND1 1 
ATOM   3942 C CD2 . HIS   C 1 54  ? 10.465  4.004   44.622  1.00 29.39 ? 33  HIS   C CD2 1 
ATOM   3943 C CE1 . HIS   C 1 54  ? 9.916   5.468   43.098  1.00 28.71 ? 33  HIS   C CE1 1 
ATOM   3944 N NE2 . HIS   C 1 54  ? 10.922  4.756   43.571  1.00 27.21 ? 33  HIS   C NE2 1 
ATOM   3945 N N   . TYR   C 1 55  ? 9.563   6.634   46.621  1.00 34.38 ? 34  TYR   C N   1 
ATOM   3946 C CA  . TYR   C 1 55  ? 9.986   7.945   46.158  1.00 31.70 ? 34  TYR   C CA  1 
ATOM   3947 C C   . TYR   C 1 55  ? 11.380  7.809   45.556  1.00 31.28 ? 34  TYR   C C   1 
ATOM   3948 O O   . TYR   C 1 55  ? 12.088  6.830   45.829  1.00 33.27 ? 34  TYR   C O   1 
ATOM   3949 C CB  . TYR   C 1 55  ? 9.921   9.001   47.275  1.00 29.37 ? 34  TYR   C CB  1 
ATOM   3950 C CG  . TYR   C 1 55  ? 10.935  8.743   48.400  1.00 33.30 ? 34  TYR   C CG  1 
ATOM   3951 C CD1 . TYR   C 1 55  ? 10.597  7.891   49.456  1.00 32.20 ? 34  TYR   C CD1 1 
ATOM   3952 C CD2 . TYR   C 1 55  ? 12.222  9.301   48.392  1.00 32.40 ? 34  TYR   C CD2 1 
ATOM   3953 C CE1 . TYR   C 1 55  ? 11.498  7.617   50.485  1.00 37.03 ? 34  TYR   C CE1 1 
ATOM   3954 C CE2 . TYR   C 1 55  ? 13.126  9.043   49.425  1.00 33.68 ? 34  TYR   C CE2 1 
ATOM   3955 C CZ  . TYR   C 1 55  ? 12.761  8.195   50.465  1.00 37.37 ? 34  TYR   C CZ  1 
ATOM   3956 O OH  . TYR   C 1 55  ? 13.591  7.883   51.510  1.00 40.49 ? 34  TYR   C OH  1 
ATOM   3957 N N   . HIS   C 1 56  ? 11.739  8.806   44.746  1.00 32.65 ? 35  HIS   C N   1 
ATOM   3958 C CA  . HIS   C 1 56  ? 13.097  8.965   44.246  1.00 33.51 ? 35  HIS   C CA  1 
ATOM   3959 C C   . HIS   C 1 56  ? 13.732  10.171  44.964  1.00 38.16 ? 35  HIS   C C   1 
ATOM   3960 O O   . HIS   C 1 56  ? 14.578  9.980   45.828  1.00 38.69 ? 35  HIS   C O   1 
ATOM   3961 C CB  . HIS   C 1 56  ? 13.081  9.076   42.726  1.00 34.45 ? 35  HIS   C CB  1 
ATOM   3962 C CG  . HIS   C 1 56  ? 14.423  9.329   42.102  1.00 39.09 ? 35  HIS   C CG  1 
ATOM   3963 N ND1 . HIS   C 1 56  ? 14.559  9.956   40.877  1.00 37.17 ? 35  HIS   C ND1 1 
ATOM   3964 C CD2 . HIS   C 1 56  ? 15.675  9.041   42.523  1.00 43.56 ? 35  HIS   C CD2 1 
ATOM   3965 C CE1 . HIS   C 1 56  ? 15.856  10.074  40.586  1.00 46.63 ? 35  HIS   C CE1 1 
ATOM   3966 N NE2 . HIS   C 1 56  ? 16.559  9.520   41.567  1.00 44.44 ? 35  HIS   C NE2 1 
ATOM   3967 N N   . ASN   C 1 57  ? 13.303  11.399  44.620  1.00 34.64 ? 36  ASN   C N   1 
ATOM   3968 C CA  . ASN   C 1 57  ? 13.870  12.649  45.125  1.00 46.92 ? 36  ASN   C CA  1 
ATOM   3969 C C   . ASN   C 1 57  ? 13.069  13.229  46.298  1.00 47.72 ? 36  ASN   C C   1 
ATOM   3970 O O   . ASN   C 1 57  ? 13.566  14.078  47.057  1.00 39.82 ? 36  ASN   C O   1 
ATOM   3971 C CB  . ASN   C 1 57  ? 13.933  13.741  44.055  1.00 39.93 ? 36  ASN   C CB  1 
ATOM   3972 C CG  . ASN   C 1 57  ? 14.951  13.464  42.977  1.00 43.17 ? 36  ASN   C CG  1 
ATOM   3973 O OD1 . ASN   C 1 57  ? 16.052  12.980  43.258  1.00 45.60 ? 36  ASN   C OD1 1 
ATOM   3974 N ND2 . ASN   C 1 57  ? 14.603  13.759  41.733  1.00 53.74 ? 36  ASN   C ND2 1 
ATOM   3975 N N   . SER   C 1 58  ? 11.828  12.764  46.470  1.00 42.02 ? 37  SER   C N   1 
ATOM   3976 C CA  . SER   C 1 58  ? 10.906  13.491  47.335  1.00 37.31 ? 37  SER   C CA  1 
ATOM   3977 C C   . SER   C 1 58  ? 10.791  12.829  48.724  1.00 41.89 ? 37  SER   C C   1 
ATOM   3978 O O   . SER   C 1 58  ? 9.708   12.397  49.179  1.00 40.13 ? 37  SER   C O   1 
ATOM   3979 C CB  . SER   C 1 58  ? 9.571   13.719  46.615  1.00 48.00 ? 37  SER   C CB  1 
ATOM   3980 O OG  . SER   C 1 58  ? 9.764   14.321  45.330  1.00 48.85 ? 37  SER   C OG  1 
ATOM   3981 N N   . ALA   C 1 59  ? 11.940  12.786  49.420  1.00 42.96 ? 38  ALA   C N   1 
ATOM   3982 C CA  . ALA   C 1 59  ? 12.030  12.154  50.729  1.00 39.63 ? 38  ALA   C CA  1 
ATOM   3983 C C   . ALA   C 1 59  ? 11.112  12.857  51.722  1.00 36.01 ? 38  ALA   C C   1 
ATOM   3984 O O   . ALA   C 1 59  ? 10.352  12.217  52.455  1.00 36.10 ? 38  ALA   C O   1 
ATOM   3985 C CB  . ALA   C 1 59  ? 13.468  12.170  51.196  1.00 42.22 ? 38  ALA   C CB  1 
ATOM   3986 N N   . GLU   C 1 60  ? 11.240  14.186  51.753  1.00 41.10 ? 39  GLU   C N   1 
ATOM   3987 C CA  . GLU   C 1 60  ? 10.557  15.007  52.745  1.00 47.98 ? 39  GLU   C CA  1 
ATOM   3988 C C   . GLU   C 1 60  ? 9.055   14.763  52.613  1.00 42.55 ? 39  GLU   C C   1 
ATOM   3989 O O   . GLU   C 1 60  ? 8.382   14.392  53.584  1.00 35.41 ? 39  GLU   C O   1 
ATOM   3990 C CB  . GLU   C 1 60  ? 11.053  16.455  52.635  1.00 47.99 ? 39  GLU   C CB  1 
ATOM   3991 C CG  . GLU   C 1 60  ? 10.410  17.405  53.642  0.50 46.42 ? 39  GLU   C CG  1 
ATOM   3992 C CD  . GLU   C 1 60  ? 10.716  18.891  53.529  0.50 46.03 ? 39  GLU   C CD  1 
ATOM   3993 O OE1 . GLU   C 1 60  ? 10.179  19.612  54.390  0.50 43.39 ? 39  GLU   C OE1 1 
ATOM   3994 O OE2 . GLU   C 1 60  ? 11.454  19.336  52.619  0.50 46.80 ? 39  GLU   C OE2 1 
ATOM   3995 N N   . ALA   C 1 61  ? 8.583   14.880  51.361  1.00 43.94 ? 40  ALA   C N   1 
ATOM   3996 C CA  . ALA   C 1 61  ? 7.185   14.701  51.011  1.00 44.12 ? 40  ALA   C CA  1 
ATOM   3997 C C   . ALA   C 1 61  ? 6.731   13.283  51.347  1.00 37.92 ? 40  ALA   C C   1 
ATOM   3998 O O   . ALA   C 1 61  ? 5.613   13.106  51.869  1.00 33.33 ? 40  ALA   C O   1 
ATOM   3999 C CB  . ALA   C 1 61  ? 6.956   15.063  49.552  1.00 40.89 ? 40  ALA   C CB  1 
ATOM   4000 N N   . ALA   C 1 62  ? 7.596   12.285  51.061  1.00 33.55 ? 41  ALA   C N   1 
ATOM   4001 C CA  . ALA   C 1 62  ? 7.253   10.894  51.328  1.00 35.41 ? 41  ALA   C CA  1 
ATOM   4002 C C   . ALA   C 1 62  ? 7.034   10.674  52.822  1.00 34.05 ? 41  ALA   C C   1 
ATOM   4003 O O   . ALA   C 1 62  ? 6.056   10.036  53.246  1.00 31.69 ? 41  ALA   C O   1 
ATOM   4004 C CB  . ALA   C 1 62  ? 8.293   9.941   50.765  1.00 38.69 ? 41  ALA   C CB  1 
ATOM   4005 N N   . VAL   C 1 63  ? 7.958   11.240  53.609  1.00 35.84 ? 42  VAL   C N   1 
ATOM   4006 C CA  . VAL   C 1 63  ? 7.928   11.069  55.053  1.00 36.75 ? 42  VAL   C CA  1 
ATOM   4007 C C   . VAL   C 1 63  ? 6.694   11.761  55.630  1.00 33.10 ? 42  VAL   C C   1 
ATOM   4008 O O   . VAL   C 1 63  ? 6.014   11.164  56.465  1.00 34.03 ? 42  VAL   C O   1 
ATOM   4009 C CB  . VAL   C 1 63  ? 9.245   11.371  55.805  1.00 38.60 ? 42  VAL   C CB  1 
ATOM   4010 C CG1 . VAL   C 1 63  ? 9.088   11.203  57.325  1.00 37.42 ? 42  VAL   C CG1 1 
ATOM   4011 C CG2 . VAL   C 1 63  ? 10.345  10.434  55.321  1.00 34.06 ? 42  VAL   C CG2 1 
ATOM   4012 N N   . SER   C 1 64  ? 6.397   12.960  55.094  1.00 37.38 ? 43  SER   C N   1 
ATOM   4013 C CA  . SER   C 1 64  ? 5.277   13.773  55.528  1.00 38.37 ? 43  SER   C CA  1 
ATOM   4014 C C   . SER   C 1 64  ? 3.973   13.012  55.325  1.00 42.57 ? 43  SER   C C   1 
ATOM   4015 O O   . SER   C 1 64  ? 3.134   12.945  56.233  1.00 39.03 ? 43  SER   C O   1 
ATOM   4016 C CB  . SER   C 1 64  ? 5.291   15.112  54.836  1.00 47.80 ? 43  SER   C CB  1 
ATOM   4017 O OG  . SER   C 1 64  ? 4.341   15.984  55.429  1.00 53.11 ? 43  SER   C OG  1 
ATOM   4018 N N   . LEU   C 1 65  ? 3.837   12.413  54.122  1.00 42.52 ? 44  LEU   C N   1 
ATOM   4019 C CA  . LEU   C 1 65  ? 2.703   11.558  53.815  1.00 35.28 ? 44  LEU   C CA  1 
ATOM   4020 C C   . LEU   C 1 65  ? 2.652   10.373  54.781  1.00 36.81 ? 44  LEU   C C   1 
ATOM   4021 O O   . LEU   C 1 65  ? 1.579   10.088  55.334  1.00 34.51 ? 44  LEU   C O   1 
ATOM   4022 C CB  . LEU   C 1 65  ? 2.640   11.115  52.341  1.00 34.21 ? 44  LEU   C CB  1 
ATOM   4023 C CG  . LEU   C 1 65  ? 1.615   10.024  52.023  1.00 38.04 ? 44  LEU   C CG  1 
ATOM   4024 C CD1 . LEU   C 1 65  ? 0.226   10.579  52.285  1.00 36.49 ? 44  LEU   C CD1 1 
ATOM   4025 C CD2 . LEU   C 1 65  ? 1.764   9.589   50.576  1.00 43.35 ? 44  LEU   C CD2 1 
ATOM   4026 N N   . ALA   C 1 66  ? 3.791   9.685   55.007  1.00 32.72 ? 45  ALA   C N   1 
ATOM   4027 C CA  . ALA   C 1 66  ? 3.746   8.494   55.860  1.00 34.12 ? 45  ALA   C CA  1 
ATOM   4028 C C   . ALA   C 1 66  ? 3.267   8.843   57.274  1.00 39.31 ? 45  ALA   C C   1 
ATOM   4029 O O   . ALA   C 1 66  ? 2.554   8.048   57.896  1.00 34.27 ? 45  ALA   C O   1 
ATOM   4030 C CB  . ALA   C 1 66  ? 5.084   7.779   55.924  1.00 36.42 ? 45  ALA   C CB  1 
ATOM   4031 N N   . ASP   C 1 67  ? 3.717   10.015  57.758  1.00 44.48 ? 46  ASP   C N   1 
ATOM   4032 C CA  . ASP   C 1 67  ? 3.422   10.530  59.091  1.00 42.11 ? 46  ASP   C CA  1 
ATOM   4033 C C   . ASP   C 1 67  ? 1.910   10.726  59.192  1.00 47.46 ? 46  ASP   C C   1 
ATOM   4034 O O   . ASP   C 1 67  ? 1.271   10.176  60.100  1.00 49.72 ? 46  ASP   C O   1 
ATOM   4035 C CB  . ASP   C 1 67  ? 4.183   11.820  59.366  1.00 42.50 ? 46  ASP   C CB  1 
ATOM   4036 C CG  . ASP   C 1 67  ? 5.646   11.694  59.791  0.50 44.92 ? 46  ASP   C CG  1 
ATOM   4037 O OD1 . ASP   C 1 67  ? 6.099   10.557  60.078  0.50 43.80 ? 46  ASP   C OD1 1 
ATOM   4038 O OD2 . ASP   C 1 67  ? 6.337   12.743  59.819  0.50 44.79 ? 46  ASP   C OD2 1 
ATOM   4039 N N   . GLU   C 1 68  ? 1.355   11.452  58.202  1.00 40.87 ? 47  GLU   C N   1 
ATOM   4040 C CA  . GLU   C 1 68  ? -0.068  11.743  58.141  1.00 46.69 ? 47  GLU   C CA  1 
ATOM   4041 C C   . GLU   C 1 68  ? -0.873  10.446  58.215  1.00 48.10 ? 47  GLU   C C   1 
ATOM   4042 O O   . GLU   C 1 68  ? -1.880  10.384  58.922  1.00 47.29 ? 47  GLU   C O   1 
ATOM   4043 C CB  . GLU   C 1 68  ? -0.436  12.611  56.933  1.00 45.63 ? 47  GLU   C CB  1 
ATOM   4044 C CG  . GLU   C 1 68  ? -1.943  12.698  56.679  0.60 50.89 ? 47  GLU   C CG  1 
ATOM   4045 C CD  . GLU   C 1 68  ? -2.375  13.243  55.325  0.60 51.80 ? 47  GLU   C CD  1 
ATOM   4046 O OE1 . GLU   C 1 68  ? -3.341  12.716  54.721  0.60 49.69 ? 47  GLU   C OE1 1 
ATOM   4047 O OE2 . GLU   C 1 68  ? -1.716  14.197  54.866  0.60 50.37 ? 47  GLU   C OE2 1 
ATOM   4048 N N   . LEU   C 1 69  ? -0.418  9.410   57.492  1.00 47.33 ? 48  LEU   C N   1 
ATOM   4049 C CA  . LEU   C 1 69  ? -1.129  8.137   57.413  1.00 41.76 ? 48  LEU   C CA  1 
ATOM   4050 C C   . LEU   C 1 69  ? -1.036  7.363   58.727  1.00 45.86 ? 48  LEU   C C   1 
ATOM   4051 O O   . LEU   C 1 69  ? -2.045  6.826   59.193  1.00 41.39 ? 48  LEU   C O   1 
ATOM   4052 C CB  . LEU   C 1 69  ? -0.702  7.261   56.229  1.00 39.25 ? 48  LEU   C CB  1 
ATOM   4053 C CG  . LEU   C 1 69  ? -1.031  7.857   54.856  1.00 38.82 ? 48  LEU   C CG  1 
ATOM   4054 C CD1 . LEU   C 1 69  ? -0.638  6.868   53.780  1.00 39.17 ? 48  LEU   C CD1 1 
ATOM   4055 C CD2 . LEU   C 1 69  ? -2.506  8.226   54.723  1.00 39.83 ? 48  LEU   C CD2 1 
ATOM   4056 N N   . ASN   C 1 70  ? 0.185   7.274   59.274  1.00 41.26 ? 49  ASN   C N   1 
ATOM   4057 C CA  . ASN   C 1 70  ? 0.454   6.569   60.526  1.00 43.28 ? 49  ASN   C CA  1 
ATOM   4058 C C   . ASN   C 1 70  ? -0.313  7.168   61.704  1.00 45.76 ? 49  ASN   C C   1 
ATOM   4059 O O   . ASN   C 1 70  ? -0.809  6.421   62.546  1.00 49.09 ? 49  ASN   C O   1 
ATOM   4060 C CB  . ASN   C 1 70  ? 1.948   6.497   60.821  1.00 40.68 ? 49  ASN   C CB  1 
ATOM   4061 C CG  . ASN   C 1 70  ? 2.555   5.388   60.001  1.00 38.15 ? 49  ASN   C CG  1 
ATOM   4062 O OD1 . ASN   C 1 70  ? 1.933   4.318   59.921  1.00 33.45 ? 49  ASN   C OD1 1 
ATOM   4063 N ND2 . ASN   C 1 70  ? 3.712   5.633   59.382  1.00 32.96 ? 49  ASN   C ND2 1 
ATOM   4064 N N   . LYS   C 1 71  ? -0.392  8.503   61.757  1.00 44.94 ? 50  LYS   C N   1 
ATOM   4065 C CA  . LYS   C 1 71  ? -1.215  9.191   62.741  1.00 43.82 ? 50  LYS   C CA  1 
ATOM   4066 C C   . LYS   C 1 71  ? -2.659  8.687   62.661  1.00 56.57 ? 50  LYS   C C   1 
ATOM   4067 O O   . LYS   C 1 71  ? -3.304  8.525   63.695  1.00 56.12 ? 50  LYS   C O   1 
ATOM   4068 C CB  . LYS   C 1 71  ? -1.183  10.709  62.530  1.00 44.47 ? 50  LYS   C CB  1 
ATOM   4069 N N   . GLU   C 1 72  ? -3.168  8.432   61.440  1.00 50.43 ? 51  GLU   C N   1 
ATOM   4070 C CA  . GLU   C 1 72  ? -4.515  7.896   61.265  1.00 46.14 ? 51  GLU   C CA  1 
ATOM   4071 C C   . GLU   C 1 72  ? -4.633  6.460   61.779  1.00 47.75 ? 51  GLU   C C   1 
ATOM   4072 O O   . GLU   C 1 72  ? -5.619  6.144   62.447  1.00 45.55 ? 51  GLU   C O   1 
ATOM   4073 C CB  . GLU   C 1 72  ? -5.073  8.015   59.842  1.00 42.13 ? 51  GLU   C CB  1 
ATOM   4074 C CG  . GLU   C 1 72  ? -5.552  9.427   59.540  0.60 41.42 ? 51  GLU   C CG  1 
ATOM   4075 C CD  . GLU   C 1 72  ? -6.835  9.733   60.290  0.60 45.34 ? 51  GLU   C CD  1 
ATOM   4076 O OE1 . GLU   C 1 72  ? -7.084  10.936  60.468  0.60 50.66 ? 51  GLU   C OE1 1 
ATOM   4077 O OE2 . GLU   C 1 72  ? -7.588  8.798   60.656  0.60 42.15 ? 51  GLU   C OE2 1 
ATOM   4078 N N   . ARG   C 1 73  ? -3.661  5.595   61.429  1.00 40.42 ? 52  ARG   C N   1 
ATOM   4079 C CA  . ARG   C 1 73  ? -3.625  4.182   61.810  1.00 44.76 ? 52  ARG   C CA  1 
ATOM   4080 C C   . ARG   C 1 73  ? -2.164  3.774   62.012  1.00 53.51 ? 52  ARG   C C   1 
ATOM   4081 O O   . ARG   C 1 73  ? -1.332  3.899   61.100  1.00 44.23 ? 52  ARG   C O   1 
ATOM   4082 C CB  . ARG   C 1 73  ? -4.278  3.137   60.885  1.00 47.26 ? 52  ARG   C CB  1 
ATOM   4083 C CG  . ARG   C 1 73  ? -5.786  3.176   60.659  0.70 49.31 ? 52  ARG   C CG  1 
ATOM   4084 C CD  . ARG   C 1 73  ? -6.381  1.866   60.130  0.70 45.29 ? 52  ARG   C CD  1 
ATOM   4085 N NE  . ARG   C 1 73  ? -5.859  1.349   58.858  0.70 42.81 ? 52  ARG   C NE  1 
ATOM   4086 C CZ  . ARG   C 1 73  ? -5.845  1.968   57.672  0.70 40.86 ? 52  ARG   C CZ  1 
ATOM   4087 N NH1 . ARG   C 1 73  ? -6.304  3.200   57.544  0.70 38.52 ? 52  ARG   C NH1 1 
ATOM   4088 N NH2 . ARG   C 1 73  ? -5.338  1.353   56.611  0.70 38.04 ? 52  ARG   C NH2 1 
ATOM   4089 N N   . SER   C 1 74  ? -1.860  3.313   63.234  1.00 47.60 ? 53  SER   C N   1 
ATOM   4090 C CA  . SER   C 1 74  ? -0.481  3.160   63.666  1.00 49.48 ? 53  SER   C CA  1 
ATOM   4091 C C   . SER   C 1 74  ? 0.263   2.137   62.814  1.00 42.93 ? 53  SER   C C   1 
ATOM   4092 O O   . SER   C 1 74  ? -0.210  1.013   62.645  1.00 41.58 ? 53  SER   C O   1 
ATOM   4093 C CB  . SER   C 1 74  ? -0.396  2.799   65.138  1.00 54.50 ? 53  SER   C CB  1 
ATOM   4094 O OG  . SER   C 1 74  ? -0.833  3.901   65.919  1.00 64.50 ? 53  SER   C OG  1 
ATOM   4095 N N   . ASN   C 1 75  ? 1.465   2.539   62.351  1.00 43.69 ? 54  ASN   C N   1 
ATOM   4096 C CA  . ASN   C 1 75  ? 2.409   1.628   61.709  1.00 37.75 ? 54  ASN   C CA  1 
ATOM   4097 C C   . ASN   C 1 75  ? 1.732   0.994   60.481  1.00 44.64 ? 54  ASN   C C   1 
ATOM   4098 O O   . ASN   C 1 75  ? 1.736   -0.224  60.294  1.00 41.13 ? 54  ASN   C O   1 
ATOM   4099 C CB  . ASN   C 1 75  ? 3.002   0.642   62.716  1.00 49.07 ? 54  ASN   C CB  1 
ATOM   4100 C CG  . ASN   C 1 75  ? 3.692   1.337   63.877  1.00 52.11 ? 54  ASN   C CG  1 
ATOM   4101 O OD1 . ASN   C 1 75  ? 3.033   1.885   64.770  1.00 50.12 ? 54  ASN   C OD1 1 
ATOM   4102 N ND2 . ASN   C 1 75  ? 5.017   1.358   63.873  1.00 51.91 ? 54  ASN   C ND2 1 
ATOM   4103 N N   . THR   C 1 76  ? 1.148   1.834   59.623  1.00 36.62 ? 55  THR   C N   1 
ATOM   4104 C CA  . THR   C 1 76  ? 0.471   1.284   58.454  1.00 37.42 ? 55  THR   C CA  1 
ATOM   4105 C C   . THR   C 1 76  ? 1.090   1.823   57.160  1.00 37.06 ? 55  THR   C C   1 
ATOM   4106 O O   . THR   C 1 76  ? 0.687   1.387   56.080  1.00 36.58 ? 55  THR   C O   1 
ATOM   4107 C CB  . THR   C 1 76  ? -1.047  1.509   58.462  1.00 36.34 ? 55  THR   C CB  1 
ATOM   4108 O OG1 . THR   C 1 76  ? -1.295  2.899   58.643  1.00 37.06 ? 55  THR   C OG1 1 
ATOM   4109 C CG2 . THR   C 1 76  ? -1.814  0.610   59.418  1.00 41.60 ? 55  THR   C CG2 1 
ATOM   4110 N N   . ALA   C 1 77  ? 2.020   2.779   57.260  1.00 35.01 ? 56  ALA   C N   1 
ATOM   4111 C CA  . ALA   C 1 77  ? 2.699   3.349   56.094  1.00 34.45 ? 56  ALA   C CA  1 
ATOM   4112 C C   . ALA   C 1 77  ? 4.219   3.379   56.300  1.00 36.67 ? 56  ALA   C C   1 
ATOM   4113 O O   . ALA   C 1 77  ? 4.707   3.883   57.323  1.00 36.78 ? 56  ALA   C O   1 
ATOM   4114 C CB  . ALA   C 1 77  ? 2.174   4.759   55.871  1.00 31.49 ? 56  ALA   C CB  1 
ATOM   4115 N N   . VAL   C 1 78  ? 4.970   2.914   55.293  1.00 32.67 ? 57  VAL   C N   1 
ATOM   4116 C CA  . VAL   C 1 78  ? 6.422   2.998   55.260  1.00 35.52 ? 57  VAL   C CA  1 
ATOM   4117 C C   . VAL   C 1 78  ? 6.860   3.635   53.939  1.00 35.15 ? 57  VAL   C C   1 
ATOM   4118 O O   . VAL   C 1 78  ? 6.090   3.667   52.965  1.00 34.62 ? 57  VAL   C O   1 
ATOM   4119 C CB  . VAL   C 1 78  ? 7.084   1.611   55.423  1.00 34.17 ? 57  VAL   C CB  1 
ATOM   4120 C CG1 . VAL   C 1 78  ? 6.824   0.960   56.784  1.00 32.44 ? 57  VAL   C CG1 1 
ATOM   4121 C CG2 . VAL   C 1 78  ? 6.712   0.659   54.283  1.00 32.47 ? 57  VAL   C CG2 1 
ATOM   4122 N N   . VAL   C 1 79  ? 8.093   4.147   53.925  1.00 28.45 ? 58  VAL   C N   1 
ATOM   4123 C CA  . VAL   C 1 79  ? 8.670   4.796   52.753  1.00 33.65 ? 58  VAL   C CA  1 
ATOM   4124 C C   . VAL   C 1 79  ? 9.754   3.896   52.186  1.00 36.38 ? 58  VAL   C C   1 
ATOM   4125 O O   . VAL   C 1 79  ? 10.314  3.053   52.905  1.00 34.16 ? 58  VAL   C O   1 
ATOM   4126 C CB  . VAL   C 1 79  ? 9.212   6.223   52.961  1.00 33.07 ? 58  VAL   C CB  1 
ATOM   4127 C CG1 . VAL   C 1 79  ? 8.138   7.188   53.460  1.00 32.47 ? 58  VAL   C CG1 1 
ATOM   4128 C CG2 . VAL   C 1 79  ? 10.456  6.252   53.850  1.00 32.37 ? 58  VAL   C CG2 1 
ATOM   4129 N N   . CYS   C 1 80  ? 10.005  4.059   50.868  1.00 35.54 ? 59  CYS   C N   1 
ATOM   4130 C CA  . CYS   C 1 80  ? 10.996  3.258   50.175  1.00 30.74 ? 59  CYS   C CA  1 
ATOM   4131 C C   . CYS   C 1 80  ? 11.626  4.110   49.073  1.00 35.20 ? 59  CYS   C C   1 
ATOM   4132 O O   . CYS   C 1 80  ? 10.921  4.589   48.194  1.00 34.11 ? 59  CYS   C O   1 
ATOM   4133 C CB  . CYS   C 1 80  ? 10.365  1.978   49.631  1.00 37.30 ? 59  CYS   C CB  1 
ATOM   4134 S SG  . CYS   C 1 80  ? 11.567  0.810   48.938  1.00 42.68 ? 59  CYS   C SG  1 
ATOM   4135 N N   . GLN   C 1 81  ? 12.946  4.299   49.137  1.00 32.21 ? 60  GLN   C N   1 
ATOM   4136 C CA  . GLN   C 1 81  ? 13.680  5.056   48.140  1.00 35.46 ? 60  GLN   C CA  1 
ATOM   4137 C C   . GLN   C 1 81  ? 14.126  4.092   47.052  1.00 35.17 ? 60  GLN   C C   1 
ATOM   4138 O O   . GLN   C 1 81  ? 14.547  2.966   47.332  1.00 34.97 ? 60  GLN   C O   1 
ATOM   4139 C CB  . GLN   C 1 81  ? 14.906  5.748   48.745  1.00 39.87 ? 60  GLN   C CB  1 
ATOM   4140 C CG  . GLN   C 1 81  ? 15.445  6.935   47.944  1.00 35.15 ? 60  GLN   C CG  1 
ATOM   4141 C CD  . GLN   C 1 81  ? 16.372  6.567   46.802  1.00 38.13 ? 60  GLN   C CD  1 
ATOM   4142 O OE1 . GLN   C 1 81  ? 16.999  5.496   46.781  1.00 34.19 ? 60  GLN   C OE1 1 
ATOM   4143 N NE2 . GLN   C 1 81  ? 16.469  7.474   45.835  1.00 36.68 ? 60  GLN   C NE2 1 
ATOM   4144 N N   . ALA   C 1 82  ? 13.999  4.541   45.802  1.00 36.51 ? 61  ALA   C N   1 
ATOM   4145 C CA  . ALA   C 1 82  ? 14.716  3.905   44.699  1.00 35.36 ? 61  ALA   C CA  1 
ATOM   4146 C C   . ALA   C 1 82  ? 14.699  4.834   43.487  1.00 34.04 ? 61  ALA   C C   1 
ATOM   4147 O O   . ALA   C 1 82  ? 13.682  5.474   43.223  1.00 35.09 ? 61  ALA   C O   1 
ATOM   4148 C CB  . ALA   C 1 82  ? 14.101  2.563   44.361  1.00 35.09 ? 61  ALA   C CB  1 
ATOM   4149 N N   . ASP   C 1 83  ? 15.815  4.899   42.742  1.00 30.14 ? 62  ASP   C N   1 
ATOM   4150 C CA  . ASP   C 1 83  ? 15.765  5.473   41.394  1.00 33.40 ? 62  ASP   C CA  1 
ATOM   4151 C C   . ASP   C 1 83  ? 15.229  4.402   40.439  1.00 37.48 ? 62  ASP   C C   1 
ATOM   4152 O O   . ASP   C 1 83  ? 15.631  3.232   40.544  1.00 35.43 ? 62  ASP   C O   1 
ATOM   4153 C CB  . ASP   C 1 83  ? 17.155  5.891   40.934  1.00 36.69 ? 62  ASP   C CB  1 
ATOM   4154 C CG  . ASP   C 1 83  ? 17.243  6.608   39.589  1.00 39.70 ? 62  ASP   C CG  1 
ATOM   4155 O OD1 . ASP   C 1 83  ? 16.224  6.682   38.895  1.00 40.57 ? 62  ASP   C OD1 1 
ATOM   4156 O OD2 . ASP   C 1 83  ? 18.356  7.093   39.240  1.00 49.32 ? 62  ASP   C OD2 1 
ATOM   4157 N N   . LEU   C 1 84  ? 14.309  4.781   39.523  1.00 34.91 ? 63  LEU   C N   1 
ATOM   4158 C CA  . LEU   C 1 84  ? 13.733  3.809   38.589  1.00 31.95 ? 63  LEU   C CA  1 
ATOM   4159 C C   . LEU   C 1 84  ? 14.189  4.038   37.136  1.00 32.20 ? 63  LEU   C C   1 
ATOM   4160 O O   . LEU   C 1 84  ? 13.687  3.363   36.212  1.00 37.36 ? 63  LEU   C O   1 
ATOM   4161 C CB  . LEU   C 1 84  ? 12.216  3.790   38.720  1.00 29.62 ? 63  LEU   C CB  1 
ATOM   4162 C CG  . LEU   C 1 84  ? 11.716  3.314   40.093  1.00 30.69 ? 63  LEU   C CG  1 
ATOM   4163 C CD1 . LEU   C 1 84  ? 10.206  3.436   40.197  1.00 32.29 ? 63  LEU   C CD1 1 
ATOM   4164 C CD2 . LEU   C 1 84  ? 12.145  1.884   40.374  1.00 34.32 ? 63  LEU   C CD2 1 
ATOM   4165 N N   . THR   C 1 85  ? 15.159  4.938   36.953  1.00 31.36 ? 64  THR   C N   1 
ATOM   4166 C CA  . THR   C 1 85  ? 15.943  4.993   35.713  1.00 36.69 ? 64  THR   C CA  1 
ATOM   4167 C C   . THR   C 1 85  ? 16.422  3.576   35.370  1.00 40.17 ? 64  THR   C C   1 
ATOM   4168 O O   . THR   C 1 85  ? 16.831  2.836   36.269  1.00 36.74 ? 64  THR   C O   1 
ATOM   4169 C CB  . THR   C 1 85  ? 17.125  5.954   35.898  1.00 36.89 ? 64  THR   C CB  1 
ATOM   4170 O OG1 . THR   C 1 85  ? 16.555  7.190   36.330  1.00 40.43 ? 64  THR   C OG1 1 
ATOM   4171 C CG2 . THR   C 1 85  ? 17.888  6.217   34.603  1.00 40.42 ? 64  THR   C CG2 1 
ATOM   4172 N N   . ASN   C 1 86  ? 16.389  3.182   34.083  1.00 39.45 ? 65  ASN   C N   1 
ATOM   4173 C CA  . ASN   C 1 86  ? 16.948  1.890   33.684  1.00 42.65 ? 65  ASN   C CA  1 
ATOM   4174 C C   . ASN   C 1 86  ? 18.470  1.897   33.906  1.00 46.90 ? 65  ASN   C C   1 
ATOM   4175 O O   . ASN   C 1 86  ? 19.138  2.869   33.560  1.00 39.95 ? 65  ASN   C O   1 
ATOM   4176 C CB  . ASN   C 1 86  ? 16.572  1.503   32.252  1.00 39.46 ? 65  ASN   C CB  1 
ATOM   4177 C CG  . ASN   C 1 86  ? 16.962  0.086   31.861  1.00 43.43 ? 65  ASN   C CG  1 
ATOM   4178 O OD1 . ASN   C 1 86  ? 16.782  -0.857  32.645  1.00 47.04 ? 65  ASN   C OD1 1 
ATOM   4179 N ND2 . ASN   C 1 86  ? 17.511  -0.091  30.667  1.00 34.51 ? 65  ASN   C ND2 1 
ATOM   4180 N N   . SER   C 1 87  ? 19.000  0.805   34.491  1.00 45.78 ? 66  SER   C N   1 
ATOM   4181 C CA  . SER   C 1 87  ? 20.437  0.611   34.683  1.00 39.01 ? 66  SER   C CA  1 
ATOM   4182 C C   . SER   C 1 87  ? 20.716  -0.831  35.083  1.00 41.86 ? 66  SER   C C   1 
ATOM   4183 O O   . SER   C 1 87  ? 19.783  -1.600  35.295  1.00 36.76 ? 66  SER   C O   1 
ATOM   4184 C CB  . SER   C 1 87  ? 21.004  1.552   35.710  1.00 43.84 ? 66  SER   C CB  1 
ATOM   4185 O OG  . SER   C 1 87  ? 20.846  1.013   37.017  1.00 46.04 ? 66  SER   C OG  1 
ATOM   4186 N N   . ASN   C 1 88  ? 22.009  -1.195  35.233  1.00 43.34 ? 67  ASN   C N   1 
ATOM   4187 C CA  . ASN   C 1 88  ? 22.293  -2.591  35.537  1.00 49.65 ? 67  ASN   C CA  1 
ATOM   4188 C C   . ASN   C 1 88  ? 21.746  -2.963  36.921  1.00 50.65 ? 67  ASN   C C   1 
ATOM   4189 O O   . ASN   C 1 88  ? 21.584  -4.164  37.184  1.00 45.81 ? 67  ASN   C O   1 
ATOM   4190 C CB  . ASN   C 1 88  ? 23.703  -3.029  35.124  1.00 49.30 ? 67  ASN   C CB  1 
ATOM   4191 C CG  . ASN   C 1 88  ? 23.865  -3.047  33.615  1.00 60.11 ? 67  ASN   C CG  1 
ATOM   4192 O OD1 . ASN   C 1 88  ? 24.089  -2.001  32.991  0.50 63.96 ? 67  ASN   C OD1 1 
ATOM   4193 N ND2 . ASN   C 1 88  ? 23.764  -4.219  33.002  0.50 58.71 ? 67  ASN   C ND2 1 
ATOM   4194 N N   . VAL   C 1 89  ? 21.356  -1.942  37.728  1.00 44.73 ? 68  VAL   C N   1 
ATOM   4195 C CA  . VAL   C 1 89  ? 20.867  -2.127  39.100  1.00 44.73 ? 68  VAL   C CA  1 
ATOM   4196 C C   . VAL   C 1 89  ? 19.340  -1.976  39.224  1.00 46.92 ? 68  VAL   C C   1 
ATOM   4197 O O   . VAL   C 1 89  ? 18.782  -2.141  40.326  1.00 34.02 ? 68  VAL   C O   1 
ATOM   4198 C CB  . VAL   C 1 89  ? 21.628  -1.351  40.205  1.00 46.09 ? 68  VAL   C CB  1 
ATOM   4199 C CG1 . VAL   C 1 89  ? 23.138  -1.613  40.121  1.00 45.36 ? 68  VAL   C CG1 1 
ATOM   4200 C CG2 . VAL   C 1 89  ? 21.345  0.159   40.193  1.00 39.57 ? 68  VAL   C CG2 1 
ATOM   4201 N N   . LEU   C 1 90  ? 18.668  -1.633  38.129  1.00 41.87 ? 69  LEU   C N   1 
ATOM   4202 C CA  . LEU   C 1 90  ? 17.194  -1.489  38.188  1.00 33.05 ? 69  LEU   C CA  1 
ATOM   4203 C C   . LEU   C 1 90  ? 16.584  -2.802  38.705  1.00 31.04 ? 69  LEU   C C   1 
ATOM   4204 O O   . LEU   C 1 90  ? 15.751  -2.738  39.620  1.00 31.73 ? 69  LEU   C O   1 
ATOM   4205 C CB  . LEU   C 1 90  ? 16.622  -1.069  36.843  1.00 38.33 ? 69  LEU   C CB  1 
ATOM   4206 C CG  . LEU   C 1 90  ? 15.515  -0.010  36.843  1.00 42.88 ? 69  LEU   C CG  1 
ATOM   4207 C CD1 . LEU   C 1 90  ? 14.553  -0.234  35.696  1.00 37.80 ? 69  LEU   C CD1 1 
ATOM   4208 C CD2 . LEU   C 1 90  ? 14.774  0.137   38.152  1.00 38.11 ? 69  LEU   C CD2 1 
ATOM   4209 N N   . PRO   C 1 91  ? 16.943  -3.982  38.167  1.00 28.77 ? 70  PRO   C N   1 
ATOM   4210 C CA  . PRO   C 1 91  ? 16.411  -5.212  38.712  1.00 30.23 ? 70  PRO   C CA  1 
ATOM   4211 C C   . PRO   C 1 91  ? 16.416  -5.259  40.240  1.00 35.53 ? 70  PRO   C C   1 
ATOM   4212 O O   . PRO   C 1 91  ? 15.348  -5.407  40.836  1.00 36.00 ? 70  PRO   C O   1 
ATOM   4213 C CB  . PRO   C 1 91  ? 17.283  -6.263  38.027  1.00 34.47 ? 70  PRO   C CB  1 
ATOM   4214 C CG  . PRO   C 1 91  ? 17.605  -5.669  36.651  1.00 30.16 ? 70  PRO   C CG  1 
ATOM   4215 C CD  . PRO   C 1 91  ? 17.804  -4.203  36.975  1.00 28.42 ? 70  PRO   C CD  1 
ATOM   4216 N N   . ALA   C 1 92  ? 17.589  -5.034  40.864  1.00 38.54 ? 71  ALA   C N   1 
ATOM   4217 C CA  . ALA   C 1 92  ? 17.734  -5.092  42.318  1.00 39.07 ? 71  ALA   C CA  1 
ATOM   4218 C C   . ALA   C 1 92  ? 16.899  -4.019  43.015  1.00 36.60 ? 71  ALA   C C   1 
ATOM   4219 O O   . ALA   C 1 92  ? 16.238  -4.293  44.024  1.00 35.66 ? 71  ALA   C O   1 
ATOM   4220 C CB  . ALA   C 1 92  ? 19.206  -5.044  42.736  1.00 40.34 ? 71  ALA   C CB  1 
ATOM   4221 N N   . SER   C 1 93  ? 16.863  -2.818  42.434  1.00 38.75 ? 72  SER   C N   1 
ATOM   4222 C CA  . SER   C 1 93  ? 15.997  -1.775  42.971  1.00 36.81 ? 72  SER   C CA  1 
ATOM   4223 C C   . SER   C 1 93  ? 14.541  -2.227  43.072  1.00 37.62 ? 72  SER   C C   1 
ATOM   4224 O O   . SER   C 1 93  ? 13.875  -1.991  44.093  1.00 32.23 ? 72  SER   C O   1 
ATOM   4225 C CB  . SER   C 1 93  ? 16.105  -0.555  42.154  1.00 38.29 ? 72  SER   C CB  1 
ATOM   4226 O OG  . SER   C 1 93  ? 17.436  -0.068  42.287  1.00 45.22 ? 72  SER   C OG  1 
ATOM   4227 N N   . CYS   C 1 94  ? 14.060  -2.888  41.999  1.00 35.27 ? 73  CYS   C N   1 
ATOM   4228 C CA  . CYS   C 1 94  ? 12.673  -3.265  41.899  1.00 29.46 ? 73  CYS   C CA  1 
ATOM   4229 C C   . CYS   C 1 94  ? 12.370  -4.379  42.893  1.00 33.44 ? 73  CYS   C C   1 
ATOM   4230 O O   . CYS   C 1 94  ? 11.348  -4.300  43.581  1.00 34.00 ? 73  CYS   C O   1 
ATOM   4231 C CB  . CYS   C 1 94  ? 12.266  -3.507  40.435  1.00 29.09 ? 73  CYS   C CB  1 
ATOM   4232 S SG  . CYS   C 1 94  ? 12.275  -1.968  39.476  1.00 33.82 ? 73  CYS   C SG  1 
ATOM   4233 N N   . GLU   C 1 95  ? 13.249  -5.402  42.941  1.00 35.10 ? 74  GLU   C N   1 
ATOM   4234 C CA  . GLU   C 1 95  ? 13.203  -6.432  43.976  1.00 37.35 ? 74  GLU   C CA  1 
ATOM   4235 C C   . GLU   C 1 95  ? 13.091  -5.771  45.359  1.00 33.83 ? 74  GLU   C C   1 
ATOM   4236 O O   . GLU   C 1 95  ? 12.251  -6.135  46.182  1.00 33.22 ? 74  GLU   C O   1 
ATOM   4237 C CB  . GLU   C 1 95  ? 14.365  -7.431  43.824  1.00 37.66 ? 74  GLU   C CB  1 
ATOM   4238 C CG  . GLU   C 1 95  ? 14.014  -8.812  44.376  0.50 41.78 ? 74  GLU   C CG  1 
ATOM   4239 C CD  . GLU   C 1 95  ? 14.945  -9.948  43.976  0.50 44.16 ? 74  GLU   C CD  1 
ATOM   4240 O OE1 . GLU   C 1 95  ? 15.100  -10.206 42.766  0.50 46.55 ? 74  GLU   C OE1 1 
ATOM   4241 O OE2 . GLU   C 1 95  ? 15.513  -10.591 44.874  0.50 44.24 ? 74  GLU   C OE2 1 
ATOM   4242 N N   . GLU   C 1 96  ? 13.888  -4.728  45.588  1.00 36.98 ? 75  GLU   C N   1 
ATOM   4243 C CA  . GLU   C 1 96  ? 13.931  -4.116  46.905  1.00 42.28 ? 75  GLU   C CA  1 
ATOM   4244 C C   . GLU   C 1 96  ? 12.579  -3.505  47.245  1.00 40.24 ? 75  GLU   C C   1 
ATOM   4245 O O   . GLU   C 1 96  ? 12.164  -3.611  48.404  1.00 34.69 ? 75  GLU   C O   1 
ATOM   4246 C CB  . GLU   C 1 96  ? 15.072  -3.117  47.086  1.00 44.56 ? 75  GLU   C CB  1 
ATOM   4247 C CG  . GLU   C 1 96  ? 15.033  -2.362  48.417  0.60 44.17 ? 75  GLU   C CG  1 
ATOM   4248 C CD  . GLU   C 1 96  ? 14.961  -3.064  49.775  0.60 41.57 ? 75  GLU   C CD  1 
ATOM   4249 O OE1 . GLU   C 1 96  ? 14.792  -2.281  50.726  0.60 44.72 ? 75  GLU   C OE1 1 
ATOM   4250 O OE2 . GLU   C 1 96  ? 15.054  -4.305  49.935  0.60 36.58 ? 75  GLU   C OE2 1 
ATOM   4251 N N   . ILE   C 1 97  ? 11.948  -2.837  46.253  1.00 36.17 ? 76  ILE   C N   1 
ATOM   4252 C CA  . ILE   C 1 97  ? 10.692  -2.149  46.491  1.00 29.57 ? 76  ILE   C CA  1 
ATOM   4253 C C   . ILE   C 1 97  ? 9.650   -3.183  46.917  1.00 35.07 ? 76  ILE   C C   1 
ATOM   4254 O O   . ILE   C 1 97  ? 8.930   -2.993  47.913  1.00 33.97 ? 76  ILE   C O   1 
ATOM   4255 C CB  . ILE   C 1 97  ? 10.232  -1.326  45.267  1.00 34.60 ? 76  ILE   C CB  1 
ATOM   4256 C CG1 . ILE   C 1 97  ? 11.197  -0.174  44.926  1.00 33.07 ? 76  ILE   C CG1 1 
ATOM   4257 C CG2 . ILE   C 1 97  ? 8.824   -0.800  45.517  1.00 33.97 ? 76  ILE   C CG2 1 
ATOM   4258 C CD1 . ILE   C 1 97  ? 11.015  0.427   43.535  1.00 33.52 ? 76  ILE   C CD1 1 
ATOM   4259 N N   . ILE   C 1 98  ? 9.592   -4.297  46.168  1.00 30.22 ? 77  ILE   C N   1 
ATOM   4260 C CA  . ILE   C 1 98  ? 8.621   -5.326  46.521  1.00 34.71 ? 77  ILE   C CA  1 
ATOM   4261 C C   . ILE   C 1 98  ? 8.990   -5.902  47.900  1.00 39.22 ? 77  ILE   C C   1 
ATOM   4262 O O   . ILE   C 1 98  ? 8.121   -6.115  48.768  1.00 37.18 ? 77  ILE   C O   1 
ATOM   4263 C CB  . ILE   C 1 98  ? 8.515   -6.415  45.430  1.00 28.79 ? 77  ILE   C CB  1 
ATOM   4264 C CG1 . ILE   C 1 98  ? 8.036   -5.810  44.054  1.00 33.86 ? 77  ILE   C CG1 1 
ATOM   4265 C CG2 . ILE   C 1 98  ? 7.587   -7.548  45.876  1.00 28.05 ? 77  ILE   C CG2 1 
ATOM   4266 C CD1 . ILE   C 1 98  ? 6.717   -5.039  44.099  1.00 31.46 ? 77  ILE   C CD1 1 
ATOM   4267 N N   . ASN   C 1 99  ? 10.285  -6.166  48.096  1.00 41.75 ? 78  ASN   C N   1 
ATOM   4268 C CA  . ASN   C 1 99  ? 10.708  -6.800  49.347  1.00 42.47 ? 78  ASN   C CA  1 
ATOM   4269 C C   . ASN   C 1 99  ? 10.257  -5.982  50.556  1.00 41.33 ? 78  ASN   C C   1 
ATOM   4270 O O   . ASN   C 1 99  ? 9.782   -6.543  51.549  1.00 41.93 ? 78  ASN   C O   1 
ATOM   4271 C CB  . ASN   C 1 99  ? 12.203  -7.079  49.386  1.00 46.44 ? 78  ASN   C CB  1 
ATOM   4272 C CG  . ASN   C 1 99  ? 12.545  -8.374  48.691  1.00 50.15 ? 78  ASN   C CG  1 
ATOM   4273 O OD1 . ASN   C 1 99  ? 11.671  -9.228  48.456  1.00 52.97 ? 78  ASN   C OD1 1 
ATOM   4274 N ND2 . ASN   C 1 99  ? 13.823  -8.551  48.393  1.00 54.90 ? 78  ASN   C ND2 1 
ATOM   4275 N N   . SER   C 1 100 ? 10.402  -4.659  50.456  1.00 41.39 ? 79  SER   C N   1 
ATOM   4276 C CA  . SER   C 1 100 ? 10.147  -3.791  51.591  1.00 42.98 ? 79  SER   C CA  1 
ATOM   4277 C C   . SER   C 1 100 ? 8.676   -3.896  52.003  1.00 45.92 ? 79  SER   C C   1 
ATOM   4278 O O   . SER   C 1 100 ? 8.332   -3.650  53.164  1.00 34.95 ? 79  SER   C O   1 
ATOM   4279 C CB  . SER   C 1 100 ? 10.549  -2.381  51.290  1.00 38.30 ? 79  SER   C CB  1 
ATOM   4280 O OG  . SER   C 1 100 ? 9.538   -1.760  50.496  1.00 45.74 ? 79  SER   C OG  1 
ATOM   4281 N N   . CYS   C 1 101 ? 7.828   -4.255  51.053  1.00 40.19 ? 80  CYS   C N   1 
ATOM   4282 C CA  . CYS   C 1 101 ? 6.401   -4.444  51.399  1.00 39.59 ? 80  CYS   C CA  1 
ATOM   4283 C C   . CYS   C 1 101 ? 6.275   -5.759  52.195  1.00 37.97 ? 80  CYS   C C   1 
ATOM   4284 O O   . CYS   C 1 101 ? 5.592   -5.759  53.224  1.00 35.85 ? 80  CYS   C O   1 
ATOM   4285 C CB  . CYS   C 1 101 ? 5.519   -4.347  50.154  1.00 32.38 ? 80  CYS   C CB  1 
ATOM   4286 S SG  . CYS   C 1 101 ? 3.749   -4.288  50.540  1.00 34.56 ? 80  CYS   C SG  1 
ATOM   4287 N N   . PHE   C 1 102 ? 6.947   -6.814  51.742  1.00 39.22 ? 81  PHE   C N   1 
ATOM   4288 C CA  . PHE   C 1 102 ? 6.878   -8.068  52.486  1.00 41.29 ? 81  PHE   C CA  1 
ATOM   4289 C C   . PHE   C 1 102 ? 7.461   -7.902  53.897  1.00 43.63 ? 81  PHE   C C   1 
ATOM   4290 O O   . PHE   C 1 102 ? 6.960   -8.499  54.851  1.00 40.68 ? 81  PHE   C O   1 
ATOM   4291 C CB  . PHE   C 1 102 ? 7.508   -9.213  51.696  1.00 43.51 ? 81  PHE   C CB  1 
ATOM   4292 C CG  . PHE   C 1 102 ? 6.541   -9.802  50.675  1.00 49.70 ? 81  PHE   C CG  1 
ATOM   4293 C CD1 . PHE   C 1 102 ? 5.596   -10.756 51.057  1.00 45.63 ? 81  PHE   C CD1 1 
ATOM   4294 C CD2 . PHE   C 1 102 ? 6.563   -9.382  49.342  1.00 47.27 ? 81  PHE   C CD2 1 
ATOM   4295 C CE1 . PHE   C 1 102 ? 4.719   -11.297 50.129  1.00 49.11 ? 81  PHE   C CE1 1 
ATOM   4296 C CE2 . PHE   C 1 102 ? 5.668   -9.914  48.425  1.00 45.76 ? 81  PHE   C CE2 1 
ATOM   4297 C CZ  . PHE   C 1 102 ? 4.747   -10.863 48.819  1.00 50.88 ? 81  PHE   C CZ  1 
ATOM   4298 N N   . ARG   C 1 103 ? 8.498   -7.071  54.016  1.00 44.14 ? 82  ARG   C N   1 
ATOM   4299 C CA  . ARG   C 1 103 ? 9.151   -6.847  55.295  1.00 47.05 ? 82  ARG   C CA  1 
ATOM   4300 C C   . ARG   C 1 103 ? 8.262   -6.040  56.230  1.00 49.89 ? 82  ARG   C C   1 
ATOM   4301 O O   . ARG   C 1 103 ? 8.180   -6.367  57.417  1.00 52.33 ? 82  ARG   C O   1 
ATOM   4302 C CB  . ARG   C 1 103 ? 10.499  -6.136  55.175  1.00 45.20 ? 82  ARG   C CB  1 
ATOM   4303 C CG  . ARG   C 1 103 ? 11.399  -7.098  54.424  1.00 47.04 ? 82  ARG   C CG  1 
ATOM   4304 C CD  . ARG   C 1 103 ? 12.815  -6.600  54.576  1.00 53.15 ? 82  ARG   C CD  1 
ATOM   4305 N NE  . ARG   C 1 103 ? 12.811  -5.140  54.464  1.00 50.21 ? 82  ARG   C NE  1 
ATOM   4306 C CZ  . ARG   C 1 103 ? 13.341  -4.488  53.446  1.00 49.63 ? 82  ARG   C CZ  1 
ATOM   4307 N NH1 . ARG   C 1 103 ? 13.941  -5.152  52.471  1.00 51.07 ? 82  ARG   C NH1 1 
ATOM   4308 N NH2 . ARG   C 1 103 ? 13.243  -3.172  53.395  1.00 40.43 ? 82  ARG   C NH2 1 
ATOM   4309 N N   . ALA   C 1 104 ? 7.643   -4.975  55.706  1.00 37.39 ? 83  ALA   C N   1 
ATOM   4310 C CA  . ALA   C 1 104 ? 6.815   -4.142  56.553  1.00 40.38 ? 83  ALA   C CA  1 
ATOM   4311 C C   . ALA   C 1 104 ? 5.540   -4.898  56.939  1.00 47.20 ? 83  ALA   C C   1 
ATOM   4312 O O   . ALA   C 1 104 ? 5.066   -4.751  58.069  1.00 46.46 ? 83  ALA   C O   1 
ATOM   4313 C CB  . ALA   C 1 104 ? 6.522   -2.804  55.875  1.00 38.62 ? 83  ALA   C CB  1 
ATOM   4314 N N   . PHE   C 1 105 ? 4.981   -5.723  56.031  1.00 41.38 ? 84  PHE   C N   1 
ATOM   4315 C CA  . PHE   C 1 105 ? 3.587   -6.087  56.236  1.00 40.81 ? 84  PHE   C CA  1 
ATOM   4316 C C   . PHE   C 1 105 ? 3.349   -7.580  56.057  1.00 41.17 ? 84  PHE   C C   1 
ATOM   4317 O O   . PHE   C 1 105 ? 2.238   -8.069  56.317  1.00 40.74 ? 84  PHE   C O   1 
ATOM   4318 C CB  . PHE   C 1 105 ? 2.591   -5.246  55.427  1.00 39.37 ? 84  PHE   C CB  1 
ATOM   4319 C CG  . PHE   C 1 105 ? 2.812   -3.744  55.484  1.00 38.55 ? 84  PHE   C CG  1 
ATOM   4320 C CD1 . PHE   C 1 105 ? 2.633   -3.038  56.670  1.00 32.29 ? 84  PHE   C CD1 1 
ATOM   4321 C CD2 . PHE   C 1 105 ? 3.138   -3.020  54.324  1.00 38.26 ? 84  PHE   C CD2 1 
ATOM   4322 C CE1 . PHE   C 1 105 ? 2.843   -1.664  56.715  1.00 39.28 ? 84  PHE   C CE1 1 
ATOM   4323 C CE2 . PHE   C 1 105 ? 3.304   -1.634  54.360  1.00 35.87 ? 84  PHE   C CE2 1 
ATOM   4324 C CZ  . PHE   C 1 105 ? 3.187   -0.959  55.564  1.00 37.22 ? 84  PHE   C CZ  1 
ATOM   4325 N N   . GLY   C 1 106 ? 4.385   -8.292  55.615  1.00 37.83 ? 85  GLY   C N   1 
ATOM   4326 C CA  . GLY   C 1 106 ? 4.313   -9.742  55.504  1.00 34.32 ? 85  GLY   C CA  1 
ATOM   4327 C C   . GLY   C 1 106 ? 3.513   -10.212 54.283  1.00 41.69 ? 85  GLY   C C   1 
ATOM   4328 O O   . GLY   C 1 106 ? 3.205   -11.403 54.170  1.00 36.63 ? 85  GLY   C O   1 
ATOM   4329 N N   . ARG   C 1 107 ? 3.138   -9.272  53.397  1.00 37.50 ? 86  ARG   C N   1 
ATOM   4330 C CA  . ARG   C 1 107 ? 2.402   -9.623  52.189  1.00 34.15 ? 86  ARG   C CA  1 
ATOM   4331 C C   . ARG   C 1 107 ? 2.426   -8.410  51.264  1.00 36.65 ? 86  ARG   C C   1 
ATOM   4332 O O   . ARG   C 1 107 ? 2.801   -7.316  51.693  1.00 33.77 ? 86  ARG   C O   1 
ATOM   4333 C CB  . ARG   C 1 107 ? 0.914   -9.903  52.482  1.00 32.71 ? 86  ARG   C CB  1 
ATOM   4334 C CG  . ARG   C 1 107 ? 0.191   -8.727  53.122  1.00 36.36 ? 86  ARG   C CG  1 
ATOM   4335 C CD  . ARG   C 1 107 ? -1.022  -9.253  53.867  1.00 37.91 ? 86  ARG   C CD  1 
ATOM   4336 N NE  . ARG   C 1 107 ? -2.075  -9.499  52.876  1.00 42.87 ? 86  ARG   C NE  1 
ATOM   4337 C CZ  . ARG   C 1 107 ? -3.279  -9.965  53.170  1.00 48.31 ? 86  ARG   C CZ  1 
ATOM   4338 N NH1 . ARG   C 1 107 ? -3.607  -10.230 54.425  1.00 43.61 ? 86  ARG   C NH1 1 
ATOM   4339 N NH2 . ARG   C 1 107 ? -4.153  -10.169 52.209  1.00 42.87 ? 86  ARG   C NH2 1 
ATOM   4340 N N   . CYS   C 1 108 ? 1.957   -8.614  50.017  1.00 38.19 ? 87  CYS   C N   1 
ATOM   4341 C CA  . CYS   C 1 108 ? 1.905   -7.544  49.031  1.00 38.61 ? 87  CYS   C CA  1 
ATOM   4342 C C   . CYS   C 1 108 ? 0.795   -7.875  48.042  1.00 35.06 ? 87  CYS   C C   1 
ATOM   4343 O O   . CYS   C 1 108 ? 0.897   -8.864  47.303  1.00 31.73 ? 87  CYS   C O   1 
ATOM   4344 C CB  . CYS   C 1 108 ? 3.243   -7.397  48.315  1.00 37.61 ? 87  CYS   C CB  1 
ATOM   4345 S SG  . CYS   C 1 108 ? 3.203   -6.032  47.124  1.00 35.83 ? 87  CYS   C SG  1 
ATOM   4346 N N   . ASP   C 1 109 ? -0.283  -7.086  48.108  1.00 29.41 ? 88  ASP   C N   1 
ATOM   4347 C CA  . ASP   C 1 109 ? -1.541  -7.498  47.504  1.00 36.73 ? 88  ASP   C CA  1 
ATOM   4348 C C   . ASP   C 1 109 ? -1.725  -6.708  46.216  1.00 35.11 ? 88  ASP   C C   1 
ATOM   4349 O O   . ASP   C 1 109 ? -2.351  -7.204  45.275  1.00 34.15 ? 88  ASP   C O   1 
ATOM   4350 C CB  . ASP   C 1 109 ? -2.742  -7.254  48.417  1.00 35.31 ? 88  ASP   C CB  1 
ATOM   4351 C CG  . ASP   C 1 109 ? -2.721  -8.091  49.692  1.00 41.00 ? 88  ASP   C CG  1 
ATOM   4352 O OD1 . ASP   C 1 109 ? -3.114  -9.264  49.601  1.00 38.51 ? 88  ASP   C OD1 1 
ATOM   4353 O OD2 . ASP   C 1 109 ? -2.200  -7.589  50.720  1.00 39.73 ? 88  ASP   C OD2 1 
ATOM   4354 N N   . VAL   C 1 110 ? -1.196  -5.482  46.229  1.00 32.11 ? 89  VAL   C N   1 
ATOM   4355 C CA  . VAL   C 1 110 ? -1.402  -4.557  45.120  1.00 28.67 ? 89  VAL   C CA  1 
ATOM   4356 C C   . VAL   C 1 110 ? -0.078  -3.881  44.795  1.00 29.73 ? 89  VAL   C C   1 
ATOM   4357 O O   . VAL   C 1 110 ? 0.653   -3.479  45.685  1.00 32.57 ? 89  VAL   C O   1 
ATOM   4358 C CB  . VAL   C 1 110 ? -2.481  -3.556  45.555  1.00 26.68 ? 89  VAL   C CB  1 
ATOM   4359 C CG1 . VAL   C 1 110 ? -2.501  -2.256  44.744  1.00 27.97 ? 89  VAL   C CG1 1 
ATOM   4360 C CG2 . VAL   C 1 110 ? -3.851  -4.218  45.630  1.00 33.03 ? 89  VAL   C CG2 1 
ATOM   4361 N N   . LEU   C 1 111 ? 0.233   -3.807  43.493  1.00 27.77 ? 90  LEU   C N   1 
ATOM   4362 C CA  . LEU   C 1 111 ? 1.274   -2.936  42.986  1.00 24.24 ? 90  LEU   C CA  1 
ATOM   4363 C C   . LEU   C 1 111 ? 0.642   -1.884  42.067  1.00 27.91 ? 90  LEU   C C   1 
ATOM   4364 O O   . LEU   C 1 111 ? -0.055  -2.246  41.129  1.00 26.02 ? 90  LEU   C O   1 
ATOM   4365 C CB  . LEU   C 1 111 ? 2.186   -3.816  42.158  1.00 25.23 ? 90  LEU   C CB  1 
ATOM   4366 C CG  . LEU   C 1 111 ? 3.292   -3.057  41.412  1.00 24.27 ? 90  LEU   C CG  1 
ATOM   4367 C CD1 . LEU   C 1 111 ? 4.220   -2.178  42.248  1.00 25.62 ? 90  LEU   C CD1 1 
ATOM   4368 C CD2 . LEU   C 1 111 ? 4.025   -4.033  40.531  1.00 27.10 ? 90  LEU   C CD2 1 
ATOM   4369 N N   . VAL   C 1 112 ? 0.910   -0.605  42.331  1.00 26.01 ? 91  VAL   C N   1 
ATOM   4370 C CA  . VAL   C 1 112 ? 0.477   0.493   41.481  1.00 25.77 ? 91  VAL   C CA  1 
ATOM   4371 C C   . VAL   C 1 112 ? 1.722   1.100   40.832  1.00 27.36 ? 91  VAL   C C   1 
ATOM   4372 O O   . VAL   C 1 112 ? 2.507   1.773   41.505  1.00 33.33 ? 91  VAL   C O   1 
ATOM   4373 C CB  . VAL   C 1 112 ? -0.295  1.587   42.228  1.00 23.04 ? 91  VAL   C CB  1 
ATOM   4374 C CG1 . VAL   C 1 112 ? -0.661  2.712   41.250  1.00 27.80 ? 91  VAL   C CG1 1 
ATOM   4375 C CG2 . VAL   C 1 112 ? -1.552  1.020   42.876  1.00 27.06 ? 91  VAL   C CG2 1 
ATOM   4376 N N   . ASN   C 1 113 ? 1.874   0.909   39.504  1.00 25.48 ? 92  ASN   C N   1 
ATOM   4377 C CA  . ASN   C 1 113 ? 2.974   1.495   38.743  1.00 21.30 ? 92  ASN   C CA  1 
ATOM   4378 C C   . ASN   C 1 113 ? 2.566   2.893   38.274  1.00 27.46 ? 92  ASN   C C   1 
ATOM   4379 O O   . ASN   C 1 113 ? 2.057   3.081   37.147  1.00 27.16 ? 92  ASN   C O   1 
ATOM   4380 C CB  . ASN   C 1 113 ? 3.372   0.639   37.543  1.00 23.85 ? 92  ASN   C CB  1 
ATOM   4381 C CG  . ASN   C 1 113 ? 4.063   -0.649  37.938  1.00 29.09 ? 92  ASN   C CG  1 
ATOM   4382 O OD1 . ASN   C 1 113 ? 5.049   -0.604  38.674  1.00 28.91 ? 92  ASN   C OD1 1 
ATOM   4383 N ND2 . ASN   C 1 113 ? 3.585   -1.797  37.478  1.00 28.98 ? 92  ASN   C ND2 1 
ATOM   4384 N N   . ASN   C 1 114 ? 2.874   3.884   39.119  1.00 27.76 ? 93  ASN   C N   1 
ATOM   4385 C CA  . ASN   C 1 114 ? 2.494   5.275   38.929  1.00 26.21 ? 93  ASN   C CA  1 
ATOM   4386 C C   . ASN   C 1 114 ? 3.689   6.126   38.490  1.00 29.40 ? 93  ASN   C C   1 
ATOM   4387 O O   . ASN   C 1 114 ? 3.516   7.125   37.796  1.00 29.93 ? 93  ASN   C O   1 
ATOM   4388 C CB  . ASN   C 1 114 ? 1.826   5.852   40.193  1.00 28.37 ? 93  ASN   C CB  1 
ATOM   4389 C CG  . ASN   C 1 114 ? 1.710   7.366   40.142  1.00 33.12 ? 93  ASN   C CG  1 
ATOM   4390 O OD1 . ASN   C 1 114 ? 0.747   7.876   39.555  1.00 29.10 ? 93  ASN   C OD1 1 
ATOM   4391 N ND2 . ASN   C 1 114 ? 2.649   8.117   40.730  1.00 30.12 ? 93  ASN   C ND2 1 
ATOM   4392 N N   . ALA   C 1 115 ? 4.916   5.786   38.939  1.00 32.86 ? 94  ALA   C N   1 
ATOM   4393 C CA  . ALA   C 1 115 ? 6.059   6.663   38.740  1.00 30.59 ? 94  ALA   C CA  1 
ATOM   4394 C C   . ALA   C 1 115 ? 6.370   6.829   37.261  1.00 30.86 ? 94  ALA   C C   1 
ATOM   4395 O O   . ALA   C 1 115 ? 6.245   5.910   36.472  1.00 27.64 ? 94  ALA   C O   1 
ATOM   4396 C CB  . ALA   C 1 115 ? 7.312   6.170   39.459  1.00 32.63 ? 94  ALA   C CB  1 
ATOM   4397 N N   . SER   C 1 116 ? 6.844   8.006   36.898  1.00 31.10 ? 95  SER   C N   1 
ATOM   4398 C CA  . SER   C 1 116 ? 6.920   8.250   35.475  1.00 34.95 ? 95  SER   C CA  1 
ATOM   4399 C C   . SER   C 1 116 ? 7.702   9.516   35.184  1.00 34.36 ? 95  SER   C C   1 
ATOM   4400 O O   . SER   C 1 116 ? 7.543   10.522  35.887  1.00 37.45 ? 95  SER   C O   1 
ATOM   4401 C CB  . SER   C 1 116 ? 5.510   8.378   34.923  1.00 37.07 ? 95  SER   C CB  1 
ATOM   4402 O OG  . SER   C 1 116 ? 5.542   9.133   33.725  1.00 42.65 ? 95  SER   C OG  1 
ATOM   4403 N N   . ALA   C 1 117 ? 8.474   9.482   34.089  1.00 31.22 ? 96  ALA   C N   1 
ATOM   4404 C CA  . ALA   C 1 117 ? 9.181   10.651  33.593  1.00 33.19 ? 96  ALA   C CA  1 
ATOM   4405 C C   . ALA   C 1 117 ? 8.463   11.191  32.372  1.00 33.37 ? 96  ALA   C C   1 
ATOM   4406 O O   . ALA   C 1 117 ? 7.848   10.404  31.649  1.00 32.33 ? 96  ALA   C O   1 
ATOM   4407 C CB  . ALA   C 1 117 ? 10.600  10.258  33.229  1.00 37.70 ? 96  ALA   C CB  1 
ATOM   4408 N N   . PHE   C 1 118 ? 8.541   12.513  32.148  1.00 30.13 ? 97  PHE   C N   1 
ATOM   4409 C CA  . PHE   C 1 118 ? 7.854   13.106  31.002  1.00 33.69 ? 97  PHE   C CA  1 
ATOM   4410 C C   . PHE   C 1 118 ? 8.563   14.385  30.560  1.00 36.55 ? 97  PHE   C C   1 
ATOM   4411 O O   . PHE   C 1 118 ? 8.656   15.341  31.345  1.00 35.64 ? 97  PHE   C O   1 
ATOM   4412 C CB  . PHE   C 1 118 ? 6.410   13.403  31.444  1.00 32.82 ? 97  PHE   C CB  1 
ATOM   4413 C CG  . PHE   C 1 118 ? 5.556   14.236  30.499  1.00 37.45 ? 97  PHE   C CG  1 
ATOM   4414 C CD1 . PHE   C 1 118 ? 4.857   13.643  29.443  1.00 37.33 ? 97  PHE   C CD1 1 
ATOM   4415 C CD2 . PHE   C 1 118 ? 5.408   15.615  30.686  1.00 40.45 ? 97  PHE   C CD2 1 
ATOM   4416 C CE1 . PHE   C 1 118 ? 4.082   14.412  28.577  1.00 37.89 ? 97  PHE   C CE1 1 
ATOM   4417 C CE2 . PHE   C 1 118 ? 4.613   16.376  29.830  1.00 44.50 ? 97  PHE   C CE2 1 
ATOM   4418 C CZ  . PHE   C 1 118 ? 3.945   15.772  28.779  1.00 44.29 ? 97  PHE   C CZ  1 
ATOM   4419 N N   . TYR   C 1 119 ? 9.034   14.405  29.307  1.00 31.83 ? 98  TYR   C N   1 
ATOM   4420 C CA  . TYR   C 1 119 ? 9.589   15.603  28.696  1.00 32.39 ? 98  TYR   C CA  1 
ATOM   4421 C C   . TYR   C 1 119 ? 9.822   15.365  27.209  1.00 34.77 ? 98  TYR   C C   1 
ATOM   4422 O O   . TYR   C 1 119 ? 9.909   14.213  26.777  1.00 35.65 ? 98  TYR   C O   1 
ATOM   4423 C CB  . TYR   C 1 119 ? 10.891  16.003  29.411  1.00 35.64 ? 98  TYR   C CB  1 
ATOM   4424 C CG  . TYR   C 1 119 ? 11.929  14.895  29.558  1.00 33.52 ? 98  TYR   C CG  1 
ATOM   4425 C CD1 . TYR   C 1 119 ? 12.828  14.600  28.544  1.00 36.37 ? 98  TYR   C CD1 1 
ATOM   4426 C CD2 . TYR   C 1 119 ? 12.013  14.158  30.739  1.00 35.32 ? 98  TYR   C CD2 1 
ATOM   4427 C CE1 . TYR   C 1 119 ? 13.783  13.603  28.714  1.00 34.56 ? 98  TYR   C CE1 1 
ATOM   4428 C CE2 . TYR   C 1 119 ? 12.955  13.154  30.917  1.00 35.18 ? 98  TYR   C CE2 1 
ATOM   4429 C CZ  . TYR   C 1 119 ? 13.840  12.871  29.890  1.00 35.96 ? 98  TYR   C CZ  1 
ATOM   4430 O OH  . TYR   C 1 119 ? 14.790  11.892  30.071  1.00 38.81 ? 98  TYR   C OH  1 
ATOM   4431 N N   . PRO   C 1 120 ? 9.916   16.420  26.365  1.00 36.86 ? 99  PRO   C N   1 
ATOM   4432 C CA  . PRO   C 1 120 ? 10.106  16.230  24.919  1.00 38.51 ? 99  PRO   C CA  1 
ATOM   4433 C C   . PRO   C 1 120 ? 11.432  15.593  24.534  1.00 38.33 ? 99  PRO   C C   1 
ATOM   4434 O O   . PRO   C 1 120 ? 12.426  15.803  25.220  1.00 39.26 ? 99  PRO   C O   1 
ATOM   4435 C CB  . PRO   C 1 120 ? 9.999   17.611  24.292  1.00 36.84 ? 99  PRO   C CB  1 
ATOM   4436 C CG  . PRO   C 1 120 ? 10.220  18.568  25.455  1.00 34.87 ? 99  PRO   C CG  1 
ATOM   4437 C CD  . PRO   C 1 120 ? 9.805   17.848  26.728  1.00 35.95 ? 99  PRO   C CD  1 
ATOM   4438 N N   . THR   C 1 121 ? 11.427  14.834  23.423  1.00 30.20 ? 100 THR   C N   1 
ATOM   4439 C CA  . THR   C 1 121 ? 12.621  14.246  22.838  1.00 31.25 ? 100 THR   C CA  1 
ATOM   4440 C C   . THR   C 1 121 ? 12.533  14.383  21.325  1.00 31.49 ? 100 THR   C C   1 
ATOM   4441 O O   . THR   C 1 121 ? 12.219  13.420  20.615  1.00 32.08 ? 100 THR   C O   1 
ATOM   4442 C CB  . THR   C 1 121 ? 12.824  12.804  23.299  1.00 30.80 ? 100 THR   C CB  1 
ATOM   4443 O OG1 . THR   C 1 121 ? 11.713  12.038  22.827  1.00 32.11 ? 100 THR   C OG1 1 
ATOM   4444 C CG2 . THR   C 1 121 ? 12.877  12.695  24.809  1.00 28.37 ? 100 THR   C CG2 1 
ATOM   4445 N N   . PRO   C 1 122 ? 12.746  15.608  20.801  1.00 32.19 ? 101 PRO   C N   1 
ATOM   4446 C CA  . PRO   C 1 122 ? 12.603  15.910  19.372  1.00 31.03 ? 101 PRO   C CA  1 
ATOM   4447 C C   . PRO   C 1 122 ? 13.397  14.981  18.454  1.00 31.63 ? 101 PRO   C C   1 
ATOM   4448 O O   . PRO   C 1 122 ? 14.522  14.605  18.790  1.00 33.27 ? 101 PRO   C O   1 
ATOM   4449 C CB  . PRO   C 1 122 ? 13.100  17.391  19.291  1.00 32.40 ? 101 PRO   C CB  1 
ATOM   4450 C CG  . PRO   C 1 122 ? 12.796  17.935  20.652  1.00 32.12 ? 101 PRO   C CG  1 
ATOM   4451 C CD  . PRO   C 1 122 ? 13.170  16.787  21.584  1.00 32.85 ? 101 PRO   C CD  1 
ATOM   4452 N N   . LEU   C 1 123 ? 12.805  14.577  17.312  1.00 28.13 ? 102 LEU   C N   1 
ATOM   4453 C CA  . LEU   C 1 123 ? 13.493  13.717  16.344  1.00 35.34 ? 102 LEU   C CA  1 
ATOM   4454 C C   . LEU   C 1 123 ? 14.523  14.490  15.514  1.00 40.47 ? 102 LEU   C C   1 
ATOM   4455 O O   . LEU   C 1 123 ? 15.501  13.898  15.065  1.00 41.07 ? 102 LEU   C O   1 
ATOM   4456 C CB  . LEU   C 1 123 ? 12.551  12.989  15.388  1.00 33.90 ? 102 LEU   C CB  1 
ATOM   4457 C CG  . LEU   C 1 123 ? 11.653  11.929  16.021  1.00 31.54 ? 102 LEU   C CG  1 
ATOM   4458 C CD1 . LEU   C 1 123 ? 10.568  11.589  14.992  1.00 33.84 ? 102 LEU   C CD1 1 
ATOM   4459 C CD2 . LEU   C 1 123 ? 12.454  10.668  16.401  1.00 33.44 ? 102 LEU   C CD2 1 
ATOM   4460 N N   . VAL   C 1 124 ? 14.259  15.779  15.241  1.00 44.97 ? 103 VAL   C N   1 
ATOM   4461 C CA  . VAL   C 1 124 ? 15.123  16.577  14.378  1.00 51.81 ? 103 VAL   C CA  1 
ATOM   4462 C C   . VAL   C 1 124 ? 15.867  17.616  15.235  1.00 56.22 ? 103 VAL   C C   1 
ATOM   4463 O O   . VAL   C 1 124 ? 15.182  18.255  16.065  1.00 61.45 ? 103 VAL   C O   1 
ATOM   4464 C CB  . VAL   C 1 124 ? 14.391  17.255  13.201  1.00 55.81 ? 103 VAL   C CB  1 
ATOM   4465 C CG1 . VAL   C 1 124 ? 15.371  17.919  12.236  1.00 58.59 ? 103 VAL   C CG1 1 
ATOM   4466 C CG2 . VAL   C 1 124 ? 13.509  16.275  12.437  1.00 60.23 ? 103 VAL   C CG2 1 
ATOM   4467 N N   . LYS   C 1 135 ? 20.852  16.225  28.875  1.00 48.39 ? 114 LYS   C N   1 
ATOM   4468 C CA  . LYS   C 1 135 ? 20.678  14.746  28.849  1.00 47.49 ? 114 LYS   C CA  1 
ATOM   4469 C C   . LYS   C 1 135 ? 21.136  14.185  27.500  1.00 47.79 ? 114 LYS   C C   1 
ATOM   4470 O O   . LYS   C 1 135 ? 20.713  14.667  26.443  1.00 50.13 ? 114 LYS   C O   1 
ATOM   4471 C CB  . LYS   C 1 135 ? 19.209  14.413  29.140  1.00 48.27 ? 114 LYS   C CB  1 
ATOM   4472 C CG  . LYS   C 1 135 ? 18.799  14.601  30.593  1.00 46.71 ? 114 LYS   C CG  1 
ATOM   4473 C CD  . LYS   C 1 135 ? 17.317  14.715  30.913  1.00 50.03 ? 114 LYS   C CD  1 
ATOM   4474 C CE  . LYS   C 1 135 ? 17.208  14.855  32.403  0.60 46.31 ? 114 LYS   C CE  1 
ATOM   4475 N NZ  . LYS   C 1 135 ? 15.837  14.685  32.892  0.60 46.76 ? 114 LYS   C NZ  1 
ATOM   4476 N N   . THR   C 1 136 ? 22.005  13.162  27.548  1.00 41.99 ? 115 THR   C N   1 
ATOM   4477 C CA  . THR   C 1 136 ? 22.247  12.347  26.369  1.00 38.67 ? 115 THR   C CA  1 
ATOM   4478 C C   . THR   C 1 136 ? 20.932  11.647  25.997  1.00 38.14 ? 115 THR   C C   1 
ATOM   4479 O O   . THR   C 1 136 ? 20.066  11.391  26.848  1.00 36.00 ? 115 THR   C O   1 
ATOM   4480 C CB  . THR   C 1 136 ? 23.363  11.321  26.584  1.00 35.77 ? 115 THR   C CB  1 
ATOM   4481 O OG1 . THR   C 1 136 ? 22.889  10.395  27.557  1.00 37.59 ? 115 THR   C OG1 1 
ATOM   4482 C CG2 . THR   C 1 136 ? 24.662  11.942  27.074  1.00 44.45 ? 115 THR   C CG2 1 
ATOM   4483 N N   . VAL   C 1 137 ? 20.829  11.294  24.721  1.00 38.66 ? 116 VAL   C N   1 
ATOM   4484 C CA  . VAL   C 1 137 ? 19.727  10.458  24.258  1.00 39.06 ? 116 VAL   C CA  1 
ATOM   4485 C C   . VAL   C 1 137 ? 19.608  9.174   25.085  1.00 39.07 ? 116 VAL   C C   1 
ATOM   4486 O O   . VAL   C 1 137 ? 18.489  8.746   25.381  1.00 39.02 ? 116 VAL   C O   1 
ATOM   4487 C CB  . VAL   C 1 137 ? 19.757  10.191  22.740  1.00 40.52 ? 116 VAL   C CB  1 
ATOM   4488 C CG1 . VAL   C 1 137 ? 20.941  9.330   22.334  1.00 45.72 ? 116 VAL   C CG1 1 
ATOM   4489 C CG2 . VAL   C 1 137 ? 18.443  9.576   22.247  1.00 36.22 ? 116 VAL   C CG2 1 
ATOM   4490 N N   . GLU   C 1 138 ? 20.738  8.568   25.494  1.00 32.82 ? 117 GLU   C N   1 
ATOM   4491 C CA  . GLU   C 1 138 ? 20.649  7.276   26.157  1.00 36.16 ? 117 GLU   C CA  1 
ATOM   4492 C C   . GLU   C 1 138 ? 20.199  7.429   27.619  1.00 35.86 ? 117 GLU   C C   1 
ATOM   4493 O O   . GLU   C 1 138 ? 19.581  6.524   28.186  1.00 35.88 ? 117 GLU   C O   1 
ATOM   4494 C CB  . GLU   C 1 138 ? 21.895  6.411   25.917  1.00 37.09 ? 117 GLU   C CB  1 
ATOM   4495 C CG  . GLU   C 1 138 ? 21.909  5.661   24.579  1.00 35.18 ? 117 GLU   C CG  1 
ATOM   4496 C CD  . GLU   C 1 138 ? 20.937  4.493   24.435  1.00 38.29 ? 117 GLU   C CD  1 
ATOM   4497 O OE1 . GLU   C 1 138 ? 20.684  4.054   23.275  1.00 35.39 ? 117 GLU   C OE1 1 
ATOM   4498 O OE2 . GLU   C 1 138 ? 20.482  3.993   25.503  1.00 40.69 ? 117 GLU   C OE2 1 
ATOM   4499 N N   . THR   C 1 139 ? 20.453  8.602   28.220  1.00 38.55 ? 118 THR   C N   1 
ATOM   4500 C CA  . THR   C 1 139 ? 19.874  8.947   29.512  1.00 37.72 ? 118 THR   C CA  1 
ATOM   4501 C C   . THR   C 1 139 ? 18.360  9.148   29.348  1.00 36.02 ? 118 THR   C C   1 
ATOM   4502 O O   . THR   C 1 139 ? 17.557  8.740   30.196  1.00 35.21 ? 118 THR   C O   1 
ATOM   4503 C CB  . THR   C 1 139 ? 20.544  10.230  30.010  1.00 44.45 ? 118 THR   C CB  1 
ATOM   4504 O OG1 . THR   C 1 139 ? 21.884  9.819   30.283  1.00 48.14 ? 118 THR   C OG1 1 
ATOM   4505 C CG2 . THR   C 1 139 ? 19.885  10.799  31.256  1.00 42.82 ? 118 THR   C CG2 1 
ATOM   4506 N N   . GLN   C 1 140 ? 17.975  9.735   28.218  1.00 26.39 ? 119 GLN   C N   1 
ATOM   4507 C CA  . GLN   C 1 140 ? 16.554  9.971   27.960  1.00 33.66 ? 119 GLN   C CA  1 
ATOM   4508 C C   . GLN   C 1 140 ? 15.807  8.646   27.759  1.00 30.45 ? 119 GLN   C C   1 
ATOM   4509 O O   . GLN   C 1 140 ? 14.692  8.465   28.284  1.00 29.98 ? 119 GLN   C O   1 
ATOM   4510 C CB  . GLN   C 1 140 ? 16.360  10.877  26.742  1.00 36.95 ? 119 GLN   C CB  1 
ATOM   4511 C CG  . GLN   C 1 140 ? 16.757  12.326  26.988  1.00 38.66 ? 119 GLN   C CG  1 
ATOM   4512 C CD  . GLN   C 1 140 ? 16.813  13.099  25.694  1.00 38.05 ? 119 GLN   C CD  1 
ATOM   4513 O OE1 . GLN   C 1 140 ? 16.914  12.512  24.619  1.00 39.72 ? 119 GLN   C OE1 1 
ATOM   4514 N NE2 . GLN   C 1 140 ? 16.681  14.411  25.782  1.00 48.55 ? 119 GLN   C NE2 1 
ATOM   4515 N N   . VAL   C 1 141 ? 16.463  7.687   27.087  1.00 29.97 ? 120 VAL   C N   1 
ATOM   4516 C CA  . VAL   C 1 141 ? 15.893  6.346   26.965  1.00 26.89 ? 120 VAL   C CA  1 
ATOM   4517 C C   . VAL   C 1 141 ? 15.777  5.716   28.352  1.00 34.76 ? 120 VAL   C C   1 
ATOM   4518 O O   . VAL   C 1 141 ? 14.769  5.108   28.705  1.00 29.95 ? 120 VAL   C O   1 
ATOM   4519 C CB  . VAL   C 1 141 ? 16.832  5.552   26.047  1.00 29.57 ? 120 VAL   C CB  1 
ATOM   4520 C CG1 . VAL   C 1 141 ? 16.564  4.051   26.038  1.00 29.64 ? 120 VAL   C CG1 1 
ATOM   4521 C CG2 . VAL   C 1 141 ? 16.819  6.120   24.642  1.00 25.64 ? 120 VAL   C CG2 1 
ATOM   4522 N N   . ALA   C 1 142 ? 16.832  5.862   29.160  1.00 31.70 ? 121 ALA   C N   1 
ATOM   4523 C CA  . ALA   C 1 142 ? 16.820  5.163   30.425  1.00 34.38 ? 121 ALA   C CA  1 
ATOM   4524 C C   . ALA   C 1 142 ? 15.736  5.740   31.331  1.00 32.98 ? 121 ALA   C C   1 
ATOM   4525 O O   . ALA   C 1 142 ? 15.152  5.009   32.124  1.00 34.28 ? 121 ALA   C O   1 
ATOM   4526 C CB  . ALA   C 1 142 ? 18.208  5.209   31.079  1.00 34.77 ? 121 ALA   C CB  1 
ATOM   4527 N N   . GLU   C 1 143 ? 15.535  7.059   31.276  1.00 32.96 ? 122 GLU   C N   1 
ATOM   4528 C CA  . GLU   C 1 143 ? 14.506  7.684   32.091  1.00 36.70 ? 122 GLU   C CA  1 
ATOM   4529 C C   . GLU   C 1 143 ? 13.127  7.371   31.528  1.00 33.88 ? 122 GLU   C C   1 
ATOM   4530 O O   . GLU   C 1 143 ? 12.243  6.851   32.226  1.00 41.73 ? 122 GLU   C O   1 
ATOM   4531 C CB  . GLU   C 1 143 ? 14.760  9.191   32.209  1.00 41.07 ? 122 GLU   C CB  1 
ATOM   4532 C CG  . GLU   C 1 143 ? 16.085  9.487   32.903  1.00 47.18 ? 122 GLU   C CG  1 
ATOM   4533 C CD  . GLU   C 1 143 ? 16.390  10.936  33.234  1.00 52.03 ? 122 GLU   C CD  1 
ATOM   4534 O OE1 . GLU   C 1 143 ? 15.641  11.857  32.806  1.00 48.93 ? 122 GLU   C OE1 1 
ATOM   4535 O OE2 . GLU   C 1 143 ? 17.418  11.113  33.930  1.00 52.63 ? 122 GLU   C OE2 1 
ATOM   4536 N N   . LEU   C 1 144 ? 12.970  7.652   30.241  1.00 31.08 ? 123 LEU   C N   1 
ATOM   4537 C CA  . LEU   C 1 144 ? 11.654  7.658   29.603  1.00 31.20 ? 123 LEU   C CA  1 
ATOM   4538 C C   . LEU   C 1 144 ? 11.161  6.246   29.292  1.00 36.44 ? 123 LEU   C C   1 
ATOM   4539 O O   . LEU   C 1 144 ? 9.992   5.948   29.491  1.00 49.25 ? 123 LEU   C O   1 
ATOM   4540 C CB  . LEU   C 1 144 ? 11.605  8.540   28.366  1.00 30.65 ? 123 LEU   C CB  1 
ATOM   4541 C CG  . LEU   C 1 144 ? 11.709  10.051  28.586  1.00 31.93 ? 123 LEU   C CG  1 
ATOM   4542 C CD1 . LEU   C 1 144 ? 11.618  10.654  27.211  1.00 29.06 ? 123 LEU   C CD1 1 
ATOM   4543 C CD2 . LEU   C 1 144 ? 10.545  10.548  29.417  1.00 32.74 ? 123 LEU   C CD2 1 
ATOM   4544 N N   . ILE   C 1 145 ? 12.051  5.348   28.876  1.00 31.50 ? 124 ILE   C N   1 
ATOM   4545 C CA  . ILE   C 1 145 ? 11.651  3.957   28.716  1.00 27.60 ? 124 ILE   C CA  1 
ATOM   4546 C C   . ILE   C 1 145 ? 11.859  3.227   30.033  1.00 29.96 ? 124 ILE   C C   1 
ATOM   4547 O O   . ILE   C 1 145 ? 11.048  2.396   30.437  1.00 28.67 ? 124 ILE   C O   1 
ATOM   4548 C CB  . ILE   C 1 145 ? 12.447  3.305   27.573  1.00 31.38 ? 124 ILE   C CB  1 
ATOM   4549 C CG1 . ILE   C 1 145 ? 12.360  4.123   26.294  1.00 30.95 ? 124 ILE   C CG1 1 
ATOM   4550 C CG2 . ILE   C 1 145 ? 12.012  1.845   27.364  1.00 33.01 ? 124 ILE   C CG2 1 
ATOM   4551 C CD1 . ILE   C 1 145 ? 10.944  4.320   25.721  1.00 30.20 ? 124 ILE   C CD1 1 
ATOM   4552 N N   . GLY   C 1 146 ? 12.945  3.565   30.746  1.00 28.26 ? 125 GLY   C N   1 
ATOM   4553 C CA  . GLY   C 1 146 ? 13.193  2.900   32.012  1.00 28.43 ? 125 GLY   C CA  1 
ATOM   4554 C C   . GLY   C 1 146 ? 12.083  3.072   33.036  1.00 30.08 ? 125 GLY   C C   1 
ATOM   4555 O O   . GLY   C 1 146 ? 11.552  2.096   33.559  1.00 35.62 ? 125 GLY   C O   1 
ATOM   4556 N N   . THR   C 1 147 ? 11.738  4.323   33.367  1.00 34.85 ? 126 THR   C N   1 
ATOM   4557 C CA  . THR   C 1 147 ? 10.762  4.517   34.436  1.00 35.17 ? 126 THR   C CA  1 
ATOM   4558 C C   . THR   C 1 147 ? 9.363   4.143   33.959  1.00 33.89 ? 126 THR   C C   1 
ATOM   4559 O O   . THR   C 1 147 ? 8.555   3.596   34.720  1.00 37.14 ? 126 THR   C O   1 
ATOM   4560 C CB  . THR   C 1 147 ? 10.811  5.960   34.947  1.00 42.24 ? 126 THR   C CB  1 
ATOM   4561 O OG1 . THR   C 1 147 ? 10.185  6.685   33.879  1.00 45.30 ? 126 THR   C OG1 1 
ATOM   4562 C CG2 . THR   C 1 147 ? 12.249  6.385   35.196  1.00 38.88 ? 126 THR   C CG2 1 
ATOM   4563 N N   . ASN   C 1 148 ? 9.087   4.427   32.690  1.00 30.86 ? 127 ASN   C N   1 
ATOM   4564 C CA  . ASN   C 1 148 ? 7.726   4.284   32.180  1.00 34.06 ? 127 ASN   C CA  1 
ATOM   4565 C C   . ASN   C 1 148 ? 7.385   2.823   31.865  1.00 32.44 ? 127 ASN   C C   1 
ATOM   4566 O O   . ASN   C 1 148 ? 6.215   2.457   31.829  1.00 33.37 ? 127 ASN   C O   1 
ATOM   4567 C CB  . ASN   C 1 148 ? 7.479   5.169   30.955  1.00 35.43 ? 127 ASN   C CB  1 
ATOM   4568 C CG  . ASN   C 1 148 ? 7.131   6.613   31.282  1.00 43.79 ? 127 ASN   C CG  1 
ATOM   4569 O OD1 . ASN   C 1 148 ? 6.129   6.865   31.958  1.00 50.01 ? 127 ASN   C OD1 1 
ATOM   4570 N ND2 . ASN   C 1 148 ? 7.854   7.580   30.733  1.00 35.44 ? 127 ASN   C ND2 1 
ATOM   4571 N N   . ALA   C 1 149 ? 8.385   1.982   31.575  1.00 29.13 ? 128 ALA   C N   1 
ATOM   4572 C CA  . ALA   C 1 149 ? 8.062   0.657   31.038  1.00 25.00 ? 128 ALA   C CA  1 
ATOM   4573 C C   . ALA   C 1 149 ? 8.893   -0.473  31.656  1.00 26.45 ? 128 ALA   C C   1 
ATOM   4574 O O   . ALA   C 1 149 ? 8.360   -1.498  32.088  1.00 29.20 ? 128 ALA   C O   1 
ATOM   4575 C CB  . ALA   C 1 149 ? 8.239   0.681   29.534  1.00 25.40 ? 128 ALA   C CB  1 
ATOM   4576 N N   . ILE   C 1 150 ? 10.207  -0.271  31.724  1.00 31.49 ? 129 ILE   C N   1 
ATOM   4577 C CA  . ILE   C 1 150 ? 11.071  -1.355  32.186  1.00 28.27 ? 129 ILE   C CA  1 
ATOM   4578 C C   . ILE   C 1 150 ? 10.894  -1.590  33.681  1.00 27.73 ? 129 ILE   C C   1 
ATOM   4579 O O   . ILE   C 1 150 ? 10.836  -2.715  34.129  1.00 27.21 ? 129 ILE   C O   1 
ATOM   4580 C CB  . ILE   C 1 150 ? 12.518  -1.083  31.778  1.00 29.61 ? 129 ILE   C CB  1 
ATOM   4581 C CG1 . ILE   C 1 150 ? 12.551  -0.902  30.274  1.00 28.08 ? 129 ILE   C CG1 1 
ATOM   4582 C CG2 . ILE   C 1 150 ? 13.430  -2.245  32.215  1.00 29.19 ? 129 ILE   C CG2 1 
ATOM   4583 C CD1 . ILE   C 1 150 ? 13.737  -0.121  29.744  1.00 38.28 ? 129 ILE   C CD1 1 
ATOM   4584 N N   . ALA   C 1 151 ? 10.811  -0.530  34.478  1.00 24.69 ? 130 ALA   C N   1 
ATOM   4585 C CA  . ALA   C 1 151 ? 10.620  -0.752  35.907  1.00 25.91 ? 130 ALA   C CA  1 
ATOM   4586 C C   . ALA   C 1 151 ? 9.265   -1.384  36.214  1.00 26.18 ? 130 ALA   C C   1 
ATOM   4587 O O   . ALA   C 1 151 ? 9.195   -2.388  36.945  1.00 25.74 ? 130 ALA   C O   1 
ATOM   4588 C CB  . ALA   C 1 151 ? 10.861  0.546   36.668  1.00 26.05 ? 130 ALA   C CB  1 
ATOM   4589 N N   . PRO   C 1 152 ? 8.125   -0.928  35.600  1.00 26.29 ? 131 PRO   C N   1 
ATOM   4590 C CA  . PRO   C 1 152 ? 6.884   -1.682  35.758  1.00 25.91 ? 131 PRO   C CA  1 
ATOM   4591 C C   . PRO   C 1 152 ? 7.059   -3.173  35.447  1.00 23.87 ? 131 PRO   C C   1 
ATOM   4592 O O   . PRO   C 1 152 ? 6.451   -4.026  36.099  1.00 31.93 ? 131 PRO   C O   1 
ATOM   4593 C CB  . PRO   C 1 152 ? 5.970   -0.907  34.747  1.00 25.22 ? 131 PRO   C CB  1 
ATOM   4594 C CG  . PRO   C 1 152 ? 6.405   0.537   34.947  1.00 23.45 ? 131 PRO   C CG  1 
ATOM   4595 C CD  . PRO   C 1 152 ? 7.929   0.394   34.949  1.00 27.20 ? 131 PRO   C CD  1 
ATOM   4596 N N   . PHE   C 1 153 ? 7.816   -3.464  34.383  1.00 22.44 ? 132 PHE   C N   1 
ATOM   4597 C CA  . PHE   C 1 153 ? 8.005   -4.873  34.008  1.00 24.83 ? 132 PHE   C CA  1 
ATOM   4598 C C   . PHE   C 1 153 ? 8.799   -5.647  35.092  1.00 27.31 ? 132 PHE   C C   1 
ATOM   4599 O O   . PHE   C 1 153 ? 8.436   -6.790  35.443  1.00 30.43 ? 132 PHE   C O   1 
ATOM   4600 C CB  . PHE   C 1 153 ? 8.771   -4.832  32.675  1.00 26.87 ? 132 PHE   C CB  1 
ATOM   4601 C CG  . PHE   C 1 153 ? 9.435   -6.175  32.349  1.00 32.03 ? 132 PHE   C CG  1 
ATOM   4602 C CD1 . PHE   C 1 153 ? 8.696   -7.230  31.801  1.00 32.16 ? 132 PHE   C CD1 1 
ATOM   4603 C CD2 . PHE   C 1 153 ? 10.797  -6.375  32.585  1.00 30.33 ? 132 PHE   C CD2 1 
ATOM   4604 C CE1 . PHE   C 1 153 ? 9.319   -8.458  31.508  1.00 32.39 ? 132 PHE   C CE1 1 
ATOM   4605 C CE2 . PHE   C 1 153 ? 11.426  -7.598  32.299  1.00 28.63 ? 132 PHE   C CE2 1 
ATOM   4606 C CZ  . PHE   C 1 153 ? 10.679  -8.642  31.764  1.00 30.55 ? 132 PHE   C CZ  1 
ATOM   4607 N N   . LEU   C 1 154 ? 9.840   -5.008  35.659  1.00 31.19 ? 133 LEU   C N   1 
ATOM   4608 C CA  . LEU   C 1 154 ? 10.673  -5.658  36.681  1.00 26.70 ? 133 LEU   C CA  1 
ATOM   4609 C C   . LEU   C 1 154 ? 9.920   -5.781  38.007  1.00 31.71 ? 133 LEU   C C   1 
ATOM   4610 O O   . LEU   C 1 154 ? 9.952   -6.833  38.667  1.00 29.27 ? 133 LEU   C O   1 
ATOM   4611 C CB  . LEU   C 1 154 ? 11.995  -4.927  36.845  1.00 28.57 ? 133 LEU   C CB  1 
ATOM   4612 C CG  . LEU   C 1 154 ? 12.899  -4.896  35.609  1.00 30.68 ? 133 LEU   C CG  1 
ATOM   4613 C CD1 . LEU   C 1 154 ? 13.973  -3.841  35.761  1.00 27.19 ? 133 LEU   C CD1 1 
ATOM   4614 C CD2 . LEU   C 1 154 ? 13.525  -6.280  35.495  1.00 30.64 ? 133 LEU   C CD2 1 
ATOM   4615 N N   . LEU   C 1 155 ? 9.248   -4.702  38.403  1.00 26.51 ? 134 LEU   C N   1 
ATOM   4616 C CA  . LEU   C 1 155 ? 8.352   -4.764  39.560  1.00 28.67 ? 134 LEU   C CA  1 
ATOM   4617 C C   . LEU   C 1 155 ? 7.274   -5.844  39.407  1.00 32.70 ? 134 LEU   C C   1 
ATOM   4618 O O   . LEU   C 1 155 ? 6.927   -6.537  40.377  1.00 29.84 ? 134 LEU   C O   1 
ATOM   4619 C CB  . LEU   C 1 155 ? 7.749   -3.375  39.754  1.00 28.97 ? 134 LEU   C CB  1 
ATOM   4620 C CG  . LEU   C 1 155 ? 8.695   -2.298  40.293  1.00 31.29 ? 134 LEU   C CG  1 
ATOM   4621 C CD1 . LEU   C 1 155 ? 8.200   -0.897  39.950  1.00 30.12 ? 134 LEU   C CD1 1 
ATOM   4622 C CD2 . LEU   C 1 155 ? 8.864   -2.463  41.828  1.00 28.00 ? 134 LEU   C CD2 1 
ATOM   4623 N N   . THR   C 1 156 ? 6.705   -5.991  38.188  1.00 30.15 ? 135 THR   C N   1 
ATOM   4624 C CA  . THR   C 1 156 ? 5.683   -7.004  37.946  1.00 27.32 ? 135 THR   C CA  1 
ATOM   4625 C C   . THR   C 1 156 ? 6.297   -8.384  38.190  1.00 27.10 ? 135 THR   C C   1 
ATOM   4626 O O   . THR   C 1 156 ? 5.662   -9.265  38.772  1.00 29.12 ? 135 THR   C O   1 
ATOM   4627 C CB  . THR   C 1 156 ? 5.128   -6.897  36.513  1.00 25.14 ? 135 THR   C CB  1 
ATOM   4628 O OG1 . THR   C 1 156 ? 4.387   -5.678  36.459  1.00 28.20 ? 135 THR   C OG1 1 
ATOM   4629 C CG2 . THR   C 1 156 ? 4.133   -8.005  36.196  1.00 22.41 ? 135 THR   C CG2 1 
ATOM   4630 N N   . MET   C 1 157 ? 7.499   -8.583  37.679  1.00 23.26 ? 136 MET   C N   1 
ATOM   4631 C CA  . MET   C 1 157 ? 8.201   -9.857  37.834  1.00 31.44 ? 136 MET   C CA  1 
ATOM   4632 C C   . MET   C 1 157 ? 8.413   -10.155 39.328  1.00 30.52 ? 136 MET   C C   1 
ATOM   4633 O O   . MET   C 1 157 ? 8.114   -11.263 39.796  1.00 35.56 ? 136 MET   C O   1 
ATOM   4634 C CB  . MET   C 1 157 ? 9.606   -9.768  37.219  1.00 30.72 ? 136 MET   C CB  1 
ATOM   4635 C CG  . MET   C 1 157 ? 9.716   -9.994  35.733  1.00 43.98 ? 136 MET   C CG  1 
ATOM   4636 S SD  . MET   C 1 157 ? 11.428  -10.091 35.150  1.00 47.25 ? 136 MET   C SD  1 
ATOM   4637 C CE  . MET   C 1 157 ? 11.943  -11.437 36.218  1.00 35.66 ? 136 MET   C CE  1 
ATOM   4638 N N   . SER   C 1 158 ? 8.907   -9.159  40.090  1.00 29.75 ? 137 SER   C N   1 
ATOM   4639 C CA  . SER   C 1 158 ? 9.256   -9.402  41.496  1.00 29.96 ? 137 SER   C CA  1 
ATOM   4640 C C   . SER   C 1 158 ? 7.969   -9.607  42.290  1.00 37.72 ? 137 SER   C C   1 
ATOM   4641 O O   . SER   C 1 158 ? 7.906   -10.485 43.159  1.00 39.45 ? 137 SER   C O   1 
ATOM   4642 C CB  . SER   C 1 158 ? 10.098  -8.287  42.067  1.00 35.03 ? 137 SER   C CB  1 
ATOM   4643 O OG  . SER   C 1 158 ? 11.285  -8.145  41.287  1.00 38.40 ? 137 SER   C OG  1 
ATOM   4644 N N   . PHE   C 1 159 ? 6.920   -8.834  41.931  1.00 29.06 ? 138 PHE   C N   1 
ATOM   4645 C CA  . PHE   C 1 159 ? 5.614   -8.953  42.567  1.00 31.67 ? 138 PHE   C CA  1 
ATOM   4646 C C   . PHE   C 1 159 ? 5.073   -10.376 42.411  1.00 37.75 ? 138 PHE   C C   1 
ATOM   4647 O O   . PHE   C 1 159 ? 4.504   -10.934 43.365  1.00 39.02 ? 138 PHE   C O   1 
ATOM   4648 C CB  . PHE   C 1 159 ? 4.663   -7.863  42.039  1.00 28.62 ? 138 PHE   C CB  1 
ATOM   4649 C CG  . PHE   C 1 159 ? 3.232   -8.011  42.556  1.00 30.39 ? 138 PHE   C CG  1 
ATOM   4650 C CD1 . PHE   C 1 159 ? 2.310   -8.837  41.925  1.00 30.68 ? 138 PHE   C CD1 1 
ATOM   4651 C CD2 . PHE   C 1 159 ? 2.809   -7.276  43.640  1.00 26.59 ? 138 PHE   C CD2 1 
ATOM   4652 C CE1 . PHE   C 1 159 ? 1.009   -8.971  42.422  1.00 36.11 ? 138 PHE   C CE1 1 
ATOM   4653 C CE2 . PHE   C 1 159 ? 1.508   -7.400  44.143  1.00 30.72 ? 138 PHE   C CE2 1 
ATOM   4654 C CZ  . PHE   C 1 159 ? 0.605   -8.245  43.536  1.00 34.11 ? 138 PHE   C CZ  1 
ATOM   4655 N N   . ALA   C 1 160 ? 5.202   -10.951 41.198  1.00 35.10 ? 139 ALA   C N   1 
ATOM   4656 C CA  . ALA   C 1 160 ? 4.557   -12.233 40.948  1.00 33.58 ? 139 ALA   C CA  1 
ATOM   4657 C C   . ALA   C 1 160 ? 5.390   -13.357 41.556  1.00 33.19 ? 139 ALA   C C   1 
ATOM   4658 O O   . ALA   C 1 160 ? 4.827   -14.328 42.070  1.00 37.10 ? 139 ALA   C O   1 
ATOM   4659 C CB  . ALA   C 1 160 ? 4.391   -12.496 39.464  1.00 35.26 ? 139 ALA   C CB  1 
ATOM   4660 N N   . GLN   C 1 161 ? 6.713   -13.245 41.379  1.00 32.21 ? 140 GLN   C N   1 
ATOM   4661 C CA  . GLN   C 1 161 ? 7.694   -14.209 41.883  1.00 41.70 ? 140 GLN   C CA  1 
ATOM   4662 C C   . GLN   C 1 161 ? 7.484   -14.452 43.381  1.00 43.88 ? 140 GLN   C C   1 
ATOM   4663 O O   . GLN   C 1 161 ? 7.569   -15.591 43.844  1.00 47.60 ? 140 GLN   C O   1 
ATOM   4664 C CB  . GLN   C 1 161 ? 9.114   -13.657 41.711  1.00 43.22 ? 140 GLN   C CB  1 
ATOM   4665 C CG  . GLN   C 1 161 ? 10.171  -14.674 41.293  0.70 51.91 ? 140 GLN   C CG  1 
ATOM   4666 C CD  . GLN   C 1 161 ? 10.064  -15.095 39.841  0.70 54.65 ? 140 GLN   C CD  1 
ATOM   4667 O OE1 . GLN   C 1 161 ? 9.744   -16.250 39.540  0.70 52.32 ? 140 GLN   C OE1 1 
ATOM   4668 N NE2 . GLN   C 1 161 ? 10.329  -14.171 38.921  0.70 51.84 ? 140 GLN   C NE2 1 
ATOM   4669 N N   . ARG   C 1 162 ? 7.247   -13.370 44.137  1.00 47.55 ? 141 ARG   C N   1 
ATOM   4670 C CA  . ARG   C 1 162 ? 7.118   -13.430 45.588  1.00 50.61 ? 141 ARG   C CA  1 
ATOM   4671 C C   . ARG   C 1 162 ? 5.707   -13.873 45.986  1.00 55.09 ? 141 ARG   C C   1 
ATOM   4672 O O   . ARG   C 1 162 ? 5.395   -13.905 47.176  1.00 60.55 ? 141 ARG   C O   1 
ATOM   4673 C CB  . ARG   C 1 162 ? 7.513   -12.098 46.246  1.00 43.53 ? 141 ARG   C CB  1 
ATOM   4674 C CG  . ARG   C 1 162 ? 8.990   -11.722 46.161  1.00 50.36 ? 141 ARG   C CG  1 
ATOM   4675 C CD  . ARG   C 1 162 ? 9.781   -11.997 47.440  1.00 50.35 ? 141 ARG   C CD  1 
ATOM   4676 N N   . GLN   C 1 163 ? 4.839   -14.200 45.015  1.00 49.74 ? 142 GLN   C N   1 
ATOM   4677 C CA  . GLN   C 1 163 ? 3.570   -14.796 45.406  1.00 56.94 ? 142 GLN   C CA  1 
ATOM   4678 C C   . GLN   C 1 163 ? 3.723   -16.328 45.408  1.00 66.89 ? 142 GLN   C C   1 
ATOM   4679 O O   . GLN   C 1 163 ? 4.007   -16.864 46.499  1.00 67.75 ? 142 GLN   C O   1 
ATOM   4680 C CB  . GLN   C 1 163 ? 2.363   -14.424 44.545  1.00 53.71 ? 142 GLN   C CB  1 
ATOM   4681 C CG  . GLN   C 1 163 ? 2.122   -12.932 44.353  1.00 45.28 ? 142 GLN   C CG  1 
ATOM   4682 C CD  . GLN   C 1 163 ? 1.971   -12.125 45.625  1.00 49.06 ? 142 GLN   C CD  1 
ATOM   4683 O OE1 . GLN   C 1 163 ? 1.234   -12.491 46.555  1.00 43.83 ? 142 GLN   C OE1 1 
ATOM   4684 N NE2 . GLN   C 1 163 ? 2.667   -10.993 45.654  1.00 40.67 ? 142 GLN   C NE2 1 
ATOM   4685 N N   . SER   C 1 173 ? -7.555  -14.485 48.292  1.00 50.41 ? 152 SER   C N   1 
ATOM   4686 C CA  . SER   C 1 173 ? -6.745  -13.259 48.048  1.00 55.66 ? 152 SER   C CA  1 
ATOM   4687 C C   . SER   C 1 173 ? -7.284  -12.505 46.830  1.00 57.10 ? 152 SER   C C   1 
ATOM   4688 O O   . SER   C 1 173 ? -7.972  -13.082 45.987  1.00 58.43 ? 152 SER   C O   1 
ATOM   4689 C CB  . SER   C 1 173 ? -5.273  -13.573 47.906  1.00 55.59 ? 152 SER   C CB  1 
ATOM   4690 N N   . ASN   C 1 174 ? -7.013  -11.194 46.790  1.00 51.84 ? 153 ASN   C N   1 
ATOM   4691 C CA  . ASN   C 1 174 ? -7.335  -10.340 45.656  1.00 46.31 ? 153 ASN   C CA  1 
ATOM   4692 C C   . ASN   C 1 174 ? -6.067  -9.579  45.276  1.00 37.44 ? 153 ASN   C C   1 
ATOM   4693 O O   . ASN   C 1 174 ? -5.881  -8.426  45.667  1.00 36.96 ? 153 ASN   C O   1 
ATOM   4694 C CB  . ASN   C 1 174 ? -8.513  -9.404  45.926  1.00 45.84 ? 153 ASN   C CB  1 
ATOM   4695 C CG  . ASN   C 1 174 ? -8.956  -8.669  44.675  1.00 54.50 ? 153 ASN   C CG  1 
ATOM   4696 O OD1 . ASN   C 1 174 ? -8.325  -8.788  43.620  1.00 47.24 ? 153 ASN   C OD1 1 
ATOM   4697 N ND2 . ASN   C 1 174 ? -10.037 -7.909  44.752  1.00 56.87 ? 153 ASN   C ND2 1 
ATOM   4698 N N   . LEU   C 1 175 ? -5.211  -10.259 44.512  1.00 31.45 ? 154 LEU   C N   1 
ATOM   4699 C CA  . LEU   C 1 175 ? -3.951  -9.700  44.038  1.00 27.87 ? 154 LEU   C CA  1 
ATOM   4700 C C   . LEU   C 1 175 ? -4.217  -9.024  42.691  1.00 35.47 ? 154 LEU   C C   1 
ATOM   4701 O O   . LEU   C 1 175 ? -4.855  -9.609  41.808  1.00 32.86 ? 154 LEU   C O   1 
ATOM   4702 C CB  . LEU   C 1 175 ? -2.935  -10.811 43.804  1.00 30.95 ? 154 LEU   C CB  1 
ATOM   4703 C CG  . LEU   C 1 175 ? -2.689  -11.763 44.984  1.00 40.20 ? 154 LEU   C CG  1 
ATOM   4704 C CD1 . LEU   C 1 175 ? -1.725  -12.867 44.600  1.00 37.87 ? 154 LEU   C CD1 1 
ATOM   4705 C CD2 . LEU   C 1 175 ? -2.183  -10.973 46.168  1.00 35.16 ? 154 LEU   C CD2 1 
ATOM   4706 N N   . SER   C 1 176 ? -3.710  -7.796  42.549  1.00 33.31 ? 155 SER   C N   1 
ATOM   4707 C CA  . SER   C 1 176 ? -3.798  -7.124  41.256  1.00 32.01 ? 155 SER   C CA  1 
ATOM   4708 C C   . SER   C 1 176 ? -2.676  -6.105  41.099  1.00 32.18 ? 155 SER   C C   1 
ATOM   4709 O O   . SER   C 1 176 ? -2.038  -5.678  42.089  1.00 29.88 ? 155 SER   C O   1 
ATOM   4710 C CB  . SER   C 1 176 ? -5.169  -6.541  40.982  1.00 35.61 ? 155 SER   C CB  1 
ATOM   4711 O OG  . SER   C 1 176 ? -5.367  -5.297  41.643  1.00 33.23 ? 155 SER   C OG  1 
ATOM   4712 N N   . ILE   C 1 177 ? -2.451  -5.726  39.828  1.00 26.67 ? 156 ILE   C N   1 
ATOM   4713 C CA  . ILE   C 1 177 ? -1.496  -4.707  39.465  1.00 24.79 ? 156 ILE   C CA  1 
ATOM   4714 C C   . ILE   C 1 177 ? -2.240  -3.599  38.702  1.00 27.75 ? 156 ILE   C C   1 
ATOM   4715 O O   . ILE   C 1 177 ? -3.080  -3.889  37.844  1.00 28.31 ? 156 ILE   C O   1 
ATOM   4716 C CB  . ILE   C 1 177 ? -0.361  -5.308  38.624  1.00 24.07 ? 156 ILE   C CB  1 
ATOM   4717 C CG1 . ILE   C 1 177 ? 0.373   -6.449  39.371  1.00 29.86 ? 156 ILE   C CG1 1 
ATOM   4718 C CG2 . ILE   C 1 177 ? 0.643   -4.253  38.170  1.00 25.01 ? 156 ILE   C CG2 1 
ATOM   4719 C CD1 . ILE   C 1 177 ? 1.373   -7.227  38.524  1.00 29.91 ? 156 ILE   C CD1 1 
ATOM   4720 N N   . VAL   C 1 178 ? -1.898  -2.331  38.987  1.00 27.01 ? 157 VAL   C N   1 
ATOM   4721 C CA  . VAL   C 1 178 ? -2.519  -1.247  38.216  1.00 26.82 ? 157 VAL   C CA  1 
ATOM   4722 C C   . VAL   C 1 178 ? -1.416  -0.384  37.590  1.00 26.11 ? 157 VAL   C C   1 
ATOM   4723 O O   . VAL   C 1 178 ? -0.591  0.210   38.295  1.00 29.76 ? 157 VAL   C O   1 
ATOM   4724 C CB  . VAL   C 1 178 ? -3.508  -0.373  39.032  1.00 26.10 ? 157 VAL   C CB  1 
ATOM   4725 C CG1 . VAL   C 1 178 ? -4.123  0.707   38.127  1.00 24.79 ? 157 VAL   C CG1 1 
ATOM   4726 C CG2 . VAL   C 1 178 ? -4.607  -1.201  39.705  1.00 26.19 ? 157 VAL   C CG2 1 
ATOM   4727 N N   . ASN   C 1 179 ? -1.391  -0.278  36.247  1.00 23.89 ? 158 ASN   C N   1 
ATOM   4728 C CA  . ASN   C 1 179 ? -0.432  0.565   35.550  1.00 21.91 ? 158 ASN   C CA  1 
ATOM   4729 C C   . ASN   C 1 179 ? -1.017  1.919   35.128  1.00 25.63 ? 158 ASN   C C   1 
ATOM   4730 O O   . ASN   C 1 179 ? -2.090  1.937   34.551  1.00 27.39 ? 158 ASN   C O   1 
ATOM   4731 C CB  . ASN   C 1 179 ? 0.088   -0.154  34.306  1.00 26.26 ? 158 ASN   C CB  1 
ATOM   4732 C CG  . ASN   C 1 179 ? 0.859   -1.388  34.724  1.00 31.32 ? 158 ASN   C CG  1 
ATOM   4733 O OD1 . ASN   C 1 179 ? 1.515   -1.329  35.776  1.00 28.70 ? 158 ASN   C OD1 1 
ATOM   4734 N ND2 . ASN   C 1 179 ? 0.776   -2.489  33.967  1.00 25.84 ? 158 ASN   C ND2 1 
ATOM   4735 N N   . LEU   C 1 180 ? -0.324  3.040   35.405  1.00 23.83 ? 159 LEU   C N   1 
ATOM   4736 C CA  . LEU   C 1 180 ? -0.765  4.375   34.994  1.00 22.75 ? 159 LEU   C CA  1 
ATOM   4737 C C   . LEU   C 1 180 ? -0.340  4.652   33.544  1.00 25.12 ? 159 LEU   C C   1 
ATOM   4738 O O   . LEU   C 1 180 ? 0.827   4.903   33.232  1.00 25.71 ? 159 LEU   C O   1 
ATOM   4739 C CB  . LEU   C 1 180 ? -0.258  5.489   35.926  1.00 26.64 ? 159 LEU   C CB  1 
ATOM   4740 C CG  . LEU   C 1 180 ? -1.088  5.765   37.185  1.00 30.58 ? 159 LEU   C CG  1 
ATOM   4741 C CD1 . LEU   C 1 180 ? -2.345  6.499   36.747  1.00 28.85 ? 159 LEU   C CD1 1 
ATOM   4742 C CD2 . LEU   C 1 180 ? -1.445  4.498   37.936  1.00 27.22 ? 159 LEU   C CD2 1 
ATOM   4743 N N   . CYS   C 1 181 ? -1.343  4.584   32.645  1.00 24.81 ? 160 CYS   C N   1 
ATOM   4744 C CA  . CYS   C 1 181 ? -1.115  4.672   31.210  1.00 25.00 ? 160 CYS   C CA  1 
ATOM   4745 C C   . CYS   C 1 181 ? -1.383  6.120   30.757  1.00 29.76 ? 160 CYS   C C   1 
ATOM   4746 O O   . CYS   C 1 181 ? -1.082  7.066   31.488  1.00 32.18 ? 160 CYS   C O   1 
ATOM   4747 C CB  . CYS   C 1 181 ? -2.008  3.642   30.517  1.00 24.10 ? 160 CYS   C CB  1 
ATOM   4748 S SG  . CYS   C 1 181 ? -1.600  1.910   30.934  1.00 28.80 ? 160 CYS   C SG  1 
ATOM   4749 N N   . ASP   C 1 182 ? -1.885  6.314   29.519  1.00 27.69 ? 161 ASP   C N   1 
ATOM   4750 C CA  . ASP   C 1 182 ? -2.116  7.665   29.003  1.00 23.43 ? 161 ASP   C CA  1 
ATOM   4751 C C   . ASP   C 1 182 ? -3.169  7.589   27.893  1.00 26.10 ? 161 ASP   C C   1 
ATOM   4752 O O   . ASP   C 1 182 ? -2.996  6.815   26.956  1.00 26.16 ? 161 ASP   C O   1 
ATOM   4753 C CB  . ASP   C 1 182 ? -0.825  8.290   28.485  1.00 26.29 ? 161 ASP   C CB  1 
ATOM   4754 C CG  . ASP   C 1 182 ? -0.872  9.765   28.094  1.00 35.74 ? 161 ASP   C CG  1 
ATOM   4755 O OD1 . ASP   C 1 182 ? -1.930  10.235  27.573  1.00 34.91 ? 161 ASP   C OD1 1 
ATOM   4756 O OD2 . ASP   C 1 182 ? 0.174   10.440  28.253  1.00 32.06 ? 161 ASP   C OD2 1 
ATOM   4757 N N   . ALA   C 1 183 ? -4.281  8.331   28.072  1.00 24.56 ? 162 ALA   C N   1 
ATOM   4758 C CA  . ALA   C 1 183 ? -5.425  8.232   27.187  1.00 23.18 ? 162 ALA   C CA  1 
ATOM   4759 C C   . ALA   C 1 183 ? -5.057  8.814   25.825  1.00 25.09 ? 162 ALA   C C   1 
ATOM   4760 O O   . ALA   C 1 183 ? -5.788  8.595   24.864  1.00 25.96 ? 162 ALA   C O   1 
ATOM   4761 C CB  . ALA   C 1 183 ? -6.615  8.971   27.801  1.00 23.47 ? 162 ALA   C CB  1 
ATOM   4762 N N   . MET   C 1 184 ? -3.988  9.613   25.763  1.00 24.55 ? 163 MET   C N   1 
ATOM   4763 C CA  . MET   C 1 184 ? -3.690  10.335  24.539  1.00 26.12 ? 163 MET   C CA  1 
ATOM   4764 C C   . MET   C 1 184 ? -2.596  9.671   23.709  1.00 26.50 ? 163 MET   C C   1 
ATOM   4765 O O   . MET   C 1 184 ? -2.137  10.293  22.774  1.00 28.85 ? 163 MET   C O   1 
ATOM   4766 C CB  . MET   C 1 184 ? -3.427  11.827  24.800  1.00 27.76 ? 163 MET   C CB  1 
ATOM   4767 C CG  . MET   C 1 184 ? -4.629  12.469  25.510  1.00 28.71 ? 163 MET   C CG  1 
ATOM   4768 S SD  . MET   C 1 184 ? -6.050  12.703  24.399  1.00 32.58 ? 163 MET   C SD  1 
ATOM   4769 C CE  . MET   C 1 184 ? -5.285  13.727  23.143  1.00 36.25 ? 163 MET   C CE  1 
ATOM   4770 N N   . VAL   C 1 185 ? -2.323  8.391   23.977  1.00 27.99 ? 164 VAL   C N   1 
ATOM   4771 C CA  . VAL   C 1 185 ? -1.229  7.618   23.310  1.00 33.49 ? 164 VAL   C CA  1 
ATOM   4772 C C   . VAL   C 1 185 ? -1.367  7.617   21.787  1.00 32.25 ? 164 VAL   C C   1 
ATOM   4773 O O   . VAL   C 1 185 ? -0.336  7.569   21.107  1.00 28.64 ? 164 VAL   C O   1 
ATOM   4774 C CB  . VAL   C 1 185 ? -1.211  6.163   23.824  1.00 33.78 ? 164 VAL   C CB  1 
ATOM   4775 C CG1 . VAL   C 1 185 ? -0.376  6.010   25.086  1.00 39.04 ? 164 VAL   C CG1 1 
ATOM   4776 C CG2 . VAL   C 1 185 ? -2.608  5.589   24.002  1.00 48.48 ? 164 VAL   C CG2 1 
ATOM   4777 N N   . ASP   C 1 186 ? -2.599  7.601   21.297  1.00 26.20 ? 165 ASP   C N   1 
ATOM   4778 C CA  . ASP   C 1 186 ? -2.789  7.507   19.848  1.00 29.48 ? 165 ASP   C CA  1 
ATOM   4779 C C   . ASP   C 1 186 ? -2.925  8.869   19.177  1.00 26.43 ? 165 ASP   C C   1 
ATOM   4780 O O   . ASP   C 1 186 ? -3.040  8.952   17.956  1.00 29.39 ? 165 ASP   C O   1 
ATOM   4781 C CB  . ASP   C 1 186 ? -3.910  6.537   19.474  1.00 27.13 ? 165 ASP   C CB  1 
ATOM   4782 C CG  . ASP   C 1 186 ? -3.628  5.088   19.832  1.00 31.83 ? 165 ASP   C CG  1 
ATOM   4783 O OD1 . ASP   C 1 186 ? -2.499  4.607   19.560  1.00 33.16 ? 165 ASP   C OD1 1 
ATOM   4784 O OD2 . ASP   C 1 186 ? -4.528  4.452   20.398  1.00 31.70 ? 165 ASP   C OD2 1 
ATOM   4785 N N   . GLN   C 1 187 ? -2.962  9.940   19.965  1.00 25.92 ? 166 GLN   C N   1 
ATOM   4786 C CA  . GLN   C 1 187 ? -2.977  11.270  19.401  1.00 25.17 ? 166 GLN   C CA  1 
ATOM   4787 C C   . GLN   C 1 187 ? -1.903  12.071  20.127  1.00 28.10 ? 166 GLN   C C   1 
ATOM   4788 O O   . GLN   C 1 187 ? -2.211  12.957  20.917  1.00 27.64 ? 166 GLN   C O   1 
ATOM   4789 C CB  . GLN   C 1 187 ? -4.335  11.933  19.652  1.00 26.44 ? 166 GLN   C CB  1 
ATOM   4790 C CG  . GLN   C 1 187 ? -5.452  11.141  18.986  1.00 34.91 ? 166 GLN   C CG  1 
ATOM   4791 C CD  . GLN   C 1 187 ? -6.592  10.885  19.943  1.00 39.91 ? 166 GLN   C CD  1 
ATOM   4792 O OE1 . GLN   C 1 187 ? -6.622  9.875   20.651  1.00 36.03 ? 166 GLN   C OE1 1 
ATOM   4793 N NE2 . GLN   C 1 187 ? -7.562  11.783  19.928  1.00 36.07 ? 166 GLN   C NE2 1 
ATOM   4794 N N   . PRO   C 1 188 ? -0.620  11.714  19.925  1.00 28.24 ? 167 PRO   C N   1 
ATOM   4795 C CA  . PRO   C 1 188 ? 0.433   12.162  20.851  1.00 29.54 ? 167 PRO   C CA  1 
ATOM   4796 C C   . PRO   C 1 188 ? 0.830   13.628  20.710  1.00 27.54 ? 167 PRO   C C   1 
ATOM   4797 O O   . PRO   C 1 188 ? 0.623   14.243  19.678  1.00 28.02 ? 167 PRO   C O   1 
ATOM   4798 C CB  . PRO   C 1 188 ? 1.579   11.186  20.501  1.00 28.16 ? 167 PRO   C CB  1 
ATOM   4799 C CG  . PRO   C 1 188 ? 1.437   10.997  19.029  1.00 28.17 ? 167 PRO   C CG  1 
ATOM   4800 C CD  . PRO   C 1 188 ? -0.116  10.850  18.836  1.00 24.62 ? 167 PRO   C CD  1 
ATOM   4801 N N   . CYS   C 1 189 ? 1.411   14.180  21.778  1.00 30.45 ? 168 CYS   C N   1 
ATOM   4802 C CA  . CYS   C 1 189 ? 2.008   15.494  21.716  1.00 33.10 ? 168 CYS   C CA  1 
ATOM   4803 C C   . CYS   C 1 189 ? 3.211   15.438  20.778  1.00 29.84 ? 168 CYS   C C   1 
ATOM   4804 O O   . CYS   C 1 189 ? 4.001   14.486  20.779  1.00 29.01 ? 168 CYS   C O   1 
ATOM   4805 C CB  . CYS   C 1 189 ? 2.414   15.976  23.104  1.00 37.95 ? 168 CYS   C CB  1 
ATOM   4806 S SG  . CYS   C 1 189 ? 1.051   16.695  24.065  1.00 54.23 ? 168 CYS   C SG  1 
ATOM   4807 N N   . MET   C 1 190 ? 3.315   16.480  19.966  1.00 31.10 ? 169 MET   C N   1 
ATOM   4808 C CA  . MET   C 1 190 ? 4.412   16.728  19.045  1.00 35.90 ? 169 MET   C CA  1 
ATOM   4809 C C   . MET   C 1 190 ? 5.750   16.655  19.802  1.00 32.86 ? 169 MET   C C   1 
ATOM   4810 O O   . MET   C 1 190 ? 5.856   17.171  20.918  1.00 30.52 ? 169 MET   C O   1 
ATOM   4811 C CB  . MET   C 1 190 ? 4.195   18.150  18.501  1.00 39.18 ? 169 MET   C CB  1 
ATOM   4812 C CG  . MET   C 1 190 ? 5.266   18.629  17.570  1.00 49.60 ? 169 MET   C CG  1 
ATOM   4813 S SD  . MET   C 1 190 ? 5.175   17.482  16.183  1.00 56.49 ? 169 MET   C SD  1 
ATOM   4814 C CE  . MET   C 1 190 ? 3.674   18.059  15.373  1.00 46.65 ? 169 MET   C CE  1 
ATOM   4815 N N   . ALA   C 1 191 ? 6.702   15.877  19.260  1.00 30.67 ? 170 ALA   C N   1 
ATOM   4816 C CA  . ALA   C 1 191 ? 8.075   15.753  19.757  1.00 32.49 ? 170 ALA   C CA  1 
ATOM   4817 C C   . ALA   C 1 191 ? 8.201   14.964  21.065  1.00 31.64 ? 170 ALA   C C   1 
ATOM   4818 O O   . ALA   C 1 191 ? 9.165   15.142  21.801  1.00 32.38 ? 170 ALA   C O   1 
ATOM   4819 C CB  . ALA   C 1 191 ? 8.738   17.123  19.877  1.00 32.76 ? 170 ALA   C CB  1 
ATOM   4820 N N   . PHE   C 1 192 ? 7.245   14.084  21.359  1.00 27.52 ? 171 PHE   C N   1 
ATOM   4821 C CA  . PHE   C 1 192 ? 7.290   13.273  22.552  1.00 25.84 ? 171 PHE   C CA  1 
ATOM   4822 C C   . PHE   C 1 192 ? 7.408   11.799  22.166  1.00 26.49 ? 171 PHE   C C   1 
ATOM   4823 O O   . PHE   C 1 192 ? 6.862   10.948  22.847  1.00 26.89 ? 171 PHE   C O   1 
ATOM   4824 C CB  . PHE   C 1 192 ? 6.075   13.534  23.433  1.00 27.24 ? 171 PHE   C CB  1 
ATOM   4825 C CG  . PHE   C 1 192 ? 6.178   14.770  24.334  1.00 29.48 ? 171 PHE   C CG  1 
ATOM   4826 C CD1 . PHE   C 1 192 ? 5.948   16.033  23.810  1.00 29.88 ? 171 PHE   C CD1 1 
ATOM   4827 C CD2 . PHE   C 1 192 ? 6.434   14.641  25.703  1.00 31.75 ? 171 PHE   C CD2 1 
ATOM   4828 C CE1 . PHE   C 1 192 ? 6.036   17.155  24.639  1.00 33.39 ? 171 PHE   C CE1 1 
ATOM   4829 C CE2 . PHE   C 1 192 ? 6.510   15.756  26.531  1.00 33.34 ? 171 PHE   C CE2 1 
ATOM   4830 C CZ  . PHE   C 1 192 ? 6.305   17.013  25.988  1.00 32.25 ? 171 PHE   C CZ  1 
ATOM   4831 N N   . SER   C 1 193 ? 8.192   11.509  21.122  1.00 24.75 ? 172 SER   C N   1 
ATOM   4832 C CA  . SER   C 1 193 ? 8.373   10.130  20.657  1.00 28.98 ? 172 SER   C CA  1 
ATOM   4833 C C   . SER   C 1 193 ? 8.706   9.169   21.780  1.00 28.17 ? 172 SER   C C   1 
ATOM   4834 O O   . SER   C 1 193 ? 8.021   8.161   21.945  1.00 28.01 ? 172 SER   C O   1 
ATOM   4835 C CB  . SER   C 1 193 ? 9.483   10.007  19.590  1.00 29.70 ? 172 SER   C CB  1 
ATOM   4836 O OG  . SER   C 1 193 ? 8.961   10.413  18.346  1.00 40.08 ? 172 SER   C OG  1 
ATOM   4837 N N   . LEU   C 1 194 ? 9.812   9.421   22.512  1.00 28.51 ? 173 LEU   C N   1 
ATOM   4838 C CA  . LEU   C 1 194 ? 10.241  8.434   23.494  1.00 25.43 ? 173 LEU   C CA  1 
ATOM   4839 C C   . LEU   C 1 194 ? 9.188   8.196   24.562  1.00 26.69 ? 173 LEU   C C   1 
ATOM   4840 O O   . LEU   C 1 194 ? 9.020   7.077   25.043  1.00 25.71 ? 173 LEU   C O   1 
ATOM   4841 C CB  . LEU   C 1 194 ? 11.588  8.752   24.180  1.00 24.58 ? 173 LEU   C CB  1 
ATOM   4842 C CG  . LEU   C 1 194 ? 12.831  8.358   23.383  1.00 31.85 ? 173 LEU   C CG  1 
ATOM   4843 C CD1 . LEU   C 1 194 ? 14.064  8.809   24.217  1.00 30.06 ? 173 LEU   C CD1 1 
ATOM   4844 C CD2 . LEU   C 1 194 ? 12.861  6.854   23.162  1.00 25.87 ? 173 LEU   C CD2 1 
ATOM   4845 N N   . TYR   C 1 195 ? 8.609   9.290   25.069  1.00 25.64 ? 174 TYR   C N   1 
ATOM   4846 C CA  . TYR   C 1 195 ? 7.557   9.178   26.048  1.00 24.56 ? 174 TYR   C CA  1 
ATOM   4847 C C   . TYR   C 1 195 ? 6.439   8.282   25.513  1.00 21.08 ? 174 TYR   C C   1 
ATOM   4848 O O   . TYR   C 1 195 ? 5.940   7.440   26.267  1.00 25.04 ? 174 TYR   C O   1 
ATOM   4849 C CB  . TYR   C 1 195 ? 7.027   10.577  26.408  1.00 26.22 ? 174 TYR   C CB  1 
ATOM   4850 C CG  . TYR   C 1 195 ? 5.824   10.458  27.320  1.00 23.67 ? 174 TYR   C CG  1 
ATOM   4851 C CD1 . TYR   C 1 195 ? 5.942   10.176  28.683  1.00 25.13 ? 174 TYR   C CD1 1 
ATOM   4852 C CD2 . TYR   C 1 195 ? 4.551   10.635  26.785  1.00 24.92 ? 174 TYR   C CD2 1 
ATOM   4853 C CE1 . TYR   C 1 195 ? 4.820   10.040  29.482  1.00 30.39 ? 174 TYR   C CE1 1 
ATOM   4854 C CE2 . TYR   C 1 195 ? 3.422   10.560  27.585  1.00 28.11 ? 174 TYR   C CE2 1 
ATOM   4855 C CZ  . TYR   C 1 195 ? 3.557   10.238  28.923  1.00 28.79 ? 174 TYR   C CZ  1 
ATOM   4856 O OH  . TYR   C 1 195 ? 2.432   10.126  29.700  1.00 28.30 ? 174 TYR   C OH  1 
ATOM   4857 N N   . ASN   C 1 196 ? 6.006   8.548   24.272  1.00 22.31 ? 175 ASN   C N   1 
ATOM   4858 C CA  A ASN   C 1 196 ? 4.867   7.839   23.686  0.70 23.77 ? 175 ASN   C CA  1 
ATOM   4859 C CA  B ASN   C 1 196 ? 4.882   7.838   23.675  0.30 22.44 ? 175 ASN   C CA  1 
ATOM   4860 C C   . ASN   C 1 196 ? 5.242   6.367   23.502  1.00 22.67 ? 175 ASN   C C   1 
ATOM   4861 O O   . ASN   C 1 196 ? 4.448   5.478   23.785  1.00 22.57 ? 175 ASN   C O   1 
ATOM   4862 C CB  A ASN   C 1 196 ? 4.418   8.530   22.403  0.70 26.38 ? 175 ASN   C CB  1 
ATOM   4863 C CB  B ASN   C 1 196 ? 4.447   8.535   22.395  0.30 22.37 ? 175 ASN   C CB  1 
ATOM   4864 C CG  A ASN   C 1 196 ? 3.145   7.944   21.834  0.70 29.27 ? 175 ASN   C CG  1 
ATOM   4865 C CG  B ASN   C 1 196 ? 3.543   9.692   22.729  0.30 22.32 ? 175 ASN   C CG  1 
ATOM   4866 O OD1 A ASN   C 1 196 ? 3.151   7.413   20.715  0.70 36.07 ? 175 ASN   C OD1 1 
ATOM   4867 O OD1 B ASN   C 1 196 ? 2.392   9.464   23.119  0.30 24.44 ? 175 ASN   C OD1 1 
ATOM   4868 N ND2 A ASN   C 1 196 ? 2.057   8.022   22.581  0.70 27.38 ? 175 ASN   C ND2 1 
ATOM   4869 N ND2 B ASN   C 1 196 ? 4.057   10.913  22.648  0.30 21.08 ? 175 ASN   C ND2 1 
ATOM   4870 N N   . MET   C 1 197 ? 6.502   6.122   23.104  1.00 22.72 ? 176 MET   C N   1 
ATOM   4871 C CA  . MET   C 1 197 ? 6.993   4.738   22.993  1.00 23.91 ? 176 MET   C CA  1 
ATOM   4872 C C   . MET   C 1 197 ? 6.878   4.008   24.326  1.00 23.73 ? 176 MET   C C   1 
ATOM   4873 O O   . MET   C 1 197 ? 6.425   2.866   24.382  1.00 23.72 ? 176 MET   C O   1 
ATOM   4874 C CB  . MET   C 1 197 ? 8.441   4.731   22.489  1.00 24.08 ? 176 MET   C CB  1 
ATOM   4875 C CG  . MET   C 1 197 ? 8.534   5.113   21.016  1.00 21.36 ? 176 MET   C CG  1 
ATOM   4876 S SD  . MET   C 1 197 ? 10.243  5.457   20.543  1.00 25.43 ? 176 MET   C SD  1 
ATOM   4877 C CE  . MET   C 1 197 ? 10.844  3.775   20.745  1.00 27.85 ? 176 MET   C CE  1 
ATOM   4878 N N   . GLY   C 1 198 ? 7.347   4.655   25.408  1.00 22.95 ? 177 GLY   C N   1 
ATOM   4879 C CA  . GLY   C 1 198 ? 7.286   4.083   26.742  1.00 22.95 ? 177 GLY   C CA  1 
ATOM   4880 C C   . GLY   C 1 198 ? 5.846   3.774   27.148  1.00 24.91 ? 177 GLY   C C   1 
ATOM   4881 O O   . GLY   C 1 198 ? 5.578   2.758   27.770  1.00 21.59 ? 177 GLY   C O   1 
ATOM   4882 N N   . LYS   C 1 199 ? 4.914   4.705   26.866  1.00 21.74 ? 178 LYS   C N   1 
ATOM   4883 C CA  . LYS   C 1 199 ? 3.544   4.445   27.304  1.00 21.43 ? 178 LYS   C CA  1 
ATOM   4884 C C   . LYS   C 1 199 ? 2.866   3.377   26.444  1.00 20.93 ? 178 LYS   C C   1 
ATOM   4885 O O   . LYS   C 1 199 ? 2.058   2.605   26.959  1.00 19.96 ? 178 LYS   C O   1 
ATOM   4886 C CB  . LYS   C 1 199 ? 2.763   5.766   27.377  1.00 22.70 ? 178 LYS   C CB  1 
ATOM   4887 C CG  . LYS   C 1 199 ? 3.305   6.655   28.542  1.00 22.73 ? 178 LYS   C CG  1 
ATOM   4888 C CD  . LYS   C 1 199 ? 2.936   6.096   29.914  1.00 25.09 ? 178 LYS   C CD  1 
ATOM   4889 C CE  . LYS   C 1 199 ? 2.960   7.119   31.016  1.00 30.60 ? 178 LYS   C CE  1 
ATOM   4890 N NZ  . LYS   C 1 199 ? 2.891   6.493   32.336  1.00 30.64 ? 178 LYS   C NZ  1 
ATOM   4891 N N   . HIS   C 1 200 ? 3.243   3.288   25.175  1.00 21.17 ? 179 HIS   C N   1 
ATOM   4892 C CA  . HIS   C 1 200 ? 2.724   2.183   24.374  1.00 21.74 ? 179 HIS   C CA  1 
ATOM   4893 C C   . HIS   C 1 200 ? 3.268   0.867   24.927  1.00 21.84 ? 179 HIS   C C   1 
ATOM   4894 O O   . HIS   C 1 200 ? 2.529   -0.138  24.972  1.00 21.22 ? 179 HIS   C O   1 
ATOM   4895 C CB  . HIS   C 1 200 ? 3.108   2.385   22.907  1.00 21.45 ? 179 HIS   C CB  1 
ATOM   4896 C CG  . HIS   C 1 200 ? 2.094   3.120   22.078  1.00 24.97 ? 179 HIS   C CG  1 
ATOM   4897 N ND1 . HIS   C 1 200 ? 1.056   2.510   21.394  1.00 27.85 ? 179 HIS   C ND1 1 
ATOM   4898 C CD2 . HIS   C 1 200 ? 1.970   4.423   21.848  1.00 25.80 ? 179 HIS   C CD2 1 
ATOM   4899 C CE1 . HIS   C 1 200 ? 0.334   3.422   20.755  1.00 25.18 ? 179 HIS   C CE1 1 
ATOM   4900 N NE2 . HIS   C 1 200 ? 0.878   4.603   21.017  1.00 27.51 ? 179 HIS   C NE2 1 
ATOM   4901 N N   . ALA   C 1 201 ? 4.566   0.866   25.289  1.00 21.76 ? 180 ALA   C N   1 
ATOM   4902 C CA  . ALA   C 1 201 ? 5.178   -0.351  25.852  1.00 22.66 ? 180 ALA   C CA  1 
ATOM   4903 C C   . ALA   C 1 201 ? 4.421   -0.828  27.083  1.00 22.19 ? 180 ALA   C C   1 
ATOM   4904 O O   . ALA   C 1 201 ? 4.236   -2.021  27.306  1.00 22.28 ? 180 ALA   C O   1 
ATOM   4905 C CB  . ALA   C 1 201 ? 6.670   -0.153  26.139  1.00 23.72 ? 180 ALA   C CB  1 
ATOM   4906 N N   . LEU   C 1 202 ? 4.009   0.129   27.928  1.00 19.47 ? 181 LEU   C N   1 
ATOM   4907 C CA  . LEU   C 1 202 ? 3.269   -0.138  29.155  1.00 23.68 ? 181 LEU   C CA  1 
ATOM   4908 C C   . LEU   C 1 202 ? 1.907   -0.776  28.836  1.00 23.35 ? 181 LEU   C C   1 
ATOM   4909 O O   . LEU   C 1 202 ? 1.472   -1.676  29.551  1.00 24.98 ? 181 LEU   C O   1 
ATOM   4910 C CB  . LEU   C 1 202 ? 3.168   1.169   29.974  1.00 23.80 ? 181 LEU   C CB  1 
ATOM   4911 C CG  . LEU   C 1 202 ? 2.570   1.022   31.382  1.00 28.85 ? 181 LEU   C CG  1 
ATOM   4912 C CD1 . LEU   C 1 202 ? 3.382   0.061   32.284  1.00 26.19 ? 181 LEU   C CD1 1 
ATOM   4913 C CD2 . LEU   C 1 202 ? 2.397   2.392   32.067  1.00 26.32 ? 181 LEU   C CD2 1 
ATOM   4914 N N   . VAL   C 1 203 ? 1.209   -0.293  27.785  1.00 24.17 ? 182 VAL   C N   1 
ATOM   4915 C CA  . VAL   C 1 203 ? 0.014   -1.004  27.301  1.00 21.28 ? 182 VAL   C CA  1 
ATOM   4916 C C   . VAL   C 1 203 ? 0.339   -2.468  26.990  1.00 20.01 ? 182 VAL   C C   1 
ATOM   4917 O O   . VAL   C 1 203 ? -0.405  -3.357  27.406  1.00 22.39 ? 182 VAL   C O   1 
ATOM   4918 C CB  . VAL   C 1 203 ? -0.653  -0.314  26.094  1.00 23.55 ? 182 VAL   C CB  1 
ATOM   4919 C CG1 . VAL   C 1 203 ? -1.785  -1.160  25.467  1.00 22.26 ? 182 VAL   C CG1 1 
ATOM   4920 C CG2 . VAL   C 1 203 ? -1.204  1.026   26.562  1.00 25.29 ? 182 VAL   C CG2 1 
ATOM   4921 N N   . GLY   C 1 204 ? 1.438   -2.687  26.257  1.00 23.03 ? 183 GLY   C N   1 
ATOM   4922 C CA  . GLY   C 1 204 ? 1.877   -4.039  25.893  1.00 23.75 ? 183 GLY   C CA  1 
ATOM   4923 C C   . GLY   C 1 204 ? 2.126   -4.887  27.143  1.00 23.27 ? 183 GLY   C C   1 
ATOM   4924 O O   . GLY   C 1 204 ? 1.711   -6.030  27.210  1.00 23.38 ? 183 GLY   C O   1 
ATOM   4925 N N   . LEU   C 1 205 ? 2.798   -4.301  28.149  1.00 23.45 ? 184 LEU   C N   1 
ATOM   4926 C CA  . LEU   C 1 205 ? 3.058   -4.986  29.412  1.00 25.78 ? 184 LEU   C CA  1 
ATOM   4927 C C   . LEU   C 1 205 ? 1.754   -5.320  30.132  1.00 24.06 ? 184 LEU   C C   1 
ATOM   4928 O O   . LEU   C 1 205 ? 1.580   -6.424  30.660  1.00 23.12 ? 184 LEU   C O   1 
ATOM   4929 C CB  . LEU   C 1 205 ? 3.982   -4.159  30.316  1.00 23.65 ? 184 LEU   C CB  1 
ATOM   4930 C CG  . LEU   C 1 205 ? 4.109   -4.739  31.720  1.00 25.11 ? 184 LEU   C CG  1 
ATOM   4931 C CD1 . LEU   C 1 205 ? 4.806   -6.124  31.742  1.00 26.51 ? 184 LEU   C CD1 1 
ATOM   4932 C CD2 . LEU   C 1 205 ? 4.872   -3.692  32.532  1.00 25.88 ? 184 LEU   C CD2 1 
ATOM   4933 N N   . THR   C 1 206 ? 0.819   -4.359  30.163  1.00 22.20 ? 185 THR   C N   1 
ATOM   4934 C CA  . THR   C 1 206 ? -0.479  -4.569  30.788  1.00 21.18 ? 185 THR   C CA  1 
ATOM   4935 C C   . THR   C 1 206 ? -1.140  -5.819  30.207  1.00 21.26 ? 185 THR   C C   1 
ATOM   4936 O O   . THR   C 1 206 ? -1.575  -6.689  30.944  1.00 23.69 ? 185 THR   C O   1 
ATOM   4937 C CB  . THR   C 1 206 ? -1.396  -3.338  30.697  1.00 21.23 ? 185 THR   C CB  1 
ATOM   4938 O OG1 . THR   C 1 206 ? -0.652  -2.252  31.246  1.00 23.55 ? 185 THR   C OG1 1 
ATOM   4939 C CG2 . THR   C 1 206 ? -2.639  -3.503  31.547  1.00 23.17 ? 185 THR   C CG2 1 
ATOM   4940 N N   . GLN   C 1 207 ? -1.189  -5.917  28.867  1.00 21.67 ? 186 GLN   C N   1 
ATOM   4941 C CA  . GLN   C 1 207 ? -1.850  -7.039  28.227  1.00 20.10 ? 186 GLN   C CA  1 
ATOM   4942 C C   . GLN   C 1 207 ? -1.090  -8.336  28.459  1.00 20.30 ? 186 GLN   C C   1 
ATOM   4943 O O   . GLN   C 1 207 ? -1.728  -9.355  28.742  1.00 22.85 ? 186 GLN   C O   1 
ATOM   4944 C CB  . GLN   C 1 207 ? -1.896  -6.788  26.723  1.00 22.58 ? 186 GLN   C CB  1 
ATOM   4945 C CG  . GLN   C 1 207 ? -2.797  -5.587  26.475  1.00 25.73 ? 186 GLN   C CG  1 
ATOM   4946 C CD  . GLN   C 1 207 ? -2.936  -5.140  25.039  1.00 28.58 ? 186 GLN   C CD  1 
ATOM   4947 O OE1 . GLN   C 1 207 ? -3.967  -4.553  24.708  1.00 35.99 ? 186 GLN   C OE1 1 
ATOM   4948 N NE2 . GLN   C 1 207 ? -1.955  -5.408  24.189  1.00 30.79 ? 186 GLN   C NE2 1 
ATOM   4949 N N   . SER   C 1 208 ? 0.230   -8.294  28.207  1.00 22.46 ? 187 SER   C N   1 
ATOM   4950 C CA  . SER   C 1 208 ? 1.050   -9.513  28.277  1.00 23.90 ? 187 SER   C CA  1 
ATOM   4951 C C   . SER   C 1 208 ? 1.048   -10.112 29.689  1.00 26.19 ? 187 SER   C C   1 
ATOM   4952 O O   . SER   C 1 208 ? 1.009   -11.334 29.841  1.00 25.63 ? 187 SER   C O   1 
ATOM   4953 C CB  . SER   C 1 208 ? 2.468   -9.344  27.761  1.00 25.81 ? 187 SER   C CB  1 
ATOM   4954 O OG  . SER   C 1 208 ? 2.578   -9.176  26.340  1.00 26.02 ? 187 SER   C OG  1 
ATOM   4955 N N   . ALA   C 1 209 ? 1.153   -9.254  30.709  1.00 25.28 ? 188 ALA   C N   1 
ATOM   4956 C CA  . ALA   C 1 209 ? 1.186   -9.690  32.104  1.00 26.45 ? 188 ALA   C CA  1 
ATOM   4957 C C   . ALA   C 1 209 ? -0.203  -10.124 32.561  1.00 29.65 ? 188 ALA   C C   1 
ATOM   4958 O O   . ALA   C 1 209 ? -0.330  -11.096 33.331  1.00 27.41 ? 188 ALA   C O   1 
ATOM   4959 C CB  . ALA   C 1 209 ? 1.732   -8.578  32.967  1.00 26.19 ? 188 ALA   C CB  1 
ATOM   4960 N N   . ALA   C 1 210 ? -1.255  -9.459  32.029  1.00 24.47 ? 189 ALA   C N   1 
ATOM   4961 C CA  . ALA   C 1 210 ? -2.591  -9.914  32.345  1.00 23.62 ? 189 ALA   C CA  1 
ATOM   4962 C C   . ALA   C 1 210 ? -2.726  -11.354 31.873  1.00 27.16 ? 189 ALA   C C   1 
ATOM   4963 O O   . ALA   C 1 210 ? -3.208  -12.198 32.625  1.00 24.69 ? 189 ALA   C O   1 
ATOM   4964 C CB  . ALA   C 1 210 ? -3.681  -9.036  31.742  1.00 25.54 ? 189 ALA   C CB  1 
ATOM   4965 N N   . LEU   C 1 211 ? -2.285  -11.631 30.633  1.00 24.10 ? 190 LEU   C N   1 
ATOM   4966 C CA  . LEU   C 1 211 ? -2.455  -12.988 30.143  1.00 27.16 ? 190 LEU   C CA  1 
ATOM   4967 C C   . LEU   C 1 211 ? -1.639  -13.990 30.977  1.00 29.56 ? 190 LEU   C C   1 
ATOM   4968 O O   . LEU   C 1 211 ? -2.101  -15.096 31.301  1.00 31.52 ? 190 LEU   C O   1 
ATOM   4969 C CB  . LEU   C 1 211 ? -1.946  -12.965 28.700  1.00 28.60 ? 190 LEU   C CB  1 
ATOM   4970 C CG  . LEU   C 1 211 ? -2.016  -14.301 27.941  1.00 30.56 ? 190 LEU   C CG  1 
ATOM   4971 C CD1 . LEU   C 1 211 ? -3.480  -14.642 27.631  1.00 31.20 ? 190 LEU   C CD1 1 
ATOM   4972 C CD2 . LEU   C 1 211 ? -1.289  -14.079 26.616  1.00 32.90 ? 190 LEU   C CD2 1 
ATOM   4973 N N   . GLU   C 1 212 ? -0.387  -13.630 31.239  1.00 26.91 ? 191 GLU   C N   1 
ATOM   4974 C CA  . GLU   C 1 212 ? 0.563   -14.585 31.803  1.00 31.60 ? 191 GLU   C CA  1 
ATOM   4975 C C   . GLU   C 1 212 ? 0.294   -14.855 33.281  1.00 32.62 ? 191 GLU   C C   1 
ATOM   4976 O O   . GLU   C 1 212 ? 0.588   -15.957 33.768  1.00 30.66 ? 191 GLU   C O   1 
ATOM   4977 C CB  . GLU   C 1 212 ? 1.975   -14.052 31.618  1.00 32.50 ? 191 GLU   C CB  1 
ATOM   4978 C CG  . GLU   C 1 212 ? 3.046   -15.020 32.115  1.00 38.09 ? 191 GLU   C CG  1 
ATOM   4979 C CD  . GLU   C 1 212 ? 4.405   -14.596 31.596  1.00 37.45 ? 191 GLU   C CD  1 
ATOM   4980 O OE1 . GLU   C 1 212 ? 5.378   -15.248 32.040  1.00 36.84 ? 191 GLU   C OE1 1 
ATOM   4981 O OE2 . GLU   C 1 212 ? 4.515   -13.670 30.739  1.00 36.45 ? 191 GLU   C OE2 1 
ATOM   4982 N N   . LEU   C 1 213 ? -0.250  -13.856 33.984  1.00 27.46 ? 192 LEU   C N   1 
ATOM   4983 C CA  . LEU   C 1 213 ? -0.432  -13.962 35.435  1.00 27.84 ? 192 LEU   C CA  1 
ATOM   4984 C C   . LEU   C 1 213 ? -1.848  -14.344 35.822  1.00 31.87 ? 192 LEU   C C   1 
ATOM   4985 O O   . LEU   C 1 213 ? -2.106  -14.587 37.010  1.00 32.28 ? 192 LEU   C O   1 
ATOM   4986 C CB  . LEU   C 1 213 ? -0.040  -12.651 36.102  1.00 27.94 ? 192 LEU   C CB  1 
ATOM   4987 C CG  . LEU   C 1 213 ? 1.401   -12.214 35.822  1.00 27.26 ? 192 LEU   C CG  1 
ATOM   4988 C CD1 . LEU   C 1 213 ? 1.727   -10.964 36.639  1.00 29.98 ? 192 LEU   C CD1 1 
ATOM   4989 C CD2 . LEU   C 1 213 ? 2.382   -13.351 36.199  1.00 30.85 ? 192 LEU   C CD2 1 
ATOM   4990 N N   . ALA   C 1 214 ? -2.757  -14.413 34.846  1.00 29.08 ? 193 ALA   C N   1 
ATOM   4991 C CA  . ALA   C 1 214 ? -4.128  -14.785 35.173  1.00 30.83 ? 193 ALA   C CA  1 
ATOM   4992 C C   . ALA   C 1 214 ? -4.136  -16.150 35.865  1.00 34.08 ? 193 ALA   C C   1 
ATOM   4993 O O   . ALA   C 1 214 ? -4.916  -16.360 36.802  1.00 33.97 ? 193 ALA   C O   1 
ATOM   4994 C CB  . ALA   C 1 214 ? -5.004  -14.776 33.938  1.00 30.13 ? 193 ALA   C CB  1 
ATOM   4995 N N   . PRO   C 1 215 ? -3.319  -17.127 35.397  1.00 39.13 ? 194 PRO   C N   1 
ATOM   4996 C CA  . PRO   C 1 215 ? -3.183  -18.418 36.081  1.00 40.91 ? 194 PRO   C CA  1 
ATOM   4997 C C   . PRO   C 1 215 ? -2.915  -18.345 37.581  1.00 45.97 ? 194 PRO   C C   1 
ATOM   4998 O O   . PRO   C 1 215 ? -3.376  -19.208 38.315  1.00 53.06 ? 194 PRO   C O   1 
ATOM   4999 C CB  . PRO   C 1 215 ? -2.042  -19.097 35.302  1.00 43.02 ? 194 PRO   C CB  1 
ATOM   5000 C CG  . PRO   C 1 215 ? -2.239  -18.573 33.891  1.00 43.41 ? 194 PRO   C CG  1 
ATOM   5001 C CD  . PRO   C 1 215 ? -2.538  -17.097 34.140  1.00 37.24 ? 194 PRO   C CD  1 
ATOM   5002 N N   . TYR   C 1 216 ? -2.228  -17.292 38.030  1.00 45.29 ? 195 TYR   C N   1 
ATOM   5003 C CA  . TYR   C 1 216 ? -1.892  -17.131 39.435  1.00 40.02 ? 195 TYR   C CA  1 
ATOM   5004 C C   . TYR   C 1 216 ? -2.939  -16.284 40.149  1.00 43.09 ? 195 TYR   C C   1 
ATOM   5005 O O   . TYR   C 1 216 ? -2.749  -15.934 41.305  1.00 48.38 ? 195 TYR   C O   1 
ATOM   5006 C CB  . TYR   C 1 216 ? -0.518  -16.463 39.526  1.00 40.31 ? 195 TYR   C CB  1 
ATOM   5007 C CG  . TYR   C 1 216 ? 0.539   -17.272 38.800  0.70 44.02 ? 195 TYR   C CG  1 
ATOM   5008 C CD1 . TYR   C 1 216 ? 0.931   -18.523 39.268  0.70 49.36 ? 195 TYR   C CD1 1 
ATOM   5009 C CD2 . TYR   C 1 216 ? 1.136   -16.789 37.647  0.70 45.94 ? 195 TYR   C CD2 1 
ATOM   5010 C CE1 . TYR   C 1 216 ? 1.884   -19.275 38.601  0.70 52.65 ? 195 TYR   C CE1 1 
ATOM   5011 C CE2 . TYR   C 1 216 ? 2.091   -17.530 36.971  0.70 47.94 ? 195 TYR   C CE2 1 
ATOM   5012 C CZ  . TYR   C 1 216 ? 2.467   -18.771 37.452  0.70 53.76 ? 195 TYR   C CZ  1 
ATOM   5013 O OH  . TYR   C 1 216 ? 3.410   -19.493 36.790  0.70 56.65 ? 195 TYR   C OH  1 
ATOM   5014 N N   . GLY   C 1 217 ? -4.017  -15.914 39.449  1.00 36.75 ? 196 GLY   C N   1 
ATOM   5015 C CA  . GLY   C 1 217 ? -5.068  -15.119 40.063  1.00 37.77 ? 196 GLY   C CA  1 
ATOM   5016 C C   . GLY   C 1 217 ? -4.610  -13.674 40.262  1.00 37.84 ? 196 GLY   C C   1 
ATOM   5017 O O   . GLY   C 1 217 ? -5.242  -12.910 40.996  1.00 40.98 ? 196 GLY   C O   1 
ATOM   5018 N N   . ILE   C 1 218 ? -3.519  -13.294 39.582  1.00 30.51 ? 197 ILE   C N   1 
ATOM   5019 C CA  . ILE   C 1 218 ? -3.084  -11.905 39.634  1.00 29.21 ? 197 ILE   C CA  1 
ATOM   5020 C C   . ILE   C 1 218 ? -3.739  -11.168 38.460  1.00 28.73 ? 197 ILE   C C   1 
ATOM   5021 O O   . ILE   C 1 218 ? -3.471  -11.523 37.307  1.00 31.85 ? 197 ILE   C O   1 
ATOM   5022 C CB  . ILE   C 1 218 ? -1.554  -11.766 39.575  1.00 26.88 ? 197 ILE   C CB  1 
ATOM   5023 C CG1 . ILE   C 1 218 ? -0.822  -12.543 40.703  1.00 29.19 ? 197 ILE   C CG1 1 
ATOM   5024 C CG2 . ILE   C 1 218 ? -1.147  -10.299 39.627  1.00 27.48 ? 197 ILE   C CG2 1 
ATOM   5025 C CD1 . ILE   C 1 218 ? 0.673   -12.645 40.452  1.00 29.77 ? 197 ILE   C CD1 1 
ATOM   5026 N N   . ARG   C 1 219 ? -4.484  -10.106 38.784  1.00 28.03 ? 198 ARG   C N   1 
ATOM   5027 C CA  . ARG   C 1 219 ? -5.099  -9.260  37.761  1.00 27.81 ? 198 ARG   C CA  1 
ATOM   5028 C C   . ARG   C 1 219 ? -4.140  -8.130  37.394  1.00 27.06 ? 198 ARG   C C   1 
ATOM   5029 O O   . ARG   C 1 219 ? -3.386  -7.610  38.235  1.00 28.18 ? 198 ARG   C O   1 
ATOM   5030 C CB  . ARG   C 1 219 ? -6.483  -8.745  38.157  1.00 24.46 ? 198 ARG   C CB  1 
ATOM   5031 C CG  . ARG   C 1 219 ? -7.519  -9.818  38.433  1.00 26.51 ? 198 ARG   C CG  1 
ATOM   5032 C CD  . ARG   C 1 219 ? -8.844  -9.311  38.958  1.00 31.60 ? 198 ARG   C CD  1 
ATOM   5033 N NE  . ARG   C 1 219 ? -8.704  -8.523  40.186  1.00 30.45 ? 198 ARG   C NE  1 
ATOM   5034 C CZ  . ARG   C 1 219 ? -8.798  -7.210  40.242  1.00 36.09 ? 198 ARG   C CZ  1 
ATOM   5035 N NH1 . ARG   C 1 219 ? -8.958  -6.529  39.106  1.00 31.45 ? 198 ARG   C NH1 1 
ATOM   5036 N NH2 . ARG   C 1 219 ? -8.691  -6.578  41.416  1.00 32.13 ? 198 ARG   C NH2 1 
ATOM   5037 N N   . VAL   C 1 220 ? -4.195  -7.693  36.115  1.00 25.63 ? 199 VAL   C N   1 
ATOM   5038 C CA  . VAL   C 1 220 ? -3.292  -6.646  35.653  1.00 22.80 ? 199 VAL   C CA  1 
ATOM   5039 C C   . VAL   C 1 220 ? -4.097  -5.684  34.771  1.00 25.08 ? 199 VAL   C C   1 
ATOM   5040 O O   . VAL   C 1 220 ? -4.518  -6.081  33.678  1.00 23.90 ? 199 VAL   C O   1 
ATOM   5041 C CB  . VAL   C 1 220 ? -2.100  -7.219  34.868  1.00 25.20 ? 199 VAL   C CB  1 
ATOM   5042 C CG1 . VAL   C 1 220 ? -1.100  -6.143  34.523  1.00 22.09 ? 199 VAL   C CG1 1 
ATOM   5043 C CG2 . VAL   C 1 220 ? -1.350  -8.349  35.620  1.00 27.30 ? 199 VAL   C CG2 1 
ATOM   5044 N N   . ASN   C 1 221 ? -4.185  -4.409  35.205  1.00 23.74 ? 200 ASN   C N   1 
ATOM   5045 C CA  . ASN   C 1 221 ? -5.058  -3.441  34.545  1.00 23.54 ? 200 ASN   C CA  1 
ATOM   5046 C C   . ASN   C 1 221 ? -4.386  -2.084  34.443  1.00 23.57 ? 200 ASN   C C   1 
ATOM   5047 O O   . ASN   C 1 221 ? -3.290  -1.864  34.954  1.00 24.91 ? 200 ASN   C O   1 
ATOM   5048 C CB  . ASN   C 1 221 ? -6.410  -3.282  35.243  1.00 24.20 ? 200 ASN   C CB  1 
ATOM   5049 C CG  . ASN   C 1 221 ? -7.209  -4.566  35.211  1.00 28.03 ? 200 ASN   C CG  1 
ATOM   5050 O OD1 . ASN   C 1 221 ? -7.617  -5.023  34.128  1.00 25.11 ? 200 ASN   C OD1 1 
ATOM   5051 N ND2 . ASN   C 1 221 ? -7.389  -5.207  36.364  1.00 24.27 ? 200 ASN   C ND2 1 
ATOM   5052 N N   . GLY   C 1 222 ? -5.044  -1.163  33.705  1.00 23.28 ? 201 GLY   C N   1 
ATOM   5053 C CA  . GLY   C 1 222 ? -4.475  0.160   33.533  1.00 24.55 ? 201 GLY   C CA  1 
ATOM   5054 C C   . GLY   C 1 222 ? -5.500  1.270   33.809  1.00 20.62 ? 201 GLY   C C   1 
ATOM   5055 O O   . GLY   C 1 222 ? -6.693  1.074   33.683  1.00 23.99 ? 201 GLY   C O   1 
ATOM   5056 N N   . VAL   C 1 223 ? -4.978  2.453   34.143  1.00 23.99 ? 202 VAL   C N   1 
ATOM   5057 C CA  . VAL   C 1 223 ? -5.785  3.649   34.251  1.00 23.46 ? 202 VAL   C CA  1 
ATOM   5058 C C   . VAL   C 1 223 ? -5.064  4.684   33.395  1.00 21.29 ? 202 VAL   C C   1 
ATOM   5059 O O   . VAL   C 1 223 ? -3.853  4.908   33.541  1.00 23.96 ? 202 VAL   C O   1 
ATOM   5060 C CB  . VAL   C 1 223 ? -5.924  4.134   35.716  1.00 22.59 ? 202 VAL   C CB  1 
ATOM   5061 C CG1 . VAL   C 1 223 ? -6.561  5.527   35.766  1.00 25.14 ? 202 VAL   C CG1 1 
ATOM   5062 C CG2 . VAL   C 1 223 ? -6.727  3.158   36.557  1.00 22.23 ? 202 VAL   C CG2 1 
ATOM   5063 N N   . ALA   C 1 224 ? -5.815  5.335   32.498  1.00 21.69 ? 203 ALA   C N   1 
ATOM   5064 C CA  . ALA   C 1 224 ? -5.250  6.213   31.496  1.00 21.64 ? 203 ALA   C CA  1 
ATOM   5065 C C   . ALA   C 1 224 ? -5.822  7.615   31.672  1.00 25.52 ? 203 ALA   C C   1 
ATOM   5066 O O   . ALA   C 1 224 ? -6.909  7.904   31.172  1.00 23.87 ? 203 ALA   C O   1 
ATOM   5067 C CB  . ALA   C 1 224 ? -5.598  5.636   30.106  1.00 24.30 ? 203 ALA   C CB  1 
ATOM   5068 N N   . PRO   C 1 225 ? -5.097  8.529   32.352  1.00 24.89 ? 204 PRO   C N   1 
ATOM   5069 C CA  . PRO   C 1 225 ? -5.531  9.930   32.509  1.00 26.22 ? 204 PRO   C CA  1 
ATOM   5070 C C   . PRO   C 1 225 ? -5.373  10.656  31.177  1.00 27.54 ? 204 PRO   C C   1 
ATOM   5071 O O   . PRO   C 1 225 ? -4.533  10.298  30.351  1.00 28.80 ? 204 PRO   C O   1 
ATOM   5072 C CB  . PRO   C 1 225 ? -4.555  10.514  33.570  1.00 28.02 ? 204 PRO   C CB  1 
ATOM   5073 C CG  . PRO   C 1 225 ? -3.896  9.266   34.173  1.00 27.37 ? 204 PRO   C CG  1 
ATOM   5074 C CD  . PRO   C 1 225 ? -3.804  8.253   33.008  1.00 27.95 ? 204 PRO   C CD  1 
ATOM   5075 N N   . GLY   C 1 226 ? -6.162  11.722  30.996  1.00 26.44 ? 205 GLY   C N   1 
ATOM   5076 C CA  . GLY   C 1 226 ? -5.963  12.630  29.886  1.00 28.92 ? 205 GLY   C CA  1 
ATOM   5077 C C   . GLY   C 1 226 ? -5.135  13.826  30.343  1.00 35.05 ? 205 GLY   C C   1 
ATOM   5078 O O   . GLY   C 1 226 ? -3.907  13.775  30.351  1.00 39.63 ? 205 GLY   C O   1 
ATOM   5079 N N   . VAL   C 1 227 ? -5.816  14.908  30.721  1.00 33.81 ? 206 VAL   C N   1 
ATOM   5080 C CA  . VAL   C 1 227 ? -5.136  15.976  31.427  1.00 33.48 ? 206 VAL   C CA  1 
ATOM   5081 C C   . VAL   C 1 227 ? -5.639  15.903  32.858  1.00 33.73 ? 206 VAL   C C   1 
ATOM   5082 O O   . VAL   C 1 227 ? -6.846  15.936  33.122  1.00 33.76 ? 206 VAL   C O   1 
ATOM   5083 C CB  . VAL   C 1 227 ? -5.270  17.369  30.783  1.00 38.57 ? 206 VAL   C CB  1 
ATOM   5084 C CG1 . VAL   C 1 227 ? -4.566  17.388  29.428  1.00 42.56 ? 206 VAL   C CG1 1 
ATOM   5085 C CG2 . VAL   C 1 227 ? -6.726  17.779  30.624  1.00 32.90 ? 206 VAL   C CG2 1 
ATOM   5086 N N   . SER   C 1 228 ? -4.701  15.617  33.757  1.00 40.86 ? 207 SER   C N   1 
ATOM   5087 C CA  . SER   C 1 228 ? -4.960  15.689  35.179  1.00 44.71 ? 207 SER   C CA  1 
ATOM   5088 C C   . SER   C 1 228 ? -4.178  16.902  35.663  1.00 55.50 ? 207 SER   C C   1 
ATOM   5089 O O   . SER   C 1 228 ? -3.934  17.806  34.856  1.00 53.99 ? 207 SER   C O   1 
ATOM   5090 C CB  . SER   C 1 228 ? -4.507  14.423  35.853  1.00 41.85 ? 207 SER   C CB  1 
ATOM   5091 O OG  . SER   C 1 228 ? -5.071  14.301  37.149  1.00 46.84 ? 207 SER   C OG  1 
ATOM   5092 N N   . LEU   C 1 229 ? -3.761  16.894  36.942  1.00 61.36 ? 208 LEU   C N   1 
ATOM   5093 C CA  . LEU   C 1 229 ? -2.807  17.867  37.470  1.00 61.59 ? 208 LEU   C CA  1 
ATOM   5094 C C   . LEU   C 1 229 ? -1.771  18.179  36.393  1.00 64.57 ? 208 LEU   C C   1 
ATOM   5095 O O   . LEU   C 1 229 ? -1.084  17.287  35.890  1.00 69.69 ? 208 LEU   C O   1 
ATOM   5096 C CB  . LEU   C 1 229 ? -2.111  17.336  38.725  1.00 55.17 ? 208 LEU   C CB  1 
ATOM   5097 C CG  . LEU   C 1 229 ? -3.021  16.924  39.883  1.00 57.43 ? 208 LEU   C CG  1 
ATOM   5098 C CD1 . LEU   C 1 229 ? -2.181  16.399  41.043  1.00 58.98 ? 208 LEU   C CD1 1 
ATOM   5099 C CD2 . LEU   C 1 229 ? -3.860  18.117  40.307  1.00 58.36 ? 208 LEU   C CD2 1 
ATOM   5100 N N   . LEU   C 1 230 ? -1.686  19.451  36.018  1.00 57.85 ? 209 LEU   C N   1 
ATOM   5101 C CA  . LEU   C 1 230 ? -0.788  19.816  34.941  1.00 65.79 ? 209 LEU   C CA  1 
ATOM   5102 C C   . LEU   C 1 230 ? 0.604   20.053  35.529  1.00 72.89 ? 209 LEU   C C   1 
ATOM   5103 O O   . LEU   C 1 230 ? 0.718   20.299  36.731  1.00 65.43 ? 209 LEU   C O   1 
ATOM   5104 C CB  . LEU   C 1 230 ? -1.405  21.010  34.212  1.00 65.52 ? 209 LEU   C CB  1 
ATOM   5105 C CG  . LEU   C 1 230 ? -2.738  20.703  33.513  1.00 65.84 ? 209 LEU   C CG  1 
ATOM   5106 C CD1 . LEU   C 1 230 ? -3.478  21.936  33.036  1.00 63.83 ? 209 LEU   C CD1 1 
ATOM   5107 C CD2 . LEU   C 1 230 ? -2.535  19.709  32.363  1.00 65.78 ? 209 LEU   C CD2 1 
ATOM   5108 N N   . PRO   C 1 231 ? 1.697   19.885  34.737  1.00 82.48 ? 210 PRO   C N   1 
ATOM   5109 C CA  . PRO   C 1 231 ? 3.059   20.129  35.229  1.00 86.51 ? 210 PRO   C CA  1 
ATOM   5110 C C   . PRO   C 1 231 ? 3.220   21.506  35.875  1.00 89.26 ? 210 PRO   C C   1 
ATOM   5111 O O   . PRO   C 1 231 ? 2.693   22.499  35.367  1.00 86.18 ? 210 PRO   C O   1 
ATOM   5112 C CB  . PRO   C 1 231 ? 3.943   19.962  33.974  1.00 84.50 ? 210 PRO   C CB  1 
ATOM   5113 C CG  . PRO   C 1 231 ? 3.138   19.060  33.066  1.00 85.70 ? 210 PRO   C CG  1 
ATOM   5114 C CD  . PRO   C 1 231 ? 1.684   19.424  33.337  1.00 81.85 ? 210 PRO   C CD  1 
ATOM   5115 N N   . VAL   C 1 232 ? 3.953   21.542  37.000  1.00 87.68 ? 211 VAL   C N   1 
ATOM   5116 C CA  . VAL   C 1 232 ? 4.207   22.759  37.759  1.00 87.16 ? 211 VAL   C CA  1 
ATOM   5117 C C   . VAL   C 1 232 ? 4.835   23.804  36.836  1.00 83.51 ? 211 VAL   C C   1 
ATOM   5118 O O   . VAL   C 1 232 ? 4.565   24.998  36.961  1.00 74.35 ? 211 VAL   C O   1 
ATOM   5119 C CB  . VAL   C 1 232 ? 5.113   22.458  38.970  1.00 80.82 ? 211 VAL   C CB  1 
ATOM   5120 N N   . ALA   C 1 233 ? 5.632   23.315  35.877  1.00 86.72 ? 212 ALA   C N   1 
ATOM   5121 C CA  . ALA   C 1 233 ? 6.457   24.125  34.995  1.00 87.60 ? 212 ALA   C CA  1 
ATOM   5122 C C   . ALA   C 1 233 ? 5.627   24.866  33.944  1.00 84.31 ? 212 ALA   C C   1 
ATOM   5123 O O   . ALA   C 1 233 ? 5.909   26.031  33.669  1.00 80.78 ? 212 ALA   C O   1 
ATOM   5124 C CB  . ALA   C 1 233 ? 7.528   23.264  34.354  1.00 81.21 ? 212 ALA   C CB  1 
ATOM   5125 N N   . MET   C 1 234 ? 4.623   24.193  33.357  1.00 85.86 ? 213 MET   C N   1 
ATOM   5126 C CA  . MET   C 1 234 ? 3.962   24.701  32.158  1.00 79.71 ? 213 MET   C CA  1 
ATOM   5127 C C   . MET   C 1 234 ? 3.155   25.964  32.458  1.00 75.85 ? 213 MET   C C   1 
ATOM   5128 O O   . MET   C 1 234 ? 2.564   26.097  33.531  1.00 72.45 ? 213 MET   C O   1 
ATOM   5129 C CB  . MET   C 1 234 ? 3.113   23.644  31.437  1.00 80.60 ? 213 MET   C CB  1 
ATOM   5130 C CG  . MET   C 1 234 ? 1.848   23.199  32.154  0.60 69.94 ? 213 MET   C CG  1 
ATOM   5131 S SD  . MET   C 1 234 ? 0.706   22.341  31.048  0.60 60.52 ? 213 MET   C SD  1 
ATOM   5132 C CE  . MET   C 1 234 ? 0.440   23.607  29.804  0.60 54.08 ? 213 MET   C CE  1 
ATOM   5133 N N   . GLY   C 1 235 ? 3.146   26.880  31.478  1.00 73.67 ? 214 GLY   C N   1 
ATOM   5134 C CA  . GLY   C 1 235 ? 2.440   28.150  31.558  1.00 73.12 ? 214 GLY   C CA  1 
ATOM   5135 C C   . GLY   C 1 235 ? 0.995   27.974  32.018  1.00 78.35 ? 214 GLY   C C   1 
ATOM   5136 O O   . GLY   C 1 235 ? 0.400   26.917  31.813  1.00 77.71 ? 214 GLY   C O   1 
ATOM   5137 N N   . GLU   C 1 236 ? 0.452   29.028  32.641  1.00 79.67 ? 215 GLU   C N   1 
ATOM   5138 C CA  . GLU   C 1 236 ? -0.917  29.041  33.139  1.00 76.30 ? 215 GLU   C CA  1 
ATOM   5139 C C   . GLU   C 1 236 ? -1.880  29.239  31.966  1.00 70.56 ? 215 GLU   C C   1 
ATOM   5140 O O   . GLU   C 1 236 ? -3.008  28.743  31.997  1.00 68.20 ? 215 GLU   C O   1 
ATOM   5141 C CB  . GLU   C 1 236 ? -1.058  30.066  34.268  1.00 73.27 ? 215 GLU   C CB  1 
ATOM   5142 C CG  . GLU   C 1 236 ? -2.299  29.886  35.140  1.00 73.91 ? 215 GLU   C CG  1 
ATOM   5143 C CD  . GLU   C 1 236 ? -2.491  28.476  35.680  1.00 81.33 ? 215 GLU   C CD  1 
ATOM   5144 O OE1 . GLU   C 1 236 ? -1.522  27.836  36.160  1.00 76.13 ? 215 GLU   C OE1 1 
ATOM   5145 O OE2 . GLU   C 1 236 ? -3.647  28.011  35.621  1.00 80.06 ? 215 GLU   C OE2 1 
ATOM   5146 N N   . GLU   C 1 237 ? -1.406  29.946  30.930  1.00 65.86 ? 216 GLU   C N   1 
ATOM   5147 C CA  . GLU   C 1 237 ? -2.152  30.148  29.696  1.00 65.09 ? 216 GLU   C CA  1 
ATOM   5148 C C   . GLU   C 1 237 ? -2.193  28.850  28.886  1.00 73.47 ? 216 GLU   C C   1 
ATOM   5149 O O   . GLU   C 1 237 ? -3.232  28.512  28.311  1.00 70.64 ? 216 GLU   C O   1 
ATOM   5150 C CB  . GLU   C 1 237 ? -1.554  31.277  28.859  1.00 54.44 ? 216 GLU   C CB  1 
ATOM   5151 N N   . GLU   C 1 238 ? -1.056  28.135  28.840  1.00 73.23 ? 217 GLU   C N   1 
ATOM   5152 C CA  . GLU   C 1 238 ? -0.970  26.846  28.162  1.00 68.90 ? 217 GLU   C CA  1 
ATOM   5153 C C   . GLU   C 1 238 ? -1.880  25.831  28.865  1.00 67.09 ? 217 GLU   C C   1 
ATOM   5154 O O   . GLU   C 1 238 ? -2.478  24.973  28.214  1.00 60.41 ? 217 GLU   C O   1 
ATOM   5155 C CB  . GLU   C 1 238 ? 0.480   26.374  28.011  1.00 57.45 ? 217 GLU   C CB  1 
ATOM   5156 N N   . LYS   C 1 239 ? -1.982  25.941  30.199  1.00 62.58 ? 218 LYS   C N   1 
ATOM   5157 C CA  . LYS   C 1 239 ? -2.810  25.049  31.000  1.00 56.85 ? 218 LYS   C CA  1 
ATOM   5158 C C   . LYS   C 1 239 ? -4.283  25.234  30.629  1.00 52.95 ? 218 LYS   C C   1 
ATOM   5159 O O   . LYS   C 1 239 ? -5.010  24.250  30.479  1.00 54.13 ? 218 LYS   C O   1 
ATOM   5160 C CB  . LYS   C 1 239 ? -2.583  25.221  32.509  1.00 47.85 ? 218 LYS   C CB  1 
ATOM   5161 C CG  . LYS   C 1 239 ? -1.286  24.684  33.095  0.60 50.17 ? 218 LYS   C CG  1 
ATOM   5162 C CD  . LYS   C 1 239 ? -1.227  24.881  34.605  0.60 45.05 ? 218 LYS   C CD  1 
ATOM   5163 C CE  . LYS   C 1 239 ? 0.051   24.396  35.211  0.60 46.71 ? 218 LYS   C CE  1 
ATOM   5164 N NZ  . LYS   C 1 239 ? 0.353   25.133  36.437  0.60 46.14 ? 218 LYS   C NZ  1 
ATOM   5165 N N   . ASP   C 1 240 ? -4.722  26.493  30.482  1.00 55.80 ? 219 ASP   C N   1 
ATOM   5166 C CA  . ASP   C 1 240 ? -6.134  26.774  30.246  1.00 55.59 ? 219 ASP   C CA  1 
ATOM   5167 C C   . ASP   C 1 240 ? -6.507  26.321  28.833  1.00 51.49 ? 219 ASP   C C   1 
ATOM   5168 O O   . ASP   C 1 240 ? -7.654  25.942  28.574  1.00 48.97 ? 219 ASP   C O   1 
ATOM   5169 C CB  . ASP   C 1 240 ? -6.522  28.218  30.563  1.00 57.91 ? 219 ASP   C CB  1 
ATOM   5170 C CG  . ASP   C 1 240 ? -6.590  28.612  32.039  0.60 56.35 ? 219 ASP   C CG  1 
ATOM   5171 O OD1 . ASP   C 1 240 ? -7.162  27.839  32.841  0.60 53.15 ? 219 ASP   C OD1 1 
ATOM   5172 O OD2 . ASP   C 1 240 ? -6.112  29.720  32.377  0.60 54.23 ? 219 ASP   C OD2 1 
ATOM   5173 N N   . LYS   C 1 241 ? -5.517  26.356  27.932  1.00 47.02 ? 220 LYS   C N   1 
ATOM   5174 C CA  . LYS   C 1 241 ? -5.703  25.918  26.557  1.00 50.40 ? 220 LYS   C CA  1 
ATOM   5175 C C   . LYS   C 1 241 ? -6.095  24.438  26.545  1.00 50.09 ? 220 LYS   C C   1 
ATOM   5176 O O   . LYS   C 1 241 ? -6.954  24.028  25.760  1.00 50.56 ? 220 LYS   C O   1 
ATOM   5177 C CB  . LYS   C 1 241 ? -4.474  26.203  25.684  1.00 48.19 ? 220 LYS   C CB  1 
ATOM   5178 C CG  . LYS   C 1 241 ? -4.781  26.315  24.193  1.00 48.82 ? 220 LYS   C CG  1 
ATOM   5179 N N   . TRP   C 1 242 ? -5.467  23.655  27.440  1.00 48.81 ? 221 TRP   C N   1 
ATOM   5180 C CA  . TRP   C 1 242 ? -5.790  22.244  27.601  1.00 49.58 ? 221 TRP   C CA  1 
ATOM   5181 C C   . TRP   C 1 242 ? -7.141  22.058  28.293  1.00 50.41 ? 221 TRP   C C   1 
ATOM   5182 O O   . TRP   C 1 242 ? -7.954  21.253  27.844  1.00 43.50 ? 221 TRP   C O   1 
ATOM   5183 C CB  . TRP   C 1 242 ? -4.668  21.495  28.329  1.00 45.06 ? 221 TRP   C CB  1 
ATOM   5184 C CG  . TRP   C 1 242 ? -3.535  21.098  27.426  1.00 48.34 ? 221 TRP   C CG  1 
ATOM   5185 C CD1 . TRP   C 1 242 ? -2.292  21.646  27.364  1.00 51.74 ? 221 TRP   C CD1 1 
ATOM   5186 C CD2 . TRP   C 1 242 ? -3.561  20.040  26.444  1.00 47.49 ? 221 TRP   C CD2 1 
ATOM   5187 N NE1 . TRP   C 1 242 ? -1.537  20.998  26.424  1.00 49.01 ? 221 TRP   C NE1 1 
ATOM   5188 C CE2 . TRP   C 1 242 ? -2.284  20.006  25.845  1.00 51.57 ? 221 TRP   C CE2 1 
ATOM   5189 C CE3 . TRP   C 1 242 ? -4.532  19.122  26.023  1.00 47.54 ? 221 TRP   C CE3 1 
ATOM   5190 C CZ2 . TRP   C 1 242 ? -1.956  19.086  24.845  1.00 47.62 ? 221 TRP   C CZ2 1 
ATOM   5191 C CZ3 . TRP   C 1 242 ? -4.202  18.203  25.047  1.00 45.64 ? 221 TRP   C CZ3 1 
ATOM   5192 C CH2 . TRP   C 1 242 ? -2.929  18.178  24.485  1.00 39.73 ? 221 TRP   C CH2 1 
ATOM   5193 N N   . ARG   C 1 243 ? -7.384  22.818  29.369  1.00 43.53 ? 222 ARG   C N   1 
ATOM   5194 C CA  . ARG   C 1 243 ? -8.640  22.728  30.098  1.00 45.55 ? 222 ARG   C CA  1 
ATOM   5195 C C   . ARG   C 1 243 ? -9.814  22.914  29.137  1.00 43.07 ? 222 ARG   C C   1 
ATOM   5196 O O   . ARG   C 1 243 ? -10.813 22.209  29.233  1.00 41.46 ? 222 ARG   C O   1 
ATOM   5197 C CB  . ARG   C 1 243 ? -8.660  23.769  31.227  1.00 48.57 ? 222 ARG   C CB  1 
ATOM   5198 C CG  . ARG   C 1 243 ? -7.664  23.463  32.337  0.80 49.77 ? 222 ARG   C CG  1 
ATOM   5199 C CD  . ARG   C 1 243 ? -7.628  24.546  33.418  0.80 54.93 ? 222 ARG   C CD  1 
ATOM   5200 N NE  . ARG   C 1 243 ? -6.779  24.175  34.557  0.80 46.61 ? 222 ARG   C NE  1 
ATOM   5201 C CZ  . ARG   C 1 243 ? -5.797  24.906  35.095  0.80 46.64 ? 222 ARG   C CZ  1 
ATOM   5202 N NH1 . ARG   C 1 243 ? -5.486  26.091  34.602  0.80 41.41 ? 222 ARG   C NH1 1 
ATOM   5203 N NH2 . ARG   C 1 243 ? -5.103  24.436  36.116  0.80 44.75 ? 222 ARG   C NH2 1 
ATOM   5204 N N   . ARG   C 1 244 ? -9.687  23.877  28.216  1.00 40.70 ? 223 ARG   C N   1 
ATOM   5205 C CA  . ARG   C 1 244 ? -10.784 24.266  27.341  1.00 40.50 ? 223 ARG   C CA  1 
ATOM   5206 C C   . ARG   C 1 244 ? -11.166 23.142  26.360  1.00 40.02 ? 223 ARG   C C   1 
ATOM   5207 O O   . ARG   C 1 244 ? -12.277 23.136  25.849  1.00 38.96 ? 223 ARG   C O   1 
ATOM   5208 C CB  . ARG   C 1 244 ? -10.398 25.559  26.609  1.00 42.13 ? 223 ARG   C CB  1 
ATOM   5209 N N   . LYS   C 1 245 ? -10.261 22.180  26.120  1.00 40.84 ? 224 LYS   C N   1 
ATOM   5210 C CA  . LYS   C 1 245 ? -10.467 21.144  25.110  1.00 34.99 ? 224 LYS   C CA  1 
ATOM   5211 C C   . LYS   C 1 245 ? -11.306 20.002  25.681  1.00 32.50 ? 224 LYS   C C   1 
ATOM   5212 O O   . LYS   C 1 245 ? -11.849 19.203  24.918  1.00 31.46 ? 224 LYS   C O   1 
ATOM   5213 C CB  . LYS   C 1 245 ? -9.127  20.609  24.581  0.70 36.42 ? 224 LYS   C CB  1 
ATOM   5214 C CG  . LYS   C 1 245 ? -8.196  21.568  23.823  0.70 38.89 ? 224 LYS   C CG  1 
ATOM   5215 C CD  . LYS   C 1 245 ? -6.818  20.912  23.827  0.70 40.54 ? 224 LYS   C CD  1 
ATOM   5216 C CE  . LYS   C 1 245 ? -5.628  21.791  23.545  0.70 43.27 ? 224 LYS   C CE  1 
ATOM   5217 N NZ  . LYS   C 1 245 ? -5.371  21.990  22.123  0.70 43.19 ? 224 LYS   C NZ  1 
ATOM   5218 N N   . VAL   C 1 246 ? -11.431 19.929  27.017  1.00 29.40 ? 225 VAL   C N   1 
ATOM   5219 C CA  . VAL   C 1 246 ? -12.030 18.774  27.672  1.00 28.05 ? 225 VAL   C CA  1 
ATOM   5220 C C   . VAL   C 1 246 ? -13.559 18.857  27.593  1.00 31.60 ? 225 VAL   C C   1 
ATOM   5221 O O   . VAL   C 1 246 ? -14.158 19.763  28.193  1.00 30.31 ? 225 VAL   C O   1 
ATOM   5222 C CB  . VAL   C 1 246 ? -11.561 18.588  29.132  1.00 26.15 ? 225 VAL   C CB  1 
ATOM   5223 C CG1 . VAL   C 1 246 ? -12.278 17.449  29.833  1.00 23.88 ? 225 VAL   C CG1 1 
ATOM   5224 C CG2 . VAL   C 1 246 ? -10.027 18.419  29.292  1.00 27.40 ? 225 VAL   C CG2 1 
ATOM   5225 N N   . PRO   C 1 247 ? -14.263 17.899  26.928  1.00 28.09 ? 226 PRO   C N   1 
ATOM   5226 C CA  . PRO   C 1 247 ? -15.731 17.948  26.839  1.00 28.15 ? 226 PRO   C CA  1 
ATOM   5227 C C   . PRO   C 1 247 ? -16.444 18.043  28.184  1.00 29.28 ? 226 PRO   C C   1 
ATOM   5228 O O   . PRO   C 1 247 ? -17.374 18.824  28.307  1.00 27.97 ? 226 PRO   C O   1 
ATOM   5229 C CB  . PRO   C 1 247 ? -16.108 16.642  26.100  1.00 28.50 ? 226 PRO   C CB  1 
ATOM   5230 C CG  . PRO   C 1 247 ? -14.886 16.365  25.252  1.00 28.95 ? 226 PRO   C CG  1 
ATOM   5231 C CD  . PRO   C 1 247 ? -13.708 16.766  26.157  1.00 28.41 ? 226 PRO   C CD  1 
ATOM   5232 N N   . LEU   C 1 248 ? -16.043 17.208  29.151  1.00 24.98 ? 227 LEU   C N   1 
ATOM   5233 C CA  . LEU   C 1 248 ? -16.742 17.097  30.416  1.00 29.47 ? 227 LEU   C CA  1 
ATOM   5234 C C   . LEU   C 1 248 ? -16.194 18.137  31.399  1.00 30.69 ? 227 LEU   C C   1 
ATOM   5235 O O   . LEU   C 1 248 ? -15.351 17.808  32.211  1.00 33.31 ? 227 LEU   C O   1 
ATOM   5236 C CB  . LEU   C 1 248 ? -16.569 15.671  30.945  1.00 28.25 ? 227 LEU   C CB  1 
ATOM   5237 C CG  . LEU   C 1 248 ? -17.578 15.169  31.977  1.00 29.50 ? 227 LEU   C CG  1 
ATOM   5238 C CD1 . LEU   C 1 248 ? -18.987 15.053  31.397  1.00 29.46 ? 227 LEU   C CD1 1 
ATOM   5239 C CD2 . LEU   C 1 248 ? -17.101 13.810  32.538  1.00 30.79 ? 227 LEU   C CD2 1 
ATOM   5240 N N   . GLY   C 1 249 ? -16.694 19.375  31.329  1.00 39.24 ? 228 GLY   C N   1 
ATOM   5241 C CA  . GLY   C 1 249 ? -16.492 20.348  32.402  1.00 31.17 ? 228 GLY   C CA  1 
ATOM   5242 C C   . GLY   C 1 249 ? -15.339 21.304  32.126  1.00 36.51 ? 228 GLY   C C   1 
ATOM   5243 O O   . GLY   C 1 249 ? -14.992 22.100  32.992  1.00 38.06 ? 228 GLY   C O   1 
ATOM   5244 N N   . ARG   C 1 250 ? -14.712 21.204  30.943  1.00 34.82 ? 229 ARG   C N   1 
ATOM   5245 C CA  . ARG   C 1 250 ? -13.660 22.135  30.534  1.00 36.26 ? 229 ARG   C CA  1 
ATOM   5246 C C   . ARG   C 1 250 ? -12.585 22.294  31.620  1.00 43.11 ? 229 ARG   C C   1 
ATOM   5247 O O   . ARG   C 1 250 ? -12.075 23.397  31.836  1.00 34.36 ? 229 ARG   C O   1 
ATOM   5248 C CB  . ARG   C 1 250 ? -14.271 23.467  30.051  1.00 37.53 ? 229 ARG   C CB  1 
ATOM   5249 C CG  . ARG   C 1 250 ? -15.329 23.380  28.955  0.70 39.07 ? 229 ARG   C CG  1 
ATOM   5250 C CD  . ARG   C 1 250 ? -14.755 22.919  27.628  0.70 44.82 ? 229 ARG   C CD  1 
ATOM   5251 N NE  . ARG   C 1 250 ? -15.730 22.396  26.658  0.70 45.41 ? 229 ARG   C NE  1 
ATOM   5252 C CZ  . ARG   C 1 250 ? -15.482 22.002  25.409  0.70 40.96 ? 229 ARG   C CZ  1 
ATOM   5253 N NH1 . ARG   C 1 250 ? -14.255 22.031  24.919  0.70 40.11 ? 229 ARG   C NH1 1 
ATOM   5254 N NH2 . ARG   C 1 250 ? -16.473 21.589  24.635  0.70 40.24 ? 229 ARG   C NH2 1 
ATOM   5255 N N   . ARG   C 1 251 ? -12.184 21.174  32.247  1.00 37.27 ? 230 ARG   C N   1 
ATOM   5256 C CA  . ARG   C 1 251 ? -11.263 21.180  33.376  1.00 36.74 ? 230 ARG   C CA  1 
ATOM   5257 C C   . ARG   C 1 251 ? -10.486 19.867  33.406  1.00 40.03 ? 230 ARG   C C   1 
ATOM   5258 O O   . ARG   C 1 251 ? -10.944 18.859  32.846  1.00 33.87 ? 230 ARG   C O   1 
ATOM   5259 C CB  . ARG   C 1 251 ? -12.073 21.316  34.678  1.00 37.99 ? 230 ARG   C CB  1 
ATOM   5260 C CG  . ARG   C 1 251 ? -12.949 20.144  35.126  1.00 39.38 ? 230 ARG   C CG  1 
ATOM   5261 C CD  . ARG   C 1 251 ? -13.429 20.273  36.580  1.00 46.98 ? 230 ARG   C CD  1 
ATOM   5262 N N   . GLU   C 1 252 ? -9.323  19.889  34.084  1.00 39.07 ? 231 GLU   C N   1 
ATOM   5263 C CA  . GLU   C 1 252 ? -8.550  18.674  34.323  1.00 42.38 ? 231 GLU   C CA  1 
ATOM   5264 C C   . GLU   C 1 252 ? -9.197  17.780  35.390  1.00 38.50 ? 231 GLU   C C   1 
ATOM   5265 O O   . GLU   C 1 252 ? -10.009 18.230  36.220  1.00 33.78 ? 231 GLU   C O   1 
ATOM   5266 C CB  . GLU   C 1 252 ? -7.102  18.978  34.728  1.00 50.07 ? 231 GLU   C CB  1 
ATOM   5267 C CG  . GLU   C 1 252 ? -6.975  19.643  36.097  1.00 51.97 ? 231 GLU   C CG  1 
ATOM   5268 C CD  . GLU   C 1 252 ? -6.942  21.159  35.986  1.00 60.20 ? 231 GLU   C CD  1 
ATOM   5269 O OE1 . GLU   C 1 252 ? -6.042  21.734  36.633  1.00 56.55 ? 231 GLU   C OE1 1 
ATOM   5270 O OE2 . GLU   C 1 252 ? -7.767  21.758  35.251  1.00 54.94 ? 231 GLU   C OE2 1 
ATOM   5271 N N   . ALA   C 1 253 ? -8.797  16.495  35.368  1.00 32.45 ? 232 ALA   C N   1 
ATOM   5272 C CA  . ALA   C 1 253 ? -9.110  15.571  36.446  1.00 37.40 ? 232 ALA   C CA  1 
ATOM   5273 C C   . ALA   C 1 253 ? -8.294  16.014  37.649  1.00 37.48 ? 232 ALA   C C   1 
ATOM   5274 O O   . ALA   C 1 253 ? -7.121  16.358  37.500  1.00 37.07 ? 232 ALA   C O   1 
ATOM   5275 C CB  . ALA   C 1 253 ? -8.709  14.129  36.136  1.00 32.08 ? 232 ALA   C CB  1 
ATOM   5276 N N   . SER   C 1 254 ? -8.921  15.913  38.814  1.00 35.76 ? 233 SER   C N   1 
ATOM   5277 C CA  . SER   C 1 254 ? -8.166  15.945  40.046  1.00 36.59 ? 233 SER   C CA  1 
ATOM   5278 C C   . SER   C 1 254 ? -7.380  14.641  40.158  1.00 38.58 ? 233 SER   C C   1 
ATOM   5279 O O   . SER   C 1 254 ? -7.742  13.637  39.544  1.00 32.07 ? 233 SER   C O   1 
ATOM   5280 C CB  . SER   C 1 254 ? -9.106  16.083  41.196  1.00 31.29 ? 233 SER   C CB  1 
ATOM   5281 O OG  . SER   C 1 254 ? -9.986  14.974  41.214  1.00 35.85 ? 233 SER   C OG  1 
ATOM   5282 N N   . ALA   C 1 255 ? -6.312  14.665  40.961  1.00 32.91 ? 234 ALA   C N   1 
ATOM   5283 C CA  . ALA   C 1 255 ? -5.623  13.434  41.299  1.00 33.82 ? 234 ALA   C CA  1 
ATOM   5284 C C   . ALA   C 1 255 ? -6.589  12.400  41.870  1.00 33.00 ? 234 ALA   C C   1 
ATOM   5285 O O   . ALA   C 1 255 ? -6.445  11.210  41.602  1.00 33.70 ? 234 ALA   C O   1 
ATOM   5286 C CB  . ALA   C 1 255 ? -4.428  13.718  42.210  1.00 35.91 ? 234 ALA   C CB  1 
ATOM   5287 N N   . GLU   C 1 256 ? -7.577  12.826  42.661  1.00 30.94 ? 235 GLU   C N   1 
ATOM   5288 C CA  A GLU   C 1 256 ? -8.441  11.887  43.358  0.70 33.24 ? 235 GLU   C CA  1 
ATOM   5289 C CA  B GLU   C 1 256 ? -8.453  11.897  43.364  0.30 31.03 ? 235 GLU   C CA  1 
ATOM   5290 C C   . GLU   C 1 256 ? -9.357  11.140  42.386  1.00 31.44 ? 235 GLU   C C   1 
ATOM   5291 O O   . GLU   C 1 256 ? -9.745  9.997   42.635  1.00 31.71 ? 235 GLU   C O   1 
ATOM   5292 C CB  A GLU   C 1 256 ? -9.330  12.628  44.351  0.70 36.77 ? 235 GLU   C CB  1 
ATOM   5293 C CB  B GLU   C 1 256 ? -9.284  12.595  44.443  0.30 30.19 ? 235 GLU   C CB  1 
ATOM   5294 C CG  A GLU   C 1 256 ? -8.553  13.282  45.487  0.70 46.78 ? 235 GLU   C CG  1 
ATOM   5295 C CG  B GLU   C 1 256 ? -8.486  12.999  45.682  0.30 30.96 ? 235 GLU   C CG  1 
ATOM   5296 C CD  A GLU   C 1 256 ? -9.487  13.370  46.673  0.70 51.13 ? 235 GLU   C CD  1 
ATOM   5297 C CD  B GLU   C 1 256 ? -7.765  14.335  45.607  0.30 31.52 ? 235 GLU   C CD  1 
ATOM   5298 O OE1 A GLU   C 1 256 ? -10.544 12.695  46.602  0.70 51.66 ? 235 GLU   C OE1 1 
ATOM   5299 O OE1 B GLU   C 1 256 ? -7.815  14.979  44.539  0.30 29.53 ? 235 GLU   C OE1 1 
ATOM   5300 O OE2 A GLU   C 1 256 ? -9.157  14.085  47.651  0.70 60.18 ? 235 GLU   C OE2 1 
ATOM   5301 O OE2 B GLU   C 1 256 ? -7.165  14.737  46.632  0.30 32.78 ? 235 GLU   C OE2 1 
ATOM   5302 N N   . GLN   C 1 257 ? -9.745  11.802  41.292  1.00 32.20 ? 236 GLN   C N   1 
ATOM   5303 C CA  . GLN   C 1 257 ? -10.575 11.137  40.288  1.00 32.13 ? 236 GLN   C CA  1 
ATOM   5304 C C   . GLN   C 1 257 ? -9.778  9.989   39.655  1.00 26.50 ? 236 GLN   C C   1 
ATOM   5305 O O   . GLN   C 1 257 ? -10.291 8.905   39.397  1.00 28.98 ? 236 GLN   C O   1 
ATOM   5306 C CB  . GLN   C 1 257 ? -11.055 12.190  39.278  1.00 34.98 ? 236 GLN   C CB  1 
ATOM   5307 C CG  . GLN   C 1 257 ? -11.951 13.234  39.940  1.00 34.35 ? 236 GLN   C CG  1 
ATOM   5308 C CD  . GLN   C 1 257 ? -12.396 14.346  39.016  1.00 28.68 ? 236 GLN   C CD  1 
ATOM   5309 O OE1 . GLN   C 1 257 ? -11.589 14.985  38.339  1.00 32.43 ? 236 GLN   C OE1 1 
ATOM   5310 N NE2 . GLN   C 1 257 ? -13.686 14.606  39.037  1.00 33.25 ? 236 GLN   C NE2 1 
ATOM   5311 N N   . ILE   C 1 258 ? -8.493  10.219  39.443  1.00 24.93 ? 237 ILE   C N   1 
ATOM   5312 C CA  . ILE   C 1 258 ? -7.633  9.161   38.929  1.00 28.76 ? 237 ILE   C CA  1 
ATOM   5313 C C   . ILE   C 1 258 ? -7.567  8.019   39.944  1.00 30.70 ? 237 ILE   C C   1 
ATOM   5314 O O   . ILE   C 1 258 ? -7.695  6.849   39.605  1.00 25.73 ? 237 ILE   C O   1 
ATOM   5315 C CB  . ILE   C 1 258 ? -6.257  9.721   38.508  1.00 28.22 ? 237 ILE   C CB  1 
ATOM   5316 C CG1 . ILE   C 1 258 ? -6.366  10.874  37.493  1.00 32.25 ? 237 ILE   C CG1 1 
ATOM   5317 C CG2 . ILE   C 1 258 ? -5.304  8.618   38.034  1.00 32.89 ? 237 ILE   C CG2 1 
ATOM   5318 C CD1 . ILE   C 1 258 ? -7.259  10.565  36.299  1.00 30.65 ? 237 ILE   C CD1 1 
ATOM   5319 N N   . ALA   C 1 259 ? -7.403  8.354   41.229  1.00 29.10 ? 238 ALA   C N   1 
ATOM   5320 C CA  . ALA   C 1 259 ? -7.257  7.327   42.250  1.00 27.47 ? 238 ALA   C CA  1 
ATOM   5321 C C   . ALA   C 1 259 ? -8.525  6.505   42.357  1.00 26.86 ? 238 ALA   C C   1 
ATOM   5322 O O   . ALA   C 1 259 ? -8.458  5.327   42.679  1.00 28.53 ? 238 ALA   C O   1 
ATOM   5323 C CB  . ALA   C 1 259 ? -6.930  8.026   43.580  1.00 32.01 ? 238 ALA   C CB  1 
ATOM   5324 N N   . ASP   C 1 260 ? -9.682  7.156   42.167  1.00 25.26 ? 239 ASP   C N   1 
ATOM   5325 C CA  . ASP   C 1 260 ? -10.982 6.503   42.260  1.00 30.56 ? 239 ASP   C CA  1 
ATOM   5326 C C   . ASP   C 1 260 ? -11.017 5.264   41.360  1.00 26.87 ? 239 ASP   C C   1 
ATOM   5327 O O   . ASP   C 1 260 ? -11.531 4.222   41.740  1.00 29.24 ? 239 ASP   C O   1 
ATOM   5328 C CB  . ASP   C 1 260 ? -12.120 7.463   41.916  1.00 31.97 ? 239 ASP   C CB  1 
ATOM   5329 C CG  . ASP   C 1 260 ? -12.624 8.295   43.090  1.00 36.15 ? 239 ASP   C CG  1 
ATOM   5330 O OD1 . ASP   C 1 260 ? -12.466 7.828   44.231  1.00 37.00 ? 239 ASP   C OD1 1 
ATOM   5331 O OD2 . ASP   C 1 260 ? -13.065 9.426   42.860  1.00 33.22 ? 239 ASP   C OD2 1 
ATOM   5332 N N   . ALA   C 1 261 ? -10.480 5.412   40.144  1.00 29.65 ? 240 ALA   C N   1 
ATOM   5333 C CA  . ALA   C 1 261 ? -10.440 4.313   39.179  1.00 25.70 ? 240 ALA   C CA  1 
ATOM   5334 C C   . ALA   C 1 261 ? -9.453  3.229   39.625  1.00 27.27 ? 240 ALA   C C   1 
ATOM   5335 O O   . ALA   C 1 261 ? -9.668  2.038   39.384  1.00 27.04 ? 240 ALA   C O   1 
ATOM   5336 C CB  . ALA   C 1 261 ? -9.984  4.895   37.852  1.00 27.55 ? 240 ALA   C CB  1 
ATOM   5337 N N   . VAL   C 1 262 ? -8.326  3.653   40.197  1.00 27.51 ? 241 VAL   C N   1 
ATOM   5338 C CA  . VAL   C 1 262 ? -7.395  2.682   40.763  1.00 33.71 ? 241 VAL   C CA  1 
ATOM   5339 C C   . VAL   C 1 262 ? -8.088  1.824   41.818  1.00 31.48 ? 241 VAL   C C   1 
ATOM   5340 O O   . VAL   C 1 262 ? -8.013  0.594   41.801  1.00 31.26 ? 241 VAL   C O   1 
ATOM   5341 C CB  . VAL   C 1 262 ? -6.127  3.336   41.328  1.00 32.38 ? 241 VAL   C CB  1 
ATOM   5342 C CG1 . VAL   C 1 262 ? -5.259  2.305   42.042  1.00 30.85 ? 241 VAL   C CG1 1 
ATOM   5343 C CG2 . VAL   C 1 262 ? -5.336  4.032   40.236  1.00 32.06 ? 241 VAL   C CG2 1 
ATOM   5344 N N   . ILE   C 1 263 ? -8.747  2.497   42.763  1.00 35.10 ? 242 ILE   C N   1 
ATOM   5345 C CA  . ILE   C 1 263 ? -9.508  1.849   43.819  1.00 34.06 ? 242 ILE   C CA  1 
ATOM   5346 C C   . ILE   C 1 263 ? -10.506 0.841   43.261  1.00 36.66 ? 242 ILE   C C   1 
ATOM   5347 O O   . ILE   C 1 263 ? -10.619 -0.252  43.803  1.00 29.70 ? 242 ILE   C O   1 
ATOM   5348 C CB  . ILE   C 1 263 ? -10.231 2.903   44.676  1.00 32.71 ? 242 ILE   C CB  1 
ATOM   5349 C CG1 . ILE   C 1 263 ? -9.235  3.802   45.365  1.00 39.37 ? 242 ILE   C CG1 1 
ATOM   5350 C CG2 . ILE   C 1 263 ? -11.204 2.242   45.662  1.00 36.68 ? 242 ILE   C CG2 1 
ATOM   5351 C CD1 . ILE   C 1 263 ? -8.280  3.067   46.287  1.00 39.31 ? 242 ILE   C CD1 1 
ATOM   5352 N N   . PHE   C 1 264 ? -11.270 1.229   42.222  1.00 30.43 ? 243 PHE   C N   1 
ATOM   5353 C CA  . PHE   C 1 264 ? -12.204 0.282   41.630  1.00 30.54 ? 243 PHE   C CA  1 
ATOM   5354 C C   . PHE   C 1 264 ? -11.432 -0.977  41.196  1.00 28.69 ? 243 PHE   C C   1 
ATOM   5355 O O   . PHE   C 1 264 ? -11.798 -2.098  41.558  1.00 31.56 ? 243 PHE   C O   1 
ATOM   5356 C CB  . PHE   C 1 264 ? -13.000 0.961   40.496  1.00 27.00 ? 243 PHE   C CB  1 
ATOM   5357 C CG  . PHE   C 1 264 ? -13.741 -0.090  39.691  1.00 26.28 ? 243 PHE   C CG  1 
ATOM   5358 C CD1 . PHE   C 1 264 ? -14.822 -0.768  40.238  1.00 25.77 ? 243 PHE   C CD1 1 
ATOM   5359 C CD2 . PHE   C 1 264 ? -13.381 -0.365  38.363  1.00 31.40 ? 243 PHE   C CD2 1 
ATOM   5360 C CE1 . PHE   C 1 264 ? -15.519 -1.726  39.498  1.00 32.83 ? 243 PHE   C CE1 1 
ATOM   5361 C CE2 . PHE   C 1 264 ? -14.092 -1.319  37.636  1.00 28.45 ? 243 PHE   C CE2 1 
ATOM   5362 C CZ  . PHE   C 1 264 ? -15.148 -2.008  38.203  1.00 29.58 ? 243 PHE   C CZ  1 
ATOM   5363 N N   . LEU   C 1 265 ? -10.344 -0.793  40.441  1.00 28.45 ? 244 LEU   C N   1 
ATOM   5364 C CA  . LEU   C 1 265 ? -9.699  -1.946  39.810  1.00 28.31 ? 244 LEU   C CA  1 
ATOM   5365 C C   . LEU   C 1 265 ? -9.141  -2.928  40.852  1.00 29.75 ? 244 LEU   C C   1 
ATOM   5366 O O   . LEU   C 1 265 ? -9.071  -4.136  40.601  1.00 27.70 ? 244 LEU   C O   1 
ATOM   5367 C CB  . LEU   C 1 265 ? -8.625  -1.448  38.845  1.00 28.66 ? 244 LEU   C CB  1 
ATOM   5368 C CG  . LEU   C 1 265 ? -9.179  -0.906  37.516  1.00 26.77 ? 244 LEU   C CG  1 
ATOM   5369 C CD1 . LEU   C 1 265 ? -8.085  -0.187  36.738  1.00 26.51 ? 244 LEU   C CD1 1 
ATOM   5370 C CD2 . LEU   C 1 265 ? -9.667  -2.079  36.651  1.00 26.91 ? 244 LEU   C CD2 1 
ATOM   5371 N N   . VAL   C 1 266 ? -8.733  -2.415  42.021  1.00 28.39 ? 245 VAL   C N   1 
ATOM   5372 C CA  . VAL   C 1 266 ? -8.168  -3.299  43.048  1.00 32.20 ? 245 VAL   C CA  1 
ATOM   5373 C C   . VAL   C 1 266 ? -9.251  -4.021  43.871  1.00 33.80 ? 245 VAL   C C   1 
ATOM   5374 O O   . VAL   C 1 266 ? -9.002  -5.064  44.502  1.00 33.61 ? 245 VAL   C O   1 
ATOM   5375 C CB  . VAL   C 1 266 ? -7.073  -2.628  43.910  1.00 33.44 ? 245 VAL   C CB  1 
ATOM   5376 C CG1 . VAL   C 1 266 ? -5.955  -2.035  43.057  1.00 33.61 ? 245 VAL   C CG1 1 
ATOM   5377 C CG2 . VAL   C 1 266 ? -7.580  -1.571  44.871  1.00 33.39 ? 245 VAL   C CG2 1 
ATOM   5378 N N   . SER   C 1 267 ? -10.483 -3.516  43.810  1.00 35.75 ? 246 SER   C N   1 
ATOM   5379 C CA  . SER   C 1 267 ? -11.561 -3.918  44.701  1.00 34.18 ? 246 SER   C CA  1 
ATOM   5380 C C   . SER   C 1 267 ? -12.147 -5.267  44.300  1.00 40.58 ? 246 SER   C C   1 
ATOM   5381 O O   . SER   C 1 267 ? -11.868 -5.804  43.214  1.00 37.23 ? 246 SER   C O   1 
ATOM   5382 C CB  . SER   C 1 267 ? -12.644 -2.855  44.699  1.00 36.05 ? 246 SER   C CB  1 
ATOM   5383 O OG  . SER   C 1 267 ? -13.509 -3.026  43.589  1.00 37.57 ? 246 SER   C OG  1 
ATOM   5384 N N   . GLY   C 1 268 ? -13.010 -5.787  45.180  1.00 37.12 ? 247 GLY   C N   1 
ATOM   5385 C CA  . GLY   C 1 268 ? -13.735 -7.013  44.879  1.00 36.87 ? 247 GLY   C CA  1 
ATOM   5386 C C   . GLY   C 1 268 ? -14.740 -6.787  43.751  1.00 33.08 ? 247 GLY   C C   1 
ATOM   5387 O O   . GLY   C 1 268 ? -15.205 -7.746  43.153  1.00 37.53 ? 247 GLY   C O   1 
ATOM   5388 N N   . SER   C 1 269 ? -15.056 -5.511  43.473  1.00 33.12 ? 248 SER   C N   1 
ATOM   5389 C CA  . SER   C 1 269 ? -15.985 -5.170  42.400  1.00 33.35 ? 248 SER   C CA  1 
ATOM   5390 C C   . SER   C 1 269 ? -15.349 -5.331  41.012  1.00 39.58 ? 248 SER   C C   1 
ATOM   5391 O O   . SER   C 1 269 ? -16.067 -5.219  40.015  1.00 36.21 ? 248 SER   C O   1 
ATOM   5392 C CB  . SER   C 1 269 ? -16.559 -3.787  42.571  1.00 38.00 ? 248 SER   C CB  1 
ATOM   5393 O OG  . SER   C 1 269 ? -17.380 -3.746  43.731  1.00 40.44 ? 248 SER   C OG  1 
ATOM   5394 N N   . ALA   C 1 270 ? -14.029 -5.586  40.952  1.00 29.66 ? 249 ALA   C N   1 
ATOM   5395 C CA  . ALA   C 1 270 ? -13.365 -5.813  39.666  1.00 32.40 ? 249 ALA   C CA  1 
ATOM   5396 C C   . ALA   C 1 270 ? -12.681 -7.181  39.593  1.00 32.13 ? 249 ALA   C C   1 
ATOM   5397 O O   . ALA   C 1 270 ? -11.705 -7.337  38.858  1.00 29.54 ? 249 ALA   C O   1 
ATOM   5398 C CB  . ALA   C 1 270 ? -12.357 -4.714  39.427  1.00 25.43 ? 249 ALA   C CB  1 
ATOM   5399 N N   . GLN   C 1 271 ? -13.228 -8.198  40.283  1.00 32.40 ? 250 GLN   C N   1 
ATOM   5400 C CA  A GLN   C 1 271 ? -12.533 -9.469  40.426  0.50 36.71 ? 250 GLN   C CA  1 
ATOM   5401 C CA  B GLN   C 1 271 ? -12.548 -9.481  40.434  0.50 35.21 ? 250 GLN   C CA  1 
ATOM   5402 C C   . GLN   C 1 271 ? -12.452 -10.227 39.097  1.00 35.21 ? 250 GLN   C C   1 
ATOM   5403 O O   . GLN   C 1 271 ? -11.694 -11.192 38.976  1.00 35.50 ? 250 GLN   C O   1 
ATOM   5404 C CB  A GLN   C 1 271 ? -13.276 -10.330 41.442  0.50 40.02 ? 250 GLN   C CB  1 
ATOM   5405 C CB  B GLN   C 1 271 ? -13.208 -10.348 41.510  0.50 35.47 ? 250 GLN   C CB  1 
ATOM   5406 C CG  A GLN   C 1 271 ? -12.386 -11.264 42.252  0.50 45.81 ? 250 GLN   C CG  1 
ATOM   5407 C CG  B GLN   C 1 271 ? -14.713 -10.513 41.317  0.50 37.79 ? 250 GLN   C CG  1 
ATOM   5408 C CD  A GLN   C 1 271 ? -13.005 -11.550 43.601  0.50 48.31 ? 250 GLN   C CD  1 
ATOM   5409 C CD  B GLN   C 1 271 ? -15.467 -11.141 42.471  0.50 36.55 ? 250 GLN   C CD  1 
ATOM   5410 O OE1 A GLN   C 1 271 ? -12.502 -11.114 44.643  0.50 41.06 ? 250 GLN   C OE1 1 
ATOM   5411 O OE1 B GLN   C 1 271 ? -16.436 -11.876 42.259  0.50 36.33 ? 250 GLN   C OE1 1 
ATOM   5412 N NE2 A GLN   C 1 271 ? -14.152 -12.219 43.569  0.50 46.80 ? 250 GLN   C NE2 1 
ATOM   5413 N NE2 B GLN   C 1 271 ? -15.092 -10.811 43.700  0.50 37.82 ? 250 GLN   C NE2 1 
ATOM   5414 N N   . TYR   C 1 272 ? -13.235 -9.805  38.102  1.00 31.49 ? 251 TYR   C N   1 
ATOM   5415 C CA  . TYR   C 1 272 ? -13.221 -10.492 36.816  1.00 26.83 ? 251 TYR   C CA  1 
ATOM   5416 C C   . TYR   C 1 272 ? -12.490 -9.648  35.766  1.00 28.12 ? 251 TYR   C C   1 
ATOM   5417 O O   . TYR   C 1 272 ? -12.374 -10.085 34.624  1.00 26.64 ? 251 TYR   C O   1 
ATOM   5418 C CB  . TYR   C 1 272 ? -14.638 -10.859 36.348  1.00 29.96 ? 251 TYR   C CB  1 
ATOM   5419 C CG  . TYR   C 1 272 ? -14.695 -11.943 35.285  1.00 29.09 ? 251 TYR   C CG  1 
ATOM   5420 C CD1 . TYR   C 1 272 ? -14.405 -13.269 35.583  1.00 30.57 ? 251 TYR   C CD1 1 
ATOM   5421 C CD2 . TYR   C 1 272 ? -15.023 -11.639 33.957  1.00 29.56 ? 251 TYR   C CD2 1 
ATOM   5422 C CE1 . TYR   C 1 272 ? -14.444 -14.257 34.611  1.00 30.32 ? 251 TYR   C CE1 1 
ATOM   5423 C CE2 . TYR   C 1 272 ? -15.056 -12.620 32.973  1.00 26.37 ? 251 TYR   C CE2 1 
ATOM   5424 C CZ  . TYR   C 1 272 ? -14.759 -13.934 33.297  1.00 29.56 ? 251 TYR   C CZ  1 
ATOM   5425 O OH  . TYR   C 1 272 ? -14.857 -14.905 32.328  1.00 27.34 ? 251 TYR   C OH  1 
ATOM   5426 N N   . ILE   C 1 273 ? -12.043 -8.440  36.145  1.00 27.54 ? 252 ILE   C N   1 
ATOM   5427 C CA  . ILE   C 1 273 ? -11.380 -7.518  35.220  1.00 28.95 ? 252 ILE   C CA  1 
ATOM   5428 C C   . ILE   C 1 273 ? -9.858  -7.743  35.221  1.00 30.10 ? 252 ILE   C C   1 
ATOM   5429 O O   . ILE   C 1 273 ? -9.187  -7.531  36.246  1.00 29.77 ? 252 ILE   C O   1 
ATOM   5430 C CB  . ILE   C 1 273 ? -11.788 -6.062  35.572  1.00 25.26 ? 252 ILE   C CB  1 
ATOM   5431 C CG1 . ILE   C 1 273 ? -13.324 -5.863  35.562  1.00 24.71 ? 252 ILE   C CG1 1 
ATOM   5432 C CG2 . ILE   C 1 273 ? -11.072 -5.049  34.665  1.00 26.25 ? 252 ILE   C CG2 1 
ATOM   5433 C CD1 . ILE   C 1 273 ? -13.783 -4.451  35.949  1.00 23.28 ? 252 ILE   C CD1 1 
ATOM   5434 N N   . THR   C 1 274 ? -9.277  -8.126  34.050  1.00 22.39 ? 253 THR   C N   1 
ATOM   5435 C CA  . THR   C 1 274 ? -7.836  -8.100  33.833  1.00 25.27 ? 253 THR   C CA  1 
ATOM   5436 C C   . THR   C 1 274 ? -7.575  -7.787  32.350  1.00 23.83 ? 253 THR   C C   1 
ATOM   5437 O O   . THR   C 1 274 ? -8.398  -8.119  31.495  1.00 25.43 ? 253 THR   C O   1 
ATOM   5438 C CB  . THR   C 1 274 ? -7.170  -9.410  34.279  1.00 26.10 ? 253 THR   C CB  1 
ATOM   5439 O OG1 . THR   C 1 274 ? -5.760  -9.217  34.306  1.00 26.43 ? 253 THR   C OG1 1 
ATOM   5440 C CG2 . THR   C 1 274 ? -7.564  -10.603 33.419  1.00 27.57 ? 253 THR   C CG2 1 
ATOM   5441 N N   . GLY   C 1 275 ? -6.488  -7.063  32.101  1.00 23.14 ? 254 GLY   C N   1 
ATOM   5442 C CA  . GLY   C 1 275 ? -6.088  -6.609  30.776  1.00 26.76 ? 254 GLY   C CA  1 
ATOM   5443 C C   . GLY   C 1 275 ? -6.897  -5.414  30.270  1.00 29.30 ? 254 GLY   C C   1 
ATOM   5444 O O   . GLY   C 1 275 ? -6.893  -5.115  29.067  1.00 27.03 ? 254 GLY   C O   1 
ATOM   5445 N N   . SER   C 1 276 ? -7.604  -4.737  31.176  1.00 26.63 ? 255 SER   C N   1 
ATOM   5446 C CA  . SER   C 1 276 ? -8.454  -3.614  30.802  1.00 24.37 ? 255 SER   C CA  1 
ATOM   5447 C C   . SER   C 1 276 ? -7.747  -2.329  31.178  1.00 25.19 ? 255 SER   C C   1 
ATOM   5448 O O   . SER   C 1 276 ? -7.102  -2.292  32.215  1.00 28.51 ? 255 SER   C O   1 
ATOM   5449 C CB  . SER   C 1 276 ? -9.786  -3.669  31.490  1.00 25.95 ? 255 SER   C CB  1 
ATOM   5450 O OG  . SER   C 1 276 ? -10.607 -4.755  31.072  1.00 31.13 ? 255 SER   C OG  1 
ATOM   5451 N N   . ILE   C 1 277 ? -7.865  -1.314  30.311  1.00 23.29 ? 256 ILE   C N   1 
ATOM   5452 C CA  . ILE   C 1 277 ? -7.338  0.016   30.578  1.00 23.84 ? 256 ILE   C CA  1 
ATOM   5453 C C   . ILE   C 1 277 ? -8.525  0.969   30.575  1.00 26.32 ? 256 ILE   C C   1 
ATOM   5454 O O   . ILE   C 1 277 ? -9.208  1.076   29.568  1.00 26.06 ? 256 ILE   C O   1 
ATOM   5455 C CB  . ILE   C 1 277 ? -6.262  0.435   29.559  1.00 24.82 ? 256 ILE   C CB  1 
ATOM   5456 C CG1 . ILE   C 1 277 ? -5.049  -0.519  29.633  1.00 28.97 ? 256 ILE   C CG1 1 
ATOM   5457 C CG2 . ILE   C 1 277 ? -5.847  1.893   29.824  1.00 25.52 ? 256 ILE   C CG2 1 
ATOM   5458 C CD1 . ILE   C 1 277 ? -4.044  -0.313  28.513  1.00 28.00 ? 256 ILE   C CD1 1 
ATOM   5459 N N   . ILE   C 1 278 ? -8.762  1.621   31.718  1.00 25.23 ? 257 ILE   C N   1 
ATOM   5460 C CA  . ILE   C 1 278 ? -9.886  2.516   31.853  1.00 22.69 ? 257 ILE   C CA  1 
ATOM   5461 C C   . ILE   C 1 278 ? -9.386  3.929   31.614  1.00 25.00 ? 257 ILE   C C   1 
ATOM   5462 O O   . ILE   C 1 278 ? -8.529  4.412   32.380  1.00 23.37 ? 257 ILE   C O   1 
ATOM   5463 C CB  . ILE   C 1 278 ? -10.465 2.404   33.274  1.00 26.20 ? 257 ILE   C CB  1 
ATOM   5464 C CG1 . ILE   C 1 278 ? -10.906 0.950   33.609  1.00 28.81 ? 257 ILE   C CG1 1 
ATOM   5465 C CG2 . ILE   C 1 278 ? -11.611 3.411   33.435  1.00 28.82 ? 257 ILE   C CG2 1 
ATOM   5466 C CD1 . ILE   C 1 278 ? -11.505 0.807   35.011  1.00 33.83 ? 257 ILE   C CD1 1 
ATOM   5467 N N   . LYS   C 1 279 ? -9.953  4.606   30.587  1.00 23.36 ? 258 LYS   C N   1 
ATOM   5468 C CA  . LYS   C 1 279 ? -9.606  6.007   30.379  1.00 23.97 ? 258 LYS   C CA  1 
ATOM   5469 C C   . LYS   C 1 279 ? -10.338 6.821   31.435  1.00 21.25 ? 258 LYS   C C   1 
ATOM   5470 O O   . LYS   C 1 279 ? -11.517 6.584   31.717  1.00 23.26 ? 258 LYS   C O   1 
ATOM   5471 C CB  . LYS   C 1 279 ? -10.056 6.692   29.070  1.00 25.91 ? 258 LYS   C CB  1 
ATOM   5472 C CG  . LYS   C 1 279 ? -9.406  6.182   27.805  1.00 31.10 ? 258 LYS   C CG  1 
ATOM   5473 C CD  . LYS   C 1 279 ? -10.045 6.819   26.562  1.00 27.97 ? 258 LYS   C CD  1 
ATOM   5474 C CE  . LYS   C 1 279 ? -11.455 6.340   26.274  1.00 29.92 ? 258 LYS   C CE  1 
ATOM   5475 N NZ  . LYS   C 1 279 ? -12.146 6.939   25.092  1.00 26.37 ? 258 LYS   C NZ  1 
ATOM   5476 N N   . VAL   C 1 280 ? -9.638  7.823   31.980  1.00 24.18 ? 259 VAL   C N   1 
ATOM   5477 C CA  . VAL   C 1 280 ? -10.264 8.792   32.868  1.00 24.34 ? 259 VAL   C CA  1 
ATOM   5478 C C   . VAL   C 1 280 ? -9.862  10.177  32.364  1.00 24.60 ? 259 VAL   C C   1 
ATOM   5479 O O   . VAL   C 1 280 ? -8.888  10.735  32.855  1.00 26.03 ? 259 VAL   C O   1 
ATOM   5480 C CB  . VAL   C 1 280 ? -9.816  8.569   34.328  1.00 24.09 ? 259 VAL   C CB  1 
ATOM   5481 C CG1 . VAL   C 1 280 ? -10.515 9.548   35.269  1.00 24.85 ? 259 VAL   C CG1 1 
ATOM   5482 C CG2 . VAL   C 1 280 ? -10.073 7.128   34.752  1.00 25.13 ? 259 VAL   C CG2 1 
ATOM   5483 N N   . ASP   C 1 281 ? -10.551 10.662  31.317  1.00 24.50 ? 260 ASP   C N   1 
ATOM   5484 C CA  . ASP   C 1 281 ? -10.053 11.771  30.526  1.00 22.71 ? 260 ASP   C CA  1 
ATOM   5485 C C   . ASP   C 1 281 ? -11.148 12.788  30.186  1.00 20.16 ? 260 ASP   C C   1 
ATOM   5486 O O   . ASP   C 1 281 ? -10.879 13.693  29.398  1.00 22.41 ? 260 ASP   C O   1 
ATOM   5487 C CB  . ASP   C 1 281 ? -9.432  11.280  29.226  1.00 24.49 ? 260 ASP   C CB  1 
ATOM   5488 C CG  . ASP   C 1 281 ? -10.378 10.776  28.135  1.00 26.17 ? 260 ASP   C CG  1 
ATOM   5489 O OD1 . ASP   C 1 281 ? -11.571 10.499  28.406  1.00 25.95 ? 260 ASP   C OD1 1 
ATOM   5490 O OD2 . ASP   C 1 281 ? -9.903  10.653  26.990  1.00 26.24 ? 260 ASP   C OD2 1 
ATOM   5491 N N   . GLY   C 1 282 ? -12.342 12.631  30.764  1.00 26.08 ? 261 GLY   C N   1 
ATOM   5492 C CA  . GLY   C 1 282 ? -13.474 13.534  30.515  1.00 23.09 ? 261 GLY   C CA  1 
ATOM   5493 C C   . GLY   C 1 282 ? -13.827 13.685  29.030  1.00 25.40 ? 261 GLY   C C   1 
ATOM   5494 O O   . GLY   C 1 282 ? -14.289 14.747  28.609  1.00 24.26 ? 261 GLY   C O   1 
ATOM   5495 N N   . GLY   C 1 283 ? -13.510 12.660  28.213  1.00 20.33 ? 262 GLY   C N   1 
ATOM   5496 C CA  . GLY   C 1 283 ? -13.817 12.680  26.792  1.00 20.96 ? 262 GLY   C CA  1 
ATOM   5497 C C   . GLY   C 1 283 ? -12.737 13.316  25.924  1.00 20.59 ? 262 GLY   C C   1 
ATOM   5498 O O   . GLY   C 1 283 ? -12.931 13.433  24.725  1.00 21.75 ? 262 GLY   C O   1 
ATOM   5499 N N   . LEU   C 1 284 ? -11.596 13.731  26.514  1.00 21.40 ? 263 LEU   C N   1 
ATOM   5500 C CA  . LEU   C 1 284 ? -10.594 14.485  25.766  1.00 21.35 ? 263 LEU   C CA  1 
ATOM   5501 C C   . LEU   C 1 284 ? -10.154 13.709  24.512  1.00 19.76 ? 263 LEU   C C   1 
ATOM   5502 O O   . LEU   C 1 284 ? -9.983  14.270  23.429  1.00 20.93 ? 263 LEU   C O   1 
ATOM   5503 C CB  . LEU   C 1 284 ? -9.370  14.800  26.650  1.00 22.71 ? 263 LEU   C CB  1 
ATOM   5504 C CG  . LEU   C 1 284 ? -8.202  15.462  25.903  1.00 26.35 ? 263 LEU   C CG  1 
ATOM   5505 C CD1 . LEU   C 1 284 ? -8.522  16.857  25.367  1.00 27.67 ? 263 LEU   C CD1 1 
ATOM   5506 C CD2 . LEU   C 1 284 ? -6.976  15.504  26.824  1.00 33.86 ? 263 LEU   C CD2 1 
ATOM   5507 N N   . SER   C 1 285 ? -9.923  12.391  24.655  1.00 22.23 ? 264 SER   C N   1 
ATOM   5508 C CA  . SER   C 1 285 ? -9.437  11.608  23.522  1.00 22.97 ? 264 SER   C CA  1 
ATOM   5509 C C   . SER   C 1 285 ? -10.440 11.447  22.360  1.00 23.25 ? 264 SER   C C   1 
ATOM   5510 O O   . SER   C 1 285 ? -10.036 11.018  21.272  1.00 24.21 ? 264 SER   C O   1 
ATOM   5511 C CB  . SER   C 1 285 ? -8.981  10.244  23.973  1.00 23.20 ? 264 SER   C CB  1 
ATOM   5512 O OG  . SER   C 1 285 ? -10.089 9.525   24.487  1.00 25.11 ? 264 SER   C OG  1 
ATOM   5513 N N   . LEU   C 1 286 ? -11.725 11.768  22.571  1.00 23.58 ? 265 LEU   C N   1 
ATOM   5514 C CA  . LEU   C 1 286 ? -12.755 11.754  21.532  1.00 23.72 ? 265 LEU   C CA  1 
ATOM   5515 C C   . LEU   C 1 286 ? -12.766 13.022  20.674  1.00 25.06 ? 265 LEU   C C   1 
ATOM   5516 O O   . LEU   C 1 286 ? -13.499 13.058  19.676  1.00 24.87 ? 265 LEU   C O   1 
ATOM   5517 C CB  . LEU   C 1 286 ? -14.120 11.649  22.224  1.00 22.02 ? 265 LEU   C CB  1 
ATOM   5518 C CG  . LEU   C 1 286 ? -14.268 10.456  23.174  1.00 28.49 ? 265 LEU   C CG  1 
ATOM   5519 C CD1 . LEU   C 1 286 ? -15.635 10.596  23.812  1.00 31.45 ? 265 LEU   C CD1 1 
ATOM   5520 C CD2 . LEU   C 1 286 ? -14.065 9.071   22.559  1.00 28.26 ? 265 LEU   C CD2 1 
ATOM   5521 N N   . VAL   C 1 287 ? -12.003 14.068  21.041  1.00 25.84 ? 266 VAL   C N   1 
ATOM   5522 C CA  . VAL   C 1 287 ? -12.140 15.353  20.347  1.00 23.43 ? 266 VAL   C CA  1 
ATOM   5523 C C   . VAL   C 1 287 ? -11.190 15.420  19.137  1.00 24.33 ? 266 VAL   C C   1 
ATOM   5524 O O   . VAL   C 1 287 ? -9.977  15.268  19.287  1.00 28.72 ? 266 VAL   C O   1 
ATOM   5525 C CB  . VAL   C 1 287 ? -11.843 16.505  21.328  1.00 24.95 ? 266 VAL   C CB  1 
ATOM   5526 C CG1 . VAL   C 1 287 ? -11.939 17.896  20.675  1.00 27.31 ? 266 VAL   C CG1 1 
ATOM   5527 C CG2 . VAL   C 1 287 ? -12.759 16.414  22.559  1.00 26.35 ? 266 VAL   C CG2 1 
ATOM   5528 N N   . HIS   C 1 288 ? -11.722 15.708  17.941  1.00 26.53 ? 267 HIS   C N   1 
ATOM   5529 C CA  . HIS   C 1 288 ? -10.861 15.786  16.773  1.00 28.08 ? 267 HIS   C CA  1 
ATOM   5530 C C   . HIS   C 1 288 ? -10.065 17.086  16.774  1.00 32.12 ? 267 HIS   C C   1 
ATOM   5531 O O   . HIS   C 1 288 ? -10.362 18.011  17.527  1.00 32.99 ? 267 HIS   C O   1 
ATOM   5532 C CB  . HIS   C 1 288 ? -11.629 15.592  15.457  1.00 30.87 ? 267 HIS   C CB  1 
ATOM   5533 C CG  . HIS   C 1 288 ? -12.669 16.642  15.213  1.00 33.54 ? 267 HIS   C CG  1 
ATOM   5534 N ND1 . HIS   C 1 288 ? -12.330 17.948  14.919  1.00 33.30 ? 267 HIS   C ND1 1 
ATOM   5535 C CD2 . HIS   C 1 288 ? -14.016 16.597  15.261  1.00 32.74 ? 267 HIS   C CD2 1 
ATOM   5536 C CE1 . HIS   C 1 288 ? -13.435 18.670  14.780  1.00 35.66 ? 267 HIS   C CE1 1 
ATOM   5537 N NE2 . HIS   C 1 288 ? -14.482 17.867  14.982  1.00 37.68 ? 267 HIS   C NE2 1 
ATOM   5538 N N   . ALA   C 1 289 ? -9.057  17.129  15.889  1.00 32.35 ? 268 ALA   C N   1 
ATOM   5539 C CA  . ALA   C 1 289 ? -8.195  18.284  15.685  1.00 36.39 ? 268 ALA   C CA  1 
ATOM   5540 C C   . ALA   C 1 289 ? -9.024  19.524  15.314  1.00 35.08 ? 268 ALA   C C   1 
ATOM   5541 O O   . ALA   C 1 289 ? -8.569  20.632  15.661  1.00 40.12 ? 268 ALA   C O   1 
ATOM   5542 C CB  . ALA   C 1 289 ? -7.208  17.960  14.588  1.00 39.10 ? 268 ALA   C CB  1 
ATOM   5543 O OXT . ALA   C 1 289 ? -10.069 19.351  14.665  1.00 35.79 ? 268 ALA   C OXT 1 
ATOM   5544 N N   . GLU   D 1 23  ? -35.357 13.047  46.980  1.00 65.75 ? 2   GLU   D N   1 
ATOM   5545 C CA  . GLU   D 1 23  ? -35.871 11.776  46.401  1.00 64.50 ? 2   GLU   D CA  1 
ATOM   5546 C C   . GLU   D 1 23  ? -34.689 10.923  45.927  1.00 61.72 ? 2   GLU   D C   1 
ATOM   5547 O O   . GLU   D 1 23  ? -33.593 11.430  45.702  1.00 59.86 ? 2   GLU   D O   1 
ATOM   5548 C CB  . GLU   D 1 23  ? -36.943 12.054  45.340  1.00 66.96 ? 2   GLU   D CB  1 
ATOM   5549 C CG  . GLU   D 1 23  ? -38.309 11.458  45.683  1.00 60.38 ? 2   GLU   D CG  1 
ATOM   5550 N N   . ALA   D 1 24  ? -34.915 9.605   45.840  1.00 57.92 ? 3   ALA   D N   1 
ATOM   5551 C CA  . ALA   D 1 24  ? -33.941 8.667   45.311  1.00 42.95 ? 3   ALA   D CA  1 
ATOM   5552 C C   . ALA   D 1 24  ? -33.850 8.846   43.788  1.00 45.91 ? 3   ALA   D C   1 
ATOM   5553 O O   . ALA   D 1 24  ? -34.844 9.134   43.132  1.00 41.90 ? 3   ALA   D O   1 
ATOM   5554 C CB  . ALA   D 1 24  ? -34.364 7.260   45.690  1.00 38.52 ? 3   ALA   D CB  1 
ATOM   5555 N N   . PRO   D 1 25  ? -32.655 8.705   43.164  1.00 42.94 ? 4   PRO   D N   1 
ATOM   5556 C CA  . PRO   D 1 25  ? -32.553 8.778   41.693  1.00 36.79 ? 4   PRO   D CA  1 
ATOM   5557 C C   . PRO   D 1 25  ? -33.258 7.587   41.039  1.00 39.54 ? 4   PRO   D C   1 
ATOM   5558 O O   . PRO   D 1 25  ? -33.553 6.603   41.722  1.00 42.14 ? 4   PRO   D O   1 
ATOM   5559 C CB  . PRO   D 1 25  ? -31.036 8.788   41.457  1.00 38.96 ? 4   PRO   D CB  1 
ATOM   5560 C CG  . PRO   D 1 25  ? -30.473 8.052   42.679  1.00 45.62 ? 4   PRO   D CG  1 
ATOM   5561 C CD  . PRO   D 1 25  ? -31.373 8.470   43.853  1.00 38.12 ? 4   PRO   D CD  1 
ATOM   5562 N N   . ALA   D 1 26  ? -33.529 7.667   39.720  1.00 33.54 ? 5   ALA   D N   1 
ATOM   5563 C CA  . ALA   D 1 26  ? -34.241 6.596   39.035  1.00 33.60 ? 5   ALA   D CA  1 
ATOM   5564 C C   . ALA   D 1 26  ? -33.438 6.124   37.816  1.00 34.64 ? 5   ALA   D C   1 
ATOM   5565 O O   . ALA   D 1 26  ? -32.753 6.921   37.184  1.00 31.16 ? 5   ALA   D O   1 
ATOM   5566 C CB  . ALA   D 1 26  ? -35.611 7.068   38.610  1.00 30.98 ? 5   ALA   D CB  1 
ATOM   5567 N N   . ALA   D 1 27  ? -33.580 4.840   37.483  1.00 32.38 ? 6   ALA   D N   1 
ATOM   5568 C CA  . ALA   D 1 27  ? -32.835 4.266   36.362  1.00 34.98 ? 6   ALA   D CA  1 
ATOM   5569 C C   . ALA   D 1 27  ? -33.761 3.444   35.476  1.00 35.06 ? 6   ALA   D C   1 
ATOM   5570 O O   . ALA   D 1 27  ? -34.716 2.843   35.953  1.00 34.22 ? 6   ALA   D O   1 
ATOM   5571 C CB  . ALA   D 1 27  ? -31.666 3.455   36.856  1.00 29.36 ? 6   ALA   D CB  1 
ATOM   5572 N N   . VAL   D 1 28  ? -33.503 3.467   34.153  1.00 30.07 ? 7   VAL   D N   1 
ATOM   5573 C CA  . VAL   D 1 28  ? -34.141 2.525   33.239  1.00 28.02 ? 7   VAL   D CA  1 
ATOM   5574 C C   . VAL   D 1 28  ? -33.089 1.490   32.864  1.00 29.13 ? 7   VAL   D C   1 
ATOM   5575 O O   . VAL   D 1 28  ? -31.952 1.858   32.516  1.00 26.44 ? 7   VAL   D O   1 
ATOM   5576 C CB  . VAL   D 1 28  ? -34.656 3.217   31.952  1.00 32.22 ? 7   VAL   D CB  1 
ATOM   5577 C CG1 . VAL   D 1 28  ? -35.110 2.209   30.872  1.00 25.77 ? 7   VAL   D CG1 1 
ATOM   5578 C CG2 . VAL   D 1 28  ? -35.734 4.247   32.249  1.00 31.36 ? 7   VAL   D CG2 1 
ATOM   5579 N N   . VAL   D 1 29  ? -33.474 0.210   32.962  1.00 26.14 ? 8   VAL   D N   1 
ATOM   5580 C CA  . VAL   D 1 29  ? -32.643 -0.896  32.494  1.00 29.89 ? 8   VAL   D CA  1 
ATOM   5581 C C   . VAL   D 1 29  ? -33.449 -1.631  31.426  1.00 31.77 ? 8   VAL   D C   1 
ATOM   5582 O O   . VAL   D 1 29  ? -34.536 -2.136  31.711  1.00 29.29 ? 8   VAL   D O   1 
ATOM   5583 C CB  . VAL   D 1 29  ? -32.229 -1.866  33.627  1.00 30.44 ? 8   VAL   D CB  1 
ATOM   5584 C CG1 . VAL   D 1 29  ? -31.334 -3.008  33.132  1.00 31.94 ? 8   VAL   D CG1 1 
ATOM   5585 C CG2 . VAL   D 1 29  ? -31.571 -1.152  34.790  1.00 29.17 ? 8   VAL   D CG2 1 
ATOM   5586 N N   . THR   D 1 30  ? -32.918 -1.721  30.186  1.00 27.83 ? 9   THR   D N   1 
ATOM   5587 C CA  . THR   D 1 30  ? -33.660 -2.429  29.156  1.00 25.93 ? 9   THR   D CA  1 
ATOM   5588 C C   . THR   D 1 30  ? -33.339 -3.909  29.248  1.00 24.72 ? 9   THR   D C   1 
ATOM   5589 O O   . THR   D 1 30  ? -32.281 -4.262  29.745  1.00 26.54 ? 9   THR   D O   1 
ATOM   5590 C CB  . THR   D 1 30  ? -33.396 -1.911  27.747  1.00 27.78 ? 9   THR   D CB  1 
ATOM   5591 O OG1 . THR   D 1 30  ? -31.999 -2.081  27.463  1.00 25.56 ? 9   THR   D OG1 1 
ATOM   5592 C CG2 . THR   D 1 30  ? -33.876 -0.481  27.568  1.00 26.25 ? 9   THR   D CG2 1 
ATOM   5593 N N   . GLY   D 1 31  ? -34.306 -4.763  28.853  1.00 24.97 ? 10  GLY   D N   1 
ATOM   5594 C CA  . GLY   D 1 31  ? -34.110 -6.211  28.950  1.00 27.59 ? 10  GLY   D CA  1 
ATOM   5595 C C   . GLY   D 1 31  ? -33.756 -6.686  30.368  1.00 28.55 ? 10  GLY   D C   1 
ATOM   5596 O O   . GLY   D 1 31  ? -32.844 -7.489  30.575  1.00 29.45 ? 10  GLY   D O   1 
ATOM   5597 N N   . ALA   D 1 32  ? -34.471 -6.158  31.377  1.00 29.39 ? 11  ALA   D N   1 
ATOM   5598 C CA  . ALA   D 1 32  ? -34.043 -6.332  32.763  1.00 28.80 ? 11  ALA   D CA  1 
ATOM   5599 C C   . ALA   D 1 32  ? -34.776 -7.470  33.500  1.00 34.23 ? 11  ALA   D C   1 
ATOM   5600 O O   . ALA   D 1 32  ? -34.579 -7.640  34.710  1.00 32.60 ? 11  ALA   D O   1 
ATOM   5601 C CB  . ALA   D 1 32  ? -34.225 -5.001  33.494  1.00 33.55 ? 11  ALA   D CB  1 
ATOM   5602 N N   . ALA   D 1 33  ? -35.568 -8.293  32.802  1.00 32.96 ? 12  ALA   D N   1 
ATOM   5603 C CA  . ALA   D 1 33  ? -36.334 -9.322  33.509  1.00 35.59 ? 12  ALA   D CA  1 
ATOM   5604 C C   . ALA   D 1 33  ? -35.459 -10.496 33.932  1.00 44.17 ? 12  ALA   D C   1 
ATOM   5605 O O   . ALA   D 1 33  ? -35.770 -11.181 34.912  1.00 44.85 ? 12  ALA   D O   1 
ATOM   5606 C CB  . ALA   D 1 33  ? -37.528 -9.802  32.708  1.00 34.68 ? 12  ALA   D CB  1 
ATOM   5607 N N   . LYS   D 1 34  ? -34.376 -10.740 33.189  1.00 40.03 ? 13  LYS   D N   1 
ATOM   5608 C CA  . LYS   D 1 34  ? -33.619 -11.963 33.388  1.00 39.84 ? 13  LYS   D CA  1 
ATOM   5609 C C   . LYS   D 1 34  ? -32.127 -11.644 33.289  1.00 40.94 ? 13  LYS   D C   1 
ATOM   5610 O O   . LYS   D 1 34  ? -31.759 -10.555 32.846  1.00 36.50 ? 13  LYS   D O   1 
ATOM   5611 C CB  . LYS   D 1 34  ? -33.974 -12.935 32.249  1.00 44.96 ? 13  LYS   D CB  1 
ATOM   5612 C CG  . LYS   D 1 34  ? -35.322 -13.637 32.325  1.00 49.82 ? 13  LYS   D CG  1 
ATOM   5613 C CD  . LYS   D 1 34  ? -35.651 -14.601 31.187  1.00 48.74 ? 13  LYS   D CD  1 
ATOM   5614 N N   . ARG   D 1 35  ? -31.290 -12.600 33.713  1.00 38.30 ? 14  ARG   D N   1 
ATOM   5615 C CA  . ARG   D 1 35  ? -29.853 -12.659 33.414  1.00 34.79 ? 14  ARG   D CA  1 
ATOM   5616 C C   . ARG   D 1 35  ? -29.139 -11.360 33.777  1.00 37.30 ? 14  ARG   D C   1 
ATOM   5617 O O   . ARG   D 1 35  ? -29.231 -10.888 34.913  1.00 32.40 ? 14  ARG   D O   1 
ATOM   5618 C CB  . ARG   D 1 35  ? -29.687 -13.092 31.955  1.00 37.07 ? 14  ARG   D CB  1 
ATOM   5619 C CG  . ARG   D 1 35  ? -30.239 -14.499 31.791  1.00 38.22 ? 14  ARG   D CG  1 
ATOM   5620 C CD  . ARG   D 1 35  ? -30.526 -14.844 30.336  1.00 44.18 ? 14  ARG   D CD  1 
ATOM   5621 N NE  . ARG   D 1 35  ? -29.336 -14.747 29.478  1.00 44.11 ? 14  ARG   D NE  1 
ATOM   5622 C CZ  . ARG   D 1 35  ? -28.274 -15.574 29.432  1.00 51.96 ? 14  ARG   D CZ  1 
ATOM   5623 N NH1 . ARG   D 1 35  ? -28.171 -16.638 30.220  1.00 38.26 ? 14  ARG   D NH1 1 
ATOM   5624 N NH2 . ARG   D 1 35  ? -27.305 -15.332 28.558  1.00 52.33 ? 14  ARG   D NH2 1 
ATOM   5625 N N   . ILE   D 1 36  ? -28.388 -10.780 32.823  1.00 31.33 ? 15  ILE   D N   1 
ATOM   5626 C CA  . ILE   D 1 36  ? -27.531 -9.665  33.205  1.00 27.54 ? 15  ILE   D CA  1 
ATOM   5627 C C   . ILE   D 1 36  ? -28.357 -8.408  33.527  1.00 25.24 ? 15  ILE   D C   1 
ATOM   5628 O O   . ILE   D 1 36  ? -28.022 -7.666  34.459  1.00 27.43 ? 15  ILE   D O   1 
ATOM   5629 C CB  . ILE   D 1 36  ? -26.416 -9.418  32.157  1.00 27.47 ? 15  ILE   D CB  1 
ATOM   5630 C CG1 . ILE   D 1 36  ? -25.377 -10.519 32.225  1.00 35.98 ? 15  ILE   D CG1 1 
ATOM   5631 C CG2 . ILE   D 1 36  ? -25.730 -8.058  32.346  1.00 24.52 ? 15  ILE   D CG2 1 
ATOM   5632 C CD1 . ILE   D 1 36  ? -24.408 -10.534 31.052  1.00 36.76 ? 15  ILE   D CD1 1 
ATOM   5633 N N   . GLY   D 1 37  ? -29.402 -8.145  32.743  1.00 25.10 ? 16  GLY   D N   1 
ATOM   5634 C CA  . GLY   D 1 37  ? -30.238 -6.953  32.948  1.00 27.94 ? 16  GLY   D CA  1 
ATOM   5635 C C   . GLY   D 1 37  ? -30.886 -6.978  34.345  1.00 31.63 ? 16  GLY   D C   1 
ATOM   5636 O O   . GLY   D 1 37  ? -30.922 -5.970  35.071  1.00 31.56 ? 16  GLY   D O   1 
ATOM   5637 N N   . ARG   D 1 38  ? -31.326 -8.172  34.743  1.00 33.24 ? 17  ARG   D N   1 
ATOM   5638 C CA  . ARG   D 1 38  ? -31.901 -8.319  36.079  1.00 36.26 ? 17  ARG   D CA  1 
ATOM   5639 C C   . ARG   D 1 38  ? -30.862 -7.986  37.157  1.00 33.96 ? 17  ARG   D C   1 
ATOM   5640 O O   . ARG   D 1 38  ? -31.134 -7.223  38.092  1.00 35.53 ? 17  ARG   D O   1 
ATOM   5641 C CB  . ARG   D 1 38  ? -32.481 -9.733  36.213  1.00 39.20 ? 17  ARG   D CB  1 
ATOM   5642 C CG  . ARG   D 1 38  ? -33.116 -9.969  37.582  1.00 36.31 ? 17  ARG   D CG  1 
ATOM   5643 C CD  . ARG   D 1 38  ? -33.491 -11.436 37.781  0.70 37.77 ? 17  ARG   D CD  1 
ATOM   5644 N NE  . ARG   D 1 38  ? -34.530 -11.616 38.809  0.70 40.53 ? 17  ARG   D NE  1 
ATOM   5645 C CZ  . ARG   D 1 38  ? -34.385 -11.481 40.129  0.70 44.44 ? 17  ARG   D CZ  1 
ATOM   5646 N NH1 . ARG   D 1 38  ? -33.200 -11.219 40.669  0.70 38.98 ? 17  ARG   D NH1 1 
ATOM   5647 N NH2 . ARG   D 1 38  ? -35.441 -11.643 40.912  0.70 42.98 ? 17  ARG   D NH2 1 
ATOM   5648 N N   . ALA   D 1 39  ? -29.655 -8.556  37.036  1.00 34.03 ? 18  ALA   D N   1 
ATOM   5649 C CA  . ALA   D 1 39  ? -28.614 -8.316  38.015  1.00 30.34 ? 18  ALA   D CA  1 
ATOM   5650 C C   . ALA   D 1 39  ? -28.282 -6.830  38.120  1.00 35.04 ? 18  ALA   D C   1 
ATOM   5651 O O   . ALA   D 1 39  ? -28.057 -6.336  39.220  1.00 32.82 ? 18  ALA   D O   1 
ATOM   5652 C CB  . ALA   D 1 39  ? -27.380 -9.157  37.761  1.00 29.30 ? 18  ALA   D CB  1 
ATOM   5653 N N   . ILE   D 1 40  ? -28.292 -6.116  36.977  1.00 29.80 ? 19  ILE   D N   1 
ATOM   5654 C CA  . ILE   D 1 40  ? -28.073 -4.678  36.961  1.00 27.17 ? 19  ILE   D CA  1 
ATOM   5655 C C   . ILE   D 1 40  ? -29.198 -3.950  37.715  1.00 29.91 ? 19  ILE   D C   1 
ATOM   5656 O O   . ILE   D 1 40  ? -28.906 -3.015  38.470  1.00 31.41 ? 19  ILE   D O   1 
ATOM   5657 C CB  . ILE   D 1 40  ? -27.912 -4.176  35.507  1.00 28.21 ? 19  ILE   D CB  1 
ATOM   5658 C CG1 . ILE   D 1 40  ? -26.619 -4.751  34.915  1.00 32.31 ? 19  ILE   D CG1 1 
ATOM   5659 C CG2 . ILE   D 1 40  ? -27.891 -2.640  35.452  1.00 29.44 ? 19  ILE   D CG2 1 
ATOM   5660 C CD1 . ILE   D 1 40  ? -26.413 -4.508  33.430  1.00 30.33 ? 19  ILE   D CD1 1 
ATOM   5661 N N   . ALA   D 1 41  ? -30.461 -4.334  37.469  1.00 31.41 ? 20  ALA   D N   1 
ATOM   5662 C CA  . ALA   D 1 41  ? -31.618 -3.695  38.088  1.00 31.60 ? 20  ALA   D CA  1 
ATOM   5663 C C   . ALA   D 1 41  ? -31.554 -3.903  39.603  1.00 34.53 ? 20  ALA   D C   1 
ATOM   5664 O O   . ALA   D 1 41  ? -31.721 -2.947  40.364  1.00 36.39 ? 20  ALA   D O   1 
ATOM   5665 C CB  . ALA   D 1 41  ? -32.909 -4.248  37.510  1.00 32.35 ? 20  ALA   D CB  1 
ATOM   5666 N N   . VAL   D 1 42  ? -31.266 -5.144  40.006  1.00 33.04 ? 21  VAL   D N   1 
ATOM   5667 C CA  . VAL   D 1 42  ? -31.175 -5.532  41.411  1.00 38.02 ? 21  VAL   D CA  1 
ATOM   5668 C C   . VAL   D 1 42  ? -30.124 -4.675  42.110  1.00 39.41 ? 21  VAL   D C   1 
ATOM   5669 O O   . VAL   D 1 42  ? -30.404 -4.002  43.113  1.00 40.17 ? 21  VAL   D O   1 
ATOM   5670 C CB  . VAL   D 1 42  ? -30.857 -7.035  41.561  1.00 36.91 ? 21  VAL   D CB  1 
ATOM   5671 C CG1 . VAL   D 1 42  ? -30.454 -7.387  42.990  1.00 39.00 ? 21  VAL   D CG1 1 
ATOM   5672 C CG2 . VAL   D 1 42  ? -32.019 -7.898  41.096  1.00 40.99 ? 21  VAL   D CG2 1 
ATOM   5673 N N   . LYS   D 1 43  ? -28.917 -4.657  41.522  1.00 39.85 ? 22  LYS   D N   1 
ATOM   5674 C CA  . LYS   D 1 43  ? -27.774 -3.958  42.075  1.00 35.52 ? 22  LYS   D CA  1 
ATOM   5675 C C   . LYS   D 1 43  ? -27.998 -2.442  42.144  1.00 36.18 ? 22  LYS   D C   1 
ATOM   5676 O O   . LYS   D 1 43  ? -27.628 -1.831  43.148  1.00 36.36 ? 22  LYS   D O   1 
ATOM   5677 C CB  . LYS   D 1 43  ? -26.469 -4.474  41.449  1.00 37.33 ? 22  LYS   D CB  1 
ATOM   5678 C CG  . LYS   D 1 43  ? -25.249 -4.186  42.281  1.00 42.12 ? 22  LYS   D CG  1 
ATOM   5679 C CD  . LYS   D 1 43  ? -24.021 -4.964  41.830  1.00 40.26 ? 22  LYS   D CD  1 
ATOM   5680 C CE  . LYS   D 1 43  ? -24.034 -6.434  42.053  1.00 48.74 ? 22  LYS   D CE  1 
ATOM   5681 N NZ  . LYS   D 1 43  ? -23.474 -6.737  43.373  1.00 49.20 ? 22  LYS   D NZ  1 
ATOM   5682 N N   . LEU   D 1 44  ? -28.599 -1.835  41.096  1.00 30.94 ? 23  LEU   D N   1 
ATOM   5683 C CA  . LEU   D 1 44  ? -28.947 -0.418  41.134  1.00 29.87 ? 23  LEU   D CA  1 
ATOM   5684 C C   . LEU   D 1 44  ? -29.922 -0.146  42.295  1.00 34.51 ? 23  LEU   D C   1 
ATOM   5685 O O   . LEU   D 1 44  ? -29.789 0.836   43.047  1.00 34.95 ? 23  LEU   D O   1 
ATOM   5686 C CB  . LEU   D 1 44  ? -29.578 -0.039  39.792  1.00 32.02 ? 23  LEU   D CB  1 
ATOM   5687 C CG  . LEU   D 1 44  ? -28.605 0.137   38.611  1.00 32.95 ? 23  LEU   D CG  1 
ATOM   5688 C CD1 . LEU   D 1 44  ? -29.435 0.288   37.343  1.00 33.58 ? 23  LEU   D CD1 1 
ATOM   5689 C CD2 . LEU   D 1 44  ? -27.694 1.316   38.785  1.00 29.75 ? 23  LEU   D CD2 1 
ATOM   5690 N N   . HIS   D 1 45  ? -30.906 -1.029  42.418  1.00 37.51 ? 24  HIS   D N   1 
ATOM   5691 C CA  . HIS   D 1 45  ? -31.933 -0.910  43.451  1.00 40.04 ? 24  HIS   D CA  1 
ATOM   5692 C C   . HIS   D 1 45  ? -31.273 -0.970  44.829  1.00 39.04 ? 24  HIS   D C   1 
ATOM   5693 O O   . HIS   D 1 45  ? -31.572 -0.163  45.712  1.00 43.60 ? 24  HIS   D O   1 
ATOM   5694 C CB  . HIS   D 1 45  ? -33.030 -1.958  43.228  1.00 35.87 ? 24  HIS   D CB  1 
ATOM   5695 C CG  . HIS   D 1 45  ? -34.230 -1.727  44.089  1.00 45.06 ? 24  HIS   D CG  1 
ATOM   5696 N ND1 . HIS   D 1 45  ? -34.474 -2.431  45.247  1.00 48.56 ? 24  HIS   D ND1 1 
ATOM   5697 C CD2 . HIS   D 1 45  ? -35.236 -0.849  43.968  1.00 47.70 ? 24  HIS   D CD2 1 
ATOM   5698 C CE1 . HIS   D 1 45  ? -35.593 -1.985  45.792  1.00 43.87 ? 24  HIS   D CE1 1 
ATOM   5699 N NE2 . HIS   D 1 45  ? -36.074 -1.026  45.041  1.00 51.48 ? 24  HIS   D NE2 1 
ATOM   5700 N N   . GLN   D 1 46  ? -30.346 -1.909  44.989  1.00 37.66 ? 25  GLN   D N   1 
ATOM   5701 C CA  . GLN   D 1 46  ? -29.622 -2.051  46.243  1.00 39.53 ? 25  GLN   D CA  1 
ATOM   5702 C C   . GLN   D 1 46  ? -28.760 -0.833  46.554  1.00 43.22 ? 25  GLN   D C   1 
ATOM   5703 O O   . GLN   D 1 46  ? -28.385 -0.636  47.704  1.00 45.37 ? 25  GLN   D O   1 
ATOM   5704 C CB  . GLN   D 1 46  ? -28.824 -3.339  46.317  1.00 36.49 ? 25  GLN   D CB  1 
ATOM   5705 C CG  . GLN   D 1 46  ? -29.699 -4.571  46.155  1.00 38.27 ? 25  GLN   D CG  1 
ATOM   5706 C CD  . GLN   D 1 46  ? -28.896 -5.841  46.019  1.00 41.90 ? 25  GLN   D CD  1 
ATOM   5707 O OE1 . GLN   D 1 46  ? -27.704 -5.819  45.688  1.00 46.79 ? 25  GLN   D OE1 1 
ATOM   5708 N NE2 . GLN   D 1 46  ? -29.574 -6.960  46.224  1.00 47.78 ? 25  GLN   D NE2 1 
ATOM   5709 N N   . THR   D 1 47  ? -28.490 0.012   45.555  1.00 43.19 ? 26  THR   D N   1 
ATOM   5710 C CA  . THR   D 1 47  ? -27.642 1.182   45.729  1.00 38.10 ? 26  THR   D CA  1 
ATOM   5711 C C   . THR   D 1 47  ? -28.494 2.401   46.079  1.00 43.01 ? 26  THR   D C   1 
ATOM   5712 O O   . THR   D 1 47  ? -27.957 3.447   46.437  1.00 42.20 ? 26  THR   D O   1 
ATOM   5713 C CB  . THR   D 1 47  ? -26.845 1.402   44.433  1.00 41.58 ? 26  THR   D CB  1 
ATOM   5714 O OG1 . THR   D 1 47  ? -25.772 0.470   44.403  1.00 44.40 ? 26  THR   D OG1 1 
ATOM   5715 C CG2 . THR   D 1 47  ? -26.185 2.765   44.332  1.00 39.97 ? 26  THR   D CG2 1 
ATOM   5716 N N   . GLY   D 1 48  ? -29.818 2.300   45.910  1.00 44.61 ? 27  GLY   D N   1 
ATOM   5717 C CA  . GLY   D 1 48  ? -30.699 3.405   46.269  1.00 41.89 ? 27  GLY   D CA  1 
ATOM   5718 C C   . GLY   D 1 48  ? -31.593 3.868   45.119  1.00 43.52 ? 27  GLY   D C   1 
ATOM   5719 O O   . GLY   D 1 48  ? -32.361 4.810   45.282  1.00 41.66 ? 27  GLY   D O   1 
ATOM   5720 N N   . TYR   D 1 49  ? -31.474 3.237   43.936  1.00 39.88 ? 28  TYR   D N   1 
ATOM   5721 C CA  . TYR   D 1 49  ? -32.209 3.720   42.777  1.00 38.33 ? 28  TYR   D CA  1 
ATOM   5722 C C   . TYR   D 1 49  ? -33.623 3.150   42.766  1.00 32.85 ? 28  TYR   D C   1 
ATOM   5723 O O   . TYR   D 1 49  ? -33.810 1.979   43.109  1.00 35.37 ? 28  TYR   D O   1 
ATOM   5724 C CB  . TYR   D 1 49  ? -31.538 3.271   41.466  1.00 33.01 ? 28  TYR   D CB  1 
ATOM   5725 C CG  . TYR   D 1 49  ? -30.319 4.115   41.146  1.00 31.14 ? 28  TYR   D CG  1 
ATOM   5726 C CD1 . TYR   D 1 49  ? -29.047 3.787   41.635  1.00 34.15 ? 28  TYR   D CD1 1 
ATOM   5727 C CD2 . TYR   D 1 49  ? -30.456 5.256   40.364  1.00 38.73 ? 28  TYR   D CD2 1 
ATOM   5728 C CE1 . TYR   D 1 49  ? -27.940 4.568   41.327  1.00 33.51 ? 28  TYR   D CE1 1 
ATOM   5729 C CE2 . TYR   D 1 49  ? -29.353 6.035   40.037  1.00 34.95 ? 28  TYR   D CE2 1 
ATOM   5730 C CZ  . TYR   D 1 49  ? -28.107 5.688   40.524  1.00 33.38 ? 28  TYR   D CZ  1 
ATOM   5731 O OH  . TYR   D 1 49  ? -27.076 6.521   40.204  1.00 36.53 ? 28  TYR   D OH  1 
ATOM   5732 N N   . ARG   D 1 50  ? -34.561 3.968   42.272  1.00 30.88 ? 29  ARG   D N   1 
ATOM   5733 C CA  . ARG   D 1 50  ? -35.830 3.452   41.758  1.00 33.25 ? 29  ARG   D CA  1 
ATOM   5734 C C   . ARG   D 1 50  ? -35.582 2.946   40.328  1.00 34.79 ? 29  ARG   D C   1 
ATOM   5735 O O   . ARG   D 1 50  ? -34.738 3.521   39.640  1.00 35.71 ? 29  ARG   D O   1 
ATOM   5736 C CB  . ARG   D 1 50  ? -36.920 4.523   41.860  1.00 37.10 ? 29  ARG   D CB  1 
ATOM   5737 C CG  . ARG   D 1 50  ? -37.146 4.858   43.334  1.00 38.72 ? 29  ARG   D CG  1 
ATOM   5738 C CD  . ARG   D 1 50  ? -38.091 6.008   43.501  1.00 39.76 ? 29  ARG   D CD  1 
ATOM   5739 N NE  . ARG   D 1 50  ? -37.532 7.313   43.134  1.00 41.63 ? 29  ARG   D NE  1 
ATOM   5740 C CZ  . ARG   D 1 50  ? -38.273 8.413   43.038  1.00 44.26 ? 29  ARG   D CZ  1 
ATOM   5741 N NH1 . ARG   D 1 50  ? -39.586 8.317   43.187  1.00 43.27 ? 29  ARG   D NH1 1 
ATOM   5742 N NH2 . ARG   D 1 50  ? -37.710 9.591   42.795  1.00 47.59 ? 29  ARG   D NH2 1 
ATOM   5743 N N   . VAL   D 1 51  ? -36.257 1.861   39.925  1.00 35.33 ? 30  VAL   D N   1 
ATOM   5744 C CA  . VAL   D 1 51  ? -35.943 1.182   38.664  1.00 34.87 ? 30  VAL   D CA  1 
ATOM   5745 C C   . VAL   D 1 51  ? -37.167 0.992   37.762  1.00 37.16 ? 30  VAL   D C   1 
ATOM   5746 O O   . VAL   D 1 51  ? -38.252 0.602   38.218  1.00 39.61 ? 30  VAL   D O   1 
ATOM   5747 C CB  . VAL   D 1 51  ? -35.176 -0.138  38.864  1.00 33.84 ? 30  VAL   D CB  1 
ATOM   5748 C CG1 . VAL   D 1 51  ? -33.884 0.054   39.664  1.00 37.44 ? 30  VAL   D CG1 1 
ATOM   5749 C CG2 . VAL   D 1 51  ? -36.038 -1.227  39.483  1.00 34.85 ? 30  VAL   D CG2 1 
ATOM   5750 N N   . VAL   D 1 52  ? -36.986 1.275   36.455  1.00 30.75 ? 31  VAL   D N   1 
ATOM   5751 C CA  . VAL   D 1 52  ? -37.903 0.830   35.414  1.00 33.18 ? 31  VAL   D CA  1 
ATOM   5752 C C   . VAL   D 1 52  ? -37.300 -0.420  34.799  1.00 33.54 ? 31  VAL   D C   1 
ATOM   5753 O O   . VAL   D 1 52  ? -36.172 -0.374  34.272  1.00 31.29 ? 31  VAL   D O   1 
ATOM   5754 C CB  . VAL   D 1 52  ? -38.161 1.876   34.310  1.00 29.97 ? 31  VAL   D CB  1 
ATOM   5755 C CG1 . VAL   D 1 52  ? -38.999 1.297   33.172  1.00 33.49 ? 31  VAL   D CG1 1 
ATOM   5756 C CG2 . VAL   D 1 52  ? -38.824 3.140   34.829  1.00 32.35 ? 31  VAL   D CG2 1 
ATOM   5757 N N   . ILE   D 1 53  ? -38.043 -1.526  34.926  1.00 32.42 ? 32  ILE   D N   1 
ATOM   5758 C CA  . ILE   D 1 53  ? -37.674 -2.824  34.386  1.00 31.83 ? 32  ILE   D CA  1 
ATOM   5759 C C   . ILE   D 1 53  ? -38.327 -2.990  33.026  1.00 35.24 ? 32  ILE   D C   1 
ATOM   5760 O O   . ILE   D 1 53  ? -39.516 -3.293  32.937  1.00 33.29 ? 32  ILE   D O   1 
ATOM   5761 C CB  . ILE   D 1 53  ? -38.127 -3.930  35.351  1.00 35.73 ? 32  ILE   D CB  1 
ATOM   5762 C CG1 . ILE   D 1 53  ? -37.517 -3.735  36.732  1.00 33.24 ? 32  ILE   D CG1 1 
ATOM   5763 C CG2 . ILE   D 1 53  ? -37.866 -5.336  34.795  1.00 31.36 ? 32  ILE   D CG2 1 
ATOM   5764 C CD1 . ILE   D 1 53  ? -38.370 -4.304  37.859  1.00 41.11 ? 32  ILE   D CD1 1 
ATOM   5765 N N   . HIS   D 1 54  ? -37.553 -2.741  31.957  1.00 31.61 ? 33  HIS   D N   1 
ATOM   5766 C CA  . HIS   D 1 54  ? -38.084 -2.899  30.613  1.00 29.42 ? 33  HIS   D CA  1 
ATOM   5767 C C   . HIS   D 1 54  ? -38.045 -4.386  30.273  1.00 28.33 ? 33  HIS   D C   1 
ATOM   5768 O O   . HIS   D 1 54  ? -37.124 -5.080  30.685  1.00 28.99 ? 33  HIS   D O   1 
ATOM   5769 C CB  . HIS   D 1 54  ? -37.347 -2.030  29.575  1.00 24.80 ? 33  HIS   D CB  1 
ATOM   5770 C CG  . HIS   D 1 54  ? -37.527 -2.612  28.207  1.00 28.11 ? 33  HIS   D CG  1 
ATOM   5771 N ND1 . HIS   D 1 54  ? -36.710 -3.624  27.752  1.00 29.08 ? 33  HIS   D ND1 1 
ATOM   5772 C CD2 . HIS   D 1 54  ? -38.451 -2.438  27.261  1.00 28.10 ? 33  HIS   D CD2 1 
ATOM   5773 C CE1 . HIS   D 1 54  ? -37.126 -4.039  26.566  1.00 29.33 ? 33  HIS   D CE1 1 
ATOM   5774 N NE2 . HIS   D 1 54  ? -38.181 -3.332  26.248  1.00 28.64 ? 33  HIS   D NE2 1 
ATOM   5775 N N   . TYR   D 1 55  ? -39.065 -4.851  29.540  1.00 30.08 ? 34  TYR   D N   1 
ATOM   5776 C CA  . TYR   D 1 55  ? -39.064 -6.237  29.099  1.00 31.74 ? 34  TYR   D CA  1 
ATOM   5777 C C   . TYR   D 1 55  ? -39.775 -6.323  27.751  1.00 29.86 ? 34  TYR   D C   1 
ATOM   5778 O O   . TYR   D 1 55  ? -40.493 -5.405  27.333  1.00 29.13 ? 34  TYR   D O   1 
ATOM   5779 C CB  . TYR   D 1 55  ? -39.653 -7.161  30.179  1.00 33.51 ? 34  TYR   D CB  1 
ATOM   5780 C CG  . TYR   D 1 55  ? -41.174 -7.032  30.237  1.00 38.71 ? 34  TYR   D CG  1 
ATOM   5781 C CD1 . TYR   D 1 55  ? -41.792 -6.014  30.981  1.00 34.77 ? 34  TYR   D CD1 1 
ATOM   5782 C CD2 . TYR   D 1 55  ? -41.981 -7.900  29.504  1.00 37.25 ? 34  TYR   D CD2 1 
ATOM   5783 C CE1 . TYR   D 1 55  ? -43.173 -5.883  30.999  1.00 34.37 ? 34  TYR   D CE1 1 
ATOM   5784 C CE2 . TYR   D 1 55  ? -43.363 -7.772  29.518  1.00 38.74 ? 34  TYR   D CE2 1 
ATOM   5785 C CZ  . TYR   D 1 55  ? -43.956 -6.788  30.294  1.00 41.74 ? 34  TYR   D CZ  1 
ATOM   5786 O OH  . TYR   D 1 55  ? -45.318 -6.659  30.301  1.00 43.72 ? 34  TYR   D OH  1 
ATOM   5787 N N   . HIS   D 1 56  ? -39.577 -7.455  27.067  1.00 30.51 ? 35  HIS   D N   1 
ATOM   5788 C CA  . HIS   D 1 56  ? -40.241 -7.662  25.797  1.00 35.87 ? 35  HIS   D CA  1 
ATOM   5789 C C   . HIS   D 1 56  ? -41.214 -8.823  25.970  1.00 36.35 ? 35  HIS   D C   1 
ATOM   5790 O O   . HIS   D 1 56  ? -42.418 -8.610  26.041  1.00 38.94 ? 35  HIS   D O   1 
ATOM   5791 C CB  . HIS   D 1 56  ? -39.232 -7.868  24.659  1.00 32.26 ? 35  HIS   D CB  1 
ATOM   5792 C CG  . HIS   D 1 56  ? -39.909 -8.146  23.359  1.00 33.95 ? 35  HIS   D CG  1 
ATOM   5793 N ND1 . HIS   D 1 56  ? -39.412 -9.107  22.509  1.00 37.61 ? 35  HIS   D ND1 1 
ATOM   5794 C CD2 . HIS   D 1 56  ? -41.050 -7.695  22.790  1.00 36.12 ? 35  HIS   D CD2 1 
ATOM   5795 C CE1 . HIS   D 1 56  ? -40.208 -9.195  21.435  1.00 37.84 ? 35  HIS   D CE1 1 
ATOM   5796 N NE2 . HIS   D 1 56  ? -41.205 -8.340  21.586  1.00 39.55 ? 35  HIS   D NE2 1 
ATOM   5797 N N   . ASN   D 1 57  ? -40.673 -10.034 26.053  1.00 35.26 ? 36  ASN   D N   1 
ATOM   5798 C CA  . ASN   D 1 57  ? -41.495 -11.225 26.162  1.00 40.63 ? 36  ASN   D CA  1 
ATOM   5799 C C   . ASN   D 1 57  ? -41.604 -11.726 27.602  1.00 40.52 ? 36  ASN   D C   1 
ATOM   5800 O O   . ASN   D 1 57  ? -42.515 -12.498 27.889  1.00 48.82 ? 36  ASN   D O   1 
ATOM   5801 C CB  . ASN   D 1 57  ? -40.963 -12.370 25.309  1.00 42.24 ? 36  ASN   D CB  1 
ATOM   5802 C CG  . ASN   D 1 57  ? -41.170 -12.145 23.829  1.00 46.30 ? 36  ASN   D CG  1 
ATOM   5803 O OD1 . ASN   D 1 57  ? -42.149 -11.509 23.416  1.00 47.81 ? 36  ASN   D OD1 1 
ATOM   5804 N ND2 . ASN   D 1 57  ? -40.258 -12.649 23.011  1.00 46.96 ? 36  ASN   D ND2 1 
ATOM   5805 N N   . SER   D 1 58  ? -40.688 -11.340 28.505  1.00 36.46 ? 37  SER   D N   1 
ATOM   5806 C CA  . SER   D 1 58  ? -40.655 -12.012 29.792  1.00 38.50 ? 37  SER   D CA  1 
ATOM   5807 C C   . SER   D 1 58  ? -41.546 -11.303 30.817  1.00 39.58 ? 37  SER   D C   1 
ATOM   5808 O O   . SER   D 1 58  ? -41.046 -10.801 31.817  1.00 37.05 ? 37  SER   D O   1 
ATOM   5809 C CB  . SER   D 1 58  ? -39.246 -12.206 30.306  1.00 40.05 ? 37  SER   D CB  1 
ATOM   5810 O OG  . SER   D 1 58  ? -38.460 -13.016 29.439  1.00 43.44 ? 37  SER   D OG  1 
ATOM   5811 N N   . ALA   D 1 59  ? -42.865 -11.299 30.572  1.00 41.71 ? 38  ALA   D N   1 
ATOM   5812 C CA  . ALA   D 1 59  ? -43.821 -10.590 31.422  1.00 39.16 ? 38  ALA   D CA  1 
ATOM   5813 C C   . ALA   D 1 59  ? -43.823 -11.144 32.847  1.00 36.82 ? 38  ALA   D C   1 
ATOM   5814 O O   . ALA   D 1 59  ? -43.675 -10.385 33.805  1.00 42.05 ? 38  ALA   D O   1 
ATOM   5815 C CB  . ALA   D 1 59  ? -45.199 -10.604 30.790  1.00 40.73 ? 38  ALA   D CB  1 
ATOM   5816 N N   . GLU   D 1 60  ? -43.920 -12.475 32.985  1.00 38.66 ? 39  GLU   D N   1 
ATOM   5817 C CA  . GLU   D 1 60  ? -43.962 -13.094 34.305  1.00 43.81 ? 39  GLU   D CA  1 
ATOM   5818 C C   . GLU   D 1 60  ? -42.754 -12.664 35.131  1.00 42.85 ? 39  GLU   D C   1 
ATOM   5819 O O   . GLU   D 1 60  ? -42.921 -12.137 36.217  1.00 40.79 ? 39  GLU   D O   1 
ATOM   5820 C CB  . GLU   D 1 60  ? -44.122 -14.616 34.334  1.00 43.44 ? 39  GLU   D CB  1 
ATOM   5821 C CG  . GLU   D 1 60  ? -45.395 -15.107 33.651  0.60 50.64 ? 39  GLU   D CG  1 
ATOM   5822 C CD  . GLU   D 1 60  ? -45.693 -16.590 33.813  0.60 52.01 ? 39  GLU   D CD  1 
ATOM   5823 O OE1 . GLU   D 1 60  ? -44.828 -17.408 33.444  0.60 53.91 ? 39  GLU   D OE1 1 
ATOM   5824 O OE2 . GLU   D 1 60  ? -46.795 -16.924 34.299  0.60 51.92 ? 39  GLU   D OE2 1 
ATOM   5825 N N   . ALA   D 1 61  ? -41.542 -12.847 34.586  1.00 44.12 ? 40  ALA   D N   1 
ATOM   5826 C CA  . ALA   D 1 61  ? -40.309 -12.555 35.302  1.00 35.17 ? 40  ALA   D CA  1 
ATOM   5827 C C   . ALA   D 1 61  ? -40.121 -11.053 35.541  1.00 39.15 ? 40  ALA   D C   1 
ATOM   5828 O O   . ALA   D 1 61  ? -39.622 -10.644 36.592  1.00 34.52 ? 40  ALA   D O   1 
ATOM   5829 C CB  . ALA   D 1 61  ? -39.128 -13.187 34.587  1.00 36.42 ? 40  ALA   D CB  1 
ATOM   5830 N N   . ALA   D 1 62  ? -40.511 -10.224 34.567  1.00 38.29 ? 41  ALA   D N   1 
ATOM   5831 C CA  . ALA   D 1 62  ? -40.545 -8.789  34.816  1.00 39.27 ? 41  ALA   D CA  1 
ATOM   5832 C C   . ALA   D 1 62  ? -41.326 -8.485  36.103  1.00 40.77 ? 41  ALA   D C   1 
ATOM   5833 O O   . ALA   D 1 62  ? -40.801 -7.827  37.001  1.00 38.21 ? 41  ALA   D O   1 
ATOM   5834 C CB  . ALA   D 1 62  ? -41.129 -8.050  33.643  1.00 32.62 ? 41  ALA   D CB  1 
ATOM   5835 N N   . VAL   D 1 63  ? -42.605 -8.899  36.139  1.00 43.55 ? 42  VAL   D N   1 
ATOM   5836 C CA  . VAL   D 1 63  ? -43.520 -8.498  37.209  1.00 44.23 ? 42  VAL   D CA  1 
ATOM   5837 C C   . VAL   D 1 63  ? -43.049 -9.113  38.532  1.00 36.57 ? 42  VAL   D C   1 
ATOM   5838 O O   . VAL   D 1 63  ? -43.063 -8.454  39.568  1.00 42.62 ? 42  VAL   D O   1 
ATOM   5839 C CB  . VAL   D 1 63  ? -45.013 -8.727  36.878  1.00 45.35 ? 42  VAL   D CB  1 
ATOM   5840 C CG1 . VAL   D 1 63  ? -45.921 -8.769  38.109  1.00 43.16 ? 42  VAL   D CG1 1 
ATOM   5841 C CG2 . VAL   D 1 63  ? -45.527 -7.679  35.894  1.00 43.95 ? 42  VAL   D CG2 1 
ATOM   5842 N N   . SER   D 1 64  ? -42.550 -10.346 38.463  1.00 40.07 ? 43  SER   D N   1 
ATOM   5843 C CA  . SER   D 1 64  ? -41.937 -11.006 39.604  1.00 41.60 ? 43  SER   D CA  1 
ATOM   5844 C C   . SER   D 1 64  ? -40.774 -10.199 40.188  1.00 46.35 ? 43  SER   D C   1 
ATOM   5845 O O   . SER   D 1 64  ? -40.662 -10.072 41.410  1.00 49.44 ? 43  SER   D O   1 
ATOM   5846 C CB  . SER   D 1 64  ? -41.555 -12.421 39.245  1.00 43.27 ? 43  SER   D CB  1 
ATOM   5847 O OG  . SER   D 1 64  ? -40.803 -13.012 40.290  1.00 48.79 ? 43  SER   D OG  1 
ATOM   5848 N N   . LEU   D 1 65  ? -39.894 -9.641  39.332  1.00 40.89 ? 44  LEU   D N   1 
ATOM   5849 C CA  . LEU   D 1 65  ? -38.761 -8.892  39.859  1.00 36.16 ? 44  LEU   D CA  1 
ATOM   5850 C C   . LEU   D 1 65  ? -39.229 -7.597  40.531  1.00 33.79 ? 44  LEU   D C   1 
ATOM   5851 O O   . LEU   D 1 65  ? -38.670 -7.190  41.544  1.00 40.93 ? 44  LEU   D O   1 
ATOM   5852 C CB  . LEU   D 1 65  ? -37.749 -8.604  38.742  1.00 40.10 ? 44  LEU   D CB  1 
ATOM   5853 C CG  . LEU   D 1 65  ? -36.648 -7.587  39.087  1.00 41.68 ? 44  LEU   D CG  1 
ATOM   5854 C CD1 . LEU   D 1 65  ? -35.672 -8.157  40.090  1.00 36.51 ? 44  LEU   D CD1 1 
ATOM   5855 C CD2 . LEU   D 1 65  ? -35.921 -7.071  37.835  1.00 44.38 ? 44  LEU   D CD2 1 
ATOM   5856 N N   . ALA   D 1 66  ? -40.197 -6.903  39.918  1.00 36.17 ? 45  ALA   D N   1 
ATOM   5857 C CA  . ALA   D 1 66  ? -40.708 -5.659  40.471  1.00 36.89 ? 45  ALA   D CA  1 
ATOM   5858 C C   . ALA   D 1 66  ? -41.302 -5.930  41.861  1.00 38.00 ? 45  ALA   D C   1 
ATOM   5859 O O   . ALA   D 1 66  ? -41.044 -5.180  42.794  1.00 36.38 ? 45  ALA   D O   1 
ATOM   5860 C CB  . ALA   D 1 66  ? -41.736 -5.071  39.543  1.00 38.74 ? 45  ALA   D CB  1 
ATOM   5861 N N   . ASP   D 1 67  ? -42.022 -7.055  41.988  1.00 49.77 ? 46  ASP   D N   1 
ATOM   5862 C CA  . ASP   D 1 67  ? -42.661 -7.467  43.234  1.00 46.46 ? 46  ASP   D CA  1 
ATOM   5863 C C   . ASP   D 1 67  ? -41.617 -7.596  44.332  1.00 46.01 ? 46  ASP   D C   1 
ATOM   5864 O O   . ASP   D 1 67  ? -41.790 -7.037  45.415  1.00 44.72 ? 46  ASP   D O   1 
ATOM   5865 C CB  . ASP   D 1 67  ? -43.518 -8.709  43.047  1.00 53.98 ? 46  ASP   D CB  1 
ATOM   5866 C CG  . ASP   D 1 67  ? -44.848 -8.480  42.336  1.00 63.34 ? 46  ASP   D CG  1 
ATOM   5867 O OD1 . ASP   D 1 67  ? -45.114 -7.312  41.945  1.00 63.14 ? 46  ASP   D OD1 1 
ATOM   5868 O OD2 . ASP   D 1 67  ? -45.607 -9.474  42.167  1.00 55.63 ? 46  ASP   D OD2 1 
ATOM   5869 N N   . GLU   D 1 68  ? -40.519 -8.297  44.025  1.00 46.13 ? 47  GLU   D N   1 
ATOM   5870 C CA  . GLU   D 1 68  ? -39.408 -8.484  44.945  1.00 44.27 ? 47  GLU   D CA  1 
ATOM   5871 C C   . GLU   D 1 68  ? -38.811 -7.142  45.369  1.00 44.30 ? 47  GLU   D C   1 
ATOM   5872 O O   . GLU   D 1 68  ? -38.560 -6.911  46.551  1.00 50.17 ? 47  GLU   D O   1 
ATOM   5873 C CB  . GLU   D 1 68  ? -38.398 -9.474  44.362  1.00 48.20 ? 47  GLU   D CB  1 
ATOM   5874 C CG  . GLU   D 1 68  ? -37.412 -10.015 45.394  0.60 55.13 ? 47  GLU   D CG  1 
ATOM   5875 C CD  . GLU   D 1 68  ? -36.262 -10.838 44.838  0.60 59.34 ? 47  GLU   D CD  1 
ATOM   5876 O OE1 . GLU   D 1 68  ? -35.103 -10.401 45.008  0.60 62.12 ? 47  GLU   D OE1 1 
ATOM   5877 O OE2 . GLU   D 1 68  ? -36.514 -11.910 44.250  0.60 60.07 ? 47  GLU   D OE2 1 
ATOM   5878 N N   . LEU   D 1 69  ? -38.560 -6.247  44.412  1.00 41.21 ? 48  LEU   D N   1 
ATOM   5879 C CA  . LEU   D 1 69  ? -37.960 -4.959  44.745  1.00 39.90 ? 48  LEU   D CA  1 
ATOM   5880 C C   . LEU   D 1 69  ? -38.914 -4.091  45.566  1.00 34.97 ? 48  LEU   D C   1 
ATOM   5881 O O   . LEU   D 1 69  ? -38.482 -3.337  46.446  1.00 41.73 ? 48  LEU   D O   1 
ATOM   5882 C CB  . LEU   D 1 69  ? -37.508 -4.216  43.485  1.00 39.92 ? 48  LEU   D CB  1 
ATOM   5883 C CG  . LEU   D 1 69  ? -36.388 -4.893  42.687  1.00 45.62 ? 48  LEU   D CG  1 
ATOM   5884 C CD1 . LEU   D 1 69  ? -35.743 -3.888  41.730  1.00 42.04 ? 48  LEU   D CD1 1 
ATOM   5885 C CD2 . LEU   D 1 69  ? -35.338 -5.526  43.582  1.00 40.42 ? 48  LEU   D CD2 1 
ATOM   5886 N N   . ASN   D 1 70  ? -40.195 -4.122  45.202  1.00 43.77 ? 49  ASN   D N   1 
ATOM   5887 C CA  . ASN   D 1 70  ? -41.191 -3.282  45.864  1.00 45.23 ? 49  ASN   D CA  1 
ATOM   5888 C C   . ASN   D 1 70  ? -41.412 -3.784  47.298  1.00 45.41 ? 49  ASN   D C   1 
ATOM   5889 O O   . ASN   D 1 70  ? -41.674 -2.990  48.206  1.00 47.42 ? 49  ASN   D O   1 
ATOM   5890 C CB  . ASN   D 1 70  ? -42.477 -3.189  45.047  1.00 41.26 ? 49  ASN   D CB  1 
ATOM   5891 C CG  . ASN   D 1 70  ? -42.375 -2.215  43.899  1.00 36.58 ? 49  ASN   D CG  1 
ATOM   5892 O OD1 . ASN   D 1 70  ? -41.783 -1.137  44.043  1.00 41.85 ? 49  ASN   D OD1 1 
ATOM   5893 N ND2 . ASN   D 1 70  ? -43.004 -2.549  42.783  1.00 38.59 ? 49  ASN   D ND2 1 
ATOM   5894 N N   . LYS   D 1 71  ? -41.277 -5.104  47.492  1.00 43.11 ? 50  LYS   D N   1 
ATOM   5895 C CA  . LYS   D 1 71  ? -41.398 -5.705  48.814  1.00 49.62 ? 50  LYS   D CA  1 
ATOM   5896 C C   . LYS   D 1 71  ? -40.299 -5.174  49.729  1.00 54.70 ? 50  LYS   D C   1 
ATOM   5897 O O   . LYS   D 1 71  ? -40.514 -5.039  50.926  1.00 54.72 ? 50  LYS   D O   1 
ATOM   5898 C CB  . LYS   D 1 71  ? -41.377 -7.234  48.823  1.00 46.33 ? 50  LYS   D CB  1 
ATOM   5899 N N   . GLU   D 1 72  ? -39.141 -4.844  49.149  1.00 52.51 ? 51  GLU   D N   1 
ATOM   5900 C CA  . GLU   D 1 72  ? -37.987 -4.374  49.899  1.00 51.35 ? 51  GLU   D CA  1 
ATOM   5901 C C   . GLU   D 1 72  ? -38.120 -2.878  50.200  1.00 49.94 ? 51  GLU   D C   1 
ATOM   5902 O O   . GLU   D 1 72  ? -37.753 -2.410  51.277  1.00 53.07 ? 51  GLU   D O   1 
ATOM   5903 C CB  . GLU   D 1 72  ? -36.758 -4.686  49.043  1.00 54.59 ? 51  GLU   D CB  1 
ATOM   5904 C CG  . GLU   D 1 72  ? -35.436 -4.437  49.757  1.00 56.49 ? 51  GLU   D CG  1 
ATOM   5905 C CD  . GLU   D 1 72  ? -35.159 -5.472  50.832  1.00 66.65 ? 51  GLU   D CD  1 
ATOM   5906 O OE1 . GLU   D 1 72  ? -34.277 -5.158  51.662  1.00 68.05 ? 51  GLU   D OE1 1 
ATOM   5907 O OE2 . GLU   D 1 72  ? -35.783 -6.570  50.841  1.00 63.28 ? 51  GLU   D OE2 1 
ATOM   5908 N N   . ARG   D 1 73  ? -38.590 -2.111  49.217  1.00 48.52 ? 52  ARG   D N   1 
ATOM   5909 C CA  . ARG   D 1 73  ? -38.900 -0.702  49.411  1.00 48.40 ? 52  ARG   D CA  1 
ATOM   5910 C C   . ARG   D 1 73  ? -40.099 -0.412  48.527  1.00 52.24 ? 52  ARG   D C   1 
ATOM   5911 O O   . ARG   D 1 73  ? -40.041 -0.601  47.314  1.00 49.72 ? 52  ARG   D O   1 
ATOM   5912 C CB  . ARG   D 1 73  ? -37.761 0.275   49.078  1.00 49.99 ? 52  ARG   D CB  1 
ATOM   5913 C CG  . ARG   D 1 73  ? -36.410 0.159   49.776  1.00 46.60 ? 52  ARG   D CG  1 
ATOM   5914 C CD  . ARG   D 1 73  ? -35.545 1.409   49.634  1.00 45.97 ? 52  ARG   D CD  1 
ATOM   5915 N NE  . ARG   D 1 73  ? -35.276 1.767   48.234  1.00 46.30 ? 52  ARG   D NE  1 
ATOM   5916 C CZ  . ARG   D 1 73  ? -34.401 1.159   47.430  1.00 53.26 ? 52  ARG   D CZ  1 
ATOM   5917 N NH1 . ARG   D 1 73  ? -34.166 1.629   46.211  1.00 43.75 ? 52  ARG   D NH1 1 
ATOM   5918 N NH2 . ARG   D 1 73  ? -33.740 0.096   47.860  1.00 53.96 ? 52  ARG   D NH2 1 
ATOM   5919 N N   . SER   D 1 74  ? -41.210 -0.010  49.135  1.00 48.10 ? 53  SER   D N   1 
ATOM   5920 C CA  . SER   D 1 74  ? -42.424 0.117   48.345  1.00 48.33 ? 53  SER   D CA  1 
ATOM   5921 C C   . SER   D 1 74  ? -42.278 1.232   47.304  1.00 39.82 ? 53  SER   D C   1 
ATOM   5922 O O   . SER   D 1 74  ? -41.625 2.249   47.562  1.00 38.89 ? 53  SER   D O   1 
ATOM   5923 C CB  . SER   D 1 74  ? -43.611 0.374   49.233  1.00 58.29 ? 53  SER   D CB  1 
ATOM   5924 O OG  . SER   D 1 74  ? -43.371 1.556   49.985  1.00 67.48 ? 53  SER   D OG  1 
ATOM   5925 N N   . ASN   D 1 75  ? -42.938 1.035   46.156  1.00 41.65 ? 54  ASN   D N   1 
ATOM   5926 C CA  . ASN   D 1 75  ? -43.037 2.037   45.104  1.00 45.50 ? 54  ASN   D CA  1 
ATOM   5927 C C   . ASN   D 1 75  ? -41.654 2.400   44.561  1.00 45.10 ? 54  ASN   D C   1 
ATOM   5928 O O   . ASN   D 1 75  ? -41.353 3.576   44.374  1.00 45.93 ? 54  ASN   D O   1 
ATOM   5929 C CB  . ASN   D 1 75  ? -43.685 3.322   45.611  1.00 52.18 ? 54  ASN   D CB  1 
ATOM   5930 C CG  . ASN   D 1 75  ? -45.046 3.073   46.212  1.00 45.50 ? 54  ASN   D CG  1 
ATOM   5931 O OD1 . ASN   D 1 75  ? -45.761 2.171   45.767  1.00 44.27 ? 54  ASN   D OD1 1 
ATOM   5932 N ND2 . ASN   D 1 75  ? -45.395 3.833   47.237  1.00 45.35 ? 54  ASN   D ND2 1 
ATOM   5933 N N   . THR   D 1 76  ? -40.807 1.398   44.325  1.00 39.13 ? 55  THR   D N   1 
ATOM   5934 C CA  . THR   D 1 76  ? -39.482 1.728   43.813  1.00 45.41 ? 55  THR   D CA  1 
ATOM   5935 C C   . THR   D 1 76  ? -39.195 1.007   42.491  1.00 41.84 ? 55  THR   D C   1 
ATOM   5936 O O   . THR   D 1 76  ? -38.072 1.133   41.984  1.00 42.89 ? 55  THR   D O   1 
ATOM   5937 C CB  . THR   D 1 76  ? -38.373 1.464   44.838  1.00 38.06 ? 55  THR   D CB  1 
ATOM   5938 O OG1 . THR   D 1 76  ? -38.579 0.116   45.242  1.00 39.37 ? 55  THR   D OG1 1 
ATOM   5939 C CG2 . THR   D 1 76  ? -38.360 2.408   46.029  1.00 42.30 ? 55  THR   D CG2 1 
ATOM   5940 N N   . ALA   D 1 77  ? -40.171 0.238   41.978  1.00 40.58 ? 56  ALA   D N   1 
ATOM   5941 C CA  . ALA   D 1 77  ? -40.047 -0.512  40.727  1.00 35.52 ? 56  ALA   D CA  1 
ATOM   5942 C C   . ALA   D 1 77  ? -41.346 -0.509  39.919  1.00 41.25 ? 56  ALA   D C   1 
ATOM   5943 O O   . ALA   D 1 77  ? -42.447 -0.730  40.440  1.00 41.00 ? 56  ALA   D O   1 
ATOM   5944 C CB  . ALA   D 1 77  ? -39.559 -1.918  40.982  1.00 32.72 ? 56  ALA   D CB  1 
ATOM   5945 N N   . VAL   D 1 78  ? -41.210 -0.243  38.612  1.00 36.24 ? 57  VAL   D N   1 
ATOM   5946 C CA  . VAL   D 1 78  ? -42.278 -0.444  37.645  1.00 39.19 ? 57  VAL   D CA  1 
ATOM   5947 C C   . VAL   D 1 78  ? -41.705 -1.304  36.513  1.00 41.30 ? 57  VAL   D C   1 
ATOM   5948 O O   . VAL   D 1 78  ? -40.479 -1.373  36.340  1.00 39.19 ? 57  VAL   D O   1 
ATOM   5949 C CB  . VAL   D 1 78  ? -42.901 0.879   37.136  1.00 44.76 ? 57  VAL   D CB  1 
ATOM   5950 C CG1 . VAL   D 1 78  ? -43.508 1.713   38.263  1.00 40.40 ? 57  VAL   D CG1 1 
ATOM   5951 C CG2 . VAL   D 1 78  ? -41.942 1.756   36.334  1.00 36.69 ? 57  VAL   D CG2 1 
ATOM   5952 N N   . VAL   D 1 79  ? -42.587 -2.015  35.807  1.00 39.15 ? 58  VAL   D N   1 
ATOM   5953 C CA  . VAL   D 1 79  ? -42.223 -2.659  34.554  1.00 36.04 ? 58  VAL   D CA  1 
ATOM   5954 C C   . VAL   D 1 79  ? -42.673 -1.772  33.395  1.00 38.37 ? 58  VAL   D C   1 
ATOM   5955 O O   . VAL   D 1 79  ? -43.498 -0.876  33.571  1.00 36.24 ? 58  VAL   D O   1 
ATOM   5956 C CB  . VAL   D 1 79  ? -42.790 -4.089  34.426  1.00 36.02 ? 58  VAL   D CB  1 
ATOM   5957 C CG1 . VAL   D 1 79  ? -42.299 -4.999  35.545  1.00 37.76 ? 58  VAL   D CG1 1 
ATOM   5958 C CG2 . VAL   D 1 79  ? -44.315 -4.108  34.346  1.00 34.83 ? 58  VAL   D CG2 1 
ATOM   5959 N N   . CYS   D 1 80  ? -42.121 -2.027  32.192  1.00 30.98 ? 59  CYS   D N   1 
ATOM   5960 C CA  . CYS   D 1 80  ? -42.548 -1.301  31.001  1.00 32.83 ? 59  CYS   D CA  1 
ATOM   5961 C C   . CYS   D 1 80  ? -42.284 -2.218  29.816  1.00 32.24 ? 59  CYS   D C   1 
ATOM   5962 O O   . CYS   D 1 80  ? -41.160 -2.676  29.675  1.00 32.52 ? 59  CYS   D O   1 
ATOM   5963 C CB  . CYS   D 1 80  ? -41.793 0.027   30.889  1.00 31.87 ? 59  CYS   D CB  1 
ATOM   5964 S SG  . CYS   D 1 80  ? -42.105 0.929   29.354  1.00 38.41 ? 59  CYS   D SG  1 
ATOM   5965 N N   . GLN   D 1 81  ? -43.316 -2.510  28.999  1.00 32.31 ? 60  GLN   D N   1 
ATOM   5966 C CA  . GLN   D 1 81  ? -43.171 -3.508  27.949  1.00 33.30 ? 60  GLN   D CA  1 
ATOM   5967 C C   . GLN   D 1 81  ? -42.917 -2.786  26.628  1.00 31.58 ? 60  GLN   D C   1 
ATOM   5968 O O   . GLN   D 1 81  ? -43.546 -1.758  26.343  1.00 29.72 ? 60  GLN   D O   1 
ATOM   5969 C CB  . GLN   D 1 81  ? -44.412 -4.393  27.810  1.00 37.28 ? 60  GLN   D CB  1 
ATOM   5970 C CG  . GLN   D 1 81  ? -44.249 -5.593  26.875  1.00 33.86 ? 60  GLN   D CG  1 
ATOM   5971 C CD  . GLN   D 1 81  ? -44.366 -5.272  25.399  1.00 37.70 ? 60  GLN   D CD  1 
ATOM   5972 O OE1 . GLN   D 1 81  ? -45.006 -4.296  24.982  1.00 41.66 ? 60  GLN   D OE1 1 
ATOM   5973 N NE2 . GLN   D 1 81  ? -43.727 -6.106  24.584  1.00 38.49 ? 60  GLN   D NE2 1 
ATOM   5974 N N   . ALA   D 1 82  ? -41.980 -3.333  25.829  1.00 34.14 ? 61  ALA   D N   1 
ATOM   5975 C CA  . ALA   D 1 82  ? -41.678 -2.734  24.535  1.00 31.02 ? 61  ALA   D CA  1 
ATOM   5976 C C   . ALA   D 1 82  ? -40.831 -3.677  23.681  1.00 28.78 ? 61  ALA   D C   1 
ATOM   5977 O O   . ALA   D 1 82  ? -39.890 -4.313  24.173  1.00 30.61 ? 61  ALA   D O   1 
ATOM   5978 C CB  . ALA   D 1 82  ? -41.003 -1.392  24.726  1.00 30.28 ? 61  ALA   D CB  1 
ATOM   5979 N N   . ASP   D 1 83  ? -41.207 -3.765  22.402  1.00 32.18 ? 62  ASP   D N   1 
ATOM   5980 C CA  . ASP   D 1 83  ? -40.397 -4.407  21.372  1.00 32.27 ? 62  ASP   D CA  1 
ATOM   5981 C C   . ASP   D 1 83  ? -39.344 -3.405  20.891  1.00 29.51 ? 62  ASP   D C   1 
ATOM   5982 O O   . ASP   D 1 83  ? -39.703 -2.287  20.510  1.00 30.17 ? 62  ASP   D O   1 
ATOM   5983 C CB  . ASP   D 1 83  ? -41.269 -4.857  20.212  1.00 34.31 ? 62  ASP   D CB  1 
ATOM   5984 C CG  . ASP   D 1 83  ? -40.566 -5.659  19.126  1.00 36.10 ? 62  ASP   D CG  1 
ATOM   5985 O OD1 . ASP   D 1 83  ? -39.337 -5.893  19.257  1.00 31.20 ? 62  ASP   D OD1 1 
ATOM   5986 O OD2 . ASP   D 1 83  ? -41.240 -6.046  18.156  1.00 36.79 ? 62  ASP   D OD2 1 
ATOM   5987 N N   . LEU   D 1 84  ? -38.058 -3.817  20.912  1.00 27.11 ? 63  LEU   D N   1 
ATOM   5988 C CA  . LEU   D 1 84  ? -36.974 -2.906  20.528  1.00 27.05 ? 63  LEU   D CA  1 
ATOM   5989 C C   . LEU   D 1 84  ? -36.430 -3.207  19.125  1.00 27.17 ? 63  LEU   D C   1 
ATOM   5990 O O   . LEU   D 1 84  ? -35.436 -2.618  18.689  1.00 27.21 ? 63  LEU   D O   1 
ATOM   5991 C CB  . LEU   D 1 84  ? -35.892 -2.822  21.603  1.00 23.52 ? 63  LEU   D CB  1 
ATOM   5992 C CG  . LEU   D 1 84  ? -36.362 -2.314  22.975  1.00 23.75 ? 63  LEU   D CG  1 
ATOM   5993 C CD1 . LEU   D 1 84  ? -35.205 -2.308  24.019  1.00 25.02 ? 63  LEU   D CD1 1 
ATOM   5994 C CD2 . LEU   D 1 84  ? -36.944 -0.925  22.843  1.00 27.93 ? 63  LEU   D CD2 1 
ATOM   5995 N N   . THR   D 1 85  ? -37.117 -4.091  18.401  1.00 26.79 ? 64  THR   D N   1 
ATOM   5996 C CA  . THR   D 1 85  ? -36.951 -4.244  16.951  1.00 25.53 ? 64  THR   D CA  1 
ATOM   5997 C C   . THR   D 1 85  ? -37.052 -2.894  16.250  1.00 23.79 ? 64  THR   D C   1 
ATOM   5998 O O   . THR   D 1 85  ? -37.969 -2.118  16.533  1.00 24.65 ? 64  THR   D O   1 
ATOM   5999 C CB  . THR   D 1 85  ? -38.002 -5.217  16.403  1.00 27.66 ? 64  THR   D CB  1 
ATOM   6000 O OG1 . THR   D 1 85  ? -37.745 -6.438  17.086  1.00 30.22 ? 64  THR   D OG1 1 
ATOM   6001 C CG2 . THR   D 1 85  ? -37.837 -5.504  14.923  1.00 32.28 ? 64  THR   D CG2 1 
ATOM   6002 N N   . ASN   D 1 86  ? -36.200 -2.665  15.219  1.00 24.07 ? 65  ASN   D N   1 
ATOM   6003 C CA  . ASN   D 1 86  ? -36.293 -1.456  14.411  1.00 24.25 ? 65  ASN   D CA  1 
ATOM   6004 C C   . ASN   D 1 86  ? -37.587 -1.448  13.582  1.00 30.99 ? 65  ASN   D C   1 
ATOM   6005 O O   . ASN   D 1 86  ? -37.992 -2.467  13.021  1.00 26.54 ? 65  ASN   D O   1 
ATOM   6006 C CB  . ASN   D 1 86  ? -35.086 -1.318  13.479  1.00 26.83 ? 65  ASN   D CB  1 
ATOM   6007 C CG  . ASN   D 1 86  ? -35.025 0.028   12.797  1.00 28.53 ? 65  ASN   D CG  1 
ATOM   6008 O OD1 . ASN   D 1 86  ? -35.245 1.047   13.443  1.00 30.45 ? 65  ASN   D OD1 1 
ATOM   6009 N ND2 . ASN   D 1 86  ? -34.744 0.061   11.503  1.00 28.97 ? 65  ASN   D ND2 1 
ATOM   6010 N N   . SER   D 1 87  ? -38.262 -0.286  13.537  1.00 29.32 ? 66  SER   D N   1 
ATOM   6011 C CA  . SER   D 1 87  ? -39.426 -0.042  12.692  1.00 28.57 ? 66  SER   D CA  1 
ATOM   6012 C C   . SER   D 1 87  ? -39.697 1.463   12.733  1.00 28.79 ? 66  SER   D C   1 
ATOM   6013 O O   . SER   D 1 87  ? -39.061 2.188   13.500  1.00 29.74 ? 66  SER   D O   1 
ATOM   6014 C CB  . SER   D 1 87  ? -40.647 -0.787  13.224  1.00 33.22 ? 66  SER   D CB  1 
ATOM   6015 O OG  . SER   D 1 87  ? -41.143 -0.106  14.375  1.00 31.08 ? 66  SER   D OG  1 
ATOM   6016 N N   . ASN   D 1 88  ? -40.709 1.915   11.992  1.00 28.55 ? 67  ASN   D N   1 
ATOM   6017 C CA  . ASN   D 1 88  ? -41.058 3.328   11.966  1.00 29.23 ? 67  ASN   D CA  1 
ATOM   6018 C C   . ASN   D 1 88  ? -41.653 3.797   13.297  1.00 29.92 ? 67  ASN   D C   1 
ATOM   6019 O O   . ASN   D 1 88  ? -41.730 5.016   13.528  1.00 32.07 ? 67  ASN   D O   1 
ATOM   6020 C CB  . ASN   D 1 88  ? -41.900 3.692   10.749  1.00 29.42 ? 67  ASN   D CB  1 
ATOM   6021 C CG  . ASN   D 1 88  ? -41.092 3.836   9.483   1.00 39.32 ? 67  ASN   D CG  1 
ATOM   6022 O OD1 . ASN   D 1 88  ? -39.861 3.932   9.528   1.00 37.45 ? 67  ASN   D OD1 1 
ATOM   6023 N ND2 . ASN   D 1 88  ? -41.757 3.884   8.336   1.00 39.70 ? 67  ASN   D ND2 1 
ATOM   6024 N N   . VAL   D 1 89  ? -42.032 2.860   14.184  1.00 25.59 ? 68  VAL   D N   1 
ATOM   6025 C CA  . VAL   D 1 89  ? -42.559 3.217   15.499  1.00 26.00 ? 68  VAL   D CA  1 
ATOM   6026 C C   . VAL   D 1 89  ? -41.557 2.976   16.635  1.00 28.36 ? 68  VAL   D C   1 
ATOM   6027 O O   . VAL   D 1 89  ? -41.855 3.212   17.804  1.00 26.86 ? 68  VAL   D O   1 
ATOM   6028 C CB  . VAL   D 1 89  ? -43.934 2.626   15.878  1.00 32.16 ? 68  VAL   D CB  1 
ATOM   6029 C CG1 . VAL   D 1 89  ? -44.975 2.885   14.794  1.00 29.74 ? 68  VAL   D CG1 1 
ATOM   6030 C CG2 . VAL   D 1 89  ? -43.841 1.157   16.293  1.00 33.31 ? 68  VAL   D CG2 1 
ATOM   6031 N N   . LEU   D 1 90  ? -40.328 2.555   16.324  1.00 28.01 ? 69  LEU   D N   1 
ATOM   6032 C CA  . LEU   D 1 90  ? -39.395 2.395   17.433  1.00 24.85 ? 69  LEU   D CA  1 
ATOM   6033 C C   . LEU   D 1 90  ? -39.123 3.718   18.166  1.00 22.91 ? 69  LEU   D C   1 
ATOM   6034 O O   . LEU   D 1 90  ? -39.021 3.728   19.386  1.00 25.01 ? 69  LEU   D O   1 
ATOM   6035 C CB  . LEU   D 1 90  ? -38.122 1.711   16.915  1.00 25.78 ? 69  LEU   D CB  1 
ATOM   6036 C CG  . LEU   D 1 90  ? -37.054 1.425   17.973  1.00 26.72 ? 69  LEU   D CG  1 
ATOM   6037 C CD1 . LEU   D 1 90  ? -37.502 0.504   19.156  1.00 23.60 ? 69  LEU   D CD1 1 
ATOM   6038 C CD2 . LEU   D 1 90  ? -35.875 0.783   17.232  1.00 25.41 ? 69  LEU   D CD2 1 
ATOM   6039 N N   . PRO   D 1 91  ? -39.007 4.888   17.503  1.00 22.60 ? 70  PRO   D N   1 
ATOM   6040 C CA  . PRO   D 1 91  ? -38.792 6.130   18.239  1.00 26.01 ? 70  PRO   D CA  1 
ATOM   6041 C C   . PRO   D 1 91  ? -39.861 6.383   19.311  1.00 28.57 ? 70  PRO   D C   1 
ATOM   6042 O O   . PRO   D 1 91  ? -39.558 6.785   20.438  1.00 26.99 ? 70  PRO   D O   1 
ATOM   6043 C CB  . PRO   D 1 91  ? -38.788 7.176   17.142  1.00 22.60 ? 70  PRO   D CB  1 
ATOM   6044 C CG  . PRO   D 1 91  ? -38.303 6.421   15.921  1.00 25.28 ? 70  PRO   D CG  1 
ATOM   6045 C CD  . PRO   D 1 91  ? -39.030 5.084   16.054  1.00 24.80 ? 70  PRO   D CD  1 
ATOM   6046 N N   . ALA   D 1 92  ? -41.126 6.120   18.955  1.00 26.84 ? 71  ALA   D N   1 
ATOM   6047 C CA  . ALA   D 1 92  ? -42.206 6.276   19.910  1.00 30.39 ? 71  ALA   D CA  1 
ATOM   6048 C C   . ALA   D 1 92  ? -42.079 5.282   21.062  1.00 26.92 ? 71  ALA   D C   1 
ATOM   6049 O O   . ALA   D 1 92  ? -42.286 5.655   22.211  1.00 29.98 ? 71  ALA   D O   1 
ATOM   6050 C CB  . ALA   D 1 92  ? -43.549 6.219   19.212  1.00 31.40 ? 71  ALA   D CB  1 
ATOM   6051 N N   . SER   D 1 93  ? -41.738 4.020   20.784  1.00 28.47 ? 72  SER   D N   1 
ATOM   6052 C CA  . SER   D 1 93  ? -41.580 3.087   21.886  1.00 25.71 ? 72  SER   D CA  1 
ATOM   6053 C C   . SER   D 1 93  ? -40.467 3.519   22.830  1.00 28.72 ? 72  SER   D C   1 
ATOM   6054 O O   . SER   D 1 93  ? -40.560 3.328   24.041  1.00 29.15 ? 72  SER   D O   1 
ATOM   6055 C CB  . SER   D 1 93  ? -41.260 1.708   21.400  1.00 28.18 ? 72  SER   D CB  1 
ATOM   6056 O OG  . SER   D 1 93  ? -42.322 1.223   20.600  1.00 29.85 ? 72  SER   D OG  1 
ATOM   6057 N N   . CYS   D 1 94  ? -39.356 4.022   22.261  1.00 24.22 ? 73  CYS   D N   1 
ATOM   6058 C CA  . CYS   D 1 94  ? -38.229 4.415   23.098  1.00 25.57 ? 73  CYS   D CA  1 
ATOM   6059 C C   . CYS   D 1 94  ? -38.624 5.647   23.919  1.00 24.98 ? 73  CYS   D C   1 
ATOM   6060 O O   . CYS   D 1 94  ? -38.285 5.734   25.084  1.00 26.10 ? 73  CYS   D O   1 
ATOM   6061 C CB  . CYS   D 1 94  ? -36.964 4.651   22.264  1.00 24.07 ? 73  CYS   D CB  1 
ATOM   6062 S SG  . CYS   D 1 94  ? -36.366 3.067   21.602  1.00 25.93 ? 73  CYS   D SG  1 
ATOM   6063 N N   . GLU   D 1 95  ? -39.354 6.576   23.305  1.00 28.38 ? 74  GLU   D N   1 
ATOM   6064 C CA  . GLU   D 1 95  ? -39.796 7.747   24.043  1.00 29.54 ? 74  GLU   D CA  1 
ATOM   6065 C C   . GLU   D 1 95  ? -40.665 7.290   25.222  1.00 33.27 ? 74  GLU   D C   1 
ATOM   6066 O O   . GLU   D 1 95  ? -40.596 7.838   26.327  1.00 31.53 ? 74  GLU   D O   1 
ATOM   6067 C CB  . GLU   D 1 95  ? -40.556 8.662   23.087  1.00 34.42 ? 74  GLU   D CB  1 
ATOM   6068 C CG  . GLU   D 1 95  ? -41.156 9.854   23.824  1.00 43.20 ? 74  GLU   D CG  1 
ATOM   6069 C CD  . GLU   D 1 95  ? -41.415 11.047  22.950  1.00 53.50 ? 74  GLU   D CD  1 
ATOM   6070 O OE1 . GLU   D 1 95  ? -40.767 12.074  23.227  1.00 64.46 ? 74  GLU   D OE1 1 
ATOM   6071 O OE2 . GLU   D 1 95  ? -42.261 10.956  22.035  1.00 62.93 ? 74  GLU   D OE2 1 
ATOM   6072 N N   . GLU   D 1 96  ? -41.462 6.240   24.981  1.00 31.50 ? 75  GLU   D N   1 
ATOM   6073 C CA  . GLU   D 1 96  ? -42.411 5.758   25.957  1.00 32.53 ? 75  GLU   D CA  1 
ATOM   6074 C C   . GLU   D 1 96  ? -41.685 5.129   27.134  1.00 33.35 ? 75  GLU   D C   1 
ATOM   6075 O O   . GLU   D 1 96  ? -42.116 5.313   28.262  1.00 28.99 ? 75  GLU   D O   1 
ATOM   6076 C CB  . GLU   D 1 96  ? -43.443 4.824   25.321  1.00 36.02 ? 75  GLU   D CB  1 
ATOM   6077 C CG  . GLU   D 1 96  ? -44.433 4.261   26.341  1.00 37.98 ? 75  GLU   D CG  1 
ATOM   6078 C CD  . GLU   D 1 96  ? -45.143 5.258   27.259  1.00 34.27 ? 75  GLU   D CD  1 
ATOM   6079 O OE1 . GLU   D 1 96  ? -45.544 4.781   28.335  1.00 37.45 ? 75  GLU   D OE1 1 
ATOM   6080 O OE2 . GLU   D 1 96  ? -45.328 6.461   26.918  1.00 38.02 ? 75  GLU   D OE2 1 
ATOM   6081 N N   . ILE   D 1 97  ? -40.595 4.376   26.879  1.00 26.09 ? 76  ILE   D N   1 
ATOM   6082 C CA  . ILE   D 1 97  ? -39.780 3.836   27.961  1.00 29.57 ? 76  ILE   D CA  1 
ATOM   6083 C C   . ILE   D 1 97  ? -39.250 4.927   28.894  1.00 29.70 ? 76  ILE   D C   1 
ATOM   6084 O O   . ILE   D 1 97  ? -39.311 4.765   30.119  1.00 33.82 ? 76  ILE   D O   1 
ATOM   6085 C CB  . ILE   D 1 97  ? -38.644 2.962   27.397  1.00 26.95 ? 76  ILE   D CB  1 
ATOM   6086 C CG1 . ILE   D 1 97  ? -39.250 1.736   26.714  1.00 25.14 ? 76  ILE   D CG1 1 
ATOM   6087 C CG2 . ILE   D 1 97  ? -37.700 2.533   28.514  1.00 26.99 ? 76  ILE   D CG2 1 
ATOM   6088 C CD1 . ILE   D 1 97  ? -38.290 1.024   25.794  1.00 24.12 ? 76  ILE   D CD1 1 
ATOM   6089 N N   . ILE   D 1 98  ? -38.698 6.007   28.320  1.00 26.36 ? 77  ILE   D N   1 
ATOM   6090 C CA  . ILE   D 1 98  ? -38.190 7.100   29.132  1.00 28.95 ? 77  ILE   D CA  1 
ATOM   6091 C C   . ILE   D 1 98  ? -39.366 7.762   29.858  1.00 33.21 ? 77  ILE   D C   1 
ATOM   6092 O O   . ILE   D 1 98  ? -39.272 7.996   31.053  1.00 32.15 ? 77  ILE   D O   1 
ATOM   6093 C CB  . ILE   D 1 98  ? -37.367 8.100   28.299  1.00 27.56 ? 77  ILE   D CB  1 
ATOM   6094 C CG1 . ILE   D 1 98  ? -36.172 7.390   27.663  1.00 23.66 ? 77  ILE   D CG1 1 
ATOM   6095 C CG2 . ILE   D 1 98  ? -36.921 9.332   29.093  1.00 27.67 ? 77  ILE   D CG2 1 
ATOM   6096 C CD1 . ILE   D 1 98  ? -35.235 6.693   28.630  1.00 24.74 ? 77  ILE   D CD1 1 
ATOM   6097 N N   . ASN   D 1 99  ? -40.448 8.052   29.123  1.00 32.52 ? 78  ASN   D N   1 
ATOM   6098 C CA  . ASN   D 1 99  ? -41.643 8.680   29.685  1.00 33.45 ? 78  ASN   D CA  1 
ATOM   6099 C C   . ASN   D 1 99  ? -42.154 7.879   30.882  1.00 31.72 ? 78  ASN   D C   1 
ATOM   6100 O O   . ASN   D 1 99  ? -42.628 8.465   31.862  1.00 35.87 ? 78  ASN   D O   1 
ATOM   6101 C CB  . ASN   D 1 99  ? -42.766 8.800   28.659  1.00 34.29 ? 78  ASN   D CB  1 
ATOM   6102 C CG  . ASN   D 1 99  ? -42.541 9.932   27.691  1.00 36.83 ? 78  ASN   D CG  1 
ATOM   6103 O OD1 . ASN   D 1 99  ? -41.730 10.832  27.946  1.00 43.61 ? 78  ASN   D OD1 1 
ATOM   6104 N ND2 . ASN   D 1 99  ? -43.256 9.906   26.576  1.00 44.11 ? 78  ASN   D ND2 1 
ATOM   6105 N N   . SER   D 1 100 ? -42.066 6.547   30.803  1.00 31.09 ? 79  SER   D N   1 
ATOM   6106 C CA  . SER   D 1 100 ? -42.486 5.686   31.892  1.00 35.44 ? 79  SER   D CA  1 
ATOM   6107 C C   . SER   D 1 100 ? -41.742 6.002   33.172  1.00 36.99 ? 79  SER   D C   1 
ATOM   6108 O O   . SER   D 1 100 ? -42.317 5.941   34.256  1.00 37.15 ? 79  SER   D O   1 
ATOM   6109 C CB  . SER   D 1 100 ? -42.344 4.246   31.549  1.00 38.95 ? 79  SER   D CB  1 
ATOM   6110 O OG  . SER   D 1 100 ? -43.372 3.978   30.612  1.00 45.43 ? 79  SER   D OG  1 
ATOM   6111 N N   . CYS   D 1 101 ? -40.443 6.275   33.050  1.00 30.54 ? 80  CYS   D N   1 
ATOM   6112 C CA  . CYS   D 1 101 ? -39.637 6.532   34.225  1.00 33.68 ? 80  CYS   D CA  1 
ATOM   6113 C C   . CYS   D 1 101 ? -40.086 7.857   34.850  1.00 35.59 ? 80  CYS   D C   1 
ATOM   6114 O O   . CYS   D 1 101 ? -40.114 7.993   36.081  1.00 37.15 ? 80  CYS   D O   1 
ATOM   6115 C CB  . CYS   D 1 101 ? -38.150 6.620   33.869  1.00 31.17 ? 80  CYS   D CB  1 
ATOM   6116 S SG  . CYS   D 1 101 ? -37.031 6.487   35.281  1.00 31.98 ? 80  CYS   D SG  1 
ATOM   6117 N N   . PHE   D 1 102 ? -40.406 8.834   34.001  1.00 35.51 ? 81  PHE   D N   1 
ATOM   6118 C CA  . PHE   D 1 102 ? -40.814 10.132  34.512  1.00 38.32 ? 81  PHE   D CA  1 
ATOM   6119 C C   . PHE   D 1 102 ? -42.202 10.025  35.147  1.00 44.26 ? 81  PHE   D C   1 
ATOM   6120 O O   . PHE   D 1 102 ? -42.467 10.670  36.163  1.00 44.30 ? 81  PHE   D O   1 
ATOM   6121 C CB  . PHE   D 1 102 ? -40.785 11.229  33.447  1.00 38.52 ? 81  PHE   D CB  1 
ATOM   6122 C CG  . PHE   D 1 102 ? -39.383 11.770  33.221  1.00 39.06 ? 81  PHE   D CG  1 
ATOM   6123 C CD1 . PHE   D 1 102 ? -38.501 11.119  32.358  1.00 40.89 ? 81  PHE   D CD1 1 
ATOM   6124 C CD2 . PHE   D 1 102 ? -38.938 12.907  33.887  1.00 37.32 ? 81  PHE   D CD2 1 
ATOM   6125 C CE1 . PHE   D 1 102 ? -37.210 11.601  32.168  1.00 40.62 ? 81  PHE   D CE1 1 
ATOM   6126 C CE2 . PHE   D 1 102 ? -37.660 13.402  33.669  1.00 41.21 ? 81  PHE   D CE2 1 
ATOM   6127 C CZ  . PHE   D 1 102 ? -36.792 12.746  32.819  1.00 41.02 ? 81  PHE   D CZ  1 
ATOM   6128 N N   . ARG   D 1 103 ? -43.073 9.208   34.548  1.00 40.99 ? 82  ARG   D N   1 
ATOM   6129 C CA  . ARG   D 1 103 ? -44.434 9.038   35.046  1.00 47.15 ? 82  ARG   D CA  1 
ATOM   6130 C C   . ARG   D 1 103 ? -44.406 8.378   36.426  1.00 42.88 ? 82  ARG   D C   1 
ATOM   6131 O O   . ARG   D 1 103 ? -45.076 8.851   37.353  1.00 41.72 ? 82  ARG   D O   1 
ATOM   6132 C CB  . ARG   D 1 103 ? -45.330 8.332   34.014  1.00 44.72 ? 82  ARG   D CB  1 
ATOM   6133 C CG  . ARG   D 1 103 ? -46.662 7.707   34.413  1.00 54.38 ? 82  ARG   D CG  1 
ATOM   6134 C CD  . ARG   D 1 103 ? -47.153 6.689   33.372  1.00 48.70 ? 82  ARG   D CD  1 
ATOM   6135 N NE  . ARG   D 1 103 ? -46.881 7.191   32.020  1.00 46.39 ? 82  ARG   D NE  1 
ATOM   6136 C CZ  . ARG   D 1 103 ? -46.312 6.499   31.026  1.00 38.46 ? 82  ARG   D CZ  1 
ATOM   6137 N NH1 . ARG   D 1 103 ? -46.131 5.191   31.116  1.00 40.28 ? 82  ARG   D NH1 1 
ATOM   6138 N NH2 . ARG   D 1 103 ? -45.955 7.137   29.939  1.00 38.82 ? 82  ARG   D NH2 1 
ATOM   6139 N N   . ALA   D 1 104 ? -43.617 7.303   36.572  1.00 38.62 ? 83  ALA   D N   1 
ATOM   6140 C CA  . ALA   D 1 104 ? -43.520 6.611   37.853  1.00 38.10 ? 83  ALA   D CA  1 
ATOM   6141 C C   . ALA   D 1 104 ? -42.701 7.379   38.893  1.00 42.23 ? 83  ALA   D C   1 
ATOM   6142 O O   . ALA   D 1 104 ? -43.041 7.303   40.078  1.00 45.41 ? 83  ALA   D O   1 
ATOM   6143 C CB  . ALA   D 1 104 ? -43.023 5.189   37.705  1.00 35.40 ? 83  ALA   D CB  1 
ATOM   6144 N N   . PHE   D 1 105 ? -41.644 8.115   38.498  1.00 37.46 ? 84  PHE   D N   1 
ATOM   6145 C CA  . PHE   D 1 105 ? -40.684 8.538   39.511  1.00 33.62 ? 84  PHE   D CA  1 
ATOM   6146 C C   . PHE   D 1 105 ? -40.339 10.023  39.476  1.00 31.43 ? 84  PHE   D C   1 
ATOM   6147 O O   . PHE   D 1 105 ? -39.561 10.477  40.313  1.00 37.42 ? 84  PHE   D O   1 
ATOM   6148 C CB  . PHE   D 1 105 ? -39.381 7.744   39.475  1.00 39.82 ? 84  PHE   D CB  1 
ATOM   6149 C CG  . PHE   D 1 105 ? -39.572 6.241   39.574  1.00 40.55 ? 84  PHE   D CG  1 
ATOM   6150 C CD1 . PHE   D 1 105 ? -40.060 5.664   40.738  1.00 36.65 ? 84  PHE   D CD1 1 
ATOM   6151 C CD2 . PHE   D 1 105 ? -39.224 5.411   38.509  1.00 40.57 ? 84  PHE   D CD2 1 
ATOM   6152 C CE1 . PHE   D 1 105 ? -40.230 4.290   40.824  1.00 40.88 ? 84  PHE   D CE1 1 
ATOM   6153 C CE2 . PHE   D 1 105 ? -39.377 4.036   38.595  1.00 36.16 ? 84  PHE   D CE2 1 
ATOM   6154 C CZ  . PHE   D 1 105 ? -39.875 3.474   39.764  1.00 43.93 ? 84  PHE   D CZ  1 
ATOM   6155 N N   . GLY   D 1 106 ? -40.863 10.742  38.485  1.00 34.37 ? 85  GLY   D N   1 
ATOM   6156 C CA  . GLY   D 1 106 ? -40.674 12.170  38.283  1.00 38.79 ? 85  GLY   D CA  1 
ATOM   6157 C C   . GLY   D 1 106 ? -39.254 12.556  37.866  1.00 39.22 ? 85  GLY   D C   1 
ATOM   6158 O O   . GLY   D 1 106 ? -38.916 13.746  37.855  1.00 36.12 ? 85  GLY   D O   1 
ATOM   6159 N N   . ARG   D 1 107 ? -38.418 11.562  37.525  1.00 37.68 ? 86  ARG   D N   1 
ATOM   6160 C CA  . ARG   D 1 107 ? -37.067 11.868  37.051  1.00 35.23 ? 86  ARG   D CA  1 
ATOM   6161 C C   . ARG   D 1 107 ? -36.496 10.637  36.341  1.00 33.99 ? 86  ARG   D C   1 
ATOM   6162 O O   . ARG   D 1 107 ? -37.021 9.541   36.501  1.00 35.30 ? 86  ARG   D O   1 
ATOM   6163 C CB  . ARG   D 1 107 ? -36.146 12.214  38.229  1.00 31.97 ? 86  ARG   D CB  1 
ATOM   6164 C CG  . ARG   D 1 107 ? -36.101 11.105  39.267  1.00 36.52 ? 86  ARG   D CG  1 
ATOM   6165 C CD  . ARG   D 1 107 ? -35.476 11.579  40.574  1.00 37.05 ? 86  ARG   D CD  1 
ATOM   6166 N NE  . ARG   D 1 107 ? -34.070 11.955  40.441  1.00 37.39 ? 86  ARG   D NE  1 
ATOM   6167 C CZ  . ARG   D 1 107 ? -33.331 12.520  41.382  1.00 40.22 ? 86  ARG   D CZ  1 
ATOM   6168 N NH1 . ARG   D 1 107 ? -33.877 12.911  42.523  1.00 37.87 ? 86  ARG   D NH1 1 
ATOM   6169 N NH2 . ARG   D 1 107 ? -32.056 12.708  41.163  1.00 34.93 ? 86  ARG   D NH2 1 
ATOM   6170 N N   . CYS   D 1 108 ? -35.383 10.828  35.613  1.00 36.95 ? 87  CYS   D N   1 
ATOM   6171 C CA  . CYS   D 1 108 ? -34.645 9.725   34.997  1.00 35.31 ? 87  CYS   D CA  1 
ATOM   6172 C C   . CYS   D 1 108 ? -33.156 10.074  34.984  1.00 29.73 ? 87  CYS   D C   1 
ATOM   6173 O O   . CYS   D 1 108 ? -32.735 10.971  34.263  1.00 31.95 ? 87  CYS   D O   1 
ATOM   6174 C CB  . CYS   D 1 108 ? -35.133 9.455   33.574  1.00 34.40 ? 87  CYS   D CB  1 
ATOM   6175 S SG  . CYS   D 1 108 ? -34.435 7.922   32.900  1.00 31.40 ? 87  CYS   D SG  1 
ATOM   6176 N N   . ASP   D 1 109 ? -32.388 9.431   35.870  1.00 29.44 ? 88  ASP   D N   1 
ATOM   6177 C CA  . ASP   D 1 109 ? -30.991 9.801   36.071  1.00 29.10 ? 88  ASP   D CA  1 
ATOM   6178 C C   . ASP   D 1 109 ? -30.030 8.906   35.265  1.00 30.26 ? 88  ASP   D C   1 
ATOM   6179 O O   . ASP   D 1 109 ? -28.930 9.336   34.962  1.00 30.40 ? 88  ASP   D O   1 
ATOM   6180 C CB  . ASP   D 1 109 ? -30.624 9.707   37.543  1.00 31.95 ? 88  ASP   D CB  1 
ATOM   6181 C CG  . ASP   D 1 109 ? -31.502 10.615  38.395  1.00 32.97 ? 88  ASP   D CG  1 
ATOM   6182 O OD1 . ASP   D 1 109 ? -31.117 11.795  38.548  1.00 36.86 ? 88  ASP   D OD1 1 
ATOM   6183 O OD2 . ASP   D 1 109 ? -32.620 10.169  38.754  1.00 34.84 ? 88  ASP   D OD2 1 
ATOM   6184 N N   . VAL   D 1 110 ? -30.401 7.637   35.063  1.00 29.86 ? 89  VAL   D N   1 
ATOM   6185 C CA  . VAL   D 1 110 ? -29.518 6.604   34.535  1.00 29.53 ? 89  VAL   D CA  1 
ATOM   6186 C C   . VAL   D 1 110 ? -30.275 5.768   33.499  1.00 29.84 ? 89  VAL   D C   1 
ATOM   6187 O O   . VAL   D 1 110 ? -31.421 5.382   33.712  1.00 28.94 ? 89  VAL   D O   1 
ATOM   6188 C CB  . VAL   D 1 110 ? -28.960 5.698   35.646  1.00 28.13 ? 89  VAL   D CB  1 
ATOM   6189 C CG1 . VAL   D 1 110 ? -28.431 4.389   35.063  1.00 27.89 ? 89  VAL   D CG1 1 
ATOM   6190 C CG2 . VAL   D 1 110 ? -27.897 6.403   36.478  1.00 26.96 ? 89  VAL   D CG2 1 
ATOM   6191 N N   . LEU   D 1 111 ? -29.644 5.556   32.327  1.00 26.26 ? 90  LEU   D N   1 
ATOM   6192 C CA  . LEU   D 1 111 ? -30.183 4.672   31.310  1.00 24.44 ? 90  LEU   D CA  1 
ATOM   6193 C C   . LEU   D 1 111 ? -29.137 3.577   31.109  1.00 26.09 ? 90  LEU   D C   1 
ATOM   6194 O O   . LEU   D 1 111 ? -27.952 3.897   30.892  1.00 24.29 ? 90  LEU   D O   1 
ATOM   6195 C CB  . LEU   D 1 111 ? -30.469 5.469   30.029  1.00 25.05 ? 90  LEU   D CB  1 
ATOM   6196 C CG  . LEU   D 1 111 ? -30.632 4.633   28.754  1.00 22.88 ? 90  LEU   D CG  1 
ATOM   6197 C CD1 . LEU   D 1 111 ? -31.885 3.758   28.923  1.00 22.65 ? 90  LEU   D CD1 1 
ATOM   6198 C CD2 . LEU   D 1 111 ? -30.723 5.474   27.476  1.00 22.68 ? 90  LEU   D CD2 1 
ATOM   6199 N N   . VAL   D 1 112 ? -29.582 2.317   31.216  1.00 24.07 ? 91  VAL   D N   1 
ATOM   6200 C CA  . VAL   D 1 112 ? -28.717 1.160   30.966  1.00 26.79 ? 91  VAL   D CA  1 
ATOM   6201 C C   . VAL   D 1 112 ? -29.244 0.424   29.732  1.00 27.04 ? 91  VAL   D C   1 
ATOM   6202 O O   . VAL   D 1 112 ? -30.325 -0.180  29.777  1.00 26.35 ? 91  VAL   D O   1 
ATOM   6203 C CB  . VAL   D 1 112 ? -28.546 0.197   32.168  1.00 25.75 ? 91  VAL   D CB  1 
ATOM   6204 C CG1 . VAL   D 1 112 ? -27.641 -0.971  31.804  1.00 27.43 ? 91  VAL   D CG1 1 
ATOM   6205 C CG2 . VAL   D 1 112 ? -27.947 0.930   33.364  1.00 24.23 ? 91  VAL   D CG2 1 
ATOM   6206 N N   . ASN   D 1 113 ? -28.467 0.474   28.615  1.00 24.25 ? 92  ASN   D N   1 
ATOM   6207 C CA  . ASN   D 1 113 ? -28.860 -0.162  27.363  1.00 21.87 ? 92  ASN   D CA  1 
ATOM   6208 C C   . ASN   D 1 113 ? -28.344 -1.596  27.355  1.00 25.16 ? 92  ASN   D C   1 
ATOM   6209 O O   . ASN   D 1 113 ? -27.181 -1.844  26.998  1.00 26.22 ? 92  ASN   D O   1 
ATOM   6210 C CB  . ASN   D 1 113 ? -28.379 0.612   26.125  1.00 22.78 ? 92  ASN   D CB  1 
ATOM   6211 C CG  . ASN   D 1 113 ? -29.217 1.846   25.866  1.00 25.49 ? 92  ASN   D CG  1 
ATOM   6212 O OD1 . ASN   D 1 113 ? -30.450 1.772   25.743  1.00 25.98 ? 92  ASN   D OD1 1 
ATOM   6213 N ND2 . ASN   D 1 113 ? -28.588 3.012   25.836  1.00 23.72 ? 92  ASN   D ND2 1 
ATOM   6214 N N   . ASN   D 1 114 ? -29.189 -2.544  27.792  1.00 24.27 ? 93  ASN   D N   1 
ATOM   6215 C CA  . ASN   D 1 114 ? -28.785 -3.923  28.036  1.00 24.42 ? 93  ASN   D CA  1 
ATOM   6216 C C   . ASN   D 1 114 ? -29.499 -4.895  27.077  1.00 26.85 ? 93  ASN   D C   1 
ATOM   6217 O O   . ASN   D 1 114 ? -28.928 -5.928  26.741  1.00 25.89 ? 93  ASN   D O   1 
ATOM   6218 C CB  . ASN   D 1 114 ? -28.970 -4.322  29.516  1.00 24.83 ? 93  ASN   D CB  1 
ATOM   6219 C CG  . ASN   D 1 114 ? -28.892 -5.819  29.758  1.00 26.03 ? 93  ASN   D CG  1 
ATOM   6220 O OD1 . ASN   D 1 114 ? -27.811 -6.373  30.010  1.00 29.38 ? 93  ASN   D OD1 1 
ATOM   6221 N ND2 . ASN   D 1 114 ? -30.028 -6.513  29.689  1.00 26.61 ? 93  ASN   D ND2 1 
ATOM   6222 N N   . ALA   D 1 115 ? -30.760 -4.619  26.691  1.00 25.52 ? 94  ALA   D N   1 
ATOM   6223 C CA  . ALA   D 1 115 ? -31.521 -5.513  25.827  1.00 25.66 ? 94  ALA   D CA  1 
ATOM   6224 C C   . ALA   D 1 115 ? -30.718 -5.802  24.556  1.00 28.94 ? 94  ALA   D C   1 
ATOM   6225 O O   . ALA   D 1 115 ? -30.122 -4.899  23.985  1.00 27.88 ? 94  ALA   D O   1 
ATOM   6226 C CB  . ALA   D 1 115 ? -32.864 -4.927  25.470  1.00 28.24 ? 94  ALA   D CB  1 
ATOM   6227 N N   . SER   D 1 116 ? -30.771 -7.053  24.105  1.00 27.06 ? 95  SER   D N   1 
ATOM   6228 C CA  . SER   D 1 116 ? -29.962 -7.451  22.964  1.00 28.10 ? 95  SER   D CA  1 
ATOM   6229 C C   . SER   D 1 116 ? -30.535 -8.706  22.314  1.00 28.58 ? 95  SER   D C   1 
ATOM   6230 O O   . SER   D 1 116 ? -30.810 -9.679  23.002  1.00 29.16 ? 95  SER   D O   1 
ATOM   6231 C CB  . SER   D 1 116 ? -28.546 -7.701  23.408  1.00 26.17 ? 95  SER   D CB  1 
ATOM   6232 O OG  . SER   D 1 116 ? -27.784 -8.314  22.373  1.00 29.02 ? 95  SER   D OG  1 
ATOM   6233 N N   . ALA   D 1 117 ? -30.635 -8.697  20.977  1.00 29.00 ? 96  ALA   D N   1 
ATOM   6234 C CA  . ALA   D 1 117 ? -30.912 -9.899  20.203  1.00 25.52 ? 96  ALA   D CA  1 
ATOM   6235 C C   . ALA   D 1 117 ? -29.585 -10.513 19.772  1.00 29.12 ? 96  ALA   D C   1 
ATOM   6236 O O   . ALA   D 1 117 ? -28.603 -9.802  19.548  1.00 25.29 ? 96  ALA   D O   1 
ATOM   6237 C CB  . ALA   D 1 117 ? -31.819 -9.570  19.035  1.00 25.90 ? 96  ALA   D CB  1 
ATOM   6238 N N   . PHE   D 1 118 ? -29.524 -11.854 19.725  1.00 25.76 ? 97  PHE   D N   1 
ATOM   6239 C CA  . PHE   D 1 118 ? -28.248 -12.477 19.461  1.00 27.34 ? 97  PHE   D CA  1 
ATOM   6240 C C   . PHE   D 1 118 ? -28.519 -13.811 18.784  1.00 29.83 ? 97  PHE   D C   1 
ATOM   6241 O O   . PHE   D 1 118 ? -29.023 -14.723 19.430  1.00 32.81 ? 97  PHE   D O   1 
ATOM   6242 C CB  . PHE   D 1 118 ? -27.456 -12.724 20.754  1.00 30.78 ? 97  PHE   D CB  1 
ATOM   6243 C CG  . PHE   D 1 118 ? -26.187 -13.559 20.564  1.00 30.99 ? 97  PHE   D CG  1 
ATOM   6244 C CD1 . PHE   D 1 118 ? -24.975 -12.953 20.229  1.00 32.20 ? 97  PHE   D CD1 1 
ATOM   6245 C CD2 . PHE   D 1 118 ? -26.187 -14.949 20.740  1.00 36.25 ? 97  PHE   D CD2 1 
ATOM   6246 C CE1 . PHE   D 1 118 ? -23.807 -13.688 20.039  1.00 33.71 ? 97  PHE   D CE1 1 
ATOM   6247 C CE2 . PHE   D 1 118 ? -25.011 -15.686 20.588  1.00 39.57 ? 97  PHE   D CE2 1 
ATOM   6248 C CZ  . PHE   D 1 118 ? -23.811 -15.057 20.259  1.00 36.20 ? 97  PHE   D CZ  1 
ATOM   6249 N N   . TYR   D 1 119 ? -28.172 -13.924 17.500  1.00 26.00 ? 98  TYR   D N   1 
ATOM   6250 C CA  . TYR   D 1 119 ? -28.298 -15.207 16.817  1.00 23.39 ? 98  TYR   D CA  1 
ATOM   6251 C C   . TYR   D 1 119 ? -27.529 -15.093 15.503  1.00 26.56 ? 98  TYR   D C   1 
ATOM   6252 O O   . TYR   D 1 119 ? -27.260 -13.975 15.058  1.00 24.08 ? 98  TYR   D O   1 
ATOM   6253 C CB  . TYR   D 1 119 ? -29.768 -15.539 16.538  1.00 28.16 ? 98  TYR   D CB  1 
ATOM   6254 C CG  . TYR   D 1 119 ? -30.648 -14.493 15.863  1.00 26.31 ? 98  TYR   D CG  1 
ATOM   6255 C CD1 . TYR   D 1 119 ? -30.682 -14.326 14.480  1.00 26.63 ? 98  TYR   D CD1 1 
ATOM   6256 C CD2 . TYR   D 1 119 ? -31.510 -13.708 16.638  1.00 29.55 ? 98  TYR   D CD2 1 
ATOM   6257 C CE1 . TYR   D 1 119 ? -31.538 -13.395 13.892  1.00 27.87 ? 98  TYR   D CE1 1 
ATOM   6258 C CE2 . TYR   D 1 119 ? -32.357 -12.777 16.065  1.00 29.10 ? 98  TYR   D CE2 1 
ATOM   6259 C CZ  . TYR   D 1 119 ? -32.346 -12.599 14.692  1.00 25.76 ? 98  TYR   D CZ  1 
ATOM   6260 O OH  . TYR   D 1 119 ? -33.194 -11.671 14.165  1.00 29.67 ? 98  TYR   D OH  1 
ATOM   6261 N N   . PRO   D 1 120 ? -27.156 -16.225 14.872  1.00 27.48 ? 99  PRO   D N   1 
ATOM   6262 C CA  . PRO   D 1 120 ? -26.356 -16.201 13.654  1.00 29.15 ? 99  PRO   D CA  1 
ATOM   6263 C C   . PRO   D 1 120 ? -27.174 -15.663 12.483  1.00 25.76 ? 99  PRO   D C   1 
ATOM   6264 O O   . PRO   D 1 120 ? -28.358 -15.920 12.357  1.00 25.96 ? 99  PRO   D O   1 
ATOM   6265 C CB  . PRO   D 1 120 ? -25.885 -17.657 13.390  1.00 31.41 ? 99  PRO   D CB  1 
ATOM   6266 C CG  . PRO   D 1 120 ? -26.604 -18.504 14.434  1.00 31.48 ? 99  PRO   D CG  1 
ATOM   6267 C CD  . PRO   D 1 120 ? -27.409 -17.608 15.369  1.00 29.51 ? 99  PRO   D CD  1 
ATOM   6268 N N   . THR   D 1 121 ? -26.491 -14.970 11.573  1.00 25.79 ? 100 THR   D N   1 
ATOM   6269 C CA  . THR   D 1 121 ? -27.033 -14.466 10.321  1.00 23.19 ? 100 THR   D CA  1 
ATOM   6270 C C   . THR   D 1 121 ? -25.987 -14.730 9.254   1.00 26.91 ? 100 THR   D C   1 
ATOM   6271 O O   . THR   D 1 121 ? -25.258 -13.810 8.893   1.00 25.12 ? 100 THR   D O   1 
ATOM   6272 C CB  . THR   D 1 121 ? -27.299 -12.955 10.410  1.00 26.41 ? 100 THR   D CB  1 
ATOM   6273 O OG1 . THR   D 1 121 ? -26.067 -12.310 10.757  1.00 24.97 ? 100 THR   D OG1 1 
ATOM   6274 C CG2 . THR   D 1 121 ? -28.365 -12.643 11.447  1.00 23.33 ? 100 THR   D CG2 1 
ATOM   6275 N N   . PRO   D 1 122 ? -25.837 -15.989 8.767   1.00 26.65 ? 101 PRO   D N   1 
ATOM   6276 C CA  . PRO   D 1 122 ? -24.752 -16.331 7.839   1.00 26.27 ? 101 PRO   D CA  1 
ATOM   6277 C C   . PRO   D 1 122 ? -24.858 -15.533 6.553   1.00 24.91 ? 101 PRO   D C   1 
ATOM   6278 O O   . PRO   D 1 122 ? -25.965 -15.273 6.071   1.00 27.91 ? 101 PRO   D O   1 
ATOM   6279 C CB  . PRO   D 1 122 ? -24.868 -17.848 7.548   1.00 28.01 ? 101 PRO   D CB  1 
ATOM   6280 C CG  . PRO   D 1 122 ? -26.109 -18.271 8.272   1.00 31.24 ? 101 PRO   D CG  1 
ATOM   6281 C CD  . PRO   D 1 122 ? -26.655 -17.156 9.165   1.00 31.19 ? 101 PRO   D CD  1 
ATOM   6282 N N   . LEU   D 1 123 ? -23.691 -15.180 5.984   1.00 24.90 ? 102 LEU   D N   1 
ATOM   6283 C CA  . LEU   D 1 123 ? -23.658 -14.448 4.722   1.00 24.07 ? 102 LEU   D CA  1 
ATOM   6284 C C   . LEU   D 1 123 ? -24.012 -15.401 3.588   1.00 31.31 ? 102 LEU   D C   1 
ATOM   6285 O O   . LEU   D 1 123 ? -24.526 -14.947 2.570   1.00 30.75 ? 102 LEU   D O   1 
ATOM   6286 C CB  . LEU   D 1 123 ? -22.281 -13.835 4.457   1.00 23.87 ? 102 LEU   D CB  1 
ATOM   6287 C CG  . LEU   D 1 123 ? -21.882 -12.747 5.463   1.00 26.57 ? 102 LEU   D CG  1 
ATOM   6288 C CD1 . LEU   D 1 123 ? -20.427 -12.340 5.352   1.00 24.99 ? 102 LEU   D CD1 1 
ATOM   6289 C CD2 . LEU   D 1 123 ? -22.778 -11.557 5.246   1.00 26.88 ? 102 LEU   D CD2 1 
ATOM   6290 N N   . VAL   D 1 124 ? -23.685 -16.689 3.749   1.00 31.88 ? 103 VAL   D N   1 
ATOM   6291 C CA  . VAL   D 1 124 ? -23.914 -17.604 2.632   1.00 41.16 ? 103 VAL   D CA  1 
ATOM   6292 C C   . VAL   D 1 124 ? -25.009 -18.635 2.982   1.00 49.46 ? 103 VAL   D C   1 
ATOM   6293 O O   . VAL   D 1 124 ? -24.851 -19.282 4.031   1.00 44.80 ? 103 VAL   D O   1 
ATOM   6294 C CB  . VAL   D 1 124 ? -22.605 -18.240 2.127   1.00 40.69 ? 103 VAL   D CB  1 
ATOM   6295 C CG1 . VAL   D 1 124 ? -22.851 -19.375 1.141   1.00 46.73 ? 103 VAL   D CG1 1 
ATOM   6296 C CG2 . VAL   D 1 124 ? -21.693 -17.178 1.504   1.00 39.82 ? 103 VAL   D CG2 1 
ATOM   6297 N N   . GLY   D 1 134 ? -35.987 -19.049 10.724  1.00 78.22 ? 113 GLY   D N   1 
ATOM   6298 C CA  . GLY   D 1 134 ? -36.911 -18.952 9.574   1.00 69.80 ? 113 GLY   D CA  1 
ATOM   6299 C C   . GLY   D 1 134 ? -37.335 -17.510 9.292   1.00 66.55 ? 113 GLY   D C   1 
ATOM   6300 O O   . GLY   D 1 134 ? -38.293 -17.279 8.552   1.00 71.12 ? 113 GLY   D O   1 
ATOM   6301 N N   . LYS   D 1 135 ? -36.596 -16.550 9.868   1.00 56.50 ? 114 LYS   D N   1 
ATOM   6302 C CA  . LYS   D 1 135 ? -36.853 -15.122 9.715   1.00 44.78 ? 114 LYS   D CA  1 
ATOM   6303 C C   . LYS   D 1 135 ? -36.289 -14.637 8.386   1.00 38.21 ? 114 LYS   D C   1 
ATOM   6304 O O   . LYS   D 1 135 ? -35.241 -15.130 7.961   1.00 38.29 ? 114 LYS   D O   1 
ATOM   6305 C CB  . LYS   D 1 135 ? -36.097 -14.402 10.839  1.00 44.71 ? 114 LYS   D CB  1 
ATOM   6306 C CG  . LYS   D 1 135 ? -36.352 -15.015 12.194  1.00 43.78 ? 114 LYS   D CG  1 
ATOM   6307 C CD  . LYS   D 1 135 ? -35.711 -14.198 13.303  1.00 48.59 ? 114 LYS   D CD  1 
ATOM   6308 C CE  . LYS   D 1 135 ? -36.513 -14.358 14.552  1.00 41.92 ? 114 LYS   D CE  1 
ATOM   6309 N NZ  . LYS   D 1 135 ? -35.794 -13.808 15.694  1.00 49.72 ? 114 LYS   D NZ  1 
ATOM   6310 N N   . THR   D 1 136 ? -36.970 -13.669 7.759   1.00 32.04 ? 115 THR   D N   1 
ATOM   6311 C CA  . THR   D 1 136 ? -36.465 -12.991 6.576   1.00 32.95 ? 115 THR   D CA  1 
ATOM   6312 C C   . THR   D 1 136 ? -35.216 -12.199 6.959   1.00 31.36 ? 115 THR   D C   1 
ATOM   6313 O O   . THR   D 1 136 ? -35.027 -11.851 8.135   1.00 29.71 ? 115 THR   D O   1 
ATOM   6314 C CB  . THR   D 1 136 ? -37.453 -12.013 5.935   1.00 35.42 ? 115 THR   D CB  1 
ATOM   6315 O OG1 . THR   D 1 136 ? -37.717 -11.018 6.914   1.00 35.67 ? 115 THR   D OG1 1 
ATOM   6316 C CG2 . THR   D 1 136 ? -38.734 -12.639 5.411   1.00 39.56 ? 115 THR   D CG2 1 
ATOM   6317 N N   . VAL   D 1 137 ? -34.475 -11.801 5.915   1.00 31.07 ? 116 VAL   D N   1 
ATOM   6318 C CA  . VAL   D 1 137 ? -33.262 -11.030 6.168   1.00 31.00 ? 116 VAL   D CA  1 
ATOM   6319 C C   . VAL   D 1 137 ? -33.664 -9.654  6.701   1.00 32.38 ? 116 VAL   D C   1 
ATOM   6320 O O   . VAL   D 1 137 ? -32.990 -9.110  7.580   1.00 30.92 ? 116 VAL   D O   1 
ATOM   6321 C CB  . VAL   D 1 137 ? -32.245 -10.982 5.009   1.00 32.66 ? 116 VAL   D CB  1 
ATOM   6322 C CG1 . VAL   D 1 137 ? -32.716 -10.150 3.834   1.00 36.19 ? 116 VAL   D CG1 1 
ATOM   6323 C CG2 . VAL   D 1 137 ? -30.889 -10.469 5.495   1.00 36.19 ? 116 VAL   D CG2 1 
ATOM   6324 N N   . GLU   D 1 138 ? -34.791 -9.104  6.219   1.00 32.51 ? 117 GLU   D N   1 
ATOM   6325 C CA  . GLU   D 1 138 ? -35.251 -7.805  6.734   1.00 32.41 ? 117 GLU   D CA  1 
ATOM   6326 C C   . GLU   D 1 138 ? -35.559 -7.839  8.240   1.00 30.46 ? 117 GLU   D C   1 
ATOM   6327 O O   . GLU   D 1 138 ? -35.243 -6.881  8.951   1.00 28.78 ? 117 GLU   D O   1 
ATOM   6328 C CB  . GLU   D 1 138 ? -36.344 -7.079  5.940   1.00 38.39 ? 117 GLU   D CB  1 
ATOM   6329 C CG  . GLU   D 1 138 ? -37.305 -7.988  5.183   1.00 41.76 ? 117 GLU   D CG  1 
ATOM   6330 C CD  . GLU   D 1 138 ? -36.760 -8.687  3.939   1.00 52.02 ? 117 GLU   D CD  1 
ATOM   6331 O OE1 . GLU   D 1 138 ? -36.721 -8.096  2.840   1.00 59.11 ? 117 GLU   D OE1 1 
ATOM   6332 O OE2 . GLU   D 1 138 ? -36.328 -9.838  4.086   1.00 49.13 ? 117 GLU   D OE2 1 
ATOM   6333 N N   . THR   D 1 139 ? -36.151 -8.931  8.735   1.00 31.80 ? 118 THR   D N   1 
ATOM   6334 C CA  . THR   D 1 139 ? -36.426 -9.132  10.151  1.00 28.74 ? 118 THR   D CA  1 
ATOM   6335 C C   . THR   D 1 139 ? -35.120 -9.268  10.959  1.00 26.69 ? 118 THR   D C   1 
ATOM   6336 O O   . THR   D 1 139 ? -35.049 -8.771  12.078  1.00 26.82 ? 118 THR   D O   1 
ATOM   6337 C CB  . THR   D 1 139 ? -37.282 -10.390 10.318  1.00 34.09 ? 118 THR   D CB  1 
ATOM   6338 O OG1 . THR   D 1 139 ? -38.480 -10.078 9.624   1.00 39.53 ? 118 THR   D OG1 1 
ATOM   6339 C CG2 . THR   D 1 139 ? -37.556 -10.692 11.775  1.00 32.21 ? 118 THR   D CG2 1 
ATOM   6340 N N   . GLN   D 1 140 ? -34.136 -10.035 10.446  1.00 26.26 ? 119 GLN   D N   1 
ATOM   6341 C CA  . GLN   D 1 140 ? -32.837 -10.206 11.115  1.00 26.05 ? 119 GLN   D CA  1 
ATOM   6342 C C   . GLN   D 1 140 ? -32.173 -8.837  11.276  1.00 24.23 ? 119 GLN   D C   1 
ATOM   6343 O O   . GLN   D 1 140 ? -31.628 -8.515  12.332  1.00 25.11 ? 119 GLN   D O   1 
ATOM   6344 C CB  . GLN   D 1 140 ? -31.947 -11.171 10.330  1.00 29.38 ? 119 GLN   D CB  1 
ATOM   6345 C CG  . GLN   D 1 140 ? -32.623 -12.511 10.050  1.00 33.74 ? 119 GLN   D CG  1 
ATOM   6346 C CD  . GLN   D 1 140 ? -31.667 -13.570 9.554   1.00 38.74 ? 119 GLN   D CD  1 
ATOM   6347 O OE1 . GLN   D 1 140 ? -30.718 -13.291 8.815   1.00 43.42 ? 119 GLN   D OE1 1 
ATOM   6348 N NE2 . GLN   D 1 140 ? -31.851 -14.787 10.047  1.00 51.28 ? 119 GLN   D NE2 1 
ATOM   6349 N N   . VAL   D 1 141 ? -32.221 -8.034  10.217  1.00 23.96 ? 120 VAL   D N   1 
ATOM   6350 C CA  . VAL   D 1 141 ? -31.617 -6.709  10.299  1.00 23.83 ? 120 VAL   D CA  1 
ATOM   6351 C C   . VAL   D 1 141 ? -32.361 -5.887  11.347  1.00 25.24 ? 120 VAL   D C   1 
ATOM   6352 O O   . VAL   D 1 141 ? -31.735 -5.231  12.182  1.00 24.09 ? 120 VAL   D O   1 
ATOM   6353 C CB  . VAL   D 1 141 ? -31.694 -6.001  8.936   1.00 25.20 ? 120 VAL   D CB  1 
ATOM   6354 C CG1 . VAL   D 1 141 ? -31.507 -4.490  9.066   1.00 25.89 ? 120 VAL   D CG1 1 
ATOM   6355 C CG2 . VAL   D 1 141 ? -30.772 -6.617  7.890   1.00 23.35 ? 120 VAL   D CG2 1 
ATOM   6356 N N   . ALA   D 1 142 ? -33.706 -5.941  11.327  1.00 23.60 ? 121 ALA   D N   1 
ATOM   6357 C CA  . ALA   D 1 142 ? -34.481 -5.058  12.201  1.00 27.14 ? 121 ALA   D CA  1 
ATOM   6358 C C   . ALA   D 1 142 ? -34.257 -5.394  13.681  1.00 23.69 ? 121 ALA   D C   1 
ATOM   6359 O O   . ALA   D 1 142 ? -34.177 -4.520  14.544  1.00 25.17 ? 121 ALA   D O   1 
ATOM   6360 C CB  . ALA   D 1 142 ? -35.944 -5.127  11.830  1.00 28.20 ? 121 ALA   D CB  1 
ATOM   6361 N N   . GLU   D 1 143 ? -34.168 -6.680  13.998  1.00 22.90 ? 122 GLU   D N   1 
ATOM   6362 C CA  . GLU   D 1 143 ? -34.008 -7.135  15.364  1.00 26.46 ? 122 GLU   D CA  1 
ATOM   6363 C C   . GLU   D 1 143 ? -32.592 -6.919  15.873  1.00 25.43 ? 122 GLU   D C   1 
ATOM   6364 O O   . GLU   D 1 143 ? -32.408 -6.406  16.988  1.00 25.13 ? 122 GLU   D O   1 
ATOM   6365 C CB  . GLU   D 1 143 ? -34.327 -8.626  15.557  1.00 27.70 ? 122 GLU   D CB  1 
ATOM   6366 C CG  . GLU   D 1 143 ? -35.808 -8.938  15.311  1.00 30.40 ? 122 GLU   D CG  1 
ATOM   6367 C CD  . GLU   D 1 143 ? -36.181 -10.411 15.421  1.00 39.38 ? 122 GLU   D CD  1 
ATOM   6368 O OE1 . GLU   D 1 143 ? -35.301 -11.316 15.483  1.00 34.52 ? 122 GLU   D OE1 1 
ATOM   6369 O OE2 . GLU   D 1 143 ? -37.420 -10.641 15.493  1.00 42.95 ? 122 GLU   D OE2 1 
ATOM   6370 N N   . LEU   D 1 144 ? -31.597 -7.364  15.090  1.00 22.86 ? 123 LEU   D N   1 
ATOM   6371 C CA  . LEU   D 1 144 ? -30.222 -7.331  15.554  1.00 21.28 ? 123 LEU   D CA  1 
ATOM   6372 C C   . LEU   D 1 144 ? -29.704 -5.895  15.560  1.00 21.22 ? 123 LEU   D C   1 
ATOM   6373 O O   . LEU   D 1 144 ? -29.061 -5.500  16.532  1.00 23.50 ? 123 LEU   D O   1 
ATOM   6374 C CB  . LEU   D 1 144 ? -29.301 -8.270  14.775  1.00 22.89 ? 123 LEU   D CB  1 
ATOM   6375 C CG  . LEU   D 1 144 ? -29.649 -9.760  14.914  1.00 22.50 ? 123 LEU   D CG  1 
ATOM   6376 C CD1 . LEU   D 1 144 ? -29.019 -10.577 13.813  1.00 29.32 ? 123 LEU   D CD1 1 
ATOM   6377 C CD2 . LEU   D 1 144 ? -29.006 -10.144 16.262  1.00 27.13 ? 123 LEU   D CD2 1 
ATOM   6378 N N   . ILE   D 1 145 ? -30.006 -5.100  14.514  1.00 22.07 ? 124 ILE   D N   1 
ATOM   6379 C CA  . ILE   D 1 145 ? -29.513 -3.728  14.514  1.00 20.86 ? 124 ILE   D CA  1 
ATOM   6380 C C   . ILE   D 1 145 ? -30.415 -2.847  15.389  1.00 23.41 ? 124 ILE   D C   1 
ATOM   6381 O O   . ILE   D 1 145 ? -29.950 -1.911  16.052  1.00 21.67 ? 124 ILE   D O   1 
ATOM   6382 C CB  . ILE   D 1 145 ? -29.395 -3.187  13.071  1.00 21.74 ? 124 ILE   D CB  1 
ATOM   6383 C CG1 . ILE   D 1 145 ? -28.506 -4.127  12.235  1.00 22.91 ? 124 ILE   D CG1 1 
ATOM   6384 C CG2 . ILE   D 1 145 ? -28.866 -1.739  13.063  1.00 22.17 ? 124 ILE   D CG2 1 
ATOM   6385 C CD1 . ILE   D 1 145 ? -27.077 -4.269  12.743  1.00 24.18 ? 124 ILE   D CD1 1 
ATOM   6386 N N   . GLY   D 1 146 ? -31.725 -3.125  15.398  1.00 23.55 ? 125 GLY   D N   1 
ATOM   6387 C CA  . GLY   D 1 146 ? -32.619 -2.328  16.239  1.00 21.53 ? 125 GLY   D CA  1 
ATOM   6388 C C   . GLY   D 1 146 ? -32.281 -2.490  17.716  1.00 21.10 ? 125 GLY   D C   1 
ATOM   6389 O O   . GLY   D 1 146 ? -32.079 -1.510  18.456  1.00 26.17 ? 125 GLY   D O   1 
ATOM   6390 N N   . THR   D 1 147 ? -32.166 -3.745  18.192  1.00 24.48 ? 126 THR   D N   1 
ATOM   6391 C CA  . THR   D 1 147 ? -32.003 -3.907  19.628  1.00 22.64 ? 126 THR   D CA  1 
ATOM   6392 C C   . THR   D 1 147 ? -30.624 -3.450  20.072  1.00 27.15 ? 126 THR   D C   1 
ATOM   6393 O O   . THR   D 1 147 ? -30.501 -2.810  21.095  1.00 26.69 ? 126 THR   D O   1 
ATOM   6394 C CB  . THR   D 1 147 ? -32.172 -5.353  20.105  1.00 26.85 ? 126 THR   D CB  1 
ATOM   6395 O OG1 . THR   D 1 147 ? -31.162 -6.124  19.445  1.00 27.88 ? 126 THR   D OG1 1 
ATOM   6396 C CG2 . THR   D 1 147 ? -33.578 -5.872  19.897  1.00 26.76 ? 126 THR   D CG2 1 
ATOM   6397 N N   . ASN   D 1 148 ? -29.590 -3.763  19.277  1.00 24.78 ? 127 ASN   D N   1 
ATOM   6398 C CA  . ASN   D 1 148 ? -28.220 -3.542  19.714  1.00 22.75 ? 127 ASN   D CA  1 
ATOM   6399 C C   . ASN   D 1 148 ? -27.767 -2.104  19.472  1.00 23.37 ? 127 ASN   D C   1 
ATOM   6400 O O   . ASN   D 1 148 ? -26.785 -1.678  20.085  1.00 22.83 ? 127 ASN   D O   1 
ATOM   6401 C CB  . ASN   D 1 148 ? -27.309 -4.565  19.060  1.00 24.76 ? 127 ASN   D CB  1 
ATOM   6402 C CG  . ASN   D 1 148 ? -27.458 -5.941  19.679  1.00 28.42 ? 127 ASN   D CG  1 
ATOM   6403 O OD1 . ASN   D 1 148 ? -27.144 -6.139  20.862  1.00 29.23 ? 127 ASN   D OD1 1 
ATOM   6404 N ND2 . ASN   D 1 148 ? -27.874 -6.926  18.907  1.00 25.85 ? 127 ASN   D ND2 1 
ATOM   6405 N N   . ALA   D 1 149 ? -28.414 -1.385  18.548  1.00 19.91 ? 128 ALA   D N   1 
ATOM   6406 C CA  . ALA   D 1 149 ? -27.833 -0.098  18.178  1.00 22.10 ? 128 ALA   D CA  1 
ATOM   6407 C C   . ALA   D 1 149 ? -28.891 0.995   18.044  1.00 21.93 ? 128 ALA   D C   1 
ATOM   6408 O O   . ALA   D 1 149 ? -28.749 2.079   18.628  1.00 22.69 ? 128 ALA   D O   1 
ATOM   6409 C CB  . ALA   D 1 149 ? -27.041 -0.274  16.886  1.00 22.08 ? 128 ALA   D CB  1 
ATOM   6410 N N   . ILE   D 1 150 ? -29.943 0.728   17.256  1.00 21.16 ? 129 ILE   D N   1 
ATOM   6411 C CA  . ILE   D 1 150 ? -30.900 1.792   16.966  1.00 20.74 ? 129 ILE   D CA  1 
ATOM   6412 C C   . ILE   D 1 150 ? -31.683 2.173   18.231  1.00 21.21 ? 129 ILE   D C   1 
ATOM   6413 O O   . ILE   D 1 150 ? -31.861 3.353   18.537  1.00 20.45 ? 129 ILE   D O   1 
ATOM   6414 C CB  . ILE   D 1 150 ? -31.780 1.508   15.732  1.00 19.95 ? 129 ILE   D CB  1 
ATOM   6415 C CG1 . ILE   D 1 150 ? -30.860 1.320   14.470  1.00 25.34 ? 129 ILE   D CG1 1 
ATOM   6416 C CG2 . ILE   D 1 150 ? -32.766 2.672   15.491  1.00 18.21 ? 129 ILE   D CG2 1 
ATOM   6417 C CD1 . ILE   D 1 150 ? -31.589 0.658   13.306  1.00 29.62 ? 129 ILE   D CD1 1 
ATOM   6418 N N   . ALA   D 1 151 ? -32.191 1.163   18.929  1.00 21.48 ? 130 ALA   D N   1 
ATOM   6419 C CA  . ALA   D 1 151 ? -32.934 1.434   20.151  1.00 22.22 ? 130 ALA   D CA  1 
ATOM   6420 C C   . ALA   D 1 151 ? -32.064 2.159   21.173  1.00 20.61 ? 130 ALA   D C   1 
ATOM   6421 O O   . ALA   D 1 151 ? -32.451 3.213   21.707  1.00 23.19 ? 130 ALA   D O   1 
ATOM   6422 C CB  . ALA   D 1 151 ? -33.607 0.170   20.693  1.00 22.53 ? 130 ALA   D CB  1 
ATOM   6423 N N   . PRO   D 1 152 ? -30.826 1.707   21.454  1.00 21.08 ? 131 PRO   D N   1 
ATOM   6424 C CA  . PRO   D 1 152 ? -29.930 2.536   22.253  1.00 22.13 ? 131 PRO   D CA  1 
ATOM   6425 C C   . PRO   D 1 152 ? -29.869 4.002   21.842  1.00 19.75 ? 131 PRO   D C   1 
ATOM   6426 O O   . PRO   D 1 152 ? -29.803 4.869   22.712  1.00 24.42 ? 131 PRO   D O   1 
ATOM   6427 C CB  . PRO   D 1 152 ? -28.558 1.808   22.159  1.00 20.80 ? 131 PRO   D CB  1 
ATOM   6428 C CG  . PRO   D 1 152 ? -29.001 0.376   22.104  1.00 19.05 ? 131 PRO   D CG  1 
ATOM   6429 C CD  . PRO   D 1 152 ? -30.266 0.360   21.184  1.00 20.18 ? 131 PRO   D CD  1 
ATOM   6430 N N   . PHE   D 1 153 ? -29.722 4.268   20.546  1.00 19.26 ? 132 PHE   D N   1 
ATOM   6431 C CA  . PHE   D 1 153 ? -29.620 5.652   20.093  1.00 20.86 ? 132 PHE   D CA  1 
ATOM   6432 C C   . PHE   D 1 153 ? -30.889 6.451   20.403  1.00 22.70 ? 132 PHE   D C   1 
ATOM   6433 O O   . PHE   D 1 153 ? -30.827 7.628   20.804  1.00 24.31 ? 132 PHE   D O   1 
ATOM   6434 C CB  . PHE   D 1 153 ? -29.356 5.598   18.576  1.00 20.05 ? 132 PHE   D CB  1 
ATOM   6435 C CG  . PHE   D 1 153 ? -29.632 6.895   17.826  1.00 23.30 ? 132 PHE   D CG  1 
ATOM   6436 C CD1 . PHE   D 1 153 ? -28.710 7.945   17.842  1.00 23.79 ? 132 PHE   D CD1 1 
ATOM   6437 C CD2 . PHE   D 1 153 ? -30.822 7.067   17.113  1.00 26.06 ? 132 PHE   D CD2 1 
ATOM   6438 C CE1 . PHE   D 1 153 ? -29.004 9.150   17.208  1.00 22.61 ? 132 PHE   D CE1 1 
ATOM   6439 C CE2 . PHE   D 1 153 ? -31.094 8.264   16.458  1.00 25.42 ? 132 PHE   D CE2 1 
ATOM   6440 C CZ  . PHE   D 1 153 ? -30.203 9.313   16.539  1.00 23.42 ? 132 PHE   D CZ  1 
ATOM   6441 N N   . LEU   D 1 154 ? -32.042 5.831   20.160  1.00 21.40 ? 133 LEU   D N   1 
ATOM   6442 C CA  . LEU   D 1 154 ? -33.319 6.531   20.311  1.00 20.70 ? 133 LEU   D CA  1 
ATOM   6443 C C   . LEU   D 1 154 ? -33.606 6.746   21.784  1.00 20.93 ? 133 LEU   D C   1 
ATOM   6444 O O   . LEU   D 1 154 ? -34.116 7.801   22.179  1.00 24.62 ? 133 LEU   D O   1 
ATOM   6445 C CB  . LEU   D 1 154 ? -34.410 5.684   19.653  1.00 20.43 ? 133 LEU   D CB  1 
ATOM   6446 C CG  . LEU   D 1 154 ? -34.343 5.569   18.120  1.00 22.83 ? 133 LEU   D CG  1 
ATOM   6447 C CD1 . LEU   D 1 154 ? -35.357 4.536   17.568  1.00 22.68 ? 133 LEU   D CD1 1 
ATOM   6448 C CD2 . LEU   D 1 154 ? -34.534 6.894   17.416  1.00 21.56 ? 133 LEU   D CD2 1 
ATOM   6449 N N   . LEU   D 1 155 ? -33.285 5.746   22.609  1.00 21.56 ? 134 LEU   D N   1 
ATOM   6450 C CA  . LEU   D 1 155 ? -33.382 5.897   24.053  1.00 21.35 ? 134 LEU   D CA  1 
ATOM   6451 C C   . LEU   D 1 155 ? -32.445 6.988   24.574  1.00 23.89 ? 134 LEU   D C   1 
ATOM   6452 O O   . LEU   D 1 155 ? -32.836 7.783   25.432  1.00 25.79 ? 134 LEU   D O   1 
ATOM   6453 C CB  . LEU   D 1 155 ? -33.097 4.540   24.679  1.00 23.51 ? 134 LEU   D CB  1 
ATOM   6454 C CG  . LEU   D 1 155 ? -34.215 3.523   24.488  1.00 20.96 ? 134 LEU   D CG  1 
ATOM   6455 C CD1 . LEU   D 1 155 ? -33.711 2.097   24.743  1.00 21.20 ? 134 LEU   D CD1 1 
ATOM   6456 C CD2 . LEU   D 1 155 ? -35.358 3.887   25.496  1.00 25.90 ? 134 LEU   D CD2 1 
ATOM   6457 N N   . THR   D 1 156 ? -31.236 7.092   23.995  1.00 23.23 ? 135 THR   D N   1 
ATOM   6458 C CA  . THR   D 1 156 ? -30.289 8.135   24.381  1.00 22.57 ? 135 THR   D CA  1 
ATOM   6459 C C   . THR   D 1 156 ? -30.907 9.498   24.062  1.00 23.91 ? 135 THR   D C   1 
ATOM   6460 O O   . THR   D 1 156 ? -30.817 10.451  24.867  1.00 23.41 ? 135 THR   D O   1 
ATOM   6461 C CB  . THR   D 1 156 ? -28.958 7.860   23.651  1.00 21.17 ? 135 THR   D CB  1 
ATOM   6462 O OG1 . THR   D 1 156 ? -28.430 6.678   24.272  1.00 22.92 ? 135 THR   D OG1 1 
ATOM   6463 C CG2 . THR   D 1 156 ? -27.932 8.959   23.898  1.00 20.67 ? 135 THR   D CG2 1 
ATOM   6464 N N   . MET   D 1 157 ? -31.488 9.610   22.864  1.00 25.51 ? 136 MET   D N   1 
ATOM   6465 C CA  . MET   D 1 157 ? -32.071 10.906  22.429  1.00 25.29 ? 136 MET   D CA  1 
ATOM   6466 C C   . MET   D 1 157 ? -33.199 11.293  23.388  1.00 28.19 ? 136 MET   D C   1 
ATOM   6467 O O   . MET   D 1 157 ? -33.253 12.448  23.820  1.00 27.15 ? 136 MET   D O   1 
ATOM   6468 C CB  . MET   D 1 157 ? -32.740 10.821  21.057  1.00 27.89 ? 136 MET   D CB  1 
ATOM   6469 C CG  . MET   D 1 157 ? -31.843 10.731  19.852  1.00 39.55 ? 136 MET   D CG  1 
ATOM   6470 S SD  . MET   D 1 157 ? -32.852 10.911  18.366  1.00 43.19 ? 136 MET   D SD  1 
ATOM   6471 C CE  . MET   D 1 157 ? -33.717 12.434  18.755  1.00 44.38 ? 136 MET   D CE  1 
ATOM   6472 N N   . SER   D 1 158 ? -34.093 10.350  23.643  1.00 25.72 ? 137 SER   D N   1 
ATOM   6473 C CA  . SER   D 1 158 ? -35.218 10.622  24.537  1.00 27.84 ? 137 SER   D CA  1 
ATOM   6474 C C   . SER   D 1 158 ? -34.730 10.940  25.947  1.00 29.33 ? 137 SER   D C   1 
ATOM   6475 O O   . SER   D 1 158 ? -35.236 11.872  26.584  1.00 28.41 ? 137 SER   D O   1 
ATOM   6476 C CB  . SER   D 1 158 ? -36.215 9.480   24.556  1.00 27.23 ? 137 SER   D CB  1 
ATOM   6477 O OG  . SER   D 1 158 ? -36.924 9.429   23.319  1.00 29.32 ? 137 SER   D OG  1 
ATOM   6478 N N   . PHE   D 1 159 ? -33.731 10.188  26.427  1.00 27.05 ? 138 PHE   D N   1 
ATOM   6479 C CA  . PHE   D 1 159 ? -33.174 10.458  27.741  1.00 26.74 ? 138 PHE   D CA  1 
ATOM   6480 C C   . PHE   D 1 159 ? -32.670 11.898  27.790  1.00 28.51 ? 138 PHE   D C   1 
ATOM   6481 O O   . PHE   D 1 159 ? -32.956 12.646  28.727  1.00 28.87 ? 138 PHE   D O   1 
ATOM   6482 C CB  . PHE   D 1 159 ? -32.116 9.392   28.056  1.00 28.09 ? 138 PHE   D CB  1 
ATOM   6483 C CG  . PHE   D 1 159 ? -31.391 9.614   29.382  1.00 27.04 ? 138 PHE   D CG  1 
ATOM   6484 C CD1 . PHE   D 1 159 ? -30.288 10.464  29.461  1.00 26.84 ? 138 PHE   D CD1 1 
ATOM   6485 C CD2 . PHE   D 1 159 ? -31.839 8.994   30.552  1.00 27.53 ? 138 PHE   D CD2 1 
ATOM   6486 C CE1 . PHE   D 1 159 ? -29.632 10.661  30.686  1.00 26.38 ? 138 PHE   D CE1 1 
ATOM   6487 C CE2 . PHE   D 1 159 ? -31.186 9.184   31.776  1.00 27.45 ? 138 PHE   D CE2 1 
ATOM   6488 C CZ  . PHE   D 1 159 ? -30.086 10.024  31.836  1.00 27.05 ? 138 PHE   D CZ  1 
ATOM   6489 N N   . ALA   D 1 160 ? -31.923 12.307  26.763  1.00 28.30 ? 139 ALA   D N   1 
ATOM   6490 C CA  . ALA   D 1 160 ? -31.270 13.609  26.824  1.00 31.35 ? 139 ALA   D CA  1 
ATOM   6491 C C   . ALA   D 1 160 ? -32.282 14.745  26.638  1.00 34.55 ? 139 ALA   D C   1 
ATOM   6492 O O   . ALA   D 1 160 ? -32.115 15.819  27.237  1.00 34.89 ? 139 ALA   D O   1 
ATOM   6493 C CB  . ALA   D 1 160 ? -30.151 13.704  25.797  1.00 36.48 ? 139 ALA   D CB  1 
ATOM   6494 N N   . GLN   D 1 161 ? -33.295 14.520  25.783  1.00 32.06 ? 140 GLN   D N   1 
ATOM   6495 C CA  A GLN   D 1 161 ? -34.313 15.527  25.515  0.50 36.32 ? 140 GLN   D CA  1 
ATOM   6496 C CA  B GLN   D 1 161 ? -34.307 15.536  25.519  0.50 36.11 ? 140 GLN   D CA  1 
ATOM   6497 C C   . GLN   D 1 161 ? -35.067 15.827  26.814  1.00 39.16 ? 140 GLN   D C   1 
ATOM   6498 O O   . GLN   D 1 161 ? -35.328 16.980  27.137  1.00 43.01 ? 140 GLN   D O   1 
ATOM   6499 C CB  A GLN   D 1 161 ? -35.233 15.049  24.390  0.50 36.61 ? 140 GLN   D CB  1 
ATOM   6500 C CB  B GLN   D 1 161 ? -35.291 15.192  24.397  0.50 36.23 ? 140 GLN   D CB  1 
ATOM   6501 C CG  A GLN   D 1 161 ? -35.747 16.154  23.473  0.50 44.69 ? 140 GLN   D CG  1 
ATOM   6502 C CG  B GLN   D 1 161 ? -36.169 16.374  23.983  0.50 42.12 ? 140 GLN   D CG  1 
ATOM   6503 C CD  A GLN   D 1 161 ? -34.785 16.481  22.349  0.50 48.30 ? 140 GLN   D CD  1 
ATOM   6504 C CD  B GLN   D 1 161 ? -37.640 16.036  23.845  0.50 47.57 ? 140 GLN   D CD  1 
ATOM   6505 O OE1 A GLN   D 1 161 ? -34.508 17.649  22.057  0.50 46.62 ? 140 GLN   D OE1 1 
ATOM   6506 O OE1 B GLN   D 1 161 ? -38.288 15.544  24.779  0.50 48.97 ? 140 GLN   D OE1 1 
ATOM   6507 N NE2 A GLN   D 1 161 ? -34.281 15.443  21.691  0.50 50.07 ? 140 GLN   D NE2 1 
ATOM   6508 N NE2 B GLN   D 1 161 ? -38.199 16.322  22.678  0.50 55.44 ? 140 GLN   D NE2 1 
ATOM   6509 N N   . ARG   D 1 162 ? -35.397 14.777  27.573  1.00 39.32 ? 141 ARG   D N   1 
ATOM   6510 C CA  . ARG   D 1 162 ? -36.186 14.927  28.799  1.00 40.91 ? 141 ARG   D CA  1 
ATOM   6511 C C   . ARG   D 1 162 ? -35.391 15.511  29.966  1.00 50.14 ? 141 ARG   D C   1 
ATOM   6512 O O   . ARG   D 1 162 ? -35.946 15.689  31.049  1.00 58.32 ? 141 ARG   D O   1 
ATOM   6513 C CB  . ARG   D 1 162 ? -36.802 13.606  29.274  1.00 40.69 ? 141 ARG   D CB  1 
ATOM   6514 C CG  . ARG   D 1 162 ? -37.802 12.927  28.345  1.00 46.24 ? 141 ARG   D CG  1 
ATOM   6515 C CD  . ARG   D 1 162 ? -39.209 13.504  28.250  1.00 56.57 ? 141 ARG   D CD  1 
ATOM   6516 N NE  . ARG   D 1 162 ? -39.755 13.935  29.544  1.00 65.31 ? 141 ARG   D NE  1 
ATOM   6517 C CZ  . ARG   D 1 162 ? -40.817 13.466  30.203  1.00 65.01 ? 141 ARG   D CZ  1 
ATOM   6518 N NH1 . ARG   D 1 162 ? -41.460 12.387  29.788  1.00 61.25 ? 141 ARG   D NH1 1 
ATOM   6519 N NH2 . ARG   D 1 162 ? -41.216 14.082  31.301  1.00 62.86 ? 141 ARG   D NH2 1 
ATOM   6520 N N   . GLN   D 1 163 ? -34.094 15.765  29.782  1.00 47.10 ? 142 GLN   D N   1 
ATOM   6521 C CA  . GLN   D 1 163 ? -33.301 16.339  30.857  1.00 52.30 ? 142 GLN   D CA  1 
ATOM   6522 C C   . GLN   D 1 163 ? -33.388 17.874  30.798  1.00 64.23 ? 142 GLN   D C   1 
ATOM   6523 O O   . GLN   D 1 163 ? -34.402 18.396  31.317  1.00 77.74 ? 142 GLN   D O   1 
ATOM   6524 C CB  . GLN   D 1 163 ? -31.840 15.891  30.832  1.00 46.42 ? 142 GLN   D CB  1 
ATOM   6525 C CG  . GLN   D 1 163 ? -31.642 14.386  30.953  1.00 43.96 ? 142 GLN   D CG  1 
ATOM   6526 C CD  . GLN   D 1 163 ? -32.361 13.738  32.118  1.00 44.81 ? 142 GLN   D CD  1 
ATOM   6527 O OE1 . GLN   D 1 163 ? -32.477 14.311  33.208  1.00 44.56 ? 142 GLN   D OE1 1 
ATOM   6528 N NE2 . GLN   D 1 163 ? -32.827 12.512  31.905  1.00 41.25 ? 142 GLN   D NE2 1 
ATOM   6529 N N   . SER   D 1 173 ? -27.478 16.512  38.232  1.00 58.07 ? 152 SER   D N   1 
ATOM   6530 C CA  . SER   D 1 173 ? -27.021 15.686  39.382  1.00 59.91 ? 152 SER   D CA  1 
ATOM   6531 C C   . SER   D 1 173 ? -25.850 14.804  38.941  1.00 62.12 ? 152 SER   D C   1 
ATOM   6532 O O   . SER   D 1 173 ? -24.749 15.310  38.728  1.00 73.51 ? 152 SER   D O   1 
ATOM   6533 C CB  . SER   D 1 173 ? -28.173 14.896  39.988  1.00 59.11 ? 152 SER   D CB  1 
ATOM   6534 N N   . ASN   D 1 174 ? -26.085 13.490  38.796  1.00 47.76 ? 153 ASN   D N   1 
ATOM   6535 C CA  . ASN   D 1 174 ? -25.085 12.576  38.262  1.00 42.15 ? 153 ASN   D CA  1 
ATOM   6536 C C   . ASN   D 1 174 ? -25.775 11.704  37.215  1.00 36.49 ? 153 ASN   D C   1 
ATOM   6537 O O   . ASN   D 1 174 ? -26.130 10.553  37.500  1.00 36.53 ? 153 ASN   D O   1 
ATOM   6538 C CB  . ASN   D 1 174 ? -24.434 11.781  39.394  1.00 42.26 ? 153 ASN   D CB  1 
ATOM   6539 C CG  . ASN   D 1 174 ? -23.384 10.783  38.958  1.00 48.43 ? 153 ASN   D CG  1 
ATOM   6540 O OD1 . ASN   D 1 174 ? -22.731 10.927  37.907  1.00 44.05 ? 153 ASN   D OD1 1 
ATOM   6541 N ND2 . ASN   D 1 174 ? -23.180 9.789   39.811  1.00 45.13 ? 153 ASN   D ND2 1 
ATOM   6542 N N   . LEU   D 1 175 ? -25.992 12.302  36.028  1.00 32.56 ? 154 LEU   D N   1 
ATOM   6543 C CA  . LEU   D 1 175 ? -26.734 11.684  34.934  1.00 27.89 ? 154 LEU   D CA  1 
ATOM   6544 C C   . LEU   D 1 175 ? -25.768 10.825  34.116  1.00 28.06 ? 154 LEU   D C   1 
ATOM   6545 O O   . LEU   D 1 175 ? -24.682 11.271  33.771  1.00 26.66 ? 154 LEU   D O   1 
ATOM   6546 C CB  . LEU   D 1 175 ? -27.365 12.741  34.027  1.00 29.63 ? 154 LEU   D CB  1 
ATOM   6547 C CG  . LEU   D 1 175 ? -28.272 13.794  34.690  1.00 33.85 ? 154 LEU   D CG  1 
ATOM   6548 C CD1 . LEU   D 1 175 ? -28.808 14.751  33.657  1.00 34.97 ? 154 LEU   D CD1 1 
ATOM   6549 C CD2 . LEU   D 1 175 ? -29.422 13.157  35.421  1.00 30.68 ? 154 LEU   D CD2 1 
ATOM   6550 N N   . SER   D 1 176 ? -26.168 9.593   33.790  1.00 28.58 ? 155 SER   D N   1 
ATOM   6551 C CA  . SER   D 1 176 ? -25.251 8.848   32.931  1.00 28.91 ? 155 SER   D CA  1 
ATOM   6552 C C   . SER   D 1 176 ? -25.936 7.683   32.239  1.00 28.91 ? 155 SER   D C   1 
ATOM   6553 O O   . SER   D 1 176 ? -27.005 7.224   32.647  1.00 26.06 ? 155 SER   D O   1 
ATOM   6554 C CB  . SER   D 1 176 ? -24.027 8.433   33.704  1.00 31.57 ? 155 SER   D CB  1 
ATOM   6555 O OG  . SER   D 1 176 ? -24.206 7.202   34.385  1.00 31.06 ? 155 SER   D OG  1 
ATOM   6556 N N   . ILE   D 1 177 ? -25.307 7.243   31.137  1.00 25.00 ? 156 ILE   D N   1 
ATOM   6557 C CA  . ILE   D 1 177 ? -25.840 6.153   30.341  1.00 23.79 ? 156 ILE   D CA  1 
ATOM   6558 C C   . ILE   D 1 177 ? -24.735 5.104   30.323  1.00 22.01 ? 156 ILE   D C   1 
ATOM   6559 O O   . ILE   D 1 177 ? -23.567 5.467   30.182  1.00 23.15 ? 156 ILE   D O   1 
ATOM   6560 C CB  . ILE   D 1 177 ? -26.110 6.672   28.908  1.00 25.03 ? 156 ILE   D CB  1 
ATOM   6561 C CG1 . ILE   D 1 177 ? -27.154 7.853   28.891  1.00 26.68 ? 156 ILE   D CG1 1 
ATOM   6562 C CG2 . ILE   D 1 177 ? -26.523 5.509   27.982  1.00 22.73 ? 156 ILE   D CG2 1 
ATOM   6563 C CD1 . ILE   D 1 177 ? -27.378 8.487   27.519  1.00 24.23 ? 156 ILE   D CD1 1 
ATOM   6564 N N   . VAL   D 1 178 ? -25.104 3.823   30.416  1.00 22.93 ? 157 VAL   D N   1 
ATOM   6565 C CA  . VAL   D 1 178 ? -24.156 2.720   30.291  1.00 22.38 ? 157 VAL   D CA  1 
ATOM   6566 C C   . VAL   D 1 178 ? -24.692 1.768   29.228  1.00 23.35 ? 157 VAL   D C   1 
ATOM   6567 O O   . VAL   D 1 178 ? -25.819 1.275   29.326  1.00 25.23 ? 157 VAL   D O   1 
ATOM   6568 C CB  . VAL   D 1 178 ? -23.942 1.944   31.606  1.00 24.66 ? 157 VAL   D CB  1 
ATOM   6569 C CG1 . VAL   D 1 178 ? -23.033 0.751   31.378  1.00 25.80 ? 157 VAL   D CG1 1 
ATOM   6570 C CG2 . VAL   D 1 178 ? -23.403 2.848   32.713  1.00 25.12 ? 157 VAL   D CG2 1 
ATOM   6571 N N   . ASN   D 1 179 ? -23.865 1.513   28.184  1.00 22.84 ? 158 ASN   D N   1 
ATOM   6572 C CA  . ASN   D 1 179 ? -24.228 0.632   27.078  1.00 21.48 ? 158 ASN   D CA  1 
ATOM   6573 C C   . ASN   D 1 179 ? -23.543 -0.711  27.287  1.00 21.01 ? 158 ASN   D C   1 
ATOM   6574 O O   . ASN   D 1 179 ? -22.376 -0.721  27.637  1.00 24.22 ? 158 ASN   D O   1 
ATOM   6575 C CB  . ASN   D 1 179 ? -23.742 1.241   25.758  1.00 22.93 ? 158 ASN   D CB  1 
ATOM   6576 C CG  . ASN   D 1 179 ? -24.568 2.468   25.477  1.00 24.82 ? 158 ASN   D CG  1 
ATOM   6577 O OD1 . ASN   D 1 179 ? -25.731 2.512   25.896  1.00 22.40 ? 158 ASN   D OD1 1 
ATOM   6578 N ND2 . ASN   D 1 179 ? -24.016 3.483   24.839  1.00 23.49 ? 158 ASN   D ND2 1 
ATOM   6579 N N   . LEU   D 1 180 ? -24.272 -1.822  27.098  1.00 21.45 ? 159 LEU   D N   1 
ATOM   6580 C CA  . LEU   D 1 180 ? -23.685 -3.150  27.242  1.00 22.33 ? 159 LEU   D CA  1 
ATOM   6581 C C   . LEU   D 1 180 ? -23.133 -3.543  25.875  1.00 25.62 ? 159 LEU   D C   1 
ATOM   6582 O O   . LEU   D 1 180 ? -23.891 -3.754  24.924  1.00 26.31 ? 159 LEU   D O   1 
ATOM   6583 C CB  . LEU   D 1 180 ? -24.721 -4.176  27.719  1.00 23.10 ? 159 LEU   D CB  1 
ATOM   6584 C CG  . LEU   D 1 180 ? -24.903 -4.297  29.239  1.00 21.54 ? 159 LEU   D CG  1 
ATOM   6585 C CD1 . LEU   D 1 180 ? -23.728 -5.074  29.867  1.00 22.28 ? 159 LEU   D CD1 1 
ATOM   6586 C CD2 . LEU   D 1 180 ? -24.986 -2.897  29.860  1.00 25.63 ? 159 LEU   D CD2 1 
ATOM   6587 N N   . CYS   D 1 181 ? -21.794 -3.547  25.817  1.00 23.33 ? 160 CYS   D N   1 
ATOM   6588 C CA  . CYS   D 1 181 ? -21.069 -3.749  24.570  1.00 24.01 ? 160 CYS   D CA  1 
ATOM   6589 C C   . CYS   D 1 181 ? -20.614 -5.202  24.511  1.00 27.39 ? 160 CYS   D C   1 
ATOM   6590 O O   . CYS   D 1 181 ? -21.281 -6.057  25.054  1.00 29.51 ? 160 CYS   D O   1 
ATOM   6591 C CB  . CYS   D 1 181 ? -19.896 -2.783  24.551  1.00 23.50 ? 160 CYS   D CB  1 
ATOM   6592 S SG  . CYS   D 1 181 ? -20.464 -1.061  24.422  1.00 26.49 ? 160 CYS   D SG  1 
ATOM   6593 N N   . ASP   D 1 182 ? -19.498 -5.485  23.834  1.00 24.99 ? 161 ASP   D N   1 
ATOM   6594 C CA  . ASP   D 1 182 ? -19.052 -6.875  23.701  1.00 22.41 ? 161 ASP   D CA  1 
ATOM   6595 C C   . ASP   D 1 182 ? -17.527 -6.876  23.576  1.00 25.19 ? 161 ASP   D C   1 
ATOM   6596 O O   . ASP   D 1 182 ? -16.991 -6.225  22.670  1.00 24.34 ? 161 ASP   D O   1 
ATOM   6597 C CB  . ASP   D 1 182 ? -19.818 -7.590  22.583  1.00 23.57 ? 161 ASP   D CB  1 
ATOM   6598 C CG  . ASP   D 1 182 ? -19.506 -9.068  22.458  1.00 29.14 ? 161 ASP   D CG  1 
ATOM   6599 O OD1 . ASP   D 1 182 ? -18.341 -9.438  22.701  1.00 27.59 ? 161 ASP   D OD1 1 
ATOM   6600 O OD2 . ASP   D 1 182 ? -20.452 -9.842  22.162  1.00 31.93 ? 161 ASP   D OD2 1 
ATOM   6601 N N   . ALA   D 1 183 ? -16.814 -7.534  24.528  1.00 21.99 ? 162 ALA   D N   1 
ATOM   6602 C CA  . ALA   D 1 183 ? -15.348 -7.521  24.488  1.00 20.00 ? 162 ALA   D CA  1 
ATOM   6603 C C   . ALA   D 1 183 ? -14.767 -8.174  23.221  1.00 21.15 ? 162 ALA   D C   1 
ATOM   6604 O O   . ALA   D 1 183 ? -13.584 -7.952  22.919  1.00 22.98 ? 162 ALA   D O   1 
ATOM   6605 C CB  . ALA   D 1 183 ? -14.740 -8.157  25.750  1.00 24.42 ? 162 ALA   D CB  1 
ATOM   6606 N N   . MET   D 1 184 ? -15.554 -9.050  22.575  1.00 22.42 ? 163 MET   D N   1 
ATOM   6607 C CA  . MET   D 1 184 ? -15.045 -9.876  21.496  1.00 26.11 ? 163 MET   D CA  1 
ATOM   6608 C C   . MET   D 1 184 ? -15.383 -9.307  20.111  1.00 24.93 ? 163 MET   D C   1 
ATOM   6609 O O   . MET   D 1 184 ? -15.175 -9.971  19.106  1.00 28.27 ? 163 MET   D O   1 
ATOM   6610 C CB  . MET   D 1 184 ? -15.491 -11.340 21.654  1.00 26.73 ? 163 MET   D CB  1 
ATOM   6611 C CG  . MET   D 1 184 ? -15.001 -11.978 22.951  1.00 26.09 ? 163 MET   D CG  1 
ATOM   6612 S SD  . MET   D 1 184 ? -13.207 -12.065 23.019  1.00 31.17 ? 163 MET   D SD  1 
ATOM   6613 C CE  . MET   D 1 184 ? -12.991 -13.489 21.935  1.00 33.66 ? 163 MET   D CE  1 
ATOM   6614 N N   . VAL   D 1 185 ? -15.693 -8.027  20.021  1.00 23.70 ? 164 VAL   D N   1 
ATOM   6615 C CA  . VAL   D 1 185 ? -16.236 -7.529  18.760  1.00 28.24 ? 164 VAL   D CA  1 
ATOM   6616 C C   . VAL   D 1 185 ? -15.172 -7.478  17.663  1.00 28.88 ? 164 VAL   D C   1 
ATOM   6617 O O   . VAL   D 1 185 ? -15.531 -7.393  16.494  1.00 27.81 ? 164 VAL   D O   1 
ATOM   6618 C CB  . VAL   D 1 185 ? -16.970 -6.176  18.835  1.00 29.18 ? 164 VAL   D CB  1 
ATOM   6619 C CG1 . VAL   D 1 185 ? -18.344 -6.315  19.472  1.00 36.05 ? 164 VAL   D CG1 1 
ATOM   6620 C CG2 . VAL   D 1 185 ? -16.134 -5.099  19.484  1.00 26.90 ? 164 VAL   D CG2 1 
ATOM   6621 N N   . ASP   D 1 186 ? -13.887 -7.500  18.035  1.00 26.66 ? 165 ASP   D N   1 
ATOM   6622 C CA  . ASP   D 1 186 ? -12.856 -7.499  17.018  1.00 25.07 ? 165 ASP   D CA  1 
ATOM   6623 C C   . ASP   D 1 186 ? -12.305 -8.897  16.774  1.00 26.56 ? 165 ASP   D C   1 
ATOM   6624 O O   . ASP   D 1 186 ? -11.401 -9.038  15.948  1.00 27.96 ? 165 ASP   D O   1 
ATOM   6625 C CB  . ASP   D 1 186 ? -11.719 -6.575  17.392  1.00 24.02 ? 165 ASP   D CB  1 
ATOM   6626 C CG  . ASP   D 1 186 ? -12.090 -5.105  17.423  1.00 28.51 ? 165 ASP   D CG  1 
ATOM   6627 O OD1 . ASP   D 1 186 ? -12.863 -4.681  16.575  1.00 28.00 ? 165 ASP   D OD1 1 
ATOM   6628 O OD2 . ASP   D 1 186 ? -11.601 -4.410  18.338  1.00 30.78 ? 165 ASP   D OD2 1 
ATOM   6629 N N   . GLN   D 1 187 ? -12.842 -9.897  17.485  1.00 24.57 ? 166 GLN   D N   1 
ATOM   6630 C CA  . GLN   D 1 187 ? -12.525 -11.300 17.240  1.00 25.32 ? 166 GLN   D CA  1 
ATOM   6631 C C   . GLN   D 1 187 ? -13.844 -12.045 17.218  1.00 26.33 ? 166 GLN   D C   1 
ATOM   6632 O O   . GLN   D 1 187 ? -14.128 -12.887 18.096  1.00 26.83 ? 166 GLN   D O   1 
ATOM   6633 C CB  . GLN   D 1 187 ? -11.574 -11.950 18.257  1.00 28.88 ? 166 GLN   D CB  1 
ATOM   6634 C CG  . GLN   D 1 187 ? -10.187 -11.315 18.308  1.00 31.35 ? 166 GLN   D CG  1 
ATOM   6635 C CD  . GLN   D 1 187 ? -9.878  -10.844 19.711  1.00 35.89 ? 166 GLN   D CD  1 
ATOM   6636 O OE1 . GLN   D 1 187 ? -10.327 -9.778  20.144  1.00 34.33 ? 166 GLN   D OE1 1 
ATOM   6637 N NE2 . GLN   D 1 187 ? -9.127  -11.650 20.443  1.00 33.11 ? 166 GLN   D NE2 1 
ATOM   6638 N N   . PRO   D 1 188 ? -14.715 -11.739 16.229  1.00 26.14 ? 167 PRO   D N   1 
ATOM   6639 C CA  . PRO   D 1 188 ? -16.110 -12.166 16.321  1.00 26.91 ? 167 PRO   D CA  1 
ATOM   6640 C C   . PRO   D 1 188 ? -16.382 -13.652 16.103  1.00 27.36 ? 167 PRO   D C   1 
ATOM   6641 O O   . PRO   D 1 188 ? -15.584 -14.354 15.463  1.00 25.79 ? 167 PRO   D O   1 
ATOM   6642 C CB  . PRO   D 1 188 ? -16.813 -11.299 15.301  1.00 26.45 ? 167 PRO   D CB  1 
ATOM   6643 C CG  . PRO   D 1 188 ? -15.764 -11.143 14.232  1.00 26.67 ? 167 PRO   D CG  1 
ATOM   6644 C CD  . PRO   D 1 188 ? -14.420 -10.961 15.009  1.00 25.25 ? 167 PRO   D CD  1 
ATOM   6645 N N   . CYS   D 1 189 ? -17.532 -14.096 16.632  1.00 26.64 ? 168 CYS   D N   1 
ATOM   6646 C CA  . CYS   D 1 189 ? -18.089 -15.396 16.264  1.00 27.78 ? 168 CYS   D CA  1 
ATOM   6647 C C   . CYS   D 1 189 ? -18.376 -15.437 14.763  1.00 27.70 ? 168 CYS   D C   1 
ATOM   6648 O O   . CYS   D 1 189 ? -18.950 -14.510 14.202  1.00 26.37 ? 168 CYS   D O   1 
ATOM   6649 C CB  . CYS   D 1 189 ? -19.298 -15.727 17.134  1.00 35.47 ? 168 CYS   D CB  1 
ATOM   6650 S SG  . CYS   D 1 189 ? -18.791 -16.340 18.770  1.00 48.39 ? 168 CYS   D SG  1 
ATOM   6651 N N   . MET   D 1 190 ? -18.037 -16.579 14.191  1.00 29.88 ? 169 MET   D N   1 
ATOM   6652 C CA  . MET   D 1 190 ? -18.291 -16.822 12.767  1.00 31.42 ? 169 MET   D CA  1 
ATOM   6653 C C   . MET   D 1 190 ? -19.795 -16.789 12.499  1.00 29.13 ? 169 MET   D C   1 
ATOM   6654 O O   . MET   D 1 190 ? -20.533 -17.354 13.298  1.00 26.65 ? 169 MET   D O   1 
ATOM   6655 C CB  . MET   D 1 190 ? -17.751 -18.216 12.437  1.00 39.07 ? 169 MET   D CB  1 
ATOM   6656 C CG  . MET   D 1 190 ? -18.156 -18.752 11.091  1.00 47.63 ? 169 MET   D CG  1 
ATOM   6657 S SD  . MET   D 1 190 ? -17.077 -17.976 9.881   1.00 52.58 ? 169 MET   D SD  1 
ATOM   6658 C CE  . MET   D 1 190 ? -15.478 -18.635 10.366  1.00 40.40 ? 169 MET   D CE  1 
ATOM   6659 N N   . ALA   D 1 191 ? -20.194 -16.116 11.424  1.00 28.56 ? 170 ALA   D N   1 
ATOM   6660 C CA  . ALA   D 1 191 ? -21.595 -16.075 10.995  1.00 28.53 ? 170 ALA   D CA  1 
ATOM   6661 C C   . ALA   D 1 191 ? -22.477 -15.161 11.861  1.00 27.12 ? 170 ALA   D C   1 
ATOM   6662 O O   . ALA   D 1 191 ? -23.709 -15.226 11.802  1.00 28.32 ? 170 ALA   D O   1 
ATOM   6663 C CB  . ALA   D 1 191 ? -22.189 -17.495 10.805  1.00 27.47 ? 170 ALA   D CB  1 
ATOM   6664 N N   . PHE   D 1 192 ? -21.854 -14.258 12.632  1.00 22.54 ? 171 PHE   D N   1 
ATOM   6665 C CA  . PHE   D 1 192 ? -22.594 -13.328 13.472  1.00 22.42 ? 171 PHE   D CA  1 
ATOM   6666 C C   . PHE   D 1 192 ? -22.416 -11.893 12.963  1.00 21.27 ? 171 PHE   D C   1 
ATOM   6667 O O   . PHE   D 1 192 ? -22.349 -10.980 13.783  1.00 20.54 ? 171 PHE   D O   1 
ATOM   6668 C CB  . PHE   D 1 192 ? -22.203 -13.443 14.956  1.00 20.88 ? 171 PHE   D CB  1 
ATOM   6669 C CG  . PHE   D 1 192 ? -22.902 -14.639 15.615  1.00 27.84 ? 171 PHE   D CG  1 
ATOM   6670 C CD1 . PHE   D 1 192 ? -22.482 -15.942 15.357  1.00 28.84 ? 171 PHE   D CD1 1 
ATOM   6671 C CD2 . PHE   D 1 192 ? -23.983 -14.447 16.483  1.00 29.95 ? 171 PHE   D CD2 1 
ATOM   6672 C CE1 . PHE   D 1 192 ? -23.120 -17.034 15.948  1.00 35.35 ? 171 PHE   D CE1 1 
ATOM   6673 C CE2 . PHE   D 1 192 ? -24.636 -15.543 17.053  1.00 32.75 ? 171 PHE   D CE2 1 
ATOM   6674 C CZ  . PHE   D 1 192 ? -24.199 -16.829 16.799  1.00 32.23 ? 171 PHE   D CZ  1 
ATOM   6675 N N   . SER   D 1 193 ? -22.405 -11.674 11.628  1.00 22.88 ? 172 SER   D N   1 
ATOM   6676 C CA  A SER   D 1 193 ? -22.108 -10.337 11.113  0.50 21.79 ? 172 SER   D CA  1 
ATOM   6677 C CA  B SER   D 1 193 ? -22.147 -10.346 11.063  0.50 21.29 ? 172 SER   D CA  1 
ATOM   6678 C C   . SER   D 1 193 ? -23.089 -9.273  11.608  1.00 23.01 ? 172 SER   D C   1 
ATOM   6679 O O   . SER   D 1 193 ? -22.672 -8.187  12.018  1.00 19.51 ? 172 SER   D O   1 
ATOM   6680 C CB  A SER   D 1 193 ? -21.973 -10.315 9.609   0.50 24.88 ? 172 SER   D CB  1 
ATOM   6681 C CB  B SER   D 1 193 ? -22.190 -10.363 9.547   0.50 23.12 ? 172 SER   D CB  1 
ATOM   6682 O OG  A SER   D 1 193 ? -23.128 -10.879 9.013   0.50 25.83 ? 172 SER   D OG  1 
ATOM   6683 O OG  B SER   D 1 193 ? -21.064 -11.038 9.008   0.50 21.73 ? 172 SER   D OG  1 
ATOM   6684 N N   . LEU   D 1 194 ? -24.400 -9.554  11.595  1.00 22.58 ? 173 LEU   D N   1 
ATOM   6685 C CA  . LEU   D 1 194 ? -25.348 -8.492  11.934  1.00 22.43 ? 173 LEU   D CA  1 
ATOM   6686 C C   . LEU   D 1 194 ? -25.253 -8.149  13.429  1.00 22.24 ? 173 LEU   D C   1 
ATOM   6687 O O   . LEU   D 1 194 ? -25.247 -6.976  13.818  1.00 22.55 ? 173 LEU   D O   1 
ATOM   6688 C CB  . LEU   D 1 194 ? -26.793 -8.817  11.493  1.00 22.21 ? 173 LEU   D CB  1 
ATOM   6689 C CG  . LEU   D 1 194 ? -27.178 -8.466  10.052  1.00 22.64 ? 173 LEU   D CG  1 
ATOM   6690 C CD1 . LEU   D 1 194 ? -28.577 -9.066  9.790   1.00 21.58 ? 173 LEU   D CD1 1 
ATOM   6691 C CD2 . LEU   D 1 194 ? -27.170 -6.987  9.686   1.00 21.21 ? 173 LEU   D CD2 1 
ATOM   6692 N N   . TYR   D 1 195 ? -25.107 -9.153  14.298  1.00 23.02 ? 174 TYR   D N   1 
ATOM   6693 C CA  . TYR   D 1 195 ? -24.902 -8.858  15.718  1.00 21.78 ? 174 TYR   D CA  1 
ATOM   6694 C C   . TYR   D 1 195 ? -23.631 -8.016  15.922  1.00 21.63 ? 174 TYR   D C   1 
ATOM   6695 O O   . TYR   D 1 195 ? -23.654 -7.003  16.631  1.00 23.09 ? 174 TYR   D O   1 
ATOM   6696 C CB  . TYR   D 1 195 ? -24.744 -10.200 16.466  1.00 21.87 ? 174 TYR   D CB  1 
ATOM   6697 C CG  . TYR   D 1 195 ? -24.312 -10.007 17.907  1.00 23.14 ? 174 TYR   D CG  1 
ATOM   6698 C CD1 . TYR   D 1 195 ? -25.241 -9.632  18.894  1.00 23.62 ? 174 TYR   D CD1 1 
ATOM   6699 C CD2 . TYR   D 1 195 ? -22.970 -10.184 18.281  1.00 20.98 ? 174 TYR   D CD2 1 
ATOM   6700 C CE1 . TYR   D 1 195 ? -24.829 -9.428  20.211  1.00 24.36 ? 174 TYR   D CE1 1 
ATOM   6701 C CE2 . TYR   D 1 195 ? -22.549 -9.999  19.588  1.00 22.10 ? 174 TYR   D CE2 1 
ATOM   6702 C CZ  . TYR   D 1 195 ? -23.485 -9.612  20.547  1.00 24.53 ? 174 TYR   D CZ  1 
ATOM   6703 O OH  . TYR   D 1 195 ? -23.009 -9.465  21.808  1.00 28.70 ? 174 TYR   D OH  1 
ATOM   6704 N N   . ASN   D 1 196 ? -22.519 -8.411  15.281  1.00 20.38 ? 175 ASN   D N   1 
ATOM   6705 C CA  A ASN   D 1 196 ? -21.241 -7.707  15.407  0.50 20.68 ? 175 ASN   D CA  1 
ATOM   6706 C CA  B ASN   D 1 196 ? -21.263 -7.688  15.455  0.50 20.40 ? 175 ASN   D CA  1 
ATOM   6707 C C   . ASN   D 1 196 ? -21.364 -6.270  14.896  1.00 19.31 ? 175 ASN   D C   1 
ATOM   6708 O O   . ASN   D 1 196 ? -20.825 -5.334  15.495  1.00 20.20 ? 175 ASN   D O   1 
ATOM   6709 C CB  A ASN   D 1 196 ? -20.144 -8.432  14.636  0.50 20.90 ? 175 ASN   D CB  1 
ATOM   6710 C CB  B ASN   D 1 196 ? -20.082 -8.498  14.946  0.50 20.41 ? 175 ASN   D CB  1 
ATOM   6711 C CG  A ASN   D 1 196 ? -18.749 -8.026  15.060  0.50 22.44 ? 175 ASN   D CG  1 
ATOM   6712 C CG  B ASN   D 1 196 ? -19.751 -9.603  15.914  0.50 20.52 ? 175 ASN   D CG  1 
ATOM   6713 O OD1 A ASN   D 1 196 ? -18.419 -8.123  16.245  0.50 22.62 ? 175 ASN   D OD1 1 
ATOM   6714 O OD1 B ASN   D 1 196 ? -19.240 -9.336  17.014  0.50 27.31 ? 175 ASN   D OD1 1 
ATOM   6715 N ND2 A ASN   D 1 196 ? -17.898 -7.629  14.115  0.50 23.64 ? 175 ASN   D ND2 1 
ATOM   6716 N ND2 B ASN   D 1 196 ? -20.076 -10.841 15.563  0.50 19.77 ? 175 ASN   D ND2 1 
ATOM   6717 N N   . MET   D 1 197 ? -22.074 -6.103  13.781  1.00 22.08 ? 176 MET   D N   1 
ATOM   6718 C CA  . MET   D 1 197 ? -22.280 -4.751  13.256  1.00 18.20 ? 176 MET   D CA  1 
ATOM   6719 C C   . MET   D 1 197 ? -23.039 -3.906  14.285  1.00 21.17 ? 176 MET   D C   1 
ATOM   6720 O O   . MET   D 1 197 ? -22.734 -2.734  14.505  1.00 19.52 ? 176 MET   D O   1 
ATOM   6721 C CB  . MET   D 1 197 ? -23.128 -4.819  11.993  1.00 18.05 ? 176 MET   D CB  1 
ATOM   6722 C CG  . MET   D 1 197 ? -22.293 -5.294  10.779  1.00 22.14 ? 176 MET   D CG  1 
ATOM   6723 S SD  . MET   D 1 197 ? -23.361 -5.725  9.377   1.00 21.66 ? 176 MET   D SD  1 
ATOM   6724 C CE  . MET   D 1 197 ? -23.727 -4.046  8.836   1.00 20.00 ? 176 MET   D CE  1 
ATOM   6725 N N   . GLY   D 1 198 ? -24.067 -4.503  14.869  1.00 19.31 ? 177 GLY   D N   1 
ATOM   6726 C CA  . GLY   D 1 198 ? -24.821 -3.821  15.922  1.00 20.76 ? 177 GLY   D CA  1 
ATOM   6727 C C   . GLY   D 1 198 ? -23.936 -3.385  17.095  1.00 20.10 ? 177 GLY   D C   1 
ATOM   6728 O O   . GLY   D 1 198 ? -24.029 -2.254  17.577  1.00 19.12 ? 177 GLY   D O   1 
ATOM   6729 N N   . LYS   D 1 199 ? -23.115 -4.305  17.612  1.00 17.93 ? 178 LYS   D N   1 
ATOM   6730 C CA  . LYS   D 1 199 ? -22.312 -3.938  18.774  1.00 19.17 ? 178 LYS   D CA  1 
ATOM   6731 C C   . LYS   D 1 199 ? -21.240 -2.926  18.385  1.00 19.23 ? 178 LYS   D C   1 
ATOM   6732 O O   . LYS   D 1 199 ? -20.879 -2.093  19.207  1.00 18.54 ? 178 LYS   D O   1 
ATOM   6733 C CB  . LYS   D 1 199 ? -21.708 -5.195  19.403  1.00 20.93 ? 178 LYS   D CB  1 
ATOM   6734 C CG  . LYS   D 1 199 ? -22.802 -6.095  20.066  1.00 22.06 ? 178 LYS   D CG  1 
ATOM   6735 C CD  . LYS   D 1 199 ? -23.459 -5.392  21.263  1.00 20.89 ? 178 LYS   D CD  1 
ATOM   6736 C CE  . LYS   D 1 199 ? -24.231 -6.361  22.140  1.00 22.91 ? 178 LYS   D CE  1 
ATOM   6737 N NZ  . LYS   D 1 199 ? -24.969 -5.615  23.176  1.00 25.91 ? 178 LYS   D NZ  1 
ATOM   6738 N N   . HIS   D 1 200 ? -20.714 -2.995  17.141  1.00 17.95 ? 179 HIS   D N   1 
ATOM   6739 C CA  . HIS   D 1 200 ? -19.739 -1.975  16.729  1.00 19.72 ? 179 HIS   D CA  1 
ATOM   6740 C C   . HIS   D 1 200 ? -20.451 -0.628  16.713  1.00 17.63 ? 179 HIS   D C   1 
ATOM   6741 O O   . HIS   D 1 200 ? -19.858 0.404   17.100  1.00 19.31 ? 179 HIS   D O   1 
ATOM   6742 C CB  . HIS   D 1 200 ? -19.143 -2.282  15.326  1.00 20.33 ? 179 HIS   D CB  1 
ATOM   6743 C CG  . HIS   D 1 200 ? -17.892 -3.089  15.399  1.00 24.54 ? 179 HIS   D CG  1 
ATOM   6744 N ND1 . HIS   D 1 200 ? -16.671 -2.465  15.522  1.00 27.78 ? 179 HIS   D ND1 1 
ATOM   6745 C CD2 . HIS   D 1 200 ? -17.653 -4.423  15.469  1.00 25.22 ? 179 HIS   D CD2 1 
ATOM   6746 C CE1 . HIS   D 1 200 ? -15.730 -3.384  15.615  1.00 24.56 ? 179 HIS   D CE1 1 
ATOM   6747 N NE2 . HIS   D 1 200 ? -16.311 -4.568  15.592  1.00 25.81 ? 179 HIS   D NE2 1 
ATOM   6748 N N   . ALA   D 1 201 ? -21.687 -0.608  16.197  1.00 18.39 ? 180 ALA   D N   1 
ATOM   6749 C CA  . ALA   D 1 201 ? -22.431 0.658   16.128  1.00 17.46 ? 180 ALA   D CA  1 
ATOM   6750 C C   . ALA   D 1 201 ? -22.611 1.220   17.539  1.00 17.23 ? 180 ALA   D C   1 
ATOM   6751 O O   . ALA   D 1 201 ? -22.545 2.437   17.759  1.00 19.39 ? 180 ALA   D O   1 
ATOM   6752 C CB  . ALA   D 1 201 ? -23.783 0.455   15.414  1.00 20.52 ? 180 ALA   D CB  1 
ATOM   6753 N N   . LEU   D 1 202 ? -22.824 0.322   18.495  1.00 17.83 ? 181 LEU   D N   1 
ATOM   6754 C CA  . LEU   D 1 202 ? -23.024 0.708   19.907  1.00 20.37 ? 181 LEU   D CA  1 
ATOM   6755 C C   . LEU   D 1 202 ? -21.760 1.351   20.488  1.00 20.83 ? 181 LEU   D C   1 
ATOM   6756 O O   . LEU   D 1 202 ? -21.838 2.349   21.230  1.00 20.04 ? 181 LEU   D O   1 
ATOM   6757 C CB  . LEU   D 1 202 ? -23.493 -0.490  20.732  1.00 18.34 ? 181 LEU   D CB  1 
ATOM   6758 C CG  . LEU   D 1 202 ? -23.892 -0.178  22.178  1.00 22.25 ? 181 LEU   D CG  1 
ATOM   6759 C CD1 . LEU   D 1 202 ? -25.098 0.764   22.159  1.00 25.06 ? 181 LEU   D CD1 1 
ATOM   6760 C CD2 . LEU   D 1 202 ? -24.229 -1.509  22.849  1.00 21.98 ? 181 LEU   D CD2 1 
ATOM   6761 N N   . VAL   D 1 203 ? -20.580 0.875   20.044  1.00 19.92 ? 182 VAL   D N   1 
ATOM   6762 C CA  . VAL   D 1 203 ? -19.346 1.572   20.433  1.00 20.27 ? 182 VAL   D CA  1 
ATOM   6763 C C   . VAL   D 1 203 ? -19.369 2.998   19.867  1.00 19.62 ? 182 VAL   D C   1 
ATOM   6764 O O   . VAL   D 1 203 ? -18.967 3.949   20.544  1.00 19.61 ? 182 VAL   D O   1 
ATOM   6765 C CB  . VAL   D 1 203 ? -18.100 0.782   19.957  1.00 22.12 ? 182 VAL   D CB  1 
ATOM   6766 C CG1 . VAL   D 1 203 ? -16.770 1.560   20.159  1.00 19.31 ? 182 VAL   D CG1 1 
ATOM   6767 C CG2 . VAL   D 1 203 ? -18.056 -0.588  20.631  1.00 23.45 ? 182 VAL   D CG2 1 
ATOM   6768 N N   . GLY   D 1 204 ? -19.670 3.117   18.565  1.00 21.18 ? 183 GLY   D N   1 
ATOM   6769 C CA  . GLY   D 1 204 ? -19.800 4.424   17.923  1.00 19.55 ? 183 GLY   D CA  1 
ATOM   6770 C C   . GLY   D 1 204 ? -20.740 5.349   18.688  1.00 19.15 ? 183 GLY   D C   1 
ATOM   6771 O O   . GLY   D 1 204 ? -20.423 6.519   18.870  1.00 19.72 ? 183 GLY   D O   1 
ATOM   6772 N N   . LEU   D 1 205 ? -21.939 4.847   19.034  1.00 20.01 ? 184 LEU   D N   1 
ATOM   6773 C CA  . LEU   D 1 205 ? -22.895 5.617   19.826  1.00 20.92 ? 184 LEU   D CA  1 
ATOM   6774 C C   . LEU   D 1 205 ? -22.273 6.056   21.154  1.00 19.56 ? 184 LEU   D C   1 
ATOM   6775 O O   . LEU   D 1 205 ? -22.403 7.228   21.547  1.00 20.67 ? 184 LEU   D O   1 
ATOM   6776 C CB  . LEU   D 1 205 ? -24.182 4.812   20.057  1.00 19.83 ? 184 LEU   D CB  1 
ATOM   6777 C CG  . LEU   D 1 205 ? -25.152 5.466   21.063  1.00 22.12 ? 184 LEU   D CG  1 
ATOM   6778 C CD1 . LEU   D 1 205 ? -25.552 6.795   20.435  1.00 21.50 ? 184 LEU   D CD1 1 
ATOM   6779 C CD2 . LEU   D 1 205 ? -26.371 4.517   21.215  1.00 21.20 ? 184 LEU   D CD2 1 
ATOM   6780 N N   . THR   D 1 206 ? -21.628 5.111   21.854  1.00 18.75 ? 185 THR   D N   1 
ATOM   6781 C CA  . THR   D 1 206 ? -21.001 5.409   23.147  1.00 19.41 ? 185 THR   D CA  1 
ATOM   6782 C C   . THR   D 1 206 ? -20.063 6.617   23.009  1.00 20.16 ? 185 THR   D C   1 
ATOM   6783 O O   . THR   D 1 206 ? -20.181 7.590   23.757  1.00 21.89 ? 185 THR   D O   1 
ATOM   6784 C CB  . THR   D 1 206 ? -20.276 4.201   23.759  1.00 20.18 ? 185 THR   D CB  1 
ATOM   6785 O OG1 . THR   D 1 206 ? -21.221 3.142   23.844  1.00 20.04 ? 185 THR   D OG1 1 
ATOM   6786 C CG2 . THR   D 1 206 ? -19.766 4.539   25.150  1.00 20.61 ? 185 THR   D CG2 1 
ATOM   6787 N N   . GLN   D 1 207 ? -19.184 6.617   21.992  1.00 20.32 ? 186 GLN   D N   1 
ATOM   6788 C CA  . GLN   D 1 207 ? -18.254 7.743   21.802  1.00 18.87 ? 186 GLN   D CA  1 
ATOM   6789 C C   . GLN   D 1 207 ? -18.973 9.021   21.389  1.00 20.80 ? 186 GLN   D C   1 
ATOM   6790 O O   . GLN   D 1 207 ? -18.658 10.107  21.923  1.00 20.40 ? 186 GLN   D O   1 
ATOM   6791 C CB  . GLN   D 1 207 ? -17.167 7.395   20.765  1.00 21.34 ? 186 GLN   D CB  1 
ATOM   6792 C CG  . GLN   D 1 207 ? -16.428 6.169   21.314  1.00 25.39 ? 186 GLN   D CG  1 
ATOM   6793 C CD  . GLN   D 1 207 ? -15.380 5.586   20.407  1.00 29.44 ? 186 GLN   D CD  1 
ATOM   6794 O OE1 . GLN   D 1 207 ? -14.449 4.949   20.899  1.00 34.51 ? 186 GLN   D OE1 1 
ATOM   6795 N NE2 . GLN   D 1 207 ? -15.541 5.779   19.108  1.00 26.02 ? 186 GLN   D NE2 1 
ATOM   6796 N N   . SER   D 1 208 ? -19.856 8.918   20.382  1.00 20.19 ? 187 SER   D N   1 
ATOM   6797 C CA  . SER   D 1 208 ? -20.504 10.100  19.813  1.00 19.47 ? 187 SER   D CA  1 
ATOM   6798 C C   . SER   D 1 208 ? -21.392 10.783  20.859  1.00 20.40 ? 187 SER   D C   1 
ATOM   6799 O O   . SER   D 1 208 ? -21.383 12.030  21.012  1.00 21.87 ? 187 SER   D O   1 
ATOM   6800 C CB  . SER   D 1 208 ? -21.310 9.720   18.556  1.00 20.87 ? 187 SER   D CB  1 
ATOM   6801 O OG  . SER   D 1 208 ? -20.478 9.581   17.396  1.00 21.85 ? 187 SER   D OG  1 
ATOM   6802 N N   . ALA   D 1 209 ? -22.181 9.976   21.570  1.00 19.97 ? 188 ALA   D N   1 
ATOM   6803 C CA  . ALA   D 1 209 ? -23.015 10.553  22.626  1.00 22.95 ? 188 ALA   D CA  1 
ATOM   6804 C C   . ALA   D 1 209 ? -22.195 11.096  23.802  1.00 24.65 ? 188 ALA   D C   1 
ATOM   6805 O O   . ALA   D 1 209 ? -22.541 12.119  24.415  1.00 22.57 ? 188 ALA   D O   1 
ATOM   6806 C CB  . ALA   D 1 209 ? -24.061 9.563   23.073  1.00 21.55 ? 188 ALA   D CB  1 
ATOM   6807 N N   . ALA   D 1 210 ? -21.101 10.416  24.156  1.00 22.02 ? 189 ALA   D N   1 
ATOM   6808 C CA  . ALA   D 1 210 ? -20.235 10.998  25.190  1.00 22.48 ? 189 ALA   D CA  1 
ATOM   6809 C C   . ALA   D 1 210 ? -19.771 12.404  24.782  1.00 21.47 ? 189 ALA   D C   1 
ATOM   6810 O O   . ALA   D 1 210 ? -19.821 13.340  25.598  1.00 23.93 ? 189 ALA   D O   1 
ATOM   6811 C CB  . ALA   D 1 210 ? -19.077 10.063  25.466  1.00 20.88 ? 189 ALA   D CB  1 
ATOM   6812 N N   . LEU   D 1 211 ? -19.321 12.592  23.532  1.00 22.75 ? 190 LEU   D N   1 
ATOM   6813 C CA  . LEU   D 1 211 ? -18.852 13.912  23.095  1.00 21.94 ? 190 LEU   D CA  1 
ATOM   6814 C C   . LEU   D 1 211 ? -19.986 14.930  23.150  1.00 25.17 ? 190 LEU   D C   1 
ATOM   6815 O O   . LEU   D 1 211 ? -19.830 16.058  23.636  1.00 24.62 ? 190 LEU   D O   1 
ATOM   6816 C CB  . LEU   D 1 211 ? -18.334 13.750  21.654  1.00 22.40 ? 190 LEU   D CB  1 
ATOM   6817 C CG  . LEU   D 1 211 ? -17.802 15.020  20.985  1.00 27.35 ? 190 LEU   D CG  1 
ATOM   6818 C CD1 . LEU   D 1 211 ? -16.387 15.349  21.579  1.00 27.49 ? 190 LEU   D CD1 1 
ATOM   6819 C CD2 . LEU   D 1 211 ? -17.722 14.819  19.478  1.00 27.80 ? 190 LEU   D CD2 1 
ATOM   6820 N N   . GLU   D 1 212 ? -21.152 14.536  22.635  1.00 25.10 ? 191 GLU   D N   1 
ATOM   6821 C CA  . GLU   D 1 212 ? -22.216 15.501  22.383  1.00 25.14 ? 191 GLU   D CA  1 
ATOM   6822 C C   . GLU   D 1 212 ? -22.969 15.851  23.671  1.00 27.14 ? 191 GLU   D C   1 
ATOM   6823 O O   . GLU   D 1 212 ? -23.472 16.977  23.809  1.00 27.86 ? 191 GLU   D O   1 
ATOM   6824 C CB  . GLU   D 1 212 ? -23.197 14.870  21.380  1.00 23.26 ? 191 GLU   D CB  1 
ATOM   6825 C CG  . GLU   D 1 212 ? -24.263 15.863  20.890  1.00 26.13 ? 191 GLU   D CG  1 
ATOM   6826 C CD  . GLU   D 1 212 ? -25.122 15.307  19.757  1.00 32.13 ? 191 GLU   D CD  1 
ATOM   6827 O OE1 . GLU   D 1 212 ? -26.113 15.981  19.368  1.00 29.00 ? 191 GLU   D OE1 1 
ATOM   6828 O OE2 . GLU   D 1 212 ? -24.797 14.213  19.226  1.00 29.60 ? 191 GLU   D OE2 1 
ATOM   6829 N N   . LEU   D 1 213 ? -23.059 14.893  24.604  1.00 22.17 ? 192 LEU   D N   1 
ATOM   6830 C CA  . LEU   D 1 213 ? -23.832 15.116  25.821  1.00 22.76 ? 192 LEU   D CA  1 
ATOM   6831 C C   . LEU   D 1 213 ? -22.974 15.633  26.978  1.00 26.84 ? 192 LEU   D C   1 
ATOM   6832 O O   . LEU   D 1 213 ? -23.530 16.016  28.018  1.00 27.56 ? 192 LEU   D O   1 
ATOM   6833 C CB  . LEU   D 1 213 ? -24.622 13.872  26.225  1.00 21.81 ? 192 LEU   D CB  1 
ATOM   6834 C CG  . LEU   D 1 213 ? -25.556 13.335  25.130  1.00 22.88 ? 192 LEU   D CG  1 
ATOM   6835 C CD1 . LEU   D 1 213 ? -26.271 12.097  25.666  1.00 24.15 ? 192 LEU   D CD1 1 
ATOM   6836 C CD2 . LEU   D 1 213 ? -26.550 14.455  24.723  1.00 25.56 ? 192 LEU   D CD2 1 
ATOM   6837 N N   . ALA   D 1 214 ? -21.648 15.641  26.815  1.00 22.32 ? 193 ALA   D N   1 
ATOM   6838 C CA  . ALA   D 1 214 ? -20.793 16.078  27.917  1.00 28.92 ? 193 ALA   D CA  1 
ATOM   6839 C C   . ALA   D 1 214 ? -21.134 17.511  28.342  1.00 34.88 ? 193 ALA   D C   1 
ATOM   6840 O O   . ALA   D 1 214 ? -21.088 17.821  29.532  1.00 31.78 ? 193 ALA   D O   1 
ATOM   6841 C CB  . ALA   D 1 214 ? -19.342 15.989  27.520  1.00 27.76 ? 193 ALA   D CB  1 
ATOM   6842 N N   . PRO   D 1 215 ? -21.486 18.439  27.423  1.00 34.25 ? 194 PRO   D N   1 
ATOM   6843 C CA  . PRO   D 1 215 ? -21.935 19.774  27.845  1.00 36.52 ? 194 PRO   D CA  1 
ATOM   6844 C C   . PRO   D 1 215 ? -23.168 19.823  28.751  1.00 43.47 ? 194 PRO   D C   1 
ATOM   6845 O O   . PRO   D 1 215 ? -23.327 20.788  29.495  1.00 44.43 ? 194 PRO   D O   1 
ATOM   6846 C CB  . PRO   D 1 215 ? -22.130 20.517  26.524  1.00 37.87 ? 194 PRO   D CB  1 
ATOM   6847 C CG  . PRO   D 1 215 ? -21.208 19.796  25.556  1.00 40.05 ? 194 PRO   D CG  1 
ATOM   6848 C CD  . PRO   D 1 215 ? -21.352 18.331  25.958  1.00 35.37 ? 194 PRO   D CD  1 
ATOM   6849 N N   . TYR   D 1 216 ? -24.000 18.766  28.726  1.00 35.68 ? 195 TYR   D N   1 
ATOM   6850 C CA  . TYR   D 1 216 ? -25.204 18.671  29.539  1.00 37.01 ? 195 TYR   D CA  1 
ATOM   6851 C C   . TYR   D 1 216 ? -24.951 17.917  30.850  1.00 37.88 ? 195 TYR   D C   1 
ATOM   6852 O O   . TYR   D 1 216 ? -25.893 17.632  31.590  1.00 40.94 ? 195 TYR   D O   1 
ATOM   6853 C CB  . TYR   D 1 216 ? -26.343 18.038  28.724  1.00 39.98 ? 195 TYR   D CB  1 
ATOM   6854 C CG  . TYR   D 1 216 ? -26.649 18.729  27.403  0.70 36.42 ? 195 TYR   D CG  1 
ATOM   6855 C CD1 . TYR   D 1 216 ? -25.961 18.404  26.244  0.70 39.93 ? 195 TYR   D CD1 1 
ATOM   6856 C CD2 . TYR   D 1 216 ? -27.609 19.727  27.327  0.70 44.32 ? 195 TYR   D CD2 1 
ATOM   6857 C CE1 . TYR   D 1 216 ? -26.230 19.033  25.040  0.70 45.47 ? 195 TYR   D CE1 1 
ATOM   6858 C CE2 . TYR   D 1 216 ? -27.899 20.358  26.133  0.70 45.53 ? 195 TYR   D CE2 1 
ATOM   6859 C CZ  . TYR   D 1 216 ? -27.208 20.010  24.987  0.70 50.88 ? 195 TYR   D CZ  1 
ATOM   6860 O OH  . TYR   D 1 216 ? -27.510 20.636  23.815  0.70 54.56 ? 195 TYR   D OH  1 
ATOM   6861 N N   . GLY   D 1 217 ? -23.695 17.536  31.106  1.00 37.72 ? 196 GLY   D N   1 
ATOM   6862 C CA  . GLY   D 1 217 ? -23.316 16.806  32.310  1.00 34.47 ? 196 GLY   D CA  1 
ATOM   6863 C C   . GLY   D 1 217 ? -23.760 15.347  32.261  1.00 36.16 ? 196 GLY   D C   1 
ATOM   6864 O O   . GLY   D 1 217 ? -23.790 14.670  33.288  1.00 38.97 ? 196 GLY   D O   1 
ATOM   6865 N N   . ILE   D 1 218 ? -24.032 14.838  31.050  1.00 27.50 ? 197 ILE   D N   1 
ATOM   6866 C CA  . ILE   D 1 218 ? -24.447 13.440  30.927  1.00 24.28 ? 197 ILE   D CA  1 
ATOM   6867 C C   . ILE   D 1 218 ? -23.213 12.649  30.481  1.00 22.98 ? 197 ILE   D C   1 
ATOM   6868 O O   . ILE   D 1 218 ? -22.665 12.961  29.440  1.00 28.11 ? 197 ILE   D O   1 
ATOM   6869 C CB  . ILE   D 1 218 ? -25.619 13.285  29.942  1.00 23.90 ? 197 ILE   D CB  1 
ATOM   6870 C CG1 . ILE   D 1 218 ? -26.878 14.072  30.391  1.00 28.63 ? 197 ILE   D CG1 1 
ATOM   6871 C CG2 . ILE   D 1 218 ? -26.003 11.802  29.747  1.00 25.43 ? 197 ILE   D CG2 1 
ATOM   6872 C CD1 . ILE   D 1 218 ? -27.985 14.009  29.342  1.00 33.17 ? 197 ILE   D CD1 1 
ATOM   6873 N N   . ARG   D 1 219 ? -22.798 11.648  31.263  1.00 23.98 ? 198 ARG   D N   1 
ATOM   6874 C CA  . ARG   D 1 219 ? -21.645 10.831  30.893  1.00 23.26 ? 198 ARG   D CA  1 
ATOM   6875 C C   . ARG   D 1 219 ? -22.177 9.603   30.165  1.00 24.19 ? 198 ARG   D C   1 
ATOM   6876 O O   . ARG   D 1 219 ? -23.262 9.157   30.477  1.00 24.48 ? 198 ARG   D O   1 
ATOM   6877 C CB  . ARG   D 1 219 ? -20.812 10.373  32.108  1.00 23.88 ? 198 ARG   D CB  1 
ATOM   6878 C CG  . ARG   D 1 219 ? -20.223 11.562  32.862  1.00 24.54 ? 198 ARG   D CG  1 
ATOM   6879 C CD  . ARG   D 1 219 ? -19.422 11.252  34.126  1.00 27.24 ? 198 ARG   D CD  1 
ATOM   6880 N NE  . ARG   D 1 219 ? -20.281 10.563  35.103  1.00 26.76 ? 198 ARG   D NE  1 
ATOM   6881 C CZ  . ARG   D 1 219 ? -20.391 9.231   35.260  1.00 30.57 ? 198 ARG   D CZ  1 
ATOM   6882 N NH1 . ARG   D 1 219 ? -19.579 8.387   34.645  1.00 28.44 ? 198 ARG   D NH1 1 
ATOM   6883 N NH2 . ARG   D 1 219 ? -21.327 8.731   36.042  1.00 29.24 ? 198 ARG   D NH2 1 
ATOM   6884 N N   . VAL   D 1 220 ? -21.413 9.090   29.182  1.00 22.88 ? 199 VAL   D N   1 
ATOM   6885 C CA  . VAL   D 1 220 ? -21.862 7.900   28.459  1.00 22.32 ? 199 VAL   D CA  1 
ATOM   6886 C C   . VAL   D 1 220 ? -20.684 6.939   28.378  1.00 19.37 ? 199 VAL   D C   1 
ATOM   6887 O O   . VAL   D 1 220 ? -19.663 7.328   27.801  1.00 21.17 ? 199 VAL   D O   1 
ATOM   6888 C CB  . VAL   D 1 220 ? -22.315 8.330   27.045  1.00 24.70 ? 199 VAL   D CB  1 
ATOM   6889 C CG1 . VAL   D 1 220 ? -22.855 7.135   26.238  1.00 20.92 ? 199 VAL   D CG1 1 
ATOM   6890 C CG2 . VAL   D 1 220 ? -23.352 9.471   27.086  1.00 23.60 ? 199 VAL   D CG2 1 
ATOM   6891 N N   . ASN   D 1 221 ? -20.863 5.679   28.836  1.00 19.97 ? 200 ASN   D N   1 
ATOM   6892 C CA  . ASN   D 1 221 ? -19.752 4.741   28.989  1.00 21.19 ? 200 ASN   D CA  1 
ATOM   6893 C C   . ASN   D 1 221 ? -20.261 3.374   28.583  1.00 18.36 ? 200 ASN   D C   1 
ATOM   6894 O O   . ASN   D 1 221 ? -21.454 3.233   28.366  1.00 20.85 ? 200 ASN   D O   1 
ATOM   6895 C CB  . ASN   D 1 221 ? -19.201 4.729   30.417  1.00 20.06 ? 200 ASN   D CB  1 
ATOM   6896 C CG  . ASN   D 1 221 ? -18.502 6.036   30.729  1.00 21.47 ? 200 ASN   D CG  1 
ATOM   6897 O OD1 . ASN   D 1 221 ? -17.508 6.345   30.074  1.00 23.20 ? 200 ASN   D OD1 1 
ATOM   6898 N ND2 . ASN   D 1 221 ? -19.007 6.845   31.672  1.00 23.76 ? 200 ASN   D ND2 1 
ATOM   6899 N N   . GLY   D 1 222 ? -19.348 2.392   28.448  1.00 20.73 ? 201 GLY   D N   1 
ATOM   6900 C CA  . GLY   D 1 222 ? -19.784 1.039   28.143  1.00 22.58 ? 201 GLY   D CA  1 
ATOM   6901 C C   . GLY   D 1 222 ? -19.167 0.021   29.096  1.00 20.84 ? 201 GLY   D C   1 
ATOM   6902 O O   . GLY   D 1 222 ? -18.120 0.271   29.670  1.00 22.78 ? 201 GLY   D O   1 
ATOM   6903 N N   . VAL   D 1 223 ? -19.823 -1.139  29.213  1.00 21.76 ? 202 VAL   D N   1 
ATOM   6904 C CA  . VAL   D 1 223 ? -19.267 -2.305  29.858  1.00 21.14 ? 202 VAL   D CA  1 
ATOM   6905 C C   . VAL   D 1 223 ? -19.342 -3.423  28.823  1.00 20.18 ? 202 VAL   D C   1 
ATOM   6906 O O   . VAL   D 1 223 ? -20.394 -3.608  28.203  1.00 21.92 ? 202 VAL   D O   1 
ATOM   6907 C CB  . VAL   D 1 223 ? -20.122 -2.705  31.079  1.00 21.72 ? 202 VAL   D CB  1 
ATOM   6908 C CG1 . VAL   D 1 223 ? -19.631 -4.045  31.676  1.00 24.37 ? 202 VAL   D CG1 1 
ATOM   6909 C CG2 . VAL   D 1 223 ? -20.010 -1.622  32.152  1.00 24.35 ? 202 VAL   D CG2 1 
ATOM   6910 N N   . ALA   D 1 224 ? -18.200 -4.076  28.611  1.00 22.75 ? 203 ALA   D N   1 
ATOM   6911 C CA  . ALA   D 1 224 ? -18.043 -5.048  27.539  1.00 23.05 ? 203 ALA   D CA  1 
ATOM   6912 C C   . ALA   D 1 224 ? -17.749 -6.423  28.144  1.00 21.46 ? 203 ALA   D C   1 
ATOM   6913 O O   . ALA   D 1 224 ? -16.590 -6.729  28.392  1.00 21.44 ? 203 ALA   D O   1 
ATOM   6914 C CB  . ALA   D 1 224 ? -16.889 -4.638  26.642  1.00 20.29 ? 203 ALA   D CB  1 
ATOM   6915 N N   . PRO   D 1 225 ? -18.774 -7.295  28.343  1.00 24.79 ? 204 PRO   D N   1 
ATOM   6916 C CA  . PRO   D 1 225 ? -18.525 -8.661  28.822  1.00 24.27 ? 204 PRO   D CA  1 
ATOM   6917 C C   . PRO   D 1 225 ? -17.765 -9.479  27.778  1.00 29.77 ? 204 PRO   D C   1 
ATOM   6918 O O   . PRO   D 1 225 ? -17.896 -9.225  26.579  1.00 25.68 ? 204 PRO   D O   1 
ATOM   6919 C CB  . PRO   D 1 225 ? -19.945 -9.219  29.003  1.00 26.56 ? 204 PRO   D CB  1 
ATOM   6920 C CG  . PRO   D 1 225 ? -20.816 -8.010  29.083  1.00 27.50 ? 204 PRO   D CG  1 
ATOM   6921 C CD  . PRO   D 1 225 ? -20.187 -7.003  28.112  1.00 24.01 ? 204 PRO   D CD  1 
ATOM   6922 N N   . GLY   D 1 226 ? -17.036 -10.500 28.246  1.00 25.18 ? 205 GLY   D N   1 
ATOM   6923 C CA  . GLY   D 1 226 ? -16.556 -11.522 27.333  1.00 26.34 ? 205 GLY   D CA  1 
ATOM   6924 C C   . GLY   D 1 226 ? -17.547 -12.676 27.245  1.00 29.00 ? 205 GLY   D C   1 
ATOM   6925 O O   . GLY   D 1 226 ? -18.484 -12.655 26.432  1.00 33.95 ? 205 GLY   D O   1 
ATOM   6926 N N   . VAL   D 1 227 ? -17.296 -13.722 28.036  1.00 28.64 ? 206 VAL   D N   1 
ATOM   6927 C CA  . VAL   D 1 227 ? -18.345 -14.688 28.299  1.00 29.11 ? 206 VAL   D CA  1 
ATOM   6928 C C   . VAL   D 1 227 ? -18.796 -14.501 29.751  1.00 27.34 ? 206 VAL   D C   1 
ATOM   6929 O O   . VAL   D 1 227 ? -17.982 -14.508 30.673  1.00 31.57 ? 206 VAL   D O   1 
ATOM   6930 C CB  . VAL   D 1 227 ? -17.959 -16.148 28.010  1.00 35.12 ? 206 VAL   D CB  1 
ATOM   6931 C CG1 . VAL   D 1 227 ? -17.853 -16.401 26.512  1.00 38.77 ? 206 VAL   D CG1 1 
ATOM   6932 C CG2 . VAL   D 1 227 ? -16.673 -16.515 28.720  1.00 33.23 ? 206 VAL   D CG2 1 
ATOM   6933 N N   . SER   D 1 228 ? -20.092 -14.273 29.873  1.00 32.45 ? 207 SER   D N   1 
ATOM   6934 C CA  . SER   D 1 228 ? -20.828 -14.200 31.119  1.00 38.33 ? 207 SER   D CA  1 
ATOM   6935 C C   . SER   D 1 228 ? -21.888 -15.288 30.982  1.00 40.22 ? 207 SER   D C   1 
ATOM   6936 O O   . SER   D 1 228 ? -21.601 -16.314 30.354  1.00 44.61 ? 207 SER   D O   1 
ATOM   6937 C CB  . SER   D 1 228 ? -21.403 -12.809 31.321  1.00 35.28 ? 207 SER   D CB  1 
ATOM   6938 O OG  . SER   D 1 228 ? -21.974 -12.625 32.614  1.00 36.24 ? 207 SER   D OG  1 
ATOM   6939 N N   . LEU   D 1 229 ? -23.071 -15.086 31.564  1.00 43.72 ? 208 LEU   D N   1 
ATOM   6940 C CA  . LEU   D 1 229 ? -24.085 -16.138 31.603  1.00 46.42 ? 208 LEU   D CA  1 
ATOM   6941 C C   . LEU   D 1 229 ? -24.319 -16.648 30.188  1.00 51.92 ? 208 LEU   D C   1 
ATOM   6942 O O   . LEU   D 1 229 ? -24.722 -15.885 29.307  1.00 52.30 ? 208 LEU   D O   1 
ATOM   6943 C CB  . LEU   D 1 229 ? -25.393 -15.641 32.206  1.00 46.64 ? 208 LEU   D CB  1 
ATOM   6944 C CG  . LEU   D 1 229 ? -25.338 -15.203 33.673  1.00 47.79 ? 208 LEU   D CG  1 
ATOM   6945 C CD1 . LEU   D 1 229 ? -26.756 -14.801 34.051  1.00 50.31 ? 208 LEU   D CD1 1 
ATOM   6946 C CD2 . LEU   D 1 229 ? -24.822 -16.298 34.599  1.00 53.70 ? 208 LEU   D CD2 1 
ATOM   6947 N N   . LEU   D 1 230 ? -24.047 -17.939 29.995  1.00 48.79 ? 209 LEU   D N   1 
ATOM   6948 C CA  . LEU   D 1 230 ? -24.039 -18.546 28.675  1.00 54.91 ? 209 LEU   D CA  1 
ATOM   6949 C C   . LEU   D 1 230 ? -25.476 -18.815 28.230  1.00 61.28 ? 209 LEU   D C   1 
ATOM   6950 O O   . LEU   D 1 230 ? -26.359 -18.943 29.071  1.00 56.15 ? 209 LEU   D O   1 
ATOM   6951 C CB  . LEU   D 1 230 ? -23.158 -19.791 28.764  1.00 51.94 ? 209 LEU   D CB  1 
ATOM   6952 C CG  . LEU   D 1 230 ? -21.657 -19.481 28.816  1.00 51.67 ? 209 LEU   D CG  1 
ATOM   6953 C CD1 . LEU   D 1 230 ? -20.778 -20.513 29.508  1.00 54.45 ? 209 LEU   D CD1 1 
ATOM   6954 C CD2 . LEU   D 1 230 ? -21.186 -19.255 27.386  1.00 48.36 ? 209 LEU   D CD2 1 
ATOM   6955 N N   . PRO   D 1 231 ? -25.770 -18.831 26.906  1.00 73.31 ? 210 PRO   D N   1 
ATOM   6956 C CA  . PRO   D 1 231 ? -27.146 -18.992 26.420  1.00 76.67 ? 210 PRO   D CA  1 
ATOM   6957 C C   . PRO   D 1 231 ? -27.869 -20.189 27.041  1.00 81.16 ? 210 PRO   D C   1 
ATOM   6958 O O   . PRO   D 1 231 ? -27.221 -21.134 27.498  1.00 77.25 ? 210 PRO   D O   1 
ATOM   6959 C CB  . PRO   D 1 231 ? -26.975 -19.134 24.893  1.00 80.08 ? 210 PRO   D CB  1 
ATOM   6960 C CG  . PRO   D 1 231 ? -25.675 -18.418 24.597  1.00 81.80 ? 210 PRO   D CG  1 
ATOM   6961 C CD  . PRO   D 1 231 ? -24.794 -18.664 25.813  1.00 74.59 ? 210 PRO   D CD  1 
ATOM   6962 N N   . VAL   D 1 232 ? -29.212 -20.125 27.066  1.00 72.88 ? 211 VAL   D N   1 
ATOM   6963 C CA  . VAL   D 1 232 ? -30.038 -21.207 27.589  1.00 74.77 ? 211 VAL   D CA  1 
ATOM   6964 C C   . VAL   D 1 232 ? -29.947 -22.404 26.637  1.00 73.19 ? 211 VAL   D C   1 
ATOM   6965 O O   . VAL   D 1 232 ? -29.828 -23.543 27.084  1.00 67.91 ? 211 VAL   D O   1 
ATOM   6966 C CB  . VAL   D 1 232 ? -31.501 -20.800 27.869  1.00 65.65 ? 211 VAL   D CB  1 
ATOM   6967 N N   . ALA   D 1 233 ? -29.924 -22.110 25.329  1.00 79.77 ? 212 ALA   D N   1 
ATOM   6968 C CA  . ALA   D 1 233 ? -30.029 -23.099 24.266  1.00 81.90 ? 212 ALA   D CA  1 
ATOM   6969 C C   . ALA   D 1 233 ? -28.662 -23.659 23.872  1.00 83.62 ? 212 ALA   D C   1 
ATOM   6970 O O   . ALA   D 1 233 ? -28.519 -24.244 22.801  1.00 79.74 ? 212 ALA   D O   1 
ATOM   6971 C CB  . ALA   D 1 233 ? -30.737 -22.486 23.073  1.00 74.92 ? 212 ALA   D CB  1 
ATOM   6972 N N   . MET   D 1 234 ? -27.657 -23.494 24.737  1.00 81.54 ? 213 MET   D N   1 
ATOM   6973 C CA  . MET   D 1 234 ? -26.329 -24.003 24.433  1.00 77.20 ? 213 MET   D CA  1 
ATOM   6974 C C   . MET   D 1 234 ? -26.056 -25.250 25.277  1.00 72.12 ? 213 MET   D C   1 
ATOM   6975 O O   . MET   D 1 234 ? -26.434 -25.310 26.448  1.00 77.42 ? 213 MET   D O   1 
ATOM   6976 C CB  . MET   D 1 234 ? -25.265 -22.906 24.609  1.00 73.04 ? 213 MET   D CB  1 
ATOM   6977 C CG  . MET   D 1 234 ? -23.855 -23.300 24.172  0.70 64.73 ? 213 MET   D CG  1 
ATOM   6978 S SD  . MET   D 1 234 ? -22.560 -22.101 24.554  0.70 55.94 ? 213 MET   D SD  1 
ATOM   6979 C CE  . MET   D 1 234 ? -22.914 -20.811 23.352  0.70 54.31 ? 213 MET   D CE  1 
ATOM   6980 N N   . GLY   D 1 235 ? -25.402 -26.245 24.656  1.00 72.01 ? 214 GLY   D N   1 
ATOM   6981 C CA  . GLY   D 1 235 ? -25.022 -27.493 25.305  1.00 66.70 ? 214 GLY   D CA  1 
ATOM   6982 C C   . GLY   D 1 235 ? -23.874 -27.309 26.294  1.00 70.05 ? 214 GLY   D C   1 
ATOM   6983 O O   . GLY   D 1 235 ? -23.222 -26.270 26.305  1.00 76.22 ? 214 GLY   D O   1 
ATOM   6984 N N   . GLU   D 1 236 ? -23.625 -28.349 27.096  1.00 68.06 ? 215 GLU   D N   1 
ATOM   6985 C CA  . GLU   D 1 236 ? -22.683 -28.332 28.207  1.00 70.87 ? 215 GLU   D CA  1 
ATOM   6986 C C   . GLU   D 1 236 ? -21.245 -28.373 27.692  1.00 70.40 ? 215 GLU   D C   1 
ATOM   6987 O O   . GLU   D 1 236 ? -20.357 -27.754 28.285  1.00 61.40 ? 215 GLU   D O   1 
ATOM   6988 C CB  . GLU   D 1 236 ? -22.976 -29.543 29.098  1.00 72.25 ? 215 GLU   D CB  1 
ATOM   6989 C CG  . GLU   D 1 236 ? -22.006 -29.760 30.258  0.70 67.89 ? 215 GLU   D CG  1 
ATOM   6990 C CD  . GLU   D 1 236 ? -22.331 -29.001 31.530  0.70 67.37 ? 215 GLU   D CD  1 
ATOM   6991 O OE1 . GLU   D 1 236 ? -23.436 -29.213 32.058  0.70 65.98 ? 215 GLU   D OE1 1 
ATOM   6992 O OE2 . GLU   D 1 236 ? -21.487 -28.210 31.997  0.70 66.50 ? 215 GLU   D OE2 1 
ATOM   6993 N N   . GLU   D 1 237 ? -21.014 -29.139 26.614  1.00 65.72 ? 216 GLU   D N   1 
ATOM   6994 C CA  . GLU   D 1 237 ? -19.680 -29.277 26.041  1.00 62.56 ? 216 GLU   D CA  1 
ATOM   6995 C C   . GLU   D 1 237 ? -19.231 -27.934 25.448  1.00 53.93 ? 216 GLU   D C   1 
ATOM   6996 O O   . GLU   D 1 237 ? -18.090 -27.527 25.656  1.00 54.29 ? 216 GLU   D O   1 
ATOM   6997 C CB  . GLU   D 1 237 ? -19.562 -30.462 25.076  1.00 51.15 ? 216 GLU   D CB  1 
ATOM   6998 N N   . GLU   D 1 238 ? -20.145 -27.252 24.742  1.00 52.63 ? 217 GLU   D N   1 
ATOM   6999 C CA  . GLU   D 1 238 ? -19.887 -25.949 24.142  1.00 53.33 ? 217 GLU   D CA  1 
ATOM   7000 C C   . GLU   D 1 238 ? -19.686 -24.885 25.227  1.00 53.14 ? 217 GLU   D C   1 
ATOM   7001 O O   . GLU   D 1 238 ? -18.843 -24.005 25.087  1.00 50.34 ? 217 GLU   D O   1 
ATOM   7002 C CB  . GLU   D 1 238 ? -20.972 -25.540 23.142  1.00 59.81 ? 217 GLU   D CB  1 
ATOM   7003 N N   . LYS   D 1 239 ? -20.465 -24.960 26.311  1.00 48.62 ? 218 LYS   D N   1 
ATOM   7004 C CA  . LYS   D 1 239 ? -20.267 -24.076 27.451  1.00 51.48 ? 218 LYS   D CA  1 
ATOM   7005 C C   . LYS   D 1 239 ? -18.850 -24.251 27.989  1.00 45.38 ? 218 LYS   D C   1 
ATOM   7006 O O   . LYS   D 1 239 ? -18.146 -23.269 28.201  1.00 43.92 ? 218 LYS   D O   1 
ATOM   7007 C CB  . LYS   D 1 239 ? -21.331 -24.183 28.561  1.00 49.94 ? 218 LYS   D CB  1 
ATOM   7008 C CG  . LYS   D 1 239 ? -22.733 -23.682 28.199  1.00 51.16 ? 218 LYS   D CG  1 
ATOM   7009 C CD  . LYS   D 1 239 ? -23.740 -23.744 29.347  1.00 50.01 ? 218 LYS   D CD  1 
ATOM   7010 C CE  . LYS   D 1 239 ? -25.105 -23.274 28.954  1.00 54.77 ? 218 LYS   D CE  1 
ATOM   7011 N NZ  . LYS   D 1 239 ? -26.019 -23.176 30.098  1.00 62.23 ? 218 LYS   D NZ  1 
ATOM   7012 N N   . ASP   D 1 240 ? -18.426 -25.502 28.196  1.00 39.12 ? 219 ASP   D N   1 
ATOM   7013 C CA  . ASP   D 1 240 ? -17.125 -25.761 28.796  1.00 39.56 ? 219 ASP   D CA  1 
ATOM   7014 C C   . ASP   D 1 240 ? -15.980 -25.408 27.850  1.00 40.03 ? 219 ASP   D C   1 
ATOM   7015 O O   . ASP   D 1 240 ? -14.866 -25.151 28.314  1.00 35.30 ? 219 ASP   D O   1 
ATOM   7016 C CB  . ASP   D 1 240 ? -16.979 -27.189 29.295  1.00 48.91 ? 219 ASP   D CB  1 
ATOM   7017 C CG  . ASP   D 1 240 ? -17.765 -27.500 30.563  1.00 59.48 ? 219 ASP   D CG  1 
ATOM   7018 O OD1 . ASP   D 1 240 ? -18.253 -26.541 31.218  1.00 60.63 ? 219 ASP   D OD1 1 
ATOM   7019 O OD2 . ASP   D 1 240 ? -17.907 -28.701 30.873  1.00 65.44 ? 219 ASP   D OD2 1 
ATOM   7020 N N   . LYS   D 1 241 ? -16.243 -25.431 26.533  1.00 36.33 ? 220 LYS   D N   1 
ATOM   7021 C CA  . LYS   D 1 241 ? -15.197 -25.062 25.581  1.00 37.26 ? 220 LYS   D CA  1 
ATOM   7022 C C   . LYS   D 1 241 ? -14.823 -23.591 25.836  1.00 33.85 ? 220 LYS   D C   1 
ATOM   7023 O O   . LYS   D 1 241 ? -13.644 -23.214 25.863  1.00 36.21 ? 220 LYS   D O   1 
ATOM   7024 C CB  . LYS   D 1 241 ? -15.747 -25.371 24.179  1.00 39.62 ? 220 LYS   D CB  1 
ATOM   7025 C CG  . LYS   D 1 241 ? -14.829 -25.346 22.964  0.60 44.03 ? 220 LYS   D CG  1 
ATOM   7026 C CD  . LYS   D 1 241 ? -15.572 -25.230 21.632  0.60 47.39 ? 220 LYS   D CD  1 
ATOM   7027 C CE  . LYS   D 1 241 ? -16.200 -23.877 21.403  0.60 45.72 ? 220 LYS   D CE  1 
ATOM   7028 N NZ  . LYS   D 1 241 ? -16.791 -23.726 20.070  0.60 51.52 ? 220 LYS   D NZ  1 
ATOM   7029 N N   . TRP   D 1 242 ? -15.851 -22.776 26.086  1.00 32.58 ? 221 TRP   D N   1 
ATOM   7030 C CA  . TRP   D 1 242 ? -15.694 -21.339 26.261  1.00 37.05 ? 221 TRP   D CA  1 
ATOM   7031 C C   . TRP   D 1 242 ? -15.043 -21.003 27.589  1.00 38.38 ? 221 TRP   D C   1 
ATOM   7032 O O   . TRP   D 1 242 ? -14.150 -20.160 27.650  1.00 33.86 ? 221 TRP   D O   1 
ATOM   7033 C CB  . TRP   D 1 242 ? -17.037 -20.617 26.129  1.00 37.66 ? 221 TRP   D CB  1 
ATOM   7034 C CG  . TRP   D 1 242 ? -17.418 -20.390 24.696  1.00 45.57 ? 221 TRP   D CG  1 
ATOM   7035 C CD1 . TRP   D 1 242 ? -18.304 -21.108 23.955  1.00 43.27 ? 221 TRP   D CD1 1 
ATOM   7036 C CD2 . TRP   D 1 242 ? -16.865 -19.386 23.814  1.00 45.14 ? 221 TRP   D CD2 1 
ATOM   7037 N NE1 . TRP   D 1 242 ? -18.365 -20.608 22.681  1.00 47.68 ? 221 TRP   D NE1 1 
ATOM   7038 C CE2 . TRP   D 1 242 ? -17.493 -19.557 22.562  1.00 48.59 ? 221 TRP   D CE2 1 
ATOM   7039 C CE3 . TRP   D 1 242 ? -15.913 -18.375 23.965  1.00 45.22 ? 221 TRP   D CE3 1 
ATOM   7040 C CZ2 . TRP   D 1 242 ? -17.192 -18.757 21.462  1.00 46.86 ? 221 TRP   D CZ2 1 
ATOM   7041 C CZ3 . TRP   D 1 242 ? -15.615 -17.581 22.874  1.00 51.67 ? 221 TRP   D CZ3 1 
ATOM   7042 C CH2 . TRP   D 1 242 ? -16.252 -17.769 21.643  1.00 44.62 ? 221 TRP   D CH2 1 
ATOM   7043 N N   . ARG   D 1 243 ? -15.506 -21.674 28.647  1.00 36.71 ? 222 ARG   D N   1 
ATOM   7044 C CA  . ARG   D 1 243 ? -14.940 -21.482 29.969  1.00 37.00 ? 222 ARG   D CA  1 
ATOM   7045 C C   . ARG   D 1 243 ? -13.430 -21.690 29.934  1.00 34.94 ? 222 ARG   D C   1 
ATOM   7046 O O   . ARG   D 1 243 ? -12.690 -20.886 30.469  1.00 36.51 ? 222 ARG   D O   1 
ATOM   7047 C CB  . ARG   D 1 243 ? -15.630 -22.411 30.977  1.00 37.34 ? 222 ARG   D CB  1 
ATOM   7048 C CG  . ARG   D 1 243 ? -17.104 -22.078 31.111  1.00 39.49 ? 222 ARG   D CG  1 
ATOM   7049 C CD  . ARG   D 1 243 ? -17.739 -23.095 32.071  1.00 42.39 ? 222 ARG   D CD  1 
ATOM   7050 N NE  . ARG   D 1 243 ? -19.081 -22.610 32.413  1.00 45.99 ? 222 ARG   D NE  1 
ATOM   7051 C CZ  . ARG   D 1 243 ? -20.200 -23.336 32.329  1.00 47.05 ? 222 ARG   D CZ  1 
ATOM   7052 N NH1 . ARG   D 1 243 ? -20.127 -24.636 32.089  1.00 46.55 ? 222 ARG   D NH1 1 
ATOM   7053 N NH2 . ARG   D 1 243 ? -21.378 -22.756 32.493  1.00 46.05 ? 222 ARG   D NH2 1 
ATOM   7054 N N   . ARG   D 1 244 ? -12.977 -22.759 29.279  1.00 35.78 ? 223 ARG   D N   1 
ATOM   7055 C CA  . ARG   D 1 244 ? -11.579 -23.162 29.297  1.00 36.12 ? 223 ARG   D CA  1 
ATOM   7056 C C   . ARG   D 1 244 ? -10.673 -22.130 28.619  1.00 34.74 ? 223 ARG   D C   1 
ATOM   7057 O O   . ARG   D 1 244 ? -9.467  -22.167 28.798  1.00 35.29 ? 223 ARG   D O   1 
ATOM   7058 C CB  . ARG   D 1 244 ? -11.429 -24.553 28.659  1.00 37.69 ? 223 ARG   D CB  1 
ATOM   7059 N N   . LYS   D 1 245 ? -11.262 -21.204 27.855  1.00 35.90 ? 224 LYS   D N   1 
ATOM   7060 C CA  . LYS   D 1 245 ? -10.489 -20.215 27.110  1.00 34.11 ? 224 LYS   D CA  1 
ATOM   7061 C C   . LYS   D 1 245 ? -10.185 -18.992 27.978  1.00 35.03 ? 224 LYS   D C   1 
ATOM   7062 O O   . LYS   D 1 245 ? -9.317  -18.205 27.608  1.00 31.54 ? 224 LYS   D O   1 
ATOM   7063 C CB  . LYS   D 1 245 ? -11.267 -19.766 25.862  1.00 32.28 ? 224 LYS   D CB  1 
ATOM   7064 C CG  . LYS   D 1 245 ? -11.714 -20.864 24.855  1.00 34.22 ? 224 LYS   D CG  1 
ATOM   7065 C CD  . LYS   D 1 245 ? -12.654 -20.199 23.851  1.00 42.07 ? 224 LYS   D CD  1 
ATOM   7066 C CE  . LYS   D 1 245 ? -13.349 -21.019 22.795  1.00 44.56 ? 224 LYS   D CE  1 
ATOM   7067 N NZ  . LYS   D 1 245 ? -12.353 -21.771 22.045  1.00 44.36 ? 224 LYS   D NZ  1 
ATOM   7068 N N   . VAL   D 1 246 ? -10.935 -18.805 29.081  1.00 31.51 ? 225 VAL   D N   1 
ATOM   7069 C CA  . VAL   D 1 246 ? -10.812 -17.613 29.920  1.00 31.88 ? 225 VAL   D CA  1 
ATOM   7070 C C   . VAL   D 1 246 ? -9.570  -17.735 30.805  1.00 34.47 ? 225 VAL   D C   1 
ATOM   7071 O O   . VAL   D 1 246 ? -9.534  -18.585 31.708  1.00 34.08 ? 225 VAL   D O   1 
ATOM   7072 C CB  . VAL   D 1 246 ? -12.064 -17.342 30.783  1.00 30.16 ? 225 VAL   D CB  1 
ATOM   7073 C CG1 . VAL   D 1 246 ? -11.860 -16.139 31.710  1.00 29.38 ? 225 VAL   D CG1 1 
ATOM   7074 C CG2 . VAL   D 1 246 ? -13.332 -17.201 29.956  1.00 29.89 ? 225 VAL   D CG2 1 
ATOM   7075 N N   . PRO   D 1 247 ? -8.514  -16.923 30.580  1.00 30.87 ? 226 PRO   D N   1 
ATOM   7076 C CA  . PRO   D 1 247 ? -7.320  -16.968 31.431  1.00 32.96 ? 226 PRO   D CA  1 
ATOM   7077 C C   . PRO   D 1 247 ? -7.577  -16.840 32.935  1.00 32.46 ? 226 PRO   D C   1 
ATOM   7078 O O   . PRO   D 1 247 ? -6.953  -17.553 33.727  1.00 31.19 ? 226 PRO   D O   1 
ATOM   7079 C CB  . PRO   D 1 247 ? -6.439  -15.827 30.878  1.00 35.30 ? 226 PRO   D CB  1 
ATOM   7080 C CG  . PRO   D 1 247 ? -6.903  -15.665 29.454  1.00 31.76 ? 226 PRO   D CG  1 
ATOM   7081 C CD  . PRO   D 1 247 ? -8.361  -16.009 29.427  1.00 30.87 ? 226 PRO   D CD  1 
ATOM   7082 N N   . LEU   D 1 248 ? -8.502  -15.952 33.327  1.00 26.75 ? 227 LEU   D N   1 
ATOM   7083 C CA  . LEU   D 1 248 ? -8.692  -15.652 34.743  1.00 30.45 ? 227 LEU   D CA  1 
ATOM   7084 C C   . LEU   D 1 248 ? -9.732  -16.602 35.323  1.00 32.55 ? 227 LEU   D C   1 
ATOM   7085 O O   . LEU   D 1 248 ? -10.915 -16.297 35.301  1.00 33.36 ? 227 LEU   D O   1 
ATOM   7086 C CB  . LEU   D 1 248 ? -9.108  -14.202 34.960  1.00 30.56 ? 227 LEU   D CB  1 
ATOM   7087 C CG  . LEU   D 1 248 ? -9.029  -13.665 36.400  1.00 30.93 ? 227 LEU   D CG  1 
ATOM   7088 C CD1 . LEU   D 1 248 ? -7.539  -13.563 36.728  1.00 30.07 ? 227 LEU   D CD1 1 
ATOM   7089 C CD2 . LEU   D 1 248 ? -9.739  -12.308 36.505  1.00 28.89 ? 227 LEU   D CD2 1 
ATOM   7090 N N   . GLY   D 1 249 ? -9.295  -17.791 35.778  1.00 37.67 ? 228 GLY   D N   1 
ATOM   7091 C CA  . GLY   D 1 249 ? -10.215 -18.679 36.467  1.00 36.87 ? 228 GLY   D CA  1 
ATOM   7092 C C   . GLY   D 1 249 ? -10.898 -19.723 35.577  1.00 42.28 ? 228 GLY   D C   1 
ATOM   7093 O O   . GLY   D 1 249 ? -11.658 -20.548 36.097  1.00 36.22 ? 228 GLY   D O   1 
ATOM   7094 N N   . ARG   D 1 250 ? -10.685 -19.673 34.248  1.00 34.49 ? 229 ARG   D N   1 
ATOM   7095 C CA  . ARG   D 1 250 ? -11.324 -20.634 33.352  1.00 33.92 ? 229 ARG   D CA  1 
ATOM   7096 C C   . ARG   D 1 250 ? -12.822 -20.745 33.634  1.00 38.86 ? 229 ARG   D C   1 
ATOM   7097 O O   . ARG   D 1 250 ? -13.384 -21.839 33.770  1.00 33.91 ? 229 ARG   D O   1 
ATOM   7098 C CB  . ARG   D 1 250 ? -10.611 -21.986 33.469  1.00 35.86 ? 229 ARG   D CB  1 
ATOM   7099 C CG  . ARG   D 1 250 ? -9.110  -21.825 33.284  1.00 39.51 ? 229 ARG   D CG  1 
ATOM   7100 C CD  . ARG   D 1 250 ? -8.669  -21.787 31.833  1.00 46.84 ? 229 ARG   D CD  1 
ATOM   7101 N NE  . ARG   D 1 250 ? -7.289  -21.286 31.786  1.00 48.70 ? 229 ARG   D NE  1 
ATOM   7102 C CZ  . ARG   D 1 250 ? -6.675  -20.738 30.740  1.00 47.27 ? 229 ARG   D CZ  1 
ATOM   7103 N NH1 . ARG   D 1 250 ? -7.283  -20.646 29.571  1.00 48.75 ? 229 ARG   D NH1 1 
ATOM   7104 N NH2 . ARG   D 1 250 ? -5.442  -20.283 30.874  1.00 49.22 ? 229 ARG   D NH2 1 
ATOM   7105 N N   . ARG   D 1 251 ? -13.492 -19.593 33.728  1.00 35.22 ? 230 ARG   D N   1 
ATOM   7106 C CA  . ARG   D 1 251 ? -14.928 -19.627 33.916  1.00 37.13 ? 230 ARG   D CA  1 
ATOM   7107 C C   . ARG   D 1 251 ? -15.510 -18.312 33.403  1.00 33.06 ? 230 ARG   D C   1 
ATOM   7108 O O   . ARG   D 1 251 ? -14.753 -17.347 33.293  1.00 31.56 ? 230 ARG   D O   1 
ATOM   7109 C CB  . ARG   D 1 251 ? -15.185 -19.826 35.420  1.00 38.34 ? 230 ARG   D CB  1 
ATOM   7110 C CG  . ARG   D 1 251 ? -14.643 -18.707 36.304  1.00 44.19 ? 230 ARG   D CG  1 
ATOM   7111 C CD  . ARG   D 1 251 ? -14.966 -18.790 37.801  0.60 45.25 ? 230 ARG   D CD  1 
ATOM   7112 N NE  . ARG   D 1 251 ? -13.964 -19.588 38.518  0.60 50.19 ? 230 ARG   D NE  1 
ATOM   7113 C CZ  . ARG   D 1 251 ? -13.910 -20.914 38.627  0.60 52.98 ? 230 ARG   D CZ  1 
ATOM   7114 N NH1 . ARG   D 1 251 ? -12.841 -21.480 39.160  0.60 49.65 ? 230 ARG   D NH1 1 
ATOM   7115 N NH2 . ARG   D 1 251 ? -14.901 -21.676 38.189  0.60 58.74 ? 230 ARG   D NH2 1 
ATOM   7116 N N   . GLU   D 1 252 ? -16.829 -18.311 33.125  1.00 35.57 ? 231 GLU   D N   1 
ATOM   7117 C CA  . GLU   D 1 252 ? -17.605 -17.138 32.720  1.00 32.81 ? 231 GLU   D CA  1 
ATOM   7118 C C   . GLU   D 1 252 ? -17.778 -16.156 33.891  1.00 35.63 ? 231 GLU   D C   1 
ATOM   7119 O O   . GLU   D 1 252 ? -17.688 -16.541 35.057  1.00 38.39 ? 231 GLU   D O   1 
ATOM   7120 C CB  . GLU   D 1 252 ? -18.925 -17.553 32.060  1.00 37.87 ? 231 GLU   D CB  1 
ATOM   7121 C CG  . GLU   D 1 252 ? -20.011 -18.074 33.004  1.00 39.38 ? 231 GLU   D CG  1 
ATOM   7122 C CD  . GLU   D 1 252 ? -20.009 -19.560 33.345  1.00 46.90 ? 231 GLU   D CD  1 
ATOM   7123 O OE1 . GLU   D 1 252 ? -21.130 -20.104 33.448  1.00 51.26 ? 231 GLU   D OE1 1 
ATOM   7124 O OE2 . GLU   D 1 252 ? -18.923 -20.175 33.501  1.00 40.13 ? 231 GLU   D OE2 1 
ATOM   7125 N N   . ALA   D 1 253 ? -18.012 -14.873 33.579  1.00 31.66 ? 232 ALA   D N   1 
ATOM   7126 C CA  . ALA   D 1 253 ? -18.387 -13.881 34.579  1.00 32.89 ? 232 ALA   D CA  1 
ATOM   7127 C C   . ALA   D 1 253 ? -19.765 -14.202 35.138  1.00 30.61 ? 232 ALA   D C   1 
ATOM   7128 O O   . ALA   D 1 253 ? -20.645 -14.618 34.400  1.00 33.24 ? 232 ALA   D O   1 
ATOM   7129 C CB  . ALA   D 1 253 ? -18.471 -12.497 33.955  1.00 28.99 ? 232 ALA   D CB  1 
ATOM   7130 N N   . SER   D 1 254 ? -19.969 -13.942 36.448  1.00 32.41 ? 233 SER   D N   1 
ATOM   7131 C CA  . SER   D 1 254 ? -21.327 -13.919 36.969  1.00 31.97 ? 233 SER   D CA  1 
ATOM   7132 C C   . SER   D 1 254 ? -22.022 -12.677 36.417  1.00 34.10 ? 233 SER   D C   1 
ATOM   7133 O O   . SER   D 1 254 ? -21.345 -11.713 36.036  1.00 33.94 ? 233 SER   D O   1 
ATOM   7134 C CB  . SER   D 1 254 ? -21.327 -13.874 38.493  1.00 32.16 ? 233 SER   D CB  1 
ATOM   7135 O OG  . SER   D 1 254 ? -20.886 -12.596 38.939  1.00 36.54 ? 233 SER   D OG  1 
ATOM   7136 N N   . ALA   D 1 255 ? -23.362 -12.705 36.401  1.00 29.14 ? 234 ALA   D N   1 
ATOM   7137 C CA  . ALA   D 1 255 ? -24.161 -11.534 36.080  1.00 28.68 ? 234 ALA   D CA  1 
ATOM   7138 C C   . ALA   D 1 255 ? -23.791 -10.400 37.035  1.00 35.42 ? 234 ALA   D C   1 
ATOM   7139 O O   . ALA   D 1 255 ? -23.696 -9.234  36.644  1.00 32.58 ? 234 ALA   D O   1 
ATOM   7140 C CB  . ALA   D 1 255 ? -25.632 -11.899 36.185  1.00 35.21 ? 234 ALA   D CB  1 
ATOM   7141 N N   . GLU   D 1 256 ? -23.571 -10.756 38.315  1.00 35.30 ? 235 GLU   D N   1 
ATOM   7142 C CA  . GLU   D 1 256 ? -23.259 -9.759  39.333  1.00 33.68 ? 235 GLU   D CA  1 
ATOM   7143 C C   . GLU   D 1 256 ? -21.922 -9.070  39.036  1.00 31.68 ? 235 GLU   D C   1 
ATOM   7144 O O   . GLU   D 1 256 ? -21.783 -7.885  39.339  1.00 31.03 ? 235 GLU   D O   1 
ATOM   7145 C CB  . GLU   D 1 256 ? -23.360 -10.342 40.755  1.00 40.05 ? 235 GLU   D CB  1 
ATOM   7146 C CG  . GLU   D 1 256 ? -24.759 -10.893 41.057  1.00 43.99 ? 235 GLU   D CG  1 
ATOM   7147 C CD  . GLU   D 1 256 ? -25.226 -12.177 40.351  1.00 53.26 ? 235 GLU   D CD  1 
ATOM   7148 O OE1 . GLU   D 1 256 ? -24.381 -12.963 39.861  1.00 48.81 ? 235 GLU   D OE1 1 
ATOM   7149 O OE2 . GLU   D 1 256 ? -26.460 -12.403 40.254  1.00 57.00 ? 235 GLU   D OE2 1 
ATOM   7150 N N   . GLN   D 1 257 ? -20.934 -9.808  38.499  1.00 29.88 ? 236 GLN   D N   1 
ATOM   7151 C CA  . GLN   D 1 257 ? -19.632 -9.217  38.179  1.00 29.39 ? 236 GLN   D CA  1 
ATOM   7152 C C   . GLN   D 1 257 ? -19.779 -8.165  37.061  1.00 25.62 ? 236 GLN   D C   1 
ATOM   7153 O O   . GLN   D 1 257 ? -19.170 -7.090  37.136  1.00 27.04 ? 236 GLN   D O   1 
ATOM   7154 C CB  . GLN   D 1 257 ? -18.586 -10.282 37.851  1.00 33.81 ? 236 GLN   D CB  1 
ATOM   7155 C CG  . GLN   D 1 257 ? -18.107 -11.055 39.081  1.00 33.86 ? 236 GLN   D CG  1 
ATOM   7156 C CD  . GLN   D 1 257 ? -17.249 -12.261 38.743  1.00 34.25 ? 236 GLN   D CD  1 
ATOM   7157 O OE1 . GLN   D 1 257 ? -17.511 -13.004 37.793  1.00 33.84 ? 236 GLN   D OE1 1 
ATOM   7158 N NE2 . GLN   D 1 257 ? -16.227 -12.488 39.554  1.00 35.88 ? 236 GLN   D NE2 1 
ATOM   7159 N N   . ILE   D 1 258 ? -20.628 -8.445  36.075  1.00 30.02 ? 237 ILE   D N   1 
ATOM   7160 C CA  . ILE   D 1 258 ? -20.927 -7.444  35.040  1.00 29.88 ? 237 ILE   D CA  1 
ATOM   7161 C C   . ILE   D 1 258 ? -21.627 -6.234  35.661  1.00 30.46 ? 237 ILE   D C   1 
ATOM   7162 O O   . ILE   D 1 258 ? -21.287 -5.079  35.378  1.00 28.99 ? 237 ILE   D O   1 
ATOM   7163 C CB  . ILE   D 1 258 ? -21.744 -8.060  33.885  1.00 30.55 ? 237 ILE   D CB  1 
ATOM   7164 C CG1 . ILE   D 1 258 ? -21.017 -9.253  33.259  1.00 28.29 ? 237 ILE   D CG1 1 
ATOM   7165 C CG2 . ILE   D 1 258 ? -22.149 -7.000  32.839  1.00 26.16 ? 237 ILE   D CG2 1 
ATOM   7166 C CD1 . ILE   D 1 258 ? -19.554 -9.000  32.922  1.00 28.25 ? 237 ILE   D CD1 1 
ATOM   7167 N N   . ALA   D 1 259 ? -22.610 -6.491  36.524  1.00 28.83 ? 238 ALA   D N   1 
ATOM   7168 C CA  . ALA   D 1 259 ? -23.342 -5.409  37.165  1.00 30.80 ? 238 ALA   D CA  1 
ATOM   7169 C C   . ALA   D 1 259 ? -22.415 -4.502  37.978  1.00 28.43 ? 238 ALA   D C   1 
ATOM   7170 O O   . ALA   D 1 259 ? -22.644 -3.295  38.055  1.00 32.23 ? 238 ALA   D O   1 
ATOM   7171 C CB  . ALA   D 1 259 ? -24.494 -5.983  37.993  1.00 29.87 ? 238 ALA   D CB  1 
ATOM   7172 N N   . ASP   D 1 260 ? -21.375 -5.069  38.599  1.00 29.22 ? 239 ASP   D N   1 
ATOM   7173 C CA  . ASP   D 1 260 ? -20.448 -4.294  39.418  1.00 31.00 ? 239 ASP   D CA  1 
ATOM   7174 C C   . ASP   D 1 260 ? -19.801 -3.175  38.605  1.00 33.60 ? 239 ASP   D C   1 
ATOM   7175 O O   . ASP   D 1 260 ? -19.616 -2.069  39.089  1.00 29.90 ? 239 ASP   D O   1 
ATOM   7176 C CB  . ASP   D 1 260 ? -19.370 -5.152  40.061  1.00 31.76 ? 239 ASP   D CB  1 
ATOM   7177 C CG  . ASP   D 1 260 ? -19.819 -6.015  41.242  1.00 38.66 ? 239 ASP   D CG  1 
ATOM   7178 O OD1 . ASP   D 1 260 ? -20.708 -5.539  42.004  1.00 34.17 ? 239 ASP   D OD1 1 
ATOM   7179 O OD2 . ASP   D 1 260 ? -19.301 -7.154  41.375  1.00 35.55 ? 239 ASP   D OD2 1 
ATOM   7180 N N   . ALA   D 1 261 ? -19.429 -3.470  37.356  1.00 30.36 ? 240 ALA   D N   1 
ATOM   7181 C CA  . ALA   D 1 261 ? -18.839 -2.439  36.513  1.00 26.84 ? 240 ALA   D CA  1 
ATOM   7182 C C   . ALA   D 1 261 ? -19.869 -1.373  36.123  1.00 23.45 ? 240 ALA   D C   1 
ATOM   7183 O O   . ALA   D 1 261 ? -19.522 -0.198  36.009  1.00 29.13 ? 240 ALA   D O   1 
ATOM   7184 C CB  . ALA   D 1 261 ? -18.223 -3.113  35.299  1.00 29.50 ? 240 ALA   D CB  1 
ATOM   7185 N N   . VAL   D 1 262 ? -21.123 -1.764  35.929  1.00 27.43 ? 241 VAL   D N   1 
ATOM   7186 C CA  . VAL   D 1 262 ? -22.182 -0.808  35.638  1.00 28.64 ? 241 VAL   D CA  1 
ATOM   7187 C C   . VAL   D 1 262 ? -22.350 0.136   36.822  1.00 31.40 ? 241 VAL   D C   1 
ATOM   7188 O O   . VAL   D 1 262 ? -22.426 1.356   36.630  1.00 26.80 ? 241 VAL   D O   1 
ATOM   7189 C CB  . VAL   D 1 262 ? -23.502 -1.512  35.289  1.00 29.47 ? 241 VAL   D CB  1 
ATOM   7190 C CG1 . VAL   D 1 262 ? -24.665 -0.527  35.085  1.00 28.17 ? 241 VAL   D CG1 1 
ATOM   7191 C CG2 . VAL   D 1 262 ? -23.329 -2.452  34.102  1.00 30.00 ? 241 VAL   D CG2 1 
ATOM   7192 N N   . ILE   D 1 263 ? -22.386 -0.453  38.036  1.00 29.89 ? 242 ILE   D N   1 
ATOM   7193 C CA  . ILE   D 1 263 ? -22.493 0.332   39.271  1.00 32.18 ? 242 ILE   D CA  1 
ATOM   7194 C C   . ILE   D 1 263 ? -21.351 1.337   39.384  1.00 26.41 ? 242 ILE   D C   1 
ATOM   7195 O O   . ILE   D 1 263 ? -21.553 2.506   39.723  1.00 29.11 ? 242 ILE   D O   1 
ATOM   7196 C CB  . ILE   D 1 263 ? -22.635 -0.578  40.522  1.00 34.21 ? 242 ILE   D CB  1 
ATOM   7197 C CG1 . ILE   D 1 263 ? -23.980 -1.302  40.516  1.00 41.06 ? 242 ILE   D CG1 1 
ATOM   7198 C CG2 . ILE   D 1 263 ? -22.419 0.182   41.833  1.00 34.76 ? 242 ILE   D CG2 1 
ATOM   7199 C CD1 . ILE   D 1 263 ? -25.174 -0.403  40.268  1.00 42.66 ? 242 ILE   D CD1 1 
ATOM   7200 N N   . PHE   D 1 264 ? -20.123 0.889   39.145  1.00 27.83 ? 243 PHE   D N   1 
ATOM   7201 C CA  . PHE   D 1 264 ? -19.001 1.805   39.177  1.00 24.77 ? 243 PHE   D CA  1 
ATOM   7202 C C   . PHE   D 1 264 ? -19.213 3.004   38.252  1.00 28.14 ? 243 PHE   D C   1 
ATOM   7203 O O   . PHE   D 1 264 ? -19.037 4.167   38.664  1.00 26.98 ? 243 PHE   D O   1 
ATOM   7204 C CB  . PHE   D 1 264 ? -17.649 1.115   38.981  1.00 26.97 ? 243 PHE   D CB  1 
ATOM   7205 C CG  . PHE   D 1 264 ? -16.496 2.075   38.733  1.00 27.47 ? 243 PHE   D CG  1 
ATOM   7206 C CD1 . PHE   D 1 264 ? -15.994 2.867   39.761  1.00 26.85 ? 243 PHE   D CD1 1 
ATOM   7207 C CD2 . PHE   D 1 264 ? -15.918 2.195   37.461  1.00 26.14 ? 243 PHE   D CD2 1 
ATOM   7208 C CE1 . PHE   D 1 264 ? -14.949 3.753   39.534  1.00 27.66 ? 243 PHE   D CE1 1 
ATOM   7209 C CE2 . PHE   D 1 264 ? -14.872 3.070   37.253  1.00 26.64 ? 243 PHE   D CE2 1 
ATOM   7210 C CZ  . PHE   D 1 264 ? -14.383 3.852   38.272  1.00 30.34 ? 243 PHE   D CZ  1 
ATOM   7211 N N   . LEU   D 1 265 ? -19.595 2.720   37.000  1.00 25.92 ? 244 LEU   D N   1 
ATOM   7212 C CA  . LEU   D 1 265 ? -19.712 3.760   35.993  1.00 27.36 ? 244 LEU   D CA  1 
ATOM   7213 C C   . LEU   D 1 265 ? -20.769 4.803   36.341  1.00 27.32 ? 244 LEU   D C   1 
ATOM   7214 O O   . LEU   D 1 265 ? -20.612 5.972   35.978  1.00 29.04 ? 244 LEU   D O   1 
ATOM   7215 C CB  . LEU   D 1 265 ? -19.900 3.157   34.592  1.00 25.90 ? 244 LEU   D CB  1 
ATOM   7216 C CG  . LEU   D 1 265 ? -18.631 2.495   34.026  1.00 27.55 ? 244 LEU   D CG  1 
ATOM   7217 C CD1 . LEU   D 1 265 ? -18.887 1.668   32.776  1.00 26.31 ? 244 LEU   D CD1 1 
ATOM   7218 C CD2 . LEU   D 1 265 ? -17.711 3.632   33.695  1.00 27.07 ? 244 LEU   D CD2 1 
ATOM   7219 N N   . VAL   D 1 266 ? -21.834 4.397   37.034  1.00 28.70 ? 245 VAL   D N   1 
ATOM   7220 C CA  . VAL   D 1 266 ? -22.881 5.377   37.296  1.00 28.33 ? 245 VAL   D CA  1 
ATOM   7221 C C   . VAL   D 1 266 ? -22.567 6.128   38.593  1.00 33.56 ? 245 VAL   D C   1 
ATOM   7222 O O   . VAL   D 1 266 ? -23.157 7.177   38.842  1.00 33.22 ? 245 VAL   D O   1 
ATOM   7223 C CB  . VAL   D 1 266 ? -24.315 4.810   37.297  1.00 32.93 ? 245 VAL   D CB  1 
ATOM   7224 C CG1 . VAL   D 1 266 ? -24.635 4.040   36.019  1.00 26.61 ? 245 VAL   D CG1 1 
ATOM   7225 C CG2 . VAL   D 1 266 ? -24.578 3.908   38.491  1.00 33.90 ? 245 VAL   D CG2 1 
ATOM   7226 N N   . SER   D 1 267 ? -21.605 5.616   39.370  1.00 32.30 ? 246 SER   D N   1 
ATOM   7227 C CA  . SER   D 1 267 ? -21.301 6.110   40.712  1.00 32.79 ? 246 SER   D CA  1 
ATOM   7228 C C   . SER   D 1 267 ? -20.612 7.467   40.680  1.00 33.97 ? 246 SER   D C   1 
ATOM   7229 O O   . SER   D 1 267 ? -20.156 7.943   39.637  1.00 33.07 ? 246 SER   D O   1 
ATOM   7230 C CB  . SER   D 1 267 ? -20.460 5.108   41.483  1.00 29.62 ? 246 SER   D CB  1 
ATOM   7231 O OG  . SER   D 1 267 ? -19.074 5.307   41.211  1.00 30.29 ? 246 SER   D OG  1 
ATOM   7232 N N   . GLY   D 1 268 ? -20.506 8.083   41.873  1.00 35.25 ? 247 GLY   D N   1 
ATOM   7233 C CA  . GLY   D 1 268 ? -19.748 9.311   42.035  1.00 33.03 ? 247 GLY   D CA  1 
ATOM   7234 C C   . GLY   D 1 268 ? -18.231 9.125   41.915  1.00 31.88 ? 247 GLY   D C   1 
ATOM   7235 O O   . GLY   D 1 268 ? -17.516 10.117  41.880  1.00 39.23 ? 247 GLY   D O   1 
ATOM   7236 N N   . SER   D 1 269 ? -17.747 7.876   41.835  1.00 30.26 ? 248 SER   D N   1 
ATOM   7237 C CA  . SER   D 1 269 ? -16.335 7.553   41.664  1.00 28.13 ? 248 SER   D CA  1 
ATOM   7238 C C   . SER   D 1 269 ? -15.933 7.550   40.182  1.00 32.85 ? 248 SER   D C   1 
ATOM   7239 O O   . SER   D 1 269 ? -14.760 7.356   39.867  1.00 29.60 ? 248 SER   D O   1 
ATOM   7240 C CB  . SER   D 1 269 ? -15.996 6.189   42.264  1.00 32.94 ? 248 SER   D CB  1 
ATOM   7241 O OG  . SER   D 1 269 ? -16.330 6.149   43.649  1.00 38.28 ? 248 SER   D OG  1 
ATOM   7242 N N   . ALA   D 1 270 ? -16.905 7.769   39.292  1.00 30.58 ? 249 ALA   D N   1 
ATOM   7243 C CA  . ALA   D 1 270 ? -16.604 7.791   37.871  1.00 28.45 ? 249 ALA   D CA  1 
ATOM   7244 C C   . ALA   D 1 270 ? -16.984 9.128   37.248  1.00 29.07 ? 249 ALA   D C   1 
ATOM   7245 O O   . ALA   D 1 270 ? -17.194 9.199   36.044  1.00 26.01 ? 249 ALA   D O   1 
ATOM   7246 C CB  . ALA   D 1 270 ? -17.326 6.652   37.207  1.00 27.76 ? 249 ALA   D CB  1 
ATOM   7247 N N   . GLN   D 1 271 ? -16.940 10.226  38.031  1.00 27.95 ? 250 GLN   D N   1 
ATOM   7248 C CA  . GLN   D 1 271 ? -17.461 11.504  37.554  1.00 29.75 ? 250 GLN   D CA  1 
ATOM   7249 C C   . GLN   D 1 271 ? -16.638 12.162  36.445  1.00 26.16 ? 250 GLN   D C   1 
ATOM   7250 O O   . GLN   D 1 271 ? -17.126 13.108  35.822  1.00 29.63 ? 250 GLN   D O   1 
ATOM   7251 C CB  . GLN   D 1 271 ? -17.707 12.498  38.695  1.00 38.50 ? 250 GLN   D CB  1 
ATOM   7252 C CG  . GLN   D 1 271 ? -18.963 12.131  39.486  1.00 43.72 ? 250 GLN   D CG  1 
ATOM   7253 C CD  . GLN   D 1 271 ? -19.680 13.301  40.123  0.70 50.91 ? 250 GLN   D CD  1 
ATOM   7254 O OE1 . GLN   D 1 271 ? -20.799 13.157  40.632  0.70 53.01 ? 250 GLN   D OE1 1 
ATOM   7255 N NE2 . GLN   D 1 271 ? -19.060 14.474  40.084  0.70 49.69 ? 250 GLN   D NE2 1 
ATOM   7256 N N   . TYR   D 1 272 ? -15.405 11.704  36.192  1.00 26.10 ? 251 TYR   D N   1 
ATOM   7257 C CA  . TYR   D 1 272 ? -14.627 12.287  35.111  1.00 25.63 ? 251 TYR   D CA  1 
ATOM   7258 C C   . TYR   D 1 272 ? -14.516 11.295  33.944  1.00 23.16 ? 251 TYR   D C   1 
ATOM   7259 O O   . TYR   D 1 272 ? -13.822 11.587  32.985  1.00 24.62 ? 251 TYR   D O   1 
ATOM   7260 C CB  . TYR   D 1 272 ? -13.235 12.718  35.581  1.00 25.91 ? 251 TYR   D CB  1 
ATOM   7261 C CG  . TYR   D 1 272 ? -12.479 13.718  34.720  1.00 27.85 ? 251 TYR   D CG  1 
ATOM   7262 C CD1 . TYR   D 1 272 ? -12.865 15.055  34.664  1.00 29.43 ? 251 TYR   D CD1 1 
ATOM   7263 C CD2 . TYR   D 1 272 ? -11.370 13.334  33.976  1.00 23.86 ? 251 TYR   D CD2 1 
ATOM   7264 C CE1 . TYR   D 1 272 ? -12.169 15.975  33.896  1.00 27.04 ? 251 TYR   D CE1 1 
ATOM   7265 C CE2 . TYR   D 1 272 ? -10.661 14.245  33.220  1.00 27.39 ? 251 TYR   D CE2 1 
ATOM   7266 C CZ  . TYR   D 1 272 ? -11.042 15.572  33.190  1.00 27.62 ? 251 TYR   D CZ  1 
ATOM   7267 O OH  . TYR   D 1 272 ? -10.297 16.423  32.436  1.00 25.02 ? 251 TYR   D OH  1 
ATOM   7268 N N   . ILE   D 1 273 ? -15.198 10.147  34.046  1.00 25.05 ? 252 ILE   D N   1 
ATOM   7269 C CA  . ILE   D 1 273 ? -15.121 9.110   33.027  1.00 24.98 ? 252 ILE   D CA  1 
ATOM   7270 C C   . ILE   D 1 273 ? -16.301 9.286   32.079  1.00 24.02 ? 252 ILE   D C   1 
ATOM   7271 O O   . ILE   D 1 273 ? -17.472 9.224   32.485  1.00 23.79 ? 252 ILE   D O   1 
ATOM   7272 C CB  . ILE   D 1 273 ? -15.109 7.703   33.658  1.00 25.28 ? 252 ILE   D CB  1 
ATOM   7273 C CG1 . ILE   D 1 273 ? -13.889 7.562   34.600  1.00 25.75 ? 252 ILE   D CG1 1 
ATOM   7274 C CG2 . ILE   D 1 273 ? -15.118 6.614   32.566  1.00 22.29 ? 252 ILE   D CG2 1 
ATOM   7275 C CD1 . ILE   D 1 273 ? -13.860 6.240   35.354  1.00 24.38 ? 252 ILE   D CD1 1 
ATOM   7276 N N   . THR   D 1 274 ? -15.986 9.511   30.798  1.00 21.76 ? 253 THR   D N   1 
ATOM   7277 C CA  . THR   D 1 274 ? -17.026 9.459   29.766  1.00 23.53 ? 253 THR   D CA  1 
ATOM   7278 C C   . THR   D 1 274 ? -16.349 8.990   28.487  1.00 20.82 ? 253 THR   D C   1 
ATOM   7279 O O   . THR   D 1 274 ? -15.181 9.304   28.263  1.00 21.35 ? 253 THR   D O   1 
ATOM   7280 C CB  . THR   D 1 274 ? -17.748 10.798  29.543  1.00 21.86 ? 253 THR   D CB  1 
ATOM   7281 O OG1 . THR   D 1 274 ? -18.969 10.558  28.850  1.00 22.27 ? 253 THR   D OG1 1 
ATOM   7282 C CG2 . THR   D 1 274 ? -16.884 11.878  28.900  1.00 23.19 ? 253 THR   D CG2 1 
ATOM   7283 N N   . GLY   D 1 275 ? -17.090 8.212   27.710  1.00 21.38 ? 254 GLY   D N   1 
ATOM   7284 C CA  . GLY   D 1 275 ? -16.585 7.708   26.443  1.00 21.33 ? 254 GLY   D CA  1 
ATOM   7285 C C   . GLY   D 1 275 ? -15.676 6.499   26.649  1.00 24.73 ? 254 GLY   D C   1 
ATOM   7286 O O   . GLY   D 1 275 ? -14.942 6.141   25.743  1.00 25.86 ? 254 GLY   D O   1 
ATOM   7287 N N   . SER   D 1 276 ? -15.763 5.848   27.810  1.00 23.63 ? 255 SER   D N   1 
ATOM   7288 C CA  . SER   D 1 276 ? -14.858 4.752   28.116  1.00 24.54 ? 255 SER   D CA  1 
ATOM   7289 C C   . SER   D 1 276 ? -15.629 3.454   28.037  1.00 24.56 ? 255 SER   D C   1 
ATOM   7290 O O   . SER   D 1 276 ? -16.752 3.409   28.517  1.00 24.82 ? 255 SER   D O   1 
ATOM   7291 C CB  . SER   D 1 276 ? -14.275 4.895   29.520  1.00 26.42 ? 255 SER   D CB  1 
ATOM   7292 O OG  . SER   D 1 276 ? -13.359 5.988   29.577  1.00 28.44 ? 255 SER   D OG  1 
ATOM   7293 N N   . ILE   D 1 277 ? -14.960 2.386   27.565  1.00 22.03 ? 256 ILE   D N   1 
ATOM   7294 C CA  . ILE   D 1 277 ? -15.598 1.083   27.600  1.00 20.59 ? 256 ILE   D CA  1 
ATOM   7295 C C   . ILE   D 1 277 ? -14.729 0.141   28.433  1.00 25.06 ? 256 ILE   D C   1 
ATOM   7296 O O   . ILE   D 1 277 ? -13.567 -0.076  28.091  1.00 27.48 ? 256 ILE   D O   1 
ATOM   7297 C CB  . ILE   D 1 277 ? -15.821 0.556   26.174  1.00 22.21 ? 256 ILE   D CB  1 
ATOM   7298 C CG1 . ILE   D 1 277 ? -16.816 1.487   25.406  1.00 25.37 ? 256 ILE   D CG1 1 
ATOM   7299 C CG2 . ILE   D 1 277 ? -16.321 -0.897  26.193  1.00 23.89 ? 256 ILE   D CG2 1 
ATOM   7300 C CD1 . ILE   D 1 277 ? -16.876 1.204   23.905  1.00 32.12 ? 256 ILE   D CD1 1 
ATOM   7301 N N   . ILE   D 1 278 ? -15.309 -0.396  29.511  1.00 23.35 ? 257 ILE   D N   1 
ATOM   7302 C CA  . ILE   D 1 278 ? -14.568 -1.241  30.433  1.00 23.12 ? 257 ILE   D CA  1 
ATOM   7303 C C   . ILE   D 1 278 ? -14.820 -2.702  30.067  1.00 20.97 ? 257 ILE   D C   1 
ATOM   7304 O O   . ILE   D 1 278 ? -15.954 -3.154  30.197  1.00 21.07 ? 257 ILE   D O   1 
ATOM   7305 C CB  . ILE   D 1 278 ? -15.012 -0.977  31.886  1.00 24.29 ? 257 ILE   D CB  1 
ATOM   7306 C CG1 . ILE   D 1 278 ? -14.779 0.490   32.263  1.00 25.92 ? 257 ILE   D CG1 1 
ATOM   7307 C CG2 . ILE   D 1 278 ? -14.181 -1.896  32.801  1.00 26.85 ? 257 ILE   D CG2 1 
ATOM   7308 C CD1 . ILE   D 1 278 ? -15.115 0.848   33.706  1.00 27.27 ? 257 ILE   D CD1 1 
ATOM   7309 N N   . LYS   D 1 279 ? -13.757 -3.437  29.690  1.00 23.13 ? 258 LYS   D N   1 
ATOM   7310 C CA  . LYS   D 1 279 ? -13.913 -4.854  29.412  1.00 23.09 ? 258 LYS   D CA  1 
ATOM   7311 C C   . LYS   D 1 279 ? -13.995 -5.568  30.759  1.00 24.06 ? 258 LYS   D C   1 
ATOM   7312 O O   . LYS   D 1 279 ? -13.247 -5.229  31.676  1.00 27.55 ? 258 LYS   D O   1 
ATOM   7313 C CB  . LYS   D 1 279 ? -12.746 -5.561  28.709  1.00 24.81 ? 258 LYS   D CB  1 
ATOM   7314 C CG  . LYS   D 1 279 ? -12.408 -5.100  27.331  1.00 28.97 ? 258 LYS   D CG  1 
ATOM   7315 C CD  . LYS   D 1 279 ? -11.228 -5.959  26.871  1.00 26.43 ? 258 LYS   D CD  1 
ATOM   7316 C CE  . LYS   D 1 279 ? -9.920  -5.263  27.166  1.00 29.15 ? 258 LYS   D CE  1 
ATOM   7317 N NZ  . LYS   D 1 279 ? -8.725  -6.083  26.929  1.00 27.58 ? 258 LYS   D NZ  1 
ATOM   7318 N N   . VAL   D 1 280 ? -14.912 -6.533  30.854  1.00 24.39 ? 259 VAL   D N   1 
ATOM   7319 C CA  . VAL   D 1 280 ? -15.047 -7.373  32.042  1.00 24.23 ? 259 VAL   D CA  1 
ATOM   7320 C C   . VAL   D 1 280 ? -15.071 -8.811  31.502  1.00 24.28 ? 259 VAL   D C   1 
ATOM   7321 O O   . VAL   D 1 280 ? -16.131 -9.436  31.407  1.00 27.30 ? 259 VAL   D O   1 
ATOM   7322 C CB  . VAL   D 1 280 ? -16.313 -7.005  32.845  1.00 27.81 ? 259 VAL   D CB  1 
ATOM   7323 C CG1 . VAL   D 1 280 ? -16.455 -7.805  34.153  1.00 26.09 ? 259 VAL   D CG1 1 
ATOM   7324 C CG2 . VAL   D 1 280 ? -16.330 -5.500  33.172  1.00 25.32 ? 259 VAL   D CG2 1 
ATOM   7325 N N   . ASP   D 1 281 ? -13.888 -9.289  31.106  1.00 25.37 ? 260 ASP   D N   1 
ATOM   7326 C CA  . ASP   D 1 281 ? -13.805 -10.465 30.242  1.00 25.12 ? 260 ASP   D CA  1 
ATOM   7327 C C   . ASP   D 1 281 ? -12.798 -11.511 30.742  1.00 24.10 ? 260 ASP   D C   1 
ATOM   7328 O O   . ASP   D 1 281 ? -12.573 -12.513 30.045  1.00 25.39 ? 260 ASP   D O   1 
ATOM   7329 C CB  . ASP   D 1 281 ? -13.504 -10.049 28.814  1.00 22.39 ? 260 ASP   D CB  1 
ATOM   7330 C CG  . ASP   D 1 281 ? -12.051 -9.708  28.474  1.00 24.51 ? 260 ASP   D CG  1 
ATOM   7331 O OD1 . ASP   D 1 281 ? -11.213 -9.496  29.382  1.00 25.60 ? 260 ASP   D OD1 1 
ATOM   7332 O OD2 . ASP   D 1 281 ? -11.732 -9.706  27.277  1.00 25.53 ? 260 ASP   D OD2 1 
ATOM   7333 N N   . GLY   D 1 282 ? -12.187 -11.282 31.911  1.00 27.01 ? 261 GLY   D N   1 
ATOM   7334 C CA  . GLY   D 1 282 ? -11.212 -12.229 32.482  1.00 25.43 ? 261 GLY   D CA  1 
ATOM   7335 C C   . GLY   D 1 282 ? -10.015 -12.523 31.578  1.00 27.57 ? 261 GLY   D C   1 
ATOM   7336 O O   . GLY   D 1 282 ? -9.369  -13.571 31.683  1.00 25.66 ? 261 GLY   D O   1 
ATOM   7337 N N   . GLY   D 1 283 ? -9.697  -11.575 30.679  1.00 24.68 ? 262 GLY   D N   1 
ATOM   7338 C CA  . GLY   D 1 283 ? -8.577  -11.760 29.778  1.00 23.10 ? 262 GLY   D CA  1 
ATOM   7339 C C   . GLY   D 1 283 ? -8.920  -12.421 28.439  1.00 21.82 ? 262 GLY   D C   1 
ATOM   7340 O O   . GLY   D 1 283 ? -8.034  -12.530 27.581  1.00 24.81 ? 262 GLY   D O   1 
ATOM   7341 N N   . LEU   D 1 284 ? -10.174 -12.787 28.213  1.00 22.17 ? 263 LEU   D N   1 
ATOM   7342 C CA  . LEU   D 1 284 ? -10.500 -13.623 27.049  1.00 23.06 ? 263 LEU   D CA  1 
ATOM   7343 C C   . LEU   D 1 284 ? -10.062 -12.991 25.718  1.00 25.15 ? 263 LEU   D C   1 
ATOM   7344 O O   . LEU   D 1 284 ? -9.535  -13.670 24.821  1.00 23.84 ? 263 LEU   D O   1 
ATOM   7345 C CB  . LEU   D 1 284 ? -12.004 -13.877 27.067  1.00 24.08 ? 263 LEU   D CB  1 
ATOM   7346 C CG  . LEU   D 1 284 ? -12.555 -14.682 25.875  1.00 24.17 ? 263 LEU   D CG  1 
ATOM   7347 C CD1 . LEU   D 1 284 ? -12.030 -16.101 25.841  1.00 27.28 ? 263 LEU   D CD1 1 
ATOM   7348 C CD2 . LEU   D 1 284 ? -14.068 -14.722 25.900  1.00 25.48 ? 263 LEU   D CD2 1 
ATOM   7349 N N   . SER   D 1 285 ? -10.251 -11.668 25.606  1.00 23.29 ? 264 SER   D N   1 
ATOM   7350 C CA  . SER   D 1 285 ? -9.955  -10.956 24.370  1.00 24.53 ? 264 SER   D CA  1 
ATOM   7351 C C   . SER   D 1 285 ? -8.457  -10.869 24.081  1.00 24.71 ? 264 SER   D C   1 
ATOM   7352 O O   . SER   D 1 285 ? -8.072  -10.494 22.965  1.00 24.21 ? 264 SER   D O   1 
ATOM   7353 C CB  . SER   D 1 285 ? -10.620 -9.599  24.370  1.00 25.33 ? 264 SER   D CB  1 
ATOM   7354 O OG  . SER   D 1 285 ? -10.028 -8.769  25.361  1.00 26.44 ? 264 SER   D OG  1 
ATOM   7355 N N   . LEU   D 1 286 ? -7.621  -11.241 25.065  1.00 23.81 ? 265 LEU   D N   1 
ATOM   7356 C CA  . LEU   D 1 286 ? -6.162  -11.232 24.971  1.00 24.34 ? 265 LEU   D CA  1 
ATOM   7357 C C   . LEU   D 1 286 ? -5.633  -12.532 24.359  1.00 23.18 ? 265 LEU   D C   1 
ATOM   7358 O O   . LEU   D 1 286 ? -4.446  -12.604 24.055  1.00 25.18 ? 265 LEU   D O   1 
ATOM   7359 C CB  . LEU   D 1 286 ? -5.472  -10.986 26.323  1.00 26.32 ? 265 LEU   D CB  1 
ATOM   7360 C CG  . LEU   D 1 286 ? -5.865  -9.662  26.989  1.00 33.32 ? 265 LEU   D CG  1 
ATOM   7361 C CD1 . LEU   D 1 286 ? -5.107  -9.500  28.297  1.00 32.28 ? 265 LEU   D CD1 1 
ATOM   7362 C CD2 . LEU   D 1 286 ? -5.616  -8.521  26.031  1.00 30.33 ? 265 LEU   D CD2 1 
ATOM   7363 N N   . VAL   D 1 287 ? -6.490  -13.555 24.207  1.00 25.49 ? 266 VAL   D N   1 
ATOM   7364 C CA  . VAL   D 1 287 ? -6.031  -14.911 23.885  1.00 25.11 ? 266 VAL   D CA  1 
ATOM   7365 C C   . VAL   D 1 287 ? -6.032  -15.122 22.369  1.00 26.39 ? 266 VAL   D C   1 
ATOM   7366 O O   . VAL   D 1 287 ? -7.075  -14.984 21.748  1.00 27.92 ? 266 VAL   D O   1 
ATOM   7367 C CB  . VAL   D 1 287 ? -6.912  -15.959 24.586  1.00 25.87 ? 266 VAL   D CB  1 
ATOM   7368 C CG1 . VAL   D 1 287 ? -6.450  -17.406 24.300  1.00 28.00 ? 266 VAL   D CG1 1 
ATOM   7369 C CG2 . VAL   D 1 287 ? -6.907  -15.754 26.107  1.00 25.39 ? 266 VAL   D CG2 1 
ATOM   7370 N N   . HIS   D 1 288 ? -4.883  -15.489 21.784  1.00 26.28 ? 267 HIS   D N   1 
ATOM   7371 C CA  . HIS   D 1 288 ? -4.831  -15.717 20.339  1.00 29.83 ? 267 HIS   D CA  1 
ATOM   7372 C C   . HIS   D 1 288 ? -5.473  -17.055 19.996  1.00 32.05 ? 267 HIS   D C   1 
ATOM   7373 O O   . HIS   D 1 288 ? -5.667  -17.886 20.880  1.00 29.97 ? 267 HIS   D O   1 
ATOM   7374 C CB  . HIS   D 1 288 ? -3.407  -15.637 19.788  1.00 29.09 ? 267 HIS   D CB  1 
ATOM   7375 C CG  . HIS   D 1 288 ? -2.490  -16.684 20.317  1.00 30.70 ? 267 HIS   D CG  1 
ATOM   7376 N ND1 . HIS   D 1 288 ? -2.534  -17.998 19.887  1.00 31.87 ? 267 HIS   D ND1 1 
ATOM   7377 C CD2 . HIS   D 1 288 ? -1.509  -16.609 21.232  1.00 32.86 ? 267 HIS   D CD2 1 
ATOM   7378 C CE1 . HIS   D 1 288 ? -1.607  -18.697 20.548  1.00 35.25 ? 267 HIS   D CE1 1 
ATOM   7379 N NE2 . HIS   D 1 288 ? -0.959  -17.863 21.365  1.00 35.99 ? 267 HIS   D NE2 1 
ATOM   7380 N N   . ALA   D 1 289 ? -5.760  -17.226 18.692  1.00 30.10 ? 268 ALA   D N   1 
ATOM   7381 C CA  . ALA   D 1 289 ? -6.363  -18.414 18.110  1.00 33.89 ? 268 ALA   D CA  1 
ATOM   7382 C C   . ALA   D 1 289 ? -5.540  -19.655 18.452  1.00 33.09 ? 268 ALA   D C   1 
ATOM   7383 O O   . ALA   D 1 289 ? -6.173  -20.726 18.420  1.00 43.29 ? 268 ALA   D O   1 
ATOM   7384 C CB  . ALA   D 1 289 ? -6.444  -18.243 16.612  1.00 31.80 ? 268 ALA   D CB  1 
ATOM   7385 O OXT . ALA   D 1 289 ? -4.325  -19.541 18.684  1.00 35.37 ? 268 ALA   D OXT 1 
HETATM 7386 P PA  . NDP   E 2 .   ? 13.936  -12.641 11.841  0.90 28.92 ? 301 NDP   A PA  1 
HETATM 7387 O O1A . NDP   E 2 .   ? 14.405  -13.488 10.716  0.90 29.84 ? 301 NDP   A O1A 1 
HETATM 7388 O O2A . NDP   E 2 .   ? 13.491  -13.267 13.118  0.90 33.15 ? 301 NDP   A O2A 1 
HETATM 7389 O O5B . NDP   E 2 .   ? 15.034  -11.502 12.175  0.90 27.82 ? 301 NDP   A O5B 1 
HETATM 7390 C C5B . NDP   E 2 .   ? 15.465  -10.587 11.149  0.90 27.33 ? 301 NDP   A C5B 1 
HETATM 7391 C C4B . NDP   E 2 .   ? 16.890  -10.162 11.431  0.90 25.46 ? 301 NDP   A C4B 1 
HETATM 7392 O O4B . NDP   E 2 .   ? 16.982  -9.452  12.680  0.90 26.30 ? 301 NDP   A O4B 1 
HETATM 7393 C C3B . NDP   E 2 .   ? 17.897  -11.310 11.643  0.90 29.36 ? 301 NDP   A C3B 1 
HETATM 7394 O O3B . NDP   E 2 .   ? 18.278  -11.877 10.386  0.90 31.89 ? 301 NDP   A O3B 1 
HETATM 7395 C C2B . NDP   E 2 .   ? 19.027  -10.624 12.417  0.90 27.83 ? 301 NDP   A C2B 1 
HETATM 7396 O O2B . NDP   E 2 .   ? 20.130  -10.326 11.551  0.90 27.55 ? 301 NDP   A O2B 1 
HETATM 7397 C C1B . NDP   E 2 .   ? 18.371  -9.316  12.905  0.90 24.75 ? 301 NDP   A C1B 1 
HETATM 7398 N N9A . NDP   E 2 .   ? 18.672  -9.092  14.301  0.90 26.07 ? 301 NDP   A N9A 1 
HETATM 7399 C C8A . NDP   E 2 .   ? 18.326  -9.845  15.396  0.90 23.73 ? 301 NDP   A C8A 1 
HETATM 7400 N N7A . NDP   E 2 .   ? 18.872  -9.412  16.508  0.90 24.41 ? 301 NDP   A N7A 1 
HETATM 7401 C C5A . NDP   E 2 .   ? 19.658  -8.337  16.114  0.90 25.95 ? 301 NDP   A C5A 1 
HETATM 7402 C C6A . NDP   E 2 .   ? 20.518  -7.468  16.826  0.90 28.20 ? 301 NDP   A C6A 1 
HETATM 7403 N N6A . NDP   E 2 .   ? 20.743  -7.556  18.141  0.90 28.86 ? 301 NDP   A N6A 1 
HETATM 7404 N N1A . NDP   E 2 .   ? 21.165  -6.523  16.100  0.90 24.96 ? 301 NDP   A N1A 1 
HETATM 7405 C C2A . NDP   E 2 .   ? 20.917  -6.409  14.794  0.90 25.97 ? 301 NDP   A C2A 1 
HETATM 7406 N N3A . NDP   E 2 .   ? 20.149  -7.185  14.014  0.90 26.48 ? 301 NDP   A N3A 1 
HETATM 7407 C C4A . NDP   E 2 .   ? 19.558  -8.139  14.753  0.90 25.45 ? 301 NDP   A C4A 1 
HETATM 7408 O O3  . NDP   E 2 .   ? 12.761  -11.745 11.224  0.90 26.50 ? 301 NDP   A O3  1 
HETATM 7409 P PN  . NDP   E 2 .   ? 11.654  -12.212 10.157  0.90 27.14 ? 301 NDP   A PN  1 
HETATM 7410 O O1N . NDP   E 2 .   ? 11.069  -13.494 10.651  0.90 25.32 ? 301 NDP   A O1N 1 
HETATM 7411 O O2N . NDP   E 2 .   ? 12.208  -12.082 8.775   0.90 25.15 ? 301 NDP   A O2N 1 
HETATM 7412 O O5D . NDP   E 2 .   ? 10.540  -11.048 10.395  0.90 26.17 ? 301 NDP   A O5D 1 
HETATM 7413 C C5D . NDP   E 2 .   ? 10.773  -9.750  9.773   0.90 24.61 ? 301 NDP   A C5D 1 
HETATM 7414 C C4D . NDP   E 2 .   ? 10.101  -8.702  10.642  0.90 25.78 ? 301 NDP   A C4D 1 
HETATM 7415 O O4D . NDP   E 2 .   ? 8.690   -9.031  10.672  0.90 24.05 ? 301 NDP   A O4D 1 
HETATM 7416 C C3D . NDP   E 2 .   ? 10.554  -8.580  12.110  0.90 25.31 ? 301 NDP   A C3D 1 
HETATM 7417 O O3D . NDP   E 2 .   ? 10.489  -7.220  12.535  0.90 25.29 ? 301 NDP   A O3D 1 
HETATM 7418 C C2D . NDP   E 2 .   ? 9.495   -9.407  12.836  0.90 24.65 ? 301 NDP   A C2D 1 
HETATM 7419 O O2D . NDP   E 2 .   ? 9.336   -9.164  14.217  0.90 23.78 ? 301 NDP   A O2D 1 
HETATM 7420 C C1D . NDP   E 2 .   ? 8.254   -9.115  11.994  0.90 27.11 ? 301 NDP   A C1D 1 
HETATM 7421 N N1N . NDP   E 2 .   ? 7.264   -10.220 12.074  0.90 25.97 ? 301 NDP   A N1N 1 
HETATM 7422 C C2N . NDP   E 2 .   ? 7.551   -11.454 11.550  0.90 25.30 ? 301 NDP   A C2N 1 
HETATM 7423 C C3N . NDP   E 2 .   ? 6.669   -12.493 11.627  0.90 23.99 ? 301 NDP   A C3N 1 
HETATM 7424 C C7N . NDP   E 2 .   ? 6.966   -13.810 11.005  0.90 29.79 ? 301 NDP   A C7N 1 
HETATM 7425 O O7N . NDP   E 2 .   ? 6.093   -14.691 11.100  0.90 27.56 ? 301 NDP   A O7N 1 
HETATM 7426 N N7N . NDP   E 2 .   ? 8.130   -14.041 10.387  0.90 27.55 ? 301 NDP   A N7N 1 
HETATM 7427 C C4N . NDP   E 2 .   ? 5.395   -12.293 12.388  0.90 24.78 ? 301 NDP   A C4N 1 
HETATM 7428 C C5N . NDP   E 2 .   ? 5.227   -10.955 13.018  0.90 27.26 ? 301 NDP   A C5N 1 
HETATM 7429 C C6N . NDP   E 2 .   ? 6.122   -10.001 12.818  0.90 25.72 ? 301 NDP   A C6N 1 
HETATM 7430 P P2B . NDP   E 2 .   ? 21.410  -11.354 11.454  0.90 28.69 ? 301 NDP   A P2B 1 
HETATM 7431 O O1X . NDP   E 2 .   ? 22.201  -10.623 10.383  0.90 26.03 ? 301 NDP   A O1X 1 
HETATM 7432 O O2X . NDP   E 2 .   ? 22.109  -11.516 12.784  0.90 29.32 ? 301 NDP   A O2X 1 
HETATM 7433 O O3X . NDP   E 2 .   ? 20.752  -12.638 10.923  0.90 27.40 ? 301 NDP   A O3X 1 
HETATM 7434 C C   . ACT   F 3 .   ? 16.710  -16.149 2.496   1.00 32.40 ? 302 ACT   A C   1 
HETATM 7435 O O   . ACT   F 3 .   ? 15.881  -15.634 1.720   1.00 31.61 ? 302 ACT   A O   1 
HETATM 7436 O OXT . ACT   F 3 .   ? 16.443  -16.462 3.669   1.00 30.88 ? 302 ACT   A OXT 1 
HETATM 7437 C CH3 . ACT   F 3 .   ? 18.144  -16.440 1.959   1.00 33.13 ? 302 ACT   A CH3 1 
HETATM 7438 C C   . ACT   G 3 .   ? 5.946   -19.759 2.678   0.70 31.41 ? 303 ACT   A C   1 
HETATM 7439 O O   . ACT   G 3 .   ? 6.511   -18.898 2.008   0.70 31.06 ? 303 ACT   A O   1 
HETATM 7440 O OXT . ACT   G 3 .   ? 4.698   -19.797 2.829   0.70 40.10 ? 303 ACT   A OXT 1 
HETATM 7441 C CH3 . ACT   G 3 .   ? 6.796   -20.939 3.220   0.70 33.88 ? 303 ACT   A CH3 1 
HETATM 7442 C CAP . A1H0U H 4 .   ? 5.634   -17.980 16.140  0.90 54.34 ? 304 A1H0U A CAP 1 
HETATM 7443 O OAO . A1H0U H 4 .   ? 5.217   -17.225 14.980  0.90 55.92 ? 304 A1H0U A OAO 1 
HETATM 7444 C CAC . A1H0U H 4 .   ? 5.667   -15.940 15.117  0.90 51.51 ? 304 A1H0U A CAC 1 
HETATM 7445 C CAQ . A1H0U H 4 .   ? 6.996   -15.615 14.788  0.90 52.11 ? 304 A1H0U A CAQ 1 
HETATM 7446 C CAD . A1H0U H 4 .   ? 7.449   -14.365 14.957  0.90 45.11 ? 304 A1H0U A CAD 1 
HETATM 7447 N NAF . A1H0U H 4 .   ? 8.639   -13.799 14.684  0.90 46.71 ? 304 A1H0U A NAF 1 
HETATM 7448 C CAL . A1H0U H 4 .   ? 9.948   -14.514 14.383  0.90 46.24 ? 304 A1H0U A CAL 1 
HETATM 7449 C CAM . A1H0U H 4 .   ? 10.376  -15.591 15.409  0.90 48.55 ? 304 A1H0U A CAM 1 
HETATM 7450 C CAN . A1H0U H 4 .   ? 9.864   -15.264 13.059  0.90 44.06 ? 304 A1H0U A CAN 1 
HETATM 7451 N NAR . A1H0U H 4 .   ? 11.048  -13.481 14.366  0.90 39.27 ? 304 A1H0U A NAR 1 
HETATM 7452 C CAJ . A1H0U H 4 .   ? 10.877  -12.146 14.861  0.90 40.72 ? 304 A1H0U A CAJ 1 
HETATM 7453 N NAK . A1H0U H 4 .   ? 11.841  -11.240 14.934  0.90 33.20 ? 304 A1H0U A NAK 1 
HETATM 7454 N NAI . A1H0U H 4 .   ? 9.628   -11.717 15.278  0.90 39.61 ? 304 A1H0U A NAI 1 
HETATM 7455 C CAG . A1H0U H 4 .   ? 8.570   -12.551 15.230  0.90 42.57 ? 304 A1H0U A CAG 1 
HETATM 7456 N NAH . A1H0U H 4 .   ? 7.303   -12.264 15.496  0.90 40.24 ? 304 A1H0U A NAH 1 
HETATM 7457 C CAE . A1H0U H 4 .   ? 6.598   -13.400 15.407  0.90 45.33 ? 304 A1H0U A CAE 1 
HETATM 7458 C CAA . A1H0U H 4 .   ? 5.333   -13.646 15.761  0.90 44.36 ? 304 A1H0U A CAA 1 
HETATM 7459 C CAB . A1H0U H 4 .   ? 4.817   -14.939 15.613  0.90 50.76 ? 304 A1H0U A CAB 1 
HETATM 7460 P PA  . NDP   I 2 .   ? -20.366 11.475  -1.187  0.90 31.09 ? 301 NDP   B PA  1 
HETATM 7461 O O1A . NDP   I 2 .   ? -20.055 12.275  -2.395  0.90 28.86 ? 301 NDP   B O1A 1 
HETATM 7462 O O2A . NDP   I 2 .   ? -20.819 12.161  0.060   0.90 31.74 ? 301 NDP   B O2A 1 
HETATM 7463 O O5B . NDP   I 2 .   ? -21.426 10.293  -1.514  0.90 30.86 ? 301 NDP   B O5B 1 
HETATM 7464 C C5B . NDP   I 2 .   ? -21.112 9.324   -2.554  0.90 28.92 ? 301 NDP   B C5B 1 
HETATM 7465 C C4B . NDP   I 2 .   ? -22.404 8.920   -3.220  0.90 26.50 ? 301 NDP   B C4B 1 
HETATM 7466 O O4B . NDP   I 2 .   ? -23.239 8.267   -2.237  0.90 25.61 ? 301 NDP   B O4B 1 
HETATM 7467 C C3B . NDP   I 2 .   ? -23.325 10.050  -3.717  0.90 30.04 ? 301 NDP   B C3B 1 
HETATM 7468 O O3B . NDP   I 2 .   ? -22.917 10.606  -4.973  0.90 32.13 ? 301 NDP   B O3B 1 
HETATM 7469 C C2B . NDP   I 2 .   ? -24.700 9.365   -3.762  0.90 27.62 ? 301 NDP   B C2B 1 
HETATM 7470 O O2B . NDP   I 2 .   ? -25.063 8.986   -5.099  0.90 28.39 ? 301 NDP   B O2B 1 
HETATM 7471 C C1B . NDP   I 2 .   ? -24.497 8.118   -2.875  0.90 25.88 ? 301 NDP   B C1B 1 
HETATM 7472 N N9A . NDP   I 2 .   ? -25.604 8.011   -1.943  0.90 24.81 ? 301 NDP   B N9A 1 
HETATM 7473 C C8A . NDP   I 2 .   ? -25.992 8.892   -0.970  0.90 25.49 ? 301 NDP   B C8A 1 
HETATM 7474 N N7A . NDP   I 2 .   ? -27.127 8.585   -0.417  0.90 26.83 ? 301 NDP   B N7A 1 
HETATM 7475 C C5A . NDP   I 2 .   ? -27.551 7.448   -1.091  0.90 25.37 ? 301 NDP   B C5A 1 
HETATM 7476 C C6A . NDP   I 2 .   ? -28.712 6.638   -0.987  0.90 28.73 ? 301 NDP   B C6A 1 
HETATM 7477 N N6A . NDP   I 2 .   ? -29.720 6.814   -0.122  0.90 29.57 ? 301 NDP   B N6A 1 
HETATM 7478 N N1A . NDP   I 2 .   ? -28.790 5.591   -1.840  0.90 24.36 ? 301 NDP   B N1A 1 
HETATM 7479 C C2A . NDP   I 2 .   ? -27.787 5.362   -2.706  0.90 25.61 ? 301 NDP   B C2A 1 
HETATM 7480 N N3A . NDP   I 2 .   ? -26.664 6.062   -2.915  0.90 22.43 ? 301 NDP   B N3A 1 
HETATM 7481 C C4A . NDP   I 2 .   ? -26.621 7.102   -2.057  0.90 24.88 ? 301 NDP   B C4A 1 
HETATM 7482 O O3  . NDP   I 2 .   ? -19.066 10.545  -0.898  0.90 26.76 ? 301 NDP   B O3  1 
HETATM 7483 P PN  . NDP   I 2 .   ? -17.503 10.865  -1.094  0.90 25.82 ? 301 NDP   B PN  1 
HETATM 7484 O O1N . NDP   I 2 .   ? -17.240 12.181  -0.424  0.90 26.94 ? 301 NDP   B O1N 1 
HETATM 7485 O O2N . NDP   I 2 .   ? -17.137 10.687  -2.527  0.90 23.86 ? 301 NDP   B O2N 1 
HETATM 7486 O O5D . NDP   I 2 .   ? -16.748 9.692   -0.254  0.90 27.07 ? 301 NDP   B O5D 1 
HETATM 7487 C C5D . NDP   I 2 .   ? -16.744 8.312   -0.686  0.90 21.68 ? 301 NDP   B C5D 1 
HETATM 7488 C C4D . NDP   I 2 .   ? -16.744 7.425   0.544   0.90 23.85 ? 301 NDP   B C4D 1 
HETATM 7489 O O4D . NDP   I 2 .   ? -15.646 7.832   1.411   0.90 21.07 ? 301 NDP   B O4D 1 
HETATM 7490 C C3D . NDP   I 2 .   ? -18.010 7.461   1.419   0.90 22.49 ? 301 NDP   B C3D 1 
HETATM 7491 O O3D . NDP   I 2 .   ? -18.311 6.154   1.884   0.90 21.40 ? 301 NDP   B O3D 1 
HETATM 7492 C C2D . NDP   I 2 .   ? -17.630 8.389   2.576   0.90 23.80 ? 301 NDP   B C2D 1 
HETATM 7493 O O2D . NDP   I 2 .   ? -18.322 8.182   3.824   0.90 22.05 ? 301 NDP   B O2D 1 
HETATM 7494 C C1D . NDP   I 2 .   ? -16.139 8.045   2.713   0.90 21.90 ? 301 NDP   B C1D 1 
HETATM 7495 N N1N . NDP   I 2 .   ? -15.402 9.199   3.316   0.90 23.70 ? 301 NDP   B N1N 1 
HETATM 7496 C C2N . NDP   I 2 .   ? -15.254 10.383  2.621   0.90 24.46 ? 301 NDP   B C2N 1 
HETATM 7497 C C3N . NDP   I 2 .   ? -14.585 11.457  3.170   0.90 24.71 ? 301 NDP   B C3N 1 
HETATM 7498 C C7N . NDP   I 2 .   ? -14.338 12.698  2.393   0.90 26.85 ? 301 NDP   B C7N 1 
HETATM 7499 O O7N . NDP   I 2 .   ? -13.672 13.578  2.929   0.90 26.22 ? 301 NDP   B O7N 1 
HETATM 7500 N N7N . NDP   I 2 .   ? -14.839 12.892  1.175   0.90 27.79 ? 301 NDP   B N7N 1 
HETATM 7501 C C4N . NDP   I 2 .   ? -14.128 11.348  4.588   0.90 25.34 ? 301 NDP   B C4N 1 
HETATM 7502 C C5N . NDP   I 2 .   ? -14.326 10.065  5.242   0.90 26.13 ? 301 NDP   B C5N 1 
HETATM 7503 C C6N . NDP   I 2 .   ? -14.934 9.073   4.609   0.90 27.78 ? 301 NDP   B C6N 1 
HETATM 7504 P P2B . NDP   I 2 .   ? -25.876 10.004  -6.109  0.90 30.16 ? 301 NDP   B P2B 1 
HETATM 7505 O O1X . NDP   I 2 .   ? -25.042 11.223  -6.342  0.90 29.85 ? 301 NDP   B O1X 1 
HETATM 7506 O O2X . NDP   I 2 .   ? -25.957 9.172   -7.379  0.90 29.24 ? 301 NDP   B O2X 1 
HETATM 7507 O O3X . NDP   I 2 .   ? -27.203 10.268  -5.444  0.90 30.77 ? 301 NDP   B O3X 1 
HETATM 7508 C C   . ACT   J 3 .   ? -30.182 4.726   -16.890 0.70 26.45 ? 302 ACT   B C   1 
HETATM 7509 O O   . ACT   J 3 .   ? -30.431 5.943   -16.891 0.70 38.62 ? 302 ACT   B O   1 
HETATM 7510 O OXT . ACT   J 3 .   ? -30.450 3.970   -15.940 0.70 37.67 ? 302 ACT   B OXT 1 
HETATM 7511 C CH3 . ACT   J 3 .   ? -29.704 4.106   -18.164 0.70 30.64 ? 302 ACT   B CH3 1 
HETATM 7512 C CAP . A1H0U K 4 .   ? -16.072 17.535  7.268   0.70 58.30 ? 303 A1H0U B CAP 1 
HETATM 7513 O OAO . A1H0U K 4 .   ? -15.328 16.821  6.246   0.70 51.80 ? 303 A1H0U B OAO 1 
HETATM 7514 C CAC . A1H0U K 4 .   ? -15.760 15.517  6.172   0.70 44.92 ? 303 A1H0U B CAC 1 
HETATM 7515 C CAQ . A1H0U K 4 .   ? -16.615 15.067  5.134   0.70 40.57 ? 303 A1H0U B CAQ 1 
HETATM 7516 C CAD . A1H0U K 4 .   ? -17.067 13.786  5.088   0.70 38.50 ? 303 A1H0U B CAD 1 
HETATM 7517 N NAF . A1H0U K 4 .   ? -17.794 13.096  4.167   0.70 39.59 ? 303 A1H0U B NAF 1 
HETATM 7518 C CAL . A1H0U K 4 .   ? -18.560 13.690  3.020   0.70 39.71 ? 303 A1H0U B CAL 1 
HETATM 7519 C CAM . A1H0U K 4 .   ? -19.374 14.966  3.290   0.70 40.05 ? 303 A1H0U B CAM 1 
HETATM 7520 C CAN . A1H0U K 4 .   ? -17.620 14.139  1.922   0.70 42.80 ? 303 A1H0U B CAN 1 
HETATM 7521 N NAR . A1H0U K 4 .   ? -19.417 12.613  2.465   0.70 41.46 ? 303 A1H0U B NAR 1 
HETATM 7522 C CAJ . A1H0U K 4 .   ? -19.592 11.316  3.029   0.70 37.96 ? 303 A1H0U B CAJ 1 
HETATM 7523 N NAK . A1H0U K 4 .   ? -20.423 10.420  2.492   0.70 29.77 ? 303 A1H0U B NAK 1 
HETATM 7524 N NAI . A1H0U K 4 .   ? -18.852 10.943  4.139   0.70 34.41 ? 303 A1H0U B NAI 1 
HETATM 7525 C CAG . A1H0U K 4 .   ? -18.035 11.861  4.729   0.70 36.91 ? 303 A1H0U B CAG 1 
HETATM 7526 N NAH . A1H0U K 4 .   ? -17.209 11.710  5.764   0.70 35.16 ? 303 A1H0U B NAH 1 
HETATM 7527 C CAE . A1H0U K 4 .   ? -16.620 12.896  6.023   0.70 34.55 ? 303 A1H0U B CAE 1 
HETATM 7528 C CAA . A1H0U K 4 .   ? -15.850 13.288  7.042   0.70 35.35 ? 303 A1H0U B CAA 1 
HETATM 7529 C CAB . A1H0U K 4 .   ? -15.370 14.600  7.161   0.70 38.19 ? 303 A1H0U B CAB 1 
HETATM 7530 P PA  . NDP   L 2 .   ? 4.704   13.074  37.745  0.70 45.81 ? 301 NDP   C PA  1 
HETATM 7531 O O1A . NDP   L 2 .   ? 4.371   14.059  38.818  0.70 41.07 ? 301 NDP   C O1A 1 
HETATM 7532 O O2A . NDP   L 2 .   ? 5.213   13.556  36.426  0.70 32.38 ? 301 NDP   C O2A 1 
HETATM 7533 O O5B . NDP   L 2 .   ? 5.698   11.936  38.315  0.70 41.31 ? 301 NDP   C O5B 1 
HETATM 7534 C C5B . NDP   L 2 .   ? 5.277   11.085  39.413  0.70 40.80 ? 301 NDP   C C5B 1 
HETATM 7535 C C4B . NDP   L 2 .   ? 6.477   10.688  40.239  0.70 40.98 ? 301 NDP   C C4B 1 
HETATM 7536 O O4B . NDP   L 2 .   ? 7.375   9.886   39.443  0.70 36.33 ? 301 NDP   C O4B 1 
HETATM 7537 C C3B . NDP   L 2 .   ? 7.396   11.819  40.726  0.70 41.07 ? 301 NDP   C C3B 1 
HETATM 7538 O O3B . NDP   L 2 .   ? 6.832   12.398  41.893  0.70 39.08 ? 301 NDP   C O3B 1 
HETATM 7539 C C2B . NDP   L 2 .   ? 8.731   11.100  40.951  0.70 41.45 ? 301 NDP   C C2B 1 
HETATM 7540 O O2B . NDP   L 2 .   ? 8.981   10.773  42.318  0.70 38.11 ? 301 NDP   C O2B 1 
HETATM 7541 C C1B . NDP   L 2 .   ? 8.580   9.795   40.156  0.70 38.75 ? 301 NDP   C C1B 1 
HETATM 7542 N N9A . NDP   L 2 .   ? 9.706   9.591   39.252  0.70 34.00 ? 301 NDP   C N9A 1 
HETATM 7543 C C8A . NDP   L 2 .   ? 10.048  10.357  38.164  0.70 28.88 ? 301 NDP   C C8A 1 
HETATM 7544 N N7A . NDP   L 2 .   ? 11.159  9.978   37.592  0.70 31.10 ? 301 NDP   C N7A 1 
HETATM 7545 C C5A . NDP   L 2 .   ? 11.619  8.937   38.395  0.70 31.76 ? 301 NDP   C C5A 1 
HETATM 7546 C C6A . NDP   L 2 .   ? 12.773  8.126   38.341  0.70 32.00 ? 301 NDP   C C6A 1 
HETATM 7547 N N6A . NDP   L 2 .   ? 13.713  8.228   37.397  0.70 29.43 ? 301 NDP   C N6A 1 
HETATM 7548 N N1A . NDP   L 2 .   ? 12.921  7.202   39.325  0.70 31.85 ? 301 NDP   C N1A 1 
HETATM 7549 C C2A . NDP   L 2 .   ? 11.959  7.061   40.252  0.70 32.78 ? 301 NDP   C C2A 1 
HETATM 7550 N N3A . NDP   L 2 .   ? 10.826  7.746   40.385  0.70 31.94 ? 301 NDP   C N3A 1 
HETATM 7551 C C4A . NDP   L 2 .   ? 10.735  8.703   39.438  0.70 34.16 ? 301 NDP   C C4A 1 
HETATM 7552 O O3  . NDP   L 2 .   ? 3.358   12.261  37.475  0.70 42.60 ? 301 NDP   C O3  1 
HETATM 7553 P PN  . NDP   L 2 .   ? 1.802   12.640  37.604  0.70 38.95 ? 301 NDP   C PN  1 
HETATM 7554 O O1N . NDP   L 2 .   ? 1.541   13.896  36.838  0.70 37.27 ? 301 NDP   C O1N 1 
HETATM 7555 O O2N . NDP   L 2 .   ? 1.389   12.517  39.032  0.70 31.97 ? 301 NDP   C O2N 1 
HETATM 7556 O O5D . NDP   L 2 .   ? 1.208   11.393  36.777  0.70 33.64 ? 301 NDP   C O5D 1 
HETATM 7557 C C5D . NDP   L 2 .   ? 1.048   10.084  37.383  0.70 33.93 ? 301 NDP   C C5D 1 
HETATM 7558 C C4D . NDP   L 2 .   ? 0.964   9.073   36.268  0.70 36.42 ? 301 NDP   C C4D 1 
HETATM 7559 O O4D . NDP   L 2 .   ? -0.130  9.431   35.367  0.70 35.70 ? 301 NDP   C O4D 1 
HETATM 7560 C C3D . NDP   L 2 .   ? 2.214   8.962   35.381  0.70 36.55 ? 301 NDP   C C3D 1 
HETATM 7561 O O3D . NDP   L 2 .   ? 2.515   7.605   35.080  0.70 33.06 ? 301 NDP   C O3D 1 
HETATM 7562 C C2D . NDP   L 2 .   ? 1.824   9.741   34.125  0.70 37.90 ? 301 NDP   C C2D 1 
HETATM 7563 O O2D . NDP   L 2 .   ? 2.511   9.391   32.924  0.70 34.27 ? 301 NDP   C O2D 1 
HETATM 7564 C C1D . NDP   L 2 .   ? 0.328   9.458   34.038  0.70 38.55 ? 301 NDP   C C1D 1 
HETATM 7565 N N1N . NDP   L 2 .   ? -0.401  10.535  33.308  0.70 38.50 ? 301 NDP   C N1N 1 
HETATM 7566 C C2N . NDP   L 2 .   ? -0.697  11.731  33.923  0.70 38.44 ? 301 NDP   C C2N 1 
HETATM 7567 C C3N . NDP   L 2 .   ? -1.319  12.763  33.242  0.70 36.78 ? 301 NDP   C C3N 1 
HETATM 7568 C C7N . NDP   L 2 .   ? -1.577  14.071  33.902  0.70 36.95 ? 301 NDP   C C7N 1 
HETATM 7569 O O7N . NDP   L 2 .   ? -2.204  14.922  33.272  0.70 35.61 ? 301 NDP   C O7N 1 
HETATM 7570 N N7N . NDP   L 2 .   ? -1.083  14.343  35.105  0.70 36.85 ? 301 NDP   C N7N 1 
HETATM 7571 C C4N . NDP   L 2 .   ? -1.665  12.548  31.818  0.70 35.32 ? 301 NDP   C C4N 1 
HETATM 7572 C C5N . NDP   L 2 .   ? -1.382  11.208  31.270  0.70 34.88 ? 301 NDP   C C5N 1 
HETATM 7573 C C6N . NDP   L 2 .   ? -0.791  10.294  32.002  0.70 35.91 ? 301 NDP   C C6N 1 
HETATM 7574 P P2B . NDP   L 2 .   ? 9.990   11.698  43.205  0.70 39.56 ? 301 NDP   C P2B 1 
HETATM 7575 O O1X . NDP   L 2 .   ? 10.087  10.906  44.495  0.70 35.01 ? 301 NDP   C O1X 1 
HETATM 7576 O O2X . NDP   L 2 .   ? 11.350  12.032  42.626  0.70 33.15 ? 301 NDP   C O2X 1 
HETATM 7577 O O3X . NDP   L 2 .   ? 9.104   12.926  43.278  0.70 37.57 ? 301 NDP   C O3X 1 
HETATM 7578 P PA  . NDP   M 2 .   ? -29.807 -11.841 26.755  0.90 33.62 ? 301 NDP   D PA  1 
HETATM 7579 O O1A . NDP   M 2 .   ? -30.301 -12.689 27.871  0.90 35.02 ? 301 NDP   D O1A 1 
HETATM 7580 O O2A . NDP   M 2 .   ? -29.351 -12.545 25.525  0.90 38.65 ? 301 NDP   D O2A 1 
HETATM 7581 O O5B . NDP   M 2 .   ? -30.888 -10.721 26.357  0.90 34.88 ? 301 NDP   D O5B 1 
HETATM 7582 C C5B . NDP   M 2 .   ? -31.280 -9.681  27.284  0.90 35.95 ? 301 NDP   D C5B 1 
HETATM 7583 C C4B . NDP   M 2 .   ? -32.731 -9.326  27.038  0.90 34.76 ? 301 NDP   D C4B 1 
HETATM 7584 O O4B . NDP   M 2 .   ? -32.874 -8.612  25.786  0.90 31.89 ? 301 NDP   D O4B 1 
HETATM 7585 C C3B . NDP   M 2 .   ? -33.745 -10.477 26.910  0.90 36.91 ? 301 NDP   D C3B 1 
HETATM 7586 O O3B . NDP   M 2 .   ? -34.068 -11.003 28.194  0.90 41.42 ? 301 NDP   D O3B 1 
HETATM 7587 C C2B . NDP   M 2 .   ? -34.881 -9.849  26.084  0.90 35.21 ? 301 NDP   D C2B 1 
HETATM 7588 O O2B . NDP   M 2 .   ? -36.075 -9.434  26.770  0.90 36.19 ? 301 NDP   D O2B 1 
HETATM 7589 C C1B . NDP   M 2 .   ? -34.240 -8.582  25.489  0.90 31.56 ? 301 NDP   D C1B 1 
HETATM 7590 N N9A . NDP   M 2 .   ? -34.524 -8.468  24.063  0.90 29.24 ? 301 NDP   D N9A 1 
HETATM 7591 C C8A . NDP   M 2 .   ? -34.185 -9.354  23.066  0.90 25.14 ? 301 NDP   D C8A 1 
HETATM 7592 N N7A . NDP   M 2 .   ? -34.735 -9.062  21.916  0.90 28.17 ? 301 NDP   D N7A 1 
HETATM 7593 C C5A . NDP   M 2 .   ? -35.542 -7.955  22.187  0.90 26.33 ? 301 NDP   D C5A 1 
HETATM 7594 C C6A . NDP   M 2 .   ? -36.413 -7.185  21.390  0.90 27.58 ? 301 NDP   D C6A 1 
HETATM 7595 N N6A . NDP   M 2 .   ? -36.631 -7.408  20.104  0.90 29.40 ? 301 NDP   D N6A 1 
HETATM 7596 N N1A . NDP   M 2 .   ? -37.045 -6.135  21.975  0.90 29.79 ? 301 NDP   D N1A 1 
HETATM 7597 C C2A . NDP   M 2 .   ? -36.828 -5.907  23.282  0.90 27.38 ? 301 NDP   D C2A 1 
HETATM 7598 N N3A . NDP   M 2 .   ? -36.039 -6.563  24.128  0.90 27.02 ? 301 NDP   D N3A 1 
HETATM 7599 C C4A . NDP   M 2 .   ? -35.440 -7.602  23.517  0.90 25.30 ? 301 NDP   D C4A 1 
HETATM 7600 O O3  . NDP   M 2 .   ? -28.621 -10.944 27.314  0.90 33.35 ? 301 NDP   D O3  1 
HETATM 7601 P PN  . NDP   M 2 .   ? -27.518 -11.215 28.415  0.90 31.00 ? 301 NDP   D PN  1 
HETATM 7602 O O1N . NDP   M 2 .   ? -26.837 -12.511 28.081  0.90 32.15 ? 301 NDP   D O1N 1 
HETATM 7603 O O2N . NDP   M 2 .   ? -28.164 -11.057 29.768  0.90 32.51 ? 301 NDP   D O2N 1 
HETATM 7604 O O5D . NDP   M 2 .   ? -26.447 -10.023 28.182  0.90 29.51 ? 301 NDP   D O5D 1 
HETATM 7605 C C5D . NDP   M 2 .   ? -26.751 -8.654  28.558  0.90 28.62 ? 301 NDP   D C5D 1 
HETATM 7606 C C4D . NDP   M 2 .   ? -26.006 -7.728  27.623  0.90 24.82 ? 301 NDP   D C4D 1 
HETATM 7607 O O4D . NDP   M 2 .   ? -24.593 -8.032  27.649  0.90 26.10 ? 301 NDP   D O4D 1 
HETATM 7608 C C3D . NDP   M 2 .   ? -26.409 -7.789  26.139  0.90 28.04 ? 301 NDP   D C3D 1 
HETATM 7609 O O3D . NDP   M 2 .   ? -26.374 -6.477  25.588  0.90 25.39 ? 301 NDP   D O3D 1 
HETATM 7610 C C2D . NDP   M 2 .   ? -25.351 -8.704  25.517  0.90 27.16 ? 301 NDP   D C2D 1 
HETATM 7611 O O2D . NDP   M 2 .   ? -25.152 -8.416  24.130  0.90 28.33 ? 301 NDP   D O2D 1 
HETATM 7612 C C1D . NDP   M 2 .   ? -24.130 -8.327  26.342  0.90 27.13 ? 301 NDP   D C1D 1 
HETATM 7613 N N1N . NDP   M 2 .   ? -23.128 -9.432  26.360  0.90 26.74 ? 301 NDP   D N1N 1 
HETATM 7614 C C2N . NDP   M 2 .   ? -23.366 -10.633 26.988  0.90 26.49 ? 301 NDP   D C2N 1 
HETATM 7615 C C3N . NDP   M 2 .   ? -22.431 -11.627 27.026  0.90 26.79 ? 301 NDP   D C3N 1 
HETATM 7616 C C7N . NDP   M 2 .   ? -22.685 -12.857 27.793  0.90 30.07 ? 301 NDP   D C7N 1 
HETATM 7617 O O7N . NDP   M 2 .   ? -21.794 -13.704 27.867  0.90 34.42 ? 301 NDP   D O7N 1 
HETATM 7618 N N7N . NDP   M 2 .   ? -23.861 -13.016 28.391  0.90 32.62 ? 301 NDP   D N7N 1 
HETATM 7619 C C4N . NDP   M 2 .   ? -21.164 -11.467 26.272  0.90 28.14 ? 301 NDP   D C4N 1 
HETATM 7620 C C5N . NDP   M 2 .   ? -21.021 -10.192 25.558  0.90 25.67 ? 301 NDP   D C5N 1 
HETATM 7621 C C6N . NDP   M 2 .   ? -21.955 -9.266  25.634  0.90 25.74 ? 301 NDP   D C6N 1 
HETATM 7622 P P2B . NDP   M 2 .   ? -37.335 -10.465 27.052  0.90 34.81 ? 301 NDP   D P2B 1 
HETATM 7623 O O1X . NDP   M 2 .   ? -36.747 -11.690 27.697  0.90 35.07 ? 301 NDP   D O1X 1 
HETATM 7624 O O2X . NDP   M 2 .   ? -38.180 -9.645  27.978  0.90 36.60 ? 301 NDP   D O2X 1 
HETATM 7625 O O3X . NDP   M 2 .   ? -37.972 -10.740 25.702  0.90 35.37 ? 301 NDP   D O3X 1 
HETATM 7626 C CAP . A1H0U N 4 .   ? -20.904 -17.511 22.773  0.80 62.82 ? 302 A1H0U D CAP 1 
HETATM 7627 O OAO . A1H0U N 4 .   ? -21.000 -16.769 23.996  0.80 55.13 ? 302 A1H0U D OAO 1 
HETATM 7628 C CAC . A1H0U N 4 .   ? -21.447 -15.499 23.810  0.80 50.46 ? 302 A1H0U D CAC 1 
HETATM 7629 C CAQ . A1H0U N 4 .   ? -22.762 -15.143 24.152  0.80 52.53 ? 302 A1H0U D CAQ 1 
HETATM 7630 C CAD . A1H0U N 4 .   ? -23.206 -13.876 23.949  0.80 50.71 ? 302 A1H0U D CAD 1 
HETATM 7631 N NAF . A1H0U N 4 .   ? -24.392 -13.266 24.227  0.80 51.58 ? 302 A1H0U D NAF 1 
HETATM 7632 C CAL . A1H0U N 4 .   ? -25.737 -13.905 24.567  0.80 53.05 ? 302 A1H0U D CAL 1 
HETATM 7633 C CAM . A1H0U N 4 .   ? -26.210 -15.031 23.642  0.80 49.54 ? 302 A1H0U D CAM 1 
HETATM 7634 C CAN . A1H0U N 4 .   ? -25.684 -14.566 25.935  0.80 54.00 ? 302 A1H0U D CAN 1 
HETATM 7635 N NAR . A1H0U N 4 .   ? -26.824 -12.879 24.515  0.80 49.33 ? 302 A1H0U D NAR 1 
HETATM 7636 C CAJ . A1H0U N 4 .   ? -26.636 -11.574 23.965  0.80 42.29 ? 302 A1H0U D CAJ 1 
HETATM 7637 N NAK . A1H0U N 4 .   ? -27.642 -10.745 23.780  0.80 32.42 ? 302 A1H0U D NAK 1 
HETATM 7638 N NAI . A1H0U N 4 .   ? -25.382 -11.151 23.567  0.80 45.21 ? 302 A1H0U D NAI 1 
HETATM 7639 C CAG . A1H0U N 4 .   ? -24.303 -12.023 23.631  0.80 45.02 ? 302 A1H0U D CAG 1 
HETATM 7640 N NAH . A1H0U N 4 .   ? -23.020 -11.782 23.363  0.80 43.34 ? 302 A1H0U D NAH 1 
HETATM 7641 C CAE . A1H0U N 4 .   ? -22.332 -12.927 23.495  0.80 41.70 ? 302 A1H0U D CAE 1 
HETATM 7642 C CAA . A1H0U N 4 .   ? -21.095 -13.223 23.129  0.80 44.42 ? 302 A1H0U D CAA 1 
HETATM 7643 C CAB . A1H0U N 4 .   ? -20.591 -14.524 23.296  0.80 47.41 ? 302 A1H0U D CAB 1 
HETATM 7644 O O   . HOH   O 5 .   ? 28.841  7.704   11.118  1.00 45.60 ? 401 HOH   A O   1 
HETATM 7645 O O   . HOH   O 5 .   ? 30.146  1.063   8.748   1.00 41.19 ? 402 HOH   A O   1 
HETATM 7646 O O   . HOH   O 5 .   ? 9.791   13.077  19.086  1.00 26.82 ? 403 HOH   A O   1 
HETATM 7647 O O   . HOH   O 5 .   ? 4.423   -21.838 -0.887  1.00 42.23 ? 404 HOH   A O   1 
HETATM 7648 O O   . HOH   O 5 .   ? 19.460  1.067   -9.152  1.00 54.17 ? 405 HOH   A O   1 
HETATM 7649 O O   . HOH   O 5 .   ? 17.963  -18.020 4.852   1.00 36.57 ? 406 HOH   A O   1 
HETATM 7650 O O   . HOH   O 5 .   ? 1.174   7.042   19.114  1.00 48.14 ? 407 HOH   A O   1 
HETATM 7651 O O   . HOH   O 5 .   ? 22.418  -11.664 -9.785  1.00 42.55 ? 408 HOH   A O   1 
HETATM 7652 O O   . HOH   O 5 .   ? 24.769  -1.310  21.057  1.00 33.33 ? 409 HOH   A O   1 
HETATM 7653 O O   . HOH   O 5 .   ? 6.802   10.369  0.802   1.00 42.51 ? 410 HOH   A O   1 
HETATM 7654 O O   . HOH   O 5 .   ? 17.579  -11.168 7.974   1.00 44.63 ? 411 HOH   A O   1 
HETATM 7655 O O   . HOH   O 5 .   ? 19.837  -14.952 11.439  1.00 47.03 ? 412 HOH   A O   1 
HETATM 7656 O O   . HOH   O 5 .   ? 3.463   -29.479 6.832   1.00 44.50 ? 413 HOH   A O   1 
HETATM 7657 O O   . HOH   O 5 .   ? 0.622   13.407  -0.534  1.00 54.26 ? 414 HOH   A O   1 
HETATM 7658 O O   . HOH   O 5 .   ? -2.759  -14.802 23.600  1.00 28.74 ? 415 HOH   A O   1 
HETATM 7659 O O   . HOH   O 5 .   ? 22.475  11.008  13.387  1.00 44.58 ? 416 HOH   A O   1 
HETATM 7660 O O   . HOH   O 5 .   ? 22.311  -15.332 -2.077  1.00 35.31 ? 417 HOH   A O   1 
HETATM 7661 O O   . HOH   O 5 .   ? 19.460  -3.274  29.485  1.00 44.96 ? 418 HOH   A O   1 
HETATM 7662 O O   . HOH   O 5 .   ? -3.555  -17.579 1.679   1.00 34.70 ? 419 HOH   A O   1 
HETATM 7663 O O   . HOH   O 5 .   ? 28.630  2.478   2.481   1.00 42.87 ? 420 HOH   A O   1 
HETATM 7664 O O   . HOH   O 5 .   ? 7.611   18.674  13.225  1.00 47.03 ? 421 HOH   A O   1 
HETATM 7665 O O   . HOH   O 5 .   ? 13.994  -13.761 1.536   1.00 32.42 ? 422 HOH   A O   1 
HETATM 7666 O O   . HOH   O 5 .   ? 4.493   11.704  8.122   1.00 25.90 ? 423 HOH   A O   1 
HETATM 7667 O O   . HOH   O 5 .   ? 14.258  -10.625 7.991   1.00 25.88 ? 424 HOH   A O   1 
HETATM 7668 O O   . HOH   O 5 .   ? 8.906   6.393   0.091   1.00 33.14 ? 425 HOH   A O   1 
HETATM 7669 O O   . HOH   O 5 .   ? 25.677  -1.110  18.418  1.00 34.40 ? 426 HOH   A O   1 
HETATM 7670 O O   . HOH   O 5 .   ? 15.686  -1.503  12.427  1.00 26.25 ? 427 HOH   A O   1 
HETATM 7671 O O   . HOH   O 5 .   ? 15.269  -12.807 15.407  1.00 39.10 ? 428 HOH   A O   1 
HETATM 7672 O O   . HOH   O 5 .   ? 21.348  -11.002 15.281  1.00 32.83 ? 429 HOH   A O   1 
HETATM 7673 O O   . HOH   O 5 .   ? 21.171  -14.005 1.645   1.00 33.86 ? 430 HOH   A O   1 
HETATM 7674 O O   . HOH   O 5 .   ? 5.020   12.067  19.997  1.00 30.01 ? 431 HOH   A O   1 
HETATM 7675 O O   . HOH   O 5 .   ? -4.018  -24.773 15.211  1.00 49.25 ? 432 HOH   A O   1 
HETATM 7676 O O   . HOH   O 5 .   ? 13.769  -2.956  13.971  1.00 31.53 ? 433 HOH   A O   1 
HETATM 7677 O O   . HOH   O 5 .   ? 5.759   -19.347 -0.542  1.00 47.74 ? 434 HOH   A O   1 
HETATM 7678 O O   . HOH   O 5 .   ? -3.406  -8.072  17.875  1.00 25.10 ? 435 HOH   A O   1 
HETATM 7679 O O   . HOH   O 5 .   ? -6.927  -7.909  22.593  1.00 37.40 ? 436 HOH   A O   1 
HETATM 7680 O O   . HOH   O 5 .   ? 3.964   18.089  4.736   1.00 45.05 ? 437 HOH   A O   1 
HETATM 7681 O O   . HOH   O 5 .   ? 16.782  11.874  -1.313  1.00 37.68 ? 438 HOH   A O   1 
HETATM 7682 O O   . HOH   O 5 .   ? 25.803  3.829   -6.877  1.00 43.61 ? 439 HOH   A O   1 
HETATM 7683 O O   . HOH   O 5 .   ? 7.509   -20.779 6.990   1.00 32.70 ? 440 HOH   A O   1 
HETATM 7684 O O   . HOH   O 5 .   ? 15.949  -13.411 18.461  1.00 40.15 ? 441 HOH   A O   1 
HETATM 7685 O O   . HOH   O 5 .   ? 9.522   -13.695 -4.336  1.00 51.47 ? 442 HOH   A O   1 
HETATM 7686 O O   . HOH   O 5 .   ? -7.117  -9.332  9.761   1.00 23.09 ? 443 HOH   A O   1 
HETATM 7687 O O   . HOH   O 5 .   ? 2.453   -12.560 15.131  1.00 37.06 ? 444 HOH   A O   1 
HETATM 7688 O O   . HOH   O 5 .   ? 0.750   -7.523  0.760   1.00 23.22 ? 445 HOH   A O   1 
HETATM 7689 O O   . HOH   O 5 .   ? -2.062  3.936   13.258  1.00 36.19 ? 446 HOH   A O   1 
HETATM 7690 O O   . HOH   O 5 .   ? 16.867  -14.756 10.878  1.00 38.31 ? 447 HOH   A O   1 
HETATM 7691 O O   . HOH   O 5 .   ? 1.784   -12.646 8.022   1.00 26.68 ? 448 HOH   A O   1 
HETATM 7692 O O   . HOH   O 5 .   ? -7.300  -6.819  14.002  1.00 40.32 ? 449 HOH   A O   1 
HETATM 7693 O O   . HOH   O 5 .   ? 4.481   -5.328  -5.220  1.00 54.33 ? 450 HOH   A O   1 
HETATM 7694 O O   . HOH   O 5 .   ? 27.854  -3.008  16.081  1.00 43.81 ? 451 HOH   A O   1 
HETATM 7695 O O   . HOH   O 5 .   ? -3.330  -5.796  14.798  1.00 40.68 ? 452 HOH   A O   1 
HETATM 7696 O O   . HOH   O 5 .   ? 2.469   17.729  12.433  1.00 46.57 ? 453 HOH   A O   1 
HETATM 7697 O O   . HOH   O 5 .   ? 28.933  -14.914 0.807   1.00 40.40 ? 454 HOH   A O   1 
HETATM 7698 O O   . HOH   O 5 .   ? -4.591  -8.917  6.656   1.00 21.59 ? 455 HOH   A O   1 
HETATM 7699 O O   . HOH   O 5 .   ? -5.995  -14.964 16.901  1.00 32.82 ? 456 HOH   A O   1 
HETATM 7700 O O   . HOH   O 5 .   ? -4.328  -2.768  8.655   1.00 27.26 ? 457 HOH   A O   1 
HETATM 7701 O O   . HOH   O 5 .   ? -0.958  -14.678 9.332   1.00 21.70 ? 458 HOH   A O   1 
HETATM 7702 O O   . HOH   O 5 .   ? 2.996   -3.587  -4.012  1.00 33.31 ? 459 HOH   A O   1 
HETATM 7703 O O   . HOH   O 5 .   ? 11.904  6.857   -2.774  1.00 40.45 ? 460 HOH   A O   1 
HETATM 7704 O O   . HOH   O 5 .   ? 1.371   -3.898  15.460  1.00 38.64 ? 461 HOH   A O   1 
HETATM 7705 O O   . HOH   O 5 .   ? -9.334  -20.039 12.157  1.00 45.23 ? 462 HOH   A O   1 
HETATM 7706 O O   . HOH   O 5 .   ? 11.136  -4.356  13.842  1.00 35.04 ? 463 HOH   A O   1 
HETATM 7707 O O   . HOH   O 5 .   ? -17.115 -18.730 16.151  1.00 46.16 ? 464 HOH   A O   1 
HETATM 7708 O O   . HOH   O 5 .   ? 0.625   -10.413 -2.339  1.00 29.96 ? 465 HOH   A O   1 
HETATM 7709 O O   . HOH   O 5 .   ? 27.285  -8.386  18.766  1.00 45.23 ? 466 HOH   A O   1 
HETATM 7710 O O   . HOH   O 5 .   ? 30.015  -3.022  7.818   1.00 40.87 ? 467 HOH   A O   1 
HETATM 7711 O O   . HOH   O 5 .   ? -7.430  -7.655  18.137  1.00 41.30 ? 468 HOH   A O   1 
HETATM 7712 O O   . HOH   O 5 .   ? -11.814 -19.514 16.705  1.00 45.90 ? 469 HOH   A O   1 
HETATM 7713 O O   . HOH   O 5 .   ? 8.889   3.537   -4.871  1.00 37.56 ? 470 HOH   A O   1 
HETATM 7714 O O   . HOH   O 5 .   ? 14.605  -18.323 12.275  1.00 39.16 ? 471 HOH   A O   1 
HETATM 7715 O O   . HOH   O 5 .   ? 18.586  11.811  0.921   1.00 40.19 ? 472 HOH   A O   1 
HETATM 7716 O O   . HOH   O 5 .   ? 22.046  -14.191 13.795  1.00 41.81 ? 473 HOH   A O   1 
HETATM 7717 O O   . HOH   O 5 .   ? 9.792   5.523   12.607  1.00 24.57 ? 474 HOH   A O   1 
HETATM 7718 O O   . HOH   O 5 .   ? 9.782   -11.481 25.124  1.00 29.50 ? 475 HOH   A O   1 
HETATM 7719 O O   . HOH   O 5 .   ? 20.357  -9.663  8.384   1.00 30.88 ? 476 HOH   A O   1 
HETATM 7720 O O   . HOH   O 5 .   ? 27.940  -0.593  14.783  1.00 37.39 ? 477 HOH   A O   1 
HETATM 7721 O O   . HOH   O 5 .   ? 6.280   13.283  17.767  1.00 35.12 ? 478 HOH   A O   1 
HETATM 7722 O O   . HOH   O 5 .   ? -2.106  8.174   -1.418  1.00 27.35 ? 479 HOH   A O   1 
HETATM 7723 O O   . HOH   O 5 .   ? 26.152  1.114   27.414  1.00 36.85 ? 480 HOH   A O   1 
HETATM 7724 O O   . HOH   O 5 .   ? -3.300  1.981   11.168  1.00 30.81 ? 481 HOH   A O   1 
HETATM 7725 O O   . HOH   O 5 .   ? 0.471   -17.379 1.468   1.00 46.13 ? 482 HOH   A O   1 
HETATM 7726 O O   . HOH   O 5 .   ? 26.447  6.703   20.605  1.00 43.69 ? 483 HOH   A O   1 
HETATM 7727 O O   . HOH   O 5 .   ? 25.483  10.102  17.368  1.00 51.98 ? 484 HOH   A O   1 
HETATM 7728 O O   . HOH   O 5 .   ? 7.699   1.228   -4.346  1.00 37.57 ? 485 HOH   A O   1 
HETATM 7729 O O   . HOH   O 5 .   ? 25.277  -15.886 6.868   1.00 35.19 ? 486 HOH   A O   1 
HETATM 7730 O O   . HOH   O 5 .   ? 19.332  -11.486 35.338  1.00 47.56 ? 487 HOH   A O   1 
HETATM 7731 O O   . HOH   O 5 .   ? 29.333  -3.764  0.532   1.00 38.39 ? 488 HOH   A O   1 
HETATM 7732 O O   . HOH   O 5 .   ? 28.468  -6.930  16.515  1.00 42.06 ? 489 HOH   A O   1 
HETATM 7733 O O   . HOH   O 5 .   ? 3.960   -3.904  16.422  1.00 38.87 ? 490 HOH   A O   1 
HETATM 7734 O O   . HOH   O 5 .   ? 12.681  9.655   -3.593  1.00 48.81 ? 491 HOH   A O   1 
HETATM 7735 O O   . HOH   O 5 .   ? 6.046   4.666   4.494   1.00 26.49 ? 492 HOH   A O   1 
HETATM 7736 O O   . HOH   O 5 .   ? 9.050   13.201  0.255   1.00 39.15 ? 493 HOH   A O   1 
HETATM 7737 O O   . HOH   O 5 .   ? 14.176  -19.143 6.973   1.00 32.85 ? 494 HOH   A O   1 
HETATM 7738 O O   . HOH   O 5 .   ? 28.400  7.464   14.034  1.00 42.84 ? 495 HOH   A O   1 
HETATM 7739 O O   . HOH   O 5 .   ? 19.406  -1.259  27.417  1.00 39.88 ? 496 HOH   A O   1 
HETATM 7740 O O   . HOH   O 5 .   ? 21.191  7.856   16.143  1.00 34.37 ? 497 HOH   A O   1 
HETATM 7741 O O   . HOH   O 5 .   ? 3.298   -12.122 -4.049  1.00 56.07 ? 498 HOH   A O   1 
HETATM 7742 O O   . HOH   O 5 .   ? 6.930   -29.471 15.827  1.00 42.80 ? 499 HOH   A O   1 
HETATM 7743 O O   . HOH   O 5 .   ? 5.527   -19.690 25.734  1.00 52.44 ? 500 HOH   A O   1 
HETATM 7744 O O   . HOH   O 5 .   ? 14.849  10.200  -7.547  1.00 61.45 ? 501 HOH   A O   1 
HETATM 7745 O O   . HOH   O 5 .   ? 13.402  -16.286 13.227  1.00 44.46 ? 502 HOH   A O   1 
HETATM 7746 O O   . HOH   O 5 .   ? 6.107   4.890   -7.350  1.00 42.11 ? 503 HOH   A O   1 
HETATM 7747 O O   . HOH   O 5 .   ? 19.965  -10.154 19.491  1.00 53.04 ? 504 HOH   A O   1 
HETATM 7748 O O   . HOH   O 5 .   ? 3.048   3.844   -7.688  1.00 51.09 ? 505 HOH   A O   1 
HETATM 7749 O O   . HOH   O 5 .   ? 27.174  0.883   12.602  1.00 43.44 ? 506 HOH   A O   1 
HETATM 7750 O O   . HOH   O 5 .   ? 0.319   -14.362 19.074  1.00 38.57 ? 507 HOH   A O   1 
HETATM 7751 O O   . HOH   O 5 .   ? 4.279   -10.011 -7.079  1.00 62.47 ? 508 HOH   A O   1 
HETATM 7752 O O   . HOH   O 5 .   ? 9.466   0.412   -10.608 1.00 54.35 ? 509 HOH   A O   1 
HETATM 7753 O O   . HOH   O 5 .   ? 28.131  -15.805 8.274   1.00 44.31 ? 510 HOH   A O   1 
HETATM 7754 O O   . HOH   O 5 .   ? 21.962  6.075   -9.595  1.00 49.17 ? 511 HOH   A O   1 
HETATM 7755 O O   . HOH   O 5 .   ? 25.438  7.694   25.036  1.00 46.18 ? 512 HOH   A O   1 
HETATM 7756 O O   . HOH   O 5 .   ? 2.426   -23.232 3.336   1.00 49.95 ? 513 HOH   A O   1 
HETATM 7757 O O   . HOH   O 5 .   ? 29.435  -3.747  -7.646  1.00 48.34 ? 514 HOH   A O   1 
HETATM 7758 O O   . HOH   O 5 .   ? 13.880  22.096  11.660  1.00 56.07 ? 515 HOH   A O   1 
HETATM 7759 O O   . HOH   O 5 .   ? 24.026  -8.785  21.335  1.00 62.27 ? 516 HOH   A O   1 
HETATM 7760 O O   . HOH   O 5 .   ? -3.154  -2.443  12.274  1.00 42.03 ? 517 HOH   A O   1 
HETATM 7761 O O   . HOH   O 5 .   ? 26.411  -12.036 18.583  1.00 49.69 ? 518 HOH   A O   1 
HETATM 7762 O O   . HOH   O 5 .   ? 5.610   13.582  0.826   1.00 52.52 ? 519 HOH   A O   1 
HETATM 7763 O O   . HOH   O 5 .   ? 3.970   -12.172 19.992  1.00 31.81 ? 520 HOH   A O   1 
HETATM 7764 O O   . HOH   O 5 .   ? 16.396  18.096  8.386   1.00 61.17 ? 521 HOH   A O   1 
HETATM 7765 O O   . HOH   O 5 .   ? 7.310   -26.968 4.230   1.00 56.31 ? 522 HOH   A O   1 
HETATM 7766 O O   . HOH   O 5 .   ? -2.679  1.693   17.682  1.00 48.78 ? 523 HOH   A O   1 
HETATM 7767 O O   . HOH   O 5 .   ? 25.933  -4.759  -14.395 1.00 60.52 ? 524 HOH   A O   1 
HETATM 7768 O O   . HOH   O 5 .   ? 11.633  4.061   -8.208  1.00 49.94 ? 525 HOH   A O   1 
HETATM 7769 O O   . HOH   O 5 .   ? 29.017  1.977   -3.947  1.00 50.66 ? 526 HOH   A O   1 
HETATM 7770 O O   . HOH   O 5 .   ? -13.374 -17.836 14.424  1.00 35.87 ? 527 HOH   A O   1 
HETATM 7771 O O   . HOH   O 5 .   ? 28.055  8.865   -4.038  1.00 54.08 ? 528 HOH   A O   1 
HETATM 7772 O O   . HOH   O 5 .   ? 6.371   23.314  6.704   1.00 62.29 ? 529 HOH   A O   1 
HETATM 7773 O O   . HOH   O 5 .   ? -7.370  -18.284 -0.176  1.00 50.22 ? 530 HOH   A O   1 
HETATM 7774 O O   . HOH   O 5 .   ? 3.429   -0.715  -6.038  1.00 51.67 ? 531 HOH   A O   1 
HETATM 7775 O O   . HOH   O 5 .   ? 17.761  -13.670 14.456  1.00 46.65 ? 532 HOH   A O   1 
HETATM 7776 O O   . HOH   O 5 .   ? 24.491  -18.502 4.731   1.00 53.34 ? 533 HOH   A O   1 
HETATM 7777 O O   . HOH   O 5 .   ? 29.346  -5.899  -0.560  1.00 57.82 ? 534 HOH   A O   1 
HETATM 7778 O O   . HOH   O 5 .   ? 20.651  9.796   17.364  1.00 44.46 ? 535 HOH   A O   1 
HETATM 7779 O O   . HOH   O 5 .   ? 27.259  -16.171 14.268  1.00 55.70 ? 536 HOH   A O   1 
HETATM 7780 O O   . HOH   O 5 .   ? 28.313  8.297   20.973  1.00 48.50 ? 537 HOH   A O   1 
HETATM 7781 O O   . HOH   O 5 .   ? -5.891  -5.392  15.102  1.00 43.10 ? 538 HOH   A O   1 
HETATM 7782 O O   . HOH   O 5 .   ? -1.758  -4.277  13.521  1.00 40.67 ? 539 HOH   A O   1 
HETATM 7783 O O   . HOH   O 5 .   ? 13.448  -21.517 6.792   1.00 41.68 ? 540 HOH   A O   1 
HETATM 7784 O O   . HOH   O 5 .   ? 16.968  -18.474 7.572   1.00 38.51 ? 541 HOH   A O   1 
HETATM 7785 O O   . HOH   O 5 .   ? 6.186   0.499   -6.837  1.00 44.20 ? 542 HOH   A O   1 
HETATM 7786 O O   . HOH   O 5 .   ? 28.273  -2.825  18.773  1.00 48.65 ? 543 HOH   A O   1 
HETATM 7787 O O   . HOH   O 5 .   ? -11.755 -18.979 12.037  1.00 54.57 ? 544 HOH   A O   1 
HETATM 7788 O O   . HOH   O 5 .   ? -1.309  -2.470  16.713  1.00 46.82 ? 545 HOH   A O   1 
HETATM 7789 O O   . HOH   O 5 .   ? 21.916  3.613   -10.666 1.00 61.19 ? 546 HOH   A O   1 
HETATM 7790 O O   . HOH   O 5 .   ? 5.950   -18.866 19.387  1.00 52.31 ? 547 HOH   A O   1 
HETATM 7791 O O   . HOH   O 5 .   ? 17.872  -10.336 -7.979  1.00 42.68 ? 548 HOH   A O   1 
HETATM 7792 O O   . HOH   P 5 .   ? -18.245 -6.671  -21.982 1.00 40.61 ? 401 HOH   B O   1 
HETATM 7793 O O   . HOH   P 5 .   ? -40.412 9.374   14.862  1.00 56.08 ? 402 HOH   B O   1 
HETATM 7794 O O   . HOH   P 5 .   ? -20.793 9.385   -6.268  1.00 43.59 ? 403 HOH   B O   1 
HETATM 7795 O O   . HOH   P 5 .   ? -3.086  3.020   -8.089  1.00 50.02 ? 404 HOH   B O   1 
HETATM 7796 O O   . HOH   P 5 .   ? -14.861 -14.295 -11.347 1.00 38.26 ? 405 HOH   B O   1 
HETATM 7797 O O   . HOH   P 5 .   ? -21.932 1.975   1.204   1.00 26.64 ? 406 HOH   B O   1 
HETATM 7798 O O   . HOH   P 5 .   ? -7.678  7.842   17.156  1.00 38.78 ? 407 HOH   B O   1 
HETATM 7799 O O   . HOH   P 5 .   ? -8.756  29.628  0.677   1.00 31.75 ? 408 HOH   B O   1 
HETATM 7800 O O   . HOH   P 5 .   ? -17.987 12.052  -17.368 1.00 51.95 ? 409 HOH   B O   1 
HETATM 7801 O O   . HOH   P 5 .   ? -9.966  29.420  6.986   1.00 45.51 ? 410 HOH   B O   1 
HETATM 7802 O O   . HOH   P 5 .   ? -22.513 -13.381 9.200   1.00 23.50 ? 411 HOH   B O   1 
HETATM 7803 O O   . HOH   P 5 .   ? -30.903 14.134  1.613   1.00 54.52 ? 412 HOH   B O   1 
HETATM 7804 O O   . HOH   P 5 .   ? -13.217 11.995  8.257   1.00 33.10 ? 413 HOH   B O   1 
HETATM 7805 O O   . HOH   P 5 .   ? -16.729 -17.164 -8.194  1.00 44.88 ? 414 HOH   B O   1 
HETATM 7806 O O   . HOH   P 5 .   ? -14.427 15.007  18.077  1.00 28.56 ? 415 HOH   B O   1 
HETATM 7807 O O   . HOH   P 5 .   ? -22.184 9.477   -25.462 1.00 54.11 ? 416 HOH   B O   1 
HETATM 7808 O O   . HOH   P 5 .   ? -11.367 -12.925 3.854   1.00 22.80 ? 417 HOH   B O   1 
HETATM 7809 O O   . HOH   P 5 .   ? -9.754  14.325  -6.916  1.00 30.71 ? 418 HOH   B O   1 
HETATM 7810 O O   . HOH   P 5 .   ? -26.531 -5.393  -16.438 1.00 41.04 ? 419 HOH   B O   1 
HETATM 7811 O O   . HOH   P 5 .   ? -13.077 8.016   -23.239 1.00 45.37 ? 420 HOH   B O   1 
HETATM 7812 O O   . HOH   P 5 .   ? -22.123 4.036   -23.277 1.00 42.36 ? 421 HOH   B O   1 
HETATM 7813 O O   . HOH   P 5 .   ? -13.803 12.055  -9.183  1.00 32.28 ? 422 HOH   B O   1 
HETATM 7814 O O   . HOH   P 5 .   ? -18.311 9.000   -4.174  1.00 25.86 ? 423 HOH   B O   1 
HETATM 7815 O O   . HOH   P 5 .   ? -14.263 26.786  -4.339  1.00 36.72 ? 424 HOH   B O   1 
HETATM 7816 O O   . HOH   P 5 .   ? -34.818 0.807   0.131   1.00 33.99 ? 425 HOH   B O   1 
HETATM 7817 O O   . HOH   P 5 .   ? -19.147 6.170   -25.661 1.00 48.97 ? 426 HOH   B O   1 
HETATM 7818 O O   . HOH   P 5 .   ? -28.109 9.994   -2.968  1.00 34.45 ? 427 HOH   B O   1 
HETATM 7819 O O   . HOH   P 5 .   ? -11.249 23.710  -3.410  1.00 33.97 ? 428 HOH   B O   1 
HETATM 7820 O O   . HOH   P 5 .   ? -3.133  9.258   -7.446  1.00 49.61 ? 429 HOH   B O   1 
HETATM 7821 O O   . HOH   P 5 .   ? -21.272 21.128  -2.930  1.00 48.57 ? 430 HOH   B O   1 
HETATM 7822 O O   . HOH   P 5 .   ? -9.161  -19.577 1.884   1.00 41.21 ? 431 HOH   B O   1 
HETATM 7823 O O   . HOH   P 5 .   ? -19.097 -16.333 -13.448 1.00 46.30 ? 432 HOH   B O   1 
HETATM 7824 O O   . HOH   P 5 .   ? -33.971 0.030   -2.286  1.00 31.37 ? 433 HOH   B O   1 
HETATM 7825 O O   . HOH   P 5 .   ? -0.188  15.777  1.085   1.00 39.17 ? 434 HOH   B O   1 
HETATM 7826 O O   . HOH   P 5 .   ? -34.363 1.683   9.319   1.00 37.43 ? 435 HOH   B O   1 
HETATM 7827 O O   . HOH   P 5 .   ? -7.897  14.005  18.033  1.00 38.22 ? 436 HOH   B O   1 
HETATM 7828 O O   . HOH   P 5 .   ? -20.840 12.123  16.424  1.00 23.41 ? 437 HOH   B O   1 
HETATM 7829 O O   . HOH   P 5 .   ? -10.140 -9.359  -9.352  1.00 35.33 ? 438 HOH   B O   1 
HETATM 7830 O O   . HOH   P 5 .   ? -22.503 0.305   -0.827  1.00 22.60 ? 439 HOH   B O   1 
HETATM 7831 O O   . HOH   P 5 .   ? -12.004 19.336  -1.625  1.00 40.43 ? 440 HOH   B O   1 
HETATM 7832 O O   . HOH   P 5 .   ? -21.534 27.778  -1.957  1.00 36.65 ? 441 HOH   B O   1 
HETATM 7833 O O   . HOH   P 5 .   ? -2.055  19.423  12.526  1.00 34.36 ? 442 HOH   B O   1 
HETATM 7834 O O   . HOH   P 5 .   ? -9.627  -8.414  -5.711  1.00 29.62 ? 443 HOH   B O   1 
HETATM 7835 O O   . HOH   P 5 .   ? -12.167 10.739  -16.191 1.00 50.30 ? 444 HOH   B O   1 
HETATM 7836 O O   . HOH   P 5 .   ? -10.342 10.077  -11.764 1.00 36.58 ? 445 HOH   B O   1 
HETATM 7837 O O   . HOH   P 5 .   ? -19.361 11.423  -13.934 1.00 37.70 ? 446 HOH   B O   1 
HETATM 7838 O O   . HOH   P 5 .   ? -29.294 17.233  9.285   1.00 46.92 ? 447 HOH   B O   1 
HETATM 7839 O O   . HOH   P 5 .   ? -2.407  1.448   -6.157  1.00 33.03 ? 448 HOH   B O   1 
HETATM 7840 O O   . HOH   P 5 .   ? -3.945  12.820  -6.921  1.00 34.64 ? 449 HOH   B O   1 
HETATM 7841 O O   . HOH   P 5 .   ? -17.639 -14.138 -10.289 1.00 35.41 ? 450 HOH   B O   1 
HETATM 7842 O O   . HOH   P 5 .   ? -5.841  21.514  -1.195  1.00 43.06 ? 451 HOH   B O   1 
HETATM 7843 O O   . HOH   P 5 .   ? 1.386   18.758  21.062  1.00 45.61 ? 452 HOH   B O   1 
HETATM 7844 O O   . HOH   P 5 .   ? -8.574  27.793  -1.277  1.00 30.34 ? 453 HOH   B O   1 
HETATM 7845 O O   . HOH   P 5 .   ? -13.405 -0.548  -27.846 1.00 55.50 ? 454 HOH   B O   1 
HETATM 7846 O O   . HOH   P 5 .   ? -12.941 3.408   10.115  1.00 31.41 ? 455 HOH   B O   1 
HETATM 7847 O O   . HOH   P 5 .   ? -32.286 8.394   -10.491 1.00 38.49 ? 456 HOH   B O   1 
HETATM 7848 O O   . HOH   P 5 .   ? -8.882  -12.471 -3.252  1.00 35.49 ? 457 HOH   B O   1 
HETATM 7849 O O   . HOH   P 5 .   ? -34.130 2.029   -5.772  1.00 41.96 ? 458 HOH   B O   1 
HETATM 7850 O O   . HOH   P 5 .   ? -3.057  -15.452 0.155   1.00 51.39 ? 459 HOH   B O   1 
HETATM 7851 O O   . HOH   P 5 .   ? -9.930  3.418   -19.000 1.00 41.42 ? 460 HOH   B O   1 
HETATM 7852 O O   . HOH   P 5 .   ? -10.768 8.193   20.641  1.00 31.23 ? 461 HOH   B O   1 
HETATM 7853 O O   . HOH   P 5 .   ? -19.612 3.462   2.686   1.00 29.39 ? 462 HOH   B O   1 
HETATM 7854 O O   . HOH   P 5 .   ? -12.620 -18.484 8.645   1.00 35.09 ? 463 HOH   B O   1 
HETATM 7855 O O   . HOH   P 5 .   ? -2.716  8.465   10.358  1.00 24.12 ? 464 HOH   B O   1 
HETATM 7856 O O   . HOH   P 5 .   ? -21.760 13.283  -4.322  1.00 43.07 ? 465 HOH   B O   1 
HETATM 7857 O O   . HOH   P 5 .   ? -7.053  13.651  5.795   1.00 22.82 ? 466 HOH   B O   1 
HETATM 7858 O O   . HOH   P 5 .   ? -2.748  7.786   6.515   1.00 22.19 ? 467 HOH   B O   1 
HETATM 7859 O O   . HOH   P 5 .   ? -36.527 -7.171  -0.260  1.00 37.95 ? 468 HOH   B O   1 
HETATM 7860 O O   . HOH   P 5 .   ? -10.624 7.812   14.666  1.00 22.13 ? 469 HOH   B O   1 
HETATM 7861 O O   . HOH   P 5 .   ? -3.391  5.784   -1.209  1.00 23.30 ? 470 HOH   B O   1 
HETATM 7862 O O   . HOH   P 5 .   ? -7.823  14.798  14.823  1.00 43.86 ? 471 HOH   B O   1 
HETATM 7863 O O   . HOH   P 5 .   ? -23.400 8.058   -7.501  1.00 27.84 ? 472 HOH   B O   1 
HETATM 7864 O O   . HOH   P 5 .   ? -13.394 31.815  1.037   1.00 28.89 ? 473 HOH   B O   1 
HETATM 7865 O O   . HOH   P 5 .   ? -10.330 14.222  -10.985 1.00 33.93 ? 474 HOH   B O   1 
HETATM 7866 O O   . HOH   P 5 .   ? -9.073  -4.614  11.352  1.00 38.10 ? 475 HOH   B O   1 
HETATM 7867 O O   . HOH   P 5 .   ? -17.225 -19.548 6.705   1.00 46.48 ? 476 HOH   B O   1 
HETATM 7868 O O   . HOH   P 5 .   ? -23.563 11.973  0.600   1.00 45.48 ? 477 HOH   B O   1 
HETATM 7869 O O   . HOH   P 5 .   ? -8.504  11.402  3.213   1.00 27.18 ? 478 HOH   B O   1 
HETATM 7870 O O   . HOH   P 5 .   ? -3.590  4.988   -11.719 1.00 50.23 ? 479 HOH   B O   1 
HETATM 7871 O O   . HOH   P 5 .   ? -9.425  7.775   -11.084 1.00 29.83 ? 480 HOH   B O   1 
HETATM 7872 O O   . HOH   P 5 .   ? -24.875 12.079  -19.495 1.00 36.22 ? 481 HOH   B O   1 
HETATM 7873 O O   . HOH   P 5 .   ? -5.168  7.997   16.232  1.00 32.21 ? 482 HOH   B O   1 
HETATM 7874 O O   . HOH   P 5 .   ? -5.369  6.296   14.064  1.00 41.09 ? 483 HOH   B O   1 
HETATM 7875 O O   . HOH   P 5 .   ? -6.607  -6.222  -9.639  1.00 34.83 ? 484 HOH   B O   1 
HETATM 7876 O O   . HOH   P 5 .   ? -8.702  5.425   12.298  1.00 34.84 ? 485 HOH   B O   1 
HETATM 7877 O O   . HOH   P 5 .   ? -3.025  -7.487  -9.728  1.00 46.13 ? 486 HOH   B O   1 
HETATM 7878 O O   . HOH   P 5 .   ? -25.260 11.643  11.798  1.00 19.84 ? 487 HOH   B O   1 
HETATM 7879 O O   . HOH   P 5 .   ? -1.322  8.212   -4.025  1.00 29.43 ? 488 HOH   B O   1 
HETATM 7880 O O   . HOH   P 5 .   ? -25.856 13.650  -12.488 1.00 36.07 ? 489 HOH   B O   1 
HETATM 7881 O O   . HOH   P 5 .   ? -3.427  15.512  -1.535  1.00 40.91 ? 490 HOH   B O   1 
HETATM 7882 O O   . HOH   P 5 .   ? -0.410  -10.040 0.128   1.00 23.96 ? 491 HOH   B O   1 
HETATM 7883 O O   . HOH   P 5 .   ? -6.963  -2.750  10.114  1.00 26.20 ? 492 HOH   B O   1 
HETATM 7884 O O   . HOH   P 5 .   ? -29.395 -8.803  -0.797  1.00 40.93 ? 493 HOH   B O   1 
HETATM 7885 O O   . HOH   P 5 .   ? -25.848 12.700  2.361   1.00 33.10 ? 494 HOH   B O   1 
HETATM 7886 O O   . HOH   P 5 .   ? -17.217 14.355  -9.399  1.00 39.02 ? 495 HOH   B O   1 
HETATM 7887 O O   . HOH   P 5 .   ? -7.182  7.539   -12.673 1.00 42.15 ? 496 HOH   B O   1 
HETATM 7888 O O   . HOH   P 5 .   ? -10.226 -6.231  -0.578  1.00 23.79 ? 497 HOH   B O   1 
HETATM 7889 O O   . HOH   P 5 .   ? -4.386  1.712   8.559   1.00 28.34 ? 498 HOH   B O   1 
HETATM 7890 O O   . HOH   P 5 .   ? -38.921 12.483  13.714  1.00 38.65 ? 499 HOH   B O   1 
HETATM 7891 O O   . HOH   P 5 .   ? -18.153 -6.510  3.398   1.00 24.42 ? 500 HOH   B O   1 
HETATM 7892 O O   . HOH   P 5 .   ? -18.817 -13.643 10.362  1.00 28.98 ? 501 HOH   B O   1 
HETATM 7893 O O   . HOH   P 5 .   ? -10.054 -15.336 -4.961  1.00 43.15 ? 502 HOH   B O   1 
HETATM 7894 O O   . HOH   P 5 .   ? -28.568 13.669  -13.247 1.00 45.37 ? 503 HOH   B O   1 
HETATM 7895 O O   . HOH   P 5 .   ? -8.728  5.393   15.697  1.00 47.79 ? 504 HOH   B O   1 
HETATM 7896 O O   . HOH   P 5 .   ? -11.118 7.440   -18.728 1.00 51.12 ? 505 HOH   B O   1 
HETATM 7897 O O   . HOH   P 5 .   ? -18.972 27.273  4.296   1.00 42.67 ? 506 HOH   B O   1 
HETATM 7898 O O   . HOH   P 5 .   ? -29.440 0.255   -15.990 1.00 34.48 ? 507 HOH   B O   1 
HETATM 7899 O O   . HOH   P 5 .   ? 0.280   -13.156 -3.795  1.00 47.28 ? 508 HOH   B O   1 
HETATM 7900 O O   . HOH   P 5 .   ? -15.160 3.551   9.602   1.00 42.11 ? 509 HOH   B O   1 
HETATM 7901 O O   . HOH   P 5 .   ? -25.865 0.884   -18.781 1.00 37.41 ? 510 HOH   B O   1 
HETATM 7902 O O   . HOH   P 5 .   ? -5.705  -3.706  -8.922  1.00 32.64 ? 511 HOH   B O   1 
HETATM 7903 O O   . HOH   P 5 .   ? -9.153  1.523   -21.761 1.00 53.90 ? 512 HOH   B O   1 
HETATM 7904 O O   . HOH   P 5 .   ? -27.923 13.196  -4.715  1.00 48.47 ? 513 HOH   B O   1 
HETATM 7905 O O   . HOH   P 5 .   ? -33.746 -4.272  5.487   1.00 38.98 ? 514 HOH   B O   1 
HETATM 7906 O O   . HOH   P 5 .   ? -21.542 -1.745  -21.998 1.00 42.35 ? 515 HOH   B O   1 
HETATM 7907 O O   . HOH   P 5 .   ? -28.708 -12.865 -3.003  1.00 48.74 ? 516 HOH   B O   1 
HETATM 7908 O O   . HOH   P 5 .   ? -18.935 1.747   -27.270 1.00 52.11 ? 517 HOH   B O   1 
HETATM 7909 O O   . HOH   P 5 .   ? -13.852 14.337  12.814  1.00 40.78 ? 518 HOH   B O   1 
HETATM 7910 O O   . HOH   P 5 .   ? -4.059  9.498   -10.177 1.00 47.95 ? 519 HOH   B O   1 
HETATM 7911 O O   . HOH   P 5 .   ? -13.025 10.921  -11.588 1.00 36.03 ? 520 HOH   B O   1 
HETATM 7912 O O   . HOH   P 5 .   ? -21.428 27.228  2.114   1.00 48.53 ? 521 HOH   B O   1 
HETATM 7913 O O   . HOH   P 5 .   ? -3.400  -0.640  -11.547 1.00 43.28 ? 522 HOH   B O   1 
HETATM 7914 O O   . HOH   P 5 .   ? -40.503 -2.908  1.514   1.00 59.40 ? 523 HOH   B O   1 
HETATM 7915 O O   . HOH   P 5 .   ? -34.447 6.177   -6.066  1.00 48.93 ? 524 HOH   B O   1 
HETATM 7916 O O   . HOH   P 5 .   ? -36.111 -3.436  -5.301  1.00 45.79 ? 525 HOH   B O   1 
HETATM 7917 O O   . HOH   P 5 .   ? -31.917 14.370  14.836  1.00 49.10 ? 526 HOH   B O   1 
HETATM 7918 O O   . HOH   P 5 .   ? -19.508 11.806  -21.628 1.00 47.65 ? 527 HOH   B O   1 
HETATM 7919 O O   . HOH   P 5 .   ? -17.149 17.415  -5.855  1.00 55.28 ? 528 HOH   B O   1 
HETATM 7920 O O   . HOH   P 5 .   ? -2.529  19.069  17.681  1.00 45.87 ? 529 HOH   B O   1 
HETATM 7921 O O   . HOH   P 5 .   ? -7.459  1.778   10.441  1.00 44.24 ? 530 HOH   B O   1 
HETATM 7922 O O   . HOH   P 5 .   ? -35.188 -2.626  9.636   1.00 33.45 ? 531 HOH   B O   1 
HETATM 7923 O O   . HOH   P 5 .   ? -32.068 21.426  20.621  1.00 59.47 ? 532 HOH   B O   1 
HETATM 7924 O O   . HOH   P 5 .   ? -29.470 -16.074 -9.076  1.00 57.70 ? 533 HOH   B O   1 
HETATM 7925 O O   . HOH   P 5 .   ? -22.856 11.480  -21.890 1.00 46.96 ? 534 HOH   B O   1 
HETATM 7926 O O   . HOH   P 5 .   ? 1.324   -10.268 -7.629  1.00 63.60 ? 535 HOH   B O   1 
HETATM 7927 O O   . HOH   P 5 .   ? -18.537 -16.764 -10.914 1.00 51.62 ? 536 HOH   B O   1 
HETATM 7928 O O   . HOH   P 5 .   ? -17.515 11.902  11.510  1.00 29.17 ? 537 HOH   B O   1 
HETATM 7929 O O   . HOH   P 5 .   ? -36.265 2.989   9.461   1.00 37.25 ? 538 HOH   B O   1 
HETATM 7930 O O   . HOH   P 5 .   ? -28.105 11.422  1.055   1.00 51.73 ? 539 HOH   B O   1 
HETATM 7931 O O   . HOH   P 5 .   ? -24.024 1.762   -20.604 1.00 47.69 ? 540 HOH   B O   1 
HETATM 7932 O O   . HOH   P 5 .   ? -13.543 22.049  12.798  1.00 57.57 ? 541 HOH   B O   1 
HETATM 7933 O O   . HOH   P 5 .   ? -21.660 -11.612 -20.465 1.00 49.78 ? 542 HOH   B O   1 
HETATM 7934 O O   . HOH   P 5 .   ? -40.068 -0.862  5.673   1.00 49.31 ? 543 HOH   B O   1 
HETATM 7935 O O   . HOH   P 5 .   ? -27.480 -13.198 -4.989  1.00 57.20 ? 544 HOH   B O   1 
HETATM 7936 O O   . HOH   P 5 .   ? -10.748 -21.097 -1.770  1.00 58.29 ? 545 HOH   B O   1 
HETATM 7937 O O   . HOH   P 5 .   ? -23.626 17.711  5.405   1.00 56.50 ? 546 HOH   B O   1 
HETATM 7938 O O   . HOH   P 5 .   ? -32.419 10.237  -0.363  1.00 62.37 ? 547 HOH   B O   1 
HETATM 7939 O O   . HOH   P 5 .   ? -10.689 31.616  1.874   1.00 36.72 ? 548 HOH   B O   1 
HETATM 7940 O O   . HOH   P 5 .   ? -3.345  25.369  4.172   1.00 53.58 ? 549 HOH   B O   1 
HETATM 7941 O O   . HOH   P 5 .   ? -22.343 14.765  -16.526 1.00 57.84 ? 550 HOH   B O   1 
HETATM 7942 O O   . HOH   P 5 .   ? -33.530 -1.104  -7.570  1.00 47.80 ? 551 HOH   B O   1 
HETATM 7943 O O   . HOH   P 5 .   ? 4.114   16.908  2.424   1.00 47.37 ? 552 HOH   B O   1 
HETATM 7944 O O   . HOH   P 5 .   ? -14.908 -6.587  -23.742 1.00 56.33 ? 553 HOH   B O   1 
HETATM 7945 O O   . HOH   P 5 .   ? -43.132 10.602  13.956  1.00 59.50 ? 554 HOH   B O   1 
HETATM 7946 O O   . HOH   P 5 .   ? -0.494  17.350  17.087  1.00 37.57 ? 555 HOH   B O   1 
HETATM 7947 O O   . HOH   P 5 .   ? -20.856 16.996  -2.024  1.00 44.62 ? 556 HOH   B O   1 
HETATM 7948 O O   . HOH   P 5 .   ? -27.858 12.286  -1.609  1.00 45.35 ? 557 HOH   B O   1 
HETATM 7949 O O   . HOH   P 5 .   ? -12.041 14.089  -8.503  1.00 45.89 ? 558 HOH   B O   1 
HETATM 7950 O O   . HOH   P 5 .   ? -19.549 -15.315 -19.138 1.00 54.82 ? 559 HOH   B O   1 
HETATM 7951 O O   . HOH   P 5 .   ? -12.962 -5.948  -21.972 1.00 58.30 ? 560 HOH   B O   1 
HETATM 7952 O O   . HOH   P 5 .   ? -19.849 8.690   -26.084 1.00 51.41 ? 561 HOH   B O   1 
HETATM 7953 O O   . HOH   P 5 .   ? -0.889  -0.864  -5.956  1.00 39.92 ? 562 HOH   B O   1 
HETATM 7954 O O   . HOH   P 5 .   ? -0.035  18.440  13.948  1.00 47.46 ? 563 HOH   B O   1 
HETATM 7955 O O   . HOH   P 5 .   ? -6.935  -7.397  -13.579 1.00 53.74 ? 564 HOH   B O   1 
HETATM 7956 O O   . HOH   P 5 .   ? -29.350 16.096  3.535   1.00 50.89 ? 565 HOH   B O   1 
HETATM 7957 O O   . HOH   P 5 .   ? -9.409  3.771   10.287  1.00 37.18 ? 566 HOH   B O   1 
HETATM 7958 O O   . HOH   P 5 .   ? -7.916  -17.869 -3.257  1.00 50.58 ? 567 HOH   B O   1 
HETATM 7959 O O   . HOH   P 5 .   ? -20.760 27.066  -4.594  1.00 41.65 ? 568 HOH   B O   1 
HETATM 7960 O O   . HOH   P 5 .   ? -10.244 10.455  -14.552 1.00 41.94 ? 569 HOH   B O   1 
HETATM 7961 O O   . HOH   P 5 .   ? -7.127  4.952   14.102  1.00 37.00 ? 570 HOH   B O   1 
HETATM 7962 O O   . HOH   P 5 .   ? -3.012  -2.959  -9.780  1.00 42.94 ? 571 HOH   B O   1 
HETATM 7963 O O   . HOH   P 5 .   ? -6.785  -18.006 -11.984 1.00 67.40 ? 572 HOH   B O   1 
HETATM 7964 O O   . HOH   P 5 .   ? -20.604 19.137  6.663   1.00 61.80 ? 573 HOH   B O   1 
HETATM 7965 O O   . HOH   P 5 .   ? -17.381 15.387  -27.648 1.00 57.80 ? 574 HOH   B O   1 
HETATM 7966 O O   . HOH   Q 5 .   ? -18.541 -11.453 42.836  1.00 51.83 ? 401 HOH   C O   1 
HETATM 7967 O O   . HOH   Q 5 .   ? 20.021  3.353   27.678  1.00 46.16 ? 402 HOH   C O   1 
HETATM 7968 O O   . HOH   Q 5 .   ? 6.151   3.560   36.375  1.00 47.50 ? 403 HOH   C O   1 
HETATM 7969 O O   . HOH   Q 5 .   ? 17.707  1.409   40.464  1.00 34.04 ? 404 HOH   C O   1 
HETATM 7970 O O   . HOH   Q 5 .   ? 6.377   -12.562 29.714  1.00 28.14 ? 405 HOH   C O   1 
HETATM 7971 O O   . HOH   Q 5 .   ? 0.166   0.266   21.656  1.00 50.27 ? 406 HOH   C O   1 
HETATM 7972 O O   . HOH   Q 5 .   ? -2.088  14.429  45.449  1.00 44.47 ? 407 HOH   C O   1 
HETATM 7973 O O   . HOH   Q 5 .   ? 12.078  11.766  40.287  1.00 55.26 ? 408 HOH   C O   1 
HETATM 7974 O O   . HOH   Q 5 .   ? -7.208  -10.386 42.097  1.00 39.94 ? 409 HOH   C O   1 
HETATM 7975 O O   . HOH   Q 5 .   ? 15.391  -6.578  48.421  1.00 54.72 ? 410 HOH   C O   1 
HETATM 7976 O O   . HOH   Q 5 .   ? 1.526   -18.157 32.943  1.00 48.93 ? 411 HOH   C O   1 
HETATM 7977 O O   . HOH   Q 5 .   ? 18.442  7.082   44.295  1.00 51.33 ? 412 HOH   C O   1 
HETATM 7978 O O   . HOH   Q 5 .   ? 6.383   2.077   38.744  1.00 24.78 ? 413 HOH   C O   1 
HETATM 7979 O O   . HOH   Q 5 .   ? 12.979  -7.127  39.672  1.00 38.05 ? 414 HOH   C O   1 
HETATM 7980 O O   . HOH   Q 5 .   ? -18.025 20.999  27.127  1.00 49.05 ? 415 HOH   C O   1 
HETATM 7981 O O   . HOH   Q 5 .   ? 18.900  2.345   38.081  1.00 32.46 ? 416 HOH   C O   1 
HETATM 7982 O O   . HOH   Q 5 .   ? -4.490  -11.398 34.893  1.00 27.37 ? 417 HOH   C O   1 
HETATM 7983 O O   . HOH   Q 5 .   ? -7.883  7.760   19.825  1.00 40.51 ? 418 HOH   C O   1 
HETATM 7984 O O   . HOH   Q 5 .   ? -2.709  4.231   27.184  1.00 38.94 ? 419 HOH   C O   1 
HETATM 7985 O O   . HOH   Q 5 .   ? 2.209   15.903  53.476  1.00 48.44 ? 420 HOH   C O   1 
HETATM 7986 O O   . HOH   Q 5 .   ? 4.839   4.850   33.027  1.00 43.66 ? 421 HOH   C O   1 
HETATM 7987 O O   . HOH   Q 5 .   ? -13.523 5.616   45.165  1.00 47.07 ? 422 HOH   C O   1 
HETATM 7988 O O   . HOH   Q 5 .   ? 5.484   8.061   59.491  1.00 43.32 ? 423 HOH   C O   1 
HETATM 7989 O O   . HOH   Q 5 .   ? -13.875 20.170  23.047  1.00 42.31 ? 424 HOH   C O   1 
HETATM 7990 O O   . HOH   Q 5 .   ? -6.990  -17.774 37.707  1.00 46.14 ? 425 HOH   C O   1 
HETATM 7991 O O   . HOH   Q 5 .   ? -6.618  -6.161  43.943  1.00 33.55 ? 426 HOH   C O   1 
HETATM 7992 O O   . HOH   Q 5 .   ? -12.100 17.697  37.815  1.00 40.13 ? 427 HOH   C O   1 
HETATM 7993 O O   . HOH   Q 5 .   ? -2.587  12.796  28.068  1.00 47.33 ? 428 HOH   C O   1 
HETATM 7994 O O   . HOH   Q 5 .   ? -5.182  8.258   22.247  1.00 26.18 ? 429 HOH   C O   1 
HETATM 7995 O O   . HOH   Q 5 .   ? 3.471   -11.681 25.858  1.00 28.05 ? 430 HOH   C O   1 
HETATM 7996 O O   . HOH   Q 5 .   ? -12.941 9.055   30.260  1.00 22.49 ? 431 HOH   C O   1 
HETATM 7997 O O   . HOH   Q 5 .   ? -1.250  15.044  17.866  1.00 25.45 ? 432 HOH   C O   1 
HETATM 7998 O O   . HOH   Q 5 .   ? 9.983   15.959  49.254  1.00 39.43 ? 433 HOH   C O   1 
HETATM 7999 O O   . HOH   Q 5 .   ? -7.286  12.921  33.358  1.00 32.27 ? 434 HOH   C O   1 
HETATM 8000 O O   . HOH   Q 5 .   ? -13.040 9.205   26.463  1.00 24.60 ? 435 HOH   C O   1 
HETATM 8001 O O   . HOH   Q 5 .   ? -16.670 -5.816  37.390  1.00 31.23 ? 436 HOH   C O   1 
HETATM 8002 O O   . HOH   Q 5 .   ? 2.351   10.888  41.041  1.00 34.88 ? 437 HOH   C O   1 
HETATM 8003 O O   . HOH   Q 5 .   ? -1.436  -11.404 50.073  1.00 41.98 ? 438 HOH   C O   1 
HETATM 8004 O O   . HOH   Q 5 .   ? 1.045   16.765  45.567  1.00 48.38 ? 439 HOH   C O   1 
HETATM 8005 O O   . HOH   Q 5 .   ? -8.033  14.960  21.251  1.00 41.55 ? 440 HOH   C O   1 
HETATM 8006 O O   . HOH   Q 5 .   ? -17.139 18.486  15.527  1.00 45.46 ? 441 HOH   C O   1 
HETATM 8007 O O   . HOH   Q 5 .   ? 2.914   -12.890 28.536  1.00 31.03 ? 442 HOH   C O   1 
HETATM 8008 O O   . HOH   Q 5 .   ? 2.323   -5.003  34.710  1.00 29.12 ? 443 HOH   C O   1 
HETATM 8009 O O   . HOH   Q 5 .   ? 17.902  -3.377  33.085  1.00 57.13 ? 444 HOH   C O   1 
HETATM 8010 O O   . HOH   Q 5 .   ? -8.662  15.040  30.436  1.00 30.20 ? 445 HOH   C O   1 
HETATM 8011 O O   . HOH   Q 5 .   ? -7.029  -3.869  26.561  1.00 38.55 ? 446 HOH   C O   1 
HETATM 8012 O O   . HOH   Q 5 .   ? 18.310  4.173   48.880  1.00 41.58 ? 447 HOH   C O   1 
HETATM 8013 O O   . HOH   Q 5 .   ? -16.741 -8.292  40.867  1.00 36.29 ? 448 HOH   C O   1 
HETATM 8014 O O   . HOH   Q 5 .   ? -5.917  -13.073 43.726  1.00 46.09 ? 449 HOH   C O   1 
HETATM 8015 O O   . HOH   Q 5 .   ? 1.817   -3.040  60.362  1.00 48.73 ? 450 HOH   C O   1 
HETATM 8016 O O   . HOH   Q 5 .   ? 7.231   10.050  45.032  1.00 41.44 ? 451 HOH   C O   1 
HETATM 8017 O O   . HOH   Q 5 .   ? 10.017  -5.877  59.506  1.00 43.67 ? 452 HOH   C O   1 
HETATM 8018 O O   . HOH   Q 5 .   ? -13.807 3.721   43.342  1.00 43.64 ? 453 HOH   C O   1 
HETATM 8019 O O   . HOH   Q 5 .   ? -5.589  12.973  48.191  1.00 45.62 ? 454 HOH   C O   1 
HETATM 8020 O O   . HOH   Q 5 .   ? 3.666   5.017   34.993  1.00 50.29 ? 455 HOH   C O   1 
HETATM 8021 O O   . HOH   Q 5 .   ? -13.284 4.656   23.772  1.00 44.83 ? 456 HOH   C O   1 
HETATM 8022 O O   . HOH   Q 5 .   ? -8.894  -1.800  27.671  1.00 32.06 ? 457 HOH   C O   1 
HETATM 8023 O O   . HOH   Q 5 .   ? -10.344 6.962   22.851  1.00 42.50 ? 458 HOH   C O   1 
HETATM 8024 O O   . HOH   Q 5 .   ? 1.123   -11.286 49.342  1.00 36.14 ? 459 HOH   C O   1 
HETATM 8025 O O   . HOH   Q 5 .   ? -11.331 2.818   28.687  1.00 28.56 ? 460 HOH   C O   1 
HETATM 8026 O O   . HOH   Q 5 .   ? -2.889  13.564  48.263  1.00 49.70 ? 461 HOH   C O   1 
HETATM 8027 O O   . HOH   Q 5 .   ? 9.964   13.966  34.200  1.00 42.20 ? 462 HOH   C O   1 
HETATM 8028 O O   . HOH   Q 5 .   ? -15.623 -8.161  38.219  1.00 30.61 ? 463 HOH   C O   1 
HETATM 8029 O O   . HOH   Q 5 .   ? -1.754  14.664  23.222  1.00 41.22 ? 464 HOH   C O   1 
HETATM 8030 O O   . HOH   Q 5 .   ? -10.666 -1.016  46.605  1.00 38.57 ? 465 HOH   C O   1 
HETATM 8031 O O   . HOH   Q 5 .   ? 9.486   12.171  24.692  1.00 26.07 ? 466 HOH   C O   1 
HETATM 8032 O O   . HOH   Q 5 .   ? -5.878  -4.345  38.696  1.00 30.59 ? 467 HOH   C O   1 
HETATM 8033 O O   . HOH   Q 5 .   ? 13.107  15.780  50.160  1.00 46.48 ? 468 HOH   C O   1 
HETATM 8034 O O   . HOH   Q 5 .   ? -0.174  3.988   28.258  1.00 37.55 ? 469 HOH   C O   1 
HETATM 8035 O O   . HOH   Q 5 .   ? 20.106  -5.469  39.422  1.00 45.71 ? 470 HOH   C O   1 
HETATM 8036 O O   . HOH   Q 5 .   ? -14.487 10.497  40.527  1.00 32.77 ? 471 HOH   C O   1 
HETATM 8037 O O   . HOH   Q 5 .   ? -3.105  12.885  59.877  1.00 48.45 ? 472 HOH   C O   1 
HETATM 8038 O O   . HOH   Q 5 .   ? 24.249  -0.551  37.038  1.00 51.05 ? 473 HOH   C O   1 
HETATM 8039 O O   . HOH   Q 5 .   ? -5.667  17.337  42.119  1.00 50.74 ? 474 HOH   C O   1 
HETATM 8040 O O   . HOH   Q 5 .   ? -13.370 -4.891  48.005  1.00 46.45 ? 475 HOH   C O   1 
HETATM 8041 O O   . HOH   Q 5 .   ? -16.713 21.960  35.460  1.00 52.40 ? 476 HOH   C O   1 
HETATM 8042 O O   . HOH   Q 5 .   ? -3.955  3.637   65.382  1.00 49.75 ? 477 HOH   C O   1 
HETATM 8043 O O   . HOH   Q 5 .   ? -6.989  5.807   24.785  1.00 39.57 ? 478 HOH   C O   1 
HETATM 8044 O O   A HOH   Q 5 .   ? -6.614  16.003  43.760  0.70 33.73 ? 479 HOH   C O   1 
HETATM 8045 O O   . HOH   Q 5 .   ? 23.549  8.694   24.122  1.00 42.06 ? 480 HOH   C O   1 
HETATM 8046 O O   . HOH   Q 5 .   ? 14.443  3.002   51.584  1.00 40.90 ? 481 HOH   C O   1 
HETATM 8047 O O   . HOH   Q 5 .   ? -14.954 13.033  41.491  1.00 52.27 ? 482 HOH   C O   1 
HETATM 8048 O O   . HOH   Q 5 .   ? -7.085  10.250  55.945  1.00 52.40 ? 483 HOH   C O   1 
HETATM 8049 O O   . HOH   Q 5 .   ? 16.898  1.324   45.781  1.00 44.32 ? 484 HOH   C O   1 
HETATM 8050 O O   . HOH   Q 5 .   ? 2.642   -17.387 49.427  1.00 59.76 ? 485 HOH   C O   1 
HETATM 8051 O O   . HOH   Q 5 .   ? 16.232  16.546  23.335  1.00 56.50 ? 486 HOH   C O   1 
HETATM 8052 O O   . HOH   Q 5 .   ? 5.385   4.899   62.182  1.00 38.72 ? 487 HOH   C O   1 
HETATM 8053 O O   . HOH   Q 5 .   ? 4.379   -7.689  59.531  1.00 48.02 ? 488 HOH   C O   1 
HETATM 8054 O O   . HOH   Q 5 .   ? 17.977  17.961  28.610  1.00 58.53 ? 489 HOH   C O   1 
HETATM 8055 O O   . HOH   Q 5 .   ? 23.593  6.889   30.029  1.00 53.04 ? 490 HOH   C O   1 
HETATM 8056 O O   . HOH   Q 5 .   ? -9.339  -13.321 40.271  1.00 51.83 ? 491 HOH   C O   1 
HETATM 8057 O O   . HOH   Q 5 .   ? 3.203   5.268   64.167  1.00 61.76 ? 492 HOH   C O   1 
HETATM 8058 O O   . HOH   Q 5 .   ? 1.938   12.654  24.859  1.00 33.60 ? 493 HOH   C O   1 
HETATM 8059 O O   . HOH   Q 5 .   ? 5.252   2.101   60.447  1.00 52.19 ? 494 HOH   C O   1 
HETATM 8060 O O   . HOH   Q 5 .   ? 5.011   17.354  36.686  1.00 59.07 ? 495 HOH   C O   1 
HETATM 8061 O O   . HOH   Q 5 .   ? -1.609  -13.048 52.690  1.00 55.10 ? 496 HOH   C O   1 
HETATM 8062 O O   . HOH   Q 5 .   ? 7.888   18.649  30.061  1.00 56.08 ? 497 HOH   C O   1 
HETATM 8063 O O   . HOH   Q 5 .   ? 1.208   13.534  30.578  1.00 59.70 ? 498 HOH   C O   1 
HETATM 8064 O O   . HOH   Q 5 .   ? -15.283 17.578  18.688  1.00 34.28 ? 499 HOH   C O   1 
HETATM 8065 O O   . HOH   Q 5 .   ? 13.480  3.451   55.044  1.00 48.50 ? 500 HOH   C O   1 
HETATM 8066 O O   . HOH   Q 5 .   ? -6.227  4.442   26.644  1.00 39.08 ? 501 HOH   C O   1 
HETATM 8067 O O   . HOH   Q 5 .   ? -9.734  0.937   57.791  1.00 59.04 ? 502 HOH   C O   1 
HETATM 8068 O O   . HOH   Q 5 .   ? -5.159  -19.207 41.969  1.00 69.64 ? 503 HOH   C O   1 
HETATM 8069 O O   . HOH   Q 5 .   ? -15.030 1.403   43.782  1.00 43.09 ? 504 HOH   C O   1 
HETATM 8070 O O   . HOH   Q 5 .   ? 12.857  17.409  32.290  1.00 47.55 ? 505 HOH   C O   1 
HETATM 8071 O O   . HOH   Q 5 .   ? -11.235 27.568  33.231  1.00 54.00 ? 506 HOH   C O   1 
HETATM 8072 O O   . HOH   Q 5 .   ? -7.455  19.346  40.611  1.00 47.76 ? 507 HOH   C O   1 
HETATM 8073 O O   . HOH   Q 5 .   ? 5.869   -0.854  60.242  1.00 54.84 ? 508 HOH   C O   1 
HETATM 8074 O O   . HOH   Q 5 .   ? -9.713  -4.222  51.508  1.00 48.54 ? 509 HOH   C O   1 
HETATM 8075 O O   . HOH   Q 5 .   ? 2.893   15.001  32.904  1.00 63.63 ? 510 HOH   C O   1 
HETATM 8076 O O   . HOH   Q 5 .   ? -8.589  5.480   22.963  1.00 38.90 ? 511 HOH   C O   1 
HETATM 8077 O O   . HOH   Q 5 .   ? 24.323  9.902   22.229  1.00 55.44 ? 512 HOH   C O   1 
HETATM 8078 O O   . HOH   Q 5 .   ? -0.251  16.163  29.075  1.00 57.25 ? 513 HOH   C O   1 
HETATM 8079 O O   . HOH   Q 5 .   ? -13.216 -0.293  47.554  1.00 46.18 ? 514 HOH   C O   1 
HETATM 8080 O O   . HOH   R 5 .   ? -45.696 2.561   28.375  1.00 43.29 ? 401 HOH   D O   1 
HETATM 8081 O O   . HOH   R 5 .   ? -44.867 7.970   25.318  1.00 49.75 ? 402 HOH   D O   1 
HETATM 8082 O O   . HOH   R 5 .   ? -33.840 -9.950  30.284  1.00 44.33 ? 403 HOH   D O   1 
HETATM 8083 O O   . HOH   R 5 .   ? -25.598 12.968  17.303  1.00 25.70 ? 404 HOH   D O   1 
HETATM 8084 O O   . HOH   R 5 .   ? -22.133 14.446  35.085  1.00 52.24 ? 405 HOH   D O   1 
HETATM 8085 O O   . HOH   R 5 .   ? -22.748 12.089  35.676  1.00 39.44 ? 406 HOH   D O   1 
HETATM 8086 O O   . HOH   R 5 .   ? -29.689 -2.433  23.712  1.00 30.11 ? 407 HOH   D O   1 
HETATM 8087 O O   . HOH   R 5 .   ? -12.277 -15.790 37.384  1.00 39.32 ? 408 HOH   D O   1 
HETATM 8088 O O   . HOH   R 5 .   ? -37.222 -10.598 23.257  1.00 37.20 ? 409 HOH   D O   1 
HETATM 8089 O O   B HOH   R 5 .   ? -16.003 -7.313  13.949  0.50 19.74 ? 410 HOH   D O   1 
HETATM 8090 O O   . HOH   R 5 .   ? -41.375 -0.874  19.120  1.00 33.57 ? 411 HOH   D O   1 
HETATM 8091 O O   . HOH   R 5 .   ? -14.853 -13.663 29.579  1.00 30.04 ? 412 HOH   D O   1 
HETATM 8092 O O   . HOH   R 5 .   ? -13.104 -15.173 15.284  1.00 27.70 ? 413 HOH   D O   1 
HETATM 8093 O O   . HOH   R 5 .   ? -32.634 -13.808 28.275  1.00 53.54 ? 414 HOH   D O   1 
HETATM 8094 O O   . HOH   R 5 .   ? -31.040 -12.304 23.538  1.00 48.16 ? 415 HOH   D O   1 
HETATM 8095 O O   . HOH   R 5 .   ? -23.269 0.384   45.169  1.00 52.64 ? 416 HOH   D O   1 
HETATM 8096 O O   . HOH   R 5 .   ? -38.204 11.667  22.856  1.00 44.88 ? 417 HOH   D O   1 
HETATM 8097 O O   . HOH   R 5 .   ? -8.006  -13.886 19.546  1.00 33.78 ? 418 HOH   D O   1 
HETATM 8098 O O   . HOH   R 5 .   ? -27.599 8.993   39.468  1.00 45.69 ? 419 HOH   D O   1 
HETATM 8099 O O   . HOH   R 5 .   ? -19.286 -12.342 12.725  1.00 24.39 ? 420 HOH   D O   1 
HETATM 8100 O O   . HOH   R 5 .   ? -40.518 -1.389  16.771  1.00 37.02 ? 421 HOH   D O   1 
HETATM 8101 O O   . HOH   R 5 .   ? -8.892  -8.168  15.712  1.00 29.48 ? 422 HOH   D O   1 
HETATM 8102 O O   . HOH   R 5 .   ? -20.252 12.833  28.300  1.00 22.35 ? 423 HOH   D O   1 
HETATM 8103 O O   . HOH   R 5 .   ? -23.623 19.269  22.442  1.00 45.90 ? 424 HOH   D O   1 
HETATM 8104 O O   . HOH   R 5 .   ? -16.762 -15.561 37.513  1.00 41.25 ? 425 HOH   D O   1 
HETATM 8105 O O   . HOH   R 5 .   ? -24.688 8.213   36.819  1.00 35.78 ? 426 HOH   D O   1 
HETATM 8106 O O   . HOH   R 5 .   ? -30.235 -9.494  30.485  1.00 30.70 ? 427 HOH   D O   1 
HETATM 8107 O O   . HOH   R 5 .   ? -10.153 -5.418  20.379  1.00 49.66 ? 428 HOH   D O   1 
HETATM 8108 O O   . HOH   R 5 .   ? -31.492 -0.742  25.172  1.00 25.87 ? 429 HOH   D O   1 
HETATM 8109 O O   . HOH   R 5 .   ? -20.177 -13.163 41.485  1.00 51.78 ? 430 HOH   D O   1 
HETATM 8110 O O   . HOH   R 5 .   ? -6.722  -19.365 27.254  1.00 43.56 ? 431 HOH   D O   1 
HETATM 8111 O O   . HOH   R 5 .   ? -8.771  -6.434  24.242  1.00 41.04 ? 432 HOH   D O   1 
HETATM 8112 O O   . HOH   R 5 .   ? -36.363 3.498   13.138  1.00 37.20 ? 433 HOH   D O   1 
HETATM 8113 O O   . HOH   R 5 .   ? -18.242 18.266  23.712  1.00 38.51 ? 434 HOH   D O   1 
HETATM 8114 O O   . HOH   R 5 .   ? -27.341 -8.056  41.207  1.00 39.00 ? 435 HOH   D O   1 
HETATM 8115 O O   . HOH   R 5 .   ? -32.544 13.962  37.693  1.00 38.30 ? 436 HOH   D O   1 
HETATM 8116 O O   . HOH   R 5 .   ? -33.735 -17.213 8.915   1.00 56.85 ? 437 HOH   D O   1 
HETATM 8117 O O   . HOH   R 5 .   ? -8.841  -8.307  28.671  1.00 25.87 ? 438 HOH   D O   1 
HETATM 8118 O O   . HOH   R 5 .   ? -34.996 -4.291  8.060   1.00 41.37 ? 439 HOH   D O   1 
HETATM 8119 O O   . HOH   R 5 .   ? -17.100 -3.478  22.570  1.00 30.96 ? 440 HOH   D O   1 
HETATM 8120 O O   . HOH   R 5 .   ? -12.344 -7.873  20.458  1.00 25.51 ? 441 HOH   D O   1 
HETATM 8121 O O   . HOH   R 5 .   ? -18.155 -11.985 23.742  1.00 37.87 ? 442 HOH   D O   1 
HETATM 8122 O O   . HOH   R 5 .   ? -19.748 19.424  31.341  1.00 43.92 ? 443 HOH   D O   1 
HETATM 8123 O O   . HOH   R 5 .   ? -12.541 7.667   38.249  1.00 28.23 ? 444 HOH   D O   1 
HETATM 8124 O O   . HOH   R 5 .   ? -29.742 -12.336 37.212  1.00 40.54 ? 445 HOH   D O   1 
HETATM 8125 O O   . HOH   R 5 .   ? -12.544 2.763   26.250  1.00 27.75 ? 446 HOH   D O   1 
HETATM 8126 O O   . HOH   R 5 .   ? 1.133   -18.533 23.066  1.00 44.67 ? 447 HOH   D O   1 
HETATM 8127 O O   . HOH   R 5 .   ? -24.927 14.868  35.900  1.00 41.23 ? 448 HOH   D O   1 
HETATM 8128 O O   . HOH   R 5 .   ? -17.858 -11.550 30.705  1.00 35.81 ? 449 HOH   D O   1 
HETATM 8129 O O   . HOH   R 5 .   ? -22.614 -31.409 26.234  1.00 53.21 ? 450 HOH   D O   1 
HETATM 8130 O O   . HOH   R 5 .   ? -18.871 -1.431  41.733  1.00 38.70 ? 451 HOH   D O   1 
HETATM 8131 O O   . HOH   R 5 .   ? -24.842 5.963   41.845  1.00 36.76 ? 452 HOH   D O   1 
HETATM 8132 O O   . HOH   R 5 .   ? -28.216 -10.370 41.180  1.00 47.92 ? 453 HOH   D O   1 
HETATM 8133 O O   . HOH   R 5 .   ? -25.669 -11.993 13.559  1.00 24.68 ? 454 HOH   D O   1 
HETATM 8134 O O   . HOH   R 5 .   ? -11.353 -1.611  29.021  1.00 28.63 ? 455 HOH   D O   1 
HETATM 8135 O O   . HOH   R 5 .   ? -31.750 -13.215 20.881  1.00 35.19 ? 456 HOH   D O   1 
HETATM 8136 O O   . HOH   R 5 .   ? -41.758 0.377   9.827   1.00 33.22 ? 457 HOH   D O   1 
HETATM 8137 O O   . HOH   R 5 .   ? -33.226 14.608  45.860  1.00 60.86 ? 458 HOH   D O   1 
HETATM 8138 O O   . HOH   R 5 .   ? -43.552 -2.249  21.697  1.00 42.44 ? 459 HOH   D O   1 
HETATM 8139 O O   . HOH   R 5 .   ? -12.515 -5.333  23.479  1.00 39.87 ? 460 HOH   D O   1 
HETATM 8140 O O   . HOH   R 5 .   ? -9.926  -14.713 22.091  1.00 32.96 ? 461 HOH   D O   1 
HETATM 8141 O O   . HOH   R 5 .   ? -22.089 13.282  18.509  1.00 29.57 ? 462 HOH   D O   1 
HETATM 8142 O O   . HOH   R 5 .   ? -34.637 20.205  33.556  1.00 65.49 ? 463 HOH   D O   1 
HETATM 8143 O O   . HOH   R 5 .   ? -42.823 1.600   24.530  1.00 43.44 ? 464 HOH   D O   1 
HETATM 8144 O O   . HOH   R 5 .   ? -14.501 -22.167 19.228  1.00 60.00 ? 465 HOH   D O   1 
HETATM 8145 O O   . HOH   R 5 .   ? -43.769 0.026   22.809  1.00 41.70 ? 466 HOH   D O   1 
HETATM 8146 O O   . HOH   R 5 .   ? -44.311 -6.561  21.769  1.00 44.31 ? 467 HOH   D O   1 
HETATM 8147 O O   . HOH   R 5 .   ? -25.570 6.130   24.362  1.00 27.27 ? 468 HOH   D O   1 
HETATM 8148 O O   . HOH   R 5 .   ? -8.594  -7.436  20.238  1.00 46.56 ? 469 HOH   D O   1 
HETATM 8149 O O   . HOH   R 5 .   ? -13.685 10.144  37.955  1.00 32.43 ? 470 HOH   D O   1 
HETATM 8150 O O   . HOH   R 5 .   ? -36.405 -8.458  29.969  1.00 35.86 ? 471 HOH   D O   1 
HETATM 8151 O O   . HOH   R 5 .   ? -19.760 -3.539  21.672  1.00 41.54 ? 472 HOH   D O   1 
HETATM 8152 O O   . HOH   R 5 .   ? -22.655 7.573   43.787  1.00 45.40 ? 473 HOH   D O   1 
HETATM 8153 O O   . HOH   R 5 .   ? -36.993 8.202   20.663  1.00 32.61 ? 474 HOH   D O   1 
HETATM 8154 O O   . HOH   R 5 .   ? -44.149 7.855   22.727  1.00 43.68 ? 475 HOH   D O   1 
HETATM 8155 O O   . HOH   R 5 .   ? -11.361 -7.709  31.706  1.00 24.07 ? 476 HOH   D O   1 
HETATM 8156 O O   . HOH   R 5 .   ? -39.611 -9.005  14.414  1.00 48.22 ? 477 HOH   D O   1 
HETATM 8157 O O   . HOH   R 5 .   ? -32.526 -14.944 34.986  1.00 51.31 ? 478 HOH   D O   1 
HETATM 8158 O O   . HOH   R 5 .   ? -41.182 -14.521 32.190  1.00 45.46 ? 479 HOH   D O   1 
HETATM 8159 O O   . HOH   R 5 .   ? -44.000 -14.276 30.641  1.00 42.69 ? 480 HOH   D O   1 
HETATM 8160 O O   . HOH   R 5 .   ? -34.167 13.632  35.546  1.00 37.31 ? 481 HOH   D O   1 
HETATM 8161 O O   . HOH   R 5 .   ? -28.689 -14.954 7.198   1.00 43.29 ? 482 HOH   D O   1 
HETATM 8162 O O   . HOH   R 5 .   ? -21.888 5.982   32.578  1.00 26.02 ? 483 HOH   D O   1 
HETATM 8163 O O   . HOH   R 5 .   ? -32.685 -4.025  47.027  1.00 46.22 ? 484 HOH   D O   1 
HETATM 8164 O O   . HOH   R 5 .   ? -45.296 -1.996  37.062  1.00 45.16 ? 485 HOH   D O   1 
HETATM 8165 O O   . HOH   R 5 .   ? -27.017 -3.776  24.335  1.00 37.04 ? 486 HOH   D O   1 
HETATM 8166 O O   . HOH   R 5 .   ? -26.490 -7.747  43.757  1.00 44.79 ? 487 HOH   D O   1 
HETATM 8167 O O   . HOH   R 5 .   ? -3.781  -19.177 22.834  1.00 46.33 ? 488 HOH   D O   1 
HETATM 8168 O O   . HOH   R 5 .   ? -42.056 6.798   15.937  1.00 36.36 ? 489 HOH   D O   1 
HETATM 8169 O O   . HOH   R 5 .   ? -19.311 15.175  35.459  1.00 49.97 ? 490 HOH   D O   1 
HETATM 8170 O O   . HOH   R 5 .   ? -23.573 3.458   41.798  1.00 33.00 ? 491 HOH   D O   1 
HETATM 8171 O O   . HOH   R 5 .   ? -35.534 -10.127 19.172  1.00 50.22 ? 492 HOH   D O   1 
HETATM 8172 O O   . HOH   R 5 .   ? -29.802 -15.246 22.422  1.00 51.22 ? 493 HOH   D O   1 
HETATM 8173 O O   . HOH   R 5 .   ? -32.752 18.812  28.306  1.00 57.20 ? 494 HOH   D O   1 
HETATM 8174 O O   . HOH   R 5 .   ? -13.595 -14.476 38.894  1.00 48.87 ? 495 HOH   D O   1 
HETATM 8175 O O   . HOH   R 5 .   ? -19.692 -12.170 18.772  1.00 32.22 ? 496 HOH   D O   1 
HETATM 8176 O O   . HOH   R 5 .   ? -28.378 -17.916 20.332  1.00 61.29 ? 497 HOH   D O   1 
HETATM 8177 O O   . HOH   R 5 .   ? -19.124 -6.980  44.748  1.00 51.36 ? 498 HOH   D O   1 
HETATM 8178 O O   . HOH   R 5 .   ? -33.350 -7.811  46.377  1.00 53.81 ? 499 HOH   D O   1 
HETATM 8179 O O   . HOH   R 5 .   ? -39.758 5.180   5.841   1.00 50.59 ? 500 HOH   D O   1 
HETATM 8180 O O   . HOH   R 5 .   ? -22.508 -10.067 43.858  1.00 54.53 ? 501 HOH   D O   1 
HETATM 8181 O O   . HOH   R 5 .   ? -44.493 -0.468  13.116  1.00 52.03 ? 502 HOH   D O   1 
HETATM 8182 O O   . HOH   R 5 .   ? -47.392 -11.585 33.603  1.00 50.92 ? 503 HOH   D O   1 
HETATM 8183 O O   . HOH   R 5 .   ? -20.588 -17.978 36.758  1.00 49.21 ? 504 HOH   D O   1 
HETATM 8184 O O   . HOH   R 5 .   ? -44.644 4.257   41.328  1.00 50.96 ? 505 HOH   D O   1 
HETATM 8185 O O   . HOH   R 5 .   ? -18.993 2.449   43.578  1.00 54.61 ? 506 HOH   D O   1 
HETATM 8186 O O   . HOH   R 5 .   ? -24.658 -0.838  48.389  1.00 65.66 ? 507 HOH   D O   1 
HETATM 8187 O O   . HOH   R 5 .   ? -29.558 -16.065 5.136   1.00 64.54 ? 508 HOH   D O   1 
HETATM 8188 O O   . HOH   R 5 .   ? -2.681  -17.240 24.738  1.00 39.87 ? 509 HOH   D O   1 
HETATM 8189 O O   . HOH   R 5 .   ? -43.379 11.050  41.373  1.00 54.12 ? 510 HOH   D O   1 
HETATM 8190 O O   . HOH   R 5 .   ? -17.878 0.775   42.367  1.00 43.54 ? 511 HOH   D O   1 
HETATM 8191 O O   . HOH   R 5 .   ? -18.005 -28.210 21.495  1.00 60.39 ? 512 HOH   D O   1 
HETATM 8192 O O   . HOH   R 5 .   ? -30.458 2.222   49.965  1.00 57.31 ? 513 HOH   D O   1 
HETATM 8193 O O   . HOH   R 5 .   ? -44.188 -2.024  18.882  1.00 48.51 ? 514 HOH   D O   1 
HETATM 8194 O O   . HOH   R 5 .   ? -14.250 -3.725  24.503  1.00 35.95 ? 515 HOH   D O   1 
HETATM 8195 O O   . HOH   R 5 .   ? -22.223 2.623   44.232  1.00 44.53 ? 516 HOH   D O   1 
HETATM 8196 O O   . HOH   R 5 .   ? -21.763 5.975   45.242  1.00 66.26 ? 517 HOH   D O   1 
HETATM 8197 O O   . HOH   R 5 .   ? -46.225 0.869   30.554  1.00 50.53 ? 518 HOH   D O   1 
HETATM 8198 O O   . HOH   R 5 .   ? -10.010 -5.126  22.902  1.00 39.11 ? 519 HOH   D O   1 
HETATM 8199 O O   . HOH   R 5 .   ? -27.334 7.640   45.526  1.00 63.83 ? 520 HOH   D O   1 
HETATM 8200 O O   . HOH   R 5 .   ? -36.204 9.952   19.039  1.00 41.99 ? 521 HOH   D O   1 
HETATM 8201 O O   . HOH   R 5 .   ? -37.553 6.077   47.328  1.00 47.97 ? 522 HOH   D O   1 
HETATM 8202 O O   . HOH   R 5 .   ? -22.181 -18.661 20.178  1.00 60.17 ? 523 HOH   D O   1 
HETATM 8203 O O   . HOH   R 5 .   ? -8.288  -25.663 31.609  1.00 63.11 ? 524 HOH   D O   1 
HETATM 8204 O O   . HOH   R 5 .   ? -45.356 -4.388  38.512  1.00 52.09 ? 525 HOH   D O   1 
HETATM 8205 O O   . HOH   R 5 .   ? -16.340 10.129  46.600  1.00 60.23 ? 526 HOH   D O   1 
HETATM 8206 O O   . HOH   R 5 .   ? -14.546 -1.779  21.488  1.00 48.91 ? 527 HOH   D O   1 
HETATM 8207 O O   . HOH   R 5 .   ? -24.651 -19.587 20.546  1.00 52.62 ? 528 HOH   D O   1 
# 
