data_9JHZ
# 
_entry.id   9JHZ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   9JHZ         pdb_00009jhz 10.2210/pdb9jhz/pdb 
WWPDB D_1300051384 ?            ?                   
# 
_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       2024-11-13 
# 
_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                        9JHZ 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              chahong@korea.ac.kr 
_pdbx_contact_author.name_first         Hwang 
_pdbx_contact_author.name_last          'Kwang Yeon' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2076-5030 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yang, J.W.'  1 ? 
'Jeon, H.J.'  2 ? 
'Park, S.H.'  3 ? 
'Kim, S.H.'   4 ? 
'Hwang, K.Y.' 5 ? 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? CH ? ? primary 'Int J Mol Sci' ? ? 1422-0067 ? ? 25 ? ? ? 
'Structural Insights and Catalytic Mechanism of 3-Hydroxybutyryl-CoA Dehydrogenase from Faecalibacterium Prausnitzii A2-165.' 2024 
? 10.3390/ijms251910711     39409040 ? ? 
? ? ? ? ? ? ? CH ? ? 1       'Int J Mol Sci' ? ? 1422-0067 ? ? 25 ? ? ? 
'Structural Insights and Catalytic Mechanism of 3-Hydroxybutyryl-CoA Dehydrogenase from'                                      2024 
? 10.1107/S0907444904019158 39409040 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yang, J.'     1  ?                   
primary 'Jeon, H.J.'   2  ?                   
primary 'Park, S.'     3  0009-0002-1786-0448 
primary 'Park, J.'     4  ?                   
primary 'Jang, S.'     5  ?                   
primary 'Shin, B.'     6  ?                   
primary 'Bang, K.'     7  ?                   
primary 'Hawkes, H.K.' 8  ?                   
primary 'Park, S.'     9  ?                   
primary 'Kim, S.'      10 0000-0002-8303-1376 
primary 'Hwang, K.Y.'  11 0000-0002-2076-5030 
1       'Yang, J.'     12 ?                   
1       'Jeon, H.J.'   13 ?                   
1       'Park, S.'     14 0009-0002-1786-0448 
1       'Park, J.'     15 ?                   
1       'Jang, S.'     16 ?                   
1       'Shin, B.'     17 ?                   
1       'Bang, K.'     18 ?                   
1       'Hawkes, H.K.' 19 ?                   
1       'Park, S.'     20 ?                   
1       'Kim, S.'      21 0000-0002-8303-1376 
1       'Hwang, K.Y.'  22 0000-0002-2076-5030 
# 
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 '3-hydroxyacyl-CoA dehydrogenase, NAD binding domain protein' 31201.486 3   ? S117A ? ? 
2 non-polymer syn 'ACETOACETYL-COENZYME A'                                      851.607   1   ? ?     ? ? 
3 non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE                             663.425   1   ? ?     ? ? 
4 water       nat water                                                         18.015    241 ? ?     ? ? 
# 
_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       
;AMKIGVIGAGTMGQGIAKAFAQVEGNTVALCDIKQEWAENGLAKIKKGYEKLVAKGKIPQEKADAIVAAITPGLKENLCA
DCDLIVEAAFEDMKVKQTTFGELDKICKPECIFASNTASLSITEIGKGLSRPLVGMHFFNPADRMKLIEVIAGCNTPAET
VEKIKEISVAIGKNPVQVNEAAGFVVNRILIPMINEAAFIKMEGVSDIAGIDTAMKLGANHPMGPLELGDFIGLDICLAI
MDVLYHETGDSKYRACPLIRKMVRGGNLGCKTGKGFYVYNADRTKTPVDQL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AMKIGVIGAGTMGQGIAKAFAQVEGNTVALCDIKQEWAENGLAKIKKGYEKLVAKGKIPQEKADAIVAAITPGLKENLCA
DCDLIVEAAFEDMKVKQTTFGELDKICKPECIFASNTASLSITEIGKGLSRPLVGMHFFNPADRMKLIEVIAGCNTPAET
VEKIKEISVAIGKNPVQVNEAAGFVVNRILIPMINEAAFIKMEGVSDIAGIDTAMKLGANHPMGPLELGDFIGLDICLAI
MDVLYHETGDSKYRACPLIRKMVRGGNLGCKTGKGFYVYNADRTKTPVDQL
;
_entity_poly.pdbx_strand_id                 C,A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ACETOACETYL-COENZYME A'          CAA 
3 NICOTINAMIDE-ADENINE-DINUCLEOTIDE NAD 
4 water                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   MET n 
1 3   LYS n 
1 4   ILE n 
1 5   GLY n 
1 6   VAL n 
1 7   ILE n 
1 8   GLY n 
1 9   ALA n 
1 10  GLY n 
1 11  THR n 
1 12  MET n 
1 13  GLY n 
1 14  GLN n 
1 15  GLY n 
1 16  ILE n 
1 17  ALA n 
1 18  LYS n 
1 19  ALA n 
1 20  PHE n 
1 21  ALA n 
1 22  GLN n 
1 23  VAL n 
1 24  GLU n 
1 25  GLY n 
1 26  ASN n 
1 27  THR n 
1 28  VAL n 
1 29  ALA n 
1 30  LEU n 
1 31  CYS n 
1 32  ASP n 
1 33  ILE n 
1 34  LYS n 
1 35  GLN n 
1 36  GLU n 
1 37  TRP n 
1 38  ALA n 
1 39  GLU n 
1 40  ASN n 
1 41  GLY n 
1 42  LEU n 
1 43  ALA n 
1 44  LYS n 
1 45  ILE n 
1 46  LYS n 
1 47  LYS n 
1 48  GLY n 
1 49  TYR n 
1 50  GLU n 
1 51  LYS n 
1 52  LEU n 
1 53  VAL n 
1 54  ALA n 
1 55  LYS n 
1 56  GLY n 
1 57  LYS n 
1 58  ILE n 
1 59  PRO n 
1 60  GLN n 
1 61  GLU n 
1 62  LYS n 
1 63  ALA n 
1 64  ASP n 
1 65  ALA n 
1 66  ILE n 
1 67  VAL n 
1 68  ALA n 
1 69  ALA n 
1 70  ILE n 
1 71  THR n 
1 72  PRO n 
1 73  GLY n 
1 74  LEU n 
1 75  LYS n 
1 76  GLU n 
1 77  ASN n 
1 78  LEU n 
1 79  CYS n 
1 80  ALA n 
1 81  ASP n 
1 82  CYS n 
1 83  ASP n 
1 84  LEU n 
1 85  ILE n 
1 86  VAL n 
1 87  GLU n 
1 88  ALA n 
1 89  ALA n 
1 90  PHE n 
1 91  GLU n 
1 92  ASP n 
1 93  MET n 
1 94  LYS n 
1 95  VAL n 
1 96  LYS n 
1 97  GLN n 
1 98  THR n 
1 99  THR n 
1 100 PHE n 
1 101 GLY n 
1 102 GLU n 
1 103 LEU n 
1 104 ASP n 
1 105 LYS n 
1 106 ILE n 
1 107 CYS n 
1 108 LYS n 
1 109 PRO n 
1 110 GLU n 
1 111 CYS n 
1 112 ILE n 
1 113 PHE n 
1 114 ALA n 
1 115 SER n 
1 116 ASN n 
1 117 THR n 
1 118 ALA n 
1 119 SER n 
1 120 LEU n 
1 121 SER n 
1 122 ILE n 
1 123 THR n 
1 124 GLU n 
1 125 ILE n 
1 126 GLY n 
1 127 LYS n 
1 128 GLY n 
1 129 LEU n 
1 130 SER n 
1 131 ARG n 
1 132 PRO n 
1 133 LEU n 
1 134 VAL n 
1 135 GLY n 
1 136 MET n 
1 137 HIS n 
1 138 PHE n 
1 139 PHE n 
1 140 ASN n 
1 141 PRO n 
1 142 ALA n 
1 143 ASP n 
1 144 ARG n 
1 145 MET n 
1 146 LYS n 
1 147 LEU n 
1 148 ILE n 
1 149 GLU n 
1 150 VAL n 
1 151 ILE n 
1 152 ALA n 
1 153 GLY n 
1 154 CYS n 
1 155 ASN n 
1 156 THR n 
1 157 PRO n 
1 158 ALA n 
1 159 GLU n 
1 160 THR n 
1 161 VAL n 
1 162 GLU n 
1 163 LYS n 
1 164 ILE n 
1 165 LYS n 
1 166 GLU n 
1 167 ILE n 
1 168 SER n 
1 169 VAL n 
1 170 ALA n 
1 171 ILE n 
1 172 GLY n 
1 173 LYS n 
1 174 ASN n 
1 175 PRO n 
1 176 VAL n 
1 177 GLN n 
1 178 VAL n 
1 179 ASN n 
1 180 GLU n 
1 181 ALA n 
1 182 ALA n 
1 183 GLY n 
1 184 PHE n 
1 185 VAL n 
1 186 VAL n 
1 187 ASN n 
1 188 ARG n 
1 189 ILE n 
1 190 LEU n 
1 191 ILE n 
1 192 PRO n 
1 193 MET n 
1 194 ILE n 
1 195 ASN n 
1 196 GLU n 
1 197 ALA n 
1 198 ALA n 
1 199 PHE n 
1 200 ILE n 
1 201 LYS n 
1 202 MET n 
1 203 GLU n 
1 204 GLY n 
1 205 VAL n 
1 206 SER n 
1 207 ASP n 
1 208 ILE n 
1 209 ALA n 
1 210 GLY n 
1 211 ILE n 
1 212 ASP n 
1 213 THR n 
1 214 ALA n 
1 215 MET n 
1 216 LYS n 
1 217 LEU n 
1 218 GLY n 
1 219 ALA n 
1 220 ASN n 
1 221 HIS n 
1 222 PRO n 
1 223 MET n 
1 224 GLY n 
1 225 PRO n 
1 226 LEU n 
1 227 GLU n 
1 228 LEU n 
1 229 GLY n 
1 230 ASP n 
1 231 PHE n 
1 232 ILE n 
1 233 GLY n 
1 234 LEU n 
1 235 ASP n 
1 236 ILE n 
1 237 CYS n 
1 238 LEU n 
1 239 ALA n 
1 240 ILE n 
1 241 MET n 
1 242 ASP n 
1 243 VAL n 
1 244 LEU n 
1 245 TYR n 
1 246 HIS n 
1 247 GLU n 
1 248 THR n 
1 249 GLY n 
1 250 ASP n 
1 251 SER n 
1 252 LYS n 
1 253 TYR n 
1 254 ARG n 
1 255 ALA n 
1 256 CYS n 
1 257 PRO n 
1 258 LEU n 
1 259 ILE n 
1 260 ARG n 
1 261 LYS n 
1 262 MET n 
1 263 VAL n 
1 264 ARG n 
1 265 GLY n 
1 266 GLY n 
1 267 ASN n 
1 268 LEU n 
1 269 GLY n 
1 270 CYS n 
1 271 LYS n 
1 272 THR n 
1 273 GLY n 
1 274 LYS n 
1 275 GLY n 
1 276 PHE n 
1 277 TYR n 
1 278 VAL n 
1 279 TYR n 
1 280 ASN n 
1 281 ALA n 
1 282 ASP n 
1 283 ARG n 
1 284 THR n 
1 285 LYS n 
1 286 THR n 
1 287 PRO n 
1 288 VAL n 
1 289 ASP n 
1 290 GLN n 
1 291 LEU 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                   291 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 FAEPRAA2165_01580 
_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      'Faecalibacterium duncaniae (strain DSM 17677 / JCM 31915 / A2-165)' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     411483 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                           ? 'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE                          ? 'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE                        ? 'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                   ? 'C4 H7 N O4'          133.103 
CAA non-polymer         . 'ACETOACETYL-COENZYME A'          ? 'C25 H40 N7 O18 P3 S' 851.607 
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 
NAD non-polymer         . NICOTINAMIDE-ADENINE-DINUCLEOTIDE ? 'C21 H27 N7 O14 P2'   663.425 
PHE 'L-peptide linking' y PHENYLALANINE                     ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                           ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                            ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                         ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                          ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                            ? 'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   0   0   ALA ALA C . n 
A 1 2   MET 2   1   1   MET MET C . n 
A 1 3   LYS 3   2   2   LYS LYS C . n 
A 1 4   ILE 4   3   3   ILE ILE C . n 
A 1 5   GLY 5   4   4   GLY GLY C . n 
A 1 6   VAL 6   5   5   VAL VAL C . n 
A 1 7   ILE 7   6   6   ILE ILE C . n 
A 1 8   GLY 8   7   7   GLY GLY C . n 
A 1 9   ALA 9   8   8   ALA ALA C . n 
A 1 10  GLY 10  9   9   GLY GLY C . n 
A 1 11  THR 11  10  10  THR THR C . n 
A 1 12  MET 12  11  11  MET MET C . n 
A 1 13  GLY 13  12  12  GLY GLY C . n 
A 1 14  GLN 14  13  13  GLN GLN C . n 
A 1 15  GLY 15  14  14  GLY GLY C . n 
A 1 16  ILE 16  15  15  ILE ILE C . n 
A 1 17  ALA 17  16  16  ALA ALA C . n 
A 1 18  LYS 18  17  17  LYS LYS C . n 
A 1 19  ALA 19  18  18  ALA ALA C . n 
A 1 20  PHE 20  19  19  PHE PHE C . n 
A 1 21  ALA 21  20  20  ALA ALA C . n 
A 1 22  GLN 22  21  21  GLN GLN C . n 
A 1 23  VAL 23  22  22  VAL VAL C . n 
A 1 24  GLU 24  23  23  GLU GLU C . n 
A 1 25  GLY 25  24  24  GLY GLY C . n 
A 1 26  ASN 26  25  25  ASN ASN C . n 
A 1 27  THR 27  26  26  THR THR C . n 
A 1 28  VAL 28  27  27  VAL VAL C . n 
A 1 29  ALA 29  28  28  ALA ALA C . n 
A 1 30  LEU 30  29  29  LEU LEU C . n 
A 1 31  CYS 31  30  30  CYS CYS C . n 
A 1 32  ASP 32  31  31  ASP ASP C . n 
A 1 33  ILE 33  32  32  ILE ILE C . n 
A 1 34  LYS 34  33  33  LYS LYS C . n 
A 1 35  GLN 35  34  34  GLN GLN C . n 
A 1 36  GLU 36  35  35  GLU GLU C . n 
A 1 37  TRP 37  36  36  TRP TRP C . n 
A 1 38  ALA 38  37  37  ALA ALA C . n 
A 1 39  GLU 39  38  38  GLU GLU C . n 
A 1 40  ASN 40  39  39  ASN ASN C . n 
A 1 41  GLY 41  40  40  GLY GLY C . n 
A 1 42  LEU 42  41  41  LEU LEU C . n 
A 1 43  ALA 43  42  42  ALA ALA C . n 
A 1 44  LYS 44  43  43  LYS LYS C . n 
A 1 45  ILE 45  44  44  ILE ILE C . n 
A 1 46  LYS 46  45  45  LYS LYS C . n 
A 1 47  LYS 47  46  46  LYS LYS C . n 
A 1 48  GLY 48  47  47  GLY GLY C . n 
A 1 49  TYR 49  48  48  TYR TYR C . n 
A 1 50  GLU 50  49  49  GLU GLU C . n 
A 1 51  LYS 51  50  50  LYS LYS C . n 
A 1 52  LEU 52  51  51  LEU LEU C . n 
A 1 53  VAL 53  52  52  VAL VAL C . n 
A 1 54  ALA 54  53  53  ALA ALA C . n 
A 1 55  LYS 55  54  54  LYS LYS C . n 
A 1 56  GLY 56  55  55  GLY GLY C . n 
A 1 57  LYS 57  56  56  LYS LYS C . n 
A 1 58  ILE 58  57  57  ILE ILE C . n 
A 1 59  PRO 59  58  58  PRO PRO C . n 
A 1 60  GLN 60  59  59  GLN GLN C . n 
A 1 61  GLU 61  60  60  GLU GLU C . n 
A 1 62  LYS 62  61  61  LYS LYS C . n 
A 1 63  ALA 63  62  62  ALA ALA C . n 
A 1 64  ASP 64  63  63  ASP ASP C . n 
A 1 65  ALA 65  64  64  ALA ALA C . n 
A 1 66  ILE 66  65  65  ILE ILE C . n 
A 1 67  VAL 67  66  66  VAL VAL C . n 
A 1 68  ALA 68  67  67  ALA ALA C . n 
A 1 69  ALA 69  68  68  ALA ALA C . n 
A 1 70  ILE 70  69  69  ILE ILE C . n 
A 1 71  THR 71  70  70  THR THR C . n 
A 1 72  PRO 72  71  71  PRO PRO C . n 
A 1 73  GLY 73  72  72  GLY GLY C . n 
A 1 74  LEU 74  73  73  LEU LEU C . n 
A 1 75  LYS 75  74  74  LYS LYS C . n 
A 1 76  GLU 76  75  75  GLU GLU C . n 
A 1 77  ASN 77  76  76  ASN ASN C . n 
A 1 78  LEU 78  77  77  LEU LEU C . n 
A 1 79  CYS 79  78  78  CYS CYS C . n 
A 1 80  ALA 80  79  79  ALA ALA C . n 
A 1 81  ASP 81  80  80  ASP ASP C . n 
A 1 82  CYS 82  81  81  CYS CYS C . n 
A 1 83  ASP 83  82  82  ASP ASP C . n 
A 1 84  LEU 84  83  83  LEU LEU C . n 
A 1 85  ILE 85  84  84  ILE ILE C . n 
A 1 86  VAL 86  85  85  VAL VAL C . n 
A 1 87  GLU 87  86  86  GLU GLU C . n 
A 1 88  ALA 88  87  87  ALA ALA C . n 
A 1 89  ALA 89  88  88  ALA ALA C . n 
A 1 90  PHE 90  89  89  PHE PHE C . n 
A 1 91  GLU 91  90  90  GLU GLU C . n 
A 1 92  ASP 92  91  91  ASP ASP C . n 
A 1 93  MET 93  92  92  MET MET C . n 
A 1 94  LYS 94  93  93  LYS LYS C . n 
A 1 95  VAL 95  94  94  VAL VAL C . n 
A 1 96  LYS 96  95  95  LYS LYS C . n 
A 1 97  GLN 97  96  96  GLN GLN C . n 
A 1 98  THR 98  97  97  THR THR C . n 
A 1 99  THR 99  98  98  THR THR C . n 
A 1 100 PHE 100 99  99  PHE PHE C . n 
A 1 101 GLY 101 100 100 GLY GLY C . n 
A 1 102 GLU 102 101 101 GLU GLU C . n 
A 1 103 LEU 103 102 102 LEU LEU C . n 
A 1 104 ASP 104 103 103 ASP ASP C . n 
A 1 105 LYS 105 104 104 LYS LYS C . n 
A 1 106 ILE 106 105 105 ILE ILE C . n 
A 1 107 CYS 107 106 106 CYS CYS C . n 
A 1 108 LYS 108 107 107 LYS LYS C . n 
A 1 109 PRO 109 108 108 PRO PRO C . n 
A 1 110 GLU 110 109 109 GLU GLU C . n 
A 1 111 CYS 111 110 110 CYS CYS C . n 
A 1 112 ILE 112 111 111 ILE ILE C . n 
A 1 113 PHE 113 112 112 PHE PHE C . n 
A 1 114 ALA 114 113 113 ALA ALA C . n 
A 1 115 SER 115 114 114 SER SER C . n 
A 1 116 ASN 116 115 115 ASN ASN C . n 
A 1 117 THR 117 116 116 THR THR C . n 
A 1 118 ALA 118 117 117 ALA ALA C . n 
A 1 119 SER 119 118 118 SER SER C . n 
A 1 120 LEU 120 119 119 LEU LEU C . n 
A 1 121 SER 121 120 120 SER SER C . n 
A 1 122 ILE 122 121 121 ILE ILE C . n 
A 1 123 THR 123 122 122 THR THR C . n 
A 1 124 GLU 124 123 123 GLU GLU C . n 
A 1 125 ILE 125 124 124 ILE ILE C . n 
A 1 126 GLY 126 125 125 GLY GLY C . n 
A 1 127 LYS 127 126 126 LYS LYS C . n 
A 1 128 GLY 128 127 127 GLY GLY C . n 
A 1 129 LEU 129 128 128 LEU LEU C . n 
A 1 130 SER 130 129 129 SER SER C . n 
A 1 131 ARG 131 130 130 ARG ARG C . n 
A 1 132 PRO 132 131 131 PRO PRO C . n 
A 1 133 LEU 133 132 132 LEU LEU C . n 
A 1 134 VAL 134 133 133 VAL VAL C . n 
A 1 135 GLY 135 134 134 GLY GLY C . n 
A 1 136 MET 136 135 135 MET MET C . n 
A 1 137 HIS 137 136 136 HIS HIS C . n 
A 1 138 PHE 138 137 137 PHE PHE C . n 
A 1 139 PHE 139 138 138 PHE PHE C . n 
A 1 140 ASN 140 139 139 ASN ASN C . n 
A 1 141 PRO 141 140 140 PRO PRO C . n 
A 1 142 ALA 142 141 141 ALA ALA C . n 
A 1 143 ASP 143 142 142 ASP ASP C . n 
A 1 144 ARG 144 143 143 ARG ARG C . n 
A 1 145 MET 145 144 144 MET MET C . n 
A 1 146 LYS 146 145 145 LYS LYS C . n 
A 1 147 LEU 147 146 146 LEU LEU C . n 
A 1 148 ILE 148 147 147 ILE ILE C . n 
A 1 149 GLU 149 148 148 GLU GLU C . n 
A 1 150 VAL 150 149 149 VAL VAL C . n 
A 1 151 ILE 151 150 150 ILE ILE C . n 
A 1 152 ALA 152 151 151 ALA ALA C . n 
A 1 153 GLY 153 152 152 GLY GLY C . n 
A 1 154 CYS 154 153 153 CYS CYS C . n 
A 1 155 ASN 155 154 154 ASN ASN C . n 
A 1 156 THR 156 155 155 THR THR C . n 
A 1 157 PRO 157 156 156 PRO PRO C . n 
A 1 158 ALA 158 157 157 ALA ALA C . n 
A 1 159 GLU 159 158 158 GLU GLU C . n 
A 1 160 THR 160 159 159 THR THR C . n 
A 1 161 VAL 161 160 160 VAL VAL C . n 
A 1 162 GLU 162 161 161 GLU GLU C . n 
A 1 163 LYS 163 162 162 LYS LYS C . n 
A 1 164 ILE 164 163 163 ILE ILE C . n 
A 1 165 LYS 165 164 164 LYS LYS C . n 
A 1 166 GLU 166 165 165 GLU GLU C . n 
A 1 167 ILE 167 166 166 ILE ILE C . n 
A 1 168 SER 168 167 167 SER SER C . n 
A 1 169 VAL 169 168 168 VAL VAL C . n 
A 1 170 ALA 170 169 169 ALA ALA C . n 
A 1 171 ILE 171 170 170 ILE ILE C . n 
A 1 172 GLY 172 171 171 GLY GLY C . n 
A 1 173 LYS 173 172 172 LYS LYS C . n 
A 1 174 ASN 174 173 173 ASN ASN C . n 
A 1 175 PRO 175 174 174 PRO PRO C . n 
A 1 176 VAL 176 175 175 VAL VAL C . n 
A 1 177 GLN 177 176 176 GLN GLN C . n 
A 1 178 VAL 178 177 177 VAL VAL C . n 
A 1 179 ASN 179 178 178 ASN ASN C . n 
A 1 180 GLU 180 179 179 GLU GLU C . n 
A 1 181 ALA 181 180 180 ALA ALA C . n 
A 1 182 ALA 182 181 181 ALA ALA C . n 
A 1 183 GLY 183 182 182 GLY GLY C . n 
A 1 184 PHE 184 183 183 PHE PHE C . n 
A 1 185 VAL 185 184 184 VAL VAL C . n 
A 1 186 VAL 186 185 185 VAL VAL C . n 
A 1 187 ASN 187 186 186 ASN ASN C . n 
A 1 188 ARG 188 187 187 ARG ARG C . n 
A 1 189 ILE 189 188 188 ILE ILE C . n 
A 1 190 LEU 190 189 189 LEU LEU C . n 
A 1 191 ILE 191 190 190 ILE ILE C . n 
A 1 192 PRO 192 191 191 PRO PRO C . n 
A 1 193 MET 193 192 192 MET MET C . n 
A 1 194 ILE 194 193 193 ILE ILE C . n 
A 1 195 ASN 195 194 194 ASN ASN C . n 
A 1 196 GLU 196 195 195 GLU GLU C . n 
A 1 197 ALA 197 196 196 ALA ALA C . n 
A 1 198 ALA 198 197 197 ALA ALA C . n 
A 1 199 PHE 199 198 198 PHE PHE C . n 
A 1 200 ILE 200 199 199 ILE ILE C . n 
A 1 201 LYS 201 200 200 LYS LYS C . n 
A 1 202 MET 202 201 201 MET MET C . n 
A 1 203 GLU 203 202 202 GLU GLU C . n 
A 1 204 GLY 204 203 203 GLY GLY C . n 
A 1 205 VAL 205 204 204 VAL VAL C . n 
A 1 206 SER 206 205 205 SER SER C . n 
A 1 207 ASP 207 206 206 ASP ASP C . n 
A 1 208 ILE 208 207 207 ILE ILE C . n 
A 1 209 ALA 209 208 208 ALA ALA C . n 
A 1 210 GLY 210 209 209 GLY GLY C . n 
A 1 211 ILE 211 210 210 ILE ILE C . n 
A 1 212 ASP 212 211 211 ASP ASP C . n 
A 1 213 THR 213 212 212 THR THR C . n 
A 1 214 ALA 214 213 213 ALA ALA C . n 
A 1 215 MET 215 214 214 MET MET C . n 
A 1 216 LYS 216 215 215 LYS LYS C . n 
A 1 217 LEU 217 216 216 LEU LEU C . n 
A 1 218 GLY 218 217 217 GLY GLY C . n 
A 1 219 ALA 219 218 218 ALA ALA C . n 
A 1 220 ASN 220 219 219 ASN ASN C . n 
A 1 221 HIS 221 220 220 HIS HIS C . n 
A 1 222 PRO 222 221 221 PRO PRO C . n 
A 1 223 MET 223 222 222 MET MET C . n 
A 1 224 GLY 224 223 223 GLY GLY C . n 
A 1 225 PRO 225 224 224 PRO PRO C . n 
A 1 226 LEU 226 225 225 LEU LEU C . n 
A 1 227 GLU 227 226 226 GLU GLU C . n 
A 1 228 LEU 228 227 227 LEU LEU C . n 
A 1 229 GLY 229 228 228 GLY GLY C . n 
A 1 230 ASP 230 229 229 ASP ASP C . n 
A 1 231 PHE 231 230 230 PHE PHE C . n 
A 1 232 ILE 232 231 231 ILE ILE C . n 
A 1 233 GLY 233 232 232 GLY GLY C . n 
A 1 234 LEU 234 233 233 LEU LEU C . n 
A 1 235 ASP 235 234 234 ASP ASP C . n 
A 1 236 ILE 236 235 235 ILE ILE C . n 
A 1 237 CYS 237 236 236 CYS CYS C . n 
A 1 238 LEU 238 237 237 LEU LEU C . n 
A 1 239 ALA 239 238 238 ALA ALA C . n 
A 1 240 ILE 240 239 239 ILE ILE C . n 
A 1 241 MET 241 240 240 MET MET C . n 
A 1 242 ASP 242 241 241 ASP ASP C . n 
A 1 243 VAL 243 242 242 VAL VAL C . n 
A 1 244 LEU 244 243 243 LEU LEU C . n 
A 1 245 TYR 245 244 244 TYR TYR C . n 
A 1 246 HIS 246 245 245 HIS HIS C . n 
A 1 247 GLU 247 246 246 GLU GLU C . n 
A 1 248 THR 248 247 247 THR THR C . n 
A 1 249 GLY 249 248 248 GLY GLY C . n 
A 1 250 ASP 250 249 249 ASP ASP C . n 
A 1 251 SER 251 250 250 SER SER C . n 
A 1 252 LYS 252 251 251 LYS LYS C . n 
A 1 253 TYR 253 252 252 TYR TYR C . n 
A 1 254 ARG 254 253 253 ARG ARG C . n 
A 1 255 ALA 255 254 254 ALA ALA C . n 
A 1 256 CYS 256 255 255 CYS CYS C . n 
A 1 257 PRO 257 256 256 PRO PRO C . n 
A 1 258 LEU 258 257 257 LEU LEU C . n 
A 1 259 ILE 259 258 258 ILE ILE C . n 
A 1 260 ARG 260 259 259 ARG ARG C . n 
A 1 261 LYS 261 260 260 LYS LYS C . n 
A 1 262 MET 262 261 261 MET MET C . n 
A 1 263 VAL 263 262 262 VAL VAL C . n 
A 1 264 ARG 264 263 263 ARG ARG C . n 
A 1 265 GLY 265 264 264 GLY GLY C . n 
A 1 266 GLY 266 265 265 GLY GLY C . n 
A 1 267 ASN 267 266 266 ASN ASN C . n 
A 1 268 LEU 268 267 267 LEU LEU C . n 
A 1 269 GLY 269 268 268 GLY GLY C . n 
A 1 270 CYS 270 269 269 CYS CYS C . n 
A 1 271 LYS 271 270 270 LYS LYS C . n 
A 1 272 THR 272 271 271 THR THR C . n 
A 1 273 GLY 273 272 272 GLY GLY C . n 
A 1 274 LYS 274 273 273 LYS LYS C . n 
A 1 275 GLY 275 274 274 GLY GLY C . n 
A 1 276 PHE 276 275 275 PHE PHE C . n 
A 1 277 TYR 277 276 276 TYR TYR C . n 
A 1 278 VAL 278 277 277 VAL VAL C . n 
A 1 279 TYR 279 278 278 TYR TYR C . n 
A 1 280 ASN 280 279 279 ASN ASN C . n 
A 1 281 ALA 281 280 280 ALA ALA C . n 
A 1 282 ASP 282 281 281 ASP ASP C . n 
A 1 283 ARG 283 282 282 ARG ARG C . n 
A 1 284 THR 284 283 283 THR THR C . n 
A 1 285 LYS 285 284 284 LYS LYS C . n 
A 1 286 THR 286 285 285 THR THR C . n 
A 1 287 PRO 287 286 286 PRO PRO C . n 
A 1 288 VAL 288 287 287 VAL VAL C . n 
A 1 289 ASP 289 288 288 ASP ASP C . n 
A 1 290 GLN 290 289 289 GLN GLN C . n 
A 1 291 LEU 291 290 ?   ?   ?   C . n 
B 1 1   ALA 1   0   ?   ?   ?   A . n 
B 1 2   MET 2   1   1   MET MET A . n 
B 1 3   LYS 3   2   2   LYS LYS A . n 
B 1 4   ILE 4   3   3   ILE ILE A . n 
B 1 5   GLY 5   4   4   GLY GLY A . n 
B 1 6   VAL 6   5   5   VAL VAL A . n 
B 1 7   ILE 7   6   6   ILE ILE A . n 
B 1 8   GLY 8   7   7   GLY GLY A . n 
B 1 9   ALA 9   8   8   ALA ALA A . n 
B 1 10  GLY 10  9   9   GLY GLY A . n 
B 1 11  THR 11  10  10  THR THR A . n 
B 1 12  MET 12  11  11  MET MET A . n 
B 1 13  GLY 13  12  12  GLY GLY A . n 
B 1 14  GLN 14  13  13  GLN GLN A . n 
B 1 15  GLY 15  14  14  GLY GLY A . n 
B 1 16  ILE 16  15  15  ILE ILE A . n 
B 1 17  ALA 17  16  16  ALA ALA A . n 
B 1 18  LYS 18  17  17  LYS LYS A . n 
B 1 19  ALA 19  18  18  ALA ALA A . n 
B 1 20  PHE 20  19  19  PHE PHE A . n 
B 1 21  ALA 21  20  20  ALA ALA A . n 
B 1 22  GLN 22  21  21  GLN GLN A . n 
B 1 23  VAL 23  22  22  VAL VAL A . n 
B 1 24  GLU 24  23  23  GLU GLU A . n 
B 1 25  GLY 25  24  24  GLY GLY A . n 
B 1 26  ASN 26  25  25  ASN ASN A . n 
B 1 27  THR 27  26  26  THR THR A . n 
B 1 28  VAL 28  27  27  VAL VAL A . n 
B 1 29  ALA 29  28  28  ALA ALA A . n 
B 1 30  LEU 30  29  29  LEU LEU A . n 
B 1 31  CYS 31  30  30  CYS CYS A . n 
B 1 32  ASP 32  31  31  ASP ASP A . n 
B 1 33  ILE 33  32  32  ILE ILE A . n 
B 1 34  LYS 34  33  33  LYS LYS A . n 
B 1 35  GLN 35  34  34  GLN GLN A . n 
B 1 36  GLU 36  35  35  GLU GLU A . n 
B 1 37  TRP 37  36  36  TRP TRP A . n 
B 1 38  ALA 38  37  37  ALA ALA A . n 
B 1 39  GLU 39  38  38  GLU GLU A . n 
B 1 40  ASN 40  39  39  ASN ASN A . n 
B 1 41  GLY 41  40  40  GLY GLY A . n 
B 1 42  LEU 42  41  41  LEU LEU A . n 
B 1 43  ALA 43  42  42  ALA ALA A . n 
B 1 44  LYS 44  43  43  LYS LYS A . n 
B 1 45  ILE 45  44  44  ILE ILE A . n 
B 1 46  LYS 46  45  45  LYS LYS A . n 
B 1 47  LYS 47  46  46  LYS LYS A . n 
B 1 48  GLY 48  47  47  GLY GLY A . n 
B 1 49  TYR 49  48  48  TYR TYR A . n 
B 1 50  GLU 50  49  49  GLU GLU A . n 
B 1 51  LYS 51  50  50  LYS LYS A . n 
B 1 52  LEU 52  51  51  LEU LEU A . n 
B 1 53  VAL 53  52  52  VAL VAL A . n 
B 1 54  ALA 54  53  53  ALA ALA A . n 
B 1 55  LYS 55  54  54  LYS LYS A . n 
B 1 56  GLY 56  55  55  GLY GLY A . n 
B 1 57  LYS 57  56  56  LYS LYS A . n 
B 1 58  ILE 58  57  57  ILE ILE A . n 
B 1 59  PRO 59  58  58  PRO PRO A . n 
B 1 60  GLN 60  59  59  GLN GLN A . n 
B 1 61  GLU 61  60  60  GLU GLU A . n 
B 1 62  LYS 62  61  61  LYS LYS A . n 
B 1 63  ALA 63  62  62  ALA ALA A . n 
B 1 64  ASP 64  63  63  ASP ASP A . n 
B 1 65  ALA 65  64  64  ALA ALA A . n 
B 1 66  ILE 66  65  65  ILE ILE A . n 
B 1 67  VAL 67  66  66  VAL VAL A . n 
B 1 68  ALA 68  67  67  ALA ALA A . n 
B 1 69  ALA 69  68  68  ALA ALA A . n 
B 1 70  ILE 70  69  69  ILE ILE A . n 
B 1 71  THR 71  70  70  THR THR A . n 
B 1 72  PRO 72  71  71  PRO PRO A . n 
B 1 73  GLY 73  72  72  GLY GLY A . n 
B 1 74  LEU 74  73  73  LEU LEU A . n 
B 1 75  LYS 75  74  74  LYS LYS A . n 
B 1 76  GLU 76  75  75  GLU GLU A . n 
B 1 77  ASN 77  76  76  ASN ASN A . n 
B 1 78  LEU 78  77  77  LEU LEU A . n 
B 1 79  CYS 79  78  78  CYS CYS A . n 
B 1 80  ALA 80  79  79  ALA ALA A . n 
B 1 81  ASP 81  80  80  ASP ASP A . n 
B 1 82  CYS 82  81  81  CYS CYS A . n 
B 1 83  ASP 83  82  82  ASP ASP A . n 
B 1 84  LEU 84  83  83  LEU LEU A . n 
B 1 85  ILE 85  84  84  ILE ILE A . n 
B 1 86  VAL 86  85  85  VAL VAL A . n 
B 1 87  GLU 87  86  86  GLU GLU A . n 
B 1 88  ALA 88  87  87  ALA ALA A . n 
B 1 89  ALA 89  88  88  ALA ALA A . n 
B 1 90  PHE 90  89  89  PHE PHE A . n 
B 1 91  GLU 91  90  90  GLU GLU A . n 
B 1 92  ASP 92  91  91  ASP ASP A . n 
B 1 93  MET 93  92  92  MET MET A . n 
B 1 94  LYS 94  93  93  LYS LYS A . n 
B 1 95  VAL 95  94  94  VAL VAL A . n 
B 1 96  LYS 96  95  95  LYS LYS A . n 
B 1 97  GLN 97  96  96  GLN GLN A . n 
B 1 98  THR 98  97  97  THR THR A . n 
B 1 99  THR 99  98  98  THR THR A . n 
B 1 100 PHE 100 99  99  PHE PHE A . n 
B 1 101 GLY 101 100 100 GLY GLY A . n 
B 1 102 GLU 102 101 101 GLU GLU A . n 
B 1 103 LEU 103 102 102 LEU LEU A . n 
B 1 104 ASP 104 103 103 ASP ASP A . n 
B 1 105 LYS 105 104 104 LYS LYS A . n 
B 1 106 ILE 106 105 105 ILE ILE A . n 
B 1 107 CYS 107 106 106 CYS CYS A . n 
B 1 108 LYS 108 107 107 LYS LYS A . n 
B 1 109 PRO 109 108 108 PRO PRO A . n 
B 1 110 GLU 110 109 109 GLU GLU A . n 
B 1 111 CYS 111 110 110 CYS CYS A . n 
B 1 112 ILE 112 111 111 ILE ILE A . n 
B 1 113 PHE 113 112 112 PHE PHE A . n 
B 1 114 ALA 114 113 113 ALA ALA A . n 
B 1 115 SER 115 114 114 SER SER A . n 
B 1 116 ASN 116 115 115 ASN ASN A . n 
B 1 117 THR 117 116 116 THR THR A . n 
B 1 118 ALA 118 117 117 ALA ALA A . n 
B 1 119 SER 119 118 118 SER SER A . n 
B 1 120 LEU 120 119 119 LEU LEU A . n 
B 1 121 SER 121 120 120 SER SER A . n 
B 1 122 ILE 122 121 121 ILE ILE A . n 
B 1 123 THR 123 122 122 THR THR A . n 
B 1 124 GLU 124 123 123 GLU GLU A . n 
B 1 125 ILE 125 124 124 ILE ILE A . n 
B 1 126 GLY 126 125 125 GLY GLY A . n 
B 1 127 LYS 127 126 126 LYS LYS A . n 
B 1 128 GLY 128 127 127 GLY GLY A . n 
B 1 129 LEU 129 128 128 LEU LEU A . n 
B 1 130 SER 130 129 129 SER SER A . n 
B 1 131 ARG 131 130 130 ARG ARG A . n 
B 1 132 PRO 132 131 131 PRO PRO A . n 
B 1 133 LEU 133 132 132 LEU LEU A . n 
B 1 134 VAL 134 133 133 VAL VAL A . n 
B 1 135 GLY 135 134 134 GLY GLY A . n 
B 1 136 MET 136 135 135 MET MET A . n 
B 1 137 HIS 137 136 136 HIS HIS A . n 
B 1 138 PHE 138 137 137 PHE PHE A . n 
B 1 139 PHE 139 138 138 PHE PHE A . n 
B 1 140 ASN 140 139 139 ASN ASN A . n 
B 1 141 PRO 141 140 140 PRO PRO A . n 
B 1 142 ALA 142 141 141 ALA ALA A . n 
B 1 143 ASP 143 142 142 ASP ASP A . n 
B 1 144 ARG 144 143 143 ARG ARG A . n 
B 1 145 MET 145 144 144 MET MET A . n 
B 1 146 LYS 146 145 145 LYS LYS A . n 
B 1 147 LEU 147 146 146 LEU LEU A . n 
B 1 148 ILE 148 147 147 ILE ILE A . n 
B 1 149 GLU 149 148 148 GLU GLU A . n 
B 1 150 VAL 150 149 149 VAL VAL A . n 
B 1 151 ILE 151 150 150 ILE ILE A . n 
B 1 152 ALA 152 151 151 ALA ALA A . n 
B 1 153 GLY 153 152 152 GLY GLY A . n 
B 1 154 CYS 154 153 153 CYS CYS A . n 
B 1 155 ASN 155 154 154 ASN ASN A . n 
B 1 156 THR 156 155 155 THR THR A . n 
B 1 157 PRO 157 156 156 PRO PRO A . n 
B 1 158 ALA 158 157 157 ALA ALA A . n 
B 1 159 GLU 159 158 158 GLU GLU A . n 
B 1 160 THR 160 159 159 THR THR A . n 
B 1 161 VAL 161 160 160 VAL VAL A . n 
B 1 162 GLU 162 161 161 GLU GLU A . n 
B 1 163 LYS 163 162 162 LYS LYS A . n 
B 1 164 ILE 164 163 163 ILE ILE A . n 
B 1 165 LYS 165 164 164 LYS LYS A . n 
B 1 166 GLU 166 165 165 GLU GLU A . n 
B 1 167 ILE 167 166 166 ILE ILE A . n 
B 1 168 SER 168 167 167 SER SER A . n 
B 1 169 VAL 169 168 168 VAL VAL A . n 
B 1 170 ALA 170 169 169 ALA ALA A . n 
B 1 171 ILE 171 170 170 ILE ILE A . n 
B 1 172 GLY 172 171 171 GLY GLY A . n 
B 1 173 LYS 173 172 172 LYS LYS A . n 
B 1 174 ASN 174 173 173 ASN ASN A . n 
B 1 175 PRO 175 174 174 PRO PRO A . n 
B 1 176 VAL 176 175 175 VAL VAL A . n 
B 1 177 GLN 177 176 176 GLN GLN A . n 
B 1 178 VAL 178 177 177 VAL VAL A . n 
B 1 179 ASN 179 178 178 ASN ASN A . n 
B 1 180 GLU 180 179 179 GLU GLU A . n 
B 1 181 ALA 181 180 180 ALA ALA A . n 
B 1 182 ALA 182 181 181 ALA ALA A . n 
B 1 183 GLY 183 182 182 GLY GLY A . n 
B 1 184 PHE 184 183 183 PHE PHE A . n 
B 1 185 VAL 185 184 184 VAL VAL A . n 
B 1 186 VAL 186 185 185 VAL VAL A . n 
B 1 187 ASN 187 186 186 ASN ASN A . n 
B 1 188 ARG 188 187 187 ARG ARG A . n 
B 1 189 ILE 189 188 188 ILE ILE A . n 
B 1 190 LEU 190 189 189 LEU LEU A . n 
B 1 191 ILE 191 190 190 ILE ILE A . n 
B 1 192 PRO 192 191 191 PRO PRO A . n 
B 1 193 MET 193 192 192 MET MET A . n 
B 1 194 ILE 194 193 193 ILE ILE A . n 
B 1 195 ASN 195 194 194 ASN ASN A . n 
B 1 196 GLU 196 195 195 GLU GLU A . n 
B 1 197 ALA 197 196 196 ALA ALA A . n 
B 1 198 ALA 198 197 197 ALA ALA A . n 
B 1 199 PHE 199 198 198 PHE PHE A . n 
B 1 200 ILE 200 199 199 ILE ILE A . n 
B 1 201 LYS 201 200 200 LYS LYS A . n 
B 1 202 MET 202 201 201 MET MET A . n 
B 1 203 GLU 203 202 202 GLU GLU A . n 
B 1 204 GLY 204 203 203 GLY GLY A . n 
B 1 205 VAL 205 204 204 VAL VAL A . n 
B 1 206 SER 206 205 205 SER SER A . n 
B 1 207 ASP 207 206 206 ASP ASP A . n 
B 1 208 ILE 208 207 207 ILE ILE A . n 
B 1 209 ALA 209 208 208 ALA ALA A . n 
B 1 210 GLY 210 209 209 GLY GLY A . n 
B 1 211 ILE 211 210 210 ILE ILE A . n 
B 1 212 ASP 212 211 211 ASP ASP A . n 
B 1 213 THR 213 212 212 THR THR A . n 
B 1 214 ALA 214 213 213 ALA ALA A . n 
B 1 215 MET 215 214 214 MET MET A . n 
B 1 216 LYS 216 215 215 LYS LYS A . n 
B 1 217 LEU 217 216 216 LEU LEU A . n 
B 1 218 GLY 218 217 217 GLY GLY A . n 
B 1 219 ALA 219 218 218 ALA ALA A . n 
B 1 220 ASN 220 219 219 ASN ASN A . n 
B 1 221 HIS 221 220 220 HIS HIS A . n 
B 1 222 PRO 222 221 221 PRO PRO A . n 
B 1 223 MET 223 222 222 MET MET A . n 
B 1 224 GLY 224 223 223 GLY GLY A . n 
B 1 225 PRO 225 224 224 PRO PRO A . n 
B 1 226 LEU 226 225 225 LEU LEU A . n 
B 1 227 GLU 227 226 226 GLU GLU A . n 
B 1 228 LEU 228 227 227 LEU LEU A . n 
B 1 229 GLY 229 228 228 GLY GLY A . n 
B 1 230 ASP 230 229 229 ASP ASP A . n 
B 1 231 PHE 231 230 230 PHE PHE A . n 
B 1 232 ILE 232 231 231 ILE ILE A . n 
B 1 233 GLY 233 232 232 GLY GLY A . n 
B 1 234 LEU 234 233 233 LEU LEU A . n 
B 1 235 ASP 235 234 234 ASP ASP A . n 
B 1 236 ILE 236 235 235 ILE ILE A . n 
B 1 237 CYS 237 236 236 CYS CYS A . n 
B 1 238 LEU 238 237 237 LEU LEU A . n 
B 1 239 ALA 239 238 238 ALA ALA A . n 
B 1 240 ILE 240 239 239 ILE ILE A . n 
B 1 241 MET 241 240 240 MET MET A . n 
B 1 242 ASP 242 241 241 ASP ASP A . n 
B 1 243 VAL 243 242 242 VAL VAL A . n 
B 1 244 LEU 244 243 243 LEU LEU A . n 
B 1 245 TYR 245 244 244 TYR TYR A . n 
B 1 246 HIS 246 245 245 HIS HIS A . n 
B 1 247 GLU 247 246 246 GLU GLU A . n 
B 1 248 THR 248 247 247 THR THR A . n 
B 1 249 GLY 249 248 248 GLY GLY A . n 
B 1 250 ASP 250 249 249 ASP ASP A . n 
B 1 251 SER 251 250 250 SER SER A . n 
B 1 252 LYS 252 251 251 LYS LYS A . n 
B 1 253 TYR 253 252 252 TYR TYR A . n 
B 1 254 ARG 254 253 253 ARG ARG A . n 
B 1 255 ALA 255 254 254 ALA ALA A . n 
B 1 256 CYS 256 255 255 CYS CYS A . n 
B 1 257 PRO 257 256 256 PRO PRO A . n 
B 1 258 LEU 258 257 257 LEU LEU A . n 
B 1 259 ILE 259 258 258 ILE ILE A . n 
B 1 260 ARG 260 259 259 ARG ARG A . n 
B 1 261 LYS 261 260 260 LYS LYS A . n 
B 1 262 MET 262 261 261 MET MET A . n 
B 1 263 VAL 263 262 262 VAL VAL A . n 
B 1 264 ARG 264 263 263 ARG ARG A . n 
B 1 265 GLY 265 264 264 GLY GLY A . n 
B 1 266 GLY 266 265 265 GLY GLY A . n 
B 1 267 ASN 267 266 266 ASN ASN A . n 
B 1 268 LEU 268 267 267 LEU LEU A . n 
B 1 269 GLY 269 268 268 GLY GLY A . n 
B 1 270 CYS 270 269 269 CYS CYS A . n 
B 1 271 LYS 271 270 270 LYS LYS A . n 
B 1 272 THR 272 271 271 THR THR A . n 
B 1 273 GLY 273 272 272 GLY GLY A . n 
B 1 274 LYS 274 273 273 LYS LYS A . n 
B 1 275 GLY 275 274 274 GLY GLY A . n 
B 1 276 PHE 276 275 275 PHE PHE A . n 
B 1 277 TYR 277 276 276 TYR TYR A . n 
B 1 278 VAL 278 277 277 VAL VAL A . n 
B 1 279 TYR 279 278 278 TYR TYR A . n 
B 1 280 ASN 280 279 279 ASN ASN A . n 
B 1 281 ALA 281 280 280 ALA ALA A . n 
B 1 282 ASP 282 281 281 ASP ASP A . n 
B 1 283 ARG 283 282 282 ARG ARG A . n 
B 1 284 THR 284 283 283 THR THR A . n 
B 1 285 LYS 285 284 284 LYS LYS A . n 
B 1 286 THR 286 285 285 THR THR A . n 
B 1 287 PRO 287 286 286 PRO PRO A . n 
B 1 288 VAL 288 287 287 VAL VAL A . n 
B 1 289 ASP 289 288 288 ASP ASP A . n 
B 1 290 GLN 290 289 ?   ?   ?   A . n 
B 1 291 LEU 291 290 ?   ?   ?   A . n 
C 1 1   ALA 1   0   ?   ?   ?   B . n 
C 1 2   MET 2   1   1   MET MET B . n 
C 1 3   LYS 3   2   2   LYS LYS B . n 
C 1 4   ILE 4   3   3   ILE ILE B . n 
C 1 5   GLY 5   4   4   GLY GLY B . n 
C 1 6   VAL 6   5   5   VAL VAL B . n 
C 1 7   ILE 7   6   6   ILE ILE B . n 
C 1 8   GLY 8   7   7   GLY GLY B . n 
C 1 9   ALA 9   8   8   ALA ALA B . n 
C 1 10  GLY 10  9   9   GLY GLY B . n 
C 1 11  THR 11  10  10  THR THR B . n 
C 1 12  MET 12  11  11  MET MET B . n 
C 1 13  GLY 13  12  12  GLY GLY B . n 
C 1 14  GLN 14  13  13  GLN GLN B . n 
C 1 15  GLY 15  14  14  GLY GLY B . n 
C 1 16  ILE 16  15  15  ILE ILE B . n 
C 1 17  ALA 17  16  16  ALA ALA B . n 
C 1 18  LYS 18  17  17  LYS LYS B . n 
C 1 19  ALA 19  18  18  ALA ALA B . n 
C 1 20  PHE 20  19  19  PHE PHE B . n 
C 1 21  ALA 21  20  20  ALA ALA B . n 
C 1 22  GLN 22  21  21  GLN GLN B . n 
C 1 23  VAL 23  22  22  VAL VAL B . n 
C 1 24  GLU 24  23  23  GLU GLU B . n 
C 1 25  GLY 25  24  24  GLY GLY B . n 
C 1 26  ASN 26  25  25  ASN ASN B . n 
C 1 27  THR 27  26  26  THR THR B . n 
C 1 28  VAL 28  27  27  VAL VAL B . n 
C 1 29  ALA 29  28  28  ALA ALA B . n 
C 1 30  LEU 30  29  29  LEU LEU B . n 
C 1 31  CYS 31  30  30  CYS CYS B . n 
C 1 32  ASP 32  31  31  ASP ASP B . n 
C 1 33  ILE 33  32  32  ILE ILE B . n 
C 1 34  LYS 34  33  33  LYS LYS B . n 
C 1 35  GLN 35  34  34  GLN GLN B . n 
C 1 36  GLU 36  35  35  GLU GLU B . n 
C 1 37  TRP 37  36  36  TRP TRP B . n 
C 1 38  ALA 38  37  37  ALA ALA B . n 
C 1 39  GLU 39  38  38  GLU GLU B . n 
C 1 40  ASN 40  39  39  ASN ASN B . n 
C 1 41  GLY 41  40  40  GLY GLY B . n 
C 1 42  LEU 42  41  41  LEU LEU B . n 
C 1 43  ALA 43  42  42  ALA ALA B . n 
C 1 44  LYS 44  43  43  LYS LYS B . n 
C 1 45  ILE 45  44  44  ILE ILE B . n 
C 1 46  LYS 46  45  45  LYS LYS B . n 
C 1 47  LYS 47  46  46  LYS LYS B . n 
C 1 48  GLY 48  47  47  GLY GLY B . n 
C 1 49  TYR 49  48  48  TYR TYR B . n 
C 1 50  GLU 50  49  49  GLU GLU B . n 
C 1 51  LYS 51  50  50  LYS LYS B . n 
C 1 52  LEU 52  51  51  LEU LEU B . n 
C 1 53  VAL 53  52  52  VAL VAL B . n 
C 1 54  ALA 54  53  53  ALA ALA B . n 
C 1 55  LYS 55  54  54  LYS LYS B . n 
C 1 56  GLY 56  55  55  GLY GLY B . n 
C 1 57  LYS 57  56  56  LYS LYS B . n 
C 1 58  ILE 58  57  57  ILE ILE B . n 
C 1 59  PRO 59  58  58  PRO PRO B . n 
C 1 60  GLN 60  59  59  GLN GLN B . n 
C 1 61  GLU 61  60  60  GLU GLU B . n 
C 1 62  LYS 62  61  61  LYS LYS B . n 
C 1 63  ALA 63  62  62  ALA ALA B . n 
C 1 64  ASP 64  63  63  ASP ASP B . n 
C 1 65  ALA 65  64  64  ALA ALA B . n 
C 1 66  ILE 66  65  65  ILE ILE B . n 
C 1 67  VAL 67  66  66  VAL VAL B . n 
C 1 68  ALA 68  67  67  ALA ALA B . n 
C 1 69  ALA 69  68  68  ALA ALA B . n 
C 1 70  ILE 70  69  69  ILE ILE B . n 
C 1 71  THR 71  70  70  THR THR B . n 
C 1 72  PRO 72  71  71  PRO PRO B . n 
C 1 73  GLY 73  72  72  GLY GLY B . n 
C 1 74  LEU 74  73  73  LEU LEU B . n 
C 1 75  LYS 75  74  74  LYS LYS B . n 
C 1 76  GLU 76  75  75  GLU GLU B . n 
C 1 77  ASN 77  76  76  ASN ASN B . n 
C 1 78  LEU 78  77  77  LEU LEU B . n 
C 1 79  CYS 79  78  78  CYS CYS B . n 
C 1 80  ALA 80  79  79  ALA ALA B . n 
C 1 81  ASP 81  80  80  ASP ASP B . n 
C 1 82  CYS 82  81  81  CYS CYS B . n 
C 1 83  ASP 83  82  82  ASP ASP B . n 
C 1 84  LEU 84  83  83  LEU LEU B . n 
C 1 85  ILE 85  84  84  ILE ILE B . n 
C 1 86  VAL 86  85  85  VAL VAL B . n 
C 1 87  GLU 87  86  86  GLU GLU B . n 
C 1 88  ALA 88  87  87  ALA ALA B . n 
C 1 89  ALA 89  88  88  ALA ALA B . n 
C 1 90  PHE 90  89  89  PHE PHE B . n 
C 1 91  GLU 91  90  90  GLU GLU B . n 
C 1 92  ASP 92  91  91  ASP ASP B . n 
C 1 93  MET 93  92  92  MET MET B . n 
C 1 94  LYS 94  93  93  LYS LYS B . n 
C 1 95  VAL 95  94  94  VAL VAL B . n 
C 1 96  LYS 96  95  95  LYS LYS B . n 
C 1 97  GLN 97  96  96  GLN GLN B . n 
C 1 98  THR 98  97  97  THR THR B . n 
C 1 99  THR 99  98  98  THR THR B . n 
C 1 100 PHE 100 99  99  PHE PHE B . n 
C 1 101 GLY 101 100 100 GLY GLY B . n 
C 1 102 GLU 102 101 101 GLU GLU B . n 
C 1 103 LEU 103 102 102 LEU LEU B . n 
C 1 104 ASP 104 103 103 ASP ASP B . n 
C 1 105 LYS 105 104 104 LYS LYS B . n 
C 1 106 ILE 106 105 105 ILE ILE B . n 
C 1 107 CYS 107 106 106 CYS CYS B . n 
C 1 108 LYS 108 107 107 LYS LYS B . n 
C 1 109 PRO 109 108 108 PRO PRO B . n 
C 1 110 GLU 110 109 109 GLU GLU B . n 
C 1 111 CYS 111 110 110 CYS CYS B . n 
C 1 112 ILE 112 111 111 ILE ILE B . n 
C 1 113 PHE 113 112 112 PHE PHE B . n 
C 1 114 ALA 114 113 113 ALA ALA B . n 
C 1 115 SER 115 114 114 SER SER B . n 
C 1 116 ASN 116 115 115 ASN ASN B . n 
C 1 117 THR 117 116 116 THR THR B . n 
C 1 118 ALA 118 117 117 ALA ALA B . n 
C 1 119 SER 119 118 118 SER SER B . n 
C 1 120 LEU 120 119 119 LEU LEU B . n 
C 1 121 SER 121 120 120 SER SER B . n 
C 1 122 ILE 122 121 121 ILE ILE B . n 
C 1 123 THR 123 122 122 THR THR B . n 
C 1 124 GLU 124 123 123 GLU GLU B . n 
C 1 125 ILE 125 124 124 ILE ILE B . n 
C 1 126 GLY 126 125 125 GLY GLY B . n 
C 1 127 LYS 127 126 126 LYS LYS B . n 
C 1 128 GLY 128 127 127 GLY GLY B . n 
C 1 129 LEU 129 128 128 LEU LEU B . n 
C 1 130 SER 130 129 129 SER SER B . n 
C 1 131 ARG 131 130 130 ARG ARG B . n 
C 1 132 PRO 132 131 131 PRO PRO B . n 
C 1 133 LEU 133 132 132 LEU LEU B . n 
C 1 134 VAL 134 133 133 VAL VAL B . n 
C 1 135 GLY 135 134 134 GLY GLY B . n 
C 1 136 MET 136 135 135 MET MET B . n 
C 1 137 HIS 137 136 136 HIS HIS B . n 
C 1 138 PHE 138 137 137 PHE PHE B . n 
C 1 139 PHE 139 138 138 PHE PHE B . n 
C 1 140 ASN 140 139 139 ASN ASN B . n 
C 1 141 PRO 141 140 140 PRO PRO B . n 
C 1 142 ALA 142 141 141 ALA ALA B . n 
C 1 143 ASP 143 142 142 ASP ASP B . n 
C 1 144 ARG 144 143 143 ARG ARG B . n 
C 1 145 MET 145 144 144 MET MET B . n 
C 1 146 LYS 146 145 145 LYS LYS B . n 
C 1 147 LEU 147 146 146 LEU LEU B . n 
C 1 148 ILE 148 147 147 ILE ILE B . n 
C 1 149 GLU 149 148 148 GLU GLU B . n 
C 1 150 VAL 150 149 149 VAL VAL B . n 
C 1 151 ILE 151 150 150 ILE ILE B . n 
C 1 152 ALA 152 151 151 ALA ALA B . n 
C 1 153 GLY 153 152 152 GLY GLY B . n 
C 1 154 CYS 154 153 153 CYS CYS B . n 
C 1 155 ASN 155 154 154 ASN ASN B . n 
C 1 156 THR 156 155 155 THR THR B . n 
C 1 157 PRO 157 156 156 PRO PRO B . n 
C 1 158 ALA 158 157 157 ALA ALA B . n 
C 1 159 GLU 159 158 158 GLU GLU B . n 
C 1 160 THR 160 159 159 THR THR B . n 
C 1 161 VAL 161 160 160 VAL VAL B . n 
C 1 162 GLU 162 161 161 GLU GLU B . n 
C 1 163 LYS 163 162 162 LYS LYS B . n 
C 1 164 ILE 164 163 163 ILE ILE B . n 
C 1 165 LYS 165 164 164 LYS LYS B . n 
C 1 166 GLU 166 165 165 GLU GLU B . n 
C 1 167 ILE 167 166 166 ILE ILE B . n 
C 1 168 SER 168 167 167 SER SER B . n 
C 1 169 VAL 169 168 168 VAL VAL B . n 
C 1 170 ALA 170 169 169 ALA ALA B . n 
C 1 171 ILE 171 170 170 ILE ILE B . n 
C 1 172 GLY 172 171 171 GLY GLY B . n 
C 1 173 LYS 173 172 172 LYS LYS B . n 
C 1 174 ASN 174 173 173 ASN ASN B . n 
C 1 175 PRO 175 174 174 PRO PRO B . n 
C 1 176 VAL 176 175 175 VAL VAL B . n 
C 1 177 GLN 177 176 176 GLN GLN B . n 
C 1 178 VAL 178 177 177 VAL VAL B . n 
C 1 179 ASN 179 178 178 ASN ASN B . n 
C 1 180 GLU 180 179 179 GLU GLU B . n 
C 1 181 ALA 181 180 180 ALA ALA B . n 
C 1 182 ALA 182 181 181 ALA ALA B . n 
C 1 183 GLY 183 182 182 GLY GLY B . n 
C 1 184 PHE 184 183 183 PHE PHE B . n 
C 1 185 VAL 185 184 184 VAL VAL B . n 
C 1 186 VAL 186 185 185 VAL VAL B . n 
C 1 187 ASN 187 186 186 ASN ASN B . n 
C 1 188 ARG 188 187 187 ARG ARG B . n 
C 1 189 ILE 189 188 188 ILE ILE B . n 
C 1 190 LEU 190 189 189 LEU LEU B . n 
C 1 191 ILE 191 190 190 ILE ILE B . n 
C 1 192 PRO 192 191 191 PRO PRO B . n 
C 1 193 MET 193 192 192 MET MET B . n 
C 1 194 ILE 194 193 193 ILE ILE B . n 
C 1 195 ASN 195 194 194 ASN ASN B . n 
C 1 196 GLU 196 195 195 GLU GLU B . n 
C 1 197 ALA 197 196 196 ALA ALA B . n 
C 1 198 ALA 198 197 197 ALA ALA B . n 
C 1 199 PHE 199 198 198 PHE PHE B . n 
C 1 200 ILE 200 199 199 ILE ILE B . n 
C 1 201 LYS 201 200 200 LYS LYS B . n 
C 1 202 MET 202 201 201 MET MET B . n 
C 1 203 GLU 203 202 202 GLU GLU B . n 
C 1 204 GLY 204 203 203 GLY GLY B . n 
C 1 205 VAL 205 204 204 VAL VAL B . n 
C 1 206 SER 206 205 205 SER SER B . n 
C 1 207 ASP 207 206 206 ASP ASP B . n 
C 1 208 ILE 208 207 207 ILE ILE B . n 
C 1 209 ALA 209 208 208 ALA ALA B . n 
C 1 210 GLY 210 209 209 GLY GLY B . n 
C 1 211 ILE 211 210 210 ILE ILE B . n 
C 1 212 ASP 212 211 211 ASP ASP B . n 
C 1 213 THR 213 212 212 THR THR B . n 
C 1 214 ALA 214 213 213 ALA ALA B . n 
C 1 215 MET 215 214 214 MET MET B . n 
C 1 216 LYS 216 215 215 LYS LYS B . n 
C 1 217 LEU 217 216 216 LEU LEU B . n 
C 1 218 GLY 218 217 217 GLY GLY B . n 
C 1 219 ALA 219 218 218 ALA ALA B . n 
C 1 220 ASN 220 219 219 ASN ASN B . n 
C 1 221 HIS 221 220 220 HIS HIS B . n 
C 1 222 PRO 222 221 221 PRO PRO B . n 
C 1 223 MET 223 222 222 MET MET B . n 
C 1 224 GLY 224 223 223 GLY GLY B . n 
C 1 225 PRO 225 224 224 PRO PRO B . n 
C 1 226 LEU 226 225 225 LEU LEU B . n 
C 1 227 GLU 227 226 226 GLU GLU B . n 
C 1 228 LEU 228 227 227 LEU LEU B . n 
C 1 229 GLY 229 228 228 GLY GLY B . n 
C 1 230 ASP 230 229 229 ASP ASP B . n 
C 1 231 PHE 231 230 230 PHE PHE B . n 
C 1 232 ILE 232 231 231 ILE ILE B . n 
C 1 233 GLY 233 232 232 GLY GLY B . n 
C 1 234 LEU 234 233 233 LEU LEU B . n 
C 1 235 ASP 235 234 234 ASP ASP B . n 
C 1 236 ILE 236 235 235 ILE ILE B . n 
C 1 237 CYS 237 236 236 CYS CYS B . n 
C 1 238 LEU 238 237 237 LEU LEU B . n 
C 1 239 ALA 239 238 238 ALA ALA B . n 
C 1 240 ILE 240 239 239 ILE ILE B . n 
C 1 241 MET 241 240 240 MET MET B . n 
C 1 242 ASP 242 241 241 ASP ASP B . n 
C 1 243 VAL 243 242 242 VAL VAL B . n 
C 1 244 LEU 244 243 243 LEU LEU B . n 
C 1 245 TYR 245 244 244 TYR TYR B . n 
C 1 246 HIS 246 245 245 HIS HIS B . n 
C 1 247 GLU 247 246 246 GLU GLU B . n 
C 1 248 THR 248 247 247 THR THR B . n 
C 1 249 GLY 249 248 248 GLY GLY B . n 
C 1 250 ASP 250 249 249 ASP ASP B . n 
C 1 251 SER 251 250 250 SER SER B . n 
C 1 252 LYS 252 251 251 LYS LYS B . n 
C 1 253 TYR 253 252 252 TYR TYR B . n 
C 1 254 ARG 254 253 253 ARG ARG B . n 
C 1 255 ALA 255 254 254 ALA ALA B . n 
C 1 256 CYS 256 255 255 CYS CYS B . n 
C 1 257 PRO 257 256 256 PRO PRO B . n 
C 1 258 LEU 258 257 257 LEU LEU B . n 
C 1 259 ILE 259 258 258 ILE ILE B . n 
C 1 260 ARG 260 259 259 ARG ARG B . n 
C 1 261 LYS 261 260 260 LYS LYS B . n 
C 1 262 MET 262 261 261 MET MET B . n 
C 1 263 VAL 263 262 262 VAL VAL B . n 
C 1 264 ARG 264 263 263 ARG ARG B . n 
C 1 265 GLY 265 264 264 GLY GLY B . n 
C 1 266 GLY 266 265 265 GLY GLY B . n 
C 1 267 ASN 267 266 266 ASN ASN B . n 
C 1 268 LEU 268 267 267 LEU LEU B . n 
C 1 269 GLY 269 268 268 GLY GLY B . n 
C 1 270 CYS 270 269 269 CYS CYS B . n 
C 1 271 LYS 271 270 270 LYS LYS B . n 
C 1 272 THR 272 271 271 THR THR B . n 
C 1 273 GLY 273 272 272 GLY GLY B . n 
C 1 274 LYS 274 273 273 LYS LYS B . n 
C 1 275 GLY 275 274 274 GLY GLY B . n 
C 1 276 PHE 276 275 275 PHE PHE B . n 
C 1 277 TYR 277 276 276 TYR TYR B . n 
C 1 278 VAL 278 277 277 VAL VAL B . n 
C 1 279 TYR 279 278 278 TYR TYR B . n 
C 1 280 ASN 280 279 279 ASN ASN B . n 
C 1 281 ALA 281 280 280 ALA ALA B . n 
C 1 282 ASP 282 281 281 ASP ASP B . n 
C 1 283 ARG 283 282 282 ARG ARG B . n 
C 1 284 THR 284 283 283 THR THR B . n 
C 1 285 LYS 285 284 284 LYS LYS B . n 
C 1 286 THR 286 285 285 THR THR B . n 
C 1 287 PRO 287 286 286 PRO PRO B . n 
C 1 288 VAL 288 287 287 VAL VAL B . n 
C 1 289 ASP 289 288 288 ASP ASP B . n 
C 1 290 GLN 290 289 289 GLN GLN B . n 
C 1 291 LEU 291 290 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CAA ? ? CAA ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NAD ? ? NAD ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
D 2 CAA 1   401 401 CAA LIG B . 
E 3 NAD 1   402 301 NAD NAD B . 
F 4 HOH 1   301 165 HOH HOH C . 
F 4 HOH 2   302 177 HOH HOH C . 
F 4 HOH 3   303 23  HOH HOH C . 
F 4 HOH 4   304 9   HOH HOH C . 
F 4 HOH 5   305 31  HOH HOH C . 
F 4 HOH 6   306 116 HOH HOH C . 
F 4 HOH 7   307 80  HOH HOH C . 
F 4 HOH 8   308 111 HOH HOH C . 
F 4 HOH 9   309 79  HOH HOH C . 
F 4 HOH 10  310 41  HOH HOH C . 
F 4 HOH 11  311 134 HOH HOH C . 
F 4 HOH 12  312 22  HOH HOH C . 
F 4 HOH 13  313 38  HOH HOH C . 
F 4 HOH 14  314 7   HOH HOH C . 
F 4 HOH 15  315 16  HOH HOH C . 
F 4 HOH 16  316 219 HOH HOH C . 
F 4 HOH 17  317 152 HOH HOH C . 
F 4 HOH 18  318 28  HOH HOH C . 
F 4 HOH 19  319 84  HOH HOH C . 
F 4 HOH 20  320 244 HOH HOH C . 
F 4 HOH 21  321 5   HOH HOH C . 
F 4 HOH 22  322 101 HOH HOH C . 
F 4 HOH 23  323 102 HOH HOH C . 
F 4 HOH 24  324 234 HOH HOH C . 
F 4 HOH 25  325 35  HOH HOH C . 
F 4 HOH 26  326 226 HOH HOH C . 
F 4 HOH 27  327 65  HOH HOH C . 
F 4 HOH 28  328 59  HOH HOH C . 
F 4 HOH 29  329 218 HOH HOH C . 
F 4 HOH 30  330 88  HOH HOH C . 
F 4 HOH 31  331 70  HOH HOH C . 
F 4 HOH 32  332 12  HOH HOH C . 
F 4 HOH 33  333 44  HOH HOH C . 
F 4 HOH 34  334 139 HOH HOH C . 
F 4 HOH 35  335 122 HOH HOH C . 
F 4 HOH 36  336 202 HOH HOH C . 
F 4 HOH 37  337 90  HOH HOH C . 
F 4 HOH 38  338 170 HOH HOH C . 
F 4 HOH 39  339 203 HOH HOH C . 
F 4 HOH 40  340 61  HOH HOH C . 
F 4 HOH 41  341 110 HOH HOH C . 
F 4 HOH 42  342 132 HOH HOH C . 
F 4 HOH 43  343 246 HOH HOH C . 
F 4 HOH 44  344 151 HOH HOH C . 
F 4 HOH 45  345 108 HOH HOH C . 
F 4 HOH 46  346 149 HOH HOH C . 
F 4 HOH 47  347 39  HOH HOH C . 
F 4 HOH 48  348 242 HOH HOH C . 
F 4 HOH 49  349 140 HOH HOH C . 
F 4 HOH 50  350 210 HOH HOH C . 
F 4 HOH 51  351 239 HOH HOH C . 
F 4 HOH 52  352 49  HOH HOH C . 
F 4 HOH 53  353 75  HOH HOH C . 
F 4 HOH 54  354 198 HOH HOH C . 
F 4 HOH 55  355 72  HOH HOH C . 
F 4 HOH 56  356 135 HOH HOH C . 
F 4 HOH 57  357 229 HOH HOH C . 
F 4 HOH 58  358 109 HOH HOH C . 
F 4 HOH 59  359 96  HOH HOH C . 
F 4 HOH 60  360 241 HOH HOH C . 
F 4 HOH 61  361 119 HOH HOH C . 
F 4 HOH 62  362 220 HOH HOH C . 
F 4 HOH 63  363 188 HOH HOH C . 
F 4 HOH 64  364 73  HOH HOH C . 
F 4 HOH 65  365 227 HOH HOH C . 
F 4 HOH 66  366 213 HOH HOH C . 
F 4 HOH 67  367 217 HOH HOH C . 
F 4 HOH 68  368 92  HOH HOH C . 
F 4 HOH 69  369 230 HOH HOH C . 
F 4 HOH 70  370 56  HOH HOH C . 
F 4 HOH 71  371 187 HOH HOH C . 
F 4 HOH 72  372 250 HOH HOH C . 
F 4 HOH 73  373 197 HOH HOH C . 
F 4 HOH 74  374 233 HOH HOH C . 
F 4 HOH 75  375 86  HOH HOH C . 
F 4 HOH 76  376 128 HOH HOH C . 
F 4 HOH 77  377 130 HOH HOH C . 
F 4 HOH 78  378 232 HOH HOH C . 
F 4 HOH 79  379 249 HOH HOH C . 
F 4 HOH 80  380 238 HOH HOH C . 
F 4 HOH 81  381 45  HOH HOH C . 
F 4 HOH 82  382 123 HOH HOH C . 
F 4 HOH 83  383 97  HOH HOH C . 
G 4 HOH 1   301 14  HOH HOH A . 
G 4 HOH 2   302 129 HOH HOH A . 
G 4 HOH 3   303 184 HOH HOH A . 
G 4 HOH 4   304 182 HOH HOH A . 
G 4 HOH 5   305 175 HOH HOH A . 
G 4 HOH 6   306 143 HOH HOH A . 
G 4 HOH 7   307 148 HOH HOH A . 
G 4 HOH 8   308 163 HOH HOH A . 
G 4 HOH 9   309 137 HOH HOH A . 
G 4 HOH 10  310 126 HOH HOH A . 
G 4 HOH 11  311 136 HOH HOH A . 
G 4 HOH 12  312 2   HOH HOH A . 
G 4 HOH 13  313 161 HOH HOH A . 
G 4 HOH 14  314 194 HOH HOH A . 
G 4 HOH 15  315 83  HOH HOH A . 
G 4 HOH 16  316 208 HOH HOH A . 
G 4 HOH 17  317 195 HOH HOH A . 
G 4 HOH 18  318 25  HOH HOH A . 
G 4 HOH 19  319 200 HOH HOH A . 
G 4 HOH 20  320 235 HOH HOH A . 
G 4 HOH 21  321 112 HOH HOH A . 
G 4 HOH 22  322 68  HOH HOH A . 
G 4 HOH 23  323 77  HOH HOH A . 
G 4 HOH 24  324 26  HOH HOH A . 
G 4 HOH 25  325 211 HOH HOH A . 
G 4 HOH 26  326 74  HOH HOH A . 
G 4 HOH 27  327 46  HOH HOH A . 
G 4 HOH 28  328 153 HOH HOH A . 
G 4 HOH 29  329 34  HOH HOH A . 
G 4 HOH 30  330 42  HOH HOH A . 
G 4 HOH 31  331 71  HOH HOH A . 
G 4 HOH 32  332 176 HOH HOH A . 
G 4 HOH 33  333 60  HOH HOH A . 
G 4 HOH 34  334 1   HOH HOH A . 
G 4 HOH 35  335 52  HOH HOH A . 
G 4 HOH 36  336 178 HOH HOH A . 
G 4 HOH 37  337 145 HOH HOH A . 
G 4 HOH 38  338 183 HOH HOH A . 
G 4 HOH 39  339 100 HOH HOH A . 
G 4 HOH 40  340 8   HOH HOH A . 
G 4 HOH 41  341 240 HOH HOH A . 
G 4 HOH 42  342 127 HOH HOH A . 
G 4 HOH 43  343 81  HOH HOH A . 
G 4 HOH 44  344 156 HOH HOH A . 
G 4 HOH 45  345 50  HOH HOH A . 
G 4 HOH 46  346 115 HOH HOH A . 
G 4 HOH 47  347 21  HOH HOH A . 
G 4 HOH 48  348 91  HOH HOH A . 
G 4 HOH 49  349 221 HOH HOH A . 
G 4 HOH 50  350 19  HOH HOH A . 
G 4 HOH 51  351 205 HOH HOH A . 
G 4 HOH 52  352 47  HOH HOH A . 
G 4 HOH 53  353 214 HOH HOH A . 
G 4 HOH 54  354 82  HOH HOH A . 
G 4 HOH 55  355 104 HOH HOH A . 
G 4 HOH 56  356 43  HOH HOH A . 
G 4 HOH 57  357 85  HOH HOH A . 
G 4 HOH 58  358 133 HOH HOH A . 
G 4 HOH 59  359 150 HOH HOH A . 
G 4 HOH 60  360 54  HOH HOH A . 
G 4 HOH 61  361 17  HOH HOH A . 
G 4 HOH 62  362 105 HOH HOH A . 
G 4 HOH 63  363 69  HOH HOH A . 
G 4 HOH 64  364 141 HOH HOH A . 
G 4 HOH 65  365 67  HOH HOH A . 
G 4 HOH 66  366 215 HOH HOH A . 
G 4 HOH 67  367 33  HOH HOH A . 
G 4 HOH 68  368 57  HOH HOH A . 
G 4 HOH 69  369 168 HOH HOH A . 
G 4 HOH 70  370 113 HOH HOH A . 
G 4 HOH 71  371 53  HOH HOH A . 
G 4 HOH 72  372 248 HOH HOH A . 
G 4 HOH 73  373 169 HOH HOH A . 
G 4 HOH 74  374 27  HOH HOH A . 
G 4 HOH 75  375 222 HOH HOH A . 
G 4 HOH 76  376 190 HOH HOH A . 
G 4 HOH 77  377 117 HOH HOH A . 
G 4 HOH 78  378 95  HOH HOH A . 
G 4 HOH 79  379 247 HOH HOH A . 
G 4 HOH 80  380 209 HOH HOH A . 
G 4 HOH 81  381 196 HOH HOH A . 
G 4 HOH 82  382 155 HOH HOH A . 
G 4 HOH 83  383 164 HOH HOH A . 
G 4 HOH 84  384 212 HOH HOH A . 
G 4 HOH 85  385 231 HOH HOH A . 
G 4 HOH 86  386 106 HOH HOH A . 
G 4 HOH 87  387 236 HOH HOH A . 
G 4 HOH 88  388 166 HOH HOH A . 
G 4 HOH 89  389 180 HOH HOH A . 
G 4 HOH 90  390 32  HOH HOH A . 
G 4 HOH 91  391 179 HOH HOH A . 
G 4 HOH 92  392 228 HOH HOH A . 
G 4 HOH 93  393 162 HOH HOH A . 
G 4 HOH 94  394 207 HOH HOH A . 
G 4 HOH 95  395 216 HOH HOH A . 
G 4 HOH 96  396 89  HOH HOH A . 
G 4 HOH 97  397 243 HOH HOH A . 
G 4 HOH 98  398 192 HOH HOH A . 
G 4 HOH 99  399 199 HOH HOH A . 
G 4 HOH 100 400 154 HOH HOH A . 
G 4 HOH 101 401 121 HOH HOH A . 
G 4 HOH 102 402 245 HOH HOH A . 
H 4 HOH 1   501 15  HOH HOH B . 
H 4 HOH 2   502 18  HOH HOH B . 
H 4 HOH 3   503 120 HOH HOH B . 
H 4 HOH 4   504 98  HOH HOH B . 
H 4 HOH 5   505 171 HOH HOH B . 
H 4 HOH 6   506 160 HOH HOH B . 
H 4 HOH 7   507 206 HOH HOH B . 
H 4 HOH 8   508 51  HOH HOH B . 
H 4 HOH 9   509 66  HOH HOH B . 
H 4 HOH 10  510 62  HOH HOH B . 
H 4 HOH 11  511 224 HOH HOH B . 
H 4 HOH 12  512 103 HOH HOH B . 
H 4 HOH 13  513 172 HOH HOH B . 
H 4 HOH 14  514 10  HOH HOH B . 
H 4 HOH 15  515 13  HOH HOH B . 
H 4 HOH 16  516 147 HOH HOH B . 
H 4 HOH 17  517 93  HOH HOH B . 
H 4 HOH 18  518 24  HOH HOH B . 
H 4 HOH 19  519 146 HOH HOH B . 
H 4 HOH 20  520 201 HOH HOH B . 
H 4 HOH 21  521 225 HOH HOH B . 
H 4 HOH 22  522 118 HOH HOH B . 
H 4 HOH 23  523 191 HOH HOH B . 
H 4 HOH 24  524 142 HOH HOH B . 
H 4 HOH 25  525 55  HOH HOH B . 
H 4 HOH 26  526 36  HOH HOH B . 
H 4 HOH 27  527 6   HOH HOH B . 
H 4 HOH 28  528 29  HOH HOH B . 
H 4 HOH 29  529 11  HOH HOH B . 
H 4 HOH 30  530 114 HOH HOH B . 
H 4 HOH 31  531 3   HOH HOH B . 
H 4 HOH 32  532 30  HOH HOH B . 
H 4 HOH 33  533 58  HOH HOH B . 
H 4 HOH 34  534 144 HOH HOH B . 
H 4 HOH 35  535 193 HOH HOH B . 
H 4 HOH 36  536 174 HOH HOH B . 
H 4 HOH 37  537 87  HOH HOH B . 
H 4 HOH 38  538 131 HOH HOH B . 
H 4 HOH 39  539 94  HOH HOH B . 
H 4 HOH 40  540 64  HOH HOH B . 
H 4 HOH 41  541 76  HOH HOH B . 
H 4 HOH 42  542 99  HOH HOH B . 
H 4 HOH 43  543 125 HOH HOH B . 
H 4 HOH 44  544 237 HOH HOH B . 
H 4 HOH 45  545 138 HOH HOH B . 
H 4 HOH 46  546 124 HOH HOH B . 
H 4 HOH 47  547 37  HOH HOH B . 
H 4 HOH 48  548 78  HOH HOH B . 
H 4 HOH 49  549 48  HOH HOH B . 
H 4 HOH 50  550 223 HOH HOH B . 
H 4 HOH 51  551 167 HOH HOH B . 
H 4 HOH 52  552 204 HOH HOH B . 
H 4 HOH 53  553 107 HOH HOH B . 
H 4 HOH 54  554 189 HOH HOH B . 
H 4 HOH 55  555 40  HOH HOH B . 
H 4 HOH 56  556 173 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JHZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     90.562 
_cell.length_a_esd                 ? 
_cell.length_b                     90.562 
_cell.length_b_esd                 ? 
_cell.length_c                     212.496 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        18 
_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                         9JHZ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                153 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 1 2' 
_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                   9JHZ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.70 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.39 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'ammonium citrate dibasic, PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-04-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000 
_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                        'PAL/PLS BEAMLINE 11C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   11C 
_diffrn_source.pdbx_synchrotron_site       PAL/PLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JHZ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.20 
_reflns.d_resolution_low                               50.00 
_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                                     50628 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.266 
_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                                0.202 
_reflns.pdbx_Rpim_I_all                                0.058 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       515685 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.981 
_reflns.pdbx_CC_star                                   0.995 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.193 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.20 2.24 ? ? ? ? ? ? 2432 ? ? ? ? ? ? ? ? ? ? ? 3.8  0.501 ? ? 0.810 0.381 ? 1  1 0.025 0.222 ? 96.8  ? 0.708 ? ? ? ? ? ? ? ? ? 
2.24 2.28 ? ? ? ? ? ? 2443 ? ? ? ? ? ? ? ? ? ? ? 4.5  0.505 ? ? 0.763 0.338 ? 2  1 0.136 0.490 ? 98.0  ? 0.679 ? ? ? ? ? ? ? ? ? 
2.28 2.32 ? ? ? ? ? ? 2508 ? ? ? ? ? ? ? ? ? ? ? 5.2  0.485 ? ? 0.709 0.298 ? 3  1 0.111 0.447 ? 99.3  ? 0.640 ? ? ? ? ? ? ? ? ? 
2.32 2.37 ? ? ? ? ? ? 2525 ? ? ? ? ? ? ? ? ? ? ? 5.7  0.471 ? ? 0.659 0.265 ? 4  1 0.275 0.657 ? 99.4  ? 0.600 ? ? ? ? ? ? ? ? ? 
2.37 2.42 ? ? ? ? ? ? 2497 ? ? ? ? ? ? ? ? ? ? ? 6.3  0.485 ? ? 0.658 0.254 ? 5  1 0.185 0.558 ? 99.5  ? 0.604 ? ? ? ? ? ? ? ? ? 
2.42 2.48 ? ? ? ? ? ? 2501 ? ? ? ? ? ? ? ? ? ? ? 6.9  0.489 ? ? 0.621 0.229 ? 6  1 0.357 0.726 ? 99.8  ? 0.575 ? ? ? ? ? ? ? ? ? 
2.48 2.54 ? ? ? ? ? ? 2538 ? ? ? ? ? ? ? ? ? ? ? 7.0  0.485 ? ? 0.585 0.213 ? 7  1 0.415 0.766 ? 99.7  ? 0.542 ? ? ? ? ? ? ? ? ? 
2.54 2.61 ? ? ? ? ? ? 2498 ? ? ? ? ? ? ? ? ? ? ? 8.0  0.462 ? ? 0.539 0.185 ? 8  1 0.650 0.887 ? 99.9  ? 0.505 ? ? ? ? ? ? ? ? ? 
2.61 2.69 ? ? ? ? ? ? 2556 ? ? ? ? ? ? ? ? ? ? ? 9.5  0.524 ? ? 0.541 0.170 ? 9  1 0.717 0.914 ? 99.9  ? 0.512 ? ? ? ? ? ? ? ? ? 
2.69 2.77 ? ? ? ? ? ? 2497 ? ? ? ? ? ? ? ? ? ? ? 10.1 0.559 ? ? 0.502 0.153 ? 10 1 0.770 0.933 ? 99.9  ? 0.477 ? ? ? ? ? ? ? ? ? 
2.77 2.87 ? ? ? ? ? ? 2533 ? ? ? ? ? ? ? ? ? ? ? 10.6 0.610 ? ? 0.446 0.132 ? 11 1 0.847 0.958 ? 99.8  ? 0.425 ? ? ? ? ? ? ? ? ? 
2.87 2.99 ? ? ? ? ? ? 2533 ? ? ? ? ? ? ? ? ? ? ? 11.1 0.652 ? ? 0.399 0.115 ? 12 1 0.919 0.979 ? 99.8  ? 0.381 ? ? ? ? ? ? ? ? ? 
2.99 3.12 ? ? ? ? ? ? 2540 ? ? ? ? ? ? ? ? ? ? ? 10.8 0.705 ? ? 0.348 0.102 ? 13 1 0.941 0.985 ? 99.8  ? 0.332 ? ? ? ? ? ? ? ? ? 
3.12 3.29 ? ? ? ? ? ? 2520 ? ? ? ? ? ? ? ? ? ? ? 12.6 0.856 ? ? 0.276 0.074 ? 14 1 0.973 0.993 ? 100.0 ? 0.265 ? ? ? ? ? ? ? ? ? 
3.29 3.49 ? ? ? ? ? ? 2563 ? ? ? ? ? ? ? ? ? ? ? 13.8 1.099 ? ? 0.230 0.059 ? 15 1 0.985 0.996 ? 99.9  ? 0.222 ? ? ? ? ? ? ? ? ? 
3.49 3.76 ? ? ? ? ? ? 2553 ? ? ? ? ? ? ? ? ? ? ? 14.6 1.490 ? ? 0.184 0.046 ? 16 1 0.989 0.997 ? 100.0 ? 0.178 ? ? ? ? ? ? ? ? ? 
3.76 4.14 ? ? ? ? ? ? 2559 ? ? ? ? ? ? ? ? ? ? ? 14.1 1.879 ? ? 0.153 0.039 ? 17 1 0.993 0.998 ? 99.9  ? 0.148 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9JHZ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.20 
_refine.ls_d_res_low                             45.28 
_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                     50507 
_refine.ls_number_reflns_R_free                  1993 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.04 
_refine.ls_percent_reflns_R_free                 3.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1983 
_refine.ls_R_factor_R_free                       0.2433 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1965 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_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               NONE 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 24.46 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.29 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        45.28 
_refine_hist.number_atoms_solvent             241 
_refine_hist.number_atoms_total               6821 
_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        6526 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_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' ? 10.707 ? 919  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.047  ? 1040 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 1149 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.20 2.26  . . 126 3140 91.00  . . . . 0.3244 . . . . . . . . . . . 0.3522 
'X-RAY DIFFRACTION' 2.26 2.32  . . 146 3397 98.00  . . . . 0.2973 . . . . . . . . . . . 0.3299 
'X-RAY DIFFRACTION' 2.32 2.38  . . 143 3465 99.00  . . . . 0.2722 . . . . . . . . . . . 0.3170 
'X-RAY DIFFRACTION' 2.38 2.46  . . 146 3420 100.00 . . . . 0.2648 . . . . . . . . . . . 0.3105 
'X-RAY DIFFRACTION' 2.46 2.55  . . 139 3457 100.00 . . . . 0.2527 . . . . . . . . . . . 0.2908 
'X-RAY DIFFRACTION' 2.55 2.65  . . 141 3516 100.00 . . . . 0.2466 . . . . . . . . . . . 0.2948 
'X-RAY DIFFRACTION' 2.65 2.77  . . 138 3423 100.00 . . . . 0.2325 . . . . . . . . . . . 0.2957 
'X-RAY DIFFRACTION' 2.77 2.92  . . 145 3526 100.00 . . . . 0.2272 . . . . . . . . . . . 0.3189 
'X-RAY DIFFRACTION' 2.92 3.10  . . 141 3450 100.00 . . . . 0.2094 . . . . . . . . . . . 0.2586 
'X-RAY DIFFRACTION' 3.10 3.34  . . 144 3526 100.00 . . . . 0.1996 . . . . . . . . . . . 0.2478 
'X-RAY DIFFRACTION' 3.34 3.68  . . 143 3497 100.00 . . . . 0.1775 . . . . . . . . . . . 0.2202 
'X-RAY DIFFRACTION' 3.68 4.21  . . 147 3519 100.00 . . . . 0.1540 . . . . . . . . . . . 0.1889 
'X-RAY DIFFRACTION' 4.21 5.30  . . 147 3541 100.00 . . . . 0.1421 . . . . . . . . . . . 0.2072 
'X-RAY DIFFRACTION' 5.30 45.28 . . 147 3637 100.00 . . . . 0.1567 . . . . . . . . . . . 0.1827 
# 
_struct.entry_id                     9JHZ 
_struct.title                        '3-Hydroxybutyryl-CoA dehydrogenase mutant(S117A) with acetoacetyl CoA and NAD' 
_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        9JHZ 
_struct_keywords.text            'Complex with acetoacetyl CoA and NAD, 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 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    C7H5K9_FAED2 
_struct_ref.pdbx_db_accession          C7H5K9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKIGVIGAGTMGQGIAKAFAQVEGNTVALCDIKQEWAENGLAKIKKGYEKLVAKGKIPQEKADAIVAAITPGLKENLCAD
CDLIVEAAFEDMKVKQTTFGELDKICKPECIFASNTSSLSITEIGKGLSRPLVGMHFFNPADRMKLIEVIAGCNTPAETV
EKIKEISVAIGKNPVQVNEAAGFVVNRILIPMINEAAFIKMEGVSDIAGIDTAMKLGANHPMGPLELGDFIGLDICLAIM
DVLYHETGDSKYRACPLIRKMVRGGNLGCKTGKGFYVYNADRTKTPVDQL
;
_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 9JHZ C 2 ? 291 ? C7H5K9 1 ? 290 ? 1 290 
2 1 9JHZ A 2 ? 291 ? C7H5K9 1 ? 290 ? 1 290 
3 1 9JHZ B 2 ? 291 ? C7H5K9 1 ? 290 ? 1 290 
# 
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 9JHZ ALA C 1   ? UNP C7H5K9 ?   ?   'expression tag'      0   1 
1 9JHZ ALA C 118 ? UNP C7H5K9 SER 117 'engineered mutation' 117 2 
2 9JHZ ALA A 1   ? UNP C7H5K9 ?   ?   'expression tag'      0   3 
2 9JHZ ALA A 118 ? UNP C7H5K9 SER 117 'engineered mutation' 117 4 
3 9JHZ ALA B 1   ? UNP C7H5K9 ?   ?   'expression tag'      0   5 
3 9JHZ ALA B 118 ? UNP C7H5K9 SER 117 'engineered mutation' 117 6 
# 
_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   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
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)' 20150 ? 
1 MORE         -91   ? 
1 'SSA (A^2)'  69500 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z      1.0000000000 0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000  
0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 6_565 x,x-y+1,-z 0.5000000000 0.8660254038 0.0000000000 -45.2810000000 0.8660254038 -0.5000000000 
0.0000000000 78.4289926175 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 10  ? GLN A 22  ? GLY C 9   GLN C 21  1 ? 13 
HELX_P HELX_P2  AA2 LYS A 34  ? LYS A 55  ? LYS C 33  LYS C 54  1 ? 22 
HELX_P HELX_P3  AA3 PRO A 59  ? ALA A 69  ? PRO C 58  ALA C 68  1 ? 11 
HELX_P HELX_P4  AA4 LEU A 74  ? CYS A 79  ? LEU C 73  CYS C 78  1 ? 6  
HELX_P HELX_P5  AA5 ASP A 92  ? CYS A 107 ? ASP C 91  CYS C 106 1 ? 16 
HELX_P HELX_P6  AA6 SER A 121 ? GLY A 126 ? SER C 120 GLY C 125 1 ? 6  
HELX_P HELX_P7  AA7 PRO A 157 ? ILE A 171 ? PRO C 156 ILE C 170 1 ? 15 
HELX_P HELX_P8  AA8 VAL A 185 ? GLU A 203 ? VAL C 184 GLU C 202 1 ? 19 
HELX_P HELX_P9  AA9 ASP A 207 ? ALA A 219 ? ASP C 206 ALA C 218 1 ? 13 
HELX_P HELX_P10 AB1 GLY A 224 ? GLY A 233 ? GLY C 223 GLY C 232 1 ? 10 
HELX_P HELX_P11 AB2 GLY A 233 ? GLY A 249 ? GLY C 232 GLY C 248 1 ? 17 
HELX_P HELX_P12 AB3 ASP A 250 ? ARG A 254 ? ASP C 249 ARG C 253 5 ? 5  
HELX_P HELX_P13 AB4 CYS A 256 ? GLY A 265 ? CYS C 255 GLY C 264 1 ? 10 
HELX_P HELX_P14 AB5 GLY A 269 ? GLY A 273 ? GLY C 268 GLY C 272 5 ? 5  
HELX_P HELX_P15 AB6 GLY B 10  ? GLN B 22  ? GLY A 9   GLN A 21  1 ? 13 
HELX_P HELX_P16 AB7 LYS B 34  ? LYS B 55  ? LYS A 33  LYS A 54  1 ? 22 
HELX_P HELX_P17 AB8 PRO B 59  ? ALA B 69  ? PRO A 58  ALA A 68  1 ? 11 
HELX_P HELX_P18 AB9 LEU B 74  ? CYS B 79  ? LEU A 73  CYS A 78  1 ? 6  
HELX_P HELX_P19 AC1 ASP B 92  ? CYS B 107 ? ASP A 91  CYS A 106 1 ? 16 
HELX_P HELX_P20 AC2 SER B 121 ? GLY B 126 ? SER A 120 GLY A 125 1 ? 6  
HELX_P HELX_P21 AC3 PRO B 157 ? ILE B 171 ? PRO A 156 ILE A 170 1 ? 15 
HELX_P HELX_P22 AC4 VAL B 185 ? GLU B 203 ? VAL A 184 GLU A 202 1 ? 19 
HELX_P HELX_P23 AC5 ASP B 207 ? ALA B 219 ? ASP A 206 ALA A 218 1 ? 13 
HELX_P HELX_P24 AC6 GLY B 224 ? GLY B 233 ? GLY A 223 GLY A 232 1 ? 10 
HELX_P HELX_P25 AC7 GLY B 233 ? GLY B 249 ? GLY A 232 GLY A 248 1 ? 17 
HELX_P HELX_P26 AC8 ASP B 250 ? ARG B 254 ? ASP A 249 ARG A 253 5 ? 5  
HELX_P HELX_P27 AC9 CYS B 256 ? GLY B 265 ? CYS A 255 GLY A 264 1 ? 10 
HELX_P HELX_P28 AD1 GLY C 10  ? GLN C 22  ? GLY B 9   GLN B 21  1 ? 13 
HELX_P HELX_P29 AD2 LYS C 34  ? LYS C 55  ? LYS B 33  LYS B 54  1 ? 22 
HELX_P HELX_P30 AD3 PRO C 59  ? ALA C 68  ? PRO B 58  ALA B 67  1 ? 10 
HELX_P HELX_P31 AD4 ASP C 92  ? CYS C 107 ? ASP B 91  CYS B 106 1 ? 16 
HELX_P HELX_P32 AD5 SER C 121 ? GLY C 126 ? SER B 120 GLY B 125 1 ? 6  
HELX_P HELX_P33 AD6 PRO C 157 ? ILE C 171 ? PRO B 156 ILE B 170 1 ? 15 
HELX_P HELX_P34 AD7 VAL C 185 ? GLU C 203 ? VAL B 184 GLU B 202 1 ? 19 
HELX_P HELX_P35 AD8 ASP C 207 ? ASN C 220 ? ASP B 206 ASN B 219 1 ? 14 
HELX_P HELX_P36 AD9 GLY C 224 ? GLY C 233 ? GLY B 223 GLY B 232 1 ? 10 
HELX_P HELX_P37 AE1 GLY C 233 ? GLY C 249 ? GLY B 232 GLY B 248 1 ? 17 
HELX_P HELX_P38 AE2 ASP C 250 ? ARG C 254 ? ASP B 249 ARG B 253 5 ? 5  
HELX_P HELX_P39 AE3 CYS C 256 ? GLY C 265 ? CYS B 255 GLY B 264 1 ? 10 
HELX_P HELX_P40 AE4 GLY C 269 ? GLY C 273 ? GLY B 268 GLY B 272 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ASN 140 A . ? ASN 139 C PRO 141 A ? PRO 140 C 1 -3.93 
2 ASN 140 B . ? ASN 139 A PRO 141 B ? PRO 140 A 1 -4.17 
3 ASN 140 C . ? ASN 139 B PRO 141 C ? PRO 140 B 1 -4.18 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 8 ? 
AA4 ? 2 ? 
AA5 ? 8 ? 
AA6 ? 2 ? 
# 
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 ? anti-parallel 
AA1 7 8 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? anti-parallel 
AA3 7 8 ? parallel      
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA5 6 7 ? anti-parallel 
AA5 7 8 ? parallel      
AA6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 70  ? GLY A 73  ? ILE C 69  GLY C 72  
AA1 2 ASN A 26  ? CYS A 31  ? ASN C 25  CYS C 30  
AA1 3 MET A 2   ? ILE A 7   ? MET C 1   ILE C 6   
AA1 4 LEU A 84  ? GLU A 87  ? LEU C 83  GLU C 86  
AA1 5 ILE A 112 ? SER A 115 ? ILE C 111 SER C 114 
AA1 6 LEU A 133 ? HIS A 137 ? LEU C 132 HIS C 136 
AA1 7 LEU A 147 ? ALA A 152 ? LEU C 146 ALA C 151 
AA1 8 ASN A 174 ? ASN A 179 ? ASN C 173 ASN C 178 
AA2 1 TYR A 277 ? TYR A 279 ? TYR C 276 TYR C 278 
AA2 2 LYS A 285 ? PRO A 287 ? LYS C 284 PRO C 286 
AA3 1 ILE B 70  ? GLY B 73  ? ILE A 69  GLY A 72  
AA3 2 THR B 27  ? CYS B 31  ? THR A 26  CYS A 30  
AA3 3 LYS B 3   ? ILE B 7   ? LYS A 2   ILE A 6   
AA3 4 LEU B 84  ? GLU B 87  ? LEU A 83  GLU A 86  
AA3 5 ILE B 112 ? SER B 115 ? ILE A 111 SER A 114 
AA3 6 LEU B 133 ? HIS B 137 ? LEU A 132 HIS A 136 
AA3 7 LEU B 147 ? ALA B 152 ? LEU A 146 ALA A 151 
AA3 8 ASN B 174 ? ASN B 179 ? ASN A 173 ASN A 178 
AA4 1 TYR B 277 ? TYR B 279 ? TYR A 276 TYR A 278 
AA4 2 LYS B 285 ? PRO B 287 ? LYS A 284 PRO A 286 
AA5 1 ILE C 70  ? PRO C 72  ? ILE B 69  PRO B 71  
AA5 2 THR C 27  ? CYS C 31  ? THR B 26  CYS B 30  
AA5 3 LYS C 3   ? ILE C 7   ? LYS B 2   ILE B 6   
AA5 4 LEU C 84  ? GLU C 87  ? LEU B 83  GLU B 86  
AA5 5 ILE C 112 ? SER C 115 ? ILE B 111 SER B 114 
AA5 6 LEU C 133 ? HIS C 137 ? LEU B 132 HIS B 136 
AA5 7 LEU C 147 ? ALA C 152 ? LEU B 146 ALA B 151 
AA5 8 ASN C 174 ? ASN C 179 ? ASN B 173 ASN B 178 
AA6 1 TYR C 277 ? TYR C 279 ? TYR B 276 TYR B 278 
AA6 2 LYS C 285 ? PRO C 287 ? LYS B 284 PRO B 286 
# 
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 THR A 71  ? O THR C 70  N VAL A 28  ? N VAL C 27  
AA1 2 3 O THR A 27  ? O THR C 26  N ILE A 4   ? N ILE C 3   
AA1 3 4 N GLY A 5   ? N GLY C 4   O LEU A 84  ? O LEU C 83  
AA1 4 5 N ILE A 85  ? N ILE C 84  O ALA A 114 ? O ALA C 113 
AA1 5 6 N PHE A 113 ? N PHE C 112 O VAL A 134 ? O VAL C 133 
AA1 6 7 N HIS A 137 ? N HIS C 136 O GLU A 149 ? O GLU C 148 
AA1 7 8 N VAL A 150 ? N VAL C 149 O VAL A 178 ? O VAL C 177 
AA2 1 2 N VAL A 278 ? N VAL C 277 O THR A 286 ? O THR C 285 
AA3 1 2 O THR B 71  ? O THR A 70  N VAL B 28  ? N VAL A 27  
AA3 2 3 O THR B 27  ? O THR A 26  N ILE B 4   ? N ILE A 3   
AA3 3 4 N GLY B 5   ? N GLY A 4   O LEU B 84  ? O LEU A 83  
AA3 4 5 N ILE B 85  ? N ILE A 84  O ALA B 114 ? O ALA A 113 
AA3 5 6 N SER B 115 ? N SER A 114 O MET B 136 ? O MET A 135 
AA3 6 7 N HIS B 137 ? N HIS A 136 O GLU B 149 ? O GLU A 148 
AA3 7 8 N VAL B 150 ? N VAL A 149 O VAL B 178 ? O VAL A 177 
AA4 1 2 N VAL B 278 ? N VAL A 277 O THR B 286 ? O THR A 285 
AA5 1 2 O THR C 71  ? O THR B 70  N VAL C 28  ? N VAL B 27  
AA5 2 3 O THR C 27  ? O THR B 26  N ILE C 4   ? N ILE B 3   
AA5 3 4 N GLY C 5   ? N GLY B 4   O LEU C 84  ? O LEU B 83  
AA5 4 5 N ILE C 85  ? N ILE B 84  O ILE C 112 ? O ILE B 111 
AA5 5 6 N SER C 115 ? N SER B 114 O MET C 136 ? O MET B 135 
AA5 6 7 N GLY C 135 ? N GLY B 134 O ILE C 151 ? O ILE B 150 
AA5 7 8 N ILE C 148 ? N ILE B 147 O VAL C 176 ? O VAL B 175 
AA6 1 2 N VAL C 278 ? N VAL B 277 O THR C 286 ? O THR B 285 
# 
_pdbx_entry_details.entry_id                   9JHZ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   GLY 
_pdbx_validate_close_contact.auth_seq_id_1    100 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    501 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.15 
# 
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 ALA C 87  ? ? -144.64 47.79   
2  1 PHE C 183 ? ? 53.75   -120.61 
3  1 ALA A 87  ? ? -148.27 49.51   
4  1 ALA A 88  ? ? -98.44  -159.06 
5  1 PHE A 183 ? ? 52.52   -121.18 
6  1 ASP A 281 ? ? -66.49  -114.32 
7  1 ARG A 282 ? ? -143.24 -16.16  
8  1 LYS B 74  ? ? 112.05  -13.93  
9  1 GLU B 75  ? ? -172.79 -130.93 
10 1 ASN B 76  ? ? 61.05   -44.61  
11 1 CYS B 78  ? ? -73.84  47.43   
12 1 ASN B 115 ? ? -91.90  32.21   
13 1 SER B 118 ? ? -153.77 -9.69   
14 1 ASN B 154 ? ? -109.63 51.18   
15 1 PHE B 183 ? ? 53.16   -123.23 
16 1 VAL B 184 ? ? -107.77 -62.52  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG C 282 ? ? 0.134 'SIDE CHAIN' 
2 1 ARG A 282 ? ? 0.117 'SIDE CHAIN' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 318 ? G HOH . 
2 1 A HOH 364 ? G HOH . 
3 1 B HOH 555 ? H HOH . 
# 
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 C LEU 290 ? A LEU 291 
2 1 Y 1 A ALA 0   ? B ALA 1   
3 1 Y 1 A GLN 289 ? B GLN 290 
4 1 Y 1 A LEU 290 ? B LEU 291 
5 1 Y 1 B ALA 0   ? C ALA 1   
6 1 Y 1 B LEU 290 ? C LEU 291 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CAA N1A    N Y N 74  
CAA C2A    C Y N 75  
CAA N3A    N Y N 76  
CAA C4A    C Y N 77  
CAA C5A    C Y N 78  
CAA C6A    C Y N 79  
CAA N6A    N N N 80  
CAA N7A    N Y N 81  
CAA C8A    C Y N 82  
CAA N9A    N Y N 83  
CAA C1B    C N R 84  
CAA C2B    C N R 85  
CAA O2B    O N N 86  
CAA C3B    C N S 87  
CAA O3B    O N N 88  
CAA P3B    P N N 89  
CAA O7A    O N N 90  
CAA O8A    O N N 91  
CAA O9A    O N N 92  
CAA C4B    C N R 93  
CAA O4B    O N N 94  
CAA C5B    C N N 95  
CAA O5B    O N N 96  
CAA P1A    P N R 97  
CAA O1A    O N N 98  
CAA O2A    O N N 99  
CAA O3A    O N N 100 
CAA P2A    P N S 101 
CAA O4A    O N N 102 
CAA O5A    O N N 103 
CAA O6A    O N N 104 
CAA CBP    C N N 105 
CAA CCP    C N N 106 
CAA CDP    C N N 107 
CAA CEP    C N N 108 
CAA CAP    C N R 109 
CAA OAP    O N N 110 
CAA C9P    C N N 111 
CAA O9P    O N N 112 
CAA N8P    N N N 113 
CAA C7P    C N N 114 
CAA C6P    C N N 115 
CAA C5P    C N N 116 
CAA O5P    O N N 117 
CAA N4P    N N N 118 
CAA C3P    C N N 119 
CAA C2P    C N N 120 
CAA S1P    S N N 121 
CAA C1     C N N 122 
CAA O1     O N N 123 
CAA C2     C N N 124 
CAA C3     C N N 125 
CAA O3     O N N 126 
CAA C4     C N N 127 
CAA H2A    H N N 128 
CAA H61A   H N N 129 
CAA H62A   H N N 130 
CAA H8A    H N N 131 
CAA H1B    H N N 132 
CAA H2B    H N N 133 
CAA HO2A   H N N 134 
CAA H3B    H N N 135 
CAA HOA8   H N N 136 
CAA HOA9   H N N 137 
CAA H4B    H N N 138 
CAA H51A   H N N 139 
CAA H52A   H N N 140 
CAA HOA2   H N N 141 
CAA HOA5   H N N 142 
CAA H121   H N N 143 
CAA H122   H N N 144 
CAA H131   H N N 145 
CAA H132   H N N 146 
CAA H133   H N N 147 
CAA H141   H N N 148 
CAA H142   H N N 149 
CAA H143   H N N 150 
CAA H10    H N N 151 
CAA HO1    H N N 152 
CAA HN8    H N N 153 
CAA H71    H N N 154 
CAA H72    H N N 155 
CAA H61    H N N 156 
CAA H62    H N N 157 
CAA HN4    H N N 158 
CAA H31    H N N 159 
CAA H32    H N N 160 
CAA H21    H N N 161 
CAA H22    H N N 162 
CAA "H2'1" H N N 163 
CAA "H2'2" H N N 164 
CAA "H4'1" H N N 165 
CAA "H4'2" H N N 166 
CAA "H4'3" H N N 167 
CYS N      N N N 168 
CYS CA     C N R 169 
CYS C      C N N 170 
CYS O      O N N 171 
CYS CB     C N N 172 
CYS SG     S N N 173 
CYS OXT    O N N 174 
CYS H      H N N 175 
CYS H2     H N N 176 
CYS HA     H N N 177 
CYS HB2    H N N 178 
CYS HB3    H N N 179 
CYS HG     H N N 180 
CYS HXT    H N N 181 
GLN N      N N N 182 
GLN CA     C N S 183 
GLN C      C N N 184 
GLN O      O N N 185 
GLN CB     C N N 186 
GLN CG     C N N 187 
GLN CD     C N N 188 
GLN OE1    O N N 189 
GLN NE2    N N N 190 
GLN OXT    O N N 191 
GLN H      H N N 192 
GLN H2     H N N 193 
GLN HA     H N N 194 
GLN HB2    H N N 195 
GLN HB3    H N N 196 
GLN HG2    H N N 197 
GLN HG3    H N N 198 
GLN HE21   H N N 199 
GLN HE22   H N N 200 
GLN HXT    H N N 201 
GLU N      N N N 202 
GLU CA     C N S 203 
GLU C      C N N 204 
GLU O      O N N 205 
GLU CB     C N N 206 
GLU CG     C N N 207 
GLU CD     C N N 208 
GLU OE1    O N N 209 
GLU OE2    O N N 210 
GLU OXT    O N N 211 
GLU H      H N N 212 
GLU H2     H N N 213 
GLU HA     H N N 214 
GLU HB2    H N N 215 
GLU HB3    H N N 216 
GLU HG2    H N N 217 
GLU HG3    H N N 218 
GLU HE2    H N N 219 
GLU HXT    H N N 220 
GLY N      N N N 221 
GLY CA     C N N 222 
GLY C      C N N 223 
GLY O      O N N 224 
GLY OXT    O N N 225 
GLY H      H N N 226 
GLY H2     H N N 227 
GLY HA2    H N N 228 
GLY HA3    H N N 229 
GLY HXT    H N N 230 
HIS N      N N N 231 
HIS CA     C N S 232 
HIS C      C N N 233 
HIS O      O N N 234 
HIS CB     C N N 235 
HIS CG     C Y N 236 
HIS ND1    N Y N 237 
HIS CD2    C Y N 238 
HIS CE1    C Y N 239 
HIS NE2    N Y N 240 
HIS OXT    O N N 241 
HIS H      H N N 242 
HIS H2     H N N 243 
HIS HA     H N N 244 
HIS HB2    H N N 245 
HIS HB3    H N N 246 
HIS HD1    H N N 247 
HIS HD2    H N N 248 
HIS HE1    H N N 249 
HIS HE2    H N N 250 
HIS HXT    H N N 251 
HOH O      O N N 252 
HOH H1     H N N 253 
HOH H2     H N N 254 
ILE N      N N N 255 
ILE CA     C N S 256 
ILE C      C N N 257 
ILE O      O N N 258 
ILE CB     C N S 259 
ILE CG1    C N N 260 
ILE CG2    C N N 261 
ILE CD1    C N N 262 
ILE OXT    O N N 263 
ILE H      H N N 264 
ILE H2     H N N 265 
ILE HA     H N N 266 
ILE HB     H N N 267 
ILE HG12   H N N 268 
ILE HG13   H N N 269 
ILE HG21   H N N 270 
ILE HG22   H N N 271 
ILE HG23   H N N 272 
ILE HD11   H N N 273 
ILE HD12   H N N 274 
ILE HD13   H N N 275 
ILE HXT    H N N 276 
LEU N      N N N 277 
LEU CA     C N S 278 
LEU C      C N N 279 
LEU O      O N N 280 
LEU CB     C N N 281 
LEU CG     C N N 282 
LEU CD1    C N N 283 
LEU CD2    C N N 284 
LEU OXT    O N N 285 
LEU H      H N N 286 
LEU H2     H N N 287 
LEU HA     H N N 288 
LEU HB2    H N N 289 
LEU HB3    H N N 290 
LEU HG     H N N 291 
LEU HD11   H N N 292 
LEU HD12   H N N 293 
LEU HD13   H N N 294 
LEU HD21   H N N 295 
LEU HD22   H N N 296 
LEU HD23   H N N 297 
LEU HXT    H N N 298 
LYS N      N N N 299 
LYS CA     C N S 300 
LYS C      C N N 301 
LYS O      O N N 302 
LYS CB     C N N 303 
LYS CG     C N N 304 
LYS CD     C N N 305 
LYS CE     C N N 306 
LYS NZ     N N N 307 
LYS OXT    O N N 308 
LYS H      H N N 309 
LYS H2     H N N 310 
LYS HA     H N N 311 
LYS HB2    H N N 312 
LYS HB3    H N N 313 
LYS HG2    H N N 314 
LYS HG3    H N N 315 
LYS HD2    H N N 316 
LYS HD3    H N N 317 
LYS HE2    H N N 318 
LYS HE3    H N N 319 
LYS HZ1    H N N 320 
LYS HZ2    H N N 321 
LYS HZ3    H N N 322 
LYS HXT    H N N 323 
MET N      N N N 324 
MET CA     C N S 325 
MET C      C N N 326 
MET O      O N N 327 
MET CB     C N N 328 
MET CG     C N N 329 
MET SD     S N N 330 
MET CE     C N N 331 
MET OXT    O N N 332 
MET H      H N N 333 
MET H2     H N N 334 
MET HA     H N N 335 
MET HB2    H N N 336 
MET HB3    H N N 337 
MET HG2    H N N 338 
MET HG3    H N N 339 
MET HE1    H N N 340 
MET HE2    H N N 341 
MET HE3    H N N 342 
MET HXT    H N N 343 
NAD PA     P N S 344 
NAD O1A    O N N 345 
NAD O2A    O N N 346 
NAD O5B    O N N 347 
NAD C5B    C N N 348 
NAD C4B    C N R 349 
NAD O4B    O N N 350 
NAD C3B    C N S 351 
NAD O3B    O N N 352 
NAD C2B    C N R 353 
NAD O2B    O N N 354 
NAD C1B    C N R 355 
NAD N9A    N Y N 356 
NAD C8A    C Y N 357 
NAD N7A    N Y N 358 
NAD C5A    C Y N 359 
NAD C6A    C Y N 360 
NAD N6A    N N N 361 
NAD N1A    N Y N 362 
NAD C2A    C Y N 363 
NAD N3A    N Y N 364 
NAD C4A    C Y N 365 
NAD O3     O N N 366 
NAD PN     P N N 367 
NAD O1N    O N N 368 
NAD O2N    O N N 369 
NAD O5D    O N N 370 
NAD C5D    C N N 371 
NAD C4D    C N R 372 
NAD O4D    O N N 373 
NAD C3D    C N S 374 
NAD O3D    O N N 375 
NAD C2D    C N R 376 
NAD O2D    O N N 377 
NAD C1D    C N R 378 
NAD N1N    N Y N 379 
NAD C2N    C Y N 380 
NAD C3N    C Y N 381 
NAD C7N    C N N 382 
NAD O7N    O N N 383 
NAD N7N    N N N 384 
NAD C4N    C Y N 385 
NAD C5N    C Y N 386 
NAD C6N    C Y N 387 
NAD HOA2   H N N 388 
NAD H51A   H N N 389 
NAD H52A   H N N 390 
NAD H4B    H N N 391 
NAD H3B    H N N 392 
NAD HO3A   H N N 393 
NAD H2B    H N N 394 
NAD HO2A   H N N 395 
NAD H1B    H N N 396 
NAD H8A    H N N 397 
NAD H61A   H N N 398 
NAD H62A   H N N 399 
NAD H2A    H N N 400 
NAD H51N   H N N 401 
NAD H52N   H N N 402 
NAD H4D    H N N 403 
NAD H3D    H N N 404 
NAD HO3N   H N N 405 
NAD H2D    H N N 406 
NAD HO2N   H N N 407 
NAD H1D    H N N 408 
NAD H2N    H N N 409 
NAD H71N   H N N 410 
NAD H72N   H N N 411 
NAD H4N    H N N 412 
NAD H5N    H N N 413 
NAD H6N    H N N 414 
PHE N      N N N 415 
PHE CA     C N S 416 
PHE C      C N N 417 
PHE O      O N N 418 
PHE CB     C N N 419 
PHE CG     C Y N 420 
PHE CD1    C Y N 421 
PHE CD2    C Y N 422 
PHE CE1    C Y N 423 
PHE CE2    C Y N 424 
PHE CZ     C Y N 425 
PHE OXT    O N N 426 
PHE H      H N N 427 
PHE H2     H N N 428 
PHE HA     H N N 429 
PHE HB2    H N N 430 
PHE HB3    H N N 431 
PHE HD1    H N N 432 
PHE HD2    H N N 433 
PHE HE1    H N N 434 
PHE HE2    H N N 435 
PHE HZ     H N N 436 
PHE HXT    H N N 437 
PRO N      N N N 438 
PRO CA     C N S 439 
PRO C      C N N 440 
PRO O      O N N 441 
PRO CB     C N N 442 
PRO CG     C N N 443 
PRO CD     C N N 444 
PRO OXT    O N N 445 
PRO H      H N N 446 
PRO HA     H N N 447 
PRO HB2    H N N 448 
PRO HB3    H N N 449 
PRO HG2    H N N 450 
PRO HG3    H N N 451 
PRO HD2    H N N 452 
PRO HD3    H N N 453 
PRO HXT    H N N 454 
SER N      N N N 455 
SER CA     C N S 456 
SER C      C N N 457 
SER O      O N N 458 
SER CB     C N N 459 
SER OG     O N N 460 
SER OXT    O N N 461 
SER H      H N N 462 
SER H2     H N N 463 
SER HA     H N N 464 
SER HB2    H N N 465 
SER HB3    H N N 466 
SER HG     H N N 467 
SER HXT    H N N 468 
THR N      N N N 469 
THR CA     C N S 470 
THR C      C N N 471 
THR O      O N N 472 
THR CB     C N R 473 
THR OG1    O N N 474 
THR CG2    C N N 475 
THR OXT    O N N 476 
THR H      H N N 477 
THR H2     H N N 478 
THR HA     H N N 479 
THR HB     H N N 480 
THR HG1    H N N 481 
THR HG21   H N N 482 
THR HG22   H N N 483 
THR HG23   H N N 484 
THR HXT    H N N 485 
TRP N      N N N 486 
TRP CA     C N S 487 
TRP C      C N N 488 
TRP O      O N N 489 
TRP CB     C N N 490 
TRP CG     C Y N 491 
TRP CD1    C Y N 492 
TRP CD2    C Y N 493 
TRP NE1    N Y N 494 
TRP CE2    C Y N 495 
TRP CE3    C Y N 496 
TRP CZ2    C Y N 497 
TRP CZ3    C Y N 498 
TRP CH2    C Y N 499 
TRP OXT    O N N 500 
TRP H      H N N 501 
TRP H2     H N N 502 
TRP HA     H N N 503 
TRP HB2    H N N 504 
TRP HB3    H N N 505 
TRP HD1    H N N 506 
TRP HE1    H N N 507 
TRP HE3    H N N 508 
TRP HZ2    H N N 509 
TRP HZ3    H N N 510 
TRP HH2    H N N 511 
TRP HXT    H N N 512 
TYR N      N N N 513 
TYR CA     C N S 514 
TYR C      C N N 515 
TYR O      O N N 516 
TYR CB     C N N 517 
TYR CG     C Y N 518 
TYR CD1    C Y N 519 
TYR CD2    C Y N 520 
TYR CE1    C Y N 521 
TYR CE2    C Y N 522 
TYR CZ     C Y N 523 
TYR OH     O N N 524 
TYR OXT    O N N 525 
TYR H      H N N 526 
TYR H2     H N N 527 
TYR HA     H N N 528 
TYR HB2    H N N 529 
TYR HB3    H N N 530 
TYR HD1    H N N 531 
TYR HD2    H N N 532 
TYR HE1    H N N 533 
TYR HE2    H N N 534 
TYR HH     H N N 535 
TYR HXT    H N N 536 
VAL N      N N N 537 
VAL CA     C N S 538 
VAL C      C N N 539 
VAL O      O N N 540 
VAL CB     C N N 541 
VAL CG1    C N N 542 
VAL CG2    C N N 543 
VAL OXT    O N N 544 
VAL H      H N N 545 
VAL H2     H N N 546 
VAL HA     H N N 547 
VAL HB     H N N 548 
VAL HG11   H N N 549 
VAL HG12   H N N 550 
VAL HG13   H N N 551 
VAL HG21   H N N 552 
VAL HG22   H N N 553 
VAL HG23   H N N 554 
VAL HXT    H N N 555 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA     sing N N 1   
ALA N   H      sing N N 2   
ALA N   H2     sing N N 3   
ALA CA  C      sing N N 4   
ALA CA  CB     sing N N 5   
ALA CA  HA     sing N N 6   
ALA C   O      doub N N 7   
ALA C   OXT    sing N N 8   
ALA CB  HB1    sing N N 9   
ALA CB  HB2    sing N N 10  
ALA CB  HB3    sing N N 11  
ALA OXT HXT    sing N N 12  
ARG N   CA     sing N N 13  
ARG N   H      sing N N 14  
ARG N   H2     sing N N 15  
ARG CA  C      sing N N 16  
ARG CA  CB     sing N N 17  
ARG CA  HA     sing N N 18  
ARG C   O      doub N N 19  
ARG C   OXT    sing N N 20  
ARG CB  CG     sing N N 21  
ARG CB  HB2    sing N N 22  
ARG CB  HB3    sing N N 23  
ARG CG  CD     sing N N 24  
ARG CG  HG2    sing N N 25  
ARG CG  HG3    sing N N 26  
ARG CD  NE     sing N N 27  
ARG CD  HD2    sing N N 28  
ARG CD  HD3    sing N N 29  
ARG NE  CZ     sing N N 30  
ARG NE  HE     sing N N 31  
ARG CZ  NH1    sing N N 32  
ARG CZ  NH2    doub N N 33  
ARG NH1 HH11   sing N N 34  
ARG NH1 HH12   sing N N 35  
ARG NH2 HH21   sing N N 36  
ARG NH2 HH22   sing N N 37  
ARG OXT HXT    sing N N 38  
ASN N   CA     sing N N 39  
ASN N   H      sing N N 40  
ASN N   H2     sing N N 41  
ASN CA  C      sing N N 42  
ASN CA  CB     sing N N 43  
ASN CA  HA     sing N N 44  
ASN C   O      doub N N 45  
ASN C   OXT    sing N N 46  
ASN CB  CG     sing N N 47  
ASN CB  HB2    sing N N 48  
ASN CB  HB3    sing N N 49  
ASN CG  OD1    doub N N 50  
ASN CG  ND2    sing N N 51  
ASN ND2 HD21   sing N N 52  
ASN ND2 HD22   sing N N 53  
ASN OXT HXT    sing N N 54  
ASP N   CA     sing N N 55  
ASP N   H      sing N N 56  
ASP N   H2     sing N N 57  
ASP CA  C      sing N N 58  
ASP CA  CB     sing N N 59  
ASP CA  HA     sing N N 60  
ASP C   O      doub N N 61  
ASP C   OXT    sing N N 62  
ASP CB  CG     sing N N 63  
ASP CB  HB2    sing N N 64  
ASP CB  HB3    sing N N 65  
ASP CG  OD1    doub N N 66  
ASP CG  OD2    sing N N 67  
ASP OD2 HD2    sing N N 68  
ASP OXT HXT    sing N N 69  
CAA N1A C2A    sing Y N 70  
CAA N1A C6A    doub Y N 71  
CAA C2A N3A    doub Y N 72  
CAA C2A H2A    sing N N 73  
CAA N3A C4A    sing Y N 74  
CAA C4A C5A    doub Y N 75  
CAA C4A N9A    sing Y N 76  
CAA C5A C6A    sing Y N 77  
CAA C5A N7A    sing Y N 78  
CAA C6A N6A    sing N N 79  
CAA N6A H61A   sing N N 80  
CAA N6A H62A   sing N N 81  
CAA N7A C8A    doub Y N 82  
CAA C8A N9A    sing Y N 83  
CAA C8A H8A    sing N N 84  
CAA N9A C1B    sing N N 85  
CAA C1B C2B    sing N N 86  
CAA C1B O4B    sing N N 87  
CAA C1B H1B    sing N N 88  
CAA C2B O2B    sing N N 89  
CAA C2B C3B    sing N N 90  
CAA C2B H2B    sing N N 91  
CAA O2B HO2A   sing N N 92  
CAA C3B O3B    sing N N 93  
CAA C3B C4B    sing N N 94  
CAA C3B H3B    sing N N 95  
CAA O3B P3B    sing N N 96  
CAA P3B O7A    doub N N 97  
CAA P3B O8A    sing N N 98  
CAA P3B O9A    sing N N 99  
CAA O8A HOA8   sing N N 100 
CAA O9A HOA9   sing N N 101 
CAA C4B O4B    sing N N 102 
CAA C4B C5B    sing N N 103 
CAA C4B H4B    sing N N 104 
CAA C5B O5B    sing N N 105 
CAA C5B H51A   sing N N 106 
CAA C5B H52A   sing N N 107 
CAA O5B P1A    sing N N 108 
CAA P1A O1A    doub N N 109 
CAA P1A O2A    sing N N 110 
CAA P1A O3A    sing N N 111 
CAA O2A HOA2   sing N N 112 
CAA O3A P2A    sing N N 113 
CAA P2A O4A    doub N N 114 
CAA P2A O5A    sing N N 115 
CAA P2A O6A    sing N N 116 
CAA O5A HOA5   sing N N 117 
CAA O6A CCP    sing N N 118 
CAA CBP CCP    sing N N 119 
CAA CBP CDP    sing N N 120 
CAA CBP CEP    sing N N 121 
CAA CBP CAP    sing N N 122 
CAA CCP H121   sing N N 123 
CAA CCP H122   sing N N 124 
CAA CDP H131   sing N N 125 
CAA CDP H132   sing N N 126 
CAA CDP H133   sing N N 127 
CAA CEP H141   sing N N 128 
CAA CEP H142   sing N N 129 
CAA CEP H143   sing N N 130 
CAA CAP OAP    sing N N 131 
CAA CAP C9P    sing N N 132 
CAA CAP H10    sing N N 133 
CAA OAP HO1    sing N N 134 
CAA C9P O9P    doub N N 135 
CAA C9P N8P    sing N N 136 
CAA N8P C7P    sing N N 137 
CAA N8P HN8    sing N N 138 
CAA C7P C6P    sing N N 139 
CAA C7P H71    sing N N 140 
CAA C7P H72    sing N N 141 
CAA C6P C5P    sing N N 142 
CAA C6P H61    sing N N 143 
CAA C6P H62    sing N N 144 
CAA C5P O5P    doub N N 145 
CAA C5P N4P    sing N N 146 
CAA N4P C3P    sing N N 147 
CAA N4P HN4    sing N N 148 
CAA C3P C2P    sing N N 149 
CAA C3P H31    sing N N 150 
CAA C3P H32    sing N N 151 
CAA C2P S1P    sing N N 152 
CAA C2P H21    sing N N 153 
CAA C2P H22    sing N N 154 
CAA S1P C1     sing N N 155 
CAA C1  O1     doub N N 156 
CAA C1  C2     sing N N 157 
CAA C2  C3     sing N N 158 
CAA C2  "H2'1" sing N N 159 
CAA C2  "H2'2" sing N N 160 
CAA C3  O3     doub N N 161 
CAA C3  C4     sing N N 162 
CAA C4  "H4'1" sing N N 163 
CAA C4  "H4'2" sing N N 164 
CAA C4  "H4'3" sing N N 165 
CYS N   CA     sing N N 166 
CYS N   H      sing N N 167 
CYS N   H2     sing N N 168 
CYS CA  C      sing N N 169 
CYS CA  CB     sing N N 170 
CYS CA  HA     sing N N 171 
CYS C   O      doub N N 172 
CYS C   OXT    sing N N 173 
CYS CB  SG     sing N N 174 
CYS CB  HB2    sing N N 175 
CYS CB  HB3    sing N N 176 
CYS SG  HG     sing N N 177 
CYS OXT HXT    sing N N 178 
GLN N   CA     sing N N 179 
GLN N   H      sing N N 180 
GLN N   H2     sing N N 181 
GLN CA  C      sing N N 182 
GLN CA  CB     sing N N 183 
GLN CA  HA     sing N N 184 
GLN C   O      doub N N 185 
GLN C   OXT    sing N N 186 
GLN CB  CG     sing N N 187 
GLN CB  HB2    sing N N 188 
GLN CB  HB3    sing N N 189 
GLN CG  CD     sing N N 190 
GLN CG  HG2    sing N N 191 
GLN CG  HG3    sing N N 192 
GLN CD  OE1    doub N N 193 
GLN CD  NE2    sing N N 194 
GLN NE2 HE21   sing N N 195 
GLN NE2 HE22   sing N N 196 
GLN OXT HXT    sing N N 197 
GLU N   CA     sing N N 198 
GLU N   H      sing N N 199 
GLU N   H2     sing N N 200 
GLU CA  C      sing N N 201 
GLU CA  CB     sing N N 202 
GLU CA  HA     sing N N 203 
GLU C   O      doub N N 204 
GLU C   OXT    sing N N 205 
GLU CB  CG     sing N N 206 
GLU CB  HB2    sing N N 207 
GLU CB  HB3    sing N N 208 
GLU CG  CD     sing N N 209 
GLU CG  HG2    sing N N 210 
GLU CG  HG3    sing N N 211 
GLU CD  OE1    doub N N 212 
GLU CD  OE2    sing N N 213 
GLU OE2 HE2    sing N N 214 
GLU OXT HXT    sing N N 215 
GLY N   CA     sing N N 216 
GLY N   H      sing N N 217 
GLY N   H2     sing N N 218 
GLY CA  C      sing N N 219 
GLY CA  HA2    sing N N 220 
GLY CA  HA3    sing N N 221 
GLY C   O      doub N N 222 
GLY C   OXT    sing N N 223 
GLY OXT HXT    sing N N 224 
HIS N   CA     sing N N 225 
HIS N   H      sing N N 226 
HIS N   H2     sing N N 227 
HIS CA  C      sing N N 228 
HIS CA  CB     sing N N 229 
HIS CA  HA     sing N N 230 
HIS C   O      doub N N 231 
HIS C   OXT    sing N N 232 
HIS CB  CG     sing N N 233 
HIS CB  HB2    sing N N 234 
HIS CB  HB3    sing N N 235 
HIS CG  ND1    sing Y N 236 
HIS CG  CD2    doub Y N 237 
HIS ND1 CE1    doub Y N 238 
HIS ND1 HD1    sing N N 239 
HIS CD2 NE2    sing Y N 240 
HIS CD2 HD2    sing N N 241 
HIS CE1 NE2    sing Y N 242 
HIS CE1 HE1    sing N N 243 
HIS NE2 HE2    sing N N 244 
HIS OXT HXT    sing N N 245 
HOH O   H1     sing N N 246 
HOH O   H2     sing N N 247 
ILE N   CA     sing N N 248 
ILE N   H      sing N N 249 
ILE N   H2     sing N N 250 
ILE CA  C      sing N N 251 
ILE CA  CB     sing N N 252 
ILE CA  HA     sing N N 253 
ILE C   O      doub N N 254 
ILE C   OXT    sing N N 255 
ILE CB  CG1    sing N N 256 
ILE CB  CG2    sing N N 257 
ILE CB  HB     sing N N 258 
ILE CG1 CD1    sing N N 259 
ILE CG1 HG12   sing N N 260 
ILE CG1 HG13   sing N N 261 
ILE CG2 HG21   sing N N 262 
ILE CG2 HG22   sing N N 263 
ILE CG2 HG23   sing N N 264 
ILE CD1 HD11   sing N N 265 
ILE CD1 HD12   sing N N 266 
ILE CD1 HD13   sing N N 267 
ILE OXT HXT    sing N N 268 
LEU N   CA     sing N N 269 
LEU N   H      sing N N 270 
LEU N   H2     sing N N 271 
LEU CA  C      sing N N 272 
LEU CA  CB     sing N N 273 
LEU CA  HA     sing N N 274 
LEU C   O      doub N N 275 
LEU C   OXT    sing N N 276 
LEU CB  CG     sing N N 277 
LEU CB  HB2    sing N N 278 
LEU CB  HB3    sing N N 279 
LEU CG  CD1    sing N N 280 
LEU CG  CD2    sing N N 281 
LEU CG  HG     sing N N 282 
LEU CD1 HD11   sing N N 283 
LEU CD1 HD12   sing N N 284 
LEU CD1 HD13   sing N N 285 
LEU CD2 HD21   sing N N 286 
LEU CD2 HD22   sing N N 287 
LEU CD2 HD23   sing N N 288 
LEU OXT HXT    sing N N 289 
LYS N   CA     sing N N 290 
LYS N   H      sing N N 291 
LYS N   H2     sing N N 292 
LYS CA  C      sing N N 293 
LYS CA  CB     sing N N 294 
LYS CA  HA     sing N N 295 
LYS C   O      doub N N 296 
LYS C   OXT    sing N N 297 
LYS CB  CG     sing N N 298 
LYS CB  HB2    sing N N 299 
LYS CB  HB3    sing N N 300 
LYS CG  CD     sing N N 301 
LYS CG  HG2    sing N N 302 
LYS CG  HG3    sing N N 303 
LYS CD  CE     sing N N 304 
LYS CD  HD2    sing N N 305 
LYS CD  HD3    sing N N 306 
LYS CE  NZ     sing N N 307 
LYS CE  HE2    sing N N 308 
LYS CE  HE3    sing N N 309 
LYS NZ  HZ1    sing N N 310 
LYS NZ  HZ2    sing N N 311 
LYS NZ  HZ3    sing N N 312 
LYS OXT HXT    sing N N 313 
MET N   CA     sing N N 314 
MET N   H      sing N N 315 
MET N   H2     sing N N 316 
MET CA  C      sing N N 317 
MET CA  CB     sing N N 318 
MET CA  HA     sing N N 319 
MET C   O      doub N N 320 
MET C   OXT    sing N N 321 
MET CB  CG     sing N N 322 
MET CB  HB2    sing N N 323 
MET CB  HB3    sing N N 324 
MET CG  SD     sing N N 325 
MET CG  HG2    sing N N 326 
MET CG  HG3    sing N N 327 
MET SD  CE     sing N N 328 
MET CE  HE1    sing N N 329 
MET CE  HE2    sing N N 330 
MET CE  HE3    sing N N 331 
MET OXT HXT    sing N N 332 
NAD PA  O1A    doub N N 333 
NAD PA  O2A    sing N N 334 
NAD PA  O5B    sing N N 335 
NAD PA  O3     sing N N 336 
NAD O2A HOA2   sing N N 337 
NAD O5B C5B    sing N N 338 
NAD C5B C4B    sing N N 339 
NAD C5B H51A   sing N N 340 
NAD C5B H52A   sing N N 341 
NAD C4B O4B    sing N N 342 
NAD C4B C3B    sing N N 343 
NAD C4B H4B    sing N N 344 
NAD O4B C1B    sing N N 345 
NAD C3B O3B    sing N N 346 
NAD C3B C2B    sing N N 347 
NAD C3B H3B    sing N N 348 
NAD O3B HO3A   sing N N 349 
NAD C2B O2B    sing N N 350 
NAD C2B C1B    sing N N 351 
NAD C2B H2B    sing N N 352 
NAD O2B HO2A   sing N N 353 
NAD C1B N9A    sing N N 354 
NAD C1B H1B    sing N N 355 
NAD N9A C8A    sing Y N 356 
NAD N9A C4A    sing Y N 357 
NAD C8A N7A    doub Y N 358 
NAD C8A H8A    sing N N 359 
NAD N7A C5A    sing Y N 360 
NAD C5A C6A    sing Y N 361 
NAD C5A C4A    doub Y N 362 
NAD C6A N6A    sing N N 363 
NAD C6A N1A    doub Y N 364 
NAD N6A H61A   sing N N 365 
NAD N6A H62A   sing N N 366 
NAD N1A C2A    sing Y N 367 
NAD C2A N3A    doub Y N 368 
NAD C2A H2A    sing N N 369 
NAD N3A C4A    sing Y N 370 
NAD O3  PN     sing N N 371 
NAD PN  O1N    doub N N 372 
NAD PN  O2N    sing N N 373 
NAD PN  O5D    sing N N 374 
NAD O5D C5D    sing N N 375 
NAD C5D C4D    sing N N 376 
NAD C5D H51N   sing N N 377 
NAD C5D H52N   sing N N 378 
NAD C4D O4D    sing N N 379 
NAD C4D C3D    sing N N 380 
NAD C4D H4D    sing N N 381 
NAD O4D C1D    sing N N 382 
NAD C3D O3D    sing N N 383 
NAD C3D C2D    sing N N 384 
NAD C3D H3D    sing N N 385 
NAD O3D HO3N   sing N N 386 
NAD C2D O2D    sing N N 387 
NAD C2D C1D    sing N N 388 
NAD C2D H2D    sing N N 389 
NAD O2D HO2N   sing N N 390 
NAD C1D N1N    sing N N 391 
NAD C1D H1D    sing N N 392 
NAD N1N C2N    sing Y N 393 
NAD N1N C6N    doub Y N 394 
NAD C2N C3N    doub Y N 395 
NAD C2N H2N    sing N N 396 
NAD C3N C7N    sing N N 397 
NAD C3N C4N    sing Y N 398 
NAD C7N O7N    doub N N 399 
NAD C7N N7N    sing N N 400 
NAD N7N H71N   sing N N 401 
NAD N7N H72N   sing N N 402 
NAD C4N C5N    doub Y N 403 
NAD C4N H4N    sing N N 404 
NAD C5N C6N    sing Y N 405 
NAD C5N H5N    sing N N 406 
NAD C6N H6N    sing N N 407 
PHE N   CA     sing N N 408 
PHE N   H      sing N N 409 
PHE N   H2     sing N N 410 
PHE CA  C      sing N N 411 
PHE CA  CB     sing N N 412 
PHE CA  HA     sing N N 413 
PHE C   O      doub N N 414 
PHE C   OXT    sing N N 415 
PHE CB  CG     sing N N 416 
PHE CB  HB2    sing N N 417 
PHE CB  HB3    sing N N 418 
PHE CG  CD1    doub Y N 419 
PHE CG  CD2    sing Y N 420 
PHE CD1 CE1    sing Y N 421 
PHE CD1 HD1    sing N N 422 
PHE CD2 CE2    doub Y N 423 
PHE CD2 HD2    sing N N 424 
PHE CE1 CZ     doub Y N 425 
PHE CE1 HE1    sing N N 426 
PHE CE2 CZ     sing Y N 427 
PHE CE2 HE2    sing N N 428 
PHE CZ  HZ     sing N N 429 
PHE OXT HXT    sing N N 430 
PRO N   CA     sing N N 431 
PRO N   CD     sing N N 432 
PRO N   H      sing N N 433 
PRO CA  C      sing N N 434 
PRO CA  CB     sing N N 435 
PRO CA  HA     sing N N 436 
PRO C   O      doub N N 437 
PRO C   OXT    sing N N 438 
PRO CB  CG     sing N N 439 
PRO CB  HB2    sing N N 440 
PRO CB  HB3    sing N N 441 
PRO CG  CD     sing N N 442 
PRO CG  HG2    sing N N 443 
PRO CG  HG3    sing N N 444 
PRO CD  HD2    sing N N 445 
PRO CD  HD3    sing N N 446 
PRO OXT HXT    sing N N 447 
SER N   CA     sing N N 448 
SER N   H      sing N N 449 
SER N   H2     sing N N 450 
SER CA  C      sing N N 451 
SER CA  CB     sing N N 452 
SER CA  HA     sing N N 453 
SER C   O      doub N N 454 
SER C   OXT    sing N N 455 
SER CB  OG     sing N N 456 
SER CB  HB2    sing N N 457 
SER CB  HB3    sing N N 458 
SER OG  HG     sing N N 459 
SER OXT HXT    sing N N 460 
THR N   CA     sing N N 461 
THR N   H      sing N N 462 
THR N   H2     sing N N 463 
THR CA  C      sing N N 464 
THR CA  CB     sing N N 465 
THR CA  HA     sing N N 466 
THR C   O      doub N N 467 
THR C   OXT    sing N N 468 
THR CB  OG1    sing N N 469 
THR CB  CG2    sing N N 470 
THR CB  HB     sing N N 471 
THR OG1 HG1    sing N N 472 
THR CG2 HG21   sing N N 473 
THR CG2 HG22   sing N N 474 
THR CG2 HG23   sing N N 475 
THR OXT HXT    sing N N 476 
TRP N   CA     sing N N 477 
TRP N   H      sing N N 478 
TRP N   H2     sing N N 479 
TRP CA  C      sing N N 480 
TRP CA  CB     sing N N 481 
TRP CA  HA     sing N N 482 
TRP C   O      doub N N 483 
TRP C   OXT    sing N N 484 
TRP CB  CG     sing N N 485 
TRP CB  HB2    sing N N 486 
TRP CB  HB3    sing N N 487 
TRP CG  CD1    doub Y N 488 
TRP CG  CD2    sing Y N 489 
TRP CD1 NE1    sing Y N 490 
TRP CD1 HD1    sing N N 491 
TRP CD2 CE2    doub Y N 492 
TRP CD2 CE3    sing Y N 493 
TRP NE1 CE2    sing Y N 494 
TRP NE1 HE1    sing N N 495 
TRP CE2 CZ2    sing Y N 496 
TRP CE3 CZ3    doub Y N 497 
TRP CE3 HE3    sing N N 498 
TRP CZ2 CH2    doub Y N 499 
TRP CZ2 HZ2    sing N N 500 
TRP CZ3 CH2    sing Y N 501 
TRP CZ3 HZ3    sing N N 502 
TRP CH2 HH2    sing N N 503 
TRP OXT HXT    sing N N 504 
TYR N   CA     sing N N 505 
TYR N   H      sing N N 506 
TYR N   H2     sing N N 507 
TYR CA  C      sing N N 508 
TYR CA  CB     sing N N 509 
TYR CA  HA     sing N N 510 
TYR C   O      doub N N 511 
TYR C   OXT    sing N N 512 
TYR CB  CG     sing N N 513 
TYR CB  HB2    sing N N 514 
TYR CB  HB3    sing N N 515 
TYR CG  CD1    doub Y N 516 
TYR CG  CD2    sing Y N 517 
TYR CD1 CE1    sing Y N 518 
TYR CD1 HD1    sing N N 519 
TYR CD2 CE2    doub Y N 520 
TYR CD2 HD2    sing N N 521 
TYR CE1 CZ     doub Y N 522 
TYR CE1 HE1    sing N N 523 
TYR CE2 CZ     sing Y N 524 
TYR CE2 HE2    sing N N 525 
TYR CZ  OH     sing N N 526 
TYR OH  HH     sing N N 527 
TYR OXT HXT    sing N N 528 
VAL N   CA     sing N N 529 
VAL N   H      sing N N 530 
VAL N   H2     sing N N 531 
VAL CA  C      sing N N 532 
VAL CA  CB     sing N N 533 
VAL CA  HA     sing N N 534 
VAL C   O      doub N N 535 
VAL C   OXT    sing N N 536 
VAL CB  CG1    sing N N 537 
VAL CB  CG2    sing N N 538 
VAL CB  HB     sing N N 539 
VAL CG1 HG11   sing N N 540 
VAL CG1 HG12   sing N N 541 
VAL CG1 HG13   sing N N 542 
VAL CG2 HG21   sing N N 543 
VAL CG2 HG22   sing N N 544 
VAL CG2 HG23   sing N N 545 
VAL OXT HXT    sing N N 546 
# 
_pdbx_audit_support.funding_organization   'National Research Foundation (NRF, Korea)' 
_pdbx_audit_support.country                'Korea, Republic Of' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4KUE 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JHZ 
_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]   0.011042 
_atom_sites.fract_transf_matrix[1][2]   0.006375 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012750 
_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]   0.004706 
_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   . ALA A 1 1   ? -32.527 13.764  -28.484 1.00 58.57  ? 0   ALA C N   1 
ATOM   2    C CA  . ALA A 1 1   ? -32.630 14.570  -29.696 1.00 60.40  ? 0   ALA C CA  1 
ATOM   3    C C   . ALA A 1 1   ? -32.466 16.057  -29.385 1.00 53.34  ? 0   ALA C C   1 
ATOM   4    O O   . ALA A 1 1   ? -33.343 16.668  -28.771 1.00 49.68  ? 0   ALA C O   1 
ATOM   5    C CB  . ALA A 1 1   ? -33.966 14.315  -30.388 1.00 47.83  ? 0   ALA C CB  1 
ATOM   6    N N   . MET A 1 2   ? -31.341 16.635  -29.809 1.00 47.92  ? 1   MET C N   1 
ATOM   7    C CA  . MET A 1 2   ? -31.084 18.053  -29.594 1.00 47.25  ? 1   MET C CA  1 
ATOM   8    C C   . MET A 1 2   ? -30.109 18.589  -30.637 1.00 39.52  ? 1   MET C C   1 
ATOM   9    O O   . MET A 1 2   ? -29.118 17.933  -30.971 1.00 31.39  ? 1   MET C O   1 
ATOM   10   C CB  . MET A 1 2   ? -30.537 18.309  -28.187 1.00 42.54  ? 1   MET C CB  1 
ATOM   11   C CG  . MET A 1 2   ? -30.541 19.772  -27.804 1.00 44.44  ? 1   MET C CG  1 
ATOM   12   S SD  . MET A 1 2   ? -29.807 20.082  -26.193 1.00 53.48  ? 1   MET C SD  1 
ATOM   13   C CE  . MET A 1 2   ? -30.675 21.585  -25.756 1.00 38.38  ? 1   MET C CE  1 
ATOM   14   N N   . LYS A 1 3   ? -30.397 19.791  -31.134 1.00 35.16  ? 2   LYS C N   1 
ATOM   15   C CA  . LYS A 1 3   ? -29.552 20.493  -32.092 1.00 31.16  ? 2   LYS C CA  1 
ATOM   16   C C   . LYS A 1 3   ? -28.849 21.638  -31.372 1.00 37.86  ? 2   LYS C C   1 
ATOM   17   O O   . LYS A 1 3   ? -29.510 22.518  -30.810 1.00 36.91  ? 2   LYS C O   1 
ATOM   18   C CB  . LYS A 1 3   ? -30.382 21.020  -33.262 1.00 43.96  ? 2   LYS C CB  1 
ATOM   19   C CG  . LYS A 1 3   ? -30.591 20.015  -34.383 1.00 60.39  ? 2   LYS C CG  1 
ATOM   20   C CD  . LYS A 1 3   ? -30.501 20.685  -35.746 1.00 67.32  ? 2   LYS C CD  1 
ATOM   21   C CE  . LYS A 1 3   ? -29.977 19.725  -36.803 1.00 60.70  ? 2   LYS C CE  1 
ATOM   22   N NZ  . LYS A 1 3   ? -29.897 20.380  -38.138 1.00 48.89  ? 2   LYS C NZ  1 
ATOM   23   N N   . ILE A 1 4   ? -27.517 21.630  -31.394 1.00 35.11  ? 3   ILE C N   1 
ATOM   24   C CA  . ILE A 1 4   ? -26.706 22.590  -30.652 1.00 35.19  ? 3   ILE C CA  1 
ATOM   25   C C   . ILE A 1 4   ? -25.856 23.386  -31.630 1.00 34.16  ? 3   ILE C C   1 
ATOM   26   O O   . ILE A 1 4   ? -25.142 22.805  -32.455 1.00 34.80  ? 3   ILE C O   1 
ATOM   27   C CB  . ILE A 1 4   ? -25.807 21.892  -29.615 1.00 35.08  ? 3   ILE C CB  1 
ATOM   28   C CG1 . ILE A 1 4   ? -26.656 21.196  -28.552 1.00 32.82  ? 3   ILE C CG1 1 
ATOM   29   C CG2 . ILE A 1 4   ? -24.852 22.894  -28.983 1.00 28.67  ? 3   ILE C CG2 1 
ATOM   30   C CD1 . ILE A 1 4   ? -26.692 19.693  -28.702 1.00 34.88  ? 3   ILE C CD1 1 
ATOM   31   N N   . GLY A 1 5   ? -25.917 24.712  -31.522 1.00 33.10  ? 4   GLY C N   1 
ATOM   32   C CA  . GLY A 1 5   ? -25.047 25.575  -32.296 1.00 25.95  ? 4   GLY C CA  1 
ATOM   33   C C   . GLY A 1 5   ? -23.937 26.194  -31.466 1.00 35.19  ? 4   GLY C C   1 
ATOM   34   O O   . GLY A 1 5   ? -24.202 26.868  -30.465 1.00 32.58  ? 4   GLY C O   1 
ATOM   35   N N   . VAL A 1 6   ? -22.691 25.969  -31.873 1.00 27.57  ? 5   VAL C N   1 
ATOM   36   C CA  . VAL A 1 6   ? -21.512 26.504  -31.199 1.00 36.29  ? 5   VAL C CA  1 
ATOM   37   C C   . VAL A 1 6   ? -20.924 27.597  -32.084 1.00 35.57  ? 5   VAL C C   1 
ATOM   38   O O   . VAL A 1 6   ? -20.480 27.323  -33.205 1.00 35.61  ? 5   VAL C O   1 
ATOM   39   C CB  . VAL A 1 6   ? -20.474 25.403  -30.926 1.00 33.80  ? 5   VAL C CB  1 
ATOM   40   C CG1 . VAL A 1 6   ? -19.176 26.004  -30.399 1.00 26.16  ? 5   VAL C CG1 1 
ATOM   41   C CG2 . VAL A 1 6   ? -21.034 24.367  -29.969 1.00 30.84  ? 5   VAL C CG2 1 
ATOM   42   N N   . ILE A 1 7   ? -20.908 28.830  -31.586 1.00 39.74  ? 6   ILE C N   1 
ATOM   43   C CA  . ILE A 1 7   ? -20.458 29.984  -32.361 1.00 31.92  ? 6   ILE C CA  1 
ATOM   44   C C   . ILE A 1 7   ? -19.010 30.273  -31.987 1.00 32.24  ? 6   ILE C C   1 
ATOM   45   O O   . ILE A 1 7   ? -18.727 30.763  -30.888 1.00 31.10  ? 6   ILE C O   1 
ATOM   46   C CB  . ILE A 1 7   ? -21.343 31.212  -32.121 1.00 36.76  ? 6   ILE C CB  1 
ATOM   47   C CG1 . ILE A 1 7   ? -22.824 30.824  -32.125 1.00 28.36  ? 6   ILE C CG1 1 
ATOM   48   C CG2 . ILE A 1 7   ? -21.060 32.272  -33.174 1.00 25.95  ? 6   ILE C CG2 1 
ATOM   49   C CD1 . ILE A 1 7   ? -23.305 30.241  -33.427 1.00 25.74  ? 6   ILE C CD1 1 
ATOM   50   N N   . GLY A 1 8   ? -18.091 29.995  -32.908 1.00 29.97  ? 7   GLY C N   1 
ATOM   51   C CA  . GLY A 1 8   ? -16.673 30.131  -32.637 1.00 28.38  ? 7   GLY C CA  1 
ATOM   52   C C   . GLY A 1 8   ? -15.956 28.805  -32.774 1.00 35.94  ? 7   GLY C C   1 
ATOM   53   O O   . GLY A 1 8   ? -16.282 27.848  -32.067 1.00 42.12  ? 7   GLY C O   1 
ATOM   54   N N   . ALA A 1 9   ? -14.985 28.725  -33.682 1.00 37.32  ? 8   ALA C N   1 
ATOM   55   C CA  . ALA A 1 9   ? -14.326 27.464  -33.998 1.00 31.11  ? 8   ALA C CA  1 
ATOM   56   C C   . ALA A 1 9   ? -12.914 27.370  -33.435 1.00 34.51  ? 8   ALA C C   1 
ATOM   57   O O   . ALA A 1 9   ? -12.158 26.477  -33.834 1.00 32.43  ? 8   ALA C O   1 
ATOM   58   C CB  . ALA A 1 9   ? -14.300 27.251  -35.513 1.00 30.56  ? 8   ALA C CB  1 
ATOM   59   N N   . GLY A 1 10  ? -12.539 28.259  -32.519 1.00 30.77  ? 9   GLY C N   1 
ATOM   60   C CA  . GLY A 1 10  ? -11.224 28.201  -31.909 1.00 31.48  ? 9   GLY C CA  1 
ATOM   61   C C   . GLY A 1 10  ? -11.077 27.055  -30.927 1.00 32.14  ? 9   GLY C C   1 
ATOM   62   O O   . GLY A 1 10  ? -11.812 26.066  -31.007 1.00 34.91  ? 9   GLY C O   1 
ATOM   63   N N   . THR A 1 11  ? -10.136 27.179  -29.989 1.00 37.48  ? 10  THR C N   1 
ATOM   64   C CA  . THR A 1 11  ? -9.884  26.103  -29.035 1.00 36.60  ? 10  THR C CA  1 
ATOM   65   C C   . THR A 1 11  ? -11.142 25.754  -28.249 1.00 36.92  ? 10  THR C C   1 
ATOM   66   O O   . THR A 1 11  ? -11.605 24.607  -28.263 1.00 32.47  ? 10  THR C O   1 
ATOM   67   C CB  . THR A 1 11  ? -8.756  26.496  -28.079 1.00 41.84  ? 10  THR C CB  1 
ATOM   68   O OG1 . THR A 1 11  ? -7.607  26.907  -28.829 1.00 46.20  ? 10  THR C OG1 1 
ATOM   69   C CG2 . THR A 1 11  ? -8.383  25.317  -27.189 1.00 37.25  ? 10  THR C CG2 1 
ATOM   70   N N   . MET A 1 12  ? -11.715 26.743  -27.558 1.00 36.11  ? 11  MET C N   1 
ATOM   71   C CA  . MET A 1 12  ? -12.860 26.474  -26.695 1.00 33.69  ? 11  MET C CA  1 
ATOM   72   C C   . MET A 1 12  ? -14.068 26.009  -27.498 1.00 34.71  ? 11  MET C C   1 
ATOM   73   O O   . MET A 1 12  ? -14.778 25.087  -27.078 1.00 28.46  ? 11  MET C O   1 
ATOM   74   C CB  . MET A 1 12  ? -13.197 27.719  -25.875 1.00 39.36  ? 11  MET C CB  1 
ATOM   75   C CG  . MET A 1 12  ? -12.202 28.005  -24.757 1.00 36.90  ? 11  MET C CG  1 
ATOM   76   S SD  . MET A 1 12  ? -11.824 26.552  -23.750 1.00 71.45  ? 11  MET C SD  1 
ATOM   77   C CE  . MET A 1 12  ? -13.446 26.149  -23.091 1.00 37.44  ? 11  MET C CE  1 
ATOM   78   N N   . GLY A 1 13  ? -14.313 26.626  -28.656 1.00 31.96  ? 12  GLY C N   1 
ATOM   79   C CA  . GLY A 1 13  ? -15.438 26.209  -29.476 1.00 30.72  ? 12  GLY C CA  1 
ATOM   80   C C   . GLY A 1 13  ? -15.338 24.760  -29.914 1.00 32.98  ? 12  GLY C C   1 
ATOM   81   O O   . GLY A 1 13  ? -16.337 24.035  -29.930 1.00 32.63  ? 12  GLY C O   1 
ATOM   82   N N   . GLN A 1 14  ? -14.129 24.316  -30.270 1.00 27.15  ? 13  GLN C N   1 
ATOM   83   C CA  . GLN A 1 14  ? -13.931 22.920  -30.647 1.00 33.99  ? 13  GLN C CA  1 
ATOM   84   C C   . GLN A 1 14  ? -14.259 21.988  -29.488 1.00 32.94  ? 13  GLN C C   1 
ATOM   85   O O   . GLN A 1 14  ? -14.972 20.992  -29.659 1.00 34.29  ? 13  GLN C O   1 
ATOM   86   C CB  . GLN A 1 14  ? -12.494 22.699  -31.115 1.00 33.13  ? 13  GLN C CB  1 
ATOM   87   C CG  . GLN A 1 14  ? -12.167 23.289  -32.470 1.00 37.14  ? 13  GLN C CG  1 
ATOM   88   C CD  . GLN A 1 14  ? -10.676 23.509  -32.646 1.00 34.42  ? 13  GLN C CD  1 
ATOM   89   O OE1 . GLN A 1 14  ? -9.864  22.717  -32.168 1.00 34.04  ? 13  GLN C OE1 1 
ATOM   90   N NE2 . GLN A 1 14  ? -10.310 24.585  -33.330 1.00 29.24  ? 13  GLN C NE2 1 
ATOM   91   N N   . GLY A 1 15  ? -13.741 22.295  -28.296 1.00 32.82  ? 14  GLY C N   1 
ATOM   92   C CA  . GLY A 1 15  ? -13.994 21.442  -27.146 1.00 33.09  ? 14  GLY C CA  1 
ATOM   93   C C   . GLY A 1 15  ? -15.455 21.392  -26.746 1.00 33.40  ? 14  GLY C C   1 
ATOM   94   O O   . GLY A 1 15  ? -15.947 20.348  -26.307 1.00 35.75  ? 14  GLY C O   1 
ATOM   95   N N   . ILE A 1 16  ? -16.167 22.513  -26.886 1.00 31.38  ? 15  ILE C N   1 
ATOM   96   C CA  . ILE A 1 16  ? -17.593 22.540  -26.576 1.00 23.95  ? 15  ILE C CA  1 
ATOM   97   C C   . ILE A 1 16  ? -18.377 21.726  -27.598 1.00 31.58  ? 15  ILE C C   1 
ATOM   98   O O   . ILE A 1 16  ? -19.297 20.977  -27.244 1.00 34.16  ? 15  ILE C O   1 
ATOM   99   C CB  . ILE A 1 16  ? -18.085 23.996  -26.503 1.00 30.76  ? 15  ILE C CB  1 
ATOM   100  C CG1 . ILE A 1 16  ? -17.581 24.658  -25.220 1.00 26.75  ? 15  ILE C CG1 1 
ATOM   101  C CG2 . ILE A 1 16  ? -19.604 24.068  -26.599 1.00 24.30  ? 15  ILE C CG2 1 
ATOM   102  C CD1 . ILE A 1 16  ? -17.666 26.167  -25.249 1.00 35.16  ? 15  ILE C CD1 1 
ATOM   103  N N   . ALA A 1 17  ? -18.030 21.862  -28.880 1.00 31.52  ? 16  ALA C N   1 
ATOM   104  C CA  . ALA A 1 17  ? -18.656 21.042  -29.910 1.00 30.64  ? 16  ALA C CA  1 
ATOM   105  C C   . ALA A 1 17  ? -18.448 19.560  -29.626 1.00 31.60  ? 16  ALA C C   1 
ATOM   106  O O   . ALA A 1 17  ? -19.379 18.756  -29.755 1.00 26.98  ? 16  ALA C O   1 
ATOM   107  C CB  . ALA A 1 17  ? -18.096 21.413  -31.284 1.00 29.10  ? 16  ALA C CB  1 
ATOM   108  N N   . LYS A 1 18  ? -17.231 19.186  -29.222 1.00 28.03  ? 17  LYS C N   1 
ATOM   109  C CA  . LYS A 1 18  ? -16.955 17.798  -28.868 1.00 28.84  ? 17  LYS C CA  1 
ATOM   110  C C   . LYS A 1 18  ? -17.759 17.368  -27.645 1.00 35.81  ? 17  LYS C C   1 
ATOM   111  O O   . LYS A 1 18  ? -18.193 16.213  -27.556 1.00 32.80  ? 17  LYS C O   1 
ATOM   112  C CB  . LYS A 1 18  ? -15.459 17.614  -28.615 1.00 28.68  ? 17  LYS C CB  1 
ATOM   113  C CG  . LYS A 1 18  ? -14.603 17.665  -29.865 1.00 28.34  ? 17  LYS C CG  1 
ATOM   114  C CD  . LYS A 1 18  ? -13.193 17.167  -29.589 1.00 30.94  ? 17  LYS C CD  1 
ATOM   115  C CE  . LYS A 1 18  ? -12.269 18.292  -29.169 1.00 39.21  ? 17  LYS C CE  1 
ATOM   116  N NZ  . LYS A 1 18  ? -10.858 17.828  -29.154 1.00 38.42  ? 17  LYS C NZ  1 
ATOM   117  N N   . ALA A 1 19  ? -17.968 18.283  -26.691 1.00 33.69  ? 18  ALA C N   1 
ATOM   118  C CA  . ALA A 1 19  ? -18.682 17.928  -25.469 1.00 29.38  ? 18  ALA C CA  1 
ATOM   119  C C   . ALA A 1 19  ? -20.121 17.526  -25.765 1.00 26.92  ? 18  ALA C C   1 
ATOM   120  O O   . ALA A 1 19  ? -20.641 16.569  -25.178 1.00 39.35  ? 18  ALA C O   1 
ATOM   121  C CB  . ALA A 1 19  ? -18.642 19.093  -24.481 1.00 32.94  ? 18  ALA C CB  1 
ATOM   122  N N   . PHE A 1 20  ? -20.780 18.240  -26.676 1.00 28.91  ? 19  PHE C N   1 
ATOM   123  C CA  . PHE A 1 20  ? -22.147 17.899  -27.047 1.00 26.24  ? 19  PHE C CA  1 
ATOM   124  C C   . PHE A 1 20  ? -22.195 16.706  -27.997 1.00 32.66  ? 19  PHE C C   1 
ATOM   125  O O   . PHE A 1 20  ? -23.074 15.847  -27.869 1.00 35.28  ? 19  PHE C O   1 
ATOM   126  C CB  . PHE A 1 20  ? -22.834 19.111  -27.677 1.00 31.38  ? 19  PHE C CB  1 
ATOM   127  C CG  . PHE A 1 20  ? -23.259 20.146  -26.679 1.00 33.16  ? 19  PHE C CG  1 
ATOM   128  C CD1 . PHE A 1 20  ? -24.426 19.985  -25.951 1.00 33.78  ? 19  PHE C CD1 1 
ATOM   129  C CD2 . PHE A 1 20  ? -22.486 21.275  -26.461 1.00 30.29  ? 19  PHE C CD2 1 
ATOM   130  C CE1 . PHE A 1 20  ? -24.819 20.936  -25.024 1.00 33.56  ? 19  PHE C CE1 1 
ATOM   131  C CE2 . PHE A 1 20  ? -22.872 22.229  -25.535 1.00 27.76  ? 19  PHE C CE2 1 
ATOM   132  C CZ  . PHE A 1 20  ? -24.039 22.058  -24.817 1.00 36.55  ? 19  PHE C CZ  1 
ATOM   133  N N   . ALA A 1 21  ? -21.252 16.629  -28.943 1.00 29.61  ? 20  ALA C N   1 
ATOM   134  C CA  . ALA A 1 21  ? -21.272 15.568  -29.945 1.00 34.21  ? 20  ALA C CA  1 
ATOM   135  C C   . ALA A 1 21  ? -20.963 14.198  -29.358 1.00 35.29  ? 20  ALA C C   1 
ATOM   136  O O   . ALA A 1 21  ? -21.274 13.186  -29.990 1.00 32.67  ? 20  ALA C O   1 
ATOM   137  C CB  . ALA A 1 21  ? -20.279 15.882  -31.064 1.00 30.04  ? 20  ALA C CB  1 
ATOM   138  N N   . GLN A 1 22  ? -20.345 14.143  -28.177 1.00 39.48  ? 21  GLN C N   1 
ATOM   139  C CA  . GLN A 1 22  ? -20.079 12.859  -27.537 1.00 39.76  ? 21  GLN C CA  1 
ATOM   140  C C   . GLN A 1 22  ? -21.362 12.157  -27.123 1.00 34.29  ? 21  GLN C C   1 
ATOM   141  O O   . GLN A 1 22  ? -21.411 10.923  -27.097 1.00 38.54  ? 21  GLN C O   1 
ATOM   142  C CB  . GLN A 1 22  ? -19.204 13.054  -26.306 1.00 44.33  ? 21  GLN C CB  1 
ATOM   143  C CG  . GLN A 1 22  ? -17.732 13.075  -26.570 1.00 46.81  ? 21  GLN C CG  1 
ATOM   144  C CD  . GLN A 1 22  ? -16.975 13.538  -25.356 1.00 39.83  ? 21  GLN C CD  1 
ATOM   145  O OE1 . GLN A 1 22  ? -17.577 13.952  -24.363 1.00 37.45  ? 21  GLN C OE1 1 
ATOM   146  N NE2 . GLN A 1 22  ? -15.650 13.464  -25.417 1.00 52.00  ? 21  GLN C NE2 1 
ATOM   147  N N   . VAL A 1 23  ? -22.392 12.919  -26.778 1.00 35.91  ? 22  VAL C N   1 
ATOM   148  C CA  . VAL A 1 23  ? -23.633 12.349  -26.270 1.00 35.09  ? 22  VAL C CA  1 
ATOM   149  C C   . VAL A 1 23  ? -24.521 11.972  -27.444 1.00 37.93  ? 22  VAL C C   1 
ATOM   150  O O   . VAL A 1 23  ? -24.774 12.792  -28.335 1.00 42.73  ? 22  VAL C O   1 
ATOM   151  C CB  . VAL A 1 23  ? -24.338 13.338  -25.328 1.00 37.15  ? 22  VAL C CB  1 
ATOM   152  C CG1 . VAL A 1 23  ? -25.437 12.640  -24.545 1.00 32.50  ? 22  VAL C CG1 1 
ATOM   153  C CG2 . VAL A 1 23  ? -23.326 13.977  -24.383 1.00 35.75  ? 22  VAL C CG2 1 
ATOM   154  N N   . GLU A 1 24  ? -24.994 10.727  -27.448 1.00 43.43  ? 23  GLU C N   1 
ATOM   155  C CA  . GLU A 1 24  ? -25.843 10.254  -28.532 1.00 47.87  ? 23  GLU C CA  1 
ATOM   156  C C   . GLU A 1 24  ? -27.147 11.042  -28.572 1.00 46.01  ? 23  GLU C C   1 
ATOM   157  O O   . GLU A 1 24  ? -27.755 11.327  -27.536 1.00 43.99  ? 23  GLU C O   1 
ATOM   158  C CB  . GLU A 1 24  ? -26.128 8.761   -28.366 1.00 57.35  ? 23  GLU C CB  1 
ATOM   159  C CG  . GLU A 1 24  ? -26.597 8.068   -29.637 1.00 65.33  ? 23  GLU C CG  1 
ATOM   160  C CD  . GLU A 1 24  ? -28.040 7.602   -29.544 1.00 78.96  ? 23  GLU C CD  1 
ATOM   161  O OE1 . GLU A 1 24  ? -28.825 8.235   -28.805 1.00 85.65  ? 23  GLU C OE1 1 
ATOM   162  O OE2 . GLU A 1 24  ? -28.389 6.600   -30.204 1.00 83.37  ? 23  GLU C OE2 1 
ATOM   163  N N   . GLY A 1 25  ? -27.571 11.397  -29.783 1.00 51.03  ? 24  GLY C N   1 
ATOM   164  C CA  . GLY A 1 25  ? -28.761 12.195  -29.985 1.00 42.09  ? 24  GLY C CA  1 
ATOM   165  C C   . GLY A 1 25  ? -28.513 13.674  -30.188 1.00 47.61  ? 24  GLY C C   1 
ATOM   166  O O   . GLY A 1 25  ? -29.470 14.415  -30.447 1.00 51.05  ? 24  GLY C O   1 
ATOM   167  N N   . ASN A 1 26  ? -27.267 14.125  -30.082 1.00 36.92  ? 25  ASN C N   1 
ATOM   168  C CA  . ASN A 1 26  ? -26.918 15.529  -30.229 1.00 34.75  ? 25  ASN C CA  1 
ATOM   169  C C   . ASN A 1 26  ? -26.239 15.763  -31.570 1.00 35.91  ? 25  ASN C C   1 
ATOM   170  O O   . ASN A 1 26  ? -25.400 14.966  -32.004 1.00 36.63  ? 25  ASN C O   1 
ATOM   171  C CB  . ASN A 1 26  ? -25.989 15.988  -29.103 1.00 32.20  ? 25  ASN C CB  1 
ATOM   172  C CG  . ASN A 1 26  ? -26.698 16.091  -27.763 1.00 38.95  ? 25  ASN C CG  1 
ATOM   173  O OD1 . ASN A 1 26  ? -27.862 16.489  -27.684 1.00 40.43  ? 25  ASN C OD1 1 
ATOM   174  N ND2 . ASN A 1 26  ? -25.992 15.736  -26.699 1.00 29.03  ? 25  ASN C ND2 1 
ATOM   175  N N   . THR A 1 27  ? -26.605 16.859  -32.220 1.00 29.57  ? 26  THR C N   1 
ATOM   176  C CA  . THR A 1 27  ? -25.930 17.315  -33.424 1.00 41.10  ? 26  THR C CA  1 
ATOM   177  C C   . THR A 1 27  ? -25.443 18.737  -33.198 1.00 35.54  ? 26  THR C C   1 
ATOM   178  O O   . THR A 1 27  ? -26.137 19.552  -32.581 1.00 32.99  ? 26  THR C O   1 
ATOM   179  C CB  . THR A 1 27  ? -26.849 17.244  -34.646 1.00 22.92  ? 26  THR C CB  1 
ATOM   180  O OG1 . THR A 1 27  ? -28.100 17.872  -34.345 1.00 33.58  ? 26  THR C OG1 1 
ATOM   181  C CG2 . THR A 1 27  ? -27.097 15.793  -35.025 1.00 28.39  ? 26  THR C CG2 1 
ATOM   182  N N   . VAL A 1 28  ? -24.238 19.024  -33.678 1.00 28.77  ? 27  VAL C N   1 
ATOM   183  C CA  . VAL A 1 28  ? -23.580 20.299  -33.434 1.00 32.18  ? 27  VAL C CA  1 
ATOM   184  C C   . VAL A 1 28  ? -23.367 21.008  -34.762 1.00 28.17  ? 27  VAL C C   1 
ATOM   185  O O   . VAL A 1 28  ? -22.852 20.414  -35.717 1.00 31.73  ? 27  VAL C O   1 
ATOM   186  C CB  . VAL A 1 28  ? -22.243 20.117  -32.692 1.00 26.44  ? 27  VAL C CB  1 
ATOM   187  C CG1 . VAL A 1 28  ? -21.537 21.457  -32.535 1.00 26.39  ? 27  VAL C CG1 1 
ATOM   188  C CG2 . VAL A 1 28  ? -22.479 19.478  -31.341 1.00 29.31  ? 27  VAL C CG2 1 
ATOM   189  N N   . ALA A 1 29  ? -23.773 22.270  -34.819 1.00 32.66  ? 28  ALA C N   1 
ATOM   190  C CA  . ALA A 1 29  ? -23.396 23.178  -35.893 1.00 27.49  ? 28  ALA C CA  1 
ATOM   191  C C   . ALA A 1 29  ? -22.249 24.035  -35.370 1.00 37.02  ? 28  ALA C C   1 
ATOM   192  O O   . ALA A 1 29  ? -22.455 24.893  -34.505 1.00 29.46  ? 28  ALA C O   1 
ATOM   193  C CB  . ALA A 1 29  ? -24.581 24.037  -36.330 1.00 26.12  ? 28  ALA C CB  1 
ATOM   194  N N   . LEU A 1 30  ? -21.041 23.782  -35.876 1.00 35.19  ? 29  LEU C N   1 
ATOM   195  C CA  . LEU A 1 30  ? -19.840 24.515  -35.472 1.00 26.69  ? 29  LEU C CA  1 
ATOM   196  C C   . LEU A 1 30  ? -19.643 25.668  -36.448 1.00 34.43  ? 29  LEU C C   1 
ATOM   197  O O   . LEU A 1 30  ? -19.179 25.473  -37.573 1.00 36.52  ? 29  LEU C O   1 
ATOM   198  C CB  . LEU A 1 30  ? -18.631 23.587  -35.446 1.00 22.06  ? 29  LEU C CB  1 
ATOM   199  C CG  . LEU A 1 30  ? -17.299 24.176  -34.973 1.00 27.51  ? 29  LEU C CG  1 
ATOM   200  C CD1 . LEU A 1 30  ? -17.397 24.609  -33.521 1.00 31.75  ? 29  LEU C CD1 1 
ATOM   201  C CD2 . LEU A 1 30  ? -16.146 23.186  -35.169 1.00 23.59  ? 29  LEU C CD2 1 
ATOM   202  N N   . CYS A 1 31  ? -19.993 26.875  -36.020 1.00 35.54  ? 30  CYS C N   1 
ATOM   203  C CA  . CYS A 1 31  ? -20.014 28.034  -36.897 1.00 34.07  ? 30  CYS C CA  1 
ATOM   204  C C   . CYS A 1 31  ? -18.858 28.978  -36.591 1.00 43.53  ? 30  CYS C C   1 
ATOM   205  O O   . CYS A 1 31  ? -18.285 28.967  -35.497 1.00 34.52  ? 30  CYS C O   1 
ATOM   206  C CB  . CYS A 1 31  ? -21.341 28.787  -36.765 1.00 31.56  ? 30  CYS C CB  1 
ATOM   207  S SG  . CYS A 1 31  ? -22.798 27.734  -36.874 1.00 43.72  ? 30  CYS C SG  1 
ATOM   208  N N   . ASP A 1 32  ? -18.517 29.797  -37.586 1.00 45.90  ? 31  ASP C N   1 
ATOM   209  C CA  . ASP A 1 32  ? -17.580 30.895  -37.400 1.00 40.35  ? 31  ASP C CA  1 
ATOM   210  C C   . ASP A 1 32  ? -17.908 31.984  -38.414 1.00 38.37  ? 31  ASP C C   1 
ATOM   211  O O   . ASP A 1 32  ? -18.879 31.883  -39.171 1.00 37.41  ? 31  ASP C O   1 
ATOM   212  C CB  . ASP A 1 32  ? -16.126 30.425  -37.515 1.00 37.92  ? 31  ASP C CB  1 
ATOM   213  C CG  . ASP A 1 32  ? -15.218 31.106  -36.504 1.00 48.42  ? 31  ASP C CG  1 
ATOM   214  O OD1 . ASP A 1 32  ? -15.464 32.289  -36.191 1.00 52.67  ? 31  ASP C OD1 1 
ATOM   215  O OD2 . ASP A 1 32  ? -14.268 30.460  -36.014 1.00 41.83  ? 31  ASP C OD2 1 
ATOM   216  N N   . ILE A 1 33  ? -17.094 33.041  -38.413 1.00 35.80  ? 32  ILE C N   1 
ATOM   217  C CA  . ILE A 1 33  ? -17.361 34.178  -39.289 1.00 44.64  ? 32  ILE C CA  1 
ATOM   218  C C   . ILE A 1 33  ? -17.156 33.793  -40.748 1.00 35.74  ? 32  ILE C C   1 
ATOM   219  O O   . ILE A 1 33  ? -17.975 34.126  -41.612 1.00 39.91  ? 32  ILE C O   1 
ATOM   220  C CB  . ILE A 1 33  ? -16.488 35.379  -38.885 1.00 48.20  ? 32  ILE C CB  1 
ATOM   221  C CG1 . ILE A 1 33  ? -17.093 36.078  -37.667 1.00 49.31  ? 32  ILE C CG1 1 
ATOM   222  C CG2 . ILE A 1 33  ? -16.343 36.353  -40.047 1.00 44.73  ? 32  ILE C CG2 1 
ATOM   223  C CD1 . ILE A 1 33  ? -16.064 36.560  -36.671 1.00 41.31  ? 32  ILE C CD1 1 
ATOM   224  N N   . LYS A 1 34  ? -16.071 33.087  -41.048 1.00 40.64  ? 33  LYS C N   1 
ATOM   225  C CA  . LYS A 1 34  ? -15.794 32.612  -42.395 1.00 42.61  ? 33  LYS C CA  1 
ATOM   226  C C   . LYS A 1 34  ? -15.913 31.095  -42.447 1.00 39.66  ? 33  LYS C C   1 
ATOM   227  O O   . LYS A 1 34  ? -15.519 30.396  -41.508 1.00 43.65  ? 33  LYS C O   1 
ATOM   228  C CB  . LYS A 1 34  ? -14.406 33.061  -42.866 1.00 48.43  ? 33  LYS C CB  1 
ATOM   229  C CG  . LYS A 1 34  ? -14.285 34.577  -42.995 1.00 45.58  ? 33  LYS C CG  1 
ATOM   230  C CD  . LYS A 1 34  ? -13.145 34.998  -43.917 1.00 56.01  ? 33  LYS C CD  1 
ATOM   231  C CE  . LYS A 1 34  ? -11.974 35.581  -43.148 1.00 51.83  ? 33  LYS C CE  1 
ATOM   232  N NZ  . LYS A 1 34  ? -12.014 37.064  -43.100 1.00 54.34  ? 33  LYS C NZ  1 
ATOM   233  N N   . GLN A 1 35  ? -16.466 30.598  -43.556 1.00 41.72  ? 34  GLN C N   1 
ATOM   234  C CA  . GLN A 1 35  ? -16.712 29.167  -43.693 1.00 32.89  ? 34  GLN C CA  1 
ATOM   235  C C   . GLN A 1 35  ? -15.422 28.366  -43.582 1.00 36.39  ? 34  GLN C C   1 
ATOM   236  O O   . GLN A 1 35  ? -15.399 27.299  -42.960 1.00 39.15  ? 34  GLN C O   1 
ATOM   237  C CB  . GLN A 1 35  ? -17.407 28.882  -45.024 1.00 43.36  ? 34  GLN C CB  1 
ATOM   238  C CG  . GLN A 1 35  ? -17.526 27.404  -45.351 1.00 30.90  ? 34  GLN C CG  1 
ATOM   239  C CD  . GLN A 1 35  ? -18.788 26.794  -44.775 1.00 42.85  ? 34  GLN C CD  1 
ATOM   240  O OE1 . GLN A 1 35  ? -19.841 27.430  -44.747 1.00 42.29  ? 34  GLN C OE1 1 
ATOM   241  N NE2 . GLN A 1 35  ? -18.685 25.558  -44.298 1.00 46.64  ? 34  GLN C NE2 1 
ATOM   242  N N   . GLU A 1 36  ? -14.334 28.865  -44.173 1.00 40.52  ? 35  GLU C N   1 
ATOM   243  C CA  . GLU A 1 36  ? -13.068 28.146  -44.084 1.00 43.73  ? 35  GLU C CA  1 
ATOM   244  C C   . GLU A 1 36  ? -12.598 28.028  -42.638 1.00 41.40  ? 35  GLU C C   1 
ATOM   245  O O   . GLU A 1 36  ? -11.977 27.025  -42.271 1.00 41.45  ? 35  GLU C O   1 
ATOM   246  C CB  . GLU A 1 36  ? -12.004 28.830  -44.955 1.00 40.76  ? 35  GLU C CB  1 
ATOM   247  C CG  . GLU A 1 36  ? -11.663 30.261  -44.549 1.00 41.01  ? 35  GLU C CG  1 
ATOM   248  C CD  . GLU A 1 36  ? -12.391 31.301  -45.384 1.00 43.11  ? 35  GLU C CD  1 
ATOM   249  O OE1 . GLU A 1 36  ? -13.577 31.080  -45.712 1.00 42.25  ? 35  GLU C OE1 1 
ATOM   250  O OE2 . GLU A 1 36  ? -11.784 32.350  -45.694 1.00 45.34  ? 35  GLU C OE2 1 
ATOM   251  N N   . TRP A 1 37  ? -12.913 29.023  -41.799 1.00 39.29  ? 36  TRP C N   1 
ATOM   252  C CA  . TRP A 1 37  ? -12.512 28.978  -40.394 1.00 39.68  ? 36  TRP C CA  1 
ATOM   253  C C   . TRP A 1 37  ? -13.174 27.820  -39.658 1.00 41.35  ? 36  TRP C C   1 
ATOM   254  O O   . TRP A 1 37  ? -12.535 27.146  -38.841 1.00 34.27  ? 36  TRP C O   1 
ATOM   255  C CB  . TRP A 1 37  ? -12.865 30.293  -39.702 1.00 43.64  ? 36  TRP C CB  1 
ATOM   256  C CG  . TRP A 1 37  ? -12.023 31.456  -40.103 1.00 48.56  ? 36  TRP C CG  1 
ATOM   257  C CD1 . TRP A 1 37  ? -10.982 31.459  -40.986 1.00 52.77  ? 36  TRP C CD1 1 
ATOM   258  C CD2 . TRP A 1 37  ? -12.149 32.798  -39.625 1.00 48.86  ? 36  TRP C CD2 1 
ATOM   259  N NE1 . TRP A 1 37  ? -10.453 32.725  -41.089 1.00 53.75  ? 36  TRP C NE1 1 
ATOM   260  C CE2 . TRP A 1 37  ? -11.153 33.565  -40.263 1.00 54.51  ? 36  TRP C CE2 1 
ATOM   261  C CE3 . TRP A 1 37  ? -13.011 33.428  -38.721 1.00 49.10  ? 36  TRP C CE3 1 
ATOM   262  C CZ2 . TRP A 1 37  ? -10.992 34.927  -40.019 1.00 51.08  ? 36  TRP C CZ2 1 
ATOM   263  C CZ3 . TRP A 1 37  ? -12.852 34.779  -38.484 1.00 52.16  ? 36  TRP C CZ3 1 
ATOM   264  C CH2 . TRP A 1 37  ? -11.854 35.516  -39.133 1.00 55.23  ? 36  TRP C CH2 1 
ATOM   265  N N   . ALA A 1 38  ? -14.465 27.592  -39.911 1.00 40.23  ? 37  ALA C N   1 
ATOM   266  C CA  . ALA A 1 38  ? -15.150 26.470  -39.278 1.00 38.72  ? 37  ALA C CA  1 
ATOM   267  C C   . ALA A 1 38  ? -14.645 25.141  -39.824 1.00 41.79  ? 37  ALA C C   1 
ATOM   268  O O   . ALA A 1 38  ? -14.563 24.150  -39.086 1.00 37.41  ? 37  ALA C O   1 
ATOM   269  C CB  . ALA A 1 38  ? -16.660 26.594  -39.473 1.00 33.21  ? 37  ALA C CB  1 
ATOM   270  N N   . GLU A 1 39  ? -14.303 25.098  -41.114 1.00 38.29  ? 38  GLU C N   1 
ATOM   271  C CA  . GLU A 1 39  ? -13.722 23.885  -41.677 1.00 35.07  ? 38  GLU C CA  1 
ATOM   272  C C   . GLU A 1 39  ? -12.384 23.568  -41.020 1.00 34.70  ? 38  GLU C C   1 
ATOM   273  O O   . GLU A 1 39  ? -12.105 22.409  -40.690 1.00 33.38  ? 38  GLU C O   1 
ATOM   274  C CB  . GLU A 1 39  ? -13.562 24.026  -43.191 1.00 37.78  ? 38  GLU C CB  1 
ATOM   275  C CG  . GLU A 1 39  ? -14.872 24.242  -43.938 1.00 41.86  ? 38  GLU C CG  1 
ATOM   276  C CD  . GLU A 1 39  ? -15.610 22.945  -44.220 1.00 46.92  ? 38  GLU C CD  1 
ATOM   277  O OE1 . GLU A 1 39  ? -15.067 21.864  -43.901 1.00 55.14  ? 38  GLU C OE1 1 
ATOM   278  O OE2 . GLU A 1 39  ? -16.737 23.009  -44.761 1.00 48.46  ? 38  GLU C OE2 1 
ATOM   279  N N   . ASN A 1 40  ? -11.543 24.588  -40.817 1.00 32.25  ? 39  ASN C N   1 
ATOM   280  C CA  . ASN A 1 40  ? -10.292 24.373  -40.097 1.00 32.44  ? 39  ASN C CA  1 
ATOM   281  C C   . ASN A 1 40  ? -10.550 23.917  -38.670 1.00 33.42  ? 39  ASN C C   1 
ATOM   282  O O   . ASN A 1 40  ? -9.780  23.118  -38.124 1.00 32.90  ? 39  ASN C O   1 
ATOM   283  C CB  . ASN A 1 40  ? -9.439  25.646  -40.097 1.00 39.63  ? 39  ASN C CB  1 
ATOM   284  C CG  . ASN A 1 40  ? -9.265  26.243  -41.488 1.00 54.51  ? 39  ASN C CG  1 
ATOM   285  O OD1 . ASN A 1 40  ? -9.273  27.466  -41.658 1.00 47.06  ? 39  ASN C OD1 1 
ATOM   286  N ND2 . ASN A 1 40  ? -9.116  25.380  -42.490 1.00 41.92  ? 39  ASN C ND2 1 
ATOM   287  N N   . GLY A 1 41  ? -11.628 24.408  -38.053 1.00 31.80  ? 40  GLY C N   1 
ATOM   288  C CA  . GLY A 1 41  ? -11.968 23.958  -36.713 1.00 28.89  ? 40  GLY C CA  1 
ATOM   289  C C   . GLY A 1 41  ? -12.290 22.477  -36.667 1.00 33.00  ? 40  GLY C C   1 
ATOM   290  O O   . GLY A 1 41  ? -11.764 21.740  -35.830 1.00 35.06  ? 40  GLY C O   1 
ATOM   291  N N   . LEU A 1 42  ? -13.157 22.019  -37.575 1.00 31.46  ? 41  LEU C N   1 
ATOM   292  C CA  . LEU A 1 42  ? -13.499 20.600  -37.603 1.00 29.55  ? 41  LEU C CA  1 
ATOM   293  C C   . LEU A 1 42  ? -12.299 19.757  -38.014 1.00 38.03  ? 41  LEU C C   1 
ATOM   294  O O   . LEU A 1 42  ? -12.121 18.637  -37.517 1.00 39.39  ? 41  LEU C O   1 
ATOM   295  C CB  . LEU A 1 42  ? -14.682 20.354  -38.540 1.00 31.45  ? 41  LEU C CB  1 
ATOM   296  C CG  . LEU A 1 42  ? -15.101 18.890  -38.712 1.00 34.93  ? 41  LEU C CG  1 
ATOM   297  C CD1 . LEU A 1 42  ? -15.650 18.324  -37.408 1.00 34.85  ? 41  LEU C CD1 1 
ATOM   298  C CD2 . LEU A 1 42  ? -16.122 18.744  -39.822 1.00 38.62  ? 41  LEU C CD2 1 
ATOM   299  N N   . ALA A 1 43  ? -11.460 20.278  -38.914 1.00 28.60  ? 42  ALA C N   1 
ATOM   300  C CA  . ALA A 1 43  ? -10.241 19.563  -39.277 1.00 34.34  ? 42  ALA C CA  1 
ATOM   301  C C   . ALA A 1 43  ? -9.310  19.431  -38.079 1.00 29.21  ? 42  ALA C C   1 
ATOM   302  O O   . ALA A 1 43  ? -8.634  18.409  -37.914 1.00 35.07  ? 42  ALA C O   1 
ATOM   303  C CB  . ALA A 1 43  ? -9.537  20.270  -40.434 1.00 23.34  ? 42  ALA C CB  1 
ATOM   304  N N   . LYS A 1 44  ? -9.262  20.457  -37.228 1.00 29.39  ? 43  LYS C N   1 
ATOM   305  C CA  . LYS A 1 44  ? -8.462  20.367  -36.013 1.00 35.63  ? 43  LYS C CA  1 
ATOM   306  C C   . LYS A 1 44  ? -9.055  19.350  -35.044 1.00 32.35  ? 43  LYS C C   1 
ATOM   307  O O   . LYS A 1 44  ? -8.315  18.645  -34.347 1.00 35.77  ? 43  LYS C O   1 
ATOM   308  C CB  . LYS A 1 44  ? -8.344  21.750  -35.367 1.00 36.37  ? 43  LYS C CB  1 
ATOM   309  C CG  . LYS A 1 44  ? -7.434  21.820  -34.144 1.00 48.85  ? 43  LYS C CG  1 
ATOM   310  C CD  . LYS A 1 44  ? -6.113  21.097  -34.362 1.00 54.63  ? 43  LYS C CD  1 
ATOM   311  C CE  . LYS A 1 44  ? -5.422  20.815  -33.033 1.00 48.62  ? 43  LYS C CE  1 
ATOM   312  N NZ  . LYS A 1 44  ? -5.614  19.404  -32.593 1.00 53.76  ? 43  LYS C NZ  1 
ATOM   313  N N   . ILE A 1 45  ? -10.386 19.252  -34.990 1.00 33.69  ? 44  ILE C N   1 
ATOM   314  C CA  . ILE A 1 45  ? -11.023 18.204  -34.196 1.00 32.26  ? 44  ILE C CA  1 
ATOM   315  C C   . ILE A 1 45  ? -10.683 16.833  -34.766 1.00 37.97  ? 44  ILE C C   1 
ATOM   316  O O   . ILE A 1 45  ? -10.338 15.901  -34.031 1.00 37.59  ? 44  ILE C O   1 
ATOM   317  C CB  . ILE A 1 45  ? -12.546 18.419  -34.136 1.00 33.70  ? 44  ILE C CB  1 
ATOM   318  C CG1 . ILE A 1 45  ? -12.900 19.557  -33.183 1.00 29.44  ? 44  ILE C CG1 1 
ATOM   319  C CG2 . ILE A 1 45  ? -13.253 17.142  -33.694 1.00 32.47  ? 44  ILE C CG2 1 
ATOM   320  C CD1 . ILE A 1 45  ? -14.323 20.030  -33.338 1.00 23.71  ? 44  ILE C CD1 1 
ATOM   321  N N   . LYS A 1 46  ? -10.782 16.694  -36.091 1.00 36.20  ? 45  LYS C N   1 
ATOM   322  C CA  . LYS A 1 46  ? -10.452 15.431  -36.741 1.00 37.18  ? 45  LYS C CA  1 
ATOM   323  C C   . LYS A 1 46  ? -8.988  15.066  -36.524 1.00 43.21  ? 45  LYS C C   1 
ATOM   324  O O   . LYS A 1 46  ? -8.664  13.908  -36.234 1.00 36.55  ? 45  LYS C O   1 
ATOM   325  C CB  . LYS A 1 46  ? -10.774 15.525  -38.234 1.00 31.81  ? 45  LYS C CB  1 
ATOM   326  C CG  . LYS A 1 46  ? -11.191 14.222  -38.892 1.00 52.50  ? 45  LYS C CG  1 
ATOM   327  C CD  . LYS A 1 46  ? -11.408 14.418  -40.391 1.00 61.00  ? 45  LYS C CD  1 
ATOM   328  C CE  . LYS A 1 46  ? -12.308 13.340  -40.980 1.00 49.85  ? 45  LYS C CE  1 
ATOM   329  N NZ  . LYS A 1 46  ? -13.560 13.906  -41.560 1.00 58.14  ? 45  LYS C NZ  1 
ATOM   330  N N   . LYS A 1 47  ? -8.088  16.046  -36.651 1.00 38.24  ? 46  LYS C N   1 
ATOM   331  C CA  . LYS A 1 47  ? -6.665  15.780  -36.462 1.00 37.81  ? 46  LYS C CA  1 
ATOM   332  C C   . LYS A 1 47  ? -6.365  15.370  -35.026 1.00 42.86  ? 46  LYS C C   1 
ATOM   333  O O   . LYS A 1 47  ? -5.508  14.512  -34.785 1.00 44.96  ? 46  LYS C O   1 
ATOM   334  C CB  . LYS A 1 47  ? -5.847  17.012  -36.856 1.00 45.41  ? 46  LYS C CB  1 
ATOM   335  C CG  . LYS A 1 47  ? -4.343  16.880  -36.649 1.00 52.21  ? 46  LYS C CG  1 
ATOM   336  C CD  . LYS A 1 47  ? -3.577  17.835  -37.561 1.00 67.14  ? 46  LYS C CD  1 
ATOM   337  C CE  . LYS A 1 47  ? -2.284  18.318  -36.911 1.00 67.30  ? 46  LYS C CE  1 
ATOM   338  N NZ  . LYS A 1 47  ? -1.811  19.614  -37.483 1.00 59.30  ? 46  LYS C NZ  1 
ATOM   339  N N   . GLY A 1 48  ? -7.062  15.969  -34.060 1.00 41.57  ? 47  GLY C N   1 
ATOM   340  C CA  . GLY A 1 48  ? -6.844  15.595  -32.673 1.00 39.89  ? 47  GLY C CA  1 
ATOM   341  C C   . GLY A 1 48  ? -7.297  14.178  -32.375 1.00 45.42  ? 47  GLY C C   1 
ATOM   342  O O   . GLY A 1 48  ? -6.628  13.445  -31.641 1.00 45.61  ? 47  GLY C O   1 
ATOM   343  N N   . TYR A 1 49  ? -8.433  13.770  -32.945 1.00 37.27  ? 48  TYR C N   1 
ATOM   344  C CA  . TYR A 1 49  ? -8.928  12.419  -32.704 1.00 40.23  ? 48  TYR C CA  1 
ATOM   345  C C   . TYR A 1 49  ? -8.018  11.365  -33.322 1.00 42.62  ? 48  TYR C C   1 
ATOM   346  O O   . TYR A 1 49  ? -7.892  10.262  -32.777 1.00 46.13  ? 48  TYR C O   1 
ATOM   347  C CB  . TYR A 1 49  ? -10.354 12.278  -33.236 1.00 34.02  ? 48  TYR C CB  1 
ATOM   348  C CG  . TYR A 1 49  ? -11.409 12.723  -32.246 1.00 36.48  ? 48  TYR C CG  1 
ATOM   349  C CD1 . TYR A 1 49  ? -11.325 12.368  -30.904 1.00 37.90  ? 48  TYR C CD1 1 
ATOM   350  C CD2 . TYR A 1 49  ? -12.484 13.502  -32.651 1.00 33.54  ? 48  TYR C CD2 1 
ATOM   351  C CE1 . TYR A 1 49  ? -12.288 12.775  -29.996 1.00 35.38  ? 48  TYR C CE1 1 
ATOM   352  C CE2 . TYR A 1 49  ? -13.448 13.913  -31.750 1.00 29.89  ? 48  TYR C CE2 1 
ATOM   353  C CZ  . TYR A 1 49  ? -13.347 13.547  -30.428 1.00 27.66  ? 48  TYR C CZ  1 
ATOM   354  O OH  . TYR A 1 49  ? -14.310 13.955  -29.538 1.00 24.35  ? 48  TYR C OH  1 
ATOM   355  N N   . GLU A 1 50  ? -7.371  11.680  -34.447 1.00 38.45  ? 49  GLU C N   1 
ATOM   356  C CA  . GLU A 1 50  ? -6.455  10.717  -35.049 1.00 40.35  ? 49  GLU C CA  1 
ATOM   357  C C   . GLU A 1 50  ? -5.259  10.443  -34.147 1.00 42.78  ? 49  GLU C C   1 
ATOM   358  O O   . GLU A 1 50  ? -4.687  9.347   -34.194 1.00 43.82  ? 49  GLU C O   1 
ATOM   359  C CB  . GLU A 1 50  ? -5.994  11.209  -36.423 1.00 37.23  ? 49  GLU C CB  1 
ATOM   360  C CG  . GLU A 1 50  ? -7.112  11.336  -37.458 1.00 49.92  ? 49  GLU C CG  1 
ATOM   361  C CD  . GLU A 1 50  ? -8.229  10.313  -37.266 1.00 60.58  ? 49  GLU C CD  1 
ATOM   362  O OE1 . GLU A 1 50  ? -9.402  10.732  -37.135 1.00 59.50  ? 49  GLU C OE1 1 
ATOM   363  O OE2 . GLU A 1 50  ? -7.941  9.092   -37.259 1.00 52.04  ? 49  GLU C OE2 1 
ATOM   364  N N   . LYS A 1 51  ? -4.879  11.408  -33.308 1.00 43.94  ? 50  LYS C N   1 
ATOM   365  C CA  . LYS A 1 51  ? -3.775  11.183  -32.381 1.00 49.87  ? 50  LYS C CA  1 
ATOM   366  C C   . LYS A 1 51  ? -4.197  10.288  -31.221 1.00 44.42  ? 50  LYS C C   1 
ATOM   367  O O   . LYS A 1 51  ? -3.456  9.380   -30.829 1.00 48.81  ? 50  LYS C O   1 
ATOM   368  C CB  . LYS A 1 51  ? -3.234  12.516  -31.861 1.00 43.27  ? 50  LYS C CB  1 
ATOM   369  C CG  . LYS A 1 51  ? -2.585  13.406  -32.922 1.00 54.20  ? 50  LYS C CG  1 
ATOM   370  C CD  . LYS A 1 51  ? -1.080  13.168  -33.042 1.00 59.95  ? 50  LYS C CD  1 
ATOM   371  C CE  . LYS A 1 51  ? -0.756  11.894  -33.820 1.00 55.35  ? 50  LYS C CE  1 
ATOM   372  N NZ  . LYS A 1 51  ? 0.582   11.340  -33.468 1.00 52.82  ? 50  LYS C NZ  1 
ATOM   373  N N   . LEU A 1 52  ? -5.383  10.534  -30.654 1.00 42.39  ? 51  LEU C N   1 
ATOM   374  C CA  . LEU A 1 52  ? -5.865  9.698   -29.557 1.00 45.42  ? 51  LEU C CA  1 
ATOM   375  C C   . LEU A 1 52  ? -6.091  8.257   -30.001 1.00 49.54  ? 51  LEU C C   1 
ATOM   376  O O   . LEU A 1 52  ? -5.909  7.328   -29.204 1.00 47.79  ? 51  LEU C O   1 
ATOM   377  C CB  . LEU A 1 52  ? -7.154  10.280  -28.974 1.00 41.85  ? 51  LEU C CB  1 
ATOM   378  C CG  . LEU A 1 52  ? -7.102  11.729  -28.492 1.00 48.32  ? 51  LEU C CG  1 
ATOM   379  C CD1 . LEU A 1 52  ? -8.500  12.251  -28.205 1.00 39.12  ? 51  LEU C CD1 1 
ATOM   380  C CD2 . LEU A 1 52  ? -6.225  11.830  -27.259 1.00 43.86  ? 51  LEU C CD2 1 
ATOM   381  N N   . VAL A 1 53  ? -6.495  8.051   -31.259 1.00 42.58  ? 52  VAL C N   1 
ATOM   382  C CA  . VAL A 1 53  ? -6.630  6.694   -31.780 1.00 44.92  ? 52  VAL C CA  1 
ATOM   383  C C   . VAL A 1 53  ? -5.268  6.014   -31.844 1.00 48.10  ? 52  VAL C C   1 
ATOM   384  O O   . VAL A 1 53  ? -5.125  4.841   -31.473 1.00 47.79  ? 52  VAL C O   1 
ATOM   385  C CB  . VAL A 1 53  ? -7.321  6.713   -33.158 1.00 41.57  ? 52  VAL C CB  1 
ATOM   386  C CG1 . VAL A 1 53  ? -7.155  5.373   -33.861 1.00 37.83  ? 52  VAL C CG1 1 
ATOM   387  C CG2 . VAL A 1 53  ? -8.794  7.054   -33.014 1.00 45.01  ? 52  VAL C CG2 1 
ATOM   388  N N   . ALA A 1 54  ? -4.245  6.744   -32.299 1.00 48.87  ? 53  ALA C N   1 
ATOM   389  C CA  . ALA A 1 54  ? -2.904  6.175   -32.391 1.00 48.60  ? 53  ALA C CA  1 
ATOM   390  C C   . ALA A 1 54  ? -2.368  5.793   -31.016 1.00 53.57  ? 53  ALA C C   1 
ATOM   391  O O   . ALA A 1 54  ? -1.785  4.715   -30.847 1.00 56.96  ? 53  ALA C O   1 
ATOM   392  C CB  . ALA A 1 54  ? -1.964  7.162   -33.083 1.00 39.17  ? 53  ALA C CB  1 
ATOM   393  N N   . LYS A 1 55  ? -2.561  6.657   -30.020 1.00 52.43  ? 54  LYS C N   1 
ATOM   394  C CA  . LYS A 1 55  ? -2.157  6.353   -28.653 1.00 48.71  ? 54  LYS C CA  1 
ATOM   395  C C   . LYS A 1 55  ? -3.105  5.383   -27.958 1.00 50.58  ? 54  LYS C C   1 
ATOM   396  O O   . LYS A 1 55  ? -2.898  5.077   -26.778 1.00 49.10  ? 54  LYS C O   1 
ATOM   397  C CB  . LYS A 1 55  ? -2.031  7.647   -27.837 1.00 53.02  ? 54  LYS C CB  1 
ATOM   398  C CG  . LYS A 1 55  ? -1.438  8.822   -28.620 1.00 56.03  ? 54  LYS C CG  1 
ATOM   399  C CD  . LYS A 1 55  ? -1.266  10.087  -27.771 1.00 63.85  ? 54  LYS C CD  1 
ATOM   400  C CE  . LYS A 1 55  ? -1.026  9.770   -26.296 1.00 65.00  ? 54  LYS C CE  1 
ATOM   401  N NZ  . LYS A 1 55  ? -0.678  10.986  -25.506 1.00 59.47  ? 54  LYS C NZ  1 
ATOM   402  N N   . GLY A 1 56  ? -4.132  4.898   -28.654 1.00 52.61  ? 55  GLY C N   1 
ATOM   403  C CA  . GLY A 1 56  ? -4.993  3.860   -28.118 1.00 41.18  ? 55  GLY C CA  1 
ATOM   404  C C   . GLY A 1 56  ? -5.888  4.283   -26.976 1.00 47.11  ? 55  GLY C C   1 
ATOM   405  O O   . GLY A 1 56  ? -6.203  3.458   -26.112 1.00 59.52  ? 55  GLY C O   1 
ATOM   406  N N   . LYS A 1 57  ? -6.316  5.544   -26.946 1.00 48.68  ? 56  LYS C N   1 
ATOM   407  C CA  . LYS A 1 57  ? -7.183  6.034   -25.882 1.00 49.17  ? 56  LYS C CA  1 
ATOM   408  C C   . LYS A 1 57  ? -8.620  6.256   -26.334 1.00 47.94  ? 56  LYS C C   1 
ATOM   409  O O   . LYS A 1 57  ? -9.463  6.626   -25.512 1.00 49.93  ? 56  LYS C O   1 
ATOM   410  C CB  . LYS A 1 57  ? -6.613  7.330   -25.291 1.00 54.82  ? 56  LYS C CB  1 
ATOM   411  C CG  . LYS A 1 57  ? -5.269  7.141   -24.591 1.00 56.16  ? 56  LYS C CG  1 
ATOM   412  C CD  . LYS A 1 57  ? -4.967  8.269   -23.614 1.00 51.80  ? 56  LYS C CD  1 
ATOM   413  C CE  . LYS A 1 57  ? -4.020  7.806   -22.509 1.00 67.37  ? 56  LYS C CE  1 
ATOM   414  N NZ  . LYS A 1 57  ? -4.737  7.413   -21.258 1.00 52.16  ? 56  LYS C NZ  1 
ATOM   415  N N   . ILE A 1 58  ? -8.925  6.033   -27.608 1.00 55.93  ? 57  ILE C N   1 
ATOM   416  C CA  . ILE A 1 58  ? -10.288 6.160   -28.118 1.00 49.37  ? 57  ILE C CA  1 
ATOM   417  C C   . ILE A 1 58  ? -10.427 5.219   -29.310 1.00 45.21  ? 57  ILE C C   1 
ATOM   418  O O   . ILE A 1 58  ? -9.471  5.056   -30.082 1.00 45.31  ? 57  ILE C O   1 
ATOM   419  C CB  . ILE A 1 58  ? -10.613 7.621   -28.485 1.00 44.96  ? 57  ILE C CB  1 
ATOM   420  C CG1 . ILE A 1 58  ? -12.117 7.822   -28.693 1.00 49.22  ? 57  ILE C CG1 1 
ATOM   421  C CG2 . ILE A 1 58  ? -9.857  8.061   -29.722 1.00 38.29  ? 57  ILE C CG2 1 
ATOM   422  C CD1 . ILE A 1 58  ? -12.476 9.154   -29.337 1.00 36.45  ? 57  ILE C CD1 1 
ATOM   423  N N   . PRO A 1 59  ? -11.563 4.545   -29.479 1.00 50.89  ? 58  PRO C N   1 
ATOM   424  C CA  . PRO A 1 59  ? -11.754 3.738   -30.688 1.00 39.54  ? 58  PRO C CA  1 
ATOM   425  C C   . PRO A 1 59  ? -12.050 4.615   -31.893 1.00 37.89  ? 58  PRO C C   1 
ATOM   426  O O   . PRO A 1 59  ? -12.701 5.659   -31.788 1.00 41.64  ? 58  PRO C O   1 
ATOM   427  C CB  . PRO A 1 59  ? -12.950 2.837   -30.348 1.00 48.50  ? 58  PRO C CB  1 
ATOM   428  C CG  . PRO A 1 59  ? -13.345 3.153   -28.943 1.00 49.36  ? 58  PRO C CG  1 
ATOM   429  C CD  . PRO A 1 59  ? -12.674 4.411   -28.522 1.00 39.87  ? 58  PRO C CD  1 
ATOM   430  N N   . GLN A 1 60  ? -11.562 4.172   -33.054 1.00 35.94  ? 59  GLN C N   1 
ATOM   431  C CA  . GLN A 1 60  ? -11.772 4.935   -34.281 1.00 39.49  ? 59  GLN C CA  1 
ATOM   432  C C   . GLN A 1 60  ? -13.253 5.151   -34.566 1.00 39.46  ? 59  GLN C C   1 
ATOM   433  O O   . GLN A 1 60  ? -13.634 6.213   -35.072 1.00 32.51  ? 59  GLN C O   1 
ATOM   434  C CB  . GLN A 1 60  ? -11.098 4.232   -35.460 1.00 39.60  ? 59  GLN C CB  1 
ATOM   435  C CG  . GLN A 1 60  ? -11.234 4.973   -36.783 1.00 33.50  ? 59  GLN C CG  1 
ATOM   436  C CD  . GLN A 1 60  ? -10.286 6.154   -36.886 1.00 44.96  ? 59  GLN C CD  1 
ATOM   437  O OE1 . GLN A 1 60  ? -9.069  5.996   -36.792 1.00 48.39  ? 59  GLN C OE1 1 
ATOM   438  N NE2 . GLN A 1 60  ? -10.841 7.346   -37.080 1.00 40.23  ? 59  GLN C NE2 1 
ATOM   439  N N   . GLU A 1 61  ? -14.102 4.169   -34.241 1.00 38.96  ? 60  GLU C N   1 
ATOM   440  C CA  . GLU A 1 61  ? -15.537 4.322   -34.474 1.00 37.64  ? 60  GLU C CA  1 
ATOM   441  C C   . GLU A 1 61  ? -16.097 5.494   -33.683 1.00 36.14  ? 60  GLU C C   1 
ATOM   442  O O   . GLU A 1 61  ? -16.884 6.291   -34.209 1.00 33.94  ? 60  GLU C O   1 
ATOM   443  C CB  . GLU A 1 61  ? -16.290 3.043   -34.101 1.00 44.04  ? 60  GLU C CB  1 
ATOM   444  C CG  . GLU A 1 61  ? -15.553 1.743   -34.350 1.00 49.07  ? 60  GLU C CG  1 
ATOM   445  C CD  . GLU A 1 61  ? -16.128 0.600   -33.527 1.00 61.12  ? 60  GLU C CD  1 
ATOM   446  O OE1 . GLU A 1 61  ? -15.335 -0.175  -32.950 1.00 70.96  ? 60  GLU C OE1 1 
ATOM   447  O OE2 . GLU A 1 61  ? -17.372 0.487   -33.443 1.00 65.06  ? 60  GLU C OE2 1 
ATOM   448  N N   . LYS A 1 62  ? -15.713 5.607   -32.406 1.00 38.35  ? 61  LYS C N   1 
ATOM   449  C CA  . LYS A 1 62  ? -16.231 6.686   -31.570 1.00 35.53  ? 61  LYS C CA  1 
ATOM   450  C C   . LYS A 1 62  ? -15.802 8.046   -32.105 1.00 27.86  ? 61  LYS C C   1 
ATOM   451  O O   . LYS A 1 62  ? -16.614 8.978   -32.178 1.00 31.57  ? 61  LYS C O   1 
ATOM   452  C CB  . LYS A 1 62  ? -15.770 6.497   -30.123 1.00 39.52  ? 61  LYS C CB  1 
ATOM   453  C CG  . LYS A 1 62  ? -16.501 7.370   -29.106 1.00 34.57  ? 61  LYS C CG  1 
ATOM   454  C CD  . LYS A 1 62  ? -18.010 7.328   -29.312 1.00 39.76  ? 61  LYS C CD  1 
ATOM   455  C CE  . LYS A 1 62  ? -18.760 7.846   -28.091 1.00 48.39  ? 61  LYS C CE  1 
ATOM   456  N NZ  . LYS A 1 62  ? -20.170 8.211   -28.420 1.00 43.72  ? 61  LYS C NZ  1 
ATOM   457  N N   . ALA A 1 63  ? -14.532 8.171   -32.499 1.00 27.99  ? 62  ALA C N   1 
ATOM   458  C CA  . ALA A 1 63  ? -14.057 9.396   -33.137 1.00 35.81  ? 62  ALA C CA  1 
ATOM   459  C C   . ALA A 1 63  ? -14.869 9.716   -34.386 1.00 33.69  ? 62  ALA C C   1 
ATOM   460  O O   . ALA A 1 63  ? -15.300 10.858  -34.585 1.00 29.67  ? 62  ALA C O   1 
ATOM   461  C CB  . ALA A 1 63  ? -12.574 9.262   -33.482 1.00 34.80  ? 62  ALA C CB  1 
ATOM   462  N N   . ASP A 1 64  ? -15.086 8.713   -35.242 1.00 35.24  ? 63  ASP C N   1 
ATOM   463  C CA  . ASP A 1 64  ? -15.868 8.930   -36.456 1.00 27.77  ? 63  ASP C CA  1 
ATOM   464  C C   . ASP A 1 64  ? -17.305 9.310   -36.122 1.00 30.18  ? 63  ASP C C   1 
ATOM   465  O O   . ASP A 1 64  ? -17.876 10.218  -36.738 1.00 32.30  ? 63  ASP C O   1 
ATOM   466  C CB  . ASP A 1 64  ? -15.835 7.677   -37.333 1.00 38.46  ? 63  ASP C CB  1 
ATOM   467  C CG  . ASP A 1 64  ? -14.552 7.555   -38.145 1.00 46.15  ? 63  ASP C CG  1 
ATOM   468  O OD1 . ASP A 1 64  ? -13.704 8.471   -38.078 1.00 45.62  ? 63  ASP C OD1 1 
ATOM   469  O OD2 . ASP A 1 64  ? -14.394 6.536   -38.853 1.00 43.64  ? 63  ASP C OD2 1 
ATOM   470  N N   . ALA A 1 65  ? -17.903 8.629   -35.143 1.00 29.60  ? 64  ALA C N   1 
ATOM   471  C CA  . ALA A 1 65  ? -19.269 8.950   -34.745 1.00 36.40  ? 64  ALA C CA  1 
ATOM   472  C C   . ALA A 1 65  ? -19.369 10.372  -34.203 1.00 29.56  ? 64  ALA C C   1 
ATOM   473  O O   . ALA A 1 65  ? -20.348 11.077  -34.472 1.00 30.96  ? 64  ALA C O   1 
ATOM   474  C CB  . ALA A 1 65  ? -19.761 7.940   -33.709 1.00 31.13  ? 64  ALA C CB  1 
ATOM   475  N N   . ILE A 1 66  ? -18.361 10.812  -33.446 1.00 31.36  ? 65  ILE C N   1 
ATOM   476  C CA  . ILE A 1 66  ? -18.370 12.169  -32.906 1.00 35.01  ? 65  ILE C CA  1 
ATOM   477  C C   . ILE A 1 66  ? -18.236 13.190  -34.027 1.00 24.97  ? 65  ILE C C   1 
ATOM   478  O O   . ILE A 1 66  ? -18.953 14.197  -34.063 1.00 25.17  ? 65  ILE C O   1 
ATOM   479  C CB  . ILE A 1 66  ? -17.253 12.342  -31.861 1.00 33.30  ? 65  ILE C CB  1 
ATOM   480  C CG1 . ILE A 1 66  ? -17.638 11.672  -30.540 1.00 36.59  ? 65  ILE C CG1 1 
ATOM   481  C CG2 . ILE A 1 66  ? -16.947 13.822  -31.650 1.00 28.07  ? 65  ILE C CG2 1 
ATOM   482  C CD1 . ILE A 1 66  ? -16.442 11.321  -29.672 1.00 34.78  ? 65  ILE C CD1 1 
ATOM   483  N N   . VAL A 1 67  ? -17.303 12.951  -34.951 1.00 27.49  ? 66  VAL C N   1 
ATOM   484  C CA  . VAL A 1 67  ? -17.072 13.887  -36.048 1.00 33.23  ? 66  VAL C CA  1 
ATOM   485  C C   . VAL A 1 67  ? -18.303 13.979  -36.941 1.00 29.93  ? 66  VAL C C   1 
ATOM   486  O O   . VAL A 1 67  ? -18.667 15.065  -37.409 1.00 29.97  ? 66  VAL C O   1 
ATOM   487  C CB  . VAL A 1 67  ? -15.820 13.471  -36.843 1.00 35.90  ? 66  VAL C CB  1 
ATOM   488  C CG1 . VAL A 1 67  ? -15.734 14.233  -38.156 1.00 39.74  ? 66  VAL C CG1 1 
ATOM   489  C CG2 . VAL A 1 67  ? -14.565 13.680  -36.004 1.00 31.98  ? 66  VAL C CG2 1 
ATOM   490  N N   . ALA A 1 68  ? -18.976 12.848  -37.174 1.00 29.62  ? 67  ALA C N   1 
ATOM   491  C CA  . ALA A 1 68  ? -20.143 12.851  -38.051 1.00 28.12  ? 67  ALA C CA  1 
ATOM   492  C C   . ALA A 1 68  ? -21.298 13.663  -37.480 1.00 29.19  ? 67  ALA C C   1 
ATOM   493  O O   . ALA A 1 68  ? -22.240 13.981  -38.213 1.00 27.66  ? 67  ALA C O   1 
ATOM   494  C CB  . ALA A 1 68  ? -20.604 11.419  -38.328 1.00 23.20  ? 67  ALA C CB  1 
ATOM   495  N N   . ALA A 1 69  ? -21.259 13.994  -36.191 1.00 27.37  ? 68  ALA C N   1 
ATOM   496  C CA  . ALA A 1 69  ? -22.295 14.810  -35.575 1.00 35.64  ? 68  ALA C CA  1 
ATOM   497  C C   . ALA A 1 69  ? -22.010 16.306  -35.659 1.00 32.10  ? 68  ALA C C   1 
ATOM   498  O O   . ALA A 1 69  ? -22.869 17.104  -35.268 1.00 38.31  ? 68  ALA C O   1 
ATOM   499  C CB  . ALA A 1 69  ? -22.485 14.402  -34.111 1.00 34.60  ? 68  ALA C CB  1 
ATOM   500  N N   . ILE A 1 70  ? -20.842 16.708  -36.154 1.00 28.41  ? 69  ILE C N   1 
ATOM   501  C CA  . ILE A 1 70  ? -20.446 18.113  -36.205 1.00 31.42  ? 69  ILE C CA  1 
ATOM   502  C C   . ILE A 1 70  ? -20.457 18.577  -37.653 1.00 35.16  ? 69  ILE C C   1 
ATOM   503  O O   . ILE A 1 70  ? -19.791 17.983  -38.510 1.00 32.54  ? 69  ILE C O   1 
ATOM   504  C CB  . ILE A 1 70  ? -19.061 18.342  -35.576 1.00 25.24  ? 69  ILE C CB  1 
ATOM   505  C CG1 . ILE A 1 70  ? -19.031 17.856  -34.127 1.00 34.42  ? 69  ILE C CG1 1 
ATOM   506  C CG2 . ILE A 1 70  ? -18.699 19.814  -35.629 1.00 25.40  ? 69  ILE C CG2 1 
ATOM   507  C CD1 . ILE A 1 70  ? -17.630 17.801  -33.545 1.00 30.07  ? 69  ILE C CD1 1 
ATOM   508  N N   . THR A 1 71  ? -21.195 19.652  -37.920 1.00 33.34  ? 70  THR C N   1 
ATOM   509  C CA  . THR A 1 71  ? -21.295 20.231  -39.253 1.00 32.30  ? 70  THR C CA  1 
ATOM   510  C C   . THR A 1 71  ? -20.758 21.656  -39.222 1.00 39.35  ? 70  THR C C   1 
ATOM   511  O O   . THR A 1 71  ? -21.245 22.479  -38.426 1.00 35.46  ? 70  THR C O   1 
ATOM   512  C CB  . THR A 1 71  ? -22.745 20.213  -39.745 1.00 28.87  ? 70  THR C CB  1 
ATOM   513  O OG1 . THR A 1 71  ? -23.126 18.868  -40.057 1.00 44.50  ? 70  THR C OG1 1 
ATOM   514  C CG2 . THR A 1 71  ? -22.905 21.078  -40.985 1.00 27.38  ? 70  THR C CG2 1 
ATOM   515  N N   . PRO A 1 72  ? -19.769 21.996  -40.044 1.00 35.43  ? 71  PRO C N   1 
ATOM   516  C CA  . PRO A 1 72  ? -19.262 23.370  -40.077 1.00 38.02  ? 71  PRO C CA  1 
ATOM   517  C C   . PRO A 1 72  ? -20.031 24.236  -41.062 1.00 38.61  ? 71  PRO C C   1 
ATOM   518  O O   . PRO A 1 72  ? -20.559 23.764  -42.070 1.00 38.16  ? 71  PRO C O   1 
ATOM   519  C CB  . PRO A 1 72  ? -17.803 23.193  -40.529 1.00 40.56  ? 71  PRO C CB  1 
ATOM   520  C CG  . PRO A 1 72  ? -17.676 21.749  -41.007 1.00 37.07  ? 71  PRO C CG  1 
ATOM   521  C CD  . PRO A 1 72  ? -19.034 21.120  -40.967 1.00 40.27  ? 71  PRO C CD  1 
ATOM   522  N N   . GLY A 1 73  ? -20.096 25.529  -40.748 1.00 36.48  ? 72  GLY C N   1 
ATOM   523  C CA  . GLY A 1 73  ? -20.801 26.453  -41.624 1.00 33.20  ? 72  GLY C CA  1 
ATOM   524  C C   . GLY A 1 73  ? -21.004 27.810  -40.984 1.00 38.72  ? 72  GLY C C   1 
ATOM   525  O O   . GLY A 1 73  ? -20.221 28.236  -40.127 1.00 40.62  ? 72  GLY C O   1 
ATOM   526  N N   . LEU A 1 74  ? -22.064 28.484  -41.418 1.00 38.47  ? 73  LEU C N   1 
ATOM   527  C CA  . LEU A 1 74  ? -22.403 29.818  -40.948 1.00 40.09  ? 73  LEU C CA  1 
ATOM   528  C C   . LEU A 1 74  ? -23.702 29.783  -40.155 1.00 39.23  ? 73  LEU C C   1 
ATOM   529  O O   . LEU A 1 74  ? -24.612 29.005  -40.455 1.00 40.98  ? 73  LEU C O   1 
ATOM   530  C CB  . LEU A 1 74  ? -22.536 30.802  -42.115 1.00 32.83  ? 73  LEU C CB  1 
ATOM   531  C CG  . LEU A 1 74  ? -21.368 30.854  -43.102 1.00 42.19  ? 73  LEU C CG  1 
ATOM   532  C CD1 . LEU A 1 74  ? -21.732 31.679  -44.331 1.00 32.05  ? 73  LEU C CD1 1 
ATOM   533  C CD2 . LEU A 1 74  ? -20.118 31.406  -42.430 1.00 34.64  ? 73  LEU C CD2 1 
ATOM   534  N N   . LYS A 1 75  ? -23.781 30.648  -39.140 1.00 40.58  ? 74  LYS C N   1 
ATOM   535  C CA  . LYS A 1 75  ? -24.955 30.665  -38.274 1.00 44.35  ? 74  LYS C CA  1 
ATOM   536  C C   . LYS A 1 75  ? -26.216 31.047  -39.039 1.00 44.39  ? 74  LYS C C   1 
ATOM   537  O O   . LYS A 1 75  ? -27.321 30.645  -38.654 1.00 49.03  ? 74  LYS C O   1 
ATOM   538  C CB  . LYS A 1 75  ? -24.727 31.619  -37.101 1.00 37.02  ? 74  LYS C CB  1 
ATOM   539  C CG  . LYS A 1 75  ? -24.503 33.069  -37.492 1.00 35.64  ? 74  LYS C CG  1 
ATOM   540  C CD  . LYS A 1 75  ? -24.529 33.966  -36.264 1.00 38.93  ? 74  LYS C CD  1 
ATOM   541  C CE  . LYS A 1 75  ? -23.862 35.305  -36.526 1.00 39.11  ? 74  LYS C CE  1 
ATOM   542  N NZ  . LYS A 1 75  ? -23.989 35.723  -37.947 1.00 49.07  ? 74  LYS C NZ  1 
ATOM   543  N N   . GLU A 1 76  ? -26.077 31.816  -40.121 1.00 38.44  ? 75  GLU C N   1 
ATOM   544  C CA  . GLU A 1 76  ? -27.235 32.132  -40.951 1.00 41.77  ? 75  GLU C CA  1 
ATOM   545  C C   . GLU A 1 76  ? -27.794 30.886  -41.625 1.00 36.51  ? 75  GLU C C   1 
ATOM   546  O O   . GLU A 1 76  ? -28.991 30.829  -41.923 1.00 44.94  ? 75  GLU C O   1 
ATOM   547  C CB  . GLU A 1 76  ? -26.864 33.174  -42.007 1.00 38.43  ? 75  GLU C CB  1 
ATOM   548  C CG  . GLU A 1 76  ? -26.711 34.594  -41.482 1.00 47.63  ? 75  GLU C CG  1 
ATOM   549  C CD  . GLU A 1 76  ? -25.459 34.773  -40.642 1.00 58.10  ? 75  GLU C CD  1 
ATOM   550  O OE1 . GLU A 1 76  ? -24.528 33.944  -40.770 1.00 38.41  ? 75  GLU C OE1 1 
ATOM   551  O OE2 . GLU A 1 76  ? -25.401 35.749  -39.860 1.00 55.94  ? 75  GLU C OE2 1 
ATOM   552  N N   . ASN A 1 77  ? -26.953 29.880  -41.858 1.00 38.48  ? 76  ASN C N   1 
ATOM   553  C CA  . ASN A 1 77  ? -27.352 28.691  -42.596 1.00 43.59  ? 76  ASN C CA  1 
ATOM   554  C C   . ASN A 1 77  ? -27.749 27.520  -41.710 1.00 44.03  ? 76  ASN C C   1 
ATOM   555  O O   . ASN A 1 77  ? -28.558 26.689  -42.137 1.00 40.17  ? 76  ASN C O   1 
ATOM   556  C CB  . ASN A 1 77  ? -26.215 28.241  -43.522 1.00 36.63  ? 76  ASN C CB  1 
ATOM   557  C CG  . ASN A 1 77  ? -25.798 29.319  -44.508 1.00 43.12  ? 76  ASN C CG  1 
ATOM   558  O OD1 . ASN A 1 77  ? -26.601 30.169  -44.893 1.00 39.28  ? 76  ASN C OD1 1 
ATOM   559  N ND2 . ASN A 1 77  ? -24.533 29.287  -44.921 1.00 31.34  ? 76  ASN C ND2 1 
ATOM   560  N N   . LEU A 1 78  ? -27.211 27.426  -40.490 1.00 43.48  ? 77  LEU C N   1 
ATOM   561  C CA  . LEU A 1 78  ? -27.335 26.208  -39.699 1.00 43.82  ? 77  LEU C CA  1 
ATOM   562  C C   . LEU A 1 78  ? -28.039 26.372  -38.358 1.00 44.36  ? 77  LEU C C   1 
ATOM   563  O O   . LEU A 1 78  ? -28.275 25.360  -37.687 1.00 48.39  ? 77  LEU C O   1 
ATOM   564  C CB  . LEU A 1 78  ? -25.947 25.598  -39.441 1.00 36.82  ? 77  LEU C CB  1 
ATOM   565  C CG  . LEU A 1 78  ? -25.008 25.406  -40.636 1.00 44.04  ? 77  LEU C CG  1 
ATOM   566  C CD1 . LEU A 1 78  ? -23.732 24.700  -40.199 1.00 38.17  ? 77  LEU C CD1 1 
ATOM   567  C CD2 . LEU A 1 78  ? -25.691 24.630  -41.754 1.00 34.93  ? 77  LEU C CD2 1 
ATOM   568  N N   . CYS A 1 79  ? -28.386 27.588  -37.941 1.00 42.66  ? 78  CYS C N   1 
ATOM   569  C CA  . CYS A 1 79  ? -28.859 27.813  -36.580 1.00 45.27  ? 78  CYS C CA  1 
ATOM   570  C C   . CYS A 1 79  ? -30.337 28.177  -36.497 1.00 48.78  ? 78  CYS C C   1 
ATOM   571  O O   . CYS A 1 79  ? -30.791 28.626  -35.438 1.00 48.11  ? 78  CYS C O   1 
ATOM   572  C CB  . CYS A 1 79  ? -28.013 28.896  -35.903 1.00 43.63  ? 78  CYS C CB  1 
ATOM   573  S SG  . CYS A 1 79  ? -26.312 28.380  -35.538 1.00 41.17  ? 78  CYS C SG  1 
ATOM   574  N N   . ALA A 1 80  ? -31.104 27.981  -37.572 1.00 49.07  ? 79  ALA C N   1 
ATOM   575  C CA  . ALA A 1 80  ? -32.519 28.343  -37.539 1.00 43.17  ? 79  ALA C CA  1 
ATOM   576  C C   . ALA A 1 80  ? -33.293 27.469  -36.554 1.00 50.32  ? 79  ALA C C   1 
ATOM   577  O O   . ALA A 1 80  ? -34.029 27.982  -35.702 1.00 55.50  ? 79  ALA C O   1 
ATOM   578  C CB  . ALA A 1 80  ? -33.119 28.247  -38.942 1.00 44.50  ? 79  ALA C CB  1 
ATOM   579  N N   . ASP A 1 81  ? -33.134 26.149  -36.647 1.00 51.09  ? 80  ASP C N   1 
ATOM   580  C CA  . ASP A 1 81  ? -33.837 25.205  -35.777 1.00 54.76  ? 80  ASP C CA  1 
ATOM   581  C C   . ASP A 1 81  ? -32.924 24.674  -34.672 1.00 50.72  ? 80  ASP C C   1 
ATOM   582  O O   . ASP A 1 81  ? -32.968 23.493  -34.314 1.00 54.62  ? 80  ASP C O   1 
ATOM   583  C CB  . ASP A 1 81  ? -34.425 24.064  -36.612 1.00 52.23  ? 80  ASP C CB  1 
ATOM   584  C CG  . ASP A 1 81  ? -35.299 23.112  -35.797 1.00 70.87  ? 80  ASP C CG  1 
ATOM   585  O OD1 . ASP A 1 81  ? -35.968 23.574  -34.847 1.00 68.25  ? 80  ASP C OD1 1 
ATOM   586  O OD2 . ASP A 1 81  ? -35.317 21.901  -36.111 1.00 74.92  ? 80  ASP C OD2 1 
ATOM   587  N N   . CYS A 1 82  ? -32.070 25.525  -34.112 1.00 48.20  ? 81  CYS C N   1 
ATOM   588  C CA  . CYS A 1 82  ? -31.227 25.110  -33.000 1.00 45.11  ? 81  CYS C CA  1 
ATOM   589  C C   . CYS A 1 82  ? -31.995 25.215  -31.689 1.00 39.91  ? 81  CYS C C   1 
ATOM   590  O O   . CYS A 1 82  ? -32.845 26.092  -31.510 1.00 40.13  ? 81  CYS C O   1 
ATOM   591  C CB  . CYS A 1 82  ? -29.958 25.961  -32.929 1.00 43.70  ? 81  CYS C CB  1 
ATOM   592  S SG  . CYS A 1 82  ? -28.569 25.320  -33.897 1.00 49.21  ? 81  CYS C SG  1 
ATOM   593  N N   . ASP A 1 83  ? -31.696 24.299  -30.769 1.00 40.13  ? 82  ASP C N   1 
ATOM   594  C CA  . ASP A 1 83  ? -32.295 24.329  -29.441 1.00 48.09  ? 82  ASP C CA  1 
ATOM   595  C C   . ASP A 1 83  ? -31.427 25.038  -28.411 1.00 37.99  ? 82  ASP C C   1 
ATOM   596  O O   . ASP A 1 83  ? -31.951 25.482  -27.384 1.00 38.23  ? 82  ASP C O   1 
ATOM   597  C CB  . ASP A 1 83  ? -32.588 22.905  -28.954 1.00 38.71  ? 82  ASP C CB  1 
ATOM   598  C CG  . ASP A 1 83  ? -33.419 22.117  -29.943 1.00 43.72  ? 82  ASP C CG  1 
ATOM   599  O OD1 . ASP A 1 83  ? -34.527 22.582  -30.295 1.00 46.74  ? 82  ASP C OD1 1 
ATOM   600  O OD2 . ASP A 1 83  ? -32.957 21.041  -30.378 1.00 43.19  ? 82  ASP C OD2 1 
ATOM   601  N N   . LEU A 1 84  ? -30.126 25.159  -28.662 1.00 38.07  ? 83  LEU C N   1 
ATOM   602  C CA  . LEU A 1 84  ? -29.224 25.850  -27.755 1.00 32.27  ? 83  LEU C CA  1 
ATOM   603  C C   . LEU A 1 84  ? -28.094 26.470  -28.563 1.00 29.12  ? 83  LEU C C   1 
ATOM   604  O O   . LEU A 1 84  ? -27.567 25.847  -29.489 1.00 32.85  ? 83  LEU C O   1 
ATOM   605  C CB  . LEU A 1 84  ? -28.661 24.896  -26.694 1.00 28.40  ? 83  LEU C CB  1 
ATOM   606  C CG  . LEU A 1 84  ? -27.488 25.383  -25.837 1.00 32.07  ? 83  LEU C CG  1 
ATOM   607  C CD1 . LEU A 1 84  ? -27.941 26.399  -24.789 1.00 27.43  ? 83  LEU C CD1 1 
ATOM   608  C CD2 . LEU A 1 84  ? -26.799 24.205  -25.176 1.00 33.78  ? 83  LEU C CD2 1 
ATOM   609  N N   . ILE A 1 85  ? -27.732 27.700  -28.211 1.00 26.44  ? 84  ILE C N   1 
ATOM   610  C CA  . ILE A 1 85  ? -26.587 28.386  -28.796 1.00 24.72  ? 84  ILE C CA  1 
ATOM   611  C C   . ILE A 1 85  ? -25.565 28.604  -27.690 1.00 29.93  ? 84  ILE C C   1 
ATOM   612  O O   . ILE A 1 85  ? -25.871 29.242  -26.676 1.00 28.53  ? 84  ILE C O   1 
ATOM   613  C CB  . ILE A 1 85  ? -26.981 29.726  -29.435 1.00 27.62  ? 84  ILE C CB  1 
ATOM   614  C CG1 . ILE A 1 85  ? -27.879 29.514  -30.664 1.00 30.14  ? 84  ILE C CG1 1 
ATOM   615  C CG2 . ILE A 1 85  ? -25.733 30.515  -29.789 1.00 28.67  ? 84  ILE C CG2 1 
ATOM   616  C CD1 . ILE A 1 85  ? -27.190 28.856  -31.843 1.00 24.72  ? 84  ILE C CD1 1 
ATOM   617  N N   . VAL A 1 86  ? -24.360 28.074  -27.877 1.00 22.89  ? 85  VAL C N   1 
ATOM   618  C CA  . VAL A 1 86  ? -23.247 28.307  -26.959 1.00 25.38  ? 85  VAL C CA  1 
ATOM   619  C C   . VAL A 1 86  ? -22.182 29.066  -27.741 1.00 27.68  ? 85  VAL C C   1 
ATOM   620  O O   . VAL A 1 86  ? -21.459 28.478  -28.553 1.00 25.89  ? 85  VAL C O   1 
ATOM   621  C CB  . VAL A 1 86  ? -22.685 27.005  -26.377 1.00 21.82  ? 85  VAL C CB  1 
ATOM   622  C CG1 . VAL A 1 86  ? -21.510 27.311  -25.461 1.00 19.09  ? 85  VAL C CG1 1 
ATOM   623  C CG2 . VAL A 1 86  ? -23.765 26.234  -25.630 1.00 26.08  ? 85  VAL C CG2 1 
ATOM   624  N N   . GLU A 1 87  ? -22.076 30.372  -27.514 1.00 28.81  ? 86  GLU C N   1 
ATOM   625  C CA  . GLU A 1 87  ? -21.062 31.151  -28.206 1.00 33.74  ? 86  GLU C CA  1 
ATOM   626  C C   . GLU A 1 87  ? -19.732 31.038  -27.469 1.00 35.20  ? 86  GLU C C   1 
ATOM   627  O O   . GLU A 1 87  ? -19.677 31.090  -26.236 1.00 26.85  ? 86  GLU C O   1 
ATOM   628  C CB  . GLU A 1 87  ? -21.497 32.615  -28.338 1.00 30.63  ? 86  GLU C CB  1 
ATOM   629  C CG  . GLU A 1 87  ? -21.053 33.535  -27.200 1.00 38.82  ? 86  GLU C CG  1 
ATOM   630  C CD  . GLU A 1 87  ? -19.626 34.056  -27.366 1.00 48.68  ? 86  GLU C CD  1 
ATOM   631  O OE1 . GLU A 1 87  ? -19.022 34.419  -26.339 1.00 46.66  ? 86  GLU C OE1 1 
ATOM   632  O OE2 . GLU A 1 87  ? -19.108 34.084  -28.506 1.00 45.37  ? 86  GLU C OE2 1 
ATOM   633  N N   . ALA A 1 88  ? -18.660 30.872  -28.234 1.00 27.77  ? 87  ALA C N   1 
ATOM   634  C CA  . ALA A 1 88  ? -17.324 30.750  -27.668 1.00 29.79  ? 87  ALA C CA  1 
ATOM   635  C C   . ALA A 1 88  ? -16.316 31.423  -28.598 1.00 33.66  ? 87  ALA C C   1 
ATOM   636  O O   . ALA A 1 88  ? -15.267 30.865  -28.924 1.00 34.39  ? 87  ALA C O   1 
ATOM   637  C CB  . ALA A 1 88  ? -16.972 29.283  -27.424 1.00 25.90  ? 87  ALA C CB  1 
ATOM   638  N N   . ALA A 1 89  ? -16.629 32.640  -29.030 1.00 36.62  ? 88  ALA C N   1 
ATOM   639  C CA  . ALA A 1 89  ? -15.788 33.379  -29.957 1.00 38.78  ? 88  ALA C CA  1 
ATOM   640  C C   . ALA A 1 89  ? -14.798 34.254  -29.184 1.00 40.67  ? 88  ALA C C   1 
ATOM   641  O O   . ALA A 1 89  ? -14.605 34.101  -27.975 1.00 46.62  ? 88  ALA C O   1 
ATOM   642  C CB  . ALA A 1 89  ? -16.658 34.200  -30.906 1.00 40.12  ? 88  ALA C CB  1 
ATOM   643  N N   . PHE A 1 90  ? -14.163 35.190  -29.886 1.00 45.12  ? 89  PHE C N   1 
ATOM   644  C CA  . PHE A 1 90  ? -13.152 36.041  -29.274 1.00 43.38  ? 89  PHE C CA  1 
ATOM   645  C C   . PHE A 1 90  ? -13.784 36.930  -28.210 1.00 44.88  ? 89  PHE C C   1 
ATOM   646  O O   . PHE A 1 90  ? -14.897 37.435  -28.378 1.00 38.87  ? 89  PHE C O   1 
ATOM   647  C CB  . PHE A 1 90  ? -12.465 36.884  -30.354 1.00 54.31  ? 89  PHE C CB  1 
ATOM   648  C CG  . PHE A 1 90  ? -11.586 37.984  -29.818 1.00 73.08  ? 89  PHE C CG  1 
ATOM   649  C CD1 . PHE A 1 90  ? -10.619 37.725  -28.855 1.00 72.32  ? 89  PHE C CD1 1 
ATOM   650  C CD2 . PHE A 1 90  ? -11.716 39.279  -30.296 1.00 70.83  ? 89  PHE C CD2 1 
ATOM   651  C CE1 . PHE A 1 90  ? -9.812  38.745  -28.371 1.00 68.98  ? 89  PHE C CE1 1 
ATOM   652  C CE2 . PHE A 1 90  ? -10.911 40.298  -29.819 1.00 63.49  ? 89  PHE C CE2 1 
ATOM   653  C CZ  . PHE A 1 90  ? -9.959  40.031  -28.856 1.00 61.34  ? 89  PHE C CZ  1 
ATOM   654  N N   . GLU A 1 91  ? -13.065 37.109  -27.100 1.00 46.40  ? 90  GLU C N   1 
ATOM   655  C CA  . GLU A 1 91  ? -13.560 37.878  -25.958 1.00 43.86  ? 90  GLU C CA  1 
ATOM   656  C C   . GLU A 1 91  ? -13.513 39.369  -26.283 1.00 42.22  ? 90  GLU C C   1 
ATOM   657  O O   . GLU A 1 91  ? -12.599 40.103  -25.899 1.00 46.63  ? 90  GLU C O   1 
ATOM   658  C CB  . GLU A 1 91  ? -12.752 37.555  -24.706 1.00 48.80  ? 90  GLU C CB  1 
ATOM   659  C CG  . GLU A 1 91  ? -12.919 36.123  -24.213 1.00 46.46  ? 90  GLU C CG  1 
ATOM   660  C CD  . GLU A 1 91  ? -13.841 36.027  -23.012 1.00 48.53  ? 90  GLU C CD  1 
ATOM   661  O OE1 . GLU A 1 91  ? -14.843 36.775  -22.969 1.00 41.67  ? 90  GLU C OE1 1 
ATOM   662  O OE2 . GLU A 1 91  ? -13.563 35.209  -22.108 1.00 54.69  ? 90  GLU C OE2 1 
ATOM   663  N N   . ASP A 1 92  ? -14.531 39.822  -27.010 1.00 40.92  ? 91  ASP C N   1 
ATOM   664  C CA  . ASP A 1 92  ? -14.730 41.234  -27.305 1.00 35.57  ? 91  ASP C CA  1 
ATOM   665  C C   . ASP A 1 92  ? -16.212 41.537  -27.154 1.00 35.54  ? 91  ASP C C   1 
ATOM   666  O O   . ASP A 1 92  ? -17.048 40.827  -27.723 1.00 31.71  ? 91  ASP C O   1 
ATOM   667  C CB  . ASP A 1 92  ? -14.252 41.590  -28.719 1.00 40.94  ? 91  ASP C CB  1 
ATOM   668  C CG  . ASP A 1 92  ? -14.673 42.990  -29.141 1.00 46.34  ? 91  ASP C CG  1 
ATOM   669  O OD1 . ASP A 1 92  ? -13.913 43.948  -28.877 1.00 55.64  ? 91  ASP C OD1 1 
ATOM   670  O OD2 . ASP A 1 92  ? -15.768 43.137  -29.725 1.00 42.65  ? 91  ASP C OD2 1 
ATOM   671  N N   . MET A 1 93  ? -16.531 42.590  -26.398 1.00 28.89  ? 92  MET C N   1 
ATOM   672  C CA  . MET A 1 93  ? -17.923 42.883  -26.061 1.00 31.17  ? 92  MET C CA  1 
ATOM   673  C C   . MET A 1 93  ? -18.764 43.115  -27.314 1.00 33.59  ? 92  MET C C   1 
ATOM   674  O O   . MET A 1 93  ? -19.790 42.456  -27.518 1.00 28.10  ? 92  MET C O   1 
ATOM   675  C CB  . MET A 1 93  ? -17.990 44.094  -25.126 1.00 25.56  ? 92  MET C CB  1 
ATOM   676  C CG  . MET A 1 93  ? -19.402 44.495  -24.692 1.00 24.46  ? 92  MET C CG  1 
ATOM   677  S SD  . MET A 1 93  ? -20.401 43.157  -23.990 1.00 37.36  ? 92  MET C SD  1 
ATOM   678  C CE  . MET A 1 93  ? -19.441 42.762  -22.524 1.00 31.98  ? 92  MET C CE  1 
ATOM   679  N N   . LYS A 1 94  ? -18.333 44.042  -28.176 1.00 39.89  ? 93  LYS C N   1 
ATOM   680  C CA  . LYS A 1 94  ? -19.128 44.400  -29.350 1.00 39.34  ? 93  LYS C CA  1 
ATOM   681  C C   . LYS A 1 94  ? -19.368 43.202  -30.259 1.00 29.82  ? 93  LYS C C   1 
ATOM   682  O O   . LYS A 1 94  ? -20.465 43.042  -30.806 1.00 29.33  ? 93  LYS C O   1 
ATOM   683  C CB  . LYS A 1 94  ? -18.446 45.528  -30.122 1.00 46.67  ? 93  LYS C CB  1 
ATOM   684  C CG  . LYS A 1 94  ? -19.072 46.893  -29.891 1.00 53.33  ? 93  LYS C CG  1 
ATOM   685  C CD  . LYS A 1 94  ? -18.012 47.959  -29.692 1.00 63.98  ? 93  LYS C CD  1 
ATOM   686  C CE  . LYS A 1 94  ? -18.615 49.352  -29.730 1.00 62.78  ? 93  LYS C CE  1 
ATOM   687  N NZ  . LYS A 1 94  ? -17.747 50.321  -29.017 1.00 59.94  ? 93  LYS C NZ  1 
ATOM   688  N N   . VAL A 1 95  ? -18.358 42.347  -30.432 1.00 36.30  ? 94  VAL C N   1 
ATOM   689  C CA  . VAL A 1 95  ? -18.524 41.168  -31.278 1.00 32.66  ? 94  VAL C CA  1 
ATOM   690  C C   . VAL A 1 95  ? -19.603 40.254  -30.710 1.00 34.82  ? 94  VAL C C   1 
ATOM   691  O O   . VAL A 1 95  ? -20.390 39.655  -31.454 1.00 34.20  ? 94  VAL C O   1 
ATOM   692  C CB  . VAL A 1 95  ? -17.179 40.433  -31.435 1.00 39.48  ? 94  VAL C CB  1 
ATOM   693  C CG1 . VAL A 1 95  ? -17.384 39.055  -32.053 1.00 32.31  ? 94  VAL C CG1 1 
ATOM   694  C CG2 . VAL A 1 95  ? -16.212 41.266  -32.265 1.00 34.52  ? 94  VAL C CG2 1 
ATOM   695  N N   . LYS A 1 96  ? -19.672 40.153  -29.381 1.00 31.67  ? 95  LYS C N   1 
ATOM   696  C CA  . LYS A 1 96  ? -20.650 39.273  -28.749 1.00 30.32  ? 95  LYS C CA  1 
ATOM   697  C C   . LYS A 1 96  ? -22.063 39.830  -28.871 1.00 29.67  ? 95  LYS C C   1 
ATOM   698  O O   . LYS A 1 96  ? -23.011 39.078  -29.129 1.00 26.77  ? 95  LYS C O   1 
ATOM   699  C CB  . LYS A 1 96  ? -20.280 39.061  -27.283 1.00 33.35  ? 95  LYS C CB  1 
ATOM   700  C CG  . LYS A 1 96  ? -18.939 38.381  -27.096 1.00 29.65  ? 95  LYS C CG  1 
ATOM   701  C CD  . LYS A 1 96  ? -18.993 37.361  -25.993 1.00 34.55  ? 95  LYS C CD  1 
ATOM   702  C CE  . LYS A 1 96  ? -17.622 37.116  -25.392 1.00 41.50  ? 95  LYS C CE  1 
ATOM   703  N NZ  . LYS A 1 96  ? -16.968 35.925  -25.989 1.00 38.44  ? 95  LYS C NZ  1 
ATOM   704  N N   . GLN A 1 97  ? -22.230 41.142  -28.676 1.00 31.90  ? 96  GLN C N   1 
ATOM   705  C CA  . GLN A 1 97  ? -23.554 41.733  -28.832 1.00 31.27  ? 96  GLN C CA  1 
ATOM   706  C C   . GLN A 1 97  ? -24.016 41.675  -30.280 1.00 30.18  ? 96  GLN C C   1 
ATOM   707  O O   . GLN A 1 97  ? -25.214 41.517  -30.542 1.00 36.01  ? 96  GLN C O   1 
ATOM   708  C CB  . GLN A 1 97  ? -23.568 43.180  -28.328 1.00 33.26  ? 96  GLN C CB  1 
ATOM   709  C CG  . GLN A 1 97  ? -22.590 43.465  -27.194 1.00 41.10  ? 96  GLN C CG  1 
ATOM   710  C CD  . GLN A 1 97  ? -22.947 44.703  -26.392 1.00 34.26  ? 96  GLN C CD  1 
ATOM   711  O OE1 . GLN A 1 97  ? -22.362 45.770  -26.577 1.00 29.77  ? 96  GLN C OE1 1 
ATOM   712  N NE2 . GLN A 1 97  ? -23.896 44.559  -25.479 1.00 35.89  ? 96  GLN C NE2 1 
ATOM   713  N N   . THR A 1 98  ? -23.087 41.792  -31.230 1.00 33.10  ? 97  THR C N   1 
ATOM   714  C CA  . THR A 1 98  ? -23.459 41.677  -32.635 1.00 35.11  ? 97  THR C CA  1 
ATOM   715  C C   . THR A 1 98  ? -23.875 40.252  -32.976 1.00 33.59  ? 97  THR C C   1 
ATOM   716  O O   . THR A 1 98  ? -24.901 40.039  -33.634 1.00 35.71  ? 97  THR C O   1 
ATOM   717  C CB  . THR A 1 98  ? -22.301 42.129  -33.522 1.00 34.49  ? 97  THR C CB  1 
ATOM   718  O OG1 . THR A 1 98  ? -22.048 43.522  -33.298 1.00 36.63  ? 97  THR C OG1 1 
ATOM   719  C CG2 . THR A 1 98  ? -22.639 41.912  -34.992 1.00 32.19  ? 97  THR C CG2 1 
ATOM   720  N N   . THR A 1 99  ? -23.099 39.265  -32.522 1.00 32.19  ? 98  THR C N   1 
ATOM   721  C CA  . THR A 1 99  ? -23.431 37.869  -32.790 1.00 37.54  ? 98  THR C CA  1 
ATOM   722  C C   . THR A 1 99  ? -24.815 37.523  -32.259 1.00 35.47  ? 98  THR C C   1 
ATOM   723  O O   . THR A 1 99  ? -25.643 36.949  -32.976 1.00 36.43  ? 98  THR C O   1 
ATOM   724  C CB  . THR A 1 99  ? -22.380 36.948  -32.169 1.00 35.08  ? 98  THR C CB  1 
ATOM   725  O OG1 . THR A 1 99  ? -21.107 37.188  -32.780 1.00 36.36  ? 98  THR C OG1 1 
ATOM   726  C CG2 . THR A 1 99  ? -22.761 35.494  -32.379 1.00 36.99  ? 98  THR C CG2 1 
ATOM   727  N N   . PHE A 1 100 ? -25.092 37.879  -31.003 1.00 34.04  ? 99  PHE C N   1 
ATOM   728  C CA  . PHE A 1 100 ? -26.383 37.523  -30.424 1.00 34.04  ? 99  PHE C CA  1 
ATOM   729  C C   . PHE A 1 100 ? -27.515 38.361  -31.005 1.00 31.46  ? 99  PHE C C   1 
ATOM   730  O O   . PHE A 1 100 ? -28.650 37.880  -31.102 1.00 37.20  ? 99  PHE C O   1 
ATOM   731  C CB  . PHE A 1 100 ? -26.326 37.646  -28.902 1.00 31.10  ? 99  PHE C CB  1 
ATOM   732  C CG  . PHE A 1 100 ? -25.743 36.435  -28.229 1.00 32.17  ? 99  PHE C CG  1 
ATOM   733  C CD1 . PHE A 1 100 ? -26.316 35.186  -28.409 1.00 30.89  ? 99  PHE C CD1 1 
ATOM   734  C CD2 . PHE A 1 100 ? -24.610 36.539  -27.438 1.00 27.87  ? 99  PHE C CD2 1 
ATOM   735  C CE1 . PHE A 1 100 ? -25.778 34.064  -27.803 1.00 24.51  ? 99  PHE C CE1 1 
ATOM   736  C CE2 . PHE A 1 100 ? -24.067 35.422  -26.833 1.00 24.12  ? 99  PHE C CE2 1 
ATOM   737  C CZ  . PHE A 1 100 ? -24.654 34.183  -27.014 1.00 26.26  ? 99  PHE C CZ  1 
ATOM   738  N N   . GLY A 1 101 ? -27.234 39.603  -31.402 1.00 27.26  ? 100 GLY C N   1 
ATOM   739  C CA  . GLY A 1 101 ? -28.246 40.385  -32.092 1.00 34.61  ? 100 GLY C CA  1 
ATOM   740  C C   . GLY A 1 101 ? -28.672 39.743  -33.399 1.00 41.40  ? 100 GLY C C   1 
ATOM   741  O O   . GLY A 1 101 ? -29.864 39.689  -33.718 1.00 36.47  ? 100 GLY C O   1 
ATOM   742  N N   . GLU A 1 102 ? -27.705 39.232  -34.165 1.00 31.66  ? 101 GLU C N   1 
ATOM   743  C CA  . GLU A 1 102 ? -28.031 38.519  -35.395 1.00 39.24  ? 101 GLU C CA  1 
ATOM   744  C C   . GLU A 1 102 ? -28.720 37.192  -35.099 1.00 39.79  ? 101 GLU C C   1 
ATOM   745  O O   . GLU A 1 102 ? -29.711 36.842  -35.751 1.00 39.34  ? 101 GLU C O   1 
ATOM   746  C CB  . GLU A 1 102 ? -26.764 38.290  -36.218 1.00 32.32  ? 101 GLU C CB  1 
ATOM   747  C CG  . GLU A 1 102 ? -26.361 39.475  -37.073 1.00 40.22  ? 101 GLU C CG  1 
ATOM   748  C CD  . GLU A 1 102 ? -24.860 39.581  -37.240 1.00 52.29  ? 101 GLU C CD  1 
ATOM   749  O OE1 . GLU A 1 102 ? -24.156 38.603  -36.906 1.00 56.59  ? 101 GLU C OE1 1 
ATOM   750  O OE2 . GLU A 1 102 ? -24.382 40.637  -37.706 1.00 58.18  ? 101 GLU C OE2 1 
ATOM   751  N N   . LEU A 1 103 ? -28.212 36.443  -34.117 1.00 37.11  ? 102 LEU C N   1 
ATOM   752  C CA  . LEU A 1 103 ? -28.816 35.163  -33.771 1.00 36.50  ? 102 LEU C CA  1 
ATOM   753  C C   . LEU A 1 103 ? -30.243 35.321  -33.265 1.00 34.01  ? 102 LEU C C   1 
ATOM   754  O O   . LEU A 1 103 ? -31.035 34.379  -33.377 1.00 32.78  ? 102 LEU C O   1 
ATOM   755  C CB  . LEU A 1 103 ? -27.961 34.448  -32.723 1.00 36.31  ? 102 LEU C CB  1 
ATOM   756  C CG  . LEU A 1 103 ? -26.703 33.751  -33.251 1.00 39.41  ? 102 LEU C CG  1 
ATOM   757  C CD1 . LEU A 1 103 ? -25.770 33.386  -32.106 1.00 35.88  ? 102 LEU C CD1 1 
ATOM   758  C CD2 . LEU A 1 103 ? -27.055 32.519  -34.071 1.00 31.98  ? 102 LEU C CD2 1 
ATOM   759  N N   . ASP A 1 104 ? -30.591 36.489  -32.718 1.00 32.11  ? 103 ASP C N   1 
ATOM   760  C CA  . ASP A 1 104 ? -31.954 36.699  -32.244 1.00 37.93  ? 103 ASP C CA  1 
ATOM   761  C C   . ASP A 1 104 ? -32.964 36.642  -33.385 1.00 39.12  ? 103 ASP C C   1 
ATOM   762  O O   . ASP A 1 104 ? -34.106 36.217  -33.179 1.00 44.95  ? 103 ASP C O   1 
ATOM   763  C CB  . ASP A 1 104 ? -32.058 38.033  -31.505 1.00 31.92  ? 103 ASP C CB  1 
ATOM   764  C CG  . ASP A 1 104 ? -33.026 37.977  -30.335 1.00 38.86  ? 103 ASP C CG  1 
ATOM   765  O OD1 . ASP A 1 104 ? -33.544 36.877  -30.038 1.00 37.55  ? 103 ASP C OD1 1 
ATOM   766  O OD2 . ASP A 1 104 ? -33.276 39.037  -29.720 1.00 38.97  ? 103 ASP C OD2 1 
ATOM   767  N N   . LYS A 1 105 ? -32.562 37.056  -34.588 1.00 37.51  ? 104 LYS C N   1 
ATOM   768  C CA  . LYS A 1 105 ? -33.427 37.002  -35.763 1.00 38.29  ? 104 LYS C CA  1 
ATOM   769  C C   . LYS A 1 105 ? -33.398 35.650  -36.464 1.00 37.99  ? 104 LYS C C   1 
ATOM   770  O O   . LYS A 1 105 ? -34.411 35.243  -37.044 1.00 46.68  ? 104 LYS C O   1 
ATOM   771  C CB  . LYS A 1 105 ? -33.032 38.091  -36.766 1.00 42.42  ? 104 LYS C CB  1 
ATOM   772  C CG  . LYS A 1 105 ? -33.137 39.512  -36.236 1.00 27.98  ? 104 LYS C CG  1 
ATOM   773  C CD  . LYS A 1 105 ? -32.663 40.520  -37.274 1.00 38.52  ? 104 LYS C CD  1 
ATOM   774  C CE  . LYS A 1 105 ? -32.648 41.928  -36.709 1.00 49.53  ? 104 LYS C CE  1 
ATOM   775  N NZ  . LYS A 1 105 ? -31.722 42.040  -35.546 1.00 55.12  ? 104 LYS C NZ  1 
ATOM   776  N N   . ILE A 1 106 ? -32.265 34.945  -36.420 1.00 37.26  ? 105 ILE C N   1 
ATOM   777  C CA  . ILE A 1 106 ? -32.133 33.677  -37.131 1.00 38.80  ? 105 ILE C CA  1 
ATOM   778  C C   . ILE A 1 106 ? -32.839 32.547  -36.387 1.00 42.36  ? 105 ILE C C   1 
ATOM   779  O O   . ILE A 1 106 ? -33.535 31.727  -36.998 1.00 44.06  ? 105 ILE C O   1 
ATOM   780  C CB  . ILE A 1 106 ? -30.643 33.356  -37.354 1.00 31.96  ? 105 ILE C CB  1 
ATOM   781  C CG1 . ILE A 1 106 ? -29.984 34.426  -38.223 1.00 35.27  ? 105 ILE C CG1 1 
ATOM   782  C CG2 . ILE A 1 106 ? -30.469 31.975  -37.977 1.00 41.87  ? 105 ILE C CG2 1 
ATOM   783  C CD1 . ILE A 1 106 ? -28.479 34.504  -38.051 1.00 41.11  ? 105 ILE C CD1 1 
ATOM   784  N N   . CYS A 1 107 ? -32.683 32.486  -35.067 1.00 42.92  ? 106 CYS C N   1 
ATOM   785  C CA  . CYS A 1 107 ? -33.076 31.306  -34.310 1.00 42.39  ? 106 CYS C CA  1 
ATOM   786  C C   . CYS A 1 107 ? -34.563 31.317  -33.974 1.00 41.15  ? 106 CYS C C   1 
ATOM   787  O O   . CYS A 1 107 ? -35.179 32.372  -33.804 1.00 44.89  ? 106 CYS C O   1 
ATOM   788  C CB  . CYS A 1 107 ? -32.262 31.209  -33.020 1.00 37.37  ? 106 CYS C CB  1 
ATOM   789  S SG  . CYS A 1 107 ? -30.474 31.122  -33.272 1.00 39.54  ? 106 CYS C SG  1 
ATOM   790  N N   . LYS A 1 108 ? -35.133 30.113  -33.869 1.00 37.66  ? 107 LYS C N   1 
ATOM   791  C CA  . LYS A 1 108 ? -36.511 29.965  -33.430 1.00 41.29  ? 107 LYS C CA  1 
ATOM   792  C C   . LYS A 1 108 ? -36.661 30.493  -32.002 1.00 46.84  ? 107 LYS C C   1 
ATOM   793  O O   . LYS A 1 108 ? -35.677 30.602  -31.265 1.00 45.78  ? 107 LYS C O   1 
ATOM   794  C CB  . LYS A 1 108 ? -36.935 28.496  -33.511 1.00 35.03  ? 107 LYS C CB  1 
ATOM   795  C CG  . LYS A 1 108 ? -36.303 27.598  -32.458 1.00 47.94  ? 107 LYS C CG  1 
ATOM   796  C CD  . LYS A 1 108 ? -36.259 26.144  -32.912 1.00 47.35  ? 107 LYS C CD  1 
ATOM   797  C CE  . LYS A 1 108 ? -36.390 25.189  -31.729 1.00 51.01  ? 107 LYS C CE  1 
ATOM   798  N NZ  . LYS A 1 108 ? -35.838 23.832  -32.010 1.00 42.85  ? 107 LYS C NZ  1 
ATOM   799  N N   . PRO A 1 109 ? -37.885 30.843  -31.592 1.00 49.75  ? 108 PRO C N   1 
ATOM   800  C CA  . PRO A 1 109 ? -38.064 31.423  -30.248 1.00 47.76  ? 108 PRO C CA  1 
ATOM   801  C C   . PRO A 1 109 ? -37.676 30.491  -29.109 1.00 46.85  ? 108 PRO C C   1 
ATOM   802  O O   . PRO A 1 109 ? -37.215 30.971  -28.066 1.00 44.59  ? 108 PRO C O   1 
ATOM   803  C CB  . PRO A 1 109 ? -39.562 31.763  -30.211 1.00 51.53  ? 108 PRO C CB  1 
ATOM   804  C CG  . PRO A 1 109 ? -39.956 31.903  -31.643 1.00 55.21  ? 108 PRO C CG  1 
ATOM   805  C CD  . PRO A 1 109 ? -39.125 30.902  -32.388 1.00 51.13  ? 108 PRO C CD  1 
ATOM   806  N N   . GLU A 1 110 ? -37.844 29.175  -29.273 1.00 45.05  ? 109 GLU C N   1 
ATOM   807  C CA  . GLU A 1 110 ? -37.535 28.239  -28.194 1.00 42.02  ? 109 GLU C CA  1 
ATOM   808  C C   . GLU A 1 110 ? -36.040 28.135  -27.915 1.00 42.65  ? 109 GLU C C   1 
ATOM   809  O O   . GLU A 1 110 ? -35.656 27.623  -26.858 1.00 42.37  ? 109 GLU C O   1 
ATOM   810  C CB  . GLU A 1 110 ? -38.083 26.846  -28.520 1.00 40.14  ? 109 GLU C CB  1 
ATOM   811  C CG  . GLU A 1 110 ? -39.597 26.763  -28.608 1.00 56.01  ? 109 GLU C CG  1 
ATOM   812  C CD  . GLU A 1 110 ? -40.126 27.154  -29.977 1.00 63.87  ? 109 GLU C CD  1 
ATOM   813  O OE1 . GLU A 1 110 ? -39.332 27.169  -30.945 1.00 53.69  ? 109 GLU C OE1 1 
ATOM   814  O OE2 . GLU A 1 110 ? -41.336 27.447  -30.082 1.00 72.41  ? 109 GLU C OE2 1 
ATOM   815  N N   . CYS A 1 111 ? -35.197 28.607  -28.830 1.00 36.61  ? 110 CYS C N   1 
ATOM   816  C CA  . CYS A 1 111 ? -33.756 28.433  -28.701 1.00 36.62  ? 110 CYS C CA  1 
ATOM   817  C C   . CYS A 1 111 ? -33.221 29.197  -27.493 1.00 36.68  ? 110 CYS C C   1 
ATOM   818  O O   . CYS A 1 111 ? -33.560 30.367  -27.285 1.00 35.80  ? 110 CYS C O   1 
ATOM   819  C CB  . CYS A 1 111 ? -33.060 28.905  -29.975 1.00 32.75  ? 110 CYS C CB  1 
ATOM   820  S SG  . CYS A 1 111 ? -31.313 28.487  -30.066 1.00 38.50  ? 110 CYS C SG  1 
ATOM   821  N N   . ILE A 1 112 ? -32.376 28.527  -26.697 1.00 29.81  ? 111 ILE C N   1 
ATOM   822  C CA  . ILE A 1 112 ? -31.736 29.127  -25.529 1.00 33.89  ? 111 ILE C CA  1 
ATOM   823  C C   . ILE A 1 112 ? -30.406 29.742  -25.948 1.00 31.16  ? 111 ILE C C   1 
ATOM   824  O O   . ILE A 1 112 ? -29.637 29.140  -26.709 1.00 28.17  ? 111 ILE C O   1 
ATOM   825  C CB  . ILE A 1 112 ? -31.539 28.082  -24.413 1.00 35.62  ? 111 ILE C CB  1 
ATOM   826  C CG1 . ILE A 1 112 ? -32.886 27.669  -23.816 1.00 43.57  ? 111 ILE C CG1 1 
ATOM   827  C CG2 . ILE A 1 112 ? -30.627 28.622  -23.321 1.00 30.85  ? 111 ILE C CG2 1 
ATOM   828  C CD1 . ILE A 1 112 ? -33.024 26.173  -23.595 1.00 37.00  ? 111 ILE C CD1 1 
ATOM   829  N N   . PHE A 1 113 ? -30.130 30.945  -25.450 1.00 27.33  ? 112 PHE C N   1 
ATOM   830  C CA  . PHE A 1 113 ? -28.906 31.671  -25.772 1.00 33.58  ? 112 PHE C CA  1 
ATOM   831  C C   . PHE A 1 113 ? -27.938 31.589  -24.595 1.00 30.47  ? 112 PHE C C   1 
ATOM   832  O O   . PHE A 1 113 ? -28.244 32.072  -23.500 1.00 30.20  ? 112 PHE C O   1 
ATOM   833  C CB  . PHE A 1 113 ? -29.217 33.128  -26.113 1.00 29.00  ? 112 PHE C CB  1 
ATOM   834  C CG  . PHE A 1 113 ? -29.738 33.327  -27.508 1.00 30.26  ? 112 PHE C CG  1 
ATOM   835  C CD1 . PHE A 1 113 ? -29.999 32.239  -28.327 1.00 29.77  ? 112 PHE C CD1 1 
ATOM   836  C CD2 . PHE A 1 113 ? -29.962 34.601  -28.004 1.00 34.25  ? 112 PHE C CD2 1 
ATOM   837  C CE1 . PHE A 1 113 ? -30.479 32.416  -29.609 1.00 33.42  ? 112 PHE C CE1 1 
ATOM   838  C CE2 . PHE A 1 113 ? -30.445 34.786  -29.288 1.00 35.99  ? 112 PHE C CE2 1 
ATOM   839  C CZ  . PHE A 1 113 ? -30.701 33.692  -30.091 1.00 34.50  ? 112 PHE C CZ  1 
ATOM   840  N N   . ALA A 1 114 ? -26.775 30.983  -24.822 1.00 25.82  ? 113 ALA C N   1 
ATOM   841  C CA  . ALA A 1 114 ? -25.752 30.841  -23.797 1.00 23.06  ? 113 ALA C CA  1 
ATOM   842  C C   . ALA A 1 114 ? -24.418 31.353  -24.323 1.00 28.87  ? 113 ALA C C   1 
ATOM   843  O O   . ALA A 1 114 ? -24.175 31.393  -25.532 1.00 33.70  ? 113 ALA C O   1 
ATOM   844  C CB  . ALA A 1 114 ? -25.608 29.383  -23.343 1.00 19.96  ? 113 ALA C CB  1 
ATOM   845  N N   . SER A 1 115 ? -23.542 31.740  -23.397 1.00 28.13  ? 114 SER C N   1 
ATOM   846  C CA  . SER A 1 115 ? -22.210 32.208  -23.752 1.00 15.75  ? 114 SER C CA  1 
ATOM   847  C C   . SER A 1 115 ? -21.169 31.629  -22.803 1.00 26.86  ? 114 SER C C   1 
ATOM   848  O O   . SER A 1 115 ? -21.355 31.628  -21.582 1.00 24.42  ? 114 SER C O   1 
ATOM   849  C CB  . SER A 1 115 ? -22.126 33.735  -23.727 1.00 20.54  ? 114 SER C CB  1 
ATOM   850  O OG  . SER A 1 115 ? -20.778 34.150  -23.869 1.00 25.88  ? 114 SER C OG  1 
ATOM   851  N N   . ASN A 1 116 ? -20.062 31.159  -23.379 1.00 22.26  ? 115 ASN C N   1 
ATOM   852  C CA  . ASN A 1 116 ? -18.954 30.568  -22.643 1.00 26.86  ? 115 ASN C CA  1 
ATOM   853  C C   . ASN A 1 116 ? -17.955 31.613  -22.135 1.00 24.03  ? 115 ASN C C   1 
ATOM   854  O O   . ASN A 1 116 ? -16.825 31.258  -21.778 1.00 24.45  ? 115 ASN C O   1 
ATOM   855  C CB  . ASN A 1 116 ? -18.242 29.538  -23.530 1.00 25.24  ? 115 ASN C CB  1 
ATOM   856  C CG  . ASN A 1 116 ? -17.163 28.761  -22.791 1.00 26.28  ? 115 ASN C CG  1 
ATOM   857  O OD1 . ASN A 1 116 ? -17.420 28.163  -21.749 1.00 36.76  ? 115 ASN C OD1 1 
ATOM   858  N ND2 . ASN A 1 116 ? -15.945 28.787  -23.320 1.00 30.14  ? 115 ASN C ND2 1 
ATOM   859  N N   . THR A 1 117 ? -18.339 32.886  -22.091 1.00 18.31  ? 116 THR C N   1 
ATOM   860  C CA  . THR A 1 117 ? -17.387 33.920  -21.706 1.00 22.43  ? 116 THR C CA  1 
ATOM   861  C C   . THR A 1 117 ? -16.903 33.712  -20.273 1.00 38.01  ? 116 THR C C   1 
ATOM   862  O O   . THR A 1 117 ? -17.607 33.162  -19.421 1.00 34.53  ? 116 THR C O   1 
ATOM   863  C CB  . THR A 1 117 ? -18.011 35.310  -21.851 1.00 29.73  ? 116 THR C CB  1 
ATOM   864  O OG1 . THR A 1 117 ? -17.023 36.306  -21.560 1.00 31.51  ? 116 THR C OG1 1 
ATOM   865  C CG2 . THR A 1 117 ? -19.188 35.482  -20.898 1.00 25.80  ? 116 THR C CG2 1 
ATOM   866  N N   . ALA A 1 118 ? -15.667 34.141  -20.022 1.00 33.46  ? 117 ALA C N   1 
ATOM   867  C CA  . ALA A 1 118 ? -15.108 34.157  -18.680 1.00 37.15  ? 117 ALA C CA  1 
ATOM   868  C C   . ALA A 1 118 ? -14.706 35.543  -18.201 1.00 40.44  ? 117 ALA C C   1 
ATOM   869  O O   . ALA A 1 118 ? -14.602 35.745  -16.987 1.00 35.56  ? 117 ALA C O   1 
ATOM   870  C CB  . ALA A 1 118 ? -13.883 33.233  -18.593 1.00 30.63  ? 117 ALA C CB  1 
ATOM   871  N N   . SER A 1 119 ? -14.497 36.503  -19.110 1.00 39.37  ? 118 SER C N   1 
ATOM   872  C CA  . SER A 1 119 ? -14.010 37.828  -18.755 1.00 31.32  ? 118 SER C CA  1 
ATOM   873  C C   . SER A 1 119 ? -15.046 38.930  -18.900 1.00 35.86  ? 118 SER C C   1 
ATOM   874  O O   . SER A 1 119 ? -14.830 40.025  -18.375 1.00 32.40  ? 118 SER C O   1 
ATOM   875  C CB  . SER A 1 119 ? -12.800 38.199  -19.623 1.00 35.19  ? 118 SER C CB  1 
ATOM   876  O OG  . SER A 1 119 ? -12.323 37.075  -20.338 1.00 48.86  ? 118 SER C OG  1 
ATOM   877  N N   . LEU A 1 120 ? -16.143 38.682  -19.606 1.00 38.33  ? 119 LEU C N   1 
ATOM   878  C CA  . LEU A 1 120 ? -17.118 39.713  -19.916 1.00 38.27  ? 119 LEU C CA  1 
ATOM   879  C C   . LEU A 1 120 ? -18.419 39.462  -19.164 1.00 33.90  ? 119 LEU C C   1 
ATOM   880  O O   . LEU A 1 120 ? -18.675 38.364  -18.661 1.00 36.89  ? 119 LEU C O   1 
ATOM   881  C CB  . LEU A 1 120 ? -17.374 39.784  -21.428 1.00 30.53  ? 119 LEU C CB  1 
ATOM   882  C CG  . LEU A 1 120 ? -16.125 40.008  -22.289 1.00 38.58  ? 119 LEU C CG  1 
ATOM   883  C CD1 . LEU A 1 120 ? -16.495 40.227  -23.750 1.00 36.17  ? 119 LEU C CD1 1 
ATOM   884  C CD2 . LEU A 1 120 ? -15.312 41.180  -21.759 1.00 35.81  ? 119 LEU C CD2 1 
ATOM   885  N N   . SER A 1 121 ? -19.243 40.504  -19.096 1.00 28.62  ? 120 SER C N   1 
ATOM   886  C CA  . SER A 1 121 ? -20.470 40.471  -18.310 1.00 28.24  ? 120 SER C CA  1 
ATOM   887  C C   . SER A 1 121 ? -21.586 39.800  -19.102 1.00 33.38  ? 120 SER C C   1 
ATOM   888  O O   . SER A 1 121 ? -21.948 40.264  -20.190 1.00 29.84  ? 120 SER C O   1 
ATOM   889  C CB  . SER A 1 121 ? -20.877 41.887  -17.909 1.00 27.16  ? 120 SER C CB  1 
ATOM   890  O OG  . SER A 1 121 ? -22.203 41.914  -17.408 1.00 34.46  ? 120 SER C OG  1 
ATOM   891  N N   . ILE A 1 122 ? -22.129 38.709  -18.554 1.00 34.27  ? 121 ILE C N   1 
ATOM   892  C CA  . ILE A 1 122 ? -23.307 38.079  -19.146 1.00 35.38  ? 121 ILE C CA  1 
ATOM   893  C C   . ILE A 1 122 ? -24.446 39.086  -19.243 1.00 33.57  ? 121 ILE C C   1 
ATOM   894  O O   . ILE A 1 122 ? -25.188 39.118  -20.233 1.00 31.03  ? 121 ILE C O   1 
ATOM   895  C CB  . ILE A 1 122 ? -23.714 36.835  -18.329 1.00 29.51  ? 121 ILE C CB  1 
ATOM   896  C CG1 . ILE A 1 122 ? -22.808 35.647  -18.657 1.00 34.10  ? 121 ILE C CG1 1 
ATOM   897  C CG2 . ILE A 1 122 ? -25.170 36.466  -18.579 1.00 33.78  ? 121 ILE C CG2 1 
ATOM   898  C CD1 . ILE A 1 122 ? -22.846 35.230  -20.119 1.00 40.76  ? 121 ILE C CD1 1 
ATOM   899  N N   . THR A 1 123 ? -24.584 39.941  -18.226 1.00 31.66  ? 122 THR C N   1 
ATOM   900  C CA  . THR A 1 123 ? -25.664 40.922  -18.211 1.00 32.78  ? 122 THR C CA  1 
ATOM   901  C C   . THR A 1 123 ? -25.522 41.922  -19.350 1.00 33.08  ? 122 THR C C   1 
ATOM   902  O O   . THR A 1 123 ? -26.508 42.268  -20.012 1.00 28.79  ? 122 THR C O   1 
ATOM   903  C CB  . THR A 1 123 ? -25.681 41.653  -16.869 1.00 32.82  ? 122 THR C CB  1 
ATOM   904  O OG1 . THR A 1 123 ? -25.750 40.699  -15.803 1.00 39.49  ? 122 THR C OG1 1 
ATOM   905  C CG2 . THR A 1 123 ? -26.869 42.589  -16.786 1.00 28.70  ? 122 THR C CG2 1 
ATOM   906  N N   . GLU A 1 124 ? -24.298 42.391  -19.598 1.00 27.64  ? 123 GLU C N   1 
ATOM   907  C CA  . GLU A 1 124 ? -24.088 43.433  -20.597 1.00 27.27  ? 123 GLU C CA  1 
ATOM   908  C C   . GLU A 1 124 ? -24.165 42.884  -22.017 1.00 35.26  ? 123 GLU C C   1 
ATOM   909  O O   . GLU A 1 124 ? -24.608 43.593  -22.929 1.00 38.91  ? 123 GLU C O   1 
ATOM   910  C CB  . GLU A 1 124 ? -22.740 44.114  -20.357 1.00 25.78  ? 123 GLU C CB  1 
ATOM   911  C CG  . GLU A 1 124 ? -22.502 45.346  -21.208 1.00 28.21  ? 123 GLU C CG  1 
ATOM   912  C CD  . GLU A 1 124 ? -21.110 45.917  -21.021 1.00 37.73  ? 123 GLU C CD  1 
ATOM   913  O OE1 . GLU A 1 124 ? -20.390 45.454  -20.108 1.00 34.04  ? 123 GLU C OE1 1 
ATOM   914  O OE2 . GLU A 1 124 ? -20.730 46.819  -21.798 1.00 38.91  ? 123 GLU C OE2 1 
ATOM   915  N N   . ILE A 1 125 ? -23.747 41.633  -22.224 1.00 34.75  ? 124 ILE C N   1 
ATOM   916  C CA  . ILE A 1 125 ? -23.789 41.040  -23.561 1.00 32.49  ? 124 ILE C CA  1 
ATOM   917  C C   . ILE A 1 125 ? -25.228 40.935  -24.054 1.00 36.17  ? 124 ILE C C   1 
ATOM   918  O O   . ILE A 1 125 ? -25.538 41.280  -25.200 1.00 48.88  ? 124 ILE C O   1 
ATOM   919  C CB  . ILE A 1 125 ? -23.095 39.665  -23.562 1.00 37.46  ? 124 ILE C CB  1 
ATOM   920  C CG1 . ILE A 1 125 ? -21.581 39.821  -23.411 1.00 34.53  ? 124 ILE C CG1 1 
ATOM   921  C CG2 . ILE A 1 125 ? -23.424 38.899  -24.834 1.00 33.22  ? 124 ILE C CG2 1 
ATOM   922  C CD1 . ILE A 1 125 ? -20.865 38.524  -23.101 1.00 30.36  ? 124 ILE C CD1 1 
ATOM   923  N N   . GLY A 1 126 ? -26.128 40.459  -23.196 1.00 28.02  ? 125 GLY C N   1 
ATOM   924  C CA  . GLY A 1 126 ? -27.499 40.221  -23.604 1.00 35.87  ? 125 GLY C CA  1 
ATOM   925  C C   . GLY A 1 126 ? -28.473 41.324  -23.240 1.00 31.62  ? 125 GLY C C   1 
ATOM   926  O O   . GLY A 1 126 ? -29.656 41.056  -23.005 1.00 40.95  ? 125 GLY C O   1 
ATOM   927  N N   . LYS A 1 127 ? -27.994 42.569  -23.214 1.00 34.30  ? 126 LYS C N   1 
ATOM   928  C CA  . LYS A 1 127 ? -28.819 43.684  -22.754 1.00 38.20  ? 126 LYS C CA  1 
ATOM   929  C C   . LYS A 1 127 ? -30.047 43.880  -23.640 1.00 47.84  ? 126 LYS C C   1 
ATOM   930  O O   . LYS A 1 127 ? -31.189 43.770  -23.178 1.00 54.83  ? 126 LYS C O   1 
ATOM   931  C CB  . LYS A 1 127 ? -27.983 44.964  -22.704 1.00 40.47  ? 126 LYS C CB  1 
ATOM   932  C CG  . LYS A 1 127 ? -28.725 46.167  -22.140 1.00 36.82  ? 126 LYS C CG  1 
ATOM   933  C CD  . LYS A 1 127 ? -27.829 47.396  -22.101 1.00 39.54  ? 126 LYS C CD  1 
ATOM   934  C CE  . LYS A 1 127 ? -28.632 48.660  -21.839 1.00 38.99  ? 126 LYS C CE  1 
ATOM   935  N NZ  . LYS A 1 127 ? -30.083 48.370  -21.654 1.00 41.38  ? 126 LYS C NZ  1 
ATOM   936  N N   . GLY A 1 128 ? -29.833 44.177  -24.917 1.00 42.49  ? 127 GLY C N   1 
ATOM   937  C CA  . GLY A 1 128 ? -30.929 44.527  -25.797 1.00 58.35  ? 127 GLY C CA  1 
ATOM   938  C C   . GLY A 1 128 ? -31.646 43.375  -26.467 1.00 52.41  ? 127 GLY C C   1 
ATOM   939  O O   . GLY A 1 128 ? -32.421 43.607  -27.400 1.00 50.26  ? 127 GLY C O   1 
ATOM   940  N N   . LEU A 1 129 ? -31.426 42.143  -26.021 1.00 50.51  ? 128 LEU C N   1 
ATOM   941  C CA  . LEU A 1 129 ? -31.997 40.988  -26.693 1.00 38.05  ? 128 LEU C CA  1 
ATOM   942  C C   . LEU A 1 129 ? -33.477 40.824  -26.349 1.00 42.48  ? 128 LEU C C   1 
ATOM   943  O O   . LEU A 1 129 ? -33.990 41.397  -25.383 1.00 39.34  ? 128 LEU C O   1 
ATOM   944  C CB  . LEU A 1 129 ? -31.231 39.719  -26.319 1.00 37.68  ? 128 LEU C CB  1 
ATOM   945  C CG  . LEU A 1 129 ? -29.780 39.621  -26.802 1.00 42.84  ? 128 LEU C CG  1 
ATOM   946  C CD1 . LEU A 1 129 ? -29.258 38.202  -26.630 1.00 36.01  ? 128 LEU C CD1 1 
ATOM   947  C CD2 . LEU A 1 129 ? -29.647 40.072  -28.253 1.00 34.68  ? 128 LEU C CD2 1 
ATOM   948  N N   . SER A 1 130 ? -34.160 40.025  -27.167 1.00 43.08  ? 129 SER C N   1 
ATOM   949  C CA  . SER A 1 130 ? -35.568 39.699  -26.979 1.00 38.60  ? 129 SER C CA  1 
ATOM   950  C C   . SER A 1 130 ? -35.777 38.437  -26.156 1.00 42.48  ? 129 SER C C   1 
ATOM   951  O O   . SER A 1 130 ? -36.925 38.045  -25.926 1.00 33.04  ? 129 SER C O   1 
ATOM   952  C CB  . SER A 1 130 ? -36.256 39.526  -28.336 1.00 42.52  ? 129 SER C CB  1 
ATOM   953  O OG  . SER A 1 130 ? -36.285 38.156  -28.709 1.00 36.32  ? 129 SER C OG  1 
ATOM   954  N N   . ARG A 1 131 ? -34.703 37.788  -25.726 1.00 40.59  ? 130 ARG C N   1 
ATOM   955  C CA  . ARG A 1 131 ? -34.789 36.542  -24.983 1.00 36.96  ? 130 ARG C CA  1 
ATOM   956  C C   . ARG A 1 131 ? -33.644 36.511  -23.983 1.00 40.16  ? 130 ARG C C   1 
ATOM   957  O O   . ARG A 1 131 ? -32.692 37.292  -24.102 1.00 34.77  ? 130 ARG C O   1 
ATOM   958  C CB  . ARG A 1 131 ? -34.735 35.333  -25.924 1.00 34.47  ? 130 ARG C CB  1 
ATOM   959  C CG  . ARG A 1 131 ? -33.371 35.071  -26.516 1.00 36.05  ? 130 ARG C CG  1 
ATOM   960  C CD  . ARG A 1 131 ? -33.454 33.934  -27.505 1.00 35.01  ? 130 ARG C CD  1 
ATOM   961  N NE  . ARG A 1 131 ? -33.847 34.402  -28.828 1.00 34.35  ? 130 ARG C NE  1 
ATOM   962  C CZ  . ARG A 1 131 ? -34.250 33.608  -29.809 1.00 41.34  ? 130 ARG C CZ  1 
ATOM   963  N NH1 . ARG A 1 131 ? -34.349 32.298  -29.641 1.00 37.83  ? 130 ARG C NH1 1 
ATOM   964  N NH2 . ARG A 1 131 ? -34.561 34.140  -30.988 1.00 35.94  ? 130 ARG C NH2 1 
ATOM   965  N N   . PRO A 1 132 ? -33.718 35.645  -22.972 1.00 34.77  ? 131 PRO C N   1 
ATOM   966  C CA  . PRO A 1 132 ? -32.670 35.633  -21.946 1.00 34.23  ? 131 PRO C CA  1 
ATOM   967  C C   . PRO A 1 132 ? -31.317 35.216  -22.503 1.00 35.42  ? 131 PRO C C   1 
ATOM   968  O O   . PRO A 1 132 ? -31.215 34.458  -23.471 1.00 41.45  ? 131 PRO C O   1 
ATOM   969  C CB  . PRO A 1 132 ? -33.185 34.614  -20.926 1.00 32.07  ? 131 PRO C CB  1 
ATOM   970  C CG  . PRO A 1 132 ? -34.657 34.604  -21.122 1.00 39.70  ? 131 PRO C CG  1 
ATOM   971  C CD  . PRO A 1 132 ? -34.860 34.796  -22.591 1.00 36.66  ? 131 PRO C CD  1 
ATOM   972  N N   . LEU A 1 133 ? -30.270 35.735  -21.875 1.00 29.03  ? 132 LEU C N   1 
ATOM   973  C CA  . LEU A 1 133 ? -28.899 35.335  -22.143 1.00 29.65  ? 132 LEU C CA  1 
ATOM   974  C C   . LEU A 1 133 ? -28.314 34.810  -20.841 1.00 32.29  ? 132 LEU C C   1 
ATOM   975  O O   . LEU A 1 133 ? -28.423 35.463  -19.799 1.00 29.69  ? 132 LEU C O   1 
ATOM   976  C CB  . LEU A 1 133 ? -28.082 36.508  -22.705 1.00 28.57  ? 132 LEU C CB  1 
ATOM   977  C CG  . LEU A 1 133 ? -26.683 36.271  -23.289 1.00 36.16  ? 132 LEU C CG  1 
ATOM   978  C CD1 . LEU A 1 133 ? -25.615 36.334  -22.209 1.00 40.63  ? 132 LEU C CD1 1 
ATOM   979  C CD2 . LEU A 1 133 ? -26.610 34.945  -24.030 1.00 36.33  ? 132 LEU C CD2 1 
ATOM   980  N N   . VAL A 1 134 ? -27.721 33.620  -20.899 1.00 37.18  ? 133 VAL C N   1 
ATOM   981  C CA  . VAL A 1 134 ? -27.227 32.919  -19.723 1.00 29.47  ? 133 VAL C CA  1 
ATOM   982  C C   . VAL A 1 134 ? -25.792 32.490  -19.997 1.00 28.75  ? 133 VAL C C   1 
ATOM   983  O O   . VAL A 1 134 ? -25.361 32.367  -21.143 1.00 32.20  ? 133 VAL C O   1 
ATOM   984  C CB  . VAL A 1 134 ? -28.119 31.701  -19.370 1.00 23.92  ? 133 VAL C CB  1 
ATOM   985  C CG1 . VAL A 1 134 ? -28.056 30.647  -20.472 1.00 21.37  ? 133 VAL C CG1 1 
ATOM   986  C CG2 . VAL A 1 134 ? -27.738 31.099  -18.026 1.00 26.44  ? 133 VAL C CG2 1 
ATOM   987  N N   . GLY A 1 135 ? -25.030 32.296  -18.918 1.00 28.88  ? 134 GLY C N   1 
ATOM   988  C CA  . GLY A 1 135 ? -23.661 31.827  -19.022 1.00 23.71  ? 134 GLY C CA  1 
ATOM   989  C C   . GLY A 1 135 ? -23.586 30.333  -18.829 1.00 26.74  ? 134 GLY C C   1 
ATOM   990  O O   . GLY A 1 135 ? -24.135 29.783  -17.868 1.00 29.79  ? 134 GLY C O   1 
ATOM   991  N N   . MET A 1 136 ? -22.903 29.662  -19.761 1.00 31.23  ? 135 MET C N   1 
ATOM   992  C CA  . MET A 1 136 ? -22.654 28.222  -19.707 1.00 24.42  ? 135 MET C CA  1 
ATOM   993  C C   . MET A 1 136 ? -21.149 28.069  -19.883 1.00 29.39  ? 135 MET C C   1 
ATOM   994  O O   . MET A 1 136 ? -20.655 28.018  -21.011 1.00 22.78  ? 135 MET C O   1 
ATOM   995  C CB  . MET A 1 136 ? -23.426 27.474  -20.780 1.00 23.78  ? 135 MET C CB  1 
ATOM   996  C CG  . MET A 1 136 ? -23.538 25.978  -20.532 1.00 26.72  ? 135 MET C CG  1 
ATOM   997  S SD  . MET A 1 136 ? -24.519 25.169  -21.806 1.00 39.82  ? 135 MET C SD  1 
ATOM   998  C CE  . MET A 1 136 ? -24.116 23.448  -21.527 1.00 33.28  ? 135 MET C CE  1 
ATOM   999  N N   . HIS A 1 137 ? -20.424 28.004  -18.774 1.00 23.15  ? 136 HIS C N   1 
ATOM   1000 C CA  . HIS A 1 137 ? -18.972 28.101  -18.792 1.00 22.53  ? 136 HIS C CA  1 
ATOM   1001 C C   . HIS A 1 137 ? -18.357 26.711  -18.674 1.00 24.06  ? 136 HIS C C   1 
ATOM   1002 O O   . HIS A 1 137 ? -18.557 26.023  -17.668 1.00 30.82  ? 136 HIS C O   1 
ATOM   1003 C CB  . HIS A 1 137 ? -18.489 29.014  -17.667 1.00 32.36  ? 136 HIS C CB  1 
ATOM   1004 C CG  . HIS A 1 137 ? -17.035 29.348  -17.748 1.00 34.27  ? 136 HIS C CG  1 
ATOM   1005 N ND1 . HIS A 1 137 ? -16.202 29.309  -16.651 1.00 32.32  ? 136 HIS C ND1 1 
ATOM   1006 C CD2 . HIS A 1 137 ? -16.260 29.706  -18.799 1.00 32.42  ? 136 HIS C CD2 1 
ATOM   1007 C CE1 . HIS A 1 137 ? -14.977 29.640  -17.021 1.00 35.76  ? 136 HIS C CE1 1 
ATOM   1008 N NE2 . HIS A 1 137 ? -14.986 29.885  -18.319 1.00 37.07  ? 136 HIS C NE2 1 
ATOM   1009 N N   . PHE A 1 138 ? -17.621 26.306  -19.703 1.00 27.79  ? 137 PHE C N   1 
ATOM   1010 C CA  . PHE A 1 138 ? -16.907 25.039  -19.742 1.00 25.86  ? 137 PHE C CA  1 
ATOM   1011 C C   . PHE A 1 138 ? -15.453 25.249  -19.333 1.00 28.24  ? 137 PHE C C   1 
ATOM   1012 O O   . PHE A 1 138 ? -14.977 26.378  -19.186 1.00 23.67  ? 137 PHE C O   1 
ATOM   1013 C CB  . PHE A 1 138 ? -16.958 24.420  -21.142 1.00 25.39  ? 137 PHE C CB  1 
ATOM   1014 C CG  . PHE A 1 138 ? -18.321 23.950  -21.566 1.00 24.73  ? 137 PHE C CG  1 
ATOM   1015 C CD1 . PHE A 1 138 ? -19.301 24.857  -21.946 1.00 22.74  ? 137 PHE C CD1 1 
ATOM   1016 C CD2 . PHE A 1 138 ? -18.610 22.593  -21.622 1.00 29.25  ? 137 PHE C CD2 1 
ATOM   1017 C CE1 . PHE A 1 138 ? -20.550 24.415  -22.358 1.00 26.56  ? 137 PHE C CE1 1 
ATOM   1018 C CE2 . PHE A 1 138 ? -19.854 22.147  -22.028 1.00 22.93  ? 137 PHE C CE2 1 
ATOM   1019 C CZ  . PHE A 1 138 ? -20.821 23.057  -22.400 1.00 27.06  ? 137 PHE C CZ  1 
ATOM   1020 N N   . PHE A 1 139 ? -14.732 24.137  -19.181 1.00 28.54  ? 138 PHE C N   1 
ATOM   1021 C CA  . PHE A 1 139 ? -13.350 24.171  -18.717 1.00 36.00  ? 138 PHE C CA  1 
ATOM   1022 C C   . PHE A 1 139 ? -12.477 23.296  -19.603 1.00 37.13  ? 138 PHE C C   1 
ATOM   1023 O O   . PHE A 1 139 ? -12.840 22.156  -19.908 1.00 35.28  ? 138 PHE C O   1 
ATOM   1024 C CB  . PHE A 1 139 ? -13.264 23.729  -17.253 1.00 29.65  ? 138 PHE C CB  1 
ATOM   1025 C CG  . PHE A 1 139 ? -13.855 24.722  -16.304 1.00 28.55  ? 138 PHE C CG  1 
ATOM   1026 C CD1 . PHE A 1 139 ? -15.225 24.772  -16.100 1.00 23.66  ? 138 PHE C CD1 1 
ATOM   1027 C CD2 . PHE A 1 139 ? -13.047 25.628  -15.640 1.00 25.77  ? 138 PHE C CD2 1 
ATOM   1028 C CE1 . PHE A 1 139 ? -15.777 25.703  -15.243 1.00 35.26  ? 138 PHE C CE1 1 
ATOM   1029 C CE2 . PHE A 1 139 ? -13.592 26.559  -14.776 1.00 29.93  ? 138 PHE C CE2 1 
ATOM   1030 C CZ  . PHE A 1 139 ? -14.957 26.598  -14.577 1.00 29.70  ? 138 PHE C CZ  1 
ATOM   1031 N N   . ASN A 1 140 ? -11.328 23.834  -20.000 1.00 34.95  ? 139 ASN C N   1 
ATOM   1032 C CA  . ASN A 1 140 ? -10.443 23.160  -20.947 1.00 35.61  ? 139 ASN C CA  1 
ATOM   1033 C C   . ASN A 1 140 ? -9.830  21.914  -20.314 1.00 36.39  ? 139 ASN C C   1 
ATOM   1034 O O   . ASN A 1 140 ? -9.235  22.005  -19.234 1.00 44.07  ? 139 ASN C O   1 
ATOM   1035 C CB  . ASN A 1 140 ? -9.343  24.127  -21.387 1.00 37.35  ? 139 ASN C CB  1 
ATOM   1036 C CG  . ASN A 1 140 ? -8.882  23.888  -22.809 1.00 55.58  ? 139 ASN C CG  1 
ATOM   1037 O OD1 . ASN A 1 140 ? -8.957  22.773  -23.322 1.00 60.80  ? 139 ASN C OD1 1 
ATOM   1038 N ND2 . ASN A 1 140 ? -8.398  24.944  -23.456 1.00 58.98  ? 139 ASN C ND2 1 
ATOM   1039 N N   . PRO A 1 141 ? -9.950  20.731  -20.945 1.00 40.83  ? 140 PRO C N   1 
ATOM   1040 C CA  . PRO A 1 141 ? -10.688 20.426  -22.186 1.00 36.93  ? 140 PRO C CA  1 
ATOM   1041 C C   . PRO A 1 141 ? -12.171 20.184  -21.923 1.00 30.94  ? 140 PRO C C   1 
ATOM   1042 O O   . PRO A 1 141 ? -12.529 19.416  -21.034 1.00 32.01  ? 140 PRO C O   1 
ATOM   1043 C CB  . PRO A 1 141 ? -9.974  19.173  -22.705 1.00 29.49  ? 140 PRO C CB  1 
ATOM   1044 C CG  . PRO A 1 141 ? -9.493  18.473  -21.466 1.00 31.08  ? 140 PRO C CG  1 
ATOM   1045 C CD  . PRO A 1 141 ? -9.220  19.554  -20.438 1.00 36.41  ? 140 PRO C CD  1 
ATOM   1046 N N   . ALA A 1 142 ? -13.050 20.840  -22.690 1.00 35.00  ? 141 ALA C N   1 
ATOM   1047 C CA  . ALA A 1 142 ? -14.476 20.846  -22.370 1.00 32.55  ? 141 ALA C CA  1 
ATOM   1048 C C   . ALA A 1 142 ? -15.106 19.461  -22.477 1.00 35.63  ? 141 ALA C C   1 
ATOM   1049 O O   . ALA A 1 142 ? -16.081 19.173  -21.772 1.00 30.98  ? 141 ALA C O   1 
ATOM   1050 C CB  . ALA A 1 142 ? -15.212 21.827  -23.282 1.00 26.98  ? 141 ALA C CB  1 
ATOM   1051 N N   . ASP A 1 143 ? -14.579 18.596  -23.346 1.00 37.77  ? 142 ASP C N   1 
ATOM   1052 C CA  . ASP A 1 143 ? -15.156 17.270  -23.519 1.00 38.84  ? 142 ASP C CA  1 
ATOM   1053 C C   . ASP A 1 143 ? -14.795 16.308  -22.394 1.00 43.41  ? 142 ASP C C   1 
ATOM   1054 O O   . ASP A 1 143 ? -15.330 15.194  -22.366 1.00 41.69  ? 142 ASP C O   1 
ATOM   1055 C CB  . ASP A 1 143 ? -14.724 16.678  -24.863 1.00 35.98  ? 142 ASP C CB  1 
ATOM   1056 C CG  . ASP A 1 143 ? -13.218 16.577  -25.000 1.00 46.03  ? 142 ASP C CG  1 
ATOM   1057 O OD1 . ASP A 1 143 ? -12.562 17.630  -25.141 1.00 56.80  ? 142 ASP C OD1 1 
ATOM   1058 O OD2 . ASP A 1 143 ? -12.692 15.445  -24.974 1.00 56.21  ? 142 ASP C OD2 1 
ATOM   1059 N N   . ARG A 1 144 ? -13.924 16.709  -21.469 1.00 39.46  ? 143 ARG C N   1 
ATOM   1060 C CA  . ARG A 1 144 ? -13.487 15.842  -20.379 1.00 35.06  ? 143 ARG C CA  1 
ATOM   1061 C C   . ARG A 1 144 ? -13.717 16.432  -18.997 1.00 37.27  ? 143 ARG C C   1 
ATOM   1062 O O   . ARG A 1 144 ? -14.071 15.695  -18.074 1.00 47.39  ? 143 ARG C O   1 
ATOM   1063 C CB  . ARG A 1 144 ? -12.003 15.494  -20.553 1.00 39.11  ? 143 ARG C CB  1 
ATOM   1064 C CG  . ARG A 1 144 ? -11.724 14.729  -21.839 1.00 52.33  ? 143 ARG C CG  1 
ATOM   1065 C CD  . ARG A 1 144 ? -10.539 13.792  -21.699 1.00 57.80  ? 143 ARG C CD  1 
ATOM   1066 N NE  . ARG A 1 144 ? -9.302  14.515  -21.435 1.00 63.95  ? 143 ARG C NE  1 
ATOM   1067 C CZ  . ARG A 1 144 ? -8.104  14.119  -21.842 1.00 71.21  ? 143 ARG C CZ  1 
ATOM   1068 N NH1 . ARG A 1 144 ? -7.945  13.009  -22.547 1.00 71.38  ? 143 ARG C NH1 1 
ATOM   1069 N NH2 . ARG A 1 144 ? -7.038  14.855  -21.538 1.00 67.98  ? 143 ARG C NH2 1 
ATOM   1070 N N   . MET A 1 145 ? -13.529 17.738  -18.818 1.00 34.31  ? 144 MET C N   1 
ATOM   1071 C CA  . MET A 1 145 ? -13.842 18.363  -17.539 1.00 38.48  ? 144 MET C CA  1 
ATOM   1072 C C   . MET A 1 145 ? -15.350 18.355  -17.316 1.00 36.00  ? 144 MET C C   1 
ATOM   1073 O O   . MET A 1 145 ? -16.121 18.748  -18.197 1.00 36.37  ? 144 MET C O   1 
ATOM   1074 C CB  . MET A 1 145 ? -13.298 19.789  -17.493 1.00 36.36  ? 144 MET C CB  1 
ATOM   1075 C CG  . MET A 1 145 ? -11.811 19.888  -17.787 1.00 30.46  ? 144 MET C CG  1 
ATOM   1076 S SD  . MET A 1 145 ? -10.791 19.315  -16.415 1.00 47.64  ? 144 MET C SD  1 
ATOM   1077 C CE  . MET A 1 145 ? -11.299 20.434  -15.118 1.00 32.80  ? 144 MET C CE  1 
ATOM   1078 N N   . LYS A 1 146 ? -15.771 17.897  -16.137 1.00 38.49  ? 145 LYS C N   1 
ATOM   1079 C CA  . LYS A 1 146 ? -17.183 17.672  -15.857 1.00 37.28  ? 145 LYS C CA  1 
ATOM   1080 C C   . LYS A 1 146 ? -17.890 18.883  -15.266 1.00 33.61  ? 145 LYS C C   1 
ATOM   1081 O O   . LYS A 1 146 ? -19.113 18.841  -15.094 1.00 26.94  ? 145 LYS C O   1 
ATOM   1082 C CB  . LYS A 1 146 ? -17.350 16.482  -14.907 1.00 34.56  ? 145 LYS C CB  1 
ATOM   1083 C CG  . LYS A 1 146 ? -16.382 15.343  -15.170 1.00 43.12  ? 145 LYS C CG  1 
ATOM   1084 C CD  . LYS A 1 146 ? -16.655 14.166  -14.253 1.00 38.84  ? 145 LYS C CD  1 
ATOM   1085 C CE  . LYS A 1 146 ? -17.822 13.342  -14.765 1.00 55.54  ? 145 LYS C CE  1 
ATOM   1086 N NZ  . LYS A 1 146 ? -17.455 11.921  -15.026 1.00 43.11  ? 145 LYS C NZ  1 
ATOM   1087 N N   . LEU A 1 147 ? -17.167 19.951  -14.950 1.00 31.17  ? 146 LEU C N   1 
ATOM   1088 C CA  . LEU A 1 147 ? -17.778 21.128  -14.355 1.00 32.52  ? 146 LEU C CA  1 
ATOM   1089 C C   . LEU A 1 147 ? -18.338 22.056  -15.427 1.00 29.21  ? 146 LEU C C   1 
ATOM   1090 O O   . LEU A 1 147 ? -17.720 22.268  -16.476 1.00 30.22  ? 146 LEU C O   1 
ATOM   1091 C CB  . LEU A 1 147 ? -16.768 21.888  -13.495 1.00 29.36  ? 146 LEU C CB  1 
ATOM   1092 C CG  . LEU A 1 147 ? -17.304 23.220  -12.965 1.00 36.01  ? 146 LEU C CG  1 
ATOM   1093 C CD1 . LEU A 1 147 ? -18.496 22.991  -12.045 1.00 25.33  ? 146 LEU C CD1 1 
ATOM   1094 C CD2 . LEU A 1 147 ? -16.221 24.001  -12.260 1.00 31.64  ? 146 LEU C CD2 1 
ATOM   1095 N N   . ILE A 1 148 ? -19.520 22.600  -15.153 1.00 26.93  ? 147 ILE C N   1 
ATOM   1096 C CA  . ILE A 1 148 ? -20.099 23.687  -15.928 1.00 26.67  ? 147 ILE C CA  1 
ATOM   1097 C C   . ILE A 1 148 ? -20.600 24.728  -14.941 1.00 25.64  ? 147 ILE C C   1 
ATOM   1098 O O   . ILE A 1 148 ? -21.418 24.413  -14.069 1.00 30.36  ? 147 ILE C O   1 
ATOM   1099 C CB  . ILE A 1 148 ? -21.245 23.213  -16.835 1.00 31.96  ? 147 ILE C CB  1 
ATOM   1100 C CG1 . ILE A 1 148 ? -20.687 22.538  -18.087 1.00 24.84  ? 147 ILE C CG1 1 
ATOM   1101 C CG2 . ILE A 1 148 ? -22.139 24.387  -17.215 1.00 30.16  ? 147 ILE C CG2 1 
ATOM   1102 C CD1 . ILE A 1 148 ? -21.753 21.952  -18.973 1.00 35.09  ? 147 ILE C CD1 1 
ATOM   1103 N N   . GLU A 1 149 ? -20.107 25.956  -15.066 1.00 23.46  ? 148 GLU C N   1 
ATOM   1104 C CA  . GLU A 1 149 ? -20.614 27.068  -14.274 1.00 26.54  ? 148 GLU C CA  1 
ATOM   1105 C C   . GLU A 1 149 ? -21.761 27.717  -15.038 1.00 21.51  ? 148 GLU C C   1 
ATOM   1106 O O   . GLU A 1 149 ? -21.569 28.198  -16.159 1.00 28.67  ? 148 GLU C O   1 
ATOM   1107 C CB  . GLU A 1 149 ? -19.509 28.084  -13.978 1.00 27.05  ? 148 GLU C CB  1 
ATOM   1108 C CG  . GLU A 1 149 ? -18.449 27.590  -13.003 1.00 29.93  ? 148 GLU C CG  1 
ATOM   1109 C CD  . GLU A 1 149 ? -17.382 28.636  -12.711 1.00 28.26  ? 148 GLU C CD  1 
ATOM   1110 O OE1 . GLU A 1 149 ? -16.642 29.008  -13.646 1.00 35.86  ? 148 GLU C OE1 1 
ATOM   1111 O OE2 . GLU A 1 149 ? -17.270 29.076  -11.546 1.00 40.10  ? 148 GLU C OE2 1 
ATOM   1112 N N   . VAL A 1 150 ? -22.950 27.710  -14.442 1.00 25.82  ? 149 VAL C N   1 
ATOM   1113 C CA  . VAL A 1 150 ? -24.128 28.338  -15.028 1.00 21.46  ? 149 VAL C CA  1 
ATOM   1114 C C   . VAL A 1 150 ? -24.263 29.734  -14.438 1.00 28.44  ? 149 VAL C C   1 
ATOM   1115 O O   . VAL A 1 150 ? -24.432 29.889  -13.223 1.00 29.53  ? 149 VAL C O   1 
ATOM   1116 C CB  . VAL A 1 150 ? -25.389 27.503  -14.767 1.00 21.35  ? 149 VAL C CB  1 
ATOM   1117 C CG1 . VAL A 1 150 ? -26.578 28.111  -15.478 1.00 17.51  ? 149 VAL C CG1 1 
ATOM   1118 C CG2 . VAL A 1 150 ? -25.172 26.059  -15.207 1.00 24.02  ? 149 VAL C CG2 1 
ATOM   1119 N N   . ILE A 1 151 ? -24.199 30.752  -15.291 1.00 24.11  ? 150 ILE C N   1 
ATOM   1120 C CA  . ILE A 1 151 ? -24.088 32.139  -14.850 1.00 20.84  ? 150 ILE C CA  1 
ATOM   1121 C C   . ILE A 1 151 ? -25.424 32.832  -15.058 1.00 25.63  ? 150 ILE C C   1 
ATOM   1122 O O   . ILE A 1 151 ? -25.897 32.963  -16.193 1.00 26.99  ? 150 ILE C O   1 
ATOM   1123 C CB  . ILE A 1 151 ? -22.964 32.879  -15.588 1.00 24.59  ? 150 ILE C CB  1 
ATOM   1124 C CG1 . ILE A 1 151 ? -21.791 31.931  -15.855 1.00 27.11  ? 150 ILE C CG1 1 
ATOM   1125 C CG2 . ILE A 1 151 ? -22.516 34.090  -14.785 1.00 27.24  ? 150 ILE C CG2 1 
ATOM   1126 C CD1 . ILE A 1 151 ? -20.993 31.590  -14.616 1.00 22.66  ? 150 ILE C CD1 1 
ATOM   1127 N N   . ALA A 1 152 ? -26.025 33.285  -13.963 1.00 25.77  ? 151 ALA C N   1 
ATOM   1128 C CA  . ALA A 1 152 ? -27.261 34.049  -14.014 1.00 19.93  ? 151 ALA C CA  1 
ATOM   1129 C C   . ALA A 1 152 ? -26.922 35.533  -14.041 1.00 31.67  ? 151 ALA C C   1 
ATOM   1130 O O   . ALA A 1 152 ? -26.242 36.038  -13.140 1.00 34.82  ? 151 ALA C O   1 
ATOM   1131 C CB  . ALA A 1 152 ? -28.155 33.723  -12.819 1.00 27.30  ? 151 ALA C CB  1 
ATOM   1132 N N   . GLY A 1 153 ? -27.381 36.222  -15.079 1.00 30.25  ? 152 GLY C N   1 
ATOM   1133 C CA  . GLY A 1 153 ? -27.210 37.653  -15.179 1.00 26.99  ? 152 GLY C CA  1 
ATOM   1134 C C   . GLY A 1 153 ? -28.214 38.394  -14.317 1.00 32.53  ? 152 GLY C C   1 
ATOM   1135 O O   . GLY A 1 153 ? -29.004 37.811  -13.572 1.00 37.27  ? 152 GLY C O   1 
ATOM   1136 N N   . CYS A 1 154 ? -28.175 39.722  -14.432 1.00 33.14  ? 153 CYS C N   1 
ATOM   1137 C CA  . CYS A 1 154 ? -29.078 40.552  -13.644 1.00 38.74  ? 153 CYS C CA  1 
ATOM   1138 C C   . CYS A 1 154 ? -30.539 40.293  -13.998 1.00 40.65  ? 153 CYS C C   1 
ATOM   1139 O O   . CYS A 1 154 ? -31.417 40.422  -13.137 1.00 36.25  ? 153 CYS C O   1 
ATOM   1140 C CB  . CYS A 1 154 ? -28.733 42.027  -13.843 1.00 40.30  ? 153 CYS C CB  1 
ATOM   1141 S SG  . CYS A 1 154 ? -29.687 43.162  -12.821 1.00 62.55  ? 153 CYS C SG  1 
ATOM   1142 N N   . ASN A 1 155 ? -30.821 39.916  -15.246 1.00 36.12  ? 154 ASN C N   1 
ATOM   1143 C CA  . ASN A 1 155 ? -32.192 39.724  -15.702 1.00 34.38  ? 154 ASN C CA  1 
ATOM   1144 C C   . ASN A 1 155 ? -32.458 38.317  -16.225 1.00 36.72  ? 154 ASN C C   1 
ATOM   1145 O O   . ASN A 1 155 ? -33.486 38.094  -16.874 1.00 38.95  ? 154 ASN C O   1 
ATOM   1146 C CB  . ASN A 1 155 ? -32.534 40.762  -16.775 1.00 32.04  ? 154 ASN C CB  1 
ATOM   1147 C CG  . ASN A 1 155 ? -32.250 42.183  -16.315 1.00 41.38  ? 154 ASN C CG  1 
ATOM   1148 O OD1 . ASN A 1 155 ? -32.471 42.526  -15.152 1.00 45.28  ? 154 ASN C OD1 1 
ATOM   1149 N ND2 . ASN A 1 155 ? -31.758 43.017  -17.225 1.00 38.58  ? 154 ASN C ND2 1 
ATOM   1150 N N   . THR A 1 156 ? -31.574 37.362  -15.953 1.00 33.22  ? 155 THR C N   1 
ATOM   1151 C CA  . THR A 1 156 ? -31.778 35.996  -16.418 1.00 31.16  ? 155 THR C CA  1 
ATOM   1152 C C   . THR A 1 156 ? -32.848 35.314  -15.570 1.00 41.61  ? 155 THR C C   1 
ATOM   1153 O O   . THR A 1 156 ? -32.676 35.201  -14.351 1.00 34.40  ? 155 THR C O   1 
ATOM   1154 C CB  . THR A 1 156 ? -30.473 35.207  -16.360 1.00 31.20  ? 155 THR C CB  1 
ATOM   1155 O OG1 . THR A 1 156 ? -29.433 35.946  -17.012 1.00 33.19  ? 155 THR C OG1 1 
ATOM   1156 C CG2 . THR A 1 156 ? -30.627 33.861  -17.057 1.00 29.36  ? 155 THR C CG2 1 
ATOM   1157 N N   . PRO A 1 157 ? -33.953 34.857  -16.159 1.00 39.77  ? 156 PRO C N   1 
ATOM   1158 C CA  . PRO A 1 157 ? -34.985 34.181  -15.365 1.00 35.24  ? 156 PRO C CA  1 
ATOM   1159 C C   . PRO A 1 157 ? -34.511 32.824  -14.872 1.00 41.03  ? 156 PRO C C   1 
ATOM   1160 O O   . PRO A 1 157 ? -33.668 32.168  -15.490 1.00 39.65  ? 156 PRO C O   1 
ATOM   1161 C CB  . PRO A 1 157 ? -36.159 34.034  -16.344 1.00 33.26  ? 156 PRO C CB  1 
ATOM   1162 C CG  . PRO A 1 157 ? -35.808 34.876  -17.540 1.00 28.32  ? 156 PRO C CG  1 
ATOM   1163 C CD  . PRO A 1 157 ? -34.322 34.954  -17.579 1.00 37.95  ? 156 PRO C CD  1 
ATOM   1164 N N   . ALA A 1 158 ? -35.082 32.398  -13.742 1.00 40.71  ? 157 ALA C N   1 
ATOM   1165 C CA  . ALA A 1 158 ? -34.634 31.163  -13.105 1.00 42.86  ? 157 ALA C CA  1 
ATOM   1166 C C   . ALA A 1 158 ? -34.891 29.945  -13.981 1.00 40.08  ? 157 ALA C C   1 
ATOM   1167 O O   . ALA A 1 158 ? -34.183 28.938  -13.867 1.00 38.57  ? 157 ALA C O   1 
ATOM   1168 C CB  . ALA A 1 158 ? -35.313 30.994  -11.746 1.00 31.79  ? 157 ALA C CB  1 
ATOM   1169 N N   . GLU A 1 159 ? -35.886 30.006  -14.860 1.00 42.92  ? 158 GLU C N   1 
ATOM   1170 C CA  . GLU A 1 159 ? -36.137 28.863  -15.727 1.00 42.63  ? 158 GLU C CA  1 
ATOM   1171 C C   . GLU A 1 159 ? -35.013 28.686  -16.744 1.00 43.10  ? 158 GLU C C   1 
ATOM   1172 O O   . GLU A 1 159 ? -34.605 27.554  -17.038 1.00 43.41  ? 158 GLU C O   1 
ATOM   1173 C CB  . GLU A 1 159 ? -37.486 29.032  -16.422 1.00 42.71  ? 158 GLU C CB  1 
ATOM   1174 C CG  . GLU A 1 159 ? -38.733 29.051  -15.508 1.00 64.75  ? 158 GLU C CG  1 
ATOM   1175 C CD  . GLU A 1 159 ? -38.783 27.930  -14.469 1.00 74.86  ? 158 GLU C CD  1 
ATOM   1176 O OE1 . GLU A 1 159 ? -37.927 27.878  -13.561 1.00 72.65  ? 158 GLU C OE1 1 
ATOM   1177 O OE2 . GLU A 1 159 ? -39.691 27.079  -14.573 1.00 77.70  ? 158 GLU C OE2 1 
ATOM   1178 N N   . THR A 1 160 ? -34.504 29.793  -17.293 1.00 42.18  ? 159 THR C N   1 
ATOM   1179 C CA  . THR A 1 160 ? -33.360 29.713  -18.196 1.00 39.51  ? 159 THR C CA  1 
ATOM   1180 C C   . THR A 1 160 ? -32.191 29.001  -17.528 1.00 40.50  ? 159 THR C C   1 
ATOM   1181 O O   . THR A 1 160 ? -31.535 28.153  -18.145 1.00 38.22  ? 159 THR C O   1 
ATOM   1182 C CB  . THR A 1 160 ? -32.941 31.114  -18.650 1.00 36.05  ? 159 THR C CB  1 
ATOM   1183 O OG1 . THR A 1 160 ? -34.066 31.800  -19.214 1.00 37.03  ? 159 THR C OG1 1 
ATOM   1184 C CG2 . THR A 1 160 ? -31.828 31.032  -19.696 1.00 28.73  ? 159 THR C CG2 1 
ATOM   1185 N N   . VAL A 1 161 ? -31.927 29.323  -16.261 1.00 37.80  ? 160 VAL C N   1 
ATOM   1186 C CA  . VAL A 1 161 ? -30.833 28.683  -15.537 1.00 34.67  ? 160 VAL C CA  1 
ATOM   1187 C C   . VAL A 1 161 ? -31.126 27.203  -15.327 1.00 39.96  ? 160 VAL C C   1 
ATOM   1188 O O   . VAL A 1 161 ? -30.239 26.352  -15.473 1.00 30.20  ? 160 VAL C O   1 
ATOM   1189 C CB  . VAL A 1 161 ? -30.590 29.420  -14.205 1.00 31.18  ? 160 VAL C CB  1 
ATOM   1190 C CG1 . VAL A 1 161 ? -29.660 28.628  -13.295 1.00 25.62  ? 160 VAL C CG1 1 
ATOM   1191 C CG2 . VAL A 1 161 ? -30.028 30.805  -14.472 1.00 25.15  ? 160 VAL C CG2 1 
ATOM   1192 N N   . GLU A 1 162 ? -32.377 26.869  -15.002 1.00 39.41  ? 161 GLU C N   1 
ATOM   1193 C CA  . GLU A 1 162 ? -32.727 25.472  -14.770 1.00 41.79  ? 161 GLU C CA  1 
ATOM   1194 C C   . GLU A 1 162 ? -32.586 24.647  -16.045 1.00 34.14  ? 161 GLU C C   1 
ATOM   1195 O O   . GLU A 1 162 ? -32.081 23.520  -16.005 1.00 30.15  ? 161 GLU C O   1 
ATOM   1196 C CB  . GLU A 1 162 ? -34.146 25.369  -14.208 1.00 41.68  ? 161 GLU C CB  1 
ATOM   1197 C CG  . GLU A 1 162 ? -34.736 23.965  -14.253 1.00 51.61  ? 161 GLU C CG  1 
ATOM   1198 C CD  . GLU A 1 162 ? -34.044 22.996  -13.307 1.00 64.58  ? 161 GLU C CD  1 
ATOM   1199 O OE1 . GLU A 1 162 ? -34.205 21.771  -13.496 1.00 67.75  ? 161 GLU C OE1 1 
ATOM   1200 O OE2 . GLU A 1 162 ? -33.353 23.453  -12.368 1.00 75.36  ? 161 GLU C OE2 1 
ATOM   1201 N N   . LYS A 1 163 ? -33.015 25.194  -17.187 1.00 37.01  ? 162 LYS C N   1 
ATOM   1202 C CA  . LYS A 1 163 ? -32.843 24.486  -18.455 1.00 35.57  ? 162 LYS C CA  1 
ATOM   1203 C C   . LYS A 1 163 ? -31.373 24.174  -18.716 1.00 32.45  ? 162 LYS C C   1 
ATOM   1204 O O   . LYS A 1 163 ? -31.027 23.047  -19.095 1.00 31.48  ? 162 LYS C O   1 
ATOM   1205 C CB  . LYS A 1 163 ? -33.430 25.306  -19.604 1.00 33.46  ? 162 LYS C CB  1 
ATOM   1206 C CG  . LYS A 1 163 ? -34.943 25.179  -19.766 1.00 39.88  ? 162 LYS C CG  1 
ATOM   1207 C CD  . LYS A 1 163 ? -35.615 26.546  -19.771 1.00 47.97  ? 162 LYS C CD  1 
ATOM   1208 C CE  . LYS A 1 163 ? -36.155 26.920  -21.143 1.00 57.32  ? 162 LYS C CE  1 
ATOM   1209 N NZ  . LYS A 1 163 ? -37.284 27.893  -21.030 1.00 58.86  ? 162 LYS C NZ  1 
ATOM   1210 N N   . ILE A 1 164 ? -30.492 25.155  -18.503 1.00 29.27  ? 163 ILE C N   1 
ATOM   1211 C CA  . ILE A 1 164 ? -29.059 24.922  -18.667 1.00 30.12  ? 163 ILE C CA  1 
ATOM   1212 C C   . ILE A 1 164 ? -28.569 23.873  -17.678 1.00 26.91  ? 163 ILE C C   1 
ATOM   1213 O O   . ILE A 1 164 ? -27.668 23.084  -17.990 1.00 31.72  ? 163 ILE C O   1 
ATOM   1214 C CB  . ILE A 1 164 ? -28.290 26.250  -18.520 1.00 27.98  ? 163 ILE C CB  1 
ATOM   1215 C CG1 . ILE A 1 164 ? -28.670 27.209  -19.653 1.00 27.16  ? 163 ILE C CG1 1 
ATOM   1216 C CG2 . ILE A 1 164 ? -26.793 26.010  -18.517 1.00 31.80  ? 163 ILE C CG2 1 
ATOM   1217 C CD1 . ILE A 1 164 ? -28.287 26.711  -21.034 1.00 28.84  ? 163 ILE C CD1 1 
ATOM   1218 N N   . LYS A 1 165 ? -29.165 23.829  -16.484 1.00 36.44  ? 164 LYS C N   1 
ATOM   1219 C CA  . LYS A 1 165 ? -28.804 22.800  -15.514 1.00 33.82  ? 164 LYS C CA  1 
ATOM   1220 C C   . LYS A 1 165 ? -29.162 21.406  -16.021 1.00 25.37  ? 164 LYS C C   1 
ATOM   1221 O O   . LYS A 1 165 ? -28.354 20.476  -15.907 1.00 32.55  ? 164 LYS C O   1 
ATOM   1222 C CB  . LYS A 1 165 ? -29.484 23.085  -14.174 1.00 34.16  ? 164 LYS C CB  1 
ATOM   1223 C CG  . LYS A 1 165 ? -28.551 23.696  -13.134 1.00 44.01  ? 164 LYS C CG  1 
ATOM   1224 C CD  . LYS A 1 165 ? -29.248 23.901  -11.796 1.00 45.23  ? 164 LYS C CD  1 
ATOM   1225 C CE  . LYS A 1 165 ? -29.365 25.377  -11.456 1.00 52.94  ? 164 LYS C CE  1 
ATOM   1226 N NZ  . LYS A 1 165 ? -30.221 25.611  -10.256 1.00 58.38  ? 164 LYS C NZ  1 
ATOM   1227 N N   . GLU A 1 166 ? -30.360 21.240  -16.594 1.00 33.02  ? 165 GLU C N   1 
ATOM   1228 C CA  . GLU A 1 166 ? -30.736 19.938  -17.142 1.00 39.07  ? 165 GLU C CA  1 
ATOM   1229 C C   . GLU A 1 166 ? -29.853 19.558  -18.323 1.00 34.40  ? 165 GLU C C   1 
ATOM   1230 O O   . GLU A 1 166 ? -29.381 18.417  -18.411 1.00 36.64  ? 165 GLU C O   1 
ATOM   1231 C CB  . GLU A 1 166 ? -32.207 19.932  -17.563 1.00 35.21  ? 165 GLU C CB  1 
ATOM   1232 C CG  . GLU A 1 166 ? -33.096 20.854  -16.763 1.00 48.67  ? 165 GLU C CG  1 
ATOM   1233 C CD  . GLU A 1 166 ? -34.558 20.458  -16.811 1.00 61.79  ? 165 GLU C CD  1 
ATOM   1234 O OE1 . GLU A 1 166 ? -35.327 21.116  -17.543 1.00 62.66  ? 165 GLU C OE1 1 
ATOM   1235 O OE2 . GLU A 1 166 ? -34.938 19.495  -16.113 1.00 75.44  ? 165 GLU C OE2 1 
ATOM   1236 N N   . ILE A 1 167 ? -29.624 20.499  -19.243 1.00 29.06  ? 166 ILE C N   1 
ATOM   1237 C CA  . ILE A 1 167 ? -28.773 20.224  -20.397 1.00 29.97  ? 166 ILE C CA  1 
ATOM   1238 C C   . ILE A 1 167 ? -27.390 19.771  -19.944 1.00 34.05  ? 166 ILE C C   1 
ATOM   1239 O O   . ILE A 1 167 ? -26.797 18.855  -20.529 1.00 32.05  ? 166 ILE C O   1 
ATOM   1240 C CB  . ILE A 1 167 ? -28.701 21.465  -21.310 1.00 29.32  ? 166 ILE C CB  1 
ATOM   1241 C CG1 . ILE A 1 167 ? -30.067 21.733  -21.942 1.00 31.42  ? 166 ILE C CG1 1 
ATOM   1242 C CG2 . ILE A 1 167 ? -27.643 21.286  -22.391 1.00 33.34  ? 166 ILE C CG2 1 
ATOM   1243 C CD1 . ILE A 1 167 ? -30.284 23.166  -22.353 1.00 34.10  ? 166 ILE C CD1 1 
ATOM   1244 N N   . SER A 1 168 ? -26.863 20.390  -18.882 1.00 28.23  ? 167 SER C N   1 
ATOM   1245 C CA  . SER A 1 168 ? -25.547 20.000  -18.386 1.00 23.77  ? 167 SER C CA  1 
ATOM   1246 C C   . SER A 1 168 ? -25.568 18.589  -17.816 1.00 25.10  ? 167 SER C C   1 
ATOM   1247 O O   . SER A 1 168 ? -24.636 17.808  -18.042 1.00 30.04  ? 167 SER C O   1 
ATOM   1248 C CB  . SER A 1 168 ? -25.064 20.999  -17.336 1.00 30.10  ? 167 SER C CB  1 
ATOM   1249 O OG  . SER A 1 168 ? -25.296 22.327  -17.764 1.00 36.52  ? 167 SER C OG  1 
ATOM   1250 N N   . VAL A 1 169 ? -26.620 18.243  -17.072 1.00 33.33  ? 168 VAL C N   1 
ATOM   1251 C CA  . VAL A 1 169 ? -26.723 16.892  -16.531 1.00 32.45  ? 168 VAL C CA  1 
ATOM   1252 C C   . VAL A 1 169 ? -26.920 15.886  -17.659 1.00 29.27  ? 168 VAL C C   1 
ATOM   1253 O O   . VAL A 1 169 ? -26.382 14.773  -17.618 1.00 29.15  ? 168 VAL C O   1 
ATOM   1254 C CB  . VAL A 1 169 ? -27.854 16.821  -15.487 1.00 35.07  ? 168 VAL C CB  1 
ATOM   1255 C CG1 . VAL A 1 169 ? -28.131 15.380  -15.080 1.00 28.86  ? 168 VAL C CG1 1 
ATOM   1256 C CG2 . VAL A 1 169 ? -27.502 17.659  -14.271 1.00 31.80  ? 168 VAL C CG2 1 
ATOM   1257 N N   . ALA A 1 170 ? -27.661 16.272  -18.700 1.00 28.38  ? 169 ALA C N   1 
ATOM   1258 C CA  . ALA A 1 170 ? -27.917 15.353  -19.804 1.00 31.85  ? 169 ALA C CA  1 
ATOM   1259 C C   . ALA A 1 170 ? -26.648 15.018  -20.582 1.00 35.61  ? 169 ALA C C   1 
ATOM   1260 O O   . ALA A 1 170 ? -26.554 13.931  -21.166 1.00 40.58  ? 169 ALA C O   1 
ATOM   1261 C CB  . ALA A 1 170 ? -28.967 15.940  -20.746 1.00 29.94  ? 169 ALA C CB  1 
ATOM   1262 N N   . ILE A 1 171 ? -25.670 15.923  -20.612 1.00 31.52  ? 170 ILE C N   1 
ATOM   1263 C CA  . ILE A 1 171 ? -24.437 15.662  -21.350 1.00 33.90  ? 170 ILE C CA  1 
ATOM   1264 C C   . ILE A 1 171 ? -23.368 15.173  -20.384 1.00 34.03  ? 170 ILE C C   1 
ATOM   1265 O O   . ILE A 1 171 ? -22.170 15.196  -20.696 1.00 33.73  ? 170 ILE C O   1 
ATOM   1266 C CB  . ILE A 1 171 ? -23.970 16.904  -22.132 1.00 36.24  ? 170 ILE C CB  1 
ATOM   1267 C CG1 . ILE A 1 171 ? -23.604 18.038  -21.169 1.00 34.87  ? 170 ILE C CG1 1 
ATOM   1268 C CG2 . ILE A 1 171 ? -25.040 17.335  -23.138 1.00 37.03  ? 170 ILE C CG2 1 
ATOM   1269 C CD1 . ILE A 1 171 ? -23.001 19.245  -21.854 1.00 33.55  ? 170 ILE C CD1 1 
ATOM   1270 N N   . GLY A 1 172 ? -23.802 14.720  -19.208 1.00 32.24  ? 171 GLY C N   1 
ATOM   1271 C CA  . GLY A 1 172 ? -22.888 14.143  -18.247 1.00 30.85  ? 171 GLY C CA  1 
ATOM   1272 C C   . GLY A 1 172 ? -21.978 15.127  -17.552 1.00 30.00  ? 171 GLY C C   1 
ATOM   1273 O O   . GLY A 1 172 ? -20.822 14.793  -17.274 1.00 35.04  ? 171 GLY C O   1 
ATOM   1274 N N   . LYS A 1 173 ? -22.457 16.336  -17.274 1.00 28.81  ? 172 LYS C N   1 
ATOM   1275 C CA  . LYS A 1 173 ? -21.685 17.345  -16.564 1.00 32.73  ? 172 LYS C CA  1 
ATOM   1276 C C   . LYS A 1 173 ? -22.376 17.696  -15.254 1.00 31.41  ? 172 LYS C C   1 
ATOM   1277 O O   . LYS A 1 173 ? -23.551 17.385  -15.034 1.00 30.57  ? 172 LYS C O   1 
ATOM   1278 C CB  . LYS A 1 173 ? -21.494 18.613  -17.409 1.00 31.24  ? 172 LYS C CB  1 
ATOM   1279 C CG  . LYS A 1 173 ? -20.950 18.372  -18.800 1.00 33.11  ? 172 LYS C CG  1 
ATOM   1280 C CD  . LYS A 1 173 ? -19.453 18.176  -18.792 1.00 27.09  ? 172 LYS C CD  1 
ATOM   1281 C CE  . LYS A 1 173 ? -18.891 18.295  -20.203 1.00 29.37  ? 172 LYS C CE  1 
ATOM   1282 N NZ  . LYS A 1 173 ? -17.603 17.560  -20.338 1.00 30.68  ? 172 LYS C NZ  1 
ATOM   1283 N N   . ASN A 1 174 ? -21.632 18.371  -14.383 1.00 29.16  ? 173 ASN C N   1 
ATOM   1284 C CA  . ASN A 1 174 ? -22.143 18.752  -13.071 1.00 28.60  ? 173 ASN C CA  1 
ATOM   1285 C C   . ASN A 1 174 ? -22.341 20.259  -13.010 1.00 31.55  ? 173 ASN C C   1 
ATOM   1286 O O   . ASN A 1 174 ? -21.373 21.007  -12.803 1.00 30.63  ? 173 ASN C O   1 
ATOM   1287 C CB  . ASN A 1 174 ? -21.184 18.288  -11.974 1.00 38.51  ? 173 ASN C CB  1 
ATOM   1288 C CG  . ASN A 1 174 ? -21.290 16.803  -11.709 1.00 40.36  ? 173 ASN C CG  1 
ATOM   1289 O OD1 . ASN A 1 174 ? -20.479 16.014  -12.196 1.00 46.85  ? 173 ASN C OD1 1 
ATOM   1290 N ND2 . ASN A 1 174 ? -22.289 16.412  -10.929 1.00 45.26  ? 173 ASN C ND2 1 
ATOM   1291 N N   . PRO A 1 175 ? -23.563 20.754  -13.187 1.00 27.51  ? 174 PRO C N   1 
ATOM   1292 C CA  . PRO A 1 175 ? -23.773 22.203  -13.179 1.00 27.23  ? 174 PRO C CA  1 
ATOM   1293 C C   . PRO A 1 175 ? -23.651 22.776  -11.776 1.00 39.87  ? 174 PRO C C   1 
ATOM   1294 O O   . PRO A 1 175 ? -24.040 22.148  -10.788 1.00 40.10  ? 174 PRO C O   1 
ATOM   1295 C CB  . PRO A 1 175 ? -25.198 22.357  -13.721 1.00 31.47  ? 174 PRO C CB  1 
ATOM   1296 C CG  . PRO A 1 175 ? -25.868 21.075  -13.366 1.00 23.68  ? 174 PRO C CG  1 
ATOM   1297 C CD  . PRO A 1 175 ? -24.805 20.013  -13.466 1.00 29.86  ? 174 PRO C CD  1 
ATOM   1298 N N   . VAL A 1 176 ? -23.095 23.983  -11.704 1.00 35.02  ? 175 VAL C N   1 
ATOM   1299 C CA  . VAL A 1 176 ? -23.011 24.766  -10.479 1.00 29.00  ? 175 VAL C CA  1 
ATOM   1300 C C   . VAL A 1 176 ? -23.548 26.155  -10.792 1.00 35.53  ? 175 VAL C C   1 
ATOM   1301 O O   . VAL A 1 176 ? -23.080 26.802  -11.736 1.00 31.57  ? 175 VAL C O   1 
ATOM   1302 C CB  . VAL A 1 176 ? -21.566 24.848  -9.948  1.00 27.72  ? 175 VAL C CB  1 
ATOM   1303 C CG1 . VAL A 1 176 ? -21.453 25.904  -8.860  1.00 31.24  ? 175 VAL C CG1 1 
ATOM   1304 C CG2 . VAL A 1 176 ? -21.109 23.489  -9.436  1.00 29.45  ? 175 VAL C CG2 1 
ATOM   1305 N N   . GLN A 1 177 ? -24.533 26.607  -10.019 1.00 25.06  ? 176 GLN C N   1 
ATOM   1306 C CA  . GLN A 1 177 ? -25.142 27.907  -10.270 1.00 32.76  ? 176 GLN C CA  1 
ATOM   1307 C C   . GLN A 1 177 ? -24.279 29.026  -9.701  1.00 27.93  ? 176 GLN C C   1 
ATOM   1308 O O   . GLN A 1 177 ? -23.869 28.979  -8.537  1.00 41.52  ? 176 GLN C O   1 
ATOM   1309 C CB  . GLN A 1 177 ? -26.544 27.974  -9.669  1.00 35.17  ? 176 GLN C CB  1 
ATOM   1310 C CG  . GLN A 1 177 ? -27.360 29.139  -10.191 1.00 33.88  ? 176 GLN C CG  1 
ATOM   1311 C CD  . GLN A 1 177 ? -28.743 29.191  -9.585  1.00 47.80  ? 176 GLN C CD  1 
ATOM   1312 O OE1 . GLN A 1 177 ? -29.465 28.192  -9.572  1.00 48.54  ? 176 GLN C OE1 1 
ATOM   1313 N NE2 . GLN A 1 177 ? -29.125 30.361  -9.084  1.00 51.04  ? 176 GLN C NE2 1 
ATOM   1314 N N   . VAL A 1 178 ? -24.017 30.039  -10.524 1.00 24.54  ? 177 VAL C N   1 
ATOM   1315 C CA  . VAL A 1 178 ? -23.196 31.185  -10.150 1.00 28.03  ? 177 VAL C CA  1 
ATOM   1316 C C   . VAL A 1 178 ? -23.941 32.454  -10.537 1.00 28.90  ? 177 VAL C C   1 
ATOM   1317 O O   . VAL A 1 178 ? -24.313 32.625  -11.703 1.00 32.38  ? 177 VAL C O   1 
ATOM   1318 C CB  . VAL A 1 178 ? -21.819 31.155  -10.833 1.00 28.84  ? 177 VAL C CB  1 
ATOM   1319 C CG1 . VAL A 1 178 ? -21.029 32.403  -10.472 1.00 28.10  ? 177 VAL C CG1 1 
ATOM   1320 C CG2 . VAL A 1 178 ? -21.057 29.893  -10.462 1.00 28.63  ? 177 VAL C CG2 1 
ATOM   1321 N N   . ASN A 1 179 ? -24.149 33.344  -9.571  1.00 24.12  ? 178 ASN C N   1 
ATOM   1322 C CA  . ASN A 1 179 ? -24.681 34.665  -9.875  1.00 29.18  ? 178 ASN C CA  1 
ATOM   1323 C C   . ASN A 1 179 ? -23.536 35.579  -10.298 1.00 34.46  ? 178 ASN C C   1 
ATOM   1324 O O   . ASN A 1 179 ? -22.504 35.639  -9.622  1.00 29.88  ? 178 ASN C O   1 
ATOM   1325 C CB  . ASN A 1 179 ? -25.423 35.234  -8.668  1.00 31.43  ? 178 ASN C CB  1 
ATOM   1326 C CG  . ASN A 1 179 ? -26.613 34.383  -8.271  1.00 36.10  ? 178 ASN C CG  1 
ATOM   1327 O OD1 . ASN A 1 179 ? -27.561 34.226  -9.041  1.00 45.05  ? 178 ASN C OD1 1 
ATOM   1328 N ND2 . ASN A 1 179 ? -26.568 33.822  -7.068  1.00 43.40  ? 178 ASN C ND2 1 
ATOM   1329 N N   . GLU A 1 180 ? -23.728 36.290  -11.413 1.00 32.22  ? 179 GLU C N   1 
ATOM   1330 C CA  . GLU A 1 180 ? -22.629 36.931  -12.133 1.00 22.08  ? 179 GLU C CA  1 
ATOM   1331 C C   . GLU A 1 180 ? -21.768 37.796  -11.226 1.00 32.33  ? 179 GLU C C   1 
ATOM   1332 O O   . GLU A 1 180 ? -22.245 38.767  -10.630 1.00 26.72  ? 179 GLU C O   1 
ATOM   1333 C CB  . GLU A 1 180 ? -23.167 37.779  -13.284 1.00 27.19  ? 179 GLU C CB  1 
ATOM   1334 C CG  . GLU A 1 180 ? -22.056 38.393  -14.134 1.00 33.87  ? 179 GLU C CG  1 
ATOM   1335 C CD  . GLU A 1 180 ? -22.523 39.580  -14.959 1.00 40.82  ? 179 GLU C CD  1 
ATOM   1336 O OE1 . GLU A 1 180 ? -23.646 39.520  -15.504 1.00 40.89  ? 179 GLU C OE1 1 
ATOM   1337 O OE2 . GLU A 1 180 ? -21.764 40.569  -15.071 1.00 38.90  ? 179 GLU C OE2 1 
ATOM   1338 N N   . ALA A 1 181 ? -20.493 37.429  -11.137 1.00 24.59  ? 180 ALA C N   1 
ATOM   1339 C CA  . ALA A 1 181 ? -19.466 38.219  -10.480 1.00 29.35  ? 180 ALA C CA  1 
ATOM   1340 C C   . ALA A 1 181 ? -18.146 37.886  -11.153 1.00 20.53  ? 180 ALA C C   1 
ATOM   1341 O O   . ALA A 1 181 ? -17.969 36.782  -11.676 1.00 25.69  ? 180 ALA C O   1 
ATOM   1342 C CB  . ALA A 1 181 ? -19.394 37.938  -8.973  1.00 24.82  ? 180 ALA C CB  1 
ATOM   1343 N N   . ALA A 1 182 ? -17.228 38.849  -11.148 1.00 20.98  ? 181 ALA C N   1 
ATOM   1344 C CA  . ALA A 1 182 ? -15.951 38.664  -11.825 1.00 28.89  ? 181 ALA C CA  1 
ATOM   1345 C C   . ALA A 1 182 ? -15.278 37.380  -11.360 1.00 22.71  ? 181 ALA C C   1 
ATOM   1346 O O   . ALA A 1 182 ? -15.248 37.077  -10.165 1.00 27.76  ? 181 ALA C O   1 
ATOM   1347 C CB  . ALA A 1 182 ? -15.038 39.862  -11.572 1.00 33.65  ? 181 ALA C CB  1 
ATOM   1348 N N   . GLY A 1 183 ? -14.761 36.610  -12.318 1.00 26.86  ? 182 GLY C N   1 
ATOM   1349 C CA  . GLY A 1 183 ? -14.083 35.367  -12.022 1.00 27.61  ? 182 GLY C CA  1 
ATOM   1350 C C   . GLY A 1 183 ? -14.976 34.217  -11.607 1.00 28.22  ? 182 GLY C C   1 
ATOM   1351 O O   . GLY A 1 183 ? -14.471 33.096  -11.441 1.00 25.71  ? 182 GLY C O   1 
ATOM   1352 N N   . PHE A 1 184 ? -16.280 34.450  -11.437 1.00 20.02  ? 183 PHE C N   1 
ATOM   1353 C CA  . PHE A 1 184 ? -17.222 33.411  -11.036 1.00 22.92  ? 183 PHE C CA  1 
ATOM   1354 C C   . PHE A 1 184 ? -16.738 32.729  -9.759  1.00 30.97  ? 183 PHE C C   1 
ATOM   1355 O O   . PHE A 1 184 ? -16.545 33.395  -8.735  1.00 24.53  ? 183 PHE C O   1 
ATOM   1356 C CB  . PHE A 1 184 ? -17.421 32.398  -12.173 1.00 23.82  ? 183 PHE C CB  1 
ATOM   1357 C CG  . PHE A 1 184 ? -17.797 33.032  -13.496 1.00 26.11  ? 183 PHE C CG  1 
ATOM   1358 C CD1 . PHE A 1 184 ? -18.609 34.159  -13.538 1.00 24.25  ? 183 PHE C CD1 1 
ATOM   1359 C CD2 . PHE A 1 184 ? -17.332 32.505  -14.695 1.00 31.60  ? 183 PHE C CD2 1 
ATOM   1360 C CE1 . PHE A 1 184 ? -18.951 34.746  -14.746 1.00 27.15  ? 183 PHE C CE1 1 
ATOM   1361 C CE2 . PHE A 1 184 ? -17.673 33.088  -15.911 1.00 24.07  ? 183 PHE C CE2 1 
ATOM   1362 C CZ  . PHE A 1 184 ? -18.484 34.206  -15.935 1.00 25.94  ? 183 PHE C CZ  1 
ATOM   1363 N N   . VAL A 1 185 ? -16.514 31.413  -9.811  1.00 29.13  ? 184 VAL C N   1 
ATOM   1364 C CA  . VAL A 1 185 ? -16.022 30.670  -8.655  1.00 26.75  ? 184 VAL C CA  1 
ATOM   1365 C C   . VAL A 1 185 ? -14.604 30.162  -8.901  1.00 31.23  ? 184 VAL C C   1 
ATOM   1366 O O   . VAL A 1 185 ? -13.680 30.488  -8.146  1.00 28.90  ? 184 VAL C O   1 
ATOM   1367 C CB  . VAL A 1 185 ? -16.968 29.509  -8.296  1.00 28.69  ? 184 VAL C CB  1 
ATOM   1368 C CG1 . VAL A 1 185 ? -16.466 28.778  -7.059  1.00 27.71  ? 184 VAL C CG1 1 
ATOM   1369 C CG2 . VAL A 1 185 ? -18.375 30.026  -8.059  1.00 29.02  ? 184 VAL C CG2 1 
ATOM   1370 N N   . VAL A 1 186 ? -14.415 29.376  -9.965  1.00 33.24  ? 185 VAL C N   1 
ATOM   1371 C CA  . VAL A 1 186 ? -13.150 28.665  -10.154 1.00 31.12  ? 185 VAL C CA  1 
ATOM   1372 C C   . VAL A 1 186 ? -12.014 29.636  -10.460 1.00 31.05  ? 185 VAL C C   1 
ATOM   1373 O O   . VAL A 1 186 ? -10.967 29.613  -9.802  1.00 31.42  ? 185 VAL C O   1 
ATOM   1374 C CB  . VAL A 1 186 ? -13.290 27.602  -11.255 1.00 31.68  ? 185 VAL C CB  1 
ATOM   1375 C CG1 . VAL A 1 186 ? -11.927 27.025  -11.609 1.00 24.13  ? 185 VAL C CG1 1 
ATOM   1376 C CG2 . VAL A 1 186 ? -14.228 26.511  -10.797 1.00 33.77  ? 185 VAL C CG2 1 
ATOM   1377 N N   . ASN A 1 187 ? -12.190 30.483  -11.478 1.00 31.70  ? 186 ASN C N   1 
ATOM   1378 C CA  . ASN A 1 187 ? -11.138 31.432  -11.835 1.00 28.26  ? 186 ASN C CA  1 
ATOM   1379 C C   . ASN A 1 187 ? -10.823 32.366  -10.672 1.00 29.65  ? 186 ASN C C   1 
ATOM   1380 O O   . ASN A 1 187 ? -9.653  32.674  -10.410 1.00 25.49  ? 186 ASN C O   1 
ATOM   1381 C CB  . ASN A 1 187 ? -11.552 32.235  -13.071 1.00 25.57  ? 186 ASN C CB  1 
ATOM   1382 C CG  . ASN A 1 187 ? -11.115 31.583  -14.375 1.00 29.31  ? 186 ASN C CG  1 
ATOM   1383 O OD1 . ASN A 1 187 ? -10.132 30.842  -14.419 1.00 23.86  ? 186 ASN C OD1 1 
ATOM   1384 N ND2 . ASN A 1 187 ? -11.853 31.858  -15.447 1.00 35.61  ? 186 ASN C ND2 1 
ATOM   1385 N N   . ARG A 1 188 ? -11.856 32.806  -9.945  1.00 27.90  ? 187 ARG C N   1 
ATOM   1386 C CA  . ARG A 1 188 ? -11.654 33.744  -8.845  1.00 28.53  ? 187 ARG C CA  1 
ATOM   1387 C C   . ARG A 1 188 ? -10.823 33.139  -7.721  1.00 24.22  ? 187 ARG C C   1 
ATOM   1388 O O   . ARG A 1 188 ? -10.108 33.865  -7.022  1.00 23.42  ? 187 ARG C O   1 
ATOM   1389 C CB  . ARG A 1 188 ? -13.003 34.212  -8.307  1.00 25.47  ? 187 ARG C CB  1 
ATOM   1390 C CG  . ARG A 1 188 ? -12.911 35.282  -7.237  1.00 25.64  ? 187 ARG C CG  1 
ATOM   1391 C CD  . ARG A 1 188 ? -14.291 35.624  -6.742  1.00 25.15  ? 187 ARG C CD  1 
ATOM   1392 N NE  . ARG A 1 188 ? -14.278 36.346  -5.478  1.00 29.51  ? 187 ARG C NE  1 
ATOM   1393 C CZ  . ARG A 1 188 ? -15.328 36.985  -4.984  1.00 29.85  ? 187 ARG C CZ  1 
ATOM   1394 N NH1 . ARG A 1 188 ? -16.485 37.014  -5.628  1.00 21.99  ? 187 ARG C NH1 1 
ATOM   1395 N NH2 . ARG A 1 188 ? -15.216 37.610  -3.814  1.00 27.77  ? 187 ARG C NH2 1 
ATOM   1396 N N   . ILE A 1 189 ? -10.900 31.826  -7.532  1.00 24.86  ? 188 ILE C N   1 
ATOM   1397 C CA  . ILE A 1 189 ? -10.098 31.158  -6.514  1.00 29.54  ? 188 ILE C CA  1 
ATOM   1398 C C   . ILE A 1 189 ? -8.759  30.695  -7.078  1.00 32.05  ? 188 ILE C C   1 
ATOM   1399 O O   . ILE A 1 189 ? -7.718  30.848  -6.433  1.00 30.59  ? 188 ILE C O   1 
ATOM   1400 C CB  . ILE A 1 189 ? -10.893 29.979  -5.921  1.00 35.32  ? 188 ILE C CB  1 
ATOM   1401 C CG1 . ILE A 1 189 ? -12.131 30.481  -5.179  1.00 26.58  ? 188 ILE C CG1 1 
ATOM   1402 C CG2 . ILE A 1 189 ? -10.023 29.162  -4.989  1.00 29.57  ? 188 ILE C CG2 1 
ATOM   1403 C CD1 . ILE A 1 189 ? -13.005 29.364  -4.648  1.00 23.28  ? 188 ILE C CD1 1 
ATOM   1404 N N   . LEU A 1 190 ? -8.767  30.141  -8.292  1.00 27.68  ? 189 LEU C N   1 
ATOM   1405 C CA  . LEU A 1 190 ? -7.589  29.450  -8.807  1.00 28.28  ? 189 LEU C CA  1 
ATOM   1406 C C   . LEU A 1 190 ? -6.505  30.416  -9.269  1.00 25.03  ? 189 LEU C C   1 
ATOM   1407 O O   . LEU A 1 190 ? -5.317  30.151  -9.070  1.00 27.49  ? 189 LEU C O   1 
ATOM   1408 C CB  . LEU A 1 190 ? -7.988  28.524  -9.960  1.00 34.47  ? 189 LEU C CB  1 
ATOM   1409 C CG  . LEU A 1 190 ? -6.905  27.595  -10.510 1.00 33.68  ? 189 LEU C CG  1 
ATOM   1410 C CD1 . LEU A 1 190 ? -6.368  26.704  -9.404  1.00 30.87  ? 189 LEU C CD1 1 
ATOM   1411 C CD2 . LEU A 1 190 ? -7.443  26.761  -11.665 1.00 36.69  ? 189 LEU C CD2 1 
ATOM   1412 N N   . ILE A 1 191 ? -6.875  31.521  -9.909  1.00 21.88  ? 190 ILE C N   1 
ATOM   1413 C CA  . ILE A 1 191 ? -5.865  32.380  -10.526 1.00 26.41  ? 190 ILE C CA  1 
ATOM   1414 C C   . ILE A 1 191 ? -5.127  33.203  -9.471  1.00 20.88  ? 190 ILE C C   1 
ATOM   1415 O O   . ILE A 1 191 ? -3.904  33.371  -9.591  1.00 21.18  ? 190 ILE C O   1 
ATOM   1416 C CB  . ILE A 1 191 ? -6.477  33.276  -11.614 1.00 25.74  ? 190 ILE C CB  1 
ATOM   1417 C CG1 . ILE A 1 191 ? -7.240  32.426  -12.635 1.00 26.09  ? 190 ILE C CG1 1 
ATOM   1418 C CG2 . ILE A 1 191 ? -5.378  34.031  -12.335 1.00 15.52  ? 190 ILE C CG2 1 
ATOM   1419 C CD1 . ILE A 1 191 ? -6.343  31.535  -13.481 1.00 21.61  ? 190 ILE C CD1 1 
ATOM   1420 N N   . PRO A 1 192 ? -5.787  33.734  -8.433  1.00 23.79  ? 191 PRO C N   1 
ATOM   1421 C CA  . PRO A 1 192 ? -5.007  34.307  -7.324  1.00 21.32  ? 191 PRO C CA  1 
ATOM   1422 C C   . PRO A 1 192 ? -4.026  33.328  -6.688  1.00 20.88  ? 191 PRO C C   1 
ATOM   1423 O O   . PRO A 1 192 ? -3.022  33.773  -6.117  1.00 28.14  ? 191 PRO C O   1 
ATOM   1424 C CB  . PRO A 1 192 ? -6.091  34.761  -6.340  1.00 24.72  ? 191 PRO C CB  1 
ATOM   1425 C CG  . PRO A 1 192 ? -7.225  35.137  -7.217  1.00 18.57  ? 191 PRO C CG  1 
ATOM   1426 C CD  . PRO A 1 192 ? -7.213  34.106  -8.325  1.00 21.73  ? 191 PRO C CD  1 
ATOM   1427 N N   . MET A 1 193 ? -4.278  32.017  -6.766  1.00 25.11  ? 192 MET C N   1 
ATOM   1428 C CA  . MET A 1 193 ? -3.283  31.030  -6.343  1.00 24.09  ? 192 MET C CA  1 
ATOM   1429 C C   . MET A 1 193 ? -1.972  31.232  -7.085  1.00 26.01  ? 192 MET C C   1 
ATOM   1430 O O   . MET A 1 193 ? -0.914  31.439  -6.479  1.00 26.47  ? 192 MET C O   1 
ATOM   1431 C CB  . MET A 1 193 ? -3.774  29.611  -6.623  1.00 26.60  ? 192 MET C CB  1 
ATOM   1432 C CG  . MET A 1 193 ? -4.851  29.034  -5.757  1.00 37.50  ? 192 MET C CG  1 
ATOM   1433 S SD  . MET A 1 193 ? -4.604  27.243  -5.758  1.00 59.44  ? 192 MET C SD  1 
ATOM   1434 C CE  . MET A 1 193 ? -3.564  26.992  -7.198  1.00 39.39  ? 192 MET C CE  1 
ATOM   1435 N N   . ILE A 1 194 ? -2.033  31.108  -8.415  1.00 20.85  ? 193 ILE C N   1 
ATOM   1436 C CA  . ILE A 1 194 ? -0.856  31.270  -9.259  1.00 18.75  ? 193 ILE C CA  1 
ATOM   1437 C C   . ILE A 1 194 ? -0.221  32.629  -9.025  1.00 20.56  ? 193 ILE C C   1 
ATOM   1438 O O   . ILE A 1 194 ? 1.009   32.762  -8.993  1.00 25.27  ? 193 ILE C O   1 
ATOM   1439 C CB  . ILE A 1 194 ? -1.240  31.075  -10.736 1.00 18.98  ? 193 ILE C CB  1 
ATOM   1440 C CG1 . ILE A 1 194 ? -1.923  29.718  -10.930 1.00 23.85  ? 193 ILE C CG1 1 
ATOM   1441 C CG2 . ILE A 1 194 ? -0.019  31.209  -11.631 1.00 20.11  ? 193 ILE C CG2 1 
ATOM   1442 C CD1 . ILE A 1 194 ? -2.570  29.544  -12.290 1.00 21.43  ? 193 ILE C CD1 1 
ATOM   1443 N N   . ASN A 1 195 ? -1.052  33.659  -8.857  1.00 21.96  ? 194 ASN C N   1 
ATOM   1444 C CA  . ASN A 1 195 ? -0.529  34.991  -8.591  1.00 17.88  ? 194 ASN C CA  1 
ATOM   1445 C C   . ASN A 1 195 ? 0.282   35.009  -7.302  1.00 21.82  ? 194 ASN C C   1 
ATOM   1446 O O   . ASN A 1 195 ? 1.397   35.545  -7.268  1.00 25.89  ? 194 ASN C O   1 
ATOM   1447 C CB  . ASN A 1 195 ? -1.682  35.992  -8.527  1.00 15.31  ? 194 ASN C CB  1 
ATOM   1448 C CG  . ASN A 1 195 ? -1.228  37.417  -8.754  1.00 23.12  ? 194 ASN C CG  1 
ATOM   1449 O OD1 . ASN A 1 195 ? -0.636  37.732  -9.788  1.00 17.87  ? 194 ASN C OD1 1 
ATOM   1450 N ND2 . ASN A 1 195 ? -1.502  38.293  -7.784  1.00 20.47  ? 194 ASN C ND2 1 
ATOM   1451 N N   . GLU A 1 196 ? -0.251  34.401  -6.237  1.00 23.00  ? 195 GLU C N   1 
ATOM   1452 C CA  . GLU A 1 196 ? 0.463   34.374  -4.963  1.00 25.73  ? 195 GLU C CA  1 
ATOM   1453 C C   . GLU A 1 196 ? 1.776   33.609  -5.071  1.00 27.29  ? 195 GLU C C   1 
ATOM   1454 O O   . GLU A 1 196 ? 2.787   34.012  -4.482  1.00 26.93  ? 195 GLU C O   1 
ATOM   1455 C CB  . GLU A 1 196 ? -0.415  33.757  -3.878  1.00 22.12  ? 195 GLU C CB  1 
ATOM   1456 C CG  . GLU A 1 196 ? 0.142   33.950  -2.475  1.00 29.39  ? 195 GLU C CG  1 
ATOM   1457 C CD  . GLU A 1 196 ? 0.048   35.391  -2.012  1.00 35.14  ? 195 GLU C CD  1 
ATOM   1458 O OE1 . GLU A 1 196 ? -1.062  35.954  -2.064  1.00 41.97  ? 195 GLU C OE1 1 
ATOM   1459 O OE2 . GLU A 1 196 ? 1.079   35.963  -1.602  1.00 37.82  ? 195 GLU C OE2 1 
ATOM   1460 N N   . ALA A 1 197 ? 1.780   32.493  -5.802  1.00 21.35  ? 196 ALA C N   1 
ATOM   1461 C CA  . ALA A 1 197 ? 3.020   31.745  -5.979  1.00 19.26  ? 196 ALA C CA  1 
ATOM   1462 C C   . ALA A 1 197 ? 4.062   32.584  -6.697  1.00 23.26  ? 196 ALA C C   1 
ATOM   1463 O O   . ALA A 1 197 ? 5.254   32.520  -6.374  1.00 20.77  ? 196 ALA C O   1 
ATOM   1464 C CB  . ALA A 1 197 ? 2.753   30.455  -6.748  1.00 22.30  ? 196 ALA C CB  1 
ATOM   1465 N N   . ALA A 1 198 ? 3.631   33.382  -7.675  1.00 20.63  ? 197 ALA C N   1 
ATOM   1466 C CA  . ALA A 1 198 ? 4.562   34.265  -8.369  1.00 27.07  ? 197 ALA C CA  1 
ATOM   1467 C C   . ALA A 1 198 ? 5.127   35.319  -7.424  1.00 21.93  ? 197 ALA C C   1 
ATOM   1468 O O   . ALA A 1 198 ? 6.327   35.615  -7.465  1.00 22.67  ? 197 ALA C O   1 
ATOM   1469 C CB  . ALA A 1 198 ? 3.871   34.920  -9.565  1.00 19.25  ? 197 ALA C CB  1 
ATOM   1470 N N   . PHE A 1 199 ? 4.280   35.896  -6.567  1.00 25.24  ? 198 PHE C N   1 
ATOM   1471 C CA  . PHE A 1 199 ? 4.770   36.830  -5.556  1.00 22.55  ? 198 PHE C CA  1 
ATOM   1472 C C   . PHE A 1 199 ? 5.802   36.166  -4.654  1.00 25.72  ? 198 PHE C C   1 
ATOM   1473 O O   . PHE A 1 199 ? 6.837   36.764  -4.333  1.00 25.87  ? 198 PHE C O   1 
ATOM   1474 C CB  . PHE A 1 199 ? 3.603   37.365  -4.722  1.00 21.34  ? 198 PHE C CB  1 
ATOM   1475 C CG  . PHE A 1 199 ? 3.045   38.672  -5.215  1.00 26.77  ? 198 PHE C CG  1 
ATOM   1476 C CD1 . PHE A 1 199 ? 3.809   39.829  -5.180  1.00 28.92  ? 198 PHE C CD1 1 
ATOM   1477 C CD2 . PHE A 1 199 ? 1.750   38.746  -5.706  1.00 18.07  ? 198 PHE C CD2 1 
ATOM   1478 C CE1 . PHE A 1 199 ? 3.288   41.039  -5.627  1.00 25.01  ? 198 PHE C CE1 1 
ATOM   1479 C CE2 . PHE A 1 199 ? 1.226   39.948  -6.154  1.00 17.73  ? 198 PHE C CE2 1 
ATOM   1480 C CZ  . PHE A 1 199 ? 1.995   41.096  -6.114  1.00 16.17  ? 198 PHE C CZ  1 
ATOM   1481 N N   . ILE A 1 200 ? 5.535   34.925  -4.239  1.00 25.92  ? 199 ILE C N   1 
ATOM   1482 C CA  . ILE A 1 200 ? 6.469   34.189  -3.393  1.00 22.62  ? 199 ILE C CA  1 
ATOM   1483 C C   . ILE A 1 200 ? 7.824   34.065  -4.080  1.00 23.27  ? 199 ILE C C   1 
ATOM   1484 O O   . ILE A 1 200 ? 8.873   34.300  -3.467  1.00 25.49  ? 199 ILE C O   1 
ATOM   1485 C CB  . ILE A 1 200 ? 5.875   32.813  -3.034  1.00 20.74  ? 199 ILE C CB  1 
ATOM   1486 C CG1 . ILE A 1 200 ? 4.757   32.975  -2.003  1.00 22.53  ? 199 ILE C CG1 1 
ATOM   1487 C CG2 . ILE A 1 200 ? 6.946   31.872  -2.513  1.00 23.17  ? 199 ILE C CG2 1 
ATOM   1488 C CD1 . ILE A 1 200 ? 3.906   31.740  -1.834  1.00 27.16  ? 199 ILE C CD1 1 
ATOM   1489 N N   . LYS A 1 201 ? 7.820   33.719  -5.370  1.00 22.03  ? 200 LYS C N   1 
ATOM   1490 C CA  . LYS A 1 201 ? 9.063   33.630  -6.128  1.00 15.00  ? 200 LYS C CA  1 
ATOM   1491 C C   . LYS A 1 201 ? 9.713   34.999  -6.287  1.00 20.45  ? 200 LYS C C   1 
ATOM   1492 O O   . LYS A 1 201 ? 10.923  35.151  -6.078  1.00 23.22  ? 200 LYS C O   1 
ATOM   1493 C CB  . LYS A 1 201 ? 8.794   33.003  -7.498  1.00 18.67  ? 200 LYS C CB  1 
ATOM   1494 C CG  . LYS A 1 201 ? 9.944   33.145  -8.487  1.00 19.93  ? 200 LYS C CG  1 
ATOM   1495 C CD  . LYS A 1 201 ? 11.173  32.394  -7.999  1.00 27.29  ? 200 LYS C CD  1 
ATOM   1496 C CE  . LYS A 1 201 ? 12.458  32.997  -8.547  1.00 32.57  ? 200 LYS C CE  1 
ATOM   1497 N NZ  . LYS A 1 201 ? 13.646  32.195  -8.134  1.00 26.14  ? 200 LYS C NZ  1 
ATOM   1498 N N   . MET A 1 202 ? 8.928   36.010  -6.667  1.00 21.43  ? 201 MET C N   1 
ATOM   1499 C CA  . MET A 1 202 ? 9.498   37.338  -6.875  1.00 30.54  ? 201 MET C CA  1 
ATOM   1500 C C   . MET A 1 202 ? 10.122  37.877  -5.594  1.00 24.28  ? 201 MET C C   1 
ATOM   1501 O O   . MET A 1 202 ? 11.191  38.496  -5.628  1.00 23.93  ? 201 MET C O   1 
ATOM   1502 C CB  . MET A 1 202 ? 8.432   38.302  -7.400  1.00 31.63  ? 201 MET C CB  1 
ATOM   1503 C CG  . MET A 1 202 ? 8.892   39.757  -7.446  1.00 29.70  ? 201 MET C CG  1 
ATOM   1504 S SD  . MET A 1 202 ? 7.610   40.906  -7.976  1.00 34.21  ? 201 MET C SD  1 
ATOM   1505 C CE  . MET A 1 202 ? 6.872   41.310  -6.394  1.00 37.33  ? 201 MET C CE  1 
ATOM   1506 N N   . GLU A 1 203 ? 9.485   37.631  -4.451  1.00 23.21  ? 202 GLU C N   1 
ATOM   1507 C CA  . GLU A 1 203 ? 10.002  38.107  -3.177  1.00 24.20  ? 202 GLU C CA  1 
ATOM   1508 C C   . GLU A 1 203 ? 11.105  37.217  -2.607  1.00 32.18  ? 202 GLU C C   1 
ATOM   1509 O O   . GLU A 1 203 ? 11.548  37.456  -1.479  1.00 28.73  ? 202 GLU C O   1 
ATOM   1510 C CB  . GLU A 1 203 ? 8.858   38.250  -2.171  1.00 23.19  ? 202 GLU C CB  1 
ATOM   1511 C CG  . GLU A 1 203 ? 8.015   39.494  -2.413  1.00 33.70  ? 202 GLU C CG  1 
ATOM   1512 C CD  . GLU A 1 203 ? 6.652   39.424  -1.762  1.00 39.93  ? 202 GLU C CD  1 
ATOM   1513 O OE1 . GLU A 1 203 ? 6.438   38.525  -0.923  1.00 46.39  ? 202 GLU C OE1 1 
ATOM   1514 O OE2 . GLU A 1 203 ? 5.793   40.271  -2.087  1.00 46.14  ? 202 GLU C OE2 1 
ATOM   1515 N N   . GLY A 1 204 ? 11.563  36.214  -3.357  1.00 26.33  ? 203 GLY C N   1 
ATOM   1516 C CA  . GLY A 1 204 ? 12.686  35.404  -2.928  1.00 22.21  ? 203 GLY C CA  1 
ATOM   1517 C C   . GLY A 1 204 ? 12.414  34.489  -1.756  1.00 31.34  ? 203 GLY C C   1 
ATOM   1518 O O   . GLY A 1 204 ? 13.359  34.061  -1.088  1.00 25.87  ? 203 GLY C O   1 
ATOM   1519 N N   . VAL A 1 205 ? 11.147  34.172  -1.484  1.00 32.09  ? 204 VAL C N   1 
ATOM   1520 C CA  . VAL A 1 205 ? 10.824  33.296  -0.360  1.00 26.85  ? 204 VAL C CA  1 
ATOM   1521 C C   . VAL A 1 205 ? 11.312  31.877  -0.635  1.00 33.91  ? 204 VAL C C   1 
ATOM   1522 O O   . VAL A 1 205 ? 11.942  31.239  0.217   1.00 30.91  ? 204 VAL C O   1 
ATOM   1523 C CB  . VAL A 1 205 ? 9.313   33.335  -0.072  1.00 24.25  ? 204 VAL C CB  1 
ATOM   1524 C CG1 . VAL A 1 205 ? 8.930   32.271  0.947   1.00 28.33  ? 204 VAL C CG1 1 
ATOM   1525 C CG2 . VAL A 1 205 ? 8.902   34.718  0.410   1.00 26.65  ? 204 VAL C CG2 1 
ATOM   1526 N N   . SER A 1 206 ? 11.034  31.366  -1.831  1.00 23.62  ? 205 SER C N   1 
ATOM   1527 C CA  . SER A 1 206 ? 11.485  30.043  -2.237  1.00 28.08  ? 205 SER C CA  1 
ATOM   1528 C C   . SER A 1 206 ? 11.690  30.051  -3.748  1.00 36.63  ? 205 SER C C   1 
ATOM   1529 O O   . SER A 1 206 ? 11.452  31.057  -4.423  1.00 31.82  ? 205 SER C O   1 
ATOM   1530 C CB  . SER A 1 206 ? 10.486  28.965  -1.803  1.00 30.67  ? 205 SER C CB  1 
ATOM   1531 O OG  . SER A 1 206 ? 10.991  27.668  -2.063  1.00 29.90  ? 205 SER C OG  1 
ATOM   1532 N N   . ASP A 1 207 ? 12.137  28.916  -4.277  1.00 25.95  ? 206 ASP C N   1 
ATOM   1533 C CA  . ASP A 1 207 ? 12.403  28.772  -5.700  1.00 35.03  ? 206 ASP C CA  1 
ATOM   1534 C C   . ASP A 1 207 ? 11.216  28.120  -6.408  1.00 26.29  ? 206 ASP C C   1 
ATOM   1535 O O   . ASP A 1 207 ? 10.280  27.617  -5.783  1.00 28.73  ? 206 ASP C O   1 
ATOM   1536 C CB  . ASP A 1 207 ? 13.677  27.956  -5.926  1.00 35.48  ? 206 ASP C CB  1 
ATOM   1537 C CG  . ASP A 1 207 ? 13.507  26.502  -5.540  1.00 36.12  ? 206 ASP C CG  1 
ATOM   1538 O OD1 . ASP A 1 207 ? 13.196  26.234  -4.357  1.00 40.09  ? 206 ASP C OD1 1 
ATOM   1539 O OD2 . ASP A 1 207 ? 13.677  25.631  -6.420  1.00 37.65  ? 206 ASP C OD2 1 
ATOM   1540 N N   . ILE A 1 208 ? 11.282  28.125  -7.742  1.00 27.62  ? 207 ILE C N   1 
ATOM   1541 C CA  . ILE A 1 208 ? 10.147  27.706  -8.567  1.00 23.23  ? 207 ILE C CA  1 
ATOM   1542 C C   . ILE A 1 208 ? 9.800   26.242  -8.310  1.00 22.50  ? 207 ILE C C   1 
ATOM   1543 O O   . ILE A 1 208 ? 8.657   25.907  -7.977  1.00 23.99  ? 207 ILE C O   1 
ATOM   1544 C CB  . ILE A 1 208 ? 10.443  27.965  -10.055 1.00 26.23  ? 207 ILE C CB  1 
ATOM   1545 C CG1 . ILE A 1 208 ? 10.323  29.460  -10.362 1.00 26.06  ? 207 ILE C CG1 1 
ATOM   1546 C CG2 . ILE A 1 208 ? 9.512   27.153  -10.947 1.00 21.46  ? 207 ILE C CG2 1 
ATOM   1547 C CD1 . ILE A 1 208 ? 10.698  29.825  -11.777 1.00 28.02  ? 207 ILE C CD1 1 
ATOM   1548 N N   . ALA A 1 209 ? 10.779  25.347  -8.477  1.00 31.21  ? 208 ALA C N   1 
ATOM   1549 C CA  . ALA A 1 209 ? 10.530  23.928  -8.234  1.00 28.14  ? 208 ALA C CA  1 
ATOM   1550 C C   . ALA A 1 209 ? 10.109  23.672  -6.795  1.00 28.87  ? 208 ALA C C   1 
ATOM   1551 O O   . ALA A 1 209 ? 9.273   22.798  -6.537  1.00 26.80  ? 208 ALA C O   1 
ATOM   1552 C CB  . ALA A 1 209 ? 11.775  23.107  -8.569  1.00 27.66  ? 208 ALA C CB  1 
ATOM   1553 N N   . GLY A 1 210 ? 10.677  24.419  -5.846  1.00 26.88  ? 209 GLY C N   1 
ATOM   1554 C CA  . GLY A 1 210 ? 10.248  24.285  -4.464  1.00 22.81  ? 209 GLY C CA  1 
ATOM   1555 C C   . GLY A 1 210 ? 8.791   24.662  -4.277  1.00 27.67  ? 209 GLY C C   1 
ATOM   1556 O O   . GLY A 1 210 ? 8.017   23.914  -3.673  1.00 31.74  ? 209 GLY C O   1 
ATOM   1557 N N   . ILE A 1 211 ? 8.395   25.824  -4.806  1.00 24.98  ? 210 ILE C N   1 
ATOM   1558 C CA  . ILE A 1 211 ? 7.013   26.280  -4.665  1.00 21.51  ? 210 ILE C CA  1 
ATOM   1559 C C   . ILE A 1 211 ? 6.048   25.240  -5.214  1.00 24.39  ? 210 ILE C C   1 
ATOM   1560 O O   . ILE A 1 211 ? 5.030   24.923  -4.585  1.00 21.53  ? 210 ILE C O   1 
ATOM   1561 C CB  . ILE A 1 211 ? 6.825   27.640  -5.360  1.00 26.53  ? 210 ILE C CB  1 
ATOM   1562 C CG1 . ILE A 1 211 ? 7.517   28.748  -4.563  1.00 23.55  ? 210 ILE C CG1 1 
ATOM   1563 C CG2 . ILE A 1 211 ? 5.339   27.940  -5.545  1.00 15.71  ? 210 ILE C CG2 1 
ATOM   1564 C CD1 . ILE A 1 211 ? 7.990   29.903  -5.408  1.00 27.41  ? 210 ILE C CD1 1 
ATOM   1565 N N   . ASP A 1 212 ? 6.355   24.684  -6.388  1.00 27.27  ? 211 ASP C N   1 
ATOM   1566 C CA  . ASP A 1 212 ? 5.460   23.702  -6.991  1.00 32.18  ? 211 ASP C CA  1 
ATOM   1567 C C   . ASP A 1 212 ? 5.477   22.390  -6.213  1.00 26.18  ? 211 ASP C C   1 
ATOM   1568 O O   . ASP A 1 212 ? 4.422   21.787  -5.984  1.00 31.96  ? 211 ASP C O   1 
ATOM   1569 C CB  . ASP A 1 212 ? 5.844   23.478  -8.454  1.00 30.25  ? 211 ASP C CB  1 
ATOM   1570 C CG  . ASP A 1 212 ? 5.221   24.510  -9.391  1.00 41.88  ? 211 ASP C CG  1 
ATOM   1571 O OD1 . ASP A 1 212 ? 5.494   24.452  -10.610 1.00 32.75  ? 211 ASP C OD1 1 
ATOM   1572 O OD2 . ASP A 1 212 ? 4.451   25.373  -8.914  1.00 28.83  ? 211 ASP C OD2 1 
ATOM   1573 N N   . THR A 1 213 ? 6.664   21.937  -5.793  1.00 33.58  ? 212 THR C N   1 
ATOM   1574 C CA  . THR A 1 213 ? 6.756   20.724  -4.986  1.00 27.69  ? 212 THR C CA  1 
ATOM   1575 C C   . THR A 1 213 ? 5.971   20.867  -3.689  1.00 31.63  ? 212 THR C C   1 
ATOM   1576 O O   . THR A 1 213 ? 5.275   19.935  -3.266  1.00 30.33  ? 212 THR C O   1 
ATOM   1577 C CB  . THR A 1 213 ? 8.222   20.398  -4.689  1.00 29.10  ? 212 THR C CB  1 
ATOM   1578 O OG1 . THR A 1 213 ? 8.845   19.869  -5.867  1.00 29.09  ? 212 THR C OG1 1 
ATOM   1579 C CG2 . THR A 1 213 ? 8.337   19.380  -3.558  1.00 23.58  ? 212 THR C CG2 1 
ATOM   1580 N N   . ALA A 1 214 ? 6.054   22.038  -3.055  1.00 24.90  ? 213 ALA C N   1 
ATOM   1581 C CA  . ALA A 1 214 ? 5.345   22.250  -1.799  1.00 22.03  ? 213 ALA C CA  1 
ATOM   1582 C C   . ALA A 1 214 ? 3.837   22.138  -1.987  1.00 29.84  ? 213 ALA C C   1 
ATOM   1583 O O   . ALA A 1 214 ? 3.147   21.528  -1.161  1.00 29.36  ? 213 ALA C O   1 
ATOM   1584 C CB  . ALA A 1 214 ? 5.717   23.610  -1.211  1.00 21.41  ? 213 ALA C CB  1 
ATOM   1585 N N   . MET A 1 215 ? 3.305   22.701  -3.074  1.00 28.33  ? 214 MET C N   1 
ATOM   1586 C CA  . MET A 1 215 ? 1.858   22.659  -3.258  1.00 29.27  ? 214 MET C CA  1 
ATOM   1587 C C   . MET A 1 215 ? 1.387   21.276  -3.683  1.00 30.42  ? 214 MET C C   1 
ATOM   1588 O O   . MET A 1 215 ? 0.234   20.910  -3.427  1.00 29.56  ? 214 MET C O   1 
ATOM   1589 C CB  . MET A 1 215 ? 1.419   23.708  -4.274  1.00 24.00  ? 214 MET C CB  1 
ATOM   1590 C CG  . MET A 1 215 ? 1.555   25.142  -3.776  1.00 35.63  ? 214 MET C CG  1 
ATOM   1591 S SD  . MET A 1 215 ? 0.861   25.462  -2.140  1.00 31.53  ? 214 MET C SD  1 
ATOM   1592 C CE  . MET A 1 215 ? -0.836  24.933  -2.337  1.00 22.12  ? 214 MET C CE  1 
ATOM   1593 N N   . LYS A 1 216 ? 2.256   20.496  -4.326  1.00 26.91  ? 215 LYS C N   1 
ATOM   1594 C CA  . LYS A 1 216 ? 1.868   19.151  -4.732  1.00 30.15  ? 215 LYS C CA  1 
ATOM   1595 C C   . LYS A 1 216 ? 1.875   18.188  -3.550  1.00 36.76  ? 215 LYS C C   1 
ATOM   1596 O O   . LYS A 1 216 ? 0.936   17.402  -3.384  1.00 36.30  ? 215 LYS C O   1 
ATOM   1597 C CB  . LYS A 1 216 ? 2.789   18.657  -5.848  1.00 31.19  ? 215 LYS C CB  1 
ATOM   1598 C CG  . LYS A 1 216 ? 2.168   18.798  -7.235  1.00 37.58  ? 215 LYS C CG  1 
ATOM   1599 C CD  . LYS A 1 216 ? 3.152   18.492  -8.352  1.00 31.49  ? 215 LYS C CD  1 
ATOM   1600 C CE  . LYS A 1 216 ? 4.474   19.219  -8.153  1.00 40.35  ? 215 LYS C CE  1 
ATOM   1601 N NZ  . LYS A 1 216 ? 5.434   18.925  -9.260  1.00 49.72  ? 215 LYS C NZ  1 
ATOM   1602 N N   . LEU A 1 217 ? 2.905   18.245  -2.706  1.00 33.41  ? 216 LEU C N   1 
ATOM   1603 C CA  . LEU A 1 217 ? 2.988   17.346  -1.560  1.00 34.81  ? 216 LEU C CA  1 
ATOM   1604 C C   . LEU A 1 217 ? 2.264   17.883  -0.329  1.00 32.63  ? 216 LEU C C   1 
ATOM   1605 O O   . LEU A 1 217 ? 1.664   17.106  0.421   1.00 42.44  ? 216 LEU C O   1 
ATOM   1606 C CB  . LEU A 1 217 ? 4.451   17.069  -1.210  1.00 33.18  ? 216 LEU C CB  1 
ATOM   1607 C CG  . LEU A 1 217 ? 5.323   16.491  -2.321  1.00 30.95  ? 216 LEU C CG  1 
ATOM   1608 C CD1 . LEU A 1 217 ? 6.759   16.395  -1.837  1.00 33.00  ? 216 LEU C CD1 1 
ATOM   1609 C CD2 . LEU A 1 217 ? 4.805   15.131  -2.769  1.00 25.31  ? 216 LEU C CD2 1 
ATOM   1610 N N   . GLY A 1 218 ? 2.307   19.196  -0.098  1.00 41.54  ? 217 GLY C N   1 
ATOM   1611 C CA  . GLY A 1 218 ? 1.704   19.745  1.105   1.00 31.99  ? 217 GLY C CA  1 
ATOM   1612 C C   . GLY A 1 218 ? 0.200   19.898  1.036   1.00 33.71  ? 217 GLY C C   1 
ATOM   1613 O O   . GLY A 1 218 ? -0.485  19.746  2.053   1.00 34.31  ? 217 GLY C O   1 
ATOM   1614 N N   . ALA A 1 219 ? -0.336  20.206  -0.142  1.00 27.36  ? 218 ALA C N   1 
ATOM   1615 C CA  . ALA A 1 219 ? -1.770  20.384  -0.313  1.00 32.01  ? 218 ALA C CA  1 
ATOM   1616 C C   . ALA A 1 219 ? -2.404  19.296  -1.164  1.00 32.52  ? 218 ALA C C   1 
ATOM   1617 O O   . ALA A 1 219 ? -3.616  19.346  -1.401  1.00 41.43  ? 218 ALA C O   1 
ATOM   1618 C CB  . ALA A 1 219 ? -2.066  21.758  -0.926  1.00 35.43  ? 218 ALA C CB  1 
ATOM   1619 N N   . ASN A 1 220 ? -1.619  18.321  -1.629  1.00 34.39  ? 219 ASN C N   1 
ATOM   1620 C CA  . ASN A 1 220 ? -2.123  17.221  -2.454  1.00 40.05  ? 219 ASN C CA  1 
ATOM   1621 C C   . ASN A 1 220 ? -2.779  17.742  -3.734  1.00 43.72  ? 219 ASN C C   1 
ATOM   1622 O O   . ASN A 1 220 ? -3.793  17.215  -4.197  1.00 44.44  ? 219 ASN C O   1 
ATOM   1623 C CB  . ASN A 1 220 ? -3.087  16.332  -1.662  1.00 43.57  ? 219 ASN C CB  1 
ATOM   1624 C CG  . ASN A 1 220 ? -3.295  14.980  -2.306  1.00 46.38  ? 219 ASN C CG  1 
ATOM   1625 O OD1 . ASN A 1 220 ? -2.457  14.513  -3.077  1.00 56.44  ? 219 ASN C OD1 1 
ATOM   1626 N ND2 . ASN A 1 220 ? -4.416  14.340  -1.992  1.00 45.24  ? 219 ASN C ND2 1 
ATOM   1627 N N   . HIS A 1 221 ? -2.190  18.807  -4.314  1.00 40.12  ? 220 HIS C N   1 
ATOM   1628 C CA  . HIS A 1 221 ? -2.700  19.319  -5.576  1.00 35.07  ? 220 HIS C CA  1 
ATOM   1629 C C   . HIS A 1 221 ? -2.076  18.562  -6.745  1.00 35.34  ? 220 HIS C C   1 
ATOM   1630 O O   . HIS A 1 221 ? -0.936  18.095  -6.653  1.00 30.21  ? 220 HIS C O   1 
ATOM   1631 C CB  . HIS A 1 221 ? -2.400  20.810  -5.707  1.00 31.59  ? 220 HIS C CB  1 
ATOM   1632 C CG  . HIS A 1 221 ? -3.284  21.678  -4.866  1.00 37.77  ? 220 HIS C CG  1 
ATOM   1633 N ND1 . HIS A 1 221 ? -2.984  22.993  -4.581  1.00 41.71  ? 220 HIS C ND1 1 
ATOM   1634 C CD2 . HIS A 1 221 ? -4.459  21.417  -4.245  1.00 37.73  ? 220 HIS C CD2 1 
ATOM   1635 C CE1 . HIS A 1 221 ? -3.938  23.505  -3.823  1.00 48.05  ? 220 HIS C CE1 1 
ATOM   1636 N NE2 . HIS A 1 221 ? -4.845  22.569  -3.605  1.00 45.56  ? 220 HIS C NE2 1 
ATOM   1637 N N   . PRO A 1 222 ? -2.805  18.414  -7.858  1.00 39.34  ? 221 PRO C N   1 
ATOM   1638 C CA  . PRO A 1 222 ? -2.240  17.656  -8.988  1.00 34.08  ? 221 PRO C CA  1 
ATOM   1639 C C   . PRO A 1 222 ? -1.071  18.359  -9.652  1.00 36.07  ? 221 PRO C C   1 
ATOM   1640 O O   . PRO A 1 222 ? -0.104  17.699  -10.052 1.00 31.95  ? 221 PRO C O   1 
ATOM   1641 C CB  . PRO A 1 222 ? -3.434  17.504  -9.940  1.00 37.00  ? 221 PRO C CB  1 
ATOM   1642 C CG  . PRO A 1 222 ? -4.338  18.646  -9.604  1.00 36.36  ? 221 PRO C CG  1 
ATOM   1643 C CD  . PRO A 1 222 ? -4.171  18.895  -8.131  1.00 40.63  ? 221 PRO C CD  1 
ATOM   1644 N N   . MET A 1 223 ? -1.131  19.682  -9.780  1.00 36.66  ? 222 MET C N   1 
ATOM   1645 C CA  . MET A 1 223 ? -0.044  20.468  -10.338 1.00 33.47  ? 222 MET C CA  1 
ATOM   1646 C C   . MET A 1 223 ? 0.333   21.575  -9.365  1.00 34.01  ? 222 MET C C   1 
ATOM   1647 O O   . MET A 1 223 ? -0.501  22.059  -8.594  1.00 34.93  ? 222 MET C O   1 
ATOM   1648 C CB  . MET A 1 223 ? -0.426  21.085  -11.693 1.00 32.83  ? 222 MET C CB  1 
ATOM   1649 C CG  . MET A 1 223 ? -0.522  20.088  -12.829 1.00 40.44  ? 222 MET C CG  1 
ATOM   1650 S SD  . MET A 1 223 ? -0.971  20.872  -14.390 1.00 47.27  ? 222 MET C SD  1 
ATOM   1651 C CE  . MET A 1 223 ? 0.529   21.778  -14.755 1.00 34.86  ? 222 MET C CE  1 
ATOM   1652 N N   . GLY A 1 224 ? 1.602   21.970  -9.408  1.00 26.68  ? 223 GLY C N   1 
ATOM   1653 C CA  . GLY A 1 224 ? 2.038   23.170  -8.741  1.00 30.97  ? 223 GLY C CA  1 
ATOM   1654 C C   . GLY A 1 224 ? 1.404   24.391  -9.378  1.00 34.04  ? 223 GLY C C   1 
ATOM   1655 O O   . GLY A 1 224 ? 1.008   24.373  -10.548 1.00 27.30  ? 223 GLY C O   1 
ATOM   1656 N N   . PRO A 1 225 ? 1.287   25.479  -8.614  1.00 36.54  ? 224 PRO C N   1 
ATOM   1657 C CA  . PRO A 1 225 ? 0.637   26.682  -9.160  1.00 28.70  ? 224 PRO C CA  1 
ATOM   1658 C C   . PRO A 1 225 ? 1.413   27.322  -10.300 1.00 30.79  ? 224 PRO C C   1 
ATOM   1659 O O   . PRO A 1 225 ? 0.794   27.890  -11.209 1.00 24.74  ? 224 PRO C O   1 
ATOM   1660 C CB  . PRO A 1 225 ? 0.544   27.614  -7.944  1.00 24.79  ? 224 PRO C CB  1 
ATOM   1661 C CG  . PRO A 1 225 ? 1.616   27.141  -7.016  1.00 30.37  ? 224 PRO C CG  1 
ATOM   1662 C CD  . PRO A 1 225 ? 1.759   25.668  -7.232  1.00 29.18  ? 224 PRO C CD  1 
ATOM   1663 N N   . LEU A 1 226 ? 2.745   27.250  -10.282 1.00 23.78  ? 225 LEU C N   1 
ATOM   1664 C CA  . LEU A 1 226 ? 3.531   27.838  -11.360 1.00 28.45  ? 225 LEU C CA  1 
ATOM   1665 C C   . LEU A 1 226 ? 3.525   26.945  -12.598 1.00 32.13  ? 225 LEU C C   1 
ATOM   1666 O O   . LEU A 1 226 ? 3.377   27.440  -13.722 1.00 25.98  ? 225 LEU C O   1 
ATOM   1667 C CB  . LEU A 1 226 ? 4.956   28.113  -10.870 1.00 25.32  ? 225 LEU C CB  1 
ATOM   1668 C CG  . LEU A 1 226 ? 5.041   29.085  -9.682  1.00 30.73  ? 225 LEU C CG  1 
ATOM   1669 C CD1 . LEU A 1 226 ? 6.459   29.217  -9.127  1.00 21.52  ? 225 LEU C CD1 1 
ATOM   1670 C CD2 . LEU A 1 226 ? 4.488   30.458  -10.060 1.00 21.94  ? 225 LEU C CD2 1 
ATOM   1671 N N   . GLU A 1 227 ? 3.685   25.631  -12.408 1.00 37.16  ? 226 GLU C N   1 
ATOM   1672 C CA  . GLU A 1 227 ? 3.410   24.668  -13.474 1.00 34.62  ? 226 GLU C CA  1 
ATOM   1673 C C   . GLU A 1 227 ? 2.051   24.939  -14.106 1.00 33.53  ? 226 GLU C C   1 
ATOM   1674 O O   . GLU A 1 227 ? 1.914   24.977  -15.334 1.00 31.78  ? 226 GLU C O   1 
ATOM   1675 C CB  . GLU A 1 227 ? 3.445   23.247  -12.905 1.00 37.34  ? 226 GLU C CB  1 
ATOM   1676 C CG  . GLU A 1 227 ? 4.653   22.400  -13.271 1.00 53.73  ? 226 GLU C CG  1 
ATOM   1677 C CD  . GLU A 1 227 ? 4.611   21.036  -12.589 1.00 55.66  ? 226 GLU C CD  1 
ATOM   1678 O OE1 . GLU A 1 227 ? 4.113   20.970  -11.443 1.00 43.69  ? 226 GLU C OE1 1 
ATOM   1679 O OE2 . GLU A 1 227 ? 5.064   20.035  -13.189 1.00 50.03  ? 226 GLU C OE2 1 
ATOM   1680 N N   . LEU A 1 228 ? 1.034   25.139  -13.265 1.00 24.73  ? 227 LEU C N   1 
ATOM   1681 C CA  . LEU A 1 228 ? -0.325  25.354  -13.751 1.00 34.63  ? 227 LEU C CA  1 
ATOM   1682 C C   . LEU A 1 228 ? -0.439  26.658  -14.530 1.00 29.04  ? 227 LEU C C   1 
ATOM   1683 O O   . LEU A 1 228 ? -1.156  26.723  -15.535 1.00 28.74  ? 227 LEU C O   1 
ATOM   1684 C CB  . LEU A 1 228 ? -1.299  25.340  -12.573 1.00 23.43  ? 227 LEU C CB  1 
ATOM   1685 C CG  . LEU A 1 228 ? -2.778  25.587  -12.863 1.00 30.89  ? 227 LEU C CG  1 
ATOM   1686 C CD1 . LEU A 1 228 ? -3.319  24.527  -13.807 1.00 25.73  ? 227 LEU C CD1 1 
ATOM   1687 C CD2 . LEU A 1 228 ? -3.568  25.607  -11.568 1.00 27.06  ? 227 LEU C CD2 1 
ATOM   1688 N N   . GLY A 1 229 ? 0.253   27.707  -14.082 1.00 25.55  ? 228 GLY C N   1 
ATOM   1689 C CA  . GLY A 1 229 ? 0.211   28.966  -14.807 1.00 22.17  ? 228 GLY C CA  1 
ATOM   1690 C C   . GLY A 1 229 ? 0.808   28.851  -16.196 1.00 27.55  ? 228 GLY C C   1 
ATOM   1691 O O   . GLY A 1 229 ? 0.298   29.439  -17.154 1.00 25.06  ? 228 GLY C O   1 
ATOM   1692 N N   . ASP A 1 230 ? 1.900   28.095  -16.323 1.00 24.22  ? 229 ASP C N   1 
ATOM   1693 C CA  . ASP A 1 230 ? 2.480   27.839  -17.637 1.00 28.02  ? 229 ASP C CA  1 
ATOM   1694 C C   . ASP A 1 230 ? 1.514   27.058  -18.516 1.00 33.28  ? 229 ASP C C   1 
ATOM   1695 O O   . ASP A 1 230 ? 1.356   27.361  -19.705 1.00 32.62  ? 229 ASP C O   1 
ATOM   1696 C CB  . ASP A 1 230 ? 3.790   27.069  -17.486 1.00 29.37  ? 229 ASP C CB  1 
ATOM   1697 C CG  . ASP A 1 230 ? 4.967   27.962  -17.143 1.00 33.94  ? 229 ASP C CG  1 
ATOM   1698 O OD1 . ASP A 1 230 ? 4.765   29.175  -16.921 1.00 35.14  ? 229 ASP C OD1 1 
ATOM   1699 O OD2 . ASP A 1 230 ? 6.102   27.439  -17.090 1.00 29.71  ? 229 ASP C OD2 1 
ATOM   1700 N N   . PHE A 1 231 ? 0.859   26.046  -17.943 1.00 33.75  ? 230 PHE C N   1 
ATOM   1701 C CA  . PHE A 1 231 ? -0.056  25.209  -18.709 1.00 31.61  ? 230 PHE C CA  1 
ATOM   1702 C C   . PHE A 1 231 ? -1.282  25.999  -19.150 1.00 30.34  ? 230 PHE C C   1 
ATOM   1703 O O   . PHE A 1 231 ? -1.684  25.940  -20.317 1.00 30.94  ? 230 PHE C O   1 
ATOM   1704 C CB  . PHE A 1 231 ? -0.455  23.991  -17.873 1.00 31.51  ? 230 PHE C CB  1 
ATOM   1705 C CG  . PHE A 1 231 ? -1.474  23.100  -18.528 1.00 37.70  ? 230 PHE C CG  1 
ATOM   1706 C CD1 . PHE A 1 231 ? -1.103  22.228  -19.540 1.00 41.69  ? 230 PHE C CD1 1 
ATOM   1707 C CD2 . PHE A 1 231 ? -2.798  23.115  -18.115 1.00 43.89  ? 230 PHE C CD2 1 
ATOM   1708 C CE1 . PHE A 1 231 ? -2.038  21.396  -20.137 1.00 38.35  ? 230 PHE C CE1 1 
ATOM   1709 C CE2 . PHE A 1 231 ? -3.737  22.289  -18.708 1.00 43.12  ? 230 PHE C CE2 1 
ATOM   1710 C CZ  . PHE A 1 231 ? -3.355  21.427  -19.720 1.00 33.41  ? 230 PHE C CZ  1 
ATOM   1711 N N   . ILE A 1 232 ? -1.890  26.746  -18.226 1.00 24.88  ? 231 ILE C N   1 
ATOM   1712 C CA  . ILE A 1 232 ? -3.048  27.567  -18.568 1.00 25.54  ? 231 ILE C CA  1 
ATOM   1713 C C   . ILE A 1 232 ? -2.660  28.653  -19.564 1.00 30.91  ? 231 ILE C C   1 
ATOM   1714 O O   . ILE A 1 232 ? -3.429  28.983  -20.476 1.00 32.91  ? 231 ILE C O   1 
ATOM   1715 C CB  . ILE A 1 232 ? -3.666  28.173  -17.295 1.00 34.33  ? 231 ILE C CB  1 
ATOM   1716 C CG1 . ILE A 1 232 ? -4.322  27.088  -16.438 1.00 32.29  ? 231 ILE C CG1 1 
ATOM   1717 C CG2 . ILE A 1 232 ? -4.672  29.261  -17.645 1.00 19.85  ? 231 ILE C CG2 1 
ATOM   1718 C CD1 . ILE A 1 232 ? -4.859  27.606  -15.119 1.00 22.25  ? 231 ILE C CD1 1 
ATOM   1719 N N   . GLY A 1 233 ? -1.464  29.216  -19.414 1.00 31.95  ? 232 GLY C N   1 
ATOM   1720 C CA  . GLY A 1 233 ? -1.047  30.344  -20.220 1.00 28.20  ? 232 GLY C CA  1 
ATOM   1721 C C   . GLY A 1 233 ? -0.923  31.595  -19.377 1.00 24.93  ? 232 GLY C C   1 
ATOM   1722 O O   . GLY A 1 233 ? -1.918  32.086  -18.836 1.00 27.84  ? 232 GLY C O   1 
ATOM   1723 N N   . LEU A 1 234 ? 0.298   32.118  -19.246 1.00 24.41  ? 233 LEU C N   1 
ATOM   1724 C CA  . LEU A 1 234 ? 0.507   33.259  -18.361 1.00 25.21  ? 233 LEU C CA  1 
ATOM   1725 C C   . LEU A 1 234 ? -0.203  34.507  -18.868 1.00 26.47  ? 233 LEU C C   1 
ATOM   1726 O O   . LEU A 1 234 ? -0.632  35.342  -18.063 1.00 24.78  ? 233 LEU C O   1 
ATOM   1727 C CB  . LEU A 1 234 ? 2.003   33.517  -18.181 1.00 24.94  ? 233 LEU C CB  1 
ATOM   1728 C CG  . LEU A 1 234 ? 2.725   32.378  -17.454 1.00 29.89  ? 233 LEU C CG  1 
ATOM   1729 C CD1 . LEU A 1 234 ? 4.191   32.695  -17.237 1.00 26.99  ? 233 LEU C CD1 1 
ATOM   1730 C CD2 . LEU A 1 234 ? 2.035   32.086  -16.133 1.00 21.56  ? 233 LEU C CD2 1 
ATOM   1731 N N   . ASP A 1 235 ? -0.350  34.646  -20.186 1.00 27.03  ? 234 ASP C N   1 
ATOM   1732 C CA  . ASP A 1 235 ? -1.121  35.762  -20.723 1.00 27.64  ? 234 ASP C CA  1 
ATOM   1733 C C   . ASP A 1 235 ? -2.571  35.696  -20.261 1.00 27.44  ? 234 ASP C C   1 
ATOM   1734 O O   . ASP A 1 235 ? -3.194  36.730  -19.986 1.00 28.60  ? 234 ASP C O   1 
ATOM   1735 C CB  . ASP A 1 235 ? -1.035  35.762  -22.247 1.00 28.73  ? 234 ASP C CB  1 
ATOM   1736 C CG  . ASP A 1 235 ? -1.440  34.433  -22.849 1.00 41.23  ? 234 ASP C CG  1 
ATOM   1737 O OD1 . ASP A 1 235 ? -1.072  33.384  -22.272 1.00 35.00  ? 234 ASP C OD1 1 
ATOM   1738 O OD2 . ASP A 1 235 ? -2.105  34.440  -23.907 1.00 39.09  ? 234 ASP C OD2 1 
ATOM   1739 N N   . ILE A 1 236 ? -3.121  34.484  -20.158 1.00 24.62  ? 235 ILE C N   1 
ATOM   1740 C CA  . ILE A 1 236 ? -4.493  34.326  -19.688 1.00 23.20  ? 235 ILE C CA  1 
ATOM   1741 C C   . ILE A 1 236 ? -4.583  34.600  -18.191 1.00 25.34  ? 235 ILE C C   1 
ATOM   1742 O O   . ILE A 1 236 ? -5.531  35.241  -17.723 1.00 24.52  ? 235 ILE C O   1 
ATOM   1743 C CB  . ILE A 1 236 ? -5.018  32.923  -20.042 1.00 30.83  ? 235 ILE C CB  1 
ATOM   1744 C CG1 . ILE A 1 236 ? -4.916  32.689  -21.553 1.00 31.72  ? 235 ILE C CG1 1 
ATOM   1745 C CG2 . ILE A 1 236 ? -6.444  32.742  -19.535 1.00 18.30  ? 235 ILE C CG2 1 
ATOM   1746 C CD1 . ILE A 1 236 ? -5.928  31.701  -22.093 1.00 44.92  ? 235 ILE C CD1 1 
ATOM   1747 N N   . CYS A 1 237 ? -3.608  34.117  -17.416 1.00 22.51  ? 236 CYS C N   1 
ATOM   1748 C CA  . CYS A 1 237 ? -3.601  34.403  -15.984 1.00 24.05  ? 236 CYS C CA  1 
ATOM   1749 C C   . CYS A 1 237 ? -3.503  35.900  -15.726 1.00 29.20  ? 236 CYS C C   1 
ATOM   1750 O O   . CYS A 1 237 ? -4.178  36.430  -14.834 1.00 26.02  ? 236 CYS C O   1 
ATOM   1751 C CB  . CYS A 1 237 ? -2.445  33.673  -15.300 1.00 20.81  ? 236 CYS C CB  1 
ATOM   1752 S SG  . CYS A 1 237 ? -2.518  31.869  -15.399 1.00 28.45  ? 236 CYS C SG  1 
ATOM   1753 N N   . LEU A 1 238 ? -2.664  36.598  -16.495 1.00 27.69  ? 237 LEU C N   1 
ATOM   1754 C CA  . LEU A 1 238 ? -2.532  38.041  -16.326 1.00 25.09  ? 237 LEU C CA  1 
ATOM   1755 C C   . LEU A 1 238 ? -3.842  38.751  -16.634 1.00 27.38  ? 237 LEU C C   1 
ATOM   1756 O O   . LEU A 1 238 ? -4.227  39.694  -15.930 1.00 29.48  ? 237 LEU C O   1 
ATOM   1757 C CB  . LEU A 1 238 ? -1.414  38.573  -17.220 1.00 20.42  ? 237 LEU C CB  1 
ATOM   1758 C CG  . LEU A 1 238 ? -1.087  40.057  -17.056 1.00 25.22  ? 237 LEU C CG  1 
ATOM   1759 C CD1 . LEU A 1 238 ? -0.746  40.359  -15.607 1.00 23.34  ? 237 LEU C CD1 1 
ATOM   1760 C CD2 . LEU A 1 238 ? 0.058   40.459  -17.972 1.00 20.38  ? 237 LEU C CD2 1 
ATOM   1761 N N   . ALA A 1 239 ? -4.543  38.309  -17.681 1.00 21.06  ? 238 ALA C N   1 
ATOM   1762 C CA  . ALA A 1 239 ? -5.806  38.941  -18.047 1.00 21.04  ? 238 ALA C CA  1 
ATOM   1763 C C   . ALA A 1 239 ? -6.875  38.702  -16.989 1.00 20.84  ? 238 ALA C C   1 
ATOM   1764 O O   . ALA A 1 239 ? -7.675  39.599  -16.692 1.00 23.55  ? 238 ALA C O   1 
ATOM   1765 C CB  . ALA A 1 239 ? -6.273  38.427  -19.407 1.00 18.15  ? 238 ALA C CB  1 
ATOM   1766 N N   . ILE A 1 240 ? -6.912  37.496  -16.413 1.00 23.50  ? 239 ILE C N   1 
ATOM   1767 C CA  . ILE A 1 240 ? -7.881  37.220  -15.356 1.00 23.70  ? 239 ILE C CA  1 
ATOM   1768 C C   . ILE A 1 240 ? -7.579  38.071  -14.132 1.00 29.83  ? 239 ILE C C   1 
ATOM   1769 O O   . ILE A 1 240 ? -8.484  38.674  -13.540 1.00 26.94  ? 239 ILE C O   1 
ATOM   1770 C CB  . ILE A 1 240 ? -7.898  35.721  -15.005 1.00 28.92  ? 239 ILE C CB  1 
ATOM   1771 C CG1 . ILE A 1 240 ? -8.239  34.873  -16.232 1.00 27.52  ? 239 ILE C CG1 1 
ATOM   1772 C CG2 . ILE A 1 240 ? -8.904  35.457  -13.903 1.00 20.96  ? 239 ILE C CG2 1 
ATOM   1773 C CD1 . ILE A 1 240 ? -9.707  34.874  -16.587 1.00 37.31  ? 239 ILE C CD1 1 
ATOM   1774 N N   . MET A 1 241 ? -6.302  38.135  -13.735 1.00 21.23  ? 240 MET C N   1 
ATOM   1775 C CA  . MET A 1 241 ? -5.923  38.962  -12.595 1.00 24.07  ? 240 MET C CA  1 
ATOM   1776 C C   . MET A 1 241 ? -6.333  40.412  -12.816 1.00 26.47  ? 240 MET C C   1 
ATOM   1777 O O   . MET A 1 241 ? -6.881  41.056  -11.914 1.00 20.63  ? 240 MET C O   1 
ATOM   1778 C CB  . MET A 1 241 ? -4.417  38.863  -12.344 1.00 25.72  ? 240 MET C CB  1 
ATOM   1779 C CG  . MET A 1 241 ? -3.957  37.669  -11.498 1.00 18.66  ? 240 MET C CG  1 
ATOM   1780 S SD  . MET A 1 241 ? -5.199  37.040  -10.354 1.00 28.13  ? 240 MET C SD  1 
ATOM   1781 C CE  . MET A 1 241 ? -4.805  37.997  -8.885  1.00 16.14  ? 240 MET C CE  1 
ATOM   1782 N N   . ASP A 1 242 ? -6.103  40.935  -14.023 1.00 24.89  ? 241 ASP C N   1 
ATOM   1783 C CA  . ASP A 1 242 ? -6.439  42.326  -14.302 1.00 27.05  ? 241 ASP C CA  1 
ATOM   1784 C C   . ASP A 1 242 ? -7.947  42.544  -14.335 1.00 21.09  ? 241 ASP C C   1 
ATOM   1785 O O   . ASP A 1 242 ? -8.427  43.598  -13.902 1.00 26.05  ? 241 ASP C O   1 
ATOM   1786 C CB  . ASP A 1 242 ? -5.800  42.765  -15.622 1.00 23.75  ? 241 ASP C CB  1 
ATOM   1787 C CG  . ASP A 1 242 ? -4.323  43.109  -15.471 1.00 31.23  ? 241 ASP C CG  1 
ATOM   1788 O OD1 . ASP A 1 242 ? -3.893  43.436  -14.342 1.00 28.15  ? 241 ASP C OD1 1 
ATOM   1789 O OD2 . ASP A 1 242 ? -3.594  43.057  -16.484 1.00 32.34  ? 241 ASP C OD2 1 
ATOM   1790 N N   . VAL A 1 243 ? -8.706  41.564  -14.828 1.00 20.52  ? 242 VAL C N   1 
ATOM   1791 C CA  . VAL A 1 243 ? -10.162 41.687  -14.838 1.00 20.03  ? 242 VAL C CA  1 
ATOM   1792 C C   . VAL A 1 243 ? -10.711 41.686  -13.416 1.00 27.30  ? 242 VAL C C   1 
ATOM   1793 O O   . VAL A 1 243 ? -11.566 42.512  -13.066 1.00 22.52  ? 242 VAL C O   1 
ATOM   1794 C CB  . VAL A 1 243 ? -10.787 40.567  -15.692 1.00 20.58  ? 242 VAL C CB  1 
ATOM   1795 C CG1 . VAL A 1 243 ? -12.239 40.322  -15.290 1.00 21.29  ? 242 VAL C CG1 1 
ATOM   1796 C CG2 . VAL A 1 243 ? -10.689 40.918  -17.175 1.00 21.00  ? 242 VAL C CG2 1 
ATOM   1797 N N   . LEU A 1 244 ? -10.235 40.760  -12.576 1.00 25.00  ? 243 LEU C N   1 
ATOM   1798 C CA  . LEU A 1 244 ? -10.627 40.766  -11.169 1.00 23.11  ? 243 LEU C CA  1 
ATOM   1799 C C   . LEU A 1 244 ? -10.324 42.114  -10.524 1.00 25.44  ? 243 LEU C C   1 
ATOM   1800 O O   . LEU A 1 244 ? -11.161 42.669  -9.801  1.00 29.91  ? 243 LEU C O   1 
ATOM   1801 C CB  . LEU A 1 244 ? -9.911  39.639  -10.419 1.00 19.21  ? 243 LEU C CB  1 
ATOM   1802 C CG  . LEU A 1 244 ? -10.370 38.192  -10.666 1.00 28.42  ? 243 LEU C CG  1 
ATOM   1803 C CD1 . LEU A 1 244 ? -9.333  37.195  -10.157 1.00 18.78  ? 243 LEU C CD1 1 
ATOM   1804 C CD2 . LEU A 1 244 ? -11.725 37.915  -10.036 1.00 23.66  ? 243 LEU C CD2 1 
ATOM   1805 N N   . TYR A 1 245 ? -9.141  42.669  -10.803 1.00 21.98  ? 244 TYR C N   1 
ATOM   1806 C CA  . TYR A 1 245 ? -8.745  43.943  -10.209 1.00 22.65  ? 244 TYR C CA  1 
ATOM   1807 C C   . TYR A 1 245 ? -9.641  45.085  -10.687 1.00 30.65  ? 244 TYR C C   1 
ATOM   1808 O O   . TYR A 1 245 ? -10.111 45.892  -9.875  1.00 29.79  ? 244 TYR C O   1 
ATOM   1809 C CB  . TYR A 1 245 ? -7.272  44.222  -10.532 1.00 30.14  ? 244 TYR C CB  1 
ATOM   1810 C CG  . TYR A 1 245 ? -6.738  45.548  -10.031 1.00 30.35  ? 244 TYR C CG  1 
ATOM   1811 C CD1 . TYR A 1 245 ? -6.848  45.907  -8.697  1.00 26.52  ? 244 TYR C CD1 1 
ATOM   1812 C CD2 . TYR A 1 245 ? -6.113  46.438  -10.898 1.00 34.82  ? 244 TYR C CD2 1 
ATOM   1813 C CE1 . TYR A 1 245 ? -6.359  47.120  -8.238  1.00 28.45  ? 244 TYR C CE1 1 
ATOM   1814 C CE2 . TYR A 1 245 ? -5.620  47.651  -10.449 1.00 34.92  ? 244 TYR C CE2 1 
ATOM   1815 C CZ  . TYR A 1 245 ? -5.748  47.986  -9.116  1.00 22.76  ? 244 TYR C CZ  1 
ATOM   1816 O OH  . TYR A 1 245 ? -5.263  49.192  -8.665  1.00 31.27  ? 244 TYR C OH  1 
ATOM   1817 N N   . HIS A 1 246 ? -9.909  45.161  -11.994 1.00 21.46  ? 245 HIS C N   1 
ATOM   1818 C CA  . HIS A 1 246 ? -10.668 46.295  -12.516 1.00 24.41  ? 245 HIS C CA  1 
ATOM   1819 C C   . HIS A 1 246 ? -12.149 46.207  -12.156 1.00 24.97  ? 245 HIS C C   1 
ATOM   1820 O O   . HIS A 1 246 ? -12.782 47.239  -11.901 1.00 25.59  ? 245 HIS C O   1 
ATOM   1821 C CB  . HIS A 1 246 ? -10.479 46.396  -14.030 1.00 25.00  ? 245 HIS C CB  1 
ATOM   1822 C CG  . HIS A 1 246 ? -9.081  46.753  -14.434 1.00 32.58  ? 245 HIS C CG  1 
ATOM   1823 N ND1 . HIS A 1 246 ? -8.466  46.218  -15.546 1.00 38.35  ? 245 HIS C ND1 1 
ATOM   1824 C CD2 . HIS A 1 246 ? -8.174  47.582  -13.865 1.00 27.38  ? 245 HIS C CD2 1 
ATOM   1825 C CE1 . HIS A 1 246 ? -7.242  46.707  -15.648 1.00 37.00  ? 245 HIS C CE1 1 
ATOM   1826 N NE2 . HIS A 1 246 ? -7.040  47.538  -14.641 1.00 37.35  ? 245 HIS C NE2 1 
ATOM   1827 N N   . GLU A 1 247 ? -12.713 44.998  -12.114 1.00 24.12  ? 246 GLU C N   1 
ATOM   1828 C CA  . GLU A 1 247 ? -14.125 44.854  -11.766 1.00 23.77  ? 246 GLU C CA  1 
ATOM   1829 C C   . GLU A 1 247 ? -14.381 45.227  -10.311 1.00 28.68  ? 246 GLU C C   1 
ATOM   1830 O O   . GLU A 1 247 ? -15.331 45.960  -10.012 1.00 32.18  ? 246 GLU C O   1 
ATOM   1831 C CB  . GLU A 1 247 ? -14.589 43.424  -12.038 1.00 31.01  ? 246 GLU C CB  1 
ATOM   1832 C CG  . GLU A 1 247 ? -14.692 43.070  -13.512 1.00 32.03  ? 246 GLU C CG  1 
ATOM   1833 C CD  . GLU A 1 247 ? -15.882 43.723  -14.176 1.00 34.48  ? 246 GLU C CD  1 
ATOM   1834 O OE1 . GLU A 1 247 ? -16.997 43.628  -13.617 1.00 37.65  ? 246 GLU C OE1 1 
ATOM   1835 O OE2 . GLU A 1 247 ? -15.702 44.329  -15.254 1.00 36.65  ? 246 GLU C OE2 1 
ATOM   1836 N N   . THR A 1 248 ? -13.547 44.734  -9.391  1.00 25.48  ? 247 THR C N   1 
ATOM   1837 C CA  . THR A 1 248 ? -13.727 45.014  -7.971  1.00 23.04  ? 247 THR C CA  1 
ATOM   1838 C C   . THR A 1 248 ? -13.103 46.331  -7.536  1.00 27.17  ? 247 THR C C   1 
ATOM   1839 O O   . THR A 1 248 ? -13.582 46.945  -6.576  1.00 28.20  ? 247 THR C O   1 
ATOM   1840 C CB  . THR A 1 248 ? -13.124 43.895  -7.114  1.00 27.34  ? 247 THR C CB  1 
ATOM   1841 O OG1 . THR A 1 248 ? -11.700 43.899  -7.260  1.00 24.95  ? 247 THR C OG1 1 
ATOM   1842 C CG2 . THR A 1 248 ? -13.659 42.542  -7.539  1.00 28.37  ? 247 THR C CG2 1 
ATOM   1843 N N   . GLY A 1 249 ? -12.044 46.778  -8.206  1.00 31.11  ? 248 GLY C N   1 
ATOM   1844 C CA  . GLY A 1 249 ? -11.298 47.912  -7.702  1.00 25.06  ? 248 GLY C CA  1 
ATOM   1845 C C   . GLY A 1 249 ? -10.500 47.608  -6.457  1.00 26.18  ? 248 GLY C C   1 
ATOM   1846 O O   . GLY A 1 249 ? -10.056 48.532  -5.773  1.00 29.05  ? 248 GLY C O   1 
ATOM   1847 N N   . ASP A 1 250 ? -10.290 46.328  -6.159  1.00 33.35  ? 249 ASP C N   1 
ATOM   1848 C CA  . ASP A 1 250 ? -9.670  45.879  -4.919  1.00 30.67  ? 249 ASP C CA  1 
ATOM   1849 C C   . ASP A 1 250 ? -8.211  45.523  -5.176  1.00 24.80  ? 249 ASP C C   1 
ATOM   1850 O O   . ASP A 1 250 ? -7.923  44.602  -5.947  1.00 28.55  ? 249 ASP C O   1 
ATOM   1851 C CB  . ASP A 1 250 ? -10.425 44.670  -4.364  1.00 35.50  ? 249 ASP C CB  1 
ATOM   1852 C CG  . ASP A 1 250 ? -10.105 44.392  -2.906  1.00 42.08  ? 249 ASP C CG  1 
ATOM   1853 O OD1 . ASP A 1 250 ? -9.130  44.972  -2.382  1.00 41.97  ? 249 ASP C OD1 1 
ATOM   1854 O OD2 . ASP A 1 250 ? -10.825 43.576  -2.289  1.00 35.79  ? 249 ASP C OD2 1 
ATOM   1855 N N   . SER A 1 251 ? -7.296  46.234  -4.510  1.00 32.13  ? 250 SER C N   1 
ATOM   1856 C CA  . SER A 1 251 ? -5.868  45.948  -4.627  1.00 31.52  ? 250 SER C CA  1 
ATOM   1857 C C   . SER A 1 251 ? -5.523  44.514  -4.250  1.00 29.91  ? 250 SER C C   1 
ATOM   1858 O O   . SER A 1 251 ? -4.404  44.071  -4.534  1.00 23.98  ? 250 SER C O   1 
ATOM   1859 C CB  . SER A 1 251 ? -5.063  46.910  -3.748  1.00 31.47  ? 250 SER C CB  1 
ATOM   1860 O OG  . SER A 1 251 ? -4.768  48.111  -4.439  1.00 40.30  ? 250 SER C OG  1 
ATOM   1861 N N   . LYS A 1 252 ? -6.447  43.792  -3.611  1.00 28.04  ? 251 LYS C N   1 
ATOM   1862 C CA  . LYS A 1 252 ? -6.217  42.394  -3.266  1.00 26.34  ? 251 LYS C CA  1 
ATOM   1863 C C   . LYS A 1 252 ? -5.887  41.556  -4.496  1.00 22.81  ? 251 LYS C C   1 
ATOM   1864 O O   . LYS A 1 252 ? -5.087  40.618  -4.409  1.00 21.15  ? 251 LYS C O   1 
ATOM   1865 C CB  . LYS A 1 252 ? -7.449  41.850  -2.538  1.00 30.66  ? 251 LYS C CB  1 
ATOM   1866 C CG  . LYS A 1 252 ? -7.613  40.342  -2.530  1.00 26.41  ? 251 LYS C CG  1 
ATOM   1867 C CD  . LYS A 1 252 ? -8.929  39.969  -1.859  1.00 29.56  ? 251 LYS C CD  1 
ATOM   1868 C CE  . LYS A 1 252 ? -8.919  38.531  -1.370  1.00 30.75  ? 251 LYS C CE  1 
ATOM   1869 N NZ  . LYS A 1 252 ? -10.291 38.038  -1.053  1.00 33.77  ? 251 LYS C NZ  1 
ATOM   1870 N N   . TYR A 1 253 ? -6.462  41.895  -5.652  1.00 24.23  ? 252 TYR C N   1 
ATOM   1871 C CA  . TYR A 1 253 ? -6.274  41.130  -6.877  1.00 25.40  ? 252 TYR C CA  1 
ATOM   1872 C C   . TYR A 1 253 ? -5.239  41.751  -7.806  1.00 23.45  ? 252 TYR C C   1 
ATOM   1873 O O   . TYR A 1 253 ? -5.241  41.455  -9.005  1.00 24.94  ? 252 TYR C O   1 
ATOM   1874 C CB  . TYR A 1 253 ? -7.604  40.973  -7.617  1.00 23.24  ? 252 TYR C CB  1 
ATOM   1875 C CG  . TYR A 1 253 ? -8.709  40.412  -6.760  1.00 20.98  ? 252 TYR C CG  1 
ATOM   1876 C CD1 . TYR A 1 253 ? -8.721  39.070  -6.408  1.00 19.07  ? 252 TYR C CD1 1 
ATOM   1877 C CD2 . TYR A 1 253 ? -9.736  41.224  -6.297  1.00 23.07  ? 252 TYR C CD2 1 
ATOM   1878 C CE1 . TYR A 1 253 ? -9.724  38.548  -5.618  1.00 25.30  ? 252 TYR C CE1 1 
ATOM   1879 C CE2 . TYR A 1 253 ? -10.749 40.711  -5.507  1.00 23.70  ? 252 TYR C CE2 1 
ATOM   1880 C CZ  . TYR A 1 253 ? -10.735 39.370  -5.170  1.00 25.96  ? 252 TYR C CZ  1 
ATOM   1881 O OH  . TYR A 1 253 ? -11.733 38.844  -4.384  1.00 31.11  ? 252 TYR C OH  1 
ATOM   1882 N N   . ARG A 1 254 ? -4.360  42.604  -7.287  1.00 24.38  ? 253 ARG C N   1 
ATOM   1883 C CA  . ARG A 1 254 ? -3.334  43.198  -8.132  1.00 25.03  ? 253 ARG C CA  1 
ATOM   1884 C C   . ARG A 1 254 ? -2.396  42.118  -8.658  1.00 24.92  ? 253 ARG C C   1 
ATOM   1885 O O   . ARG A 1 254 ? -1.995  41.207  -7.928  1.00 25.72  ? 253 ARG C O   1 
ATOM   1886 C CB  . ARG A 1 254 ? -2.555  44.273  -7.364  1.00 26.89  ? 253 ARG C CB  1 
ATOM   1887 C CG  . ARG A 1 254 ? -1.643  43.761  -6.260  1.00 28.87  ? 253 ARG C CG  1 
ATOM   1888 C CD  . ARG A 1 254 ? -1.182  44.898  -5.359  1.00 24.95  ? 253 ARG C CD  1 
ATOM   1889 N NE  . ARG A 1 254 ? -0.276  44.436  -4.313  1.00 36.21  ? 253 ARG C NE  1 
ATOM   1890 C CZ  . ARG A 1 254 ? -0.647  44.162  -3.069  1.00 33.17  ? 253 ARG C CZ  1 
ATOM   1891 N NH1 . ARG A 1 254 ? -1.907  44.292  -2.676  1.00 21.93  ? 253 ARG C NH1 1 
ATOM   1892 N NH2 . ARG A 1 254 ? 0.266   43.746  -2.196  1.00 34.52  ? 253 ARG C NH2 1 
ATOM   1893 N N   . ALA A 1 255 ? -2.069  42.211  -9.943  1.00 26.44  ? 254 ALA C N   1 
ATOM   1894 C CA  . ALA A 1 255 ? -1.267  41.181  -10.587 1.00 27.58  ? 254 ALA C CA  1 
ATOM   1895 C C   . ALA A 1 255 ? 0.192   41.283  -10.162 1.00 27.98  ? 254 ALA C C   1 
ATOM   1896 O O   . ALA A 1 255 ? 0.732   42.373  -9.956  1.00 26.75  ? 254 ALA C O   1 
ATOM   1897 C CB  . ALA A 1 255 ? -1.369  41.291  -12.108 1.00 24.31  ? 254 ALA C CB  1 
ATOM   1898 N N   . CYS A 1 256 ? 0.829   40.129  -10.040 1.00 25.21  ? 255 CYS C N   1 
ATOM   1899 C CA  . CYS A 1 256 ? 2.242   40.098  -9.698  1.00 25.39  ? 255 CYS C CA  1 
ATOM   1900 C C   . CYS A 1 256 ? 3.063   40.700  -10.834 1.00 26.26  ? 255 CYS C C   1 
ATOM   1901 O O   . CYS A 1 256 ? 2.897   40.299  -11.993 1.00 26.83  ? 255 CYS C O   1 
ATOM   1902 C CB  . CYS A 1 256 ? 2.687   38.667  -9.419  1.00 26.53  ? 255 CYS C CB  1 
ATOM   1903 S SG  . CYS A 1 256 ? 4.449   38.516  -9.098  1.00 32.43  ? 255 CYS C SG  1 
ATOM   1904 N N   . PRO A 1 257 ? 3.946   41.661  -10.549 1.00 26.77  ? 256 PRO C N   1 
ATOM   1905 C CA  . PRO A 1 257 ? 4.739   42.276  -11.629 1.00 19.61  ? 256 PRO C CA  1 
ATOM   1906 C C   . PRO A 1 257 ? 5.659   41.299  -12.340 1.00 24.76  ? 256 PRO C C   1 
ATOM   1907 O O   . PRO A 1 257 ? 5.977   41.503  -13.521 1.00 20.87  ? 256 PRO C O   1 
ATOM   1908 C CB  . PRO A 1 257 ? 5.535   43.369  -10.901 1.00 24.48  ? 256 PRO C CB  1 
ATOM   1909 C CG  . PRO A 1 257 ? 4.801   43.600  -9.614  1.00 25.63  ? 256 PRO C CG  1 
ATOM   1910 C CD  . PRO A 1 257 ? 4.198   42.286  -9.242  1.00 23.13  ? 256 PRO C CD  1 
ATOM   1911 N N   . LEU A 1 258 ? 6.111   40.249  -11.651 1.00 21.30  ? 257 LEU C N   1 
ATOM   1912 C CA  . LEU A 1 258 ? 6.905   39.221  -12.311 1.00 21.24  ? 257 LEU C CA  1 
ATOM   1913 C C   . LEU A 1 258 ? 6.120   38.572  -13.443 1.00 24.73  ? 257 LEU C C   1 
ATOM   1914 O O   . LEU A 1 258 ? 6.665   38.319  -14.524 1.00 24.88  ? 257 LEU C O   1 
ATOM   1915 C CB  . LEU A 1 258 ? 7.355   38.174  -11.290 1.00 24.89  ? 257 LEU C CB  1 
ATOM   1916 C CG  . LEU A 1 258 ? 8.151   36.987  -11.831 1.00 22.53  ? 257 LEU C CG  1 
ATOM   1917 C CD1 . LEU A 1 258 ? 9.399   37.488  -12.543 1.00 26.03  ? 257 LEU C CD1 1 
ATOM   1918 C CD2 . LEU A 1 258 ? 8.526   36.047  -10.705 1.00 24.96  ? 257 LEU C CD2 1 
ATOM   1919 N N   . ILE A 1 259 ? 4.832   38.306  -13.215 1.00 23.11  ? 258 ILE C N   1 
ATOM   1920 C CA  . ILE A 1 259 ? 3.991   37.753  -14.271 1.00 23.58  ? 258 ILE C CA  1 
ATOM   1921 C C   . ILE A 1 259 ? 3.840   38.752  -15.410 1.00 28.06  ? 258 ILE C C   1 
ATOM   1922 O O   . ILE A 1 259 ? 3.930   38.386  -16.590 1.00 24.89  ? 258 ILE C O   1 
ATOM   1923 C CB  . ILE A 1 259 ? 2.623   37.333  -13.701 1.00 20.40  ? 258 ILE C CB  1 
ATOM   1924 C CG1 . ILE A 1 259 ? 2.780   36.131  -12.764 1.00 22.28  ? 258 ILE C CG1 1 
ATOM   1925 C CG2 . ILE A 1 259 ? 1.655   37.007  -14.829 1.00 21.44  ? 258 ILE C CG2 1 
ATOM   1926 C CD1 . ILE A 1 259 ? 1.461   35.556  -12.269 1.00 18.08  ? 258 ILE C CD1 1 
ATOM   1927 N N   . ARG A 1 260 ? 3.619   40.029  -15.083 1.00 22.72  ? 259 ARG C N   1 
ATOM   1928 C CA  . ARG A 1 260 ? 3.459   41.029  -16.133 1.00 22.78  ? 259 ARG C CA  1 
ATOM   1929 C C   . ARG A 1 260 ? 4.726   41.156  -16.970 1.00 20.95  ? 259 ARG C C   1 
ATOM   1930 O O   . ARG A 1 260 ? 4.659   41.277  -18.199 1.00 23.71  ? 259 ARG C O   1 
ATOM   1931 C CB  . ARG A 1 260 ? 3.067   42.378  -15.528 1.00 20.04  ? 259 ARG C CB  1 
ATOM   1932 C CG  . ARG A 1 260 ? 2.320   43.276  -16.516 1.00 28.68  ? 259 ARG C CG  1 
ATOM   1933 C CD  . ARG A 1 260 ? 2.030   44.663  -15.952 1.00 23.84  ? 259 ARG C CD  1 
ATOM   1934 N NE  . ARG A 1 260 ? 1.028   44.639  -14.892 1.00 23.41  ? 259 ARG C NE  1 
ATOM   1935 C CZ  . ARG A 1 260 ? -0.265  44.404  -15.078 1.00 30.12  ? 259 ARG C CZ  1 
ATOM   1936 N NH1 . ARG A 1 260 ? -0.760  44.169  -16.284 1.00 26.01  ? 259 ARG C NH1 1 
ATOM   1937 N NH2 . ARG A 1 260 ? -1.083  44.404  -14.027 1.00 17.31  ? 259 ARG C NH2 1 
ATOM   1938 N N   . LYS A 1 261 ? 5.894   41.113  -16.324 1.00 24.69  ? 260 LYS C N   1 
ATOM   1939 C CA  . LYS A 1 261 ? 7.151   41.198  -17.062 1.00 23.45  ? 260 LYS C CA  1 
ATOM   1940 C C   . LYS A 1 261 ? 7.332   40.003  -17.991 1.00 30.08  ? 260 LYS C C   1 
ATOM   1941 O O   . LYS A 1 261 ? 7.821   40.155  -19.117 1.00 31.19  ? 260 LYS C O   1 
ATOM   1942 C CB  . LYS A 1 261 ? 8.325   41.301  -16.088 1.00 20.64  ? 260 LYS C CB  1 
ATOM   1943 C CG  . LYS A 1 261 ? 9.675   41.546  -16.748 1.00 35.71  ? 260 LYS C CG  1 
ATOM   1944 C CD  . LYS A 1 261 ? 10.785  40.798  -16.028 1.00 32.52  ? 260 LYS C CD  1 
ATOM   1945 C CE  . LYS A 1 261 ? 10.954  41.299  -14.603 1.00 42.04  ? 260 LYS C CE  1 
ATOM   1946 N NZ  . LYS A 1 261 ? 12.352  41.717  -14.313 1.00 49.27  ? 260 LYS C NZ  1 
ATOM   1947 N N   . MET A 1 262 ? 6.945   38.808  -17.540 1.00 28.05  ? 261 MET C N   1 
ATOM   1948 C CA  . MET A 1 262 ? 7.132   37.614  -18.359 1.00 29.41  ? 261 MET C CA  1 
ATOM   1949 C C   . MET A 1 262 ? 6.243   37.646  -19.596 1.00 23.66  ? 261 MET C C   1 
ATOM   1950 O O   . MET A 1 262 ? 6.675   37.255  -20.685 1.00 29.81  ? 261 MET C O   1 
ATOM   1951 C CB  . MET A 1 262 ? 6.860   36.360  -17.528 1.00 24.58  ? 261 MET C CB  1 
ATOM   1952 C CG  . MET A 1 262 ? 7.976   36.027  -16.550 1.00 20.22  ? 261 MET C CG  1 
ATOM   1953 S SD  . MET A 1 262 ? 7.432   34.974  -15.187 1.00 30.81  ? 261 MET C SD  1 
ATOM   1954 C CE  . MET A 1 262 ? 7.474   33.369  -15.979 1.00 28.47  ? 261 MET C CE  1 
ATOM   1955 N N   . VAL A 1 263 ? 5.001   38.115  -19.448 1.00 20.81  ? 262 VAL C N   1 
ATOM   1956 C CA  . VAL A 1 263 ? 4.102   38.217  -20.594 1.00 29.78  ? 262 VAL C CA  1 
ATOM   1957 C C   . VAL A 1 263 ? 4.644   39.216  -21.610 1.00 33.27  ? 262 VAL C C   1 
ATOM   1958 O O   . VAL A 1 263 ? 4.542   39.006  -22.826 1.00 31.60  ? 262 VAL C O   1 
ATOM   1959 C CB  . VAL A 1 263 ? 2.681   38.589  -20.131 1.00 23.41  ? 262 VAL C CB  1 
ATOM   1960 C CG1 . VAL A 1 263 ? 1.804   38.950  -21.323 1.00 25.85  ? 262 VAL C CG1 1 
ATOM   1961 C CG2 . VAL A 1 263 ? 2.064   37.442  -19.352 1.00 19.21  ? 262 VAL C CG2 1 
ATOM   1962 N N   . ARG A 1 264 ? 5.239   40.313  -21.130 1.00 26.80  ? 263 ARG C N   1 
ATOM   1963 C CA  . ARG A 1 264 ? 5.805   41.299  -22.045 1.00 27.51  ? 263 ARG C CA  1 
ATOM   1964 C C   . ARG A 1 264 ? 6.954   40.709  -22.851 1.00 28.66  ? 263 ARG C C   1 
ATOM   1965 O O   . ARG A 1 264 ? 7.139   41.053  -24.024 1.00 38.89  ? 263 ARG C O   1 
ATOM   1966 C CB  . ARG A 1 264 ? 6.277   42.530  -21.275 1.00 35.92  ? 263 ARG C CB  1 
ATOM   1967 C CG  . ARG A 1 264 ? 5.217   43.597  -21.106 1.00 31.15  ? 263 ARG C CG  1 
ATOM   1968 C CD  . ARG A 1 264 ? 5.462   44.393  -19.846 1.00 34.65  ? 263 ARG C CD  1 
ATOM   1969 N NE  . ARG A 1 264 ? 4.479   45.452  -19.671 1.00 29.88  ? 263 ARG C NE  1 
ATOM   1970 C CZ  . ARG A 1 264 ? 4.371   46.194  -18.579 1.00 27.79  ? 263 ARG C CZ  1 
ATOM   1971 N NH1 . ARG A 1 264 ? 5.183   46.026  -17.547 1.00 28.95  ? 263 ARG C NH1 1 
ATOM   1972 N NH2 . ARG A 1 264 ? 3.422   47.123  -18.517 1.00 35.36  ? 263 ARG C NH2 1 
ATOM   1973 N N   . GLY A 1 265 ? 7.737   39.824  -22.239 1.00 28.84  ? 264 GLY C N   1 
ATOM   1974 C CA  . GLY A 1 265 ? 8.845   39.177  -22.906 1.00 36.66  ? 264 GLY C CA  1 
ATOM   1975 C C   . GLY A 1 265 ? 8.489   38.003  -23.786 1.00 35.18  ? 264 GLY C C   1 
ATOM   1976 O O   . GLY A 1 265 ? 9.381   37.420  -24.409 1.00 25.26  ? 264 GLY C O   1 
ATOM   1977 N N   . GLY A 1 266 ? 7.213   37.633  -23.863 1.00 27.44  ? 265 GLY C N   1 
ATOM   1978 C CA  . GLY A 1 266 ? 6.809   36.502  -24.671 1.00 23.96  ? 265 GLY C CA  1 
ATOM   1979 C C   . GLY A 1 266 ? 6.930   35.156  -23.995 1.00 40.97  ? 265 GLY C C   1 
ATOM   1980 O O   . GLY A 1 266 ? 6.729   34.131  -24.657 1.00 37.60  ? 265 GLY C O   1 
ATOM   1981 N N   . ASN A 1 267 ? 7.256   35.122  -22.701 1.00 30.72  ? 266 ASN C N   1 
ATOM   1982 C CA  . ASN A 1 267 ? 7.371   33.869  -21.956 1.00 33.19  ? 266 ASN C CA  1 
ATOM   1983 C C   . ASN A 1 267 ? 6.009   33.538  -21.354 1.00 36.21  ? 266 ASN C C   1 
ATOM   1984 O O   . ASN A 1 267 ? 5.731   33.773  -20.176 1.00 38.43  ? 266 ASN C O   1 
ATOM   1985 C CB  . ASN A 1 267 ? 8.454   33.980  -20.891 1.00 31.53  ? 266 ASN C CB  1 
ATOM   1986 C CG  . ASN A 1 267 ? 9.802   34.329  -21.477 1.00 37.84  ? 266 ASN C CG  1 
ATOM   1987 O OD1 . ASN A 1 267 ? 10.113  33.949  -22.604 1.00 41.06  ? 266 ASN C OD1 1 
ATOM   1988 N ND2 . ASN A 1 267 ? 10.612  35.058  -20.717 1.00 38.70  ? 266 ASN C ND2 1 
ATOM   1989 N N   . LEU A 1 268 ? 5.145   32.971  -22.191 1.00 30.81  ? 267 LEU C N   1 
ATOM   1990 C CA  . LEU A 1 268 ? 3.761   32.709  -21.822 1.00 36.47  ? 267 LEU C CA  1 
ATOM   1991 C C   . LEU A 1 268 ? 3.542   31.317  -21.250 1.00 31.60  ? 267 LEU C C   1 
ATOM   1992 O O   . LEU A 1 268 ? 2.409   30.987  -20.879 1.00 32.98  ? 267 LEU C O   1 
ATOM   1993 C CB  . LEU A 1 268 ? 2.851   32.906  -23.034 1.00 34.76  ? 267 LEU C CB  1 
ATOM   1994 C CG  . LEU A 1 268 ? 2.988   34.260  -23.725 1.00 35.98  ? 267 LEU C CG  1 
ATOM   1995 C CD1 . LEU A 1 268 ? 1.996   34.359  -24.869 1.00 29.91  ? 267 LEU C CD1 1 
ATOM   1996 C CD2 . LEU A 1 268 ? 2.784   35.385  -22.728 1.00 29.02  ? 267 LEU C CD2 1 
ATOM   1997 N N   . GLY A 1 269 ? 4.583   30.496  -21.175 1.00 31.73  ? 268 GLY C N   1 
ATOM   1998 C CA  . GLY A 1 269 ? 4.441   29.162  -20.631 1.00 30.98  ? 268 GLY C CA  1 
ATOM   1999 C C   . GLY A 1 269 ? 4.578   28.068  -21.670 1.00 34.97  ? 268 GLY C C   1 
ATOM   2000 O O   . GLY A 1 269 ? 5.491   28.097  -22.503 1.00 33.55  ? 268 GLY C O   1 
ATOM   2001 N N   . CYS A 1 270 ? 3.660   27.101  -21.633 1.00 31.19  ? 269 CYS C N   1 
ATOM   2002 C CA  . CYS A 1 270 ? 3.783   25.930  -22.495 1.00 41.62  ? 269 CYS C CA  1 
ATOM   2003 C C   . CYS A 1 270 ? 3.684   26.299  -23.968 1.00 36.30  ? 269 CYS C C   1 
ATOM   2004 O O   . CYS A 1 270 ? 4.412   25.746  -24.801 1.00 36.11  ? 269 CYS C O   1 
ATOM   2005 C CB  . CYS A 1 270 ? 2.716   24.900  -22.131 1.00 34.73  ? 269 CYS C CB  1 
ATOM   2006 S SG  . CYS A 1 270 ? 3.091   23.982  -20.630 1.00 43.63  ? 269 CYS C SG  1 
ATOM   2007 N N   . LYS A 1 271 ? 2.798   27.235  -24.312 1.00 36.55  ? 270 LYS C N   1 
ATOM   2008 C CA  . LYS A 1 271 ? 2.531   27.505  -25.719 1.00 34.31  ? 270 LYS C CA  1 
ATOM   2009 C C   . LYS A 1 271 ? 3.656   28.267  -26.408 1.00 34.88  ? 270 LYS C C   1 
ATOM   2010 O O   . LYS A 1 271 ? 3.665   28.328  -27.641 1.00 43.32  ? 270 LYS C O   1 
ATOM   2011 C CB  . LYS A 1 271 ? 1.211   28.263  -25.868 1.00 30.22  ? 270 LYS C CB  1 
ATOM   2012 C CG  . LYS A 1 271 ? 1.115   29.533  -25.053 1.00 35.82  ? 270 LYS C CG  1 
ATOM   2013 C CD  . LYS A 1 271 ? -0.102  30.338  -25.469 1.00 42.73  ? 270 LYS C CD  1 
ATOM   2014 C CE  . LYS A 1 271 ? -0.704  31.075  -24.296 1.00 32.99  ? 270 LYS C CE  1 
ATOM   2015 N NZ  . LYS A 1 271 ? -1.873  30.353  -23.715 1.00 46.97  ? 270 LYS C NZ  1 
ATOM   2016 N N   . THR A 1 272 ? 4.599   28.842  -25.661 1.00 34.75  ? 271 THR C N   1 
ATOM   2017 C CA  . THR A 1 272 ? 5.780   29.463  -26.249 1.00 26.80  ? 271 THR C CA  1 
ATOM   2018 C C   . THR A 1 272 ? 7.069   28.721  -25.917 1.00 35.70  ? 271 THR C C   1 
ATOM   2019 O O   . THR A 1 272 ? 8.151   29.184  -26.298 1.00 39.93  ? 271 THR C O   1 
ATOM   2020 C CB  . THR A 1 272 ? 5.900   30.929  -25.804 1.00 33.07  ? 271 THR C CB  1 
ATOM   2021 O OG1 . THR A 1 272 ? 6.053   30.997  -24.380 1.00 30.60  ? 271 THR C OG1 1 
ATOM   2022 C CG2 . THR A 1 272 ? 4.671   31.727  -26.227 1.00 24.59  ? 271 THR C CG2 1 
ATOM   2023 N N   . GLY A 1 273 ? 6.988   27.589  -25.220 1.00 34.35  ? 272 GLY C N   1 
ATOM   2024 C CA  . GLY A 1 273 ? 8.164   26.830  -24.849 1.00 38.49  ? 272 GLY C CA  1 
ATOM   2025 C C   . GLY A 1 273 ? 8.915   27.338  -23.638 1.00 40.88  ? 272 GLY C C   1 
ATOM   2026 O O   . GLY A 1 273 ? 9.942   26.747  -23.275 1.00 36.31  ? 272 GLY C O   1 
ATOM   2027 N N   . LYS A 1 274 ? 8.444   28.404  -22.993 1.00 36.94  ? 273 LYS C N   1 
ATOM   2028 C CA  . LYS A 1 274 ? 9.158   28.968  -21.856 1.00 30.38  ? 273 LYS C CA  1 
ATOM   2029 C C   . LYS A 1 274 ? 8.210   29.827  -21.036 1.00 36.49  ? 273 LYS C C   1 
ATOM   2030 O O   . LYS A 1 274 ? 7.540   30.711  -21.580 1.00 29.48  ? 273 LYS C O   1 
ATOM   2031 C CB  . LYS A 1 274 ? 10.356  29.797  -22.319 1.00 33.42  ? 273 LYS C CB  1 
ATOM   2032 C CG  . LYS A 1 274 ? 11.012  30.613  -21.225 1.00 26.67  ? 273 LYS C CG  1 
ATOM   2033 C CD  . LYS A 1 274 ? 12.442  30.961  -21.596 1.00 34.58  ? 273 LYS C CD  1 
ATOM   2034 C CE  . LYS A 1 274 ? 12.818  32.346  -21.098 1.00 39.25  ? 273 LYS C CE  1 
ATOM   2035 N NZ  . LYS A 1 274 ? 14.026  32.317  -20.235 1.00 46.43  ? 273 LYS C NZ  1 
ATOM   2036 N N   . GLY A 1 275 ? 8.158   29.558  -19.736 1.00 35.89  ? 274 GLY C N   1 
ATOM   2037 C CA  . GLY A 1 275 ? 7.436   30.383  -18.789 1.00 38.31  ? 274 GLY C CA  1 
ATOM   2038 C C   . GLY A 1 275 ? 8.206   30.436  -17.487 1.00 27.10  ? 274 GLY C C   1 
ATOM   2039 O O   . GLY A 1 275 ? 9.313   30.981  -17.443 1.00 25.68  ? 274 GLY C O   1 
ATOM   2040 N N   . PHE A 1 276 ? 7.634   29.875  -16.419 1.00 19.40  ? 275 PHE C N   1 
ATOM   2041 C CA  . PHE A 1 276 ? 8.424   29.590  -15.227 1.00 27.42  ? 275 PHE C CA  1 
ATOM   2042 C C   . PHE A 1 276 ? 9.329   28.385  -15.434 1.00 26.47  ? 275 PHE C C   1 
ATOM   2043 O O   . PHE A 1 276 ? 10.335  28.246  -14.731 1.00 32.26  ? 275 PHE C O   1 
ATOM   2044 C CB  . PHE A 1 276 ? 7.513   29.353  -14.022 1.00 28.24  ? 275 PHE C CB  1 
ATOM   2045 C CG  . PHE A 1 276 ? 6.771   30.577  -13.570 1.00 27.30  ? 275 PHE C CG  1 
ATOM   2046 C CD1 . PHE A 1 276 ? 7.431   31.597  -12.900 1.00 20.71  ? 275 PHE C CD1 1 
ATOM   2047 C CD2 . PHE A 1 276 ? 5.410   30.705  -13.808 1.00 27.89  ? 275 PHE C CD2 1 
ATOM   2048 C CE1 . PHE A 1 276 ? 6.747   32.724  -12.478 1.00 23.25  ? 275 PHE C CE1 1 
ATOM   2049 C CE2 . PHE A 1 276 ? 4.720   31.830  -13.392 1.00 26.71  ? 275 PHE C CE2 1 
ATOM   2050 C CZ  . PHE A 1 276 ? 5.390   32.841  -12.726 1.00 30.54  ? 275 PHE C CZ  1 
ATOM   2051 N N   . TYR A 1 277 ? 8.986   27.514  -16.379 1.00 27.66  ? 276 TYR C N   1 
ATOM   2052 C CA  . TYR A 1 277 ? 9.814   26.393  -16.790 1.00 33.79  ? 276 TYR C CA  1 
ATOM   2053 C C   . TYR A 1 277 ? 10.171  26.542  -18.263 1.00 34.98  ? 276 TYR C C   1 
ATOM   2054 O O   . TYR A 1 277 ? 9.410   27.120  -19.044 1.00 30.87  ? 276 TYR C O   1 
ATOM   2055 C CB  . TYR A 1 277 ? 9.090   25.056  -16.576 1.00 32.98  ? 276 TYR C CB  1 
ATOM   2056 C CG  . TYR A 1 277 ? 8.767   24.755  -15.137 1.00 34.43  ? 276 TYR C CG  1 
ATOM   2057 C CD1 . TYR A 1 277 ? 7.575   25.180  -14.568 1.00 34.93  ? 276 TYR C CD1 1 
ATOM   2058 C CD2 . TYR A 1 277 ? 9.656   24.044  -14.344 1.00 34.13  ? 276 TYR C CD2 1 
ATOM   2059 C CE1 . TYR A 1 277 ? 7.280   24.905  -13.245 1.00 37.52  ? 276 TYR C CE1 1 
ATOM   2060 C CE2 . TYR A 1 277 ? 9.370   23.763  -13.027 1.00 27.87  ? 276 TYR C CE2 1 
ATOM   2061 C CZ  . TYR A 1 277 ? 8.184   24.195  -12.481 1.00 29.21  ? 276 TYR C CZ  1 
ATOM   2062 O OH  . TYR A 1 277 ? 7.909   23.912  -11.162 1.00 36.79  ? 276 TYR C OH  1 
ATOM   2063 N N   . VAL A 1 278 ? 11.336  26.019  -18.638 1.00 36.88  ? 277 VAL C N   1 
ATOM   2064 C CA  . VAL A 1 278 ? 11.725  25.887  -20.037 1.00 33.80  ? 277 VAL C CA  1 
ATOM   2065 C C   . VAL A 1 278 ? 11.362  24.481  -20.486 1.00 39.97  ? 277 VAL C C   1 
ATOM   2066 O O   . VAL A 1 278 ? 11.690  23.501  -19.808 1.00 36.36  ? 277 VAL C O   1 
ATOM   2067 C CB  . VAL A 1 278 ? 13.225  26.158  -20.240 1.00 36.97  ? 277 VAL C CB  1 
ATOM   2068 C CG1 . VAL A 1 278 ? 13.664  25.670  -21.609 1.00 38.50  ? 277 VAL C CG1 1 
ATOM   2069 C CG2 . VAL A 1 278 ? 13.524  27.637  -20.083 1.00 34.20  ? 277 VAL C CG2 1 
ATOM   2070 N N   . TYR A 1 279 ? 10.675  24.380  -21.618 1.00 37.89  ? 278 TYR C N   1 
ATOM   2071 C CA  . TYR A 1 279 ? 10.209  23.102  -22.141 1.00 39.26  ? 278 TYR C CA  1 
ATOM   2072 C C   . TYR A 1 279 ? 11.101  22.703  -23.310 1.00 43.79  ? 278 TYR C C   1 
ATOM   2073 O O   . TYR A 1 279 ? 11.096  23.358  -24.357 1.00 37.58  ? 278 TYR C O   1 
ATOM   2074 C CB  . TYR A 1 279 ? 8.741   23.199  -22.545 1.00 39.51  ? 278 TYR C CB  1 
ATOM   2075 C CG  . TYR A 1 279 ? 7.864   23.610  -21.389 1.00 32.35  ? 278 TYR C CG  1 
ATOM   2076 C CD1 . TYR A 1 279 ? 7.684   24.949  -21.056 1.00 42.66  ? 278 TYR C CD1 1 
ATOM   2077 C CD2 . TYR A 1 279 ? 7.250   22.652  -20.599 1.00 45.66  ? 278 TYR C CD2 1 
ATOM   2078 C CE1 . TYR A 1 279 ? 6.894   25.317  -19.975 1.00 38.14  ? 278 TYR C CE1 1 
ATOM   2079 C CE2 . TYR A 1 279 ? 6.462   23.006  -19.527 1.00 34.72  ? 278 TYR C CE2 1 
ATOM   2080 C CZ  . TYR A 1 279 ? 6.287   24.335  -19.215 1.00 42.59  ? 278 TYR C CZ  1 
ATOM   2081 O OH  . TYR A 1 279 ? 5.501   24.661  -18.136 1.00 37.89  ? 278 TYR C OH  1 
ATOM   2082 N N   . ASN A 1 280 ? 11.807  21.590  -23.131 1.00 51.72  ? 279 ASN C N   1 
ATOM   2083 C CA  . ASN A 1 280 ? 12.788  21.145  -24.152 1.00 61.91  ? 279 ASN C CA  1 
ATOM   2084 C C   . ASN A 1 280 ? 12.244  19.958  -24.952 1.00 60.37  ? 279 ASN C C   1 
ATOM   2085 O O   . ASN A 1 280 ? 11.334  19.277  -24.452 1.00 51.13  ? 279 ASN C O   1 
ATOM   2086 C CB  . ASN A 1 280 ? 14.152  20.844  -23.519 1.00 57.50  ? 279 ASN C CB  1 
ATOM   2087 C CG  . ASN A 1 280 ? 14.558  21.803  -22.422 1.00 51.80  ? 279 ASN C CG  1 
ATOM   2088 O OD1 . ASN A 1 280 ? 15.267  22.772  -22.678 1.00 50.35  ? 279 ASN C OD1 1 
ATOM   2089 N ND2 . ASN A 1 280 ? 14.150  21.523  -21.196 1.00 49.24  ? 279 ASN C ND2 1 
ATOM   2090 N N   . ALA A 1 281 ? 12.809  19.724  -26.140 1.00 61.47  ? 280 ALA C N   1 
ATOM   2091 C CA  . ALA A 1 281 ? 12.345  18.648  -27.051 1.00 60.03  ? 280 ALA C CA  1 
ATOM   2092 C C   . ALA A 1 281 ? 12.253  17.295  -26.351 1.00 61.00  ? 280 ALA C C   1 
ATOM   2093 O O   . ALA A 1 281 ? 11.308  16.567  -26.651 1.00 63.19  ? 280 ALA C O   1 
ATOM   2094 C CB  . ALA A 1 281 ? 13.289  18.573  -28.217 1.00 49.41  ? 280 ALA C CB  1 
ATOM   2095 N N   . ASP A 1 282 ? 13.188  16.983  -25.454 1.00 69.51  ? 281 ASP C N   1 
ATOM   2096 C CA  . ASP A 1 282 ? 13.220  15.662  -24.769 1.00 66.95  ? 281 ASP C CA  1 
ATOM   2097 C C   . ASP A 1 282 ? 12.114  15.552  -23.722 1.00 64.87  ? 281 ASP C C   1 
ATOM   2098 O O   . ASP A 1 282 ? 12.246  14.693  -22.844 1.00 71.10  ? 281 ASP C O   1 
ATOM   2099 C CB  . ASP A 1 282 ? 14.583  15.431  -24.121 1.00 67.57  ? 281 ASP C CB  1 
ATOM   2100 C CG  . ASP A 1 282 ? 15.206  16.694  -23.555 1.00 77.91  ? 281 ASP C CG  1 
ATOM   2101 O OD1 . ASP A 1 282 ? 14.448  17.620  -23.224 1.00 75.64  ? 281 ASP C OD1 1 
ATOM   2102 O OD2 . ASP A 1 282 ? 16.444  16.736  -23.442 1.00 72.80  ? 281 ASP C OD2 1 
ATOM   2103 N N   . ARG A 1 283 ? 11.086  16.388  -23.804 1.00 67.51  ? 282 ARG C N   1 
ATOM   2104 C CA  . ARG A 1 283 ? 9.975   16.410  -22.811 1.00 71.26  ? 282 ARG C CA  1 
ATOM   2105 C C   . ARG A 1 283 ? 10.511  16.737  -21.409 1.00 69.42  ? 282 ARG C C   1 
ATOM   2106 O O   . ARG A 1 283 ? 9.776   16.499  -20.440 1.00 64.05  ? 282 ARG C O   1 
ATOM   2107 C CB  . ARG A 1 283 ? 9.178   15.104  -22.843 1.00 71.20  ? 282 ARG C CB  1 
ATOM   2108 C CG  . ARG A 1 283 ? 8.289   14.940  -24.066 1.00 73.75  ? 282 ARG C CG  1 
ATOM   2109 C CD  . ARG A 1 283 ? 8.467   13.566  -24.680 1.00 80.42  ? 282 ARG C CD  1 
ATOM   2110 N NE  . ARG A 1 283 ? 7.899   13.477  -26.016 1.00 89.58  ? 282 ARG C NE  1 
ATOM   2111 C CZ  . ARG A 1 283 ? 8.569   13.721  -27.136 1.00 95.21  ? 282 ARG C CZ  1 
ATOM   2112 N NH1 . ARG A 1 283 ? 9.590   14.560  -27.129 1.00 88.50  ? 282 ARG C NH1 1 
ATOM   2113 N NH2 . ARG A 1 283 ? 8.216   13.121  -28.259 1.00 89.00  ? 282 ARG C NH2 1 
ATOM   2114 N N   . THR A 1 284 ? 11.718  17.297  -21.311 1.00 66.56  ? 283 THR C N   1 
ATOM   2115 C CA  . THR A 1 284 ? 12.248  17.721  -19.989 1.00 62.06  ? 283 THR C CA  1 
ATOM   2116 C C   . THR A 1 284 ? 11.866  19.178  -19.721 1.00 65.15  ? 283 THR C C   1 
ATOM   2117 O O   . THR A 1 284 ? 11.953  19.980  -20.665 1.00 54.25  ? 283 THR C O   1 
ATOM   2118 C CB  . THR A 1 284 ? 13.767  17.549  -19.888 1.00 58.82  ? 283 THR C CB  1 
ATOM   2119 O OG1 . THR A 1 284 ? 14.413  18.482  -20.752 1.00 58.31  ? 283 THR C OG1 1 
ATOM   2120 C CG2 . THR A 1 284 ? 14.213  16.142  -20.221 1.00 60.01  ? 283 THR C CG2 1 
ATOM   2121 N N   . LYS A 1 285 ? 11.423  19.480  -18.497 1.00 55.93  ? 284 LYS C N   1 
ATOM   2122 C CA  . LYS A 1 285 ? 11.144  20.887  -18.114 1.00 52.88  ? 284 LYS C CA  1 
ATOM   2123 C C   . LYS A 1 285 ? 12.096  21.264  -16.981 1.00 48.40  ? 284 LYS C C   1 
ATOM   2124 O O   . LYS A 1 285 ? 12.279  20.459  -16.060 1.00 46.37  ? 284 LYS C O   1 
ATOM   2125 C CB  . LYS A 1 285 ? 9.671   21.125  -17.760 1.00 44.62  ? 284 LYS C CB  1 
ATOM   2126 C CG  . LYS A 1 285 ? 9.225   20.800  -16.344 1.00 39.81  ? 284 LYS C CG  1 
ATOM   2127 C CD  . LYS A 1 285 ? 7.942   21.502  -15.972 1.00 39.27  ? 284 LYS C CD  1 
ATOM   2128 C CE  . LYS A 1 285 ? 6.743   20.585  -15.960 1.00 43.65  ? 284 LYS C CE  1 
ATOM   2129 N NZ  . LYS A 1 285 ? 6.977   19.412  -15.088 1.00 54.21  ? 284 LYS C NZ  1 
ATOM   2130 N N   . THR A 1 286 ? 12.717  22.425  -17.100 1.00 44.80  ? 285 THR C N   1 
ATOM   2131 C CA  . THR A 1 286 ? 13.607  22.904  -16.064 1.00 44.44  ? 285 THR C CA  1 
ATOM   2132 C C   . THR A 1 286 ? 13.192  24.302  -15.618 1.00 44.95  ? 285 THR C C   1 
ATOM   2133 O O   . THR A 1 286 ? 12.852  25.143  -16.458 1.00 39.28  ? 285 THR C O   1 
ATOM   2134 C CB  . THR A 1 286 ? 15.062  22.926  -16.561 1.00 36.66  ? 285 THR C CB  1 
ATOM   2135 O OG1 . THR A 1 286 ? 15.861  23.738  -15.693 1.00 48.15  ? 285 THR C OG1 1 
ATOM   2136 C CG2 . THR A 1 286 ? 15.136  23.473  -17.980 1.00 47.15  ? 285 THR C CG2 1 
ATOM   2137 N N   . PRO A 1 287 ? 13.193  24.574  -14.313 1.00 39.86  ? 286 PRO C N   1 
ATOM   2138 C CA  . PRO A 1 287 ? 12.809  25.911  -13.839 1.00 30.72  ? 286 PRO C CA  1 
ATOM   2139 C C   . PRO A 1 287 ? 13.804  26.965  -14.302 1.00 30.92  ? 286 PRO C C   1 
ATOM   2140 O O   . PRO A 1 287 ? 15.016  26.742  -14.289 1.00 32.59  ? 286 PRO C O   1 
ATOM   2141 C CB  . PRO A 1 287 ? 12.817  25.766  -12.311 1.00 32.55  ? 286 PRO C CB  1 
ATOM   2142 C CG  . PRO A 1 287 ? 12.866  24.283  -12.043 1.00 31.09  ? 286 PRO C CG  1 
ATOM   2143 C CD  . PRO A 1 287 ? 13.559  23.673  -13.209 1.00 36.89  ? 286 PRO C CD  1 
ATOM   2144 N N   . VAL A 1 288 ? 13.285  28.116  -14.723 1.00 33.44  ? 287 VAL C N   1 
ATOM   2145 C CA  . VAL A 1 288 ? 14.142  29.201  -15.285 1.00 32.78  ? 287 VAL C CA  1 
ATOM   2146 C C   . VAL A 1 288 ? 15.144  29.702  -14.240 1.00 32.05  ? 287 VAL C C   1 
ATOM   2147 O O   . VAL A 1 288 ? 16.134  30.307  -14.647 1.00 38.82  ? 287 VAL C O   1 
ATOM   2148 C CB  . VAL A 1 288 ? 13.279  30.335  -15.874 1.00 32.47  ? 287 VAL C CB  1 
ATOM   2149 C CG1 . VAL A 1 288 ? 12.499  29.864  -17.089 1.00 28.29  ? 287 VAL C CG1 1 
ATOM   2150 C CG2 . VAL A 1 288 ? 12.349  30.947  -14.840 1.00 24.91  ? 287 VAL C CG2 1 
ATOM   2151 N N   . ASP A 1 289 ? 14.915  29.414  -12.961 1.00 31.67  ? 288 ASP C N   1 
ATOM   2152 C CA  . ASP A 1 289 ? 15.898  29.780  -11.908 1.00 40.25  ? 288 ASP C CA  1 
ATOM   2153 C C   . ASP A 1 289 ? 16.949  28.669  -11.800 1.00 44.86  ? 288 ASP C C   1 
ATOM   2154 O O   . ASP A 1 289 ? 17.728  28.708  -10.840 1.00 37.06  ? 288 ASP C O   1 
ATOM   2155 C CB  . ASP A 1 289 ? 15.198  30.113  -10.588 1.00 30.00  ? 288 ASP C CB  1 
ATOM   2156 C CG  . ASP A 1 289 ? 14.260  29.036  -10.073 1.00 30.00  ? 288 ASP C CG  1 
ATOM   2157 O OD1 . ASP A 1 289 ? 14.308  27.919  -10.598 1.00 30.00  ? 288 ASP C OD1 1 
ATOM   2158 O OD2 . ASP A 1 289 ? 13.495  29.331  -9.145  1.00 30.00  ? 288 ASP C OD2 1 
ATOM   2159 N N   . GLN A 1 290 ? 16.945  27.726  -12.745 1.00 42.49  ? 289 GLN C N   1 
ATOM   2160 C CA  . GLN A 1 290 ? 17.914  26.601  -12.788 1.00 45.92  ? 289 GLN C CA  1 
ATOM   2161 C C   . GLN A 1 290 ? 17.735  25.725  -11.549 1.00 47.62  ? 289 GLN C C   1 
ATOM   2162 O O   . GLN A 1 290 ? 16.891  24.823  -11.621 1.00 49.07  ? 289 GLN C O   1 
ATOM   2163 C CB  . GLN A 1 290 ? 19.336  27.123  -12.982 1.00 30.00  ? 289 GLN C CB  1 
ATOM   2164 C CG  . GLN A 1 290 ? 19.450  28.163  -14.085 1.00 30.00  ? 289 GLN C CG  1 
ATOM   2165 C CD  . GLN A 1 290 ? 19.259  27.554  -15.451 1.00 30.00  ? 289 GLN C CD  1 
ATOM   2166 O OE1 . GLN A 1 290 ? 18.164  27.556  -16.008 1.00 30.00  ? 289 GLN C OE1 1 
ATOM   2167 N NE2 . GLN A 1 290 ? 20.338  27.027  -16.004 1.00 30.00  ? 289 GLN C NE2 1 
ATOM   2168 N N   . MET B 1 2   ? 21.198  8.071   14.679  1.00 41.21  ? 1   MET A N   1 
ATOM   2169 C CA  . MET B 1 2   ? 20.915  9.443   15.096  1.00 40.58  ? 1   MET A CA  1 
ATOM   2170 C C   . MET B 1 2   ? 19.816  9.494   16.162  1.00 43.65  ? 1   MET A C   1 
ATOM   2171 O O   . MET B 1 2   ? 18.858  8.724   16.113  1.00 40.76  ? 1   MET A O   1 
ATOM   2172 C CB  . MET B 1 2   ? 20.523  10.287  13.883  1.00 50.53  ? 1   MET A CB  1 
ATOM   2173 C CG  . MET B 1 2   ? 19.948  11.647  14.221  1.00 48.45  ? 1   MET A CG  1 
ATOM   2174 S SD  . MET B 1 2   ? 19.452  12.556  12.750  1.00 59.51  ? 1   MET A SD  1 
ATOM   2175 C CE  . MET B 1 2   ? 20.685  13.853  12.759  1.00 40.16  ? 1   MET A CE  1 
ATOM   2176 N N   . LYS B 1 3   ? 19.965  10.401  17.128  1.00 42.06  ? 2   LYS A N   1 
ATOM   2177 C CA  . LYS B 1 3   ? 19.039  10.531  18.246  1.00 38.44  ? 2   LYS A CA  1 
ATOM   2178 C C   . LYS B 1 3   ? 18.364  11.895  18.201  1.00 43.90  ? 2   LYS A C   1 
ATOM   2179 O O   . LYS B 1 3   ? 19.043  12.927  18.161  1.00 44.80  ? 2   LYS A O   1 
ATOM   2180 C CB  . LYS B 1 3   ? 19.769  10.334  19.574  1.00 42.12  ? 2   LYS A CB  1 
ATOM   2181 C CG  . LYS B 1 3   ? 20.853  9.271   19.495  1.00 59.31  ? 2   LYS A CG  1 
ATOM   2182 C CD  . LYS B 1 3   ? 21.978  9.532   20.472  1.00 55.28  ? 2   LYS A CD  1 
ATOM   2183 C CE  . LYS B 1 3   ? 21.541  9.213   21.886  1.00 53.76  ? 2   LYS A CE  1 
ATOM   2184 N NZ  . LYS B 1 3   ? 22.363  9.943   22.880  1.00 65.28  ? 2   LYS A NZ  1 
ATOM   2185 N N   . ILE B 1 4   ? 17.032  11.898  18.215  1.00 31.78  ? 3   ILE A N   1 
ATOM   2186 C CA  . ILE B 1 4   ? 16.241  13.107  18.013  1.00 37.55  ? 3   ILE A CA  1 
ATOM   2187 C C   . ILE B 1 4   ? 15.450  13.391  19.283  1.00 31.65  ? 3   ILE A C   1 
ATOM   2188 O O   . ILE B 1 4   ? 14.936  12.467  19.921  1.00 31.32  ? 3   ILE A O   1 
ATOM   2189 C CB  . ILE B 1 4   ? 15.283  12.996  16.800  1.00 36.60  ? 3   ILE A CB  1 
ATOM   2190 C CG1 . ILE B 1 4   ? 16.026  12.740  15.479  1.00 39.16  ? 3   ILE A CG1 1 
ATOM   2191 C CG2 . ILE B 1 4   ? 14.409  14.242  16.680  1.00 29.85  ? 3   ILE A CG2 1 
ATOM   2192 C CD1 . ILE B 1 4   ? 16.508  11.318  15.278  1.00 44.73  ? 3   ILE A CD1 1 
ATOM   2193 N N   . GLY B 1 5   ? 15.361  14.667  19.653  1.00 26.14  ? 4   GLY A N   1 
ATOM   2194 C CA  . GLY B 1 5   ? 14.486  15.076  20.734  1.00 26.69  ? 4   GLY A CA  1 
ATOM   2195 C C   . GLY B 1 5   ? 13.271  15.836  20.236  1.00 27.94  ? 4   GLY A C   1 
ATOM   2196 O O   . GLY B 1 5   ? 13.409  16.897  19.619  1.00 35.15  ? 4   GLY A O   1 
ATOM   2197 N N   . VAL B 1 6   ? 12.078  15.300  20.486  1.00 27.00  ? 5   VAL A N   1 
ATOM   2198 C CA  . VAL B 1 6   ? 10.825  15.942  20.107  1.00 21.75  ? 5   VAL A CA  1 
ATOM   2199 C C   . VAL B 1 6   ? 10.196  16.540  21.358  1.00 34.03  ? 5   VAL A C   1 
ATOM   2200 O O   . VAL B 1 6   ? 9.838   15.810  22.291  1.00 33.70  ? 5   VAL A O   1 
ATOM   2201 C CB  . VAL B 1 6   ? 9.865   14.950  19.434  1.00 27.65  ? 5   VAL A CB  1 
ATOM   2202 C CG1 . VAL B 1 6   ? 8.511   15.605  19.207  1.00 24.11  ? 5   VAL A CG1 1 
ATOM   2203 C CG2 . VAL B 1 6   ? 10.451  14.448  18.124  1.00 21.05  ? 5   VAL A CG2 1 
ATOM   2204 N N   . ILE B 1 7   ? 10.051  17.863  21.376  1.00 28.50  ? 6   ILE A N   1 
ATOM   2205 C CA  . ILE B 1 7   ? 9.496   18.586  22.515  1.00 31.37  ? 6   ILE A CA  1 
ATOM   2206 C C   . ILE B 1 7   ? 8.028   18.881  22.229  1.00 30.86  ? 6   ILE A C   1 
ATOM   2207 O O   . ILE B 1 7   ? 7.699   19.547  21.240  1.00 33.56  ? 6   ILE A O   1 
ATOM   2208 C CB  . ILE B 1 7   ? 10.284  19.875  22.802  1.00 31.01  ? 6   ILE A CB  1 
ATOM   2209 C CG1 . ILE B 1 7   ? 11.562  19.555  23.583  1.00 38.73  ? 6   ILE A CG1 1 
ATOM   2210 C CG2 . ILE B 1 7   ? 9.446   20.853  23.609  1.00 36.15  ? 6   ILE A CG2 1 
ATOM   2211 C CD1 . ILE B 1 7   ? 12.709  19.094  22.732  1.00 38.95  ? 6   ILE A CD1 1 
ATOM   2212 N N   . GLY B 1 8   ? 7.144   18.384  23.095  1.00 35.84  ? 7   GLY A N   1 
ATOM   2213 C CA  . GLY B 1 8   ? 5.712   18.501  22.893  1.00 30.66  ? 7   GLY A CA  1 
ATOM   2214 C C   . GLY B 1 8   ? 5.093   17.192  22.441  1.00 33.58  ? 7   GLY A C   1 
ATOM   2215 O O   . GLY B 1 8   ? 5.354   16.730  21.327  1.00 31.63  ? 7   GLY A O   1 
ATOM   2216 N N   . ALA B 1 9   ? 4.279   16.577  23.299  1.00 30.38  ? 8   ALA A N   1 
ATOM   2217 C CA  . ALA B 1 9   ? 3.698   15.269  23.025  1.00 33.60  ? 8   ALA A CA  1 
ATOM   2218 C C   . ALA B 1 9   ? 2.262   15.356  22.516  1.00 29.37  ? 8   ALA A C   1 
ATOM   2219 O O   . ALA B 1 9   ? 1.500   14.399  22.673  1.00 31.97  ? 8   ALA A O   1 
ATOM   2220 C CB  . ALA B 1 9   ? 3.760   14.391  24.277  1.00 32.81  ? 8   ALA A CB  1 
ATOM   2221 N N   . GLY B 1 10  ? 1.878   16.475  21.916  1.00 35.96  ? 9   GLY A N   1 
ATOM   2222 C CA  . GLY B 1 10  ? 0.568   16.615  21.319  1.00 37.53  ? 9   GLY A CA  1 
ATOM   2223 C C   . GLY B 1 10  ? 0.482   15.827  20.026  1.00 38.68  ? 9   GLY A C   1 
ATOM   2224 O O   . GLY B 1 10  ? 1.247   14.895  19.769  1.00 36.84  ? 9   GLY A O   1 
ATOM   2225 N N   . THR B 1 11  ? -0.464  16.243  19.186  1.00 37.63  ? 10  THR A N   1 
ATOM   2226 C CA  . THR B 1 11  ? -0.675  15.571  17.907  1.00 40.70  ? 10  THR A CA  1 
ATOM   2227 C C   . THR B 1 11  ? 0.540   15.717  16.992  1.00 42.26  ? 10  THR A C   1 
ATOM   2228 O O   . THR B 1 11  ? 1.015   14.733  16.410  1.00 41.19  ? 10  THR A O   1 
ATOM   2229 C CB  . THR B 1 11  ? -1.934  16.126  17.234  1.00 46.59  ? 10  THR A CB  1 
ATOM   2230 O OG1 . THR B 1 11  ? -3.098  15.636  17.915  1.00 54.57  ? 10  THR A OG1 1 
ATOM   2231 C CG2 . THR B 1 11  ? -1.995  15.708  15.772  1.00 38.68  ? 10  THR A CG2 1 
ATOM   2232 N N   . MET B 1 12  ? 1.052   16.941  16.842  1.00 37.86  ? 11  MET A N   1 
ATOM   2233 C CA  . MET B 1 12  ? 2.168   17.164  15.926  1.00 39.93  ? 11  MET A CA  1 
ATOM   2234 C C   . MET B 1 12  ? 3.441   16.494  16.430  1.00 33.58  ? 11  MET A C   1 
ATOM   2235 O O   . MET B 1 12  ? 4.153   15.830  15.665  1.00 32.02  ? 11  MET A O   1 
ATOM   2236 C CB  . MET B 1 12  ? 2.385   18.662  15.721  1.00 44.07  ? 11  MET A CB  1 
ATOM   2237 C CG  . MET B 1 12  ? 1.450   19.281  14.689  1.00 54.01  ? 11  MET A CG  1 
ATOM   2238 S SD  . MET B 1 12  ? 1.145   18.283  13.207  1.00 56.04  ? 11  MET A SD  1 
ATOM   2239 C CE  . MET B 1 12  ? 2.798   18.027  12.567  1.00 38.80  ? 11  MET A CE  1 
ATOM   2240 N N   . GLY B 1 13  ? 3.744   16.660  17.718  1.00 31.72  ? 12  GLY A N   1 
ATOM   2241 C CA  . GLY B 1 13  ? 4.916   16.009  18.277  1.00 30.28  ? 12  GLY A CA  1 
ATOM   2242 C C   . GLY B 1 13  ? 4.846   14.499  18.169  1.00 29.92  ? 12  GLY A C   1 
ATOM   2243 O O   . GLY B 1 13  ? 5.857   13.837  17.919  1.00 33.91  ? 12  GLY A O   1 
ATOM   2244 N N   . GLN B 1 14  ? 3.652   13.932  18.352  1.00 22.82  ? 13  GLN A N   1 
ATOM   2245 C CA  . GLN B 1 14  ? 3.481   12.500  18.135  1.00 33.46  ? 13  GLN A CA  1 
ATOM   2246 C C   . GLN B 1 14  ? 3.819   12.120  16.701  1.00 30.00  ? 13  GLN A C   1 
ATOM   2247 O O   . GLN B 1 14  ? 4.520   11.131  16.461  1.00 29.94  ? 13  GLN A O   1 
ATOM   2248 C CB  . GLN B 1 14  ? 2.051   12.083  18.466  1.00 34.38  ? 13  GLN A CB  1 
ATOM   2249 C CG  . GLN B 1 14  ? 1.804   11.852  19.936  1.00 34.82  ? 13  GLN A CG  1 
ATOM   2250 C CD  . GLN B 1 14  ? 0.329   11.819  20.255  1.00 31.43  ? 13  GLN A CD  1 
ATOM   2251 O OE1 . GLN B 1 14  ? -0.446  11.142  19.581  1.00 33.75  ? 13  GLN A OE1 1 
ATOM   2252 N NE2 . GLN B 1 14  ? -0.073  12.562  21.278  1.00 33.90  ? 13  GLN A NE2 1 
ATOM   2253 N N   . GLY B 1 15  ? 3.327   12.896  15.733  1.00 30.03  ? 14  GLY A N   1 
ATOM   2254 C CA  . GLY B 1 15  ? 3.609   12.591  14.342  1.00 25.14  ? 14  GLY A CA  1 
ATOM   2255 C C   . GLY B 1 15  ? 5.083   12.708  14.010  1.00 26.64  ? 14  GLY A C   1 
ATOM   2256 O O   . GLY B 1 15  ? 5.625   11.896  13.256  1.00 31.96  ? 14  GLY A O   1 
ATOM   2257 N N   . ILE B 1 16  ? 5.754   13.714  14.573  1.00 27.14  ? 15  ILE A N   1 
ATOM   2258 C CA  . ILE B 1 16  ? 7.174   13.891  14.294  1.00 29.75  ? 15  ILE A CA  1 
ATOM   2259 C C   . ILE B 1 16  ? 7.981   12.761  14.919  1.00 29.41  ? 15  ILE A C   1 
ATOM   2260 O O   . ILE B 1 16  ? 8.943   12.262  14.323  1.00 27.44  ? 15  ILE A O   1 
ATOM   2261 C CB  . ILE B 1 16  ? 7.641   15.274  14.780  1.00 28.70  ? 15  ILE A CB  1 
ATOM   2262 C CG1 . ILE B 1 16  ? 7.047   16.367  13.886  1.00 32.30  ? 15  ILE A CG1 1 
ATOM   2263 C CG2 . ILE B 1 16  ? 9.162   15.352  14.810  1.00 20.52  ? 15  ILE A CG2 1 
ATOM   2264 C CD1 . ILE B 1 16  ? 7.162   17.765  14.456  1.00 29.81  ? 15  ILE A CD1 1 
ATOM   2265 N N   . ALA B 1 17  ? 7.596   12.330  16.120  1.00 30.34  ? 16  ALA A N   1 
ATOM   2266 C CA  . ALA B 1 17  ? 8.276   11.208  16.757  1.00 34.39  ? 16  ALA A CA  1 
ATOM   2267 C C   . ALA B 1 17  ? 8.171   9.949   15.903  1.00 30.69  ? 16  ALA A C   1 
ATOM   2268 O O   . ALA B 1 17  ? 9.165   9.247   15.689  1.00 23.36  ? 16  ALA A O   1 
ATOM   2269 C CB  . ALA B 1 17  ? 7.697   10.971  18.153  1.00 28.89  ? 16  ALA A CB  1 
ATOM   2270 N N   . LYS B 1 18  ? 6.968   9.653   15.397  1.00 31.37  ? 17  LYS A N   1 
ATOM   2271 C CA  . LYS B 1 18  ? 6.795   8.497   14.519  1.00 31.25  ? 17  LYS A CA  1 
ATOM   2272 C C   . LYS B 1 18  ? 7.601   8.649   13.238  1.00 29.57  ? 17  LYS A C   1 
ATOM   2273 O O   . LYS B 1 18  ? 8.168   7.673   12.734  1.00 32.44  ? 17  LYS A O   1 
ATOM   2274 C CB  . LYS B 1 18  ? 5.320   8.299   14.180  1.00 23.70  ? 17  LYS A CB  1 
ATOM   2275 C CG  . LYS B 1 18  ? 4.479   7.832   15.338  1.00 33.40  ? 17  LYS A CG  1 
ATOM   2276 C CD  . LYS B 1 18  ? 3.138   7.299   14.864  1.00 34.84  ? 17  LYS A CD  1 
ATOM   2277 C CE  . LYS B 1 18  ? 2.184   8.425   14.514  1.00 40.26  ? 17  LYS A CE  1 
ATOM   2278 N NZ  . LYS B 1 18  ? 0.968   7.907   13.823  1.00 44.83  ? 17  LYS A NZ  1 
ATOM   2279 N N   . ALA B 1 19  ? 7.651   9.864   12.688  1.00 33.75  ? 18  ALA A N   1 
ATOM   2280 C CA  . ALA B 1 19  ? 8.374   10.082  11.440  1.00 36.87  ? 18  ALA A CA  1 
ATOM   2281 C C   . ALA B 1 19  ? 9.850   9.741   11.591  1.00 29.01  ? 18  ALA A C   1 
ATOM   2282 O O   . ALA B 1 19  ? 10.468  9.199   10.668  1.00 30.86  ? 18  ALA A O   1 
ATOM   2283 C CB  . ALA B 1 19  ? 8.197   11.528  10.977  1.00 28.91  ? 18  ALA A CB  1 
ATOM   2284 N N   . PHE B 1 20  ? 10.432  10.042  12.751  1.00 28.54  ? 19  PHE A N   1 
ATOM   2285 C CA  . PHE B 1 20  ? 11.834  9.711   12.970  1.00 32.33  ? 19  PHE A CA  1 
ATOM   2286 C C   . PHE B 1 20  ? 12.007  8.260   13.407  1.00 33.77  ? 19  PHE A C   1 
ATOM   2287 O O   . PHE B 1 20  ? 12.916  7.571   12.929  1.00 30.88  ? 19  PHE A O   1 
ATOM   2288 C CB  . PHE B 1 20  ? 12.443  10.656  14.004  1.00 34.18  ? 19  PHE A CB  1 
ATOM   2289 C CG  . PHE B 1 20  ? 12.807  12.002  13.451  1.00 28.70  ? 19  PHE A CG  1 
ATOM   2290 C CD1 . PHE B 1 20  ? 13.938  12.160  12.664  1.00 25.90  ? 19  PHE A CD1 1 
ATOM   2291 C CD2 . PHE B 1 20  ? 12.021  13.110  13.719  1.00 27.94  ? 19  PHE A CD2 1 
ATOM   2292 C CE1 . PHE B 1 20  ? 14.276  13.400  12.154  1.00 29.00  ? 19  PHE A CE1 1 
ATOM   2293 C CE2 . PHE B 1 20  ? 12.352  14.351  13.212  1.00 36.72  ? 19  PHE A CE2 1 
ATOM   2294 C CZ  . PHE B 1 20  ? 13.482  14.497  12.426  1.00 27.76  ? 19  PHE A CZ  1 
ATOM   2295 N N   . ALA B 1 21  ? 11.149  7.778   14.311  1.00 28.74  ? 20  ALA A N   1 
ATOM   2296 C CA  . ALA B 1 21  ? 11.266  6.403   14.782  1.00 35.13  ? 20  ALA A CA  1 
ATOM   2297 C C   . ALA B 1 21  ? 10.918  5.389   13.700  1.00 37.30  ? 20  ALA A C   1 
ATOM   2298 O O   . ALA B 1 21  ? 11.298  4.221   13.822  1.00 32.76  ? 20  ALA A O   1 
ATOM   2299 C CB  . ALA B 1 21  ? 10.375  6.184   16.004  1.00 24.90  ? 20  ALA A CB  1 
ATOM   2300 N N   . GLN B 1 22  ? 10.204  5.811   12.651  1.00 33.63  ? 21  GLN A N   1 
ATOM   2301 C CA  . GLN B 1 22  ? 9.903   4.919   11.535  1.00 35.64  ? 21  GLN A CA  1 
ATOM   2302 C C   . GLN B 1 22  ? 11.168  4.389   10.879  1.00 32.35  ? 21  GLN A C   1 
ATOM   2303 O O   . GLN B 1 22  ? 11.175  3.270   10.357  1.00 42.83  ? 21  GLN A O   1 
ATOM   2304 C CB  . GLN B 1 22  ? 9.076   5.649   10.482  1.00 37.04  ? 21  GLN A CB  1 
ATOM   2305 C CG  . GLN B 1 22  ? 7.594   5.381   10.501  1.00 43.58  ? 21  GLN A CG  1 
ATOM   2306 C CD  . GLN B 1 22  ? 6.881   6.198   9.441   1.00 41.18  ? 21  GLN A CD  1 
ATOM   2307 O OE1 . GLN B 1 22  ? 7.477   7.090   8.831   1.00 28.12  ? 21  GLN A OE1 1 
ATOM   2308 N NE2 . GLN B 1 22  ? 5.609   5.895   9.209   1.00 42.24  ? 21  GLN A NE2 1 
ATOM   2309 N N   . VAL B 1 23  ? 12.233  5.179   10.873  1.00 28.10  ? 22  VAL A N   1 
ATOM   2310 C CA  . VAL B 1 23  ? 13.442  4.847   10.131  1.00 41.59  ? 22  VAL A CA  1 
ATOM   2311 C C   . VAL B 1 23  ? 14.401  4.111   11.054  1.00 37.56  ? 22  VAL A C   1 
ATOM   2312 O O   . VAL B 1 23  ? 14.678  4.564   12.171  1.00 40.42  ? 22  VAL A O   1 
ATOM   2313 C CB  . VAL B 1 23  ? 14.089  6.113   9.546   1.00 32.64  ? 22  VAL A CB  1 
ATOM   2314 C CG1 . VAL B 1 23  ? 15.316  5.756   8.724   1.00 32.13  ? 22  VAL A CG1 1 
ATOM   2315 C CG2 . VAL B 1 23  ? 13.078  6.865   8.698   1.00 27.93  ? 22  VAL A CG2 1 
ATOM   2316 N N   . GLU B 1 24  ? 14.906  2.973   10.583  1.00 44.98  ? 23  GLU A N   1 
ATOM   2317 C CA  . GLU B 1 24  ? 15.787  2.138   11.388  1.00 47.32  ? 23  GLU A CA  1 
ATOM   2318 C C   . GLU B 1 24  ? 17.036  2.907   11.800  1.00 42.23  ? 23  GLU A C   1 
ATOM   2319 O O   . GLU B 1 24  ? 17.672  3.574   10.978  1.00 45.64  ? 23  GLU A O   1 
ATOM   2320 C CB  . GLU B 1 24  ? 16.168  0.882   10.603  1.00 59.01  ? 23  GLU A CB  1 
ATOM   2321 C CG  . GLU B 1 24  ? 17.423  0.180   11.103  1.00 73.11  ? 23  GLU A CG  1 
ATOM   2322 C CD  . GLU B 1 24  ? 17.444  -1.299  10.759  1.00 78.55  ? 23  GLU A CD  1 
ATOM   2323 O OE1 . GLU B 1 24  ? 17.360  -2.131  11.689  1.00 82.00  ? 23  GLU A OE1 1 
ATOM   2324 O OE2 . GLU B 1 24  ? 17.542  -1.631  9.558   1.00 73.73  ? 23  GLU A OE2 1 
ATOM   2325 N N   . GLY B 1 25  ? 17.377  2.822   13.084  1.00 44.70  ? 24  GLY A N   1 
ATOM   2326 C CA  . GLY B 1 25  ? 18.569  3.452   13.608  1.00 51.62  ? 24  GLY A CA  1 
ATOM   2327 C C   . GLY B 1 25  ? 18.353  4.791   14.275  1.00 48.94  ? 24  GLY A C   1 
ATOM   2328 O O   . GLY B 1 25  ? 19.336  5.435   14.663  1.00 56.58  ? 24  GLY A O   1 
ATOM   2329 N N   . ASN B 1 26  ? 17.110  5.234   14.418  1.00 42.60  ? 25  ASN A N   1 
ATOM   2330 C CA  . ASN B 1 26  ? 16.805  6.496   15.072  1.00 38.13  ? 25  ASN A CA  1 
ATOM   2331 C C   . ASN B 1 26  ? 16.143  6.237   16.417  1.00 39.68  ? 25  ASN A C   1 
ATOM   2332 O O   . ASN B 1 26  ? 15.282  5.359   16.540  1.00 36.26  ? 25  ASN A O   1 
ATOM   2333 C CB  . ASN B 1 26  ? 15.901  7.364   14.195  1.00 35.89  ? 25  ASN A CB  1 
ATOM   2334 C CG  . ASN B 1 26  ? 16.661  8.041   13.072  1.00 41.23  ? 25  ASN A CG  1 
ATOM   2335 O OD1 . ASN B 1 26  ? 17.850  8.334   13.205  1.00 36.41  ? 25  ASN A OD1 1 
ATOM   2336 N ND2 . ASN B 1 26  ? 15.978  8.293   11.956  1.00 35.89  ? 25  ASN A ND2 1 
ATOM   2337 N N   . THR B 1 27  ? 16.565  6.993   17.426  1.00 36.99  ? 26  THR A N   1 
ATOM   2338 C CA  . THR B 1 27  ? 15.914  7.011   18.726  1.00 33.86  ? 26  THR A CA  1 
ATOM   2339 C C   . THR B 1 27  ? 15.329  8.395   18.961  1.00 40.80  ? 26  THR A C   1 
ATOM   2340 O O   . THR B 1 27  ? 15.908  9.404   18.542  1.00 38.12  ? 26  THR A O   1 
ATOM   2341 C CB  . THR B 1 27  ? 16.886  6.647   19.850  1.00 33.94  ? 26  THR A CB  1 
ATOM   2342 O OG1 . THR B 1 27  ? 18.169  7.227   19.583  1.00 48.00  ? 26  THR A OG1 1 
ATOM   2343 C CG2 . THR B 1 27  ? 17.028  5.140   19.949  1.00 41.16  ? 26  THR A CG2 1 
ATOM   2344 N N   . VAL B 1 28  ? 14.177  8.438   19.622  1.00 29.08  ? 27  VAL A N   1 
ATOM   2345 C CA  . VAL B 1 28  ? 13.420  9.669   19.802  1.00 29.22  ? 27  VAL A CA  1 
ATOM   2346 C C   . VAL B 1 28  ? 13.114  9.849   21.281  1.00 28.43  ? 27  VAL A C   1 
ATOM   2347 O O   . VAL B 1 28  ? 12.694  8.902   21.954  1.00 29.83  ? 27  VAL A O   1 
ATOM   2348 C CB  . VAL B 1 28  ? 12.119  9.661   18.976  1.00 18.76  ? 27  VAL A CB  1 
ATOM   2349 C CG1 . VAL B 1 28  ? 11.235  10.846  19.354  1.00 28.33  ? 27  VAL A CG1 1 
ATOM   2350 C CG2 . VAL B 1 28  ? 12.441  9.694   17.494  1.00 33.06  ? 27  VAL A CG2 1 
ATOM   2351 N N   . ALA B 1 29  ? 13.326  11.061  21.782  1.00 28.72  ? 28  ALA A N   1 
ATOM   2352 C CA  . ALA B 1 29  ? 12.920  11.443  23.129  1.00 28.42  ? 28  ALA A CA  1 
ATOM   2353 C C   . ALA B 1 29  ? 11.678  12.321  23.012  1.00 33.35  ? 28  ALA A C   1 
ATOM   2354 O O   . ALA B 1 29  ? 11.766  13.480  22.591  1.00 32.55  ? 28  ALA A O   1 
ATOM   2355 C CB  . ALA B 1 29  ? 14.051  12.170  23.853  1.00 22.03  ? 28  ALA A CB  1 
ATOM   2356 N N   . LEU B 1 30  ? 10.521  11.763  23.364  1.00 31.69  ? 29  LEU A N   1 
ATOM   2357 C CA  . LEU B 1 30  ? 9.253   12.492  23.338  1.00 30.51  ? 29  LEU A CA  1 
ATOM   2358 C C   . LEU B 1 30  ? 9.061   13.154  24.696  1.00 35.88  ? 29  LEU A C   1 
ATOM   2359 O O   . LEU B 1 30  ? 8.662   12.505  25.665  1.00 38.11  ? 29  LEU A O   1 
ATOM   2360 C CB  . LEU B 1 30  ? 8.099   11.554  23.005  1.00 25.60  ? 29  LEU A CB  1 
ATOM   2361 C CG  . LEU B 1 30  ? 6.727   12.208  22.812  1.00 34.96  ? 29  LEU A CG  1 
ATOM   2362 C CD1 . LEU B 1 30  ? 6.766   13.242  21.690  1.00 32.93  ? 29  LEU A CD1 1 
ATOM   2363 C CD2 . LEU B 1 30  ? 5.638   11.165  22.555  1.00 27.81  ? 29  LEU A CD2 1 
ATOM   2364 N N   . CYS B 1 31  ? 9.338   14.452  24.770  1.00 33.44  ? 30  CYS A N   1 
ATOM   2365 C CA  . CYS B 1 31  ? 9.289   15.192  26.021  1.00 30.30  ? 30  CYS A CA  1 
ATOM   2366 C C   . CYS B 1 31  ? 8.097   16.139  26.056  1.00 39.85  ? 30  CYS A C   1 
ATOM   2367 O O   . CYS B 1 31  ? 7.543   16.527  25.023  1.00 40.41  ? 30  CYS A O   1 
ATOM   2368 C CB  . CYS B 1 31  ? 10.576  15.994  26.237  1.00 33.75  ? 30  CYS A CB  1 
ATOM   2369 S SG  . CYS B 1 31  ? 12.073  15.128  25.754  1.00 43.24  ? 30  CYS A SG  1 
ATOM   2370 N N   . ASP B 1 32  ? 7.713   16.508  27.274  1.00 39.41  ? 31  ASP A N   1 
ATOM   2371 C CA  . ASP B 1 32  ? 6.705   17.530  27.513  1.00 40.84  ? 31  ASP A CA  1 
ATOM   2372 C C   . ASP B 1 32  ? 7.007   18.166  28.864  1.00 35.85  ? 31  ASP A C   1 
ATOM   2373 O O   . ASP B 1 32  ? 8.042   17.890  29.479  1.00 39.46  ? 31  ASP A O   1 
ATOM   2374 C CB  . ASP B 1 32  ? 5.289   16.942  27.450  1.00 40.28  ? 31  ASP A CB  1 
ATOM   2375 C CG  . ASP B 1 32  ? 4.291   17.890  26.797  1.00 46.97  ? 31  ASP A CG  1 
ATOM   2376 O OD1 . ASP B 1 32  ? 3.420   17.411  26.037  1.00 43.28  ? 31  ASP A OD1 1 
ATOM   2377 O OD2 . ASP B 1 32  ? 4.389   19.116  27.030  1.00 43.87  ? 31  ASP A OD2 1 
ATOM   2378 N N   . ILE B 1 33  ? 6.103   19.024  29.335  1.00 31.03  ? 32  ILE A N   1 
ATOM   2379 C CA  . ILE B 1 33  ? 6.346   19.683  30.613  1.00 45.30  ? 32  ILE A CA  1 
ATOM   2380 C C   . ILE B 1 33  ? 5.975   18.785  31.789  1.00 41.70  ? 32  ILE A C   1 
ATOM   2381 O O   . ILE B 1 33  ? 6.423   19.033  32.915  1.00 42.85  ? 32  ILE A O   1 
ATOM   2382 C CB  . ILE B 1 33  ? 5.604   21.032  30.674  1.00 42.39  ? 32  ILE A CB  1 
ATOM   2383 C CG1 . ILE B 1 33  ? 6.470   22.083  31.374  1.00 47.36  ? 32  ILE A CG1 1 
ATOM   2384 C CG2 . ILE B 1 33  ? 4.266   20.891  31.380  1.00 43.81  ? 32  ILE A CG2 1 
ATOM   2385 C CD1 . ILE B 1 33  ? 6.061   23.514  31.080  1.00 55.17  ? 32  ILE A CD1 1 
ATOM   2386 N N   . LYS B 1 34  ? 5.188   17.735  31.555  1.00 36.70  ? 33  LYS A N   1 
ATOM   2387 C CA  . LYS B 1 34  ? 4.813   16.781  32.589  1.00 41.26  ? 33  LYS A CA  1 
ATOM   2388 C C   . LYS B 1 34  ? 5.131   15.374  32.104  1.00 41.49  ? 33  LYS A C   1 
ATOM   2389 O O   . LYS B 1 34  ? 4.818   15.022  30.961  1.00 39.36  ? 33  LYS A O   1 
ATOM   2390 C CB  . LYS B 1 34  ? 3.326   16.895  32.945  1.00 45.47  ? 33  LYS A CB  1 
ATOM   2391 C CG  . LYS B 1 34  ? 2.932   18.223  33.572  1.00 43.86  ? 33  LYS A CG  1 
ATOM   2392 C CD  . LYS B 1 34  ? 2.646   18.075  35.056  1.00 61.84  ? 33  LYS A CD  1 
ATOM   2393 C CE  . LYS B 1 34  ? 3.895   18.329  35.888  1.00 60.31  ? 33  LYS A CE  1 
ATOM   2394 N NZ  . LYS B 1 34  ? 3.795   17.702  37.235  1.00 50.02  ? 33  LYS A NZ  1 
ATOM   2395 N N   . GLN B 1 35  ? 5.752   14.577  32.978  1.00 41.81  ? 34  GLN A N   1 
ATOM   2396 C CA  . GLN B 1 35  ? 6.119   13.209  32.625  1.00 37.86  ? 34  GLN A CA  1 
ATOM   2397 C C   . GLN B 1 35  ? 4.902   12.400  32.186  1.00 43.34  ? 34  GLN A C   1 
ATOM   2398 O O   . GLN B 1 35  ? 4.984   11.596  31.249  1.00 33.52  ? 34  GLN A O   1 
ATOM   2399 C CB  . GLN B 1 35  ? 6.816   12.546  33.814  1.00 28.73  ? 34  GLN A CB  1 
ATOM   2400 C CG  . GLN B 1 35  ? 7.188   11.093  33.598  1.00 36.66  ? 34  GLN A CG  1 
ATOM   2401 C CD  . GLN B 1 35  ? 8.449   10.937  32.775  1.00 40.11  ? 34  GLN A CD  1 
ATOM   2402 O OE1 . GLN B 1 35  ? 9.407   11.697  32.934  1.00 34.95  ? 34  GLN A OE1 1 
ATOM   2403 N NE2 . GLN B 1 35  ? 8.452   9.955   31.878  1.00 36.34  ? 34  GLN A NE2 1 
ATOM   2404 N N   . GLU B 1 36  ? 3.760   12.610  32.845  1.00 37.72  ? 35  GLU A N   1 
ATOM   2405 C CA  . GLU B 1 36  ? 2.544   11.887  32.481  1.00 41.98  ? 35  GLU A CA  1 
ATOM   2406 C C   . GLU B 1 36  ? 2.101   12.225  31.063  1.00 37.84  ? 35  GLU A C   1 
ATOM   2407 O O   . GLU B 1 36  ? 1.651   11.345  30.321  1.00 38.40  ? 35  GLU A O   1 
ATOM   2408 C CB  . GLU B 1 36  ? 1.428   12.198  33.482  1.00 42.79  ? 35  GLU A CB  1 
ATOM   2409 C CG  . GLU B 1 36  ? 1.909   12.394  34.921  1.00 59.86  ? 35  GLU A CG  1 
ATOM   2410 C CD  . GLU B 1 36  ? 2.352   13.823  35.211  1.00 69.61  ? 35  GLU A CD  1 
ATOM   2411 O OE1 . GLU B 1 36  ? 1.532   14.754  35.026  1.00 66.51  ? 35  GLU A OE1 1 
ATOM   2412 O OE2 . GLU B 1 36  ? 3.518   14.012  35.627  1.00 58.52  ? 35  GLU A OE2 1 
ATOM   2413 N N   . TRP B 1 37  ? 2.216   13.497  30.671  1.00 29.95  ? 36  TRP A N   1 
ATOM   2414 C CA  . TRP B 1 37  ? 1.848   13.890  29.315  1.00 32.27  ? 36  TRP A CA  1 
ATOM   2415 C C   . TRP B 1 37  ? 2.699   13.164  28.282  1.00 33.58  ? 36  TRP A C   1 
ATOM   2416 O O   . TRP B 1 37  ? 2.180   12.667  27.277  1.00 35.69  ? 36  TRP A O   1 
ATOM   2417 C CB  . TRP B 1 37  ? 1.991   15.402  29.145  1.00 35.94  ? 36  TRP A CB  1 
ATOM   2418 C CG  . TRP B 1 37  ? 1.032   16.212  29.956  1.00 37.64  ? 36  TRP A CG  1 
ATOM   2419 C CD1 . TRP B 1 37  ? 0.040   15.746  30.767  1.00 46.92  ? 36  TRP A CD1 1 
ATOM   2420 C CD2 . TRP B 1 37  ? 0.970   17.642  30.025  1.00 49.17  ? 36  TRP A CD2 1 
ATOM   2421 N NE1 . TRP B 1 37  ? -0.633  16.798  31.343  1.00 53.44  ? 36  TRP A NE1 1 
ATOM   2422 C CE2 . TRP B 1 37  ? -0.081  17.972  30.902  1.00 47.36  ? 36  TRP A CE2 1 
ATOM   2423 C CE3 . TRP B 1 37  ? 1.705   18.674  29.430  1.00 49.76  ? 36  TRP A CE3 1 
ATOM   2424 C CZ2 . TRP B 1 37  ? -0.416  19.291  31.199  1.00 51.72  ? 36  TRP A CZ2 1 
ATOM   2425 C CZ3 . TRP B 1 37  ? 1.368   19.982  29.723  1.00 48.85  ? 36  TRP A CZ3 1 
ATOM   2426 C CH2 . TRP B 1 37  ? 0.319   20.279  30.602  1.00 57.15  ? 36  TRP A CH2 1 
ATOM   2427 N N   . ALA B 1 38  ? 4.012   13.094  28.516  1.00 32.68  ? 37  ALA A N   1 
ATOM   2428 C CA  . ALA B 1 38  ? 4.894   12.400  27.585  1.00 37.80  ? 37  ALA A CA  1 
ATOM   2429 C C   . ALA B 1 38  ? 4.552   10.919  27.502  1.00 33.46  ? 37  ALA A C   1 
ATOM   2430 O O   . ALA B 1 38  ? 4.579   10.327  26.417  1.00 41.99  ? 37  ALA A O   1 
ATOM   2431 C CB  . ALA B 1 38  ? 6.352   12.596  27.999  1.00 33.40  ? 37  ALA A CB  1 
ATOM   2432 N N   . GLU B 1 39  ? 4.221   10.302  28.638  1.00 37.81  ? 38  GLU A N   1 
ATOM   2433 C CA  . GLU B 1 39  ? 3.818   8.900   28.622  1.00 41.26  ? 38  GLU A CA  1 
ATOM   2434 C C   . GLU B 1 39  ? 2.461   8.712   27.956  1.00 35.88  ? 38  GLU A C   1 
ATOM   2435 O O   . GLU B 1 39  ? 2.220   7.671   27.334  1.00 45.65  ? 38  GLU A O   1 
ATOM   2436 C CB  . GLU B 1 39  ? 3.798   8.343   30.045  1.00 36.21  ? 38  GLU A CB  1 
ATOM   2437 C CG  . GLU B 1 39  ? 5.142   7.826   30.519  1.00 42.14  ? 38  GLU A CG  1 
ATOM   2438 C CD  . GLU B 1 39  ? 5.278   7.844   32.031  1.00 62.73  ? 38  GLU A CD  1 
ATOM   2439 O OE1 . GLU B 1 39  ? 4.309   7.461   32.726  1.00 55.62  ? 38  GLU A OE1 1 
ATOM   2440 O OE2 . GLU B 1 39  ? 6.361   8.230   32.524  1.00 55.32  ? 38  GLU A OE2 1 
ATOM   2441 N N   . ASN B 1 40  ? 1.564   9.696   28.075  1.00 36.46  ? 39  ASN A N   1 
ATOM   2442 C CA  . ASN B 1 40  ? 0.286   9.611   27.374  1.00 33.32  ? 39  ASN A CA  1 
ATOM   2443 C C   . ASN B 1 40  ? 0.461   9.784   25.873  1.00 38.48  ? 39  ASN A C   1 
ATOM   2444 O O   . ASN B 1 40  ? -0.293  9.192   25.091  1.00 35.35  ? 39  ASN A O   1 
ATOM   2445 C CB  . ASN B 1 40  ? -0.690  10.658  27.908  1.00 33.34  ? 39  ASN A CB  1 
ATOM   2446 C CG  . ASN B 1 40  ? -1.400  10.206  29.162  1.00 45.42  ? 39  ASN A CG  1 
ATOM   2447 O OD1 . ASN B 1 40  ? -0.927  10.433  30.274  1.00 42.42  ? 39  ASN A OD1 1 
ATOM   2448 N ND2 . ASN B 1 40  ? -2.544  9.557   28.991  1.00 58.64  ? 39  ASN A ND2 1 
ATOM   2449 N N   . GLY B 1 41  ? 1.434   10.596  25.455  1.00 35.57  ? 40  GLY A N   1 
ATOM   2450 C CA  . GLY B 1 41  ? 1.712   10.730  24.035  1.00 31.09  ? 40  GLY A CA  1 
ATOM   2451 C C   . GLY B 1 41  ? 2.173   9.428   23.409  1.00 33.73  ? 40  GLY A C   1 
ATOM   2452 O O   . GLY B 1 41  ? 1.702   9.048   22.333  1.00 34.03  ? 40  GLY A O   1 
ATOM   2453 N N   . LEU B 1 42  ? 3.096   8.726   24.073  1.00 32.43  ? 41  LEU A N   1 
ATOM   2454 C CA  . LEU B 1 42  ? 3.545   7.433   23.570  1.00 35.38  ? 41  LEU A CA  1 
ATOM   2455 C C   . LEU B 1 42  ? 2.422   6.407   23.589  1.00 36.13  ? 41  LEU A C   1 
ATOM   2456 O O   . LEU B 1 42  ? 2.348   5.558   22.695  1.00 39.89  ? 41  LEU A O   1 
ATOM   2457 C CB  . LEU B 1 42  ? 4.737   6.930   24.385  1.00 29.22  ? 41  LEU A CB  1 
ATOM   2458 C CG  . LEU B 1 42  ? 5.435   5.652   23.909  1.00 32.22  ? 41  LEU A CG  1 
ATOM   2459 C CD1 . LEU B 1 42  ? 5.645   5.656   22.404  1.00 27.23  ? 41  LEU A CD1 1 
ATOM   2460 C CD2 . LEU B 1 42  ? 6.763   5.448   24.634  1.00 34.71  ? 41  LEU A CD2 1 
ATOM   2461 N N   . ALA B 1 43  ? 1.539   6.472   24.589  1.00 41.23  ? 42  ALA A N   1 
ATOM   2462 C CA  . ALA B 1 43  ? 0.406   5.552   24.631  1.00 33.27  ? 42  ALA A CA  1 
ATOM   2463 C C   . ALA B 1 43  ? -0.519  5.763   23.440  1.00 44.54  ? 42  ALA A C   1 
ATOM   2464 O O   . ALA B 1 43  ? -0.998  4.795   22.836  1.00 46.82  ? 42  ALA A O   1 
ATOM   2465 C CB  . ALA B 1 43  ? -0.360  5.720   25.942  1.00 33.71  ? 42  ALA A CB  1 
ATOM   2466 N N   . LYS B 1 44  ? -0.776  7.025   23.083  1.00 41.58  ? 43  LYS A N   1 
ATOM   2467 C CA  . LYS B 1 44  ? -1.564  7.307   21.887  1.00 47.24  ? 43  LYS A CA  1 
ATOM   2468 C C   . LYS B 1 44  ? -0.839  6.834   20.634  1.00 40.21  ? 43  LYS A C   1 
ATOM   2469 O O   . LYS B 1 44  ? -1.467  6.339   19.691  1.00 40.13  ? 43  LYS A O   1 
ATOM   2470 C CB  . LYS B 1 44  ? -1.874  8.804   21.803  1.00 42.67  ? 43  LYS A CB  1 
ATOM   2471 C CG  . LYS B 1 44  ? -3.271  9.183   22.294  1.00 52.13  ? 43  LYS A CG  1 
ATOM   2472 C CD  . LYS B 1 44  ? -3.351  10.655  22.696  1.00 62.69  ? 43  LYS A CD  1 
ATOM   2473 C CE  . LYS B 1 44  ? -3.575  11.555  21.485  1.00 59.28  ? 43  LYS A CE  1 
ATOM   2474 N NZ  . LYS B 1 44  ? -3.350  12.998  21.797  1.00 56.66  ? 43  LYS A NZ  1 
ATOM   2475 N N   . ILE B 1 45  ? 0.488   6.977   20.609  1.00 37.25  ? 44  ILE A N   1 
ATOM   2476 C CA  . ILE B 1 45  ? 1.275   6.464   19.491  1.00 38.04  ? 44  ILE A CA  1 
ATOM   2477 C C   . ILE B 1 45  ? 1.157   4.949   19.414  1.00 38.25  ? 44  ILE A C   1 
ATOM   2478 O O   . ILE B 1 45  ? 0.991   4.374   18.331  1.00 34.36  ? 44  ILE A O   1 
ATOM   2479 C CB  . ILE B 1 45  ? 2.746   6.901   19.629  1.00 33.88  ? 44  ILE A CB  1 
ATOM   2480 C CG1 . ILE B 1 45  ? 2.929   8.360   19.206  1.00 33.74  ? 44  ILE A CG1 1 
ATOM   2481 C CG2 . ILE B 1 45  ? 3.655   5.982   18.823  1.00 33.31  ? 44  ILE A CG2 1 
ATOM   2482 C CD1 . ILE B 1 45  ? 4.265   8.950   19.643  1.00 21.66  ? 44  ILE A CD1 1 
ATOM   2483 N N   . LYS B 1 46  ? 1.232   4.279   20.565  1.00 39.30  ? 45  LYS A N   1 
ATOM   2484 C CA  . LYS B 1 46  ? 1.243   2.821   20.575  1.00 44.31  ? 45  LYS A CA  1 
ATOM   2485 C C   . LYS B 1 46  ? -0.107  2.257   20.152  1.00 44.83  ? 45  LYS A C   1 
ATOM   2486 O O   . LYS B 1 46  ? -0.176  1.374   19.291  1.00 44.88  ? 45  LYS A O   1 
ATOM   2487 C CB  . LYS B 1 46  ? 1.635   2.311   21.960  1.00 31.86  ? 45  LYS A CB  1 
ATOM   2488 C CG  . LYS B 1 46  ? 1.616   0.801   22.098  1.00 44.39  ? 45  LYS A CG  1 
ATOM   2489 C CD  . LYS B 1 46  ? 1.240   0.399   23.514  1.00 57.03  ? 45  LYS A CD  1 
ATOM   2490 C CE  . LYS B 1 46  ? 1.691   -1.013  23.835  1.00 55.72  ? 45  LYS A CE  1 
ATOM   2491 N NZ  . LYS B 1 46  ? 1.157   -1.458  25.154  1.00 65.57  ? 45  LYS A NZ  1 
ATOM   2492 N N   . LYS B 1 47  ? -1.196  2.762   20.737  1.00 48.79  ? 46  LYS A N   1 
ATOM   2493 C CA  . LYS B 1 47  ? -2.512  2.231   20.399  1.00 53.82  ? 46  LYS A CA  1 
ATOM   2494 C C   . LYS B 1 47  ? -2.865  2.497   18.943  1.00 48.15  ? 46  LYS A C   1 
ATOM   2495 O O   . LYS B 1 47  ? -3.550  1.683   18.313  1.00 55.26  ? 46  LYS A O   1 
ATOM   2496 C CB  . LYS B 1 47  ? -3.578  2.813   21.330  1.00 60.88  ? 46  LYS A CB  1 
ATOM   2497 C CG  . LYS B 1 47  ? -3.309  2.565   22.815  1.00 74.40  ? 46  LYS A CG  1 
ATOM   2498 C CD  . LYS B 1 47  ? -3.795  1.188   23.262  1.00 84.51  ? 46  LYS A CD  1 
ATOM   2499 C CE  . LYS B 1 47  ? -2.786  0.515   24.186  1.00 81.01  ? 46  LYS A CE  1 
ATOM   2500 N NZ  . LYS B 1 47  ? -2.744  -0.963  23.992  1.00 79.69  ? 46  LYS A NZ  1 
ATOM   2501 N N   . GLY B 1 48  ? -2.398  3.616   18.387  1.00 47.90  ? 47  GLY A N   1 
ATOM   2502 C CA  . GLY B 1 48  ? -2.589  3.855   16.966  1.00 43.28  ? 47  GLY A CA  1 
ATOM   2503 C C   . GLY B 1 48  ? -1.897  2.824   16.096  1.00 47.62  ? 47  GLY A C   1 
ATOM   2504 O O   . GLY B 1 48  ? -2.344  2.545   14.981  1.00 43.82  ? 47  GLY A O   1 
ATOM   2505 N N   . TYR B 1 49  ? -0.804  2.239   16.592  1.00 47.38  ? 48  TYR A N   1 
ATOM   2506 C CA  . TYR B 1 49  ? -0.085  1.227   15.827  1.00 48.71  ? 48  TYR A CA  1 
ATOM   2507 C C   . TYR B 1 49  ? -0.742  -0.144  15.922  1.00 52.23  ? 48  TYR A C   1 
ATOM   2508 O O   . TYR B 1 49  ? -0.611  -0.948  14.993  1.00 53.76  ? 48  TYR A O   1 
ATOM   2509 C CB  . TYR B 1 49  ? 1.369   1.143   16.296  1.00 42.76  ? 48  TYR A CB  1 
ATOM   2510 C CG  . TYR B 1 49  ? 2.297   2.072   15.550  1.00 46.40  ? 48  TYR A CG  1 
ATOM   2511 C CD1 . TYR B 1 49  ? 2.453   1.974   14.172  1.00 39.63  ? 48  TYR A CD1 1 
ATOM   2512 C CD2 . TYR B 1 49  ? 3.012   3.053   16.222  1.00 44.87  ? 48  TYR A CD2 1 
ATOM   2513 C CE1 . TYR B 1 49  ? 3.298   2.826   13.486  1.00 33.03  ? 48  TYR A CE1 1 
ATOM   2514 C CE2 . TYR B 1 49  ? 3.857   3.910   15.546  1.00 42.43  ? 48  TYR A CE2 1 
ATOM   2515 C CZ  . TYR B 1 49  ? 3.998   3.794   14.181  1.00 39.16  ? 48  TYR A CZ  1 
ATOM   2516 O OH  . TYR B 1 49  ? 4.844   4.650   13.515  1.00 28.41  ? 48  TYR A OH  1 
ATOM   2517 N N   . GLU B 1 50  ? -1.439  -0.435  17.026  1.00 50.35  ? 49  GLU A N   1 
ATOM   2518 C CA  . GLU B 1 50  ? -2.116  -1.724  17.143  1.00 49.80  ? 49  GLU A CA  1 
ATOM   2519 C C   . GLU B 1 50  ? -3.321  -1.795  16.218  1.00 48.79  ? 49  GLU A C   1 
ATOM   2520 O O   . GLU B 1 50  ? -3.608  -2.855  15.649  1.00 56.82  ? 49  GLU A O   1 
ATOM   2521 C CB  . GLU B 1 50  ? -2.539  -1.987  18.589  1.00 55.36  ? 49  GLU A CB  1 
ATOM   2522 C CG  . GLU B 1 50  ? -1.736  -1.235  19.631  1.00 58.88  ? 49  GLU A CG  1 
ATOM   2523 C CD  . GLU B 1 50  ? -2.220  -1.498  21.045  1.00 66.84  ? 49  GLU A CD  1 
ATOM   2524 O OE1 . GLU B 1 50  ? -3.438  -1.368  21.298  1.00 67.66  ? 49  GLU A OE1 1 
ATOM   2525 O OE2 . GLU B 1 50  ? -1.380  -1.833  21.908  1.00 70.20  ? 49  GLU A OE2 1 
ATOM   2526 N N   . LYS B 1 51  ? -4.047  -0.685  16.064  1.00 47.78  ? 50  LYS A N   1 
ATOM   2527 C CA  . LYS B 1 51  ? -5.104  -0.640  15.058  1.00 56.33  ? 50  LYS A CA  1 
ATOM   2528 C C   . LYS B 1 51  ? -4.539  -0.857  13.660  1.00 56.36  ? 50  LYS A C   1 
ATOM   2529 O O   . LYS B 1 51  ? -5.216  -1.425  12.795  1.00 55.23  ? 50  LYS A O   1 
ATOM   2530 C CB  . LYS B 1 51  ? -5.856  0.693   15.131  1.00 55.17  ? 50  LYS A CB  1 
ATOM   2531 C CG  . LYS B 1 51  ? -6.578  0.939   16.454  1.00 59.68  ? 50  LYS A CG  1 
ATOM   2532 C CD  . LYS B 1 51  ? -7.662  2.011   16.326  1.00 66.19  ? 50  LYS A CD  1 
ATOM   2533 C CE  . LYS B 1 51  ? -8.437  1.883   15.016  1.00 66.93  ? 50  LYS A CE  1 
ATOM   2534 N NZ  . LYS B 1 51  ? -8.752  3.209   14.409  1.00 49.37  ? 50  LYS A NZ  1 
ATOM   2535 N N   . LEU B 1 52  ? -3.298  -0.425  13.427  1.00 53.27  ? 51  LEU A N   1 
ATOM   2536 C CA  . LEU B 1 52  ? -2.667  -0.634  12.129  1.00 51.18  ? 51  LEU A CA  1 
ATOM   2537 C C   . LEU B 1 52  ? -2.272  -2.094  11.940  1.00 53.05  ? 51  LEU A C   1 
ATOM   2538 O O   . LEU B 1 52  ? -2.404  -2.641  10.839  1.00 49.36  ? 51  LEU A O   1 
ATOM   2539 C CB  . LEU B 1 52  ? -1.450  0.279   11.995  1.00 41.51  ? 51  LEU A CB  1 
ATOM   2540 C CG  . LEU B 1 52  ? -1.648  1.577   11.213  1.00 49.71  ? 51  LEU A CG  1 
ATOM   2541 C CD1 . LEU B 1 52  ? -0.365  2.387   11.201  1.00 48.01  ? 51  LEU A CD1 1 
ATOM   2542 C CD2 . LEU B 1 52  ? -2.113  1.281   9.797   1.00 44.36  ? 51  LEU A CD2 1 
ATOM   2543 N N   . VAL B 1 53  ? -1.783  -2.738  13.002  1.00 47.35  ? 52  VAL A N   1 
ATOM   2544 C CA  . VAL B 1 53  ? -1.445  -4.157  12.927  1.00 55.55  ? 52  VAL A CA  1 
ATOM   2545 C C   . VAL B 1 53  ? -2.698  -4.988  12.678  1.00 56.23  ? 52  VAL A C   1 
ATOM   2546 O O   . VAL B 1 53  ? -2.720  -5.864  11.804  1.00 43.52  ? 52  VAL A O   1 
ATOM   2547 C CB  . VAL B 1 53  ? -0.714  -4.599  14.208  1.00 51.57  ? 52  VAL A CB  1 
ATOM   2548 C CG1 . VAL B 1 53  ? -0.761  -6.111  14.358  1.00 42.13  ? 52  VAL A CG1 1 
ATOM   2549 C CG2 . VAL B 1 53  ? 0.725   -4.103  14.201  1.00 45.68  ? 52  VAL A CG2 1 
ATOM   2550 N N   . ALA B 1 54  ? -3.764  -4.717  13.439  1.00 56.51  ? 53  ALA A N   1 
ATOM   2551 C CA  . ALA B 1 54  ? -5.021  -5.439  13.256  1.00 57.73  ? 53  ALA A CA  1 
ATOM   2552 C C   . ALA B 1 54  ? -5.570  -5.249  11.848  1.00 57.70  ? 53  ALA A C   1 
ATOM   2553 O O   . ALA B 1 54  ? -6.129  -6.183  11.260  1.00 62.09  ? 53  ALA A O   1 
ATOM   2554 C CB  . ALA B 1 54  ? -6.044  -4.982  14.296  1.00 51.46  ? 53  ALA A CB  1 
ATOM   2555 N N   . LYS B 1 55  ? -5.422  -4.044  11.291  1.00 55.50  ? 54  LYS A N   1 
ATOM   2556 C CA  . LYS B 1 55  ? -5.798  -3.783  9.906   1.00 57.09  ? 54  LYS A CA  1 
ATOM   2557 C C   . LYS B 1 55  ? -4.848  -4.434  8.910   1.00 54.48  ? 54  LYS A C   1 
ATOM   2558 O O   . LYS B 1 55  ? -5.055  -4.292  7.699   1.00 54.78  ? 54  LYS A O   1 
ATOM   2559 C CB  . LYS B 1 55  ? -5.862  -2.274  9.654   1.00 52.63  ? 54  LYS A CB  1 
ATOM   2560 C CG  . LYS B 1 55  ? -7.130  -1.594  10.164  1.00 59.64  ? 54  LYS A CG  1 
ATOM   2561 C CD  . LYS B 1 55  ? -8.386  -2.198  9.548   1.00 65.06  ? 54  LYS A CD  1 
ATOM   2562 C CE  . LYS B 1 55  ? -9.390  -2.612  10.617  1.00 71.20  ? 54  LYS A CE  1 
ATOM   2563 N NZ  . LYS B 1 55  ? -10.796 -2.588  10.116  1.00 61.28  ? 54  LYS A NZ  1 
ATOM   2564 N N   . GLY B 1 56  ? -3.819  -5.133  9.386   1.00 53.67  ? 55  GLY A N   1 
ATOM   2565 C CA  . GLY B 1 56  ? -2.907  -5.839  8.512   1.00 49.48  ? 55  GLY A CA  1 
ATOM   2566 C C   . GLY B 1 56  ? -2.025  -4.957  7.663   1.00 59.08  ? 55  GLY A C   1 
ATOM   2567 O O   . GLY B 1 56  ? -1.480  -5.428  6.663   1.00 62.36  ? 55  GLY A O   1 
ATOM   2568 N N   . LYS B 1 57  ? -1.860  -3.687  8.034   1.00 60.20  ? 56  LYS A N   1 
ATOM   2569 C CA  . LYS B 1 57  ? -1.099  -2.739  7.232   1.00 57.93  ? 56  LYS A CA  1 
ATOM   2570 C C   . LYS B 1 57  ? 0.281   -2.443  7.811   1.00 55.08  ? 56  LYS A C   1 
ATOM   2571 O O   . LYS B 1 57  ? 0.915   -1.464  7.403   1.00 58.13  ? 56  LYS A O   1 
ATOM   2572 C CB  . LYS B 1 57  ? -1.890  -1.441  7.051   1.00 54.56  ? 56  LYS A CB  1 
ATOM   2573 C CG  . LYS B 1 57  ? -3.056  -1.565  6.076   1.00 57.83  ? 56  LYS A CG  1 
ATOM   2574 C CD  . LYS B 1 57  ? -3.862  -0.279  5.992   1.00 60.07  ? 56  LYS A CD  1 
ATOM   2575 C CE  . LYS B 1 57  ? -4.492  0.068   7.333   1.00 71.99  ? 56  LYS A CE  1 
ATOM   2576 N NZ  . LYS B 1 57  ? -4.924  1.495   7.406   1.00 70.63  ? 56  LYS A NZ  1 
ATOM   2577 N N   . ILE B 1 58  ? 0.762   -3.270  8.735   1.00 58.72  ? 57  ILE A N   1 
ATOM   2578 C CA  . ILE B 1 58  ? 2.106   -3.128  9.297   1.00 46.42  ? 57  ILE A CA  1 
ATOM   2579 C C   . ILE B 1 58  ? 2.477   -4.404  10.046  1.00 50.67  ? 57  ILE A C   1 
ATOM   2580 O O   . ILE B 1 58  ? 1.649   -4.947  10.794  1.00 47.87  ? 57  ILE A O   1 
ATOM   2581 C CB  . ILE B 1 58  ? 2.206   -1.897  10.214  1.00 46.79  ? 57  ILE A CB  1 
ATOM   2582 C CG1 . ILE B 1 58  ? 3.615   -1.764  10.794  1.00 44.29  ? 57  ILE A CG1 1 
ATOM   2583 C CG2 . ILE B 1 58  ? 1.182   -1.962  11.328  1.00 58.94  ? 57  ILE A CG2 1 
ATOM   2584 C CD1 . ILE B 1 58  ? 4.543   -0.932  9.948   1.00 58.17  ? 57  ILE A CD1 1 
ATOM   2585 N N   . PRO B 1 59  ? 3.680   -4.940  9.845   1.00 54.94  ? 58  PRO A N   1 
ATOM   2586 C CA  . PRO B 1 59  ? 4.122   -6.078  10.660  1.00 49.93  ? 58  PRO A CA  1 
ATOM   2587 C C   . PRO B 1 59  ? 4.082   -5.745  12.145  1.00 55.46  ? 58  PRO A C   1 
ATOM   2588 O O   . PRO B 1 59  ? 4.418   -4.635  12.563  1.00 51.25  ? 58  PRO A O   1 
ATOM   2589 C CB  . PRO B 1 59  ? 5.556   -6.330  10.184  1.00 47.38  ? 58  PRO A CB  1 
ATOM   2590 C CG  . PRO B 1 59  ? 5.688   -5.634  8.870   1.00 54.79  ? 58  PRO A CG  1 
ATOM   2591 C CD  . PRO B 1 59  ? 4.499   -4.753  8.637   1.00 55.60  ? 58  PRO A CD  1 
ATOM   2592 N N   . GLN B 1 60  ? 3.666   -6.731  12.943  1.00 59.40  ? 59  GLN A N   1 
ATOM   2593 C CA  . GLN B 1 60  ? 3.558   -6.531  14.385  1.00 51.27  ? 59  GLN A CA  1 
ATOM   2594 C C   . GLN B 1 60  ? 4.908   -6.201  15.013  1.00 58.78  ? 59  GLN A C   1 
ATOM   2595 O O   . GLN B 1 60  ? 4.973   -5.432  15.980  1.00 53.51  ? 59  GLN A O   1 
ATOM   2596 C CB  . GLN B 1 60  ? 2.948   -7.779  15.029  1.00 47.09  ? 59  GLN A CB  1 
ATOM   2597 C CG  . GLN B 1 60  ? 3.138   -7.887  16.534  1.00 52.87  ? 59  GLN A CG  1 
ATOM   2598 C CD  . GLN B 1 60  ? 2.224   -6.957  17.305  1.00 59.63  ? 59  GLN A CD  1 
ATOM   2599 O OE1 . GLN B 1 60  ? 0.997   -7.061  17.223  1.00 52.40  ? 59  GLN A OE1 1 
ATOM   2600 N NE2 . GLN B 1 60  ? 2.817   -6.038  18.061  1.00 50.01  ? 59  GLN A NE2 1 
ATOM   2601 N N   . GLU B 1 61  ? 5.994   -6.753  14.469  1.00 59.37  ? 60  GLU A N   1 
ATOM   2602 C CA  . GLU B 1 61  ? 7.315   -6.528  15.046  1.00 60.34  ? 60  GLU A CA  1 
ATOM   2603 C C   . GLU B 1 61  ? 7.855   -5.146  14.699  1.00 55.13  ? 60  GLU A C   1 
ATOM   2604 O O   . GLU B 1 61  ? 8.551   -4.530  15.514  1.00 54.50  ? 60  GLU A O   1 
ATOM   2605 C CB  . GLU B 1 61  ? 8.287   -7.613  14.579  1.00 65.59  ? 60  GLU A CB  1 
ATOM   2606 C CG  . GLU B 1 61  ? 8.044   -8.113  13.160  1.00 83.79  ? 60  GLU A CG  1 
ATOM   2607 C CD  . GLU B 1 61  ? 7.067   -9.278  13.101  1.00 89.02  ? 60  GLU A CD  1 
ATOM   2608 O OE1 . GLU B 1 61  ? 5.855   -9.052  13.316  1.00 76.49  ? 60  GLU A OE1 1 
ATOM   2609 O OE2 . GLU B 1 61  ? 7.512   -10.417 12.845  1.00 94.91  ? 60  GLU A OE2 1 
ATOM   2610 N N   . LYS B 1 62  ? 7.554   -4.645  13.498  1.00 54.86  ? 61  LYS A N   1 
ATOM   2611 C CA  . LYS B 1 62  ? 7.974   -3.293  13.142  1.00 48.23  ? 61  LYS A CA  1 
ATOM   2612 C C   . LYS B 1 62  ? 7.300   -2.260  14.038  1.00 43.77  ? 61  LYS A C   1 
ATOM   2613 O O   . LYS B 1 62  ? 7.955   -1.334  14.533  1.00 39.19  ? 61  LYS A O   1 
ATOM   2614 C CB  . LYS B 1 62  ? 7.670   -3.017  11.668  1.00 43.51  ? 61  LYS A CB  1 
ATOM   2615 C CG  . LYS B 1 62  ? 7.960   -1.588  11.222  1.00 45.88  ? 61  LYS A CG  1 
ATOM   2616 C CD  . LYS B 1 62  ? 9.407   -1.425  10.774  1.00 46.44  ? 61  LYS A CD  1 
ATOM   2617 C CE  . LYS B 1 62  ? 9.810   0.045   10.708  1.00 45.52  ? 61  LYS A CE  1 
ATOM   2618 N NZ  . LYS B 1 62  ? 11.236  0.264   11.100  1.00 45.80  ? 61  LYS A NZ  1 
ATOM   2619 N N   . ALA B 1 63  ? 5.993   -2.411  14.268  1.00 37.27  ? 62  ALA A N   1 
ATOM   2620 C CA  . ALA B 1 63  ? 5.298   -1.508  15.179  1.00 50.85  ? 62  ALA A CA  1 
ATOM   2621 C C   . ALA B 1 63  ? 5.876   -1.598  16.584  1.00 47.42  ? 62  ALA A C   1 
ATOM   2622 O O   . ALA B 1 63  ? 5.991   -0.584  17.283  1.00 47.46  ? 62  ALA A O   1 
ATOM   2623 C CB  . ALA B 1 63  ? 3.801   -1.820  15.190  1.00 45.61  ? 62  ALA A CB  1 
ATOM   2624 N N   . ASP B 1 64  ? 6.252   -2.804  17.015  1.00 51.68  ? 63  ASP A N   1 
ATOM   2625 C CA  . ASP B 1 64  ? 6.903   -2.950  18.313  1.00 50.37  ? 63  ASP A CA  1 
ATOM   2626 C C   . ASP B 1 64  ? 8.256   -2.250  18.334  1.00 46.23  ? 63  ASP A C   1 
ATOM   2627 O O   . ASP B 1 64  ? 8.667   -1.720  19.374  1.00 40.97  ? 63  ASP A O   1 
ATOM   2628 C CB  . ASP B 1 64  ? 7.063   -4.434  18.657  1.00 55.92  ? 63  ASP A CB  1 
ATOM   2629 C CG  . ASP B 1 64  ? 5.776   -5.061  19.175  1.00 63.49  ? 63  ASP A CG  1 
ATOM   2630 O OD1 . ASP B 1 64  ? 5.651   -6.303  19.104  1.00 60.80  ? 63  ASP A OD1 1 
ATOM   2631 O OD2 . ASP B 1 64  ? 4.892   -4.317  19.655  1.00 67.99  ? 63  ASP A OD2 1 
ATOM   2632 N N   . ALA B 1 65  ? 8.954   -2.230  17.197  1.00 40.56  ? 64  ALA A N   1 
ATOM   2633 C CA  . ALA B 1 65  ? 10.267  -1.597  17.126  1.00 44.54  ? 64  ALA A CA  1 
ATOM   2634 C C   . ALA B 1 65  ? 10.162  -0.077  17.142  1.00 41.42  ? 64  ALA A C   1 
ATOM   2635 O O   . ALA B 1 65  ? 10.987  0.597   17.770  1.00 37.50  ? 64  ALA A O   1 
ATOM   2636 C CB  . ALA B 1 65  ? 11.005  -2.067  15.872  1.00 39.46  ? 64  ALA A CB  1 
ATOM   2637 N N   . ILE B 1 66  ? 9.164   0.479   16.452  1.00 41.71  ? 65  ILE A N   1 
ATOM   2638 C CA  . ILE B 1 66  ? 8.976   1.928   16.445  1.00 35.82  ? 65  ILE A CA  1 
ATOM   2639 C C   . ILE B 1 66  ? 8.684   2.429   17.852  1.00 39.08  ? 65  ILE A C   1 
ATOM   2640 O O   . ILE B 1 66  ? 9.330   3.361   18.347  1.00 38.95  ? 65  ILE A O   1 
ATOM   2641 C CB  . ILE B 1 66  ? 7.852   2.319   15.471  1.00 43.12  ? 65  ILE A CB  1 
ATOM   2642 C CG1 . ILE B 1 66  ? 8.265   2.020   14.029  1.00 34.49  ? 65  ILE A CG1 1 
ATOM   2643 C CG2 . ILE B 1 66  ? 7.485   3.786   15.651  1.00 39.16  ? 65  ILE A CG2 1 
ATOM   2644 C CD1 . ILE B 1 66  ? 7.093   1.729   13.120  1.00 37.50  ? 65  ILE A CD1 1 
ATOM   2645 N N   . VAL B 1 67  ? 7.705   1.810   18.517  1.00 32.63  ? 66  VAL A N   1 
ATOM   2646 C CA  . VAL B 1 67  ? 7.344   2.218   19.871  1.00 31.76  ? 66  VAL A CA  1 
ATOM   2647 C C   . VAL B 1 67  ? 8.544   2.094   20.802  1.00 31.08  ? 66  VAL A C   1 
ATOM   2648 O O   . VAL B 1 67  ? 8.775   2.955   21.660  1.00 32.29  ? 66  VAL A O   1 
ATOM   2649 C CB  . VAL B 1 67  ? 6.142   1.392   20.372  1.00 37.83  ? 66  VAL A CB  1 
ATOM   2650 C CG1 . VAL B 1 67  ? 5.839   1.709   21.830  1.00 30.21  ? 66  VAL A CG1 1 
ATOM   2651 C CG2 . VAL B 1 67  ? 4.920   1.650   19.501  1.00 33.99  ? 66  VAL A CG2 1 
ATOM   2652 N N   . ALA B 1 68  ? 9.344   1.038   20.628  1.00 33.51  ? 67  ALA A N   1 
ATOM   2653 C CA  . ALA B 1 68  ? 10.507  0.834   21.487  1.00 28.15  ? 67  ALA A CA  1 
ATOM   2654 C C   . ALA B 1 68  ? 11.559  1.919   21.293  1.00 32.19  ? 67  ALA A C   1 
ATOM   2655 O O   . ALA B 1 68  ? 12.326  2.205   22.219  1.00 35.91  ? 67  ALA A O   1 
ATOM   2656 C CB  . ALA B 1 68  ? 11.117  -0.544  21.229  1.00 30.15  ? 67  ALA A CB  1 
ATOM   2657 N N   . ALA B 1 69  ? 11.615  2.530   20.110  1.00 31.06  ? 68  ALA A N   1 
ATOM   2658 C CA  . ALA B 1 69  ? 12.587  3.580   19.835  1.00 35.00  ? 68  ALA A CA  1 
ATOM   2659 C C   . ALA B 1 69  ? 12.193  4.933   20.422  1.00 32.62  ? 68  ALA A C   1 
ATOM   2660 O O   . ALA B 1 69  ? 12.988  5.876   20.343  1.00 34.99  ? 68  ALA A O   1 
ATOM   2661 C CB  . ALA B 1 69  ? 12.801  3.717   18.324  1.00 26.02  ? 68  ALA A CB  1 
ATOM   2662 N N   . ILE B 1 70  ? 11.002  5.051   21.009  1.00 31.04  ? 69  ILE A N   1 
ATOM   2663 C CA  . ILE B 1 70  ? 10.498  6.307   21.557  1.00 29.14  ? 69  ILE A CA  1 
ATOM   2664 C C   . ILE B 1 70  ? 10.509  6.223   23.078  1.00 32.78  ? 69  ILE A C   1 
ATOM   2665 O O   . ILE B 1 70  ? 9.912   5.310   23.661  1.00 34.31  ? 69  ILE A O   1 
ATOM   2666 C CB  . ILE B 1 70  ? 9.083   6.618   21.039  1.00 30.06  ? 69  ILE A CB  1 
ATOM   2667 C CG1 . ILE B 1 70  ? 9.071   6.662   19.510  1.00 35.10  ? 69  ILE A CG1 1 
ATOM   2668 C CG2 . ILE B 1 70  ? 8.580   7.930   21.615  1.00 29.56  ? 69  ILE A CG2 1 
ATOM   2669 C CD1 . ILE B 1 70  ? 7.682   6.733   18.917  1.00 32.89  ? 69  ILE A CD1 1 
ATOM   2670 N N   . THR B 1 71  ? 11.174  7.180   23.718  1.00 31.74  ? 70  THR A N   1 
ATOM   2671 C CA  . THR B 1 71  ? 11.231  7.265   25.166  1.00 31.17  ? 70  THR A CA  1 
ATOM   2672 C C   . THR B 1 71  ? 10.550  8.544   25.640  1.00 34.27  ? 70  THR A C   1 
ATOM   2673 O O   . THR B 1 71  ? 10.883  9.632   25.150  1.00 34.22  ? 70  THR A O   1 
ATOM   2674 C CB  . THR B 1 71  ? 12.691  7.241   25.661  1.00 37.90  ? 70  THR A CB  1 
ATOM   2675 O OG1 . THR B 1 71  ? 13.360  6.086   25.138  1.00 38.84  ? 70  THR A OG1 1 
ATOM   2676 C CG2 . THR B 1 71  ? 12.744  7.210   27.181  1.00 28.56  ? 70  THR A CG2 1 
ATOM   2677 N N   . PRO B 1 72  ? 9.605   8.465   26.574  1.00 37.92  ? 71  PRO A N   1 
ATOM   2678 C CA  . PRO B 1 72  ? 8.979   9.674   27.113  1.00 32.15  ? 71  PRO A CA  1 
ATOM   2679 C C   . PRO B 1 72  ? 9.726   10.216  28.324  1.00 32.42  ? 71  PRO A C   1 
ATOM   2680 O O   . PRO B 1 72  ? 10.443  9.498   29.024  1.00 41.88  ? 71  PRO A O   1 
ATOM   2681 C CB  . PRO B 1 72  ? 7.574   9.196   27.521  1.00 31.97  ? 71  PRO A CB  1 
ATOM   2682 C CG  . PRO B 1 72  ? 7.590   7.680   27.403  1.00 42.65  ? 71  PRO A CG  1 
ATOM   2683 C CD  . PRO B 1 72  ? 9.004   7.248   27.139  1.00 36.19  ? 71  PRO A CD  1 
ATOM   2684 N N   . GLY B 1 73  ? 9.543   11.509  28.563  1.00 35.18  ? 72  GLY A N   1 
ATOM   2685 C CA  . GLY B 1 73  ? 10.106  12.104  29.767  1.00 36.27  ? 72  GLY A CA  1 
ATOM   2686 C C   . GLY B 1 73  ? 10.153  13.622  29.670  1.00 36.73  ? 72  GLY A C   1 
ATOM   2687 O O   . GLY B 1 73  ? 9.285   14.245  29.058  1.00 29.09  ? 72  GLY A O   1 
ATOM   2688 N N   . LEU B 1 74  ? 11.175  14.189  30.310  1.00 39.91  ? 73  LEU A N   1 
ATOM   2689 C CA  . LEU B 1 74  ? 11.420  15.623  30.321  1.00 36.96  ? 73  LEU A CA  1 
ATOM   2690 C C   . LEU B 1 74  ? 12.744  15.917  29.633  1.00 37.31  ? 73  LEU A C   1 
ATOM   2691 O O   . LEU B 1 74  ? 13.676  15.108  29.678  1.00 36.06  ? 73  LEU A O   1 
ATOM   2692 C CB  . LEU B 1 74  ? 11.446  16.172  31.747  1.00 32.22  ? 73  LEU A CB  1 
ATOM   2693 C CG  . LEU B 1 74  ? 10.444  15.514  32.690  1.00 35.82  ? 73  LEU A CG  1 
ATOM   2694 C CD1 . LEU B 1 74  ? 10.708  15.933  34.127  1.00 37.84  ? 73  LEU A CD1 1 
ATOM   2695 C CD2 . LEU B 1 74  ? 9.032   15.866  32.269  1.00 28.91  ? 73  LEU A CD2 1 
ATOM   2696 N N   . LYS B 1 75  ? 12.826  17.094  29.005  1.00 35.19  ? 74  LYS A N   1 
ATOM   2697 C CA  . LYS B 1 75  ? 13.988  17.404  28.178  1.00 37.57  ? 74  LYS A CA  1 
ATOM   2698 C C   . LYS B 1 75  ? 15.266  17.498  29.001  1.00 35.09  ? 74  LYS A C   1 
ATOM   2699 O O   . LYS B 1 75  ? 16.357  17.246  28.479  1.00 36.71  ? 74  LYS A O   1 
ATOM   2700 C CB  . LYS B 1 75  ? 13.754  18.702  27.407  1.00 36.30  ? 74  LYS A CB  1 
ATOM   2701 C CG  . LYS B 1 75  ? 13.610  19.926  28.288  1.00 40.45  ? 74  LYS A CG  1 
ATOM   2702 C CD  . LYS B 1 75  ? 12.885  21.043  27.567  1.00 37.51  ? 74  LYS A CD  1 
ATOM   2703 C CE  . LYS B 1 75  ? 13.021  22.341  28.331  1.00 39.60  ? 74  LYS A CE  1 
ATOM   2704 N NZ  . LYS B 1 75  ? 12.072  22.387  29.476  1.00 44.01  ? 74  LYS A NZ  1 
ATOM   2705 N N   . GLU B 1 76  ? 15.157  17.852  30.285  1.00 33.09  ? 75  GLU A N   1 
ATOM   2706 C CA  . GLU B 1 76  ? 16.339  17.906  31.140  1.00 39.15  ? 75  GLU A CA  1 
ATOM   2707 C C   . GLU B 1 76  ? 16.969  16.530  31.316  1.00 39.82  ? 75  GLU A C   1 
ATOM   2708 O O   . GLU B 1 76  ? 18.182  16.425  31.530  1.00 40.21  ? 75  GLU A O   1 
ATOM   2709 C CB  . GLU B 1 76  ? 15.982  18.494  32.511  1.00 28.91  ? 75  GLU A CB  1 
ATOM   2710 C CG  . GLU B 1 76  ? 15.381  19.896  32.478  1.00 50.76  ? 75  GLU A CG  1 
ATOM   2711 C CD  . GLU B 1 76  ? 13.913  19.910  32.073  1.00 59.05  ? 75  GLU A CD  1 
ATOM   2712 O OE1 . GLU B 1 76  ? 13.316  18.818  31.938  1.00 51.00  ? 75  GLU A OE1 1 
ATOM   2713 O OE2 . GLU B 1 76  ? 13.361  21.016  31.887  1.00 61.38  ? 75  GLU A OE2 1 
ATOM   2714 N N   . ASN B 1 77  ? 16.170  15.467  31.219  1.00 36.39  ? 76  ASN A N   1 
ATOM   2715 C CA  . ASN B 1 77  ? 16.653  14.118  31.479  1.00 38.50  ? 76  ASN A CA  1 
ATOM   2716 C C   . ASN B 1 77  ? 17.053  13.348  30.226  1.00 36.10  ? 76  ASN A C   1 
ATOM   2717 O O   . ASN B 1 77  ? 17.872  12.429  30.328  1.00 38.92  ? 76  ASN A O   1 
ATOM   2718 C CB  . ASN B 1 77  ? 15.587  13.311  32.231  1.00 34.48  ? 76  ASN A CB  1 
ATOM   2719 C CG  . ASN B 1 77  ? 15.186  13.953  33.547  1.00 35.77  ? 76  ASN A CG  1 
ATOM   2720 O OD1 . ASN B 1 77  ? 15.996  14.597  34.213  1.00 36.10  ? 76  ASN A OD1 1 
ATOM   2721 N ND2 . ASN B 1 77  ? 13.926  13.772  33.931  1.00 32.57  ? 76  ASN A ND2 1 
ATOM   2722 N N   . LEU B 1 78  ? 16.507  13.684  29.054  1.00 34.21  ? 77  LEU A N   1 
ATOM   2723 C CA  . LEU B 1 78  ? 16.678  12.844  27.877  1.00 30.83  ? 77  LEU A CA  1 
ATOM   2724 C C   . LEU B 1 78  ? 17.374  13.508  26.700  1.00 33.16  ? 77  LEU A C   1 
ATOM   2725 O O   . LEU B 1 78  ? 17.686  12.812  25.727  1.00 34.33  ? 77  LEU A O   1 
ATOM   2726 C CB  . LEU B 1 78  ? 15.318  12.325  27.384  1.00 34.32  ? 77  LEU A CB  1 
ATOM   2727 C CG  . LEU B 1 78  ? 14.285  11.895  28.422  1.00 40.15  ? 77  LEU A CG  1 
ATOM   2728 C CD1 . LEU B 1 78  ? 12.966  11.604  27.732  1.00 40.24  ? 77  LEU A CD1 1 
ATOM   2729 C CD2 . LEU B 1 78  ? 14.770  10.675  29.194  1.00 33.47  ? 77  LEU A CD2 1 
ATOM   2730 N N   . CYS B 1 79  ? 17.624  14.816  26.741  1.00 36.39  ? 78  CYS A N   1 
ATOM   2731 C CA  . CYS B 1 79  ? 18.023  15.555  25.548  1.00 39.05  ? 78  CYS A CA  1 
ATOM   2732 C C   . CYS B 1 79  ? 19.473  16.023  25.572  1.00 38.74  ? 78  CYS A C   1 
ATOM   2733 O O   . CYS B 1 79  ? 19.870  16.812  24.708  1.00 39.89  ? 78  CYS A O   1 
ATOM   2734 C CB  . CYS B 1 79  ? 17.092  16.754  25.345  1.00 35.98  ? 78  CYS A CB  1 
ATOM   2735 S SG  . CYS B 1 79  ? 15.424  16.311  24.807  1.00 39.22  ? 78  CYS A SG  1 
ATOM   2736 N N   . ALA B 1 80  ? 20.279  15.554  26.526  1.00 32.88  ? 79  ALA A N   1 
ATOM   2737 C CA  . ALA B 1 80  ? 21.644  16.058  26.638  1.00 30.80  ? 79  ALA A CA  1 
ATOM   2738 C C   . ALA B 1 80  ? 22.501  15.620  25.457  1.00 37.82  ? 79  ALA A C   1 
ATOM   2739 O O   . ALA B 1 80  ? 23.329  16.396  24.966  1.00 43.79  ? 79  ALA A O   1 
ATOM   2740 C CB  . ALA B 1 80  ? 22.266  15.602  27.957  1.00 36.50  ? 79  ALA A CB  1 
ATOM   2741 N N   . ASP B 1 81  ? 22.315  14.388  24.981  1.00 37.90  ? 80  ASP A N   1 
ATOM   2742 C CA  . ASP B 1 81  ? 23.107  13.845  23.884  1.00 42.89  ? 80  ASP A CA  1 
ATOM   2743 C C   . ASP B 1 81  ? 22.302  13.727  22.592  1.00 44.20  ? 80  ASP A C   1 
ATOM   2744 O O   . ASP B 1 81  ? 22.646  12.928  21.714  1.00 39.49  ? 80  ASP A O   1 
ATOM   2745 C CB  . ASP B 1 81  ? 23.694  12.488  24.282  1.00 47.99  ? 80  ASP A CB  1 
ATOM   2746 C CG  . ASP B 1 81  ? 24.799  12.021  23.341  1.00 59.49  ? 80  ASP A CG  1 
ATOM   2747 O OD1 . ASP B 1 81  ? 25.748  12.796  23.093  1.00 68.05  ? 80  ASP A OD1 1 
ATOM   2748 O OD2 . ASP B 1 81  ? 24.712  10.877  22.845  1.00 70.57  ? 80  ASP A OD2 1 
ATOM   2749 N N   . CYS B 1 82  ? 21.236  14.508  22.455  1.00 43.55  ? 81  CYS A N   1 
ATOM   2750 C CA  . CYS B 1 82  ? 20.451  14.469  21.230  1.00 41.05  ? 81  CYS A CA  1 
ATOM   2751 C C   . CYS B 1 82  ? 21.217  15.129  20.094  1.00 32.14  ? 81  CYS A C   1 
ATOM   2752 O O   . CYS B 1 82  ? 21.957  16.093  20.302  1.00 34.97  ? 81  CYS A O   1 
ATOM   2753 C CB  . CYS B 1 82  ? 19.106  15.160  21.437  1.00 35.67  ? 81  CYS A CB  1 
ATOM   2754 S SG  . CYS B 1 82  ? 17.862  14.076  22.173  1.00 49.37  ? 81  CYS A SG  1 
ATOM   2755 N N   . ASP B 1 83  ? 21.053  14.588  18.889  1.00 31.52  ? 82  ASP A N   1 
ATOM   2756 C CA  . ASP B 1 83  ? 21.695  15.147  17.708  1.00 27.82  ? 82  ASP A CA  1 
ATOM   2757 C C   . ASP B 1 83  ? 20.843  16.209  17.036  1.00 31.92  ? 82  ASP A C   1 
ATOM   2758 O O   . ASP B 1 83  ? 21.386  17.118  16.398  1.00 29.08  ? 82  ASP A O   1 
ATOM   2759 C CB  . ASP B 1 83  ? 22.010  14.036  16.703  1.00 38.50  ? 82  ASP A CB  1 
ATOM   2760 C CG  . ASP B 1 83  ? 22.856  12.931  17.307  1.00 47.55  ? 82  ASP A CG  1 
ATOM   2761 O OD1 . ASP B 1 83  ? 24.069  13.154  17.508  1.00 45.65  ? 82  ASP A OD1 1 
ATOM   2762 O OD2 . ASP B 1 83  ? 22.306  11.842  17.585  1.00 44.82  ? 82  ASP A OD2 1 
ATOM   2763 N N   . LEU B 1 84  ? 19.523  16.117  17.170  1.00 32.39  ? 83  LEU A N   1 
ATOM   2764 C CA  . LEU B 1 84  ? 18.614  17.073  16.563  1.00 24.58  ? 83  LEU A CA  1 
ATOM   2765 C C   . LEU B 1 84  ? 17.422  17.265  17.488  1.00 29.31  ? 83  LEU A C   1 
ATOM   2766 O O   . LEU B 1 84  ? 16.907  16.299  18.058  1.00 28.16  ? 83  LEU A O   1 
ATOM   2767 C CB  . LEU B 1 84  ? 18.160  16.597  15.178  1.00 28.49  ? 83  LEU A CB  1 
ATOM   2768 C CG  . LEU B 1 84  ? 16.905  17.206  14.553  1.00 27.96  ? 83  LEU A CG  1 
ATOM   2769 C CD1 . LEU B 1 84  ? 17.125  18.670  14.214  1.00 19.95  ? 83  LEU A CD1 1 
ATOM   2770 C CD2 . LEU B 1 84  ? 16.520  16.425  13.311  1.00 22.42  ? 83  LEU A CD2 1 
ATOM   2771 N N   . ILE B 1 85  ? 16.997  18.516  17.640  1.00 30.47  ? 84  ILE A N   1 
ATOM   2772 C CA  . ILE B 1 85  ? 15.850  18.875  18.462  1.00 23.00  ? 84  ILE A CA  1 
ATOM   2773 C C   . ILE B 1 85  ? 14.790  19.474  17.553  1.00 29.91  ? 84  ILE A C   1 
ATOM   2774 O O   . ILE B 1 85  ? 15.049  20.467  16.862  1.00 33.63  ? 84  ILE A O   1 
ATOM   2775 C CB  . ILE B 1 85  ? 16.228  19.869  19.568  1.00 26.52  ? 84  ILE A CB  1 
ATOM   2776 C CG1 . ILE B 1 85  ? 17.173  19.216  20.580  1.00 33.02  ? 84  ILE A CG1 1 
ATOM   2777 C CG2 . ILE B 1 85  ? 14.972  20.419  20.232  1.00 29.96  ? 84  ILE A CG2 1 
ATOM   2778 C CD1 . ILE B 1 85  ? 16.499  18.233  21.512  1.00 29.99  ? 84  ILE A CD1 1 
ATOM   2779 N N   . VAL B 1 86  ? 13.599  18.882  17.556  1.00 27.75  ? 85  VAL A N   1 
ATOM   2780 C CA  . VAL B 1 86  ? 12.450  19.424  16.840  1.00 28.05  ? 85  VAL A CA  1 
ATOM   2781 C C   . VAL B 1 86  ? 11.415  19.822  17.882  1.00 29.27  ? 85  VAL A C   1 
ATOM   2782 O O   . VAL B 1 86  ? 10.860  18.962  18.575  1.00 26.81  ? 85  VAL A O   1 
ATOM   2783 C CB  . VAL B 1 86  ? 11.864  18.426  15.835  1.00 24.17  ? 85  VAL A CB  1 
ATOM   2784 C CG1 . VAL B 1 86  ? 10.712  19.071  15.060  1.00 19.50  ? 85  VAL A CG1 1 
ATOM   2785 C CG2 . VAL B 1 86  ? 12.945  17.931  14.892  1.00 28.07  ? 85  VAL A CG2 1 
ATOM   2786 N N   . GLU B 1 87  ? 11.157  21.119  17.999  1.00 31.47  ? 86  GLU A N   1 
ATOM   2787 C CA  . GLU B 1 87  ? 10.179  21.626  18.949  1.00 30.61  ? 86  GLU A CA  1 
ATOM   2788 C C   . GLU B 1 87  ? 8.803   21.703  18.298  1.00 27.69  ? 86  GLU A C   1 
ATOM   2789 O O   . GLU B 1 87  ? 8.663   22.161  17.161  1.00 22.31  ? 86  GLU A O   1 
ATOM   2790 C CB  . GLU B 1 87  ? 10.607  23.001  19.467  1.00 33.05  ? 86  GLU A CB  1 
ATOM   2791 C CG  . GLU B 1 87  ? 9.613   23.689  20.386  1.00 35.78  ? 86  GLU A CG  1 
ATOM   2792 C CD  . GLU B 1 87  ? 8.666   24.599  19.630  1.00 43.14  ? 86  GLU A CD  1 
ATOM   2793 O OE1 . GLU B 1 87  ? 7.466   24.632  19.982  1.00 57.26  ? 86  GLU A OE1 1 
ATOM   2794 O OE2 . GLU B 1 87  ? 9.119   25.263  18.670  1.00 49.79  ? 86  GLU A OE2 1 
ATOM   2795 N N   . ALA B 1 88  ? 7.791   21.240  19.025  1.00 26.23  ? 87  ALA A N   1 
ATOM   2796 C CA  . ALA B 1 88  ? 6.413   21.273  18.545  1.00 32.78  ? 87  ALA A CA  1 
ATOM   2797 C C   . ALA B 1 88  ? 5.463   21.449  19.728  1.00 34.76  ? 87  ALA A C   1 
ATOM   2798 O O   . ALA B 1 88  ? 4.483   20.720  19.882  1.00 39.21  ? 87  ALA A O   1 
ATOM   2799 C CB  . ALA B 1 88  ? 6.082   20.012  17.747  1.00 26.76  ? 87  ALA A CB  1 
ATOM   2800 N N   . ALA B 1 89  ? 5.745   22.427  20.582  1.00 42.81  ? 88  ALA A N   1 
ATOM   2801 C CA  . ALA B 1 89  ? 4.943   22.681  21.768  1.00 44.03  ? 88  ALA A CA  1 
ATOM   2802 C C   . ALA B 1 89  ? 3.962   23.825  21.487  1.00 50.56  ? 88  ALA A C   1 
ATOM   2803 O O   . ALA B 1 89  ? 3.653   24.125  20.328  1.00 52.24  ? 88  ALA A O   1 
ATOM   2804 C CB  . ALA B 1 89  ? 5.873   22.956  22.956  1.00 31.55  ? 88  ALA A CB  1 
ATOM   2805 N N   . PHE B 1 90  ? 3.466   24.469  22.541  1.00 63.92  ? 89  PHE A N   1 
ATOM   2806 C CA  . PHE B 1 90  ? 2.443   25.493  22.369  1.00 62.22  ? 89  PHE A CA  1 
ATOM   2807 C C   . PHE B 1 90  ? 3.019   26.727  21.683  1.00 56.77  ? 89  PHE A C   1 
ATOM   2808 O O   . PHE B 1 90  ? 4.118   27.186  22.006  1.00 53.38  ? 89  PHE A O   1 
ATOM   2809 C CB  . PHE B 1 90  ? 1.834   25.874  23.717  1.00 64.81  ? 89  PHE A CB  1 
ATOM   2810 C CG  . PHE B 1 90  ? 0.545   26.636  23.600  1.00 88.60  ? 89  PHE A CG  1 
ATOM   2811 C CD1 . PHE B 1 90  ? -0.225  26.548  22.448  1.00 85.13  ? 89  PHE A CD1 1 
ATOM   2812 C CD2 . PHE B 1 90  ? 0.095   27.432  24.637  1.00 97.29  ? 89  PHE A CD2 1 
ATOM   2813 C CE1 . PHE B 1 90  ? -1.412  27.247  22.332  1.00 84.62  ? 89  PHE A CE1 1 
ATOM   2814 C CE2 . PHE B 1 90  ? -1.096  28.124  24.524  1.00 98.63  ? 89  PHE A CE2 1 
ATOM   2815 C CZ  . PHE B 1 90  ? -1.845  28.037  23.375  1.00 96.02  ? 89  PHE A CZ  1 
ATOM   2816 N N   . GLU B 1 91  ? 2.251   27.274  20.738  1.00 53.42  ? 90  GLU A N   1 
ATOM   2817 C CA  . GLU B 1 91  ? 2.686   28.391  19.896  1.00 63.20  ? 90  GLU A CA  1 
ATOM   2818 C C   . GLU B 1 91  ? 2.603   29.700  20.681  1.00 55.33  ? 90  GLU A C   1 
ATOM   2819 O O   . GLU B 1 91  ? 1.677   30.500  20.530  1.00 48.04  ? 90  GLU A O   1 
ATOM   2820 C CB  . GLU B 1 91  ? 1.840   28.460  18.628  1.00 51.21  ? 90  GLU A CB  1 
ATOM   2821 C CG  . GLU B 1 91  ? 1.961   27.250  17.711  1.00 56.23  ? 90  GLU A CG  1 
ATOM   2822 C CD  . GLU B 1 91  ? 2.884   27.498  16.530  1.00 63.76  ? 90  GLU A CD  1 
ATOM   2823 O OE1 . GLU B 1 91  ? 4.115   27.413  16.717  1.00 51.41  ? 90  GLU A OE1 1 
ATOM   2824 O OE2 . GLU B 1 91  ? 2.383   27.776  15.417  1.00 56.04  ? 90  GLU A OE2 1 
ATOM   2825 N N   . ASP B 1 92  ? 3.604   29.927  21.532  1.00 49.37  ? 91  ASP A N   1 
ATOM   2826 C CA  . ASP B 1 92  ? 3.779   31.214  22.192  1.00 44.38  ? 91  ASP A CA  1 
ATOM   2827 C C   . ASP B 1 92  ? 5.251   31.596  22.145  1.00 46.45  ? 91  ASP A C   1 
ATOM   2828 O O   . ASP B 1 92  ? 6.123   30.769  22.425  1.00 51.01  ? 91  ASP A O   1 
ATOM   2829 C CB  . ASP B 1 92  ? 3.290   31.197  23.645  1.00 53.50  ? 91  ASP A CB  1 
ATOM   2830 C CG  . ASP B 1 92  ? 3.747   32.421  24.427  1.00 63.25  ? 91  ASP A CG  1 
ATOM   2831 O OD1 . ASP B 1 92  ? 3.573   33.554  23.929  1.00 60.03  ? 91  ASP A OD1 1 
ATOM   2832 O OD2 . ASP B 1 92  ? 4.282   32.257  25.539  1.00 65.80  ? 91  ASP A OD2 1 
ATOM   2833 N N   . MET B 1 93  ? 5.517   32.856  21.791  1.00 43.48  ? 92  MET A N   1 
ATOM   2834 C CA  . MET B 1 93  ? 6.892   33.305  21.587  1.00 44.13  ? 92  MET A CA  1 
ATOM   2835 C C   . MET B 1 93  ? 7.731   33.135  22.848  1.00 42.12  ? 92  MET A C   1 
ATOM   2836 O O   . MET B 1 93  ? 8.866   32.645  22.786  1.00 38.89  ? 92  MET A O   1 
ATOM   2837 C CB  . MET B 1 93  ? 6.900   34.766  21.131  1.00 42.43  ? 92  MET A CB  1 
ATOM   2838 C CG  . MET B 1 93  ? 8.238   35.275  20.611  1.00 40.47  ? 92  MET A CG  1 
ATOM   2839 S SD  . MET B 1 93  ? 9.101   34.023  19.652  1.00 43.17  ? 92  MET A SD  1 
ATOM   2840 C CE  . MET B 1 93  ? 8.677   34.525  17.990  1.00 37.58  ? 92  MET A CE  1 
ATOM   2841 N N   . LYS B 1 94  ? 7.193   33.533  24.000  1.00 40.07  ? 93  LYS A N   1 
ATOM   2842 C CA  . LYS B 1 94  ? 7.977   33.452  25.228  1.00 53.36  ? 93  LYS A CA  1 
ATOM   2843 C C   . LYS B 1 94  ? 8.180   32.006  25.663  1.00 44.13  ? 93  LYS A C   1 
ATOM   2844 O O   . LYS B 1 94  ? 9.257   31.648  26.152  1.00 43.24  ? 93  LYS A O   1 
ATOM   2845 C CB  . LYS B 1 94  ? 7.309   34.266  26.335  1.00 50.94  ? 93  LYS A CB  1 
ATOM   2846 C CG  . LYS B 1 94  ? 7.617   35.754  26.260  1.00 51.10  ? 93  LYS A CG  1 
ATOM   2847 C CD  . LYS B 1 94  ? 6.971   36.506  27.404  1.00 54.48  ? 93  LYS A CD  1 
ATOM   2848 C CE  . LYS B 1 94  ? 5.488   36.718  27.151  1.00 58.85  ? 93  LYS A CE  1 
ATOM   2849 N NZ  . LYS B 1 94  ? 5.094   38.149  27.270  1.00 64.58  ? 93  LYS A NZ  1 
ATOM   2850 N N   . VAL B 1 95  ? 7.162   31.161  25.485  1.00 48.04  ? 94  VAL A N   1 
ATOM   2851 C CA  . VAL B 1 95  ? 7.306   29.746  25.820  1.00 41.13  ? 94  VAL A CA  1 
ATOM   2852 C C   . VAL B 1 95  ? 8.425   29.123  24.996  1.00 44.00  ? 94  VAL A C   1 
ATOM   2853 O O   . VAL B 1 95  ? 9.322   28.462  25.532  1.00 40.74  ? 94  VAL A O   1 
ATOM   2854 C CB  . VAL B 1 95  ? 5.974   29.001  25.612  1.00 44.07  ? 94  VAL A CB  1 
ATOM   2855 C CG1 . VAL B 1 95  ? 6.213   27.500  25.530  1.00 36.25  ? 94  VAL A CG1 1 
ATOM   2856 C CG2 . VAL B 1 95  ? 5.000   29.320  26.722  1.00 49.09  ? 94  VAL A CG2 1 
ATOM   2857 N N   . LYS B 1 96  ? 8.394   29.339  23.675  1.00 34.36  ? 95  LYS A N   1 
ATOM   2858 C CA  . LYS B 1 96  ? 9.410   28.758  22.803  1.00 34.02  ? 95  LYS A CA  1 
ATOM   2859 C C   . LYS B 1 96  ? 10.793  29.327  23.086  1.00 36.38  ? 95  LYS A C   1 
ATOM   2860 O O   . LYS B 1 96  ? 11.790  28.599  23.005  1.00 33.02  ? 95  LYS A O   1 
ATOM   2861 C CB  . LYS B 1 96  ? 9.040   28.988  21.339  1.00 32.07  ? 95  LYS A CB  1 
ATOM   2862 C CG  . LYS B 1 96  ? 7.860   28.167  20.857  1.00 33.99  ? 95  LYS A CG  1 
ATOM   2863 C CD  . LYS B 1 96  ? 7.853   28.087  19.341  1.00 40.66  ? 95  LYS A CD  1 
ATOM   2864 C CE  . LYS B 1 96  ? 6.458   27.844  18.791  1.00 40.40  ? 95  LYS A CE  1 
ATOM   2865 N NZ  . LYS B 1 96  ? 5.900   26.531  19.216  1.00 47.64  ? 95  LYS A NZ  1 
ATOM   2866 N N   . GLN B 1 97  ? 10.875  30.617  23.418  1.00 35.86  ? 96  GLN A N   1 
ATOM   2867 C CA  . GLN B 1 97  ? 12.174  31.235  23.659  1.00 34.27  ? 96  GLN A CA  1 
ATOM   2868 C C   . GLN B 1 97  ? 12.848  30.637  24.885  1.00 35.30  ? 96  GLN A C   1 
ATOM   2869 O O   . GLN B 1 97  ? 14.017  30.237  24.830  1.00 37.64  ? 96  GLN A O   1 
ATOM   2870 C CB  . GLN B 1 97  ? 12.014  32.744  23.820  1.00 35.74  ? 96  GLN A CB  1 
ATOM   2871 C CG  . GLN B 1 97  ? 12.265  33.528  22.553  1.00 37.20  ? 96  GLN A CG  1 
ATOM   2872 C CD  . GLN B 1 97  ? 11.693  34.924  22.625  1.00 35.84  ? 96  GLN A CD  1 
ATOM   2873 O OE1 . GLN B 1 97  ? 10.856  35.219  23.479  1.00 41.91  ? 96  GLN A OE1 1 
ATOM   2874 N NE2 . GLN B 1 97  ? 12.135  35.794  21.726  1.00 35.84  ? 96  GLN A NE2 1 
ATOM   2875 N N   . THR B 1 98  ? 12.127  30.567  26.007  1.00 31.27  ? 97  THR A N   1 
ATOM   2876 C CA  . THR B 1 98  ? 12.725  30.018  27.218  1.00 44.65  ? 97  THR A CA  1 
ATOM   2877 C C   . THR B 1 98  ? 12.989  28.522  27.084  1.00 40.57  ? 97  THR A C   1 
ATOM   2878 O O   . THR B 1 98  ? 13.969  28.018  27.644  1.00 32.78  ? 97  THR A O   1 
ATOM   2879 C CB  . THR B 1 98  ? 11.838  30.308  28.431  1.00 36.91  ? 97  THR A CB  1 
ATOM   2880 O OG1 . THR B 1 98  ? 10.579  29.640  28.284  1.00 50.72  ? 97  THR A OG1 1 
ATOM   2881 C CG2 . THR B 1 98  ? 11.596  31.806  28.562  1.00 44.89  ? 97  THR A CG2 1 
ATOM   2882 N N   . THR B 1 99  ? 12.145  27.807  26.334  1.00 35.10  ? 98  THR A N   1 
ATOM   2883 C CA  . THR B 1 99  ? 12.394  26.390  26.080  1.00 31.87  ? 98  THR A CA  1 
ATOM   2884 C C   . THR B 1 99  ? 13.748  26.183  25.410  1.00 32.09  ? 98  THR A C   1 
ATOM   2885 O O   . THR B 1 99  ? 14.521  25.299  25.800  1.00 27.61  ? 98  THR A O   1 
ATOM   2886 C CB  . THR B 1 99  ? 11.276  25.805  25.214  1.00 27.21  ? 98  THR A CB  1 
ATOM   2887 O OG1 . THR B 1 99  ? 10.028  25.898  25.911  1.00 37.08  ? 98  THR A OG1 1 
ATOM   2888 C CG2 . THR B 1 99  ? 11.559  24.347  24.894  1.00 27.07  ? 98  THR A CG2 1 
ATOM   2889 N N   . PHE B 1 100 ? 14.056  26.999  24.402  1.00 28.28  ? 99  PHE A N   1 
ATOM   2890 C CA  . PHE B 1 100 ? 15.331  26.881  23.708  1.00 33.61  ? 99  PHE A CA  1 
ATOM   2891 C C   . PHE B 1 100 ? 16.489  27.467  24.508  1.00 29.71  ? 99  PHE A C   1 
ATOM   2892 O O   . PHE B 1 100 ? 17.640  27.078  24.282  1.00 35.31  ? 99  PHE A O   1 
ATOM   2893 C CB  . PHE B 1 100 ? 15.244  27.551  22.334  1.00 33.38  ? 99  PHE A CB  1 
ATOM   2894 C CG  . PHE B 1 100 ? 14.649  26.671  21.267  1.00 33.75  ? 99  PHE A CG  1 
ATOM   2895 C CD1 . PHE B 1 100 ? 15.351  25.581  20.777  1.00 27.23  ? 99  PHE A CD1 1 
ATOM   2896 C CD2 . PHE B 1 100 ? 13.386  26.933  20.757  1.00 27.22  ? 99  PHE A CD2 1 
ATOM   2897 C CE1 . PHE B 1 100 ? 14.806  24.767  19.795  1.00 28.85  ? 99  PHE A CE1 1 
ATOM   2898 C CE2 . PHE B 1 100 ? 12.835  26.126  19.776  1.00 26.24  ? 99  PHE A CE2 1 
ATOM   2899 C CZ  . PHE B 1 100 ? 13.546  25.040  19.294  1.00 31.67  ? 99  PHE A CZ  1 
ATOM   2900 N N   . GLY B 1 101 ? 16.215  28.390  25.430  1.00 33.89  ? 100 GLY A N   1 
ATOM   2901 C CA  . GLY B 1 101 ? 17.259  28.840  26.337  1.00 34.09  ? 100 GLY A CA  1 
ATOM   2902 C C   . GLY B 1 101 ? 17.648  27.766  27.336  1.00 34.03  ? 100 GLY A C   1 
ATOM   2903 O O   . GLY B 1 101 ? 18.818  27.639  27.705  1.00 29.56  ? 100 GLY A O   1 
ATOM   2904 N N   . GLU B 1 102 ? 16.672  26.975  27.783  1.00 32.09  ? 101 GLU A N   1 
ATOM   2905 C CA  . GLU B 1 102 ? 16.978  25.849  28.657  1.00 34.18  ? 101 GLU A CA  1 
ATOM   2906 C C   . GLU B 1 102 ? 17.688  24.744  27.890  1.00 39.70  ? 101 GLU A C   1 
ATOM   2907 O O   . GLU B 1 102 ? 18.675  24.177  28.374  1.00 33.96  ? 101 GLU A O   1 
ATOM   2908 C CB  . GLU B 1 102 ? 15.695  25.323  29.298  1.00 31.92  ? 101 GLU A CB  1 
ATOM   2909 C CG  . GLU B 1 102 ? 15.227  26.134  30.499  1.00 39.82  ? 101 GLU A CG  1 
ATOM   2910 C CD  . GLU B 1 102 ? 13.730  26.014  30.735  1.00 52.74  ? 101 GLU A CD  1 
ATOM   2911 O OE1 . GLU B 1 102 ? 13.076  25.218  30.027  1.00 49.20  ? 101 GLU A OE1 1 
ATOM   2912 O OE2 . GLU B 1 102 ? 13.210  26.708  31.635  1.00 54.48  ? 101 GLU A OE2 1 
ATOM   2913 N N   . LEU B 1 103 ? 17.207  24.436  26.682  1.00 39.80  ? 102 LEU A N   1 
ATOM   2914 C CA  . LEU B 1 103 ? 17.869  23.434  25.857  1.00 22.94  ? 102 LEU A CA  1 
ATOM   2915 C C   . LEU B 1 103 ? 19.269  23.874  25.465  1.00 28.41  ? 102 LEU A C   1 
ATOM   2916 O O   . LEU B 1 103 ? 20.135  23.031  25.200  1.00 28.53  ? 102 LEU A O   1 
ATOM   2917 C CB  . LEU B 1 103 ? 17.037  23.150  24.609  1.00 36.29  ? 102 LEU A CB  1 
ATOM   2918 C CG  . LEU B 1 103 ? 15.809  22.266  24.819  1.00 36.11  ? 102 LEU A CG  1 
ATOM   2919 C CD1 . LEU B 1 103 ? 14.964  22.229  23.562  1.00 33.12  ? 102 LEU A CD1 1 
ATOM   2920 C CD2 . LEU B 1 103 ? 16.229  20.866  25.228  1.00 35.55  ? 102 LEU A CD2 1 
ATOM   2921 N N   . ASP B 1 104 ? 19.511  25.185  25.419  1.00 27.30  ? 103 ASP A N   1 
ATOM   2922 C CA  . ASP B 1 104 ? 20.844  25.673  25.089  1.00 36.35  ? 103 ASP A CA  1 
ATOM   2923 C C   . ASP B 1 104 ? 21.868  25.205  26.111  1.00 37.42  ? 103 ASP A C   1 
ATOM   2924 O O   . ASP B 1 104 ? 23.022  24.933  25.757  1.00 42.10  ? 103 ASP A O   1 
ATOM   2925 C CB  . ASP B 1 104 ? 20.834  27.199  24.997  1.00 38.25  ? 103 ASP A CB  1 
ATOM   2926 C CG  . ASP B 1 104 ? 21.782  27.728  23.935  1.00 40.25  ? 103 ASP A CG  1 
ATOM   2927 O OD1 . ASP B 1 104 ? 22.493  26.912  23.307  1.00 34.85  ? 103 ASP A OD1 1 
ATOM   2928 O OD2 . ASP B 1 104 ? 21.812  28.963  23.726  1.00 36.13  ? 103 ASP A OD2 1 
ATOM   2929 N N   . LYS B 1 105 ? 21.461  25.085  27.375  1.00 34.41  ? 104 LYS A N   1 
ATOM   2930 C CA  . LYS B 1 105 ? 22.352  24.629  28.434  1.00 41.58  ? 104 LYS A CA  1 
ATOM   2931 C C   . LYS B 1 105 ? 22.382  23.111  28.569  1.00 38.48  ? 104 LYS A C   1 
ATOM   2932 O O   . LYS B 1 105 ? 23.403  22.556  28.993  1.00 47.89  ? 104 LYS A O   1 
ATOM   2933 C CB  . LYS B 1 105 ? 21.935  25.261  29.765  1.00 43.41  ? 104 LYS A CB  1 
ATOM   2934 C CG  . LYS B 1 105 ? 21.756  26.772  29.689  1.00 44.51  ? 104 LYS A CG  1 
ATOM   2935 C CD  . LYS B 1 105 ? 22.177  27.449  30.984  1.00 55.63  ? 104 LYS A CD  1 
ATOM   2936 C CE  . LYS B 1 105 ? 21.005  28.150  31.650  1.00 57.22  ? 104 LYS A CE  1 
ATOM   2937 N NZ  . LYS B 1 105 ? 20.378  29.157  30.748  1.00 54.95  ? 104 LYS A NZ  1 
ATOM   2938 N N   . ILE B 1 106 ? 21.295  22.428  28.208  1.00 37.52  ? 105 ILE A N   1 
ATOM   2939 C CA  . ILE B 1 106 ? 21.231  20.977  28.362  1.00 35.52  ? 105 ILE A CA  1 
ATOM   2940 C C   . ILE B 1 106 ? 21.981  20.275  27.236  1.00 39.96  ? 105 ILE A C   1 
ATOM   2941 O O   . ILE B 1 106 ? 22.796  19.377  27.479  1.00 41.81  ? 105 ILE A O   1 
ATOM   2942 C CB  . ILE B 1 106 ? 19.764  20.506  28.429  1.00 32.17  ? 105 ILE A CB  1 
ATOM   2943 C CG1 . ILE B 1 106 ? 19.088  20.967  29.719  1.00 41.54  ? 105 ILE A CG1 1 
ATOM   2944 C CG2 . ILE B 1 106 ? 19.680  18.995  28.302  1.00 28.10  ? 105 ILE A CG2 1 
ATOM   2945 C CD1 . ILE B 1 106 ? 17.635  21.378  29.522  1.00 35.17  ? 105 ILE A CD1 1 
ATOM   2946 N N   . CYS B 1 107 ? 21.724  20.668  25.990  1.00 35.41  ? 106 CYS A N   1 
ATOM   2947 C CA  . CYS B 1 107 ? 22.170  19.886  24.844  1.00 35.23  ? 106 CYS A CA  1 
ATOM   2948 C C   . CYS B 1 107 ? 23.637  20.132  24.515  1.00 41.12  ? 106 CYS A C   1 
ATOM   2949 O O   . CYS B 1 107 ? 24.163  21.236  24.686  1.00 43.41  ? 106 CYS A O   1 
ATOM   2950 C CB  . CYS B 1 107 ? 21.322  20.202  23.614  1.00 31.36  ? 106 CYS A CB  1 
ATOM   2951 S SG  . CYS B 1 107 ? 19.564  19.958  23.854  1.00 35.68  ? 106 CYS A SG  1 
ATOM   2952 N N   . LYS B 1 108 ? 24.289  19.078  24.013  1.00 44.99  ? 107 LYS A N   1 
ATOM   2953 C CA  . LYS B 1 108 ? 25.674  19.165  23.584  1.00 36.75  ? 107 LYS A CA  1 
ATOM   2954 C C   . LYS B 1 108 ? 25.808  20.178  22.448  1.00 44.39  ? 107 LYS A C   1 
ATOM   2955 O O   . LYS B 1 108 ? 24.849  20.431  21.714  1.00 37.18  ? 107 LYS A O   1 
ATOM   2956 C CB  . LYS B 1 108 ? 26.178  17.793  23.136  1.00 31.98  ? 107 LYS A CB  1 
ATOM   2957 C CG  . LYS B 1 108 ? 25.211  17.027  22.247  1.00 39.51  ? 107 LYS A CG  1 
ATOM   2958 C CD  . LYS B 1 108 ? 25.863  15.778  21.674  1.00 38.32  ? 107 LYS A CD  1 
ATOM   2959 C CE  . LYS B 1 108 ? 25.061  15.221  20.507  1.00 44.51  ? 107 LYS A CE  1 
ATOM   2960 N NZ  . LYS B 1 108 ? 25.461  13.831  20.154  1.00 48.56  ? 107 LYS A NZ  1 
ATOM   2961 N N   . PRO B 1 109 ? 26.998  20.766  22.284  1.00 46.58  ? 108 PRO A N   1 
ATOM   2962 C CA  . PRO B 1 109 ? 27.137  21.888  21.336  1.00 38.59  ? 108 PRO A CA  1 
ATOM   2963 C C   . PRO B 1 109 ? 26.742  21.558  19.906  1.00 39.65  ? 108 PRO A C   1 
ATOM   2964 O O   . PRO B 1 109 ? 26.141  22.402  19.229  1.00 38.67  ? 108 PRO A O   1 
ATOM   2965 C CB  . PRO B 1 109 ? 28.627  22.244  21.443  1.00 45.11  ? 108 PRO A CB  1 
ATOM   2966 C CG  . PRO B 1 109 ? 29.028  21.787  22.803  1.00 45.33  ? 108 PRO A CG  1 
ATOM   2967 C CD  . PRO B 1 109 ? 28.228  20.545  23.064  1.00 39.35  ? 108 PRO A CD  1 
ATOM   2968 N N   . GLU B 1 110 ? 27.057  20.358  19.423  1.00 41.92  ? 109 GLU A N   1 
ATOM   2969 C CA  . GLU B 1 110 ? 26.787  20.006  18.034  1.00 43.63  ? 109 GLU A CA  1 
ATOM   2970 C C   . GLU B 1 110 ? 25.322  19.668  17.767  1.00 36.88  ? 109 GLU A C   1 
ATOM   2971 O O   . GLU B 1 110 ? 24.970  19.379  16.618  1.00 41.94  ? 109 GLU A O   1 
ATOM   2972 C CB  . GLU B 1 110 ? 27.683  18.837  17.604  1.00 38.00  ? 109 GLU A CB  1 
ATOM   2973 C CG  . GLU B 1 110 ? 27.750  17.682  18.589  1.00 52.58  ? 109 GLU A CG  1 
ATOM   2974 C CD  . GLU B 1 110 ? 28.894  17.824  19.585  1.00 61.47  ? 109 GLU A CD  1 
ATOM   2975 O OE1 . GLU B 1 110 ? 30.014  17.363  19.279  1.00 76.76  ? 109 GLU A OE1 1 
ATOM   2976 O OE2 . GLU B 1 110 ? 28.671  18.386  20.679  1.00 51.87  ? 109 GLU A OE2 1 
ATOM   2977 N N   . CYS B 1 111 ? 24.463  19.706  18.781  1.00 33.28  ? 110 CYS A N   1 
ATOM   2978 C CA  . CYS B 1 111 ? 23.048  19.419  18.577  1.00 38.29  ? 110 CYS A CA  1 
ATOM   2979 C C   . CYS B 1 111 ? 22.374  20.556  17.815  1.00 35.79  ? 110 CYS A C   1 
ATOM   2980 O O   . CYS B 1 111 ? 22.580  21.735  18.118  1.00 32.85  ? 110 CYS A O   1 
ATOM   2981 C CB  . CYS B 1 111 ? 22.360  19.201  19.926  1.00 37.16  ? 110 CYS A CB  1 
ATOM   2982 S SG  . CYS B 1 111 ? 20.590  18.874  19.836  1.00 34.68  ? 110 CYS A SG  1 
ATOM   2983 N N   . ILE B 1 112 ? 21.557  20.194  16.815  1.00 33.60  ? 111 ILE A N   1 
ATOM   2984 C CA  . ILE B 1 112 ? 20.866  21.161  15.966  1.00 36.93  ? 111 ILE A CA  1 
ATOM   2985 C C   . ILE B 1 112 ? 19.501  21.473  16.563  1.00 28.08  ? 111 ILE A C   1 
ATOM   2986 O O   . ILE B 1 112 ? 18.772  20.568  16.987  1.00 32.78  ? 111 ILE A O   1 
ATOM   2987 C CB  . ILE B 1 112 ? 20.732  20.631  14.525  1.00 34.10  ? 111 ILE A CB  1 
ATOM   2988 C CG1 . ILE B 1 112 ? 22.104  20.308  13.941  1.00 28.89  ? 111 ILE A CG1 1 
ATOM   2989 C CG2 . ILE B 1 112 ? 20.023  21.643  13.639  1.00 28.10  ? 111 ILE A CG2 1 
ATOM   2990 C CD1 . ILE B 1 112 ? 22.042  19.379  12.756  1.00 30.95  ? 111 ILE A CD1 1 
ATOM   2991 N N   . PHE B 1 113 ? 19.148  22.759  16.586  1.00 28.23  ? 112 PHE A N   1 
ATOM   2992 C CA  . PHE B 1 113 ? 17.874  23.227  17.124  1.00 30.39  ? 112 PHE A CA  1 
ATOM   2993 C C   . PHE B 1 113 ? 16.924  23.555  15.975  1.00 23.49  ? 112 PHE A C   1 
ATOM   2994 O O   . PHE B 1 113 ? 17.174  24.489  15.206  1.00 26.93  ? 112 PHE A O   1 
ATOM   2995 C CB  . PHE B 1 113 ? 18.078  24.458  18.010  1.00 28.54  ? 112 PHE A CB  1 
ATOM   2996 C CG  . PHE B 1 113 ? 18.659  24.154  19.366  1.00 30.15  ? 112 PHE A CG  1 
ATOM   2997 C CD1 . PHE B 1 113 ? 18.935  22.853  19.747  1.00 27.90  ? 112 PHE A CD1 1 
ATOM   2998 C CD2 . PHE B 1 113 ? 18.934  25.179  20.256  1.00 26.64  ? 112 PHE A CD2 1 
ATOM   2999 C CE1 . PHE B 1 113 ? 19.473  22.578  20.987  1.00 26.62  ? 112 PHE A CE1 1 
ATOM   3000 C CE2 . PHE B 1 113 ? 19.469  24.911  21.503  1.00 33.76  ? 112 PHE A CE2 1 
ATOM   3001 C CZ  . PHE B 1 113 ? 19.739  23.607  21.869  1.00 29.93  ? 112 PHE A CZ  1 
ATOM   3002 N N   . ALA B 1 114 ? 15.833  22.797  15.868  1.00 23.17  ? 113 ALA A N   1 
ATOM   3003 C CA  . ALA B 1 114 ? 14.807  23.032  14.862  1.00 29.65  ? 113 ALA A CA  1 
ATOM   3004 C C   . ALA B 1 114 ? 13.452  23.212  15.536  1.00 28.85  ? 113 ALA A C   1 
ATOM   3005 O O   . ALA B 1 114 ? 13.211  22.695  16.631  1.00 27.82  ? 113 ALA A O   1 
ATOM   3006 C CB  . ALA B 1 114 ? 14.735  21.884  13.845  1.00 23.41  ? 113 ALA A CB  1 
ATOM   3007 N N   . SER B 1 115 ? 12.567  23.960  14.869  1.00 28.68  ? 114 SER A N   1 
ATOM   3008 C CA  . SER B 1 115 ? 11.216  24.208  15.357  1.00 22.89  ? 114 SER A CA  1 
ATOM   3009 C C   . SER B 1 115 ? 10.196  23.935  14.261  1.00 23.84  ? 114 SER A C   1 
ATOM   3010 O O   . SER B 1 115 ? 10.451  24.168  13.076  1.00 24.54  ? 114 SER A O   1 
ATOM   3011 C CB  . SER B 1 115 ? 11.034  25.646  15.850  1.00 25.38  ? 114 SER A CB  1 
ATOM   3012 O OG  . SER B 1 115 ? 9.670   25.893  16.166  1.00 22.01  ? 114 SER A OG  1 
ATOM   3013 N N   . ASN B 1 116 ? 9.024   23.458  14.678  1.00 19.34  ? 115 ASN A N   1 
ATOM   3014 C CA  . ASN B 1 116 ? 7.933   23.123  13.774  1.00 26.29  ? 115 ASN A CA  1 
ATOM   3015 C C   . ASN B 1 116 ? 6.900   24.239  13.652  1.00 28.35  ? 115 ASN A C   1 
ATOM   3016 O O   . ASN B 1 116 ? 5.817   24.012  13.103  1.00 30.73  ? 115 ASN A O   1 
ATOM   3017 C CB  . ASN B 1 116 ? 7.253   21.832  14.238  1.00 24.97  ? 115 ASN A CB  1 
ATOM   3018 C CG  . ASN B 1 116 ? 6.274   21.285  13.215  1.00 24.84  ? 115 ASN A CG  1 
ATOM   3019 O OD1 . ASN B 1 116 ? 6.658   20.919  12.110  1.00 21.53  ? 115 ASN A OD1 1 
ATOM   3020 N ND2 . ASN B 1 116 ? 4.999   21.241  13.580  1.00 29.89  ? 115 ASN A ND2 1 
ATOM   3021 N N   . THR B 1 117 ? 7.205   25.439  14.136  1.00 21.04  ? 116 THR A N   1 
ATOM   3022 C CA  . THR B 1 117 ? 6.205   26.496  14.133  1.00 29.29  ? 116 THR A CA  1 
ATOM   3023 C C   . THR B 1 117 ? 5.817   26.881  12.707  1.00 35.37  ? 116 THR A C   1 
ATOM   3024 O O   . THR B 1 117 ? 6.624   26.818  11.774  1.00 29.59  ? 116 THR A O   1 
ATOM   3025 C CB  . THR B 1 117 ? 6.717   27.721  14.889  1.00 31.48  ? 116 THR A CB  1 
ATOM   3026 O OG1 . THR B 1 117 ? 5.640   28.650  15.071  1.00 23.30  ? 116 THR A OG1 1 
ATOM   3027 C CG2 . THR B 1 117 ? 7.844   28.394  14.124  1.00 26.71  ? 116 THR A CG2 1 
ATOM   3028 N N   . ALA B 1 118 ? 4.548   27.261  12.543  1.00 37.53  ? 117 ALA A N   1 
ATOM   3029 C CA  . ALA B 1 118 ? 4.039   27.748  11.270  1.00 40.45  ? 117 ALA A CA  1 
ATOM   3030 C C   . ALA B 1 118 ? 3.699   29.230  11.279  1.00 35.15  ? 117 ALA A C   1 
ATOM   3031 O O   . ALA B 1 118 ? 3.638   29.837  10.205  1.00 45.03  ? 117 ALA A O   1 
ATOM   3032 C CB  . ALA B 1 118 ? 2.790   26.957  10.854  1.00 31.48  ? 117 ALA A CB  1 
ATOM   3033 N N   . SER B 1 119 ? 3.492   29.823  12.452  1.00 28.62  ? 118 SER A N   1 
ATOM   3034 C CA  . SER B 1 119 ? 3.036   31.200  12.574  1.00 38.68  ? 118 SER A CA  1 
ATOM   3035 C C   . SER B 1 119 ? 4.013   32.117  13.296  1.00 40.91  ? 118 SER A C   1 
ATOM   3036 O O   . SER B 1 119 ? 3.981   33.327  13.063  1.00 40.95  ? 118 SER A O   1 
ATOM   3037 C CB  . SER B 1 119 ? 1.684   31.246  13.304  1.00 44.09  ? 118 SER A CB  1 
ATOM   3038 O OG  . SER B 1 119 ? 1.773   30.627  14.577  1.00 50.81  ? 118 SER A OG  1 
ATOM   3039 N N   . LEU B 1 120 ? 4.871   31.584  14.159  1.00 37.59  ? 119 LEU A N   1 
ATOM   3040 C CA  . LEU B 1 120 ? 5.827   32.401  14.891  1.00 31.23  ? 119 LEU A CA  1 
ATOM   3041 C C   . LEU B 1 120 ? 7.129   32.531  14.113  1.00 30.42  ? 119 LEU A C   1 
ATOM   3042 O O   . LEU B 1 120 ? 7.493   31.660  13.318  1.00 29.52  ? 119 LEU A O   1 
ATOM   3043 C CB  . LEU B 1 120 ? 6.101   31.807  16.273  1.00 35.06  ? 119 LEU A CB  1 
ATOM   3044 C CG  . LEU B 1 120 ? 4.896   31.757  17.213  1.00 37.86  ? 119 LEU A CG  1 
ATOM   3045 C CD1 . LEU B 1 120 ? 5.358   31.636  18.650  1.00 43.81  ? 119 LEU A CD1 1 
ATOM   3046 C CD2 . LEU B 1 120 ? 4.014   32.983  17.031  1.00 35.72  ? 119 LEU A CD2 1 
ATOM   3047 N N   . SER B 1 121 ? 7.835   33.631  14.357  1.00 24.62  ? 120 SER A N   1 
ATOM   3048 C CA  . SER B 1 121 ? 9.040   33.949  13.603  1.00 22.40  ? 120 SER A CA  1 
ATOM   3049 C C   . SER B 1 121 ? 10.191  33.060  14.054  1.00 31.80  ? 120 SER A C   1 
ATOM   3050 O O   . SER B 1 121 ? 10.557  33.059  15.235  1.00 27.27  ? 120 SER A O   1 
ATOM   3051 C CB  . SER B 1 121 ? 9.410   35.417  13.782  1.00 24.15  ? 120 SER A CB  1 
ATOM   3052 O OG  . SER B 1 121 ? 10.748  35.639  13.369  1.00 27.62  ? 120 SER A OG  1 
ATOM   3053 N N   . ILE B 1 122 ? 10.768  32.316  13.108  1.00 24.26  ? 121 ILE A N   1 
ATOM   3054 C CA  . ILE B 1 122 ? 11.952  31.513  13.406  1.00 25.13  ? 121 ILE A CA  1 
ATOM   3055 C C   . ILE B 1 122 ? 13.081  32.397  13.923  1.00 34.34  ? 121 ILE A C   1 
ATOM   3056 O O   . ILE B 1 122 ? 13.744  32.068  14.915  1.00 32.55  ? 121 ILE A O   1 
ATOM   3057 C CB  . ILE B 1 122 ? 12.377  30.717  12.157  1.00 27.16  ? 121 ILE A CB  1 
ATOM   3058 C CG1 . ILE B 1 122 ? 11.493  29.477  11.989  1.00 34.06  ? 121 ILE A CG1 1 
ATOM   3059 C CG2 . ILE B 1 122 ? 13.850  30.341  12.227  1.00 28.19  ? 121 ILE A CG2 1 
ATOM   3060 C CD1 . ILE B 1 122 ? 11.308  28.686  13.269  1.00 35.71  ? 121 ILE A CD1 1 
ATOM   3061 N N   . THR B 1 123 ? 13.302  33.543  13.269  1.00 34.07  ? 122 THR A N   1 
ATOM   3062 C CA  . THR B 1 123 ? 14.392  34.435  13.655  1.00 30.40  ? 122 THR A CA  1 
ATOM   3063 C C   . THR B 1 123 ? 14.228  34.934  15.085  1.00 34.56  ? 122 THR A C   1 
ATOM   3064 O O   . THR B 1 123 ? 15.208  35.032  15.833  1.00 37.33  ? 122 THR A O   1 
ATOM   3065 C CB  . THR B 1 123 ? 14.462  35.622  12.696  1.00 27.09  ? 122 THR A CB  1 
ATOM   3066 O OG1 . THR B 1 123 ? 14.516  35.149  11.347  1.00 31.91  ? 122 THR A OG1 1 
ATOM   3067 C CG2 . THR B 1 123 ? 15.693  36.456  12.978  1.00 34.00  ? 122 THR A CG2 1 
ATOM   3068 N N   . GLU B 1 124 ? 12.997  35.262  15.479  1.00 30.35  ? 123 GLU A N   1 
ATOM   3069 C CA  . GLU B 1 124 ? 12.765  35.773  16.825  1.00 35.80  ? 123 GLU A CA  1 
ATOM   3070 C C   . GLU B 1 124 ? 12.861  34.671  17.871  1.00 38.63  ? 123 GLU A C   1 
ATOM   3071 O O   . GLU B 1 124 ? 13.257  34.937  19.013  1.00 39.81  ? 123 GLU A O   1 
ATOM   3072 C CB  . GLU B 1 124 ? 11.399  36.455  16.891  1.00 26.81  ? 123 GLU A CB  1 
ATOM   3073 C CG  . GLU B 1 124 ? 11.142  37.220  18.178  1.00 35.46  ? 123 GLU A CG  1 
ATOM   3074 C CD  . GLU B 1 124 ? 9.858   38.022  18.127  1.00 38.15  ? 123 GLU A CD  1 
ATOM   3075 O OE1 . GLU B 1 124 ? 9.198   38.026  17.064  1.00 30.83  ? 123 GLU A OE1 1 
ATOM   3076 O OE2 . GLU B 1 124 ? 9.500   38.639  19.152  1.00 33.76  ? 123 GLU A OE2 1 
ATOM   3077 N N   . ILE B 1 125 ? 12.505  33.437  17.503  1.00 36.22  ? 124 ILE A N   1 
ATOM   3078 C CA  . ILE B 1 125 ? 12.564  32.319  18.444  1.00 34.09  ? 124 ILE A CA  1 
ATOM   3079 C C   . ILE B 1 125 ? 13.977  32.158  18.988  1.00 37.70  ? 124 ILE A C   1 
ATOM   3080 O O   . ILE B 1 125 ? 14.194  32.125  20.205  1.00 42.00  ? 124 ILE A O   1 
ATOM   3081 C CB  . ILE B 1 125 ? 12.079  31.023  17.768  1.00 40.09  ? 124 ILE A CB  1 
ATOM   3082 C CG1 . ILE B 1 125 ? 10.552  30.964  17.729  1.00 34.73  ? 124 ILE A CG1 1 
ATOM   3083 C CG2 . ILE B 1 125 ? 12.624  29.807  18.499  1.00 41.03  ? 124 ILE A CG2 1 
ATOM   3084 C CD1 . ILE B 1 125 ? 10.020  29.742  17.017  1.00 27.49  ? 124 ILE A CD1 1 
ATOM   3085 N N   . GLY B 1 126 ? 14.961  32.068  18.094  1.00 32.82  ? 125 GLY A N   1 
ATOM   3086 C CA  . GLY B 1 126 ? 16.327  31.824  18.504  1.00 41.55  ? 125 GLY A CA  1 
ATOM   3087 C C   . GLY B 1 126 ? 17.190  33.066  18.533  1.00 44.20  ? 125 GLY A C   1 
ATOM   3088 O O   . GLY B 1 126 ? 18.385  33.001  18.226  1.00 40.61  ? 125 GLY A O   1 
ATOM   3089 N N   . LYS B 1 127 ? 16.596  34.196  18.928  1.00 41.67  ? 126 LYS A N   1 
ATOM   3090 C CA  . LYS B 1 127 ? 17.283  35.483  18.857  1.00 45.82  ? 126 LYS A CA  1 
ATOM   3091 C C   . LYS B 1 127 ? 18.570  35.478  19.676  1.00 51.34  ? 126 LYS A C   1 
ATOM   3092 O O   . LYS B 1 127 ? 19.660  35.733  19.148  1.00 60.33  ? 126 LYS A O   1 
ATOM   3093 C CB  . LYS B 1 127 ? 16.343  36.598  19.325  1.00 47.39  ? 126 LYS A CB  1 
ATOM   3094 C CG  . LYS B 1 127 ? 17.052  37.870  19.783  1.00 46.32  ? 126 LYS A CG  1 
ATOM   3095 C CD  . LYS B 1 127 ? 16.246  39.122  19.446  1.00 51.95  ? 126 LYS A CD  1 
ATOM   3096 C CE  . LYS B 1 127 ? 14.755  38.914  19.704  1.00 56.69  ? 126 LYS A CE  1 
ATOM   3097 N NZ  . LYS B 1 127 ? 13.932  40.069  19.237  1.00 52.39  ? 126 LYS A NZ  1 
ATOM   3098 N N   . GLY B 1 128 ? 18.469  35.180  20.970  1.00 35.22  ? 127 GLY A N   1 
ATOM   3099 C CA  . GLY B 1 128 ? 19.633  35.274  21.832  1.00 40.73  ? 127 GLY A CA  1 
ATOM   3100 C C   . GLY B 1 128 ? 20.306  33.959  22.175  1.00 43.74  ? 127 GLY A C   1 
ATOM   3101 O O   . GLY B 1 128 ? 20.967  33.855  23.212  1.00 51.79  ? 127 GLY A O   1 
ATOM   3102 N N   . LEU B 1 129 ? 20.163  32.951  21.319  1.00 37.68  ? 128 LEU A N   1 
ATOM   3103 C CA  . LEU B 1 129 ? 20.748  31.649  21.592  1.00 34.40  ? 128 LEU A CA  1 
ATOM   3104 C C   . LEU B 1 129 ? 22.237  31.641  21.250  1.00 38.69  ? 128 LEU A C   1 
ATOM   3105 O O   . LEU B 1 129 ? 22.767  32.554  20.613  1.00 43.02  ? 128 LEU A O   1 
ATOM   3106 C CB  . LEU B 1 129 ? 20.023  30.557  20.807  1.00 30.11  ? 128 LEU A CB  1 
ATOM   3107 C CG  . LEU B 1 129 ? 18.529  30.359  21.082  1.00 34.22  ? 128 LEU A CG  1 
ATOM   3108 C CD1 . LEU B 1 129 ? 17.983  29.196  20.258  1.00 32.99  ? 128 LEU A CD1 1 
ATOM   3109 C CD2 . LEU B 1 129 ? 18.264  30.137  22.569  1.00 32.92  ? 128 LEU A CD2 1 
ATOM   3110 N N   . SER B 1 130 ? 22.914  30.582  21.684  1.00 42.98  ? 129 SER A N   1 
ATOM   3111 C CA  . SER B 1 130 ? 24.332  30.384  21.418  1.00 33.25  ? 129 SER A CA  1 
ATOM   3112 C C   . SER B 1 130 ? 24.584  29.562  20.165  1.00 35.99  ? 129 SER A C   1 
ATOM   3113 O O   . SER B 1 130 ? 25.744  29.287  19.843  1.00 45.90  ? 129 SER A O   1 
ATOM   3114 C CB  . SER B 1 130 ? 24.999  29.697  22.611  1.00 32.58  ? 129 SER A CB  1 
ATOM   3115 O OG  . SER B 1 130 ? 24.711  28.308  22.599  1.00 39.16  ? 129 SER A OG  1 
ATOM   3116 N N   . ARG B 1 131 ? 23.535  29.159  19.461  1.00 41.20  ? 130 ARG A N   1 
ATOM   3117 C CA  . ARG B 1 131 ? 23.659  28.315  18.284  1.00 37.23  ? 130 ARG A CA  1 
ATOM   3118 C C   . ARG B 1 131 ? 22.491  28.619  17.360  1.00 29.13  ? 130 ARG A C   1 
ATOM   3119 O O   . ARG B 1 131 ? 21.484  29.189  17.797  1.00 28.45  ? 130 ARG A O   1 
ATOM   3120 C CB  . ARG B 1 131 ? 23.692  26.829  18.671  1.00 33.85  ? 130 ARG A CB  1 
ATOM   3121 C CG  . ARG B 1 131 ? 22.335  26.232  18.973  1.00 40.09  ? 130 ARG A CG  1 
ATOM   3122 C CD  . ARG B 1 131 ? 22.481  24.871  19.625  1.00 36.91  ? 130 ARG A CD  1 
ATOM   3123 N NE  . ARG B 1 131 ? 22.760  24.974  21.053  1.00 35.09  ? 130 ARG A NE  1 
ATOM   3124 C CZ  . ARG B 1 131 ? 23.224  23.976  21.795  1.00 33.85  ? 130 ARG A CZ  1 
ATOM   3125 N NH1 . ARG B 1 131 ? 23.482  22.787  21.272  1.00 32.83  ? 130 ARG A NH1 1 
ATOM   3126 N NH2 . ARG B 1 131 ? 23.430  24.174  23.093  1.00 36.74  ? 130 ARG A NH2 1 
ATOM   3127 N N   . PRO B 1 132 ? 22.597  28.273  16.075  1.00 27.42  ? 131 PRO A N   1 
ATOM   3128 C CA  . PRO B 1 132 ? 21.531  28.627  15.130  1.00 29.42  ? 131 PRO A CA  1 
ATOM   3129 C C   . PRO B 1 132 ? 20.203  27.961  15.464  1.00 29.60  ? 131 PRO A C   1 
ATOM   3130 O O   . PRO B 1 132 ? 20.149  26.897  16.084  1.00 28.97  ? 131 PRO A O   1 
ATOM   3131 C CB  . PRO B 1 132 ? 22.070  28.131  13.783  1.00 30.33  ? 131 PRO A CB  1 
ATOM   3132 C CG  . PRO B 1 132 ? 23.548  28.055  13.969  1.00 24.88  ? 131 PRO A CG  1 
ATOM   3133 C CD  . PRO B 1 132 ? 23.758  27.675  15.393  1.00 23.48  ? 131 PRO A CD  1 
ATOM   3134 N N   . LEU B 1 133 ? 19.123  28.616  15.042  1.00 28.14  ? 132 LEU A N   1 
ATOM   3135 C CA  . LEU B 1 133 ? 17.774  28.068  15.086  1.00 25.83  ? 132 LEU A CA  1 
ATOM   3136 C C   . LEU B 1 133 ? 17.253  27.984  13.658  1.00 26.54  ? 132 LEU A C   1 
ATOM   3137 O O   . LEU B 1 133 ? 17.309  28.969  12.914  1.00 23.69  ? 132 LEU A O   1 
ATOM   3138 C CB  . LEU B 1 133 ? 16.852  28.936  15.957  1.00 19.99  ? 132 LEU A CB  1 
ATOM   3139 C CG  . LEU B 1 133 ? 15.520  28.387  16.492  1.00 29.28  ? 132 LEU A CG  1 
ATOM   3140 C CD1 . LEU B 1 133 ? 14.400  28.453  15.462  1.00 30.28  ? 132 LEU A CD1 1 
ATOM   3141 C CD2 . LEU B 1 133 ? 15.690  26.964  16.996  1.00 30.64  ? 132 LEU A CD2 1 
ATOM   3142 N N   . VAL B 1 134 ? 16.768  26.806  13.273  1.00 23.56  ? 133 VAL A N   1 
ATOM   3143 C CA  . VAL B 1 134 ? 16.248  26.565  11.934  1.00 24.78  ? 133 VAL A CA  1 
ATOM   3144 C C   . VAL B 1 134 ? 14.821  26.047  12.067  1.00 30.14  ? 133 VAL A C   1 
ATOM   3145 O O   . VAL B 1 134 ? 14.410  25.534  13.108  1.00 31.24  ? 133 VAL A O   1 
ATOM   3146 C CB  . VAL B 1 134 ? 17.134  25.576  11.140  1.00 25.12  ? 133 VAL A CB  1 
ATOM   3147 C CG1 . VAL B 1 134 ? 16.974  24.162  11.677  1.00 20.61  ? 133 VAL A CG1 1 
ATOM   3148 C CG2 . VAL B 1 134 ? 16.824  25.629  9.643   1.00 27.26  ? 133 VAL A CG2 1 
ATOM   3149 N N   . GLY B 1 135 ? 14.045  26.217  10.994  1.00 18.03  ? 134 GLY A N   1 
ATOM   3150 C CA  . GLY B 1 135 ? 12.681  25.731  10.951  1.00 23.98  ? 134 GLY A CA  1 
ATOM   3151 C C   . GLY B 1 135 ? 12.613  24.417  10.196  1.00 28.11  ? 134 GLY A C   1 
ATOM   3152 O O   . GLY B 1 135 ? 13.170  24.285  9.104   1.00 27.54  ? 134 GLY A O   1 
ATOM   3153 N N   . MET B 1 136 ? 11.933  23.442  10.800  1.00 25.33  ? 135 MET A N   1 
ATOM   3154 C CA  . MET B 1 136 ? 11.684  22.139  10.183  1.00 25.90  ? 135 MET A CA  1 
ATOM   3155 C C   . MET B 1 136 ? 10.188  21.884  10.313  1.00 27.69  ? 135 MET A C   1 
ATOM   3156 O O   . MET B 1 136 ? 9.732   21.267  11.279  1.00 31.83  ? 135 MET A O   1 
ATOM   3157 C CB  . MET B 1 136 ? 12.516  21.036  10.831  1.00 24.95  ? 135 MET A CB  1 
ATOM   3158 C CG  . MET B 1 136 ? 12.706  19.815  9.939   1.00 33.18  ? 135 MET A CG  1 
ATOM   3159 S SD  . MET B 1 136 ? 13.521  18.423  10.762  1.00 32.06  ? 135 MET A SD  1 
ATOM   3160 C CE  . MET B 1 136 ? 14.029  17.453  9.339   1.00 29.71  ? 135 MET A CE  1 
ATOM   3161 N N   . HIS B 1 137 ? 9.427   22.370  9.338   1.00 29.97  ? 136 HIS A N   1 
ATOM   3162 C CA  . HIS B 1 137 ? 7.971   22.368  9.412   1.00 28.62  ? 136 HIS A CA  1 
ATOM   3163 C C   . HIS B 1 137 ? 7.440   21.091  8.771   1.00 29.46  ? 136 HIS A C   1 
ATOM   3164 O O   . HIS B 1 137 ? 7.574   20.891  7.558   1.00 29.52  ? 136 HIS A O   1 
ATOM   3165 C CB  . HIS B 1 137 ? 7.402   23.609  8.731   1.00 30.27  ? 136 HIS A CB  1 
ATOM   3166 C CG  . HIS B 1 137 ? 5.911   23.701  8.800   1.00 28.40  ? 136 HIS A CG  1 
ATOM   3167 N ND1 . HIS B 1 137 ? 5.127   23.942  7.692   1.00 37.49  ? 136 HIS A ND1 1 
ATOM   3168 C CD2 . HIS B 1 137 ? 5.059   23.573  9.844   1.00 26.43  ? 136 HIS A CD2 1 
ATOM   3169 C CE1 . HIS B 1 137 ? 3.856   23.963  8.051   1.00 35.52  ? 136 HIS A CE1 1 
ATOM   3170 N NE2 . HIS B 1 137 ? 3.786   23.741  9.351   1.00 31.98  ? 136 HIS A NE2 1 
ATOM   3171 N N   . PHE B 1 138 ? 6.844   20.229  9.586   1.00 28.55  ? 137 PHE A N   1 
ATOM   3172 C CA  . PHE B 1 138 ? 6.210   19.009  9.117   1.00 27.48  ? 137 PHE A CA  1 
ATOM   3173 C C   . PHE B 1 138 ? 4.746   19.282  8.781   1.00 32.78  ? 137 PHE A C   1 
ATOM   3174 O O   . PHE B 1 138 ? 4.201   20.348  9.076   1.00 37.42  ? 137 PHE A O   1 
ATOM   3175 C CB  . PHE B 1 138 ? 6.311   17.902  10.170  1.00 28.16  ? 137 PHE A CB  1 
ATOM   3176 C CG  . PHE B 1 138 ? 7.708   17.388  10.398  1.00 26.43  ? 137 PHE A CG  1 
ATOM   3177 C CD1 . PHE B 1 138 ? 8.682   18.198  10.964  1.00 26.24  ? 137 PHE A CD1 1 
ATOM   3178 C CD2 . PHE B 1 138 ? 8.036   16.079  10.079  1.00 20.34  ? 137 PHE A CD2 1 
ATOM   3179 C CE1 . PHE B 1 138 ? 9.962   17.720  11.184  1.00 32.61  ? 137 PHE A CE1 1 
ATOM   3180 C CE2 . PHE B 1 138 ? 9.316   15.598  10.289  1.00 21.61  ? 137 PHE A CE2 1 
ATOM   3181 C CZ  . PHE B 1 138 ? 10.278  16.416  10.847  1.00 29.36  ? 137 PHE A CZ  1 
ATOM   3182 N N   . PHE B 1 139 ? 4.101   18.296  8.168   1.00 30.51  ? 138 PHE A N   1 
ATOM   3183 C CA  . PHE B 1 139 ? 2.701   18.413  7.784   1.00 39.11  ? 138 PHE A CA  1 
ATOM   3184 C C   . PHE B 1 139 ? 1.939   17.212  8.321   1.00 34.55  ? 138 PHE A C   1 
ATOM   3185 O O   . PHE B 1 139 ? 2.382   16.071  8.162   1.00 38.39  ? 138 PHE A O   1 
ATOM   3186 C CB  . PHE B 1 139 ? 2.560   18.523  6.262   1.00 25.97  ? 138 PHE A CB  1 
ATOM   3187 C CG  . PHE B 1 139 ? 2.909   19.884  5.727   1.00 40.81  ? 138 PHE A CG  1 
ATOM   3188 C CD1 . PHE B 1 139 ? 4.233   20.258  5.553   1.00 36.83  ? 138 PHE A CD1 1 
ATOM   3189 C CD2 . PHE B 1 139 ? 1.913   20.798  5.416   1.00 42.62  ? 138 PHE A CD2 1 
ATOM   3190 C CE1 . PHE B 1 139 ? 4.557   21.514  5.074   1.00 37.32  ? 138 PHE A CE1 1 
ATOM   3191 C CE2 . PHE B 1 139 ? 2.231   22.054  4.934   1.00 35.49  ? 138 PHE A CE2 1 
ATOM   3192 C CZ  . PHE B 1 139 ? 3.555   22.411  4.762   1.00 33.42  ? 138 PHE A CZ  1 
ATOM   3193 N N   . ASN B 1 140 ? 0.801   17.468  8.950   1.00 34.69  ? 139 ASN A N   1 
ATOM   3194 C CA  . ASN B 1 140 ? 0.062   16.399  9.608   1.00 41.14  ? 139 ASN A CA  1 
ATOM   3195 C C   . ASN B 1 140 ? -0.635  15.518  8.576   1.00 42.12  ? 139 ASN A C   1 
ATOM   3196 O O   . ASN B 1 140 ? -1.282  16.038  7.660   1.00 38.87  ? 139 ASN A O   1 
ATOM   3197 C CB  . ASN B 1 140 ? -0.957  16.982  10.581  1.00 42.70  ? 139 ASN A CB  1 
ATOM   3198 C CG  . ASN B 1 140 ? -1.971  15.956  11.040  1.00 48.77  ? 139 ASN A CG  1 
ATOM   3199 O OD1 . ASN B 1 140 ? -1.743  15.237  12.013  1.00 58.82  ? 139 ASN A OD1 1 
ATOM   3200 N ND2 . ASN B 1 140 ? -3.100  15.883  10.343  1.00 48.27  ? 139 ASN A ND2 1 
ATOM   3201 N N   . PRO B 1 141 ? -0.530  14.184  8.683   1.00 49.67  ? 140 PRO A N   1 
ATOM   3202 C CA  . PRO B 1 141 ? 0.267   13.418  9.656   1.00 40.27  ? 140 PRO A CA  1 
ATOM   3203 C C   . PRO B 1 141 ? 1.736   13.357  9.245   1.00 36.17  ? 140 PRO A C   1 
ATOM   3204 O O   . PRO B 1 141 ? 2.056   12.976  8.119   1.00 39.65  ? 140 PRO A O   1 
ATOM   3205 C CB  . PRO B 1 141 ? -0.406  12.040  9.640   1.00 39.68  ? 140 PRO A CB  1 
ATOM   3206 C CG  . PRO B 1 141 ? -0.961  11.910  8.252   1.00 39.42  ? 140 PRO A CG  1 
ATOM   3207 C CD  . PRO B 1 141 ? -1.343  13.305  7.821   1.00 37.84  ? 140 PRO A CD  1 
ATOM   3208 N N   . ALA B 1 142 ? 2.648   13.729  10.149  1.00 31.83  ? 141 ALA A N   1 
ATOM   3209 C CA  . ALA B 1 142 ? 4.048   13.910  9.773   1.00 33.06  ? 141 ALA A CA  1 
ATOM   3210 C C   . ALA B 1 142 ? 4.698   12.607  9.326   1.00 33.13  ? 141 ALA A C   1 
ATOM   3211 O O   . ALA B 1 142 ? 5.592   12.624  8.471   1.00 35.70  ? 141 ALA A O   1 
ATOM   3212 C CB  . ALA B 1 142 ? 4.828   14.524  10.937  1.00 30.51  ? 141 ALA A CB  1 
ATOM   3213 N N   . ASP B 1 143 ? 4.268   11.472  9.882   1.00 37.26  ? 142 ASP A N   1 
ATOM   3214 C CA  . ASP B 1 143 ? 4.844   10.191  9.489   1.00 41.45  ? 142 ASP A CA  1 
ATOM   3215 C C   . ASP B 1 143 ? 4.430   9.775   8.084   1.00 40.20  ? 142 ASP A C   1 
ATOM   3216 O O   . ASP B 1 143 ? 5.077   8.903   7.495   1.00 41.63  ? 142 ASP A O   1 
ATOM   3217 C CB  . ASP B 1 143 ? 4.450   9.104   10.494  1.00 40.77  ? 142 ASP A CB  1 
ATOM   3218 C CG  . ASP B 1 143 ? 2.948   8.889   10.565  1.00 40.07  ? 142 ASP A CG  1 
ATOM   3219 O OD1 . ASP B 1 143 ? 2.238   9.785   11.067  1.00 47.87  ? 142 ASP A OD1 1 
ATOM   3220 O OD2 . ASP B 1 143 ? 2.479   7.816   10.135  1.00 42.83  ? 142 ASP A OD2 1 
ATOM   3221 N N   . ARG B 1 144 ? 3.379   10.376  7.535   1.00 30.88  ? 143 ARG A N   1 
ATOM   3222 C CA  . ARG B 1 144 ? 2.878   10.022  6.213   1.00 42.28  ? 143 ARG A CA  1 
ATOM   3223 C C   . ARG B 1 144 ? 3.118   11.096  5.163   1.00 37.88  ? 143 ARG A C   1 
ATOM   3224 O O   . ARG B 1 144 ? 3.467   10.768  4.028   1.00 37.56  ? 143 ARG A O   1 
ATOM   3225 C CB  . ARG B 1 144 ? 1.377   9.706   6.286   1.00 47.48  ? 143 ARG A CB  1 
ATOM   3226 C CG  . ARG B 1 144 ? 0.923   8.617   5.325   1.00 58.45  ? 143 ARG A CG  1 
ATOM   3227 C CD  . ARG B 1 144 ? 1.043   7.228   5.941   1.00 56.92  ? 143 ARG A CD  1 
ATOM   3228 N NE  . ARG B 1 144 ? 1.288   6.207   4.927   1.00 71.51  ? 143 ARG A NE  1 
ATOM   3229 C CZ  . ARG B 1 144 ? 0.351   5.676   4.153   1.00 76.11  ? 143 ARG A CZ  1 
ATOM   3230 N NH1 . ARG B 1 144 ? -0.919  6.033   4.259   1.00 82.21  ? 143 ARG A NH1 1 
ATOM   3231 N NH2 . ARG B 1 144 ? 0.697   4.765   3.247   1.00 67.12  ? 143 ARG A NH2 1 
ATOM   3232 N N   . MET B 1 145 ? 2.955   12.372  5.513   1.00 37.80  ? 144 MET A N   1 
ATOM   3233 C CA  . MET B 1 145 ? 3.160   13.452  4.554   1.00 28.71  ? 144 MET A CA  1 
ATOM   3234 C C   . MET B 1 145 ? 4.641   13.627  4.241   1.00 33.15  ? 144 MET A C   1 
ATOM   3235 O O   . MET B 1 145 ? 5.493   13.592  5.134   1.00 32.46  ? 144 MET A O   1 
ATOM   3236 C CB  . MET B 1 145 ? 2.582   14.759  5.093   1.00 35.72  ? 144 MET A CB  1 
ATOM   3237 C CG  . MET B 1 145 ? 1.079   14.725  5.287   1.00 43.79  ? 144 MET A CG  1 
ATOM   3238 S SD  . MET B 1 145 ? 0.192   14.812  3.721   1.00 52.40  ? 144 MET A SD  1 
ATOM   3239 C CE  . MET B 1 145 ? -0.848  16.246  4.003   1.00 44.93  ? 144 MET A CE  1 
ATOM   3240 N N   . LYS B 1 146 ? 4.944   13.842  2.962   1.00 30.21  ? 145 LYS A N   1 
ATOM   3241 C CA  . LYS B 1 146 ? 6.313   13.769  2.476   1.00 34.63  ? 145 LYS A CA  1 
ATOM   3242 C C   . LYS B 1 146 ? 7.012   15.120  2.382   1.00 32.82  ? 145 LYS A C   1 
ATOM   3243 O O   . LYS B 1 146 ? 8.230   15.150  2.174   1.00 30.30  ? 145 LYS A O   1 
ATOM   3244 C CB  . LYS B 1 146 ? 6.338   13.074  1.107   1.00 35.46  ? 145 LYS A CB  1 
ATOM   3245 C CG  . LYS B 1 146 ? 6.185   11.554  1.200   1.00 46.80  ? 145 LYS A CG  1 
ATOM   3246 C CD  . LYS B 1 146 ? 7.499   10.835  0.905   1.00 54.00  ? 145 LYS A CD  1 
ATOM   3247 C CE  . LYS B 1 146 ? 8.011   11.169  -0.490  1.00 62.46  ? 145 LYS A CE  1 
ATOM   3248 N NZ  . LYS B 1 146 ? 9.329   10.538  -0.798  1.00 54.64  ? 145 LYS A NZ  1 
ATOM   3249 N N   . LEU B 1 147 ? 6.294   16.228  2.553   1.00 27.99  ? 146 LEU A N   1 
ATOM   3250 C CA  . LEU B 1 147 ? 6.885   17.552  2.408   1.00 27.99  ? 146 LEU A CA  1 
ATOM   3251 C C   . LEU B 1 147 ? 7.441   18.054  3.736   1.00 28.18  ? 146 LEU A C   1 
ATOM   3252 O O   . LEU B 1 147 ? 6.810   17.912  4.788   1.00 19.83  ? 146 LEU A O   1 
ATOM   3253 C CB  . LEU B 1 147 ? 5.855   18.547  1.872   1.00 25.15  ? 146 LEU A CB  1 
ATOM   3254 C CG  . LEU B 1 147 ? 6.275   20.019  1.916   1.00 30.62  ? 146 LEU A CG  1 
ATOM   3255 C CD1 . LEU B 1 147 ? 7.380   20.287  0.910   1.00 30.42  ? 146 LEU A CD1 1 
ATOM   3256 C CD2 . LEU B 1 147 ? 5.086   20.929  1.659   1.00 30.84  ? 146 LEU A CD2 1 
ATOM   3257 N N   . ILE B 1 148 ? 8.628   18.652  3.674   1.00 29.37  ? 147 ILE A N   1 
ATOM   3258 C CA  . ILE B 1 148 ? 9.256   19.304  4.816   1.00 24.26  ? 147 ILE A CA  1 
ATOM   3259 C C   . ILE B 1 148 ? 9.708   20.689  4.367   1.00 30.32  ? 147 ILE A C   1 
ATOM   3260 O O   . ILE B 1 148 ? 10.576  20.808  3.494   1.00 36.18  ? 147 ILE A O   1 
ATOM   3261 C CB  . ILE B 1 148 ? 10.450  18.498  5.355   1.00 29.16  ? 147 ILE A CB  1 
ATOM   3262 C CG1 . ILE B 1 148 ? 9.978   17.252  6.112   1.00 33.77  ? 147 ILE A CG1 1 
ATOM   3263 C CG2 . ILE B 1 148 ? 11.315  19.372  6.252   1.00 25.86  ? 147 ILE A CG2 1 
ATOM   3264 C CD1 . ILE B 1 148 ? 9.044   17.548  7.253   1.00 23.34  ? 147 ILE A CD1 1 
ATOM   3265 N N   . GLU B 1 149 ? 9.121   21.730  4.951   1.00 24.99  ? 148 GLU A N   1 
ATOM   3266 C CA  . GLU B 1 149 ? 9.562   23.100  4.718   1.00 30.36  ? 148 GLU A CA  1 
ATOM   3267 C C   . GLU B 1 149 ? 10.720  23.414  5.660   1.00 27.92  ? 148 GLU A C   1 
ATOM   3268 O O   . GLU B 1 149 ? 10.549  23.416  6.884   1.00 28.84  ? 148 GLU A O   1 
ATOM   3269 C CB  . GLU B 1 149 ? 8.413   24.091  4.922   1.00 21.47  ? 148 GLU A CB  1 
ATOM   3270 C CG  . GLU B 1 149 ? 7.299   23.965  3.883   1.00 26.07  ? 148 GLU A CG  1 
ATOM   3271 C CD  . GLU B 1 149 ? 6.183   24.991  4.059   1.00 36.21  ? 148 GLU A CD  1 
ATOM   3272 O OE1 . GLU B 1 149 ? 5.576   25.056  5.151   1.00 31.86  ? 148 GLU A OE1 1 
ATOM   3273 O OE2 . GLU B 1 149 ? 5.900   25.728  3.091   1.00 39.72  ? 148 GLU A OE2 1 
ATOM   3274 N N   . VAL B 1 150 ? 11.892  23.673  5.090   1.00 25.39  ? 149 VAL A N   1 
ATOM   3275 C CA  . VAL B 1 150 ? 13.085  24.030  5.849   1.00 19.26  ? 149 VAL A CA  1 
ATOM   3276 C C   . VAL B 1 150 ? 13.172  25.550  5.864   1.00 24.26  ? 149 VAL A C   1 
ATOM   3277 O O   . VAL B 1 150 ? 13.443  26.178  4.835   1.00 29.70  ? 149 VAL A O   1 
ATOM   3278 C CB  . VAL B 1 150 ? 14.345  23.394  5.248   1.00 18.81  ? 149 VAL A CB  1 
ATOM   3279 C CG1 . VAL B 1 150 ? 15.551  23.656  6.131   1.00 22.72  ? 149 VAL A CG1 1 
ATOM   3280 C CG2 . VAL B 1 150 ? 14.130  21.895  5.051   1.00 24.10  ? 149 VAL A CG2 1 
ATOM   3281 N N   . ILE B 1 151 ? 12.931  26.146  7.028   1.00 23.26  ? 150 ILE A N   1 
ATOM   3282 C CA  . ILE B 1 151 ? 12.795  27.592  7.161   1.00 24.83  ? 150 ILE A CA  1 
ATOM   3283 C C   . ILE B 1 151 ? 14.135  28.172  7.586   1.00 28.98  ? 150 ILE A C   1 
ATOM   3284 O O   . ILE B 1 151 ? 14.620  27.895  8.689   1.00 29.53  ? 150 ILE A O   1 
ATOM   3285 C CB  . ILE B 1 151 ? 11.698  27.961  8.171   1.00 27.64  ? 150 ILE A CB  1 
ATOM   3286 C CG1 . ILE B 1 151 ? 10.545  26.959  8.102   1.00 22.14  ? 150 ILE A CG1 1 
ATOM   3287 C CG2 . ILE B 1 151 ? 11.205  29.374  7.917   1.00 29.94  ? 150 ILE A CG2 1 
ATOM   3288 C CD1 . ILE B 1 151 ? 9.789   26.996  6.803   1.00 27.41  ? 150 ILE A CD1 1 
ATOM   3289 N N   . ALA B 1 152 ? 14.732  28.980  6.715   1.00 25.09  ? 151 ALA A N   1 
ATOM   3290 C CA  . ALA B 1 152 ? 15.968  29.680  7.033   1.00 24.79  ? 151 ALA A CA  1 
ATOM   3291 C C   . ALA B 1 152 ? 15.629  31.001  7.710   1.00 35.36  ? 151 ALA A C   1 
ATOM   3292 O O   . ALA B 1 152 ? 14.896  31.823  7.150   1.00 28.57  ? 151 ALA A O   1 
ATOM   3293 C CB  . ALA B 1 152 ? 16.802  29.919  5.775   1.00 20.66  ? 151 ALA A CB  1 
ATOM   3294 N N   . GLY B 1 153 ? 16.152  31.197  8.916   1.00 35.45  ? 152 GLY A N   1 
ATOM   3295 C CA  . GLY B 1 153 ? 16.000  32.457  9.603   1.00 28.21  ? 152 GLY A CA  1 
ATOM   3296 C C   . GLY B 1 153 ? 16.963  33.497  9.075   1.00 31.11  ? 152 GLY A C   1 
ATOM   3297 O O   . GLY B 1 153 ? 17.777  33.248  8.187   1.00 35.82  ? 152 GLY A O   1 
ATOM   3298 N N   . CYS B 1 154 ? 16.861  34.699  9.645   1.00 30.28  ? 153 CYS A N   1 
ATOM   3299 C CA  . CYS B 1 154 ? 17.709  35.797  9.193   1.00 35.31  ? 153 CYS A CA  1 
ATOM   3300 C C   . CYS B 1 154 ? 19.185  35.500  9.423   1.00 34.42  ? 153 CYS A C   1 
ATOM   3301 O O   . CYS B 1 154 ? 20.031  35.901  8.615   1.00 35.43  ? 153 CYS A O   1 
ATOM   3302 C CB  . CYS B 1 154 ? 17.310  37.093  9.898   1.00 31.35  ? 153 CYS A CB  1 
ATOM   3303 S SG  . CYS B 1 154 ? 18.369  38.507  9.530   1.00 39.05  ? 153 CYS A SG  1 
ATOM   3304 N N   . ASN B 1 155 ? 19.512  34.792  10.503  1.00 35.60  ? 154 ASN A N   1 
ATOM   3305 C CA  . ASN B 1 155 ? 20.892  34.486  10.855  1.00 34.93  ? 154 ASN A CA  1 
ATOM   3306 C C   . ASN B 1 155 ? 21.206  32.997  10.781  1.00 36.05  ? 154 ASN A C   1 
ATOM   3307 O O   . ASN B 1 155 ? 22.275  32.579  11.238  1.00 34.56  ? 154 ASN A O   1 
ATOM   3308 C CB  . ASN B 1 155 ? 21.205  35.023  12.254  1.00 26.98  ? 154 ASN A CB  1 
ATOM   3309 C CG  . ASN B 1 155 ? 21.112  36.536  12.330  1.00 34.76  ? 154 ASN A CG  1 
ATOM   3310 O OD1 . ASN B 1 155 ? 21.606  37.245  11.449  1.00 33.32  ? 154 ASN A OD1 1 
ATOM   3311 N ND2 . ASN B 1 155 ? 20.475  37.039  13.384  1.00 30.29  ? 154 ASN A ND2 1 
ATOM   3312 N N   . THR B 1 156 ? 20.313  32.190  10.223  1.00 35.57  ? 155 THR A N   1 
ATOM   3313 C CA  . THR B 1 156 ? 20.582  30.763  10.072  1.00 39.61  ? 155 THR A CA  1 
ATOM   3314 C C   . THR B 1 156 ? 21.655  30.550  9.011   1.00 35.70  ? 155 THR A C   1 
ATOM   3315 O O   . THR B 1 156 ? 21.469  30.974  7.864   1.00 33.01  ? 155 THR A O   1 
ATOM   3316 C CB  . THR B 1 156 ? 19.308  30.009  9.692   1.00 34.60  ? 155 THR A CB  1 
ATOM   3317 O OG1 . THR B 1 156 ? 18.280  30.282  10.654  1.00 31.55  ? 155 THR A OG1 1 
ATOM   3318 C CG2 . THR B 1 156 ? 19.568  28.512  9.656   1.00 36.30  ? 155 THR A CG2 1 
ATOM   3319 N N   . PRO B 1 157 ? 22.782  29.921  9.339   1.00 40.90  ? 156 PRO A N   1 
ATOM   3320 C CA  . PRO B 1 157 ? 23.809  29.673  8.322   1.00 34.50  ? 156 PRO A CA  1 
ATOM   3321 C C   . PRO B 1 157 ? 23.345  28.646  7.304   1.00 34.10  ? 156 PRO A C   1 
ATOM   3322 O O   . PRO B 1 157 ? 22.501  27.792  7.586   1.00 42.46  ? 156 PRO A O   1 
ATOM   3323 C CB  . PRO B 1 157 ? 25.002  29.149  9.134   1.00 37.36  ? 156 PRO A CB  1 
ATOM   3324 C CG  . PRO B 1 157 ? 24.697  29.496  10.567  1.00 33.89  ? 156 PRO A CG  1 
ATOM   3325 C CD  . PRO B 1 157 ? 23.208  29.482  10.676  1.00 35.96  ? 156 PRO A CD  1 
ATOM   3326 N N   . ALA B 1 158 ? 23.916  28.737  6.100   1.00 27.93  ? 157 ALA A N   1 
ATOM   3327 C CA  . ALA B 1 158 ? 23.529  27.821  5.032   1.00 33.06  ? 157 ALA A CA  1 
ATOM   3328 C C   . ALA B 1 158 ? 23.896  26.383  5.366   1.00 36.06  ? 157 ALA A C   1 
ATOM   3329 O O   . ALA B 1 158 ? 23.254  25.449  4.869   1.00 36.37  ? 157 ALA A O   1 
ATOM   3330 C CB  . ALA B 1 158 ? 24.177  28.239  3.712   1.00 30.54  ? 157 ALA A CB  1 
ATOM   3331 N N   . GLU B 1 159 ? 24.915  26.181  6.205   1.00 38.65  ? 158 GLU A N   1 
ATOM   3332 C CA  . GLU B 1 159 ? 25.290  24.823  6.585   1.00 43.11  ? 158 GLU A CA  1 
ATOM   3333 C C   . GLU B 1 159 ? 24.198  24.158  7.416   1.00 39.87  ? 158 GLU A C   1 
ATOM   3334 O O   . GLU B 1 159 ? 23.922  22.964  7.249   1.00 42.38  ? 158 GLU A O   1 
ATOM   3335 C CB  . GLU B 1 159 ? 26.616  24.835  7.344   1.00 36.03  ? 158 GLU A CB  1 
ATOM   3336 C CG  . GLU B 1 159 ? 27.212  23.448  7.553   1.00 64.23  ? 158 GLU A CG  1 
ATOM   3337 C CD  . GLU B 1 159 ? 27.056  22.555  6.331   1.00 68.90  ? 158 GLU A CD  1 
ATOM   3338 O OE1 . GLU B 1 159 ? 26.302  21.561  6.406   1.00 76.85  ? 158 GLU A OE1 1 
ATOM   3339 O OE2 . GLU B 1 159 ? 27.684  22.850  5.292   1.00 83.69  ? 158 GLU A OE2 1 
ATOM   3340 N N   . THR B 1 160 ? 23.558  24.916  8.308   1.00 33.02  ? 159 THR A N   1 
ATOM   3341 C CA  . THR B 1 160 ? 22.463  24.358  9.095   1.00 32.09  ? 159 THR A CA  1 
ATOM   3342 C C   . THR B 1 160 ? 21.273  24.011  8.209   1.00 33.13  ? 159 THR A C   1 
ATOM   3343 O O   . THR B 1 160 ? 20.639  22.964  8.391   1.00 30.57  ? 159 THR A O   1 
ATOM   3344 C CB  . THR B 1 160 ? 22.058  25.338  10.195  1.00 34.92  ? 159 THR A CB  1 
ATOM   3345 O OG1 . THR B 1 160 ? 23.180  25.579  11.053  1.00 35.61  ? 159 THR A OG1 1 
ATOM   3346 C CG2 . THR B 1 160 ? 20.906  24.778  11.022  1.00 31.89  ? 159 THR A CG2 1 
ATOM   3347 N N   . VAL B 1 161 ? 20.966  24.870  7.234   1.00 37.95  ? 160 VAL A N   1 
ATOM   3348 C CA  . VAL B 1 161 ? 19.890  24.575  6.291   1.00 35.38  ? 160 VAL A CA  1 
ATOM   3349 C C   . VAL B 1 161 ? 20.190  23.290  5.529   1.00 36.17  ? 160 VAL A C   1 
ATOM   3350 O O   . VAL B 1 161 ? 19.307  22.444  5.336   1.00 37.16  ? 160 VAL A O   1 
ATOM   3351 C CB  . VAL B 1 161 ? 19.679  25.766  5.335   1.00 32.58  ? 160 VAL A CB  1 
ATOM   3352 C CG1 . VAL B 1 161 ? 18.835  25.353  4.135   1.00 33.25  ? 160 VAL A CG1 1 
ATOM   3353 C CG2 . VAL B 1 161 ? 19.040  26.935  6.070   1.00 28.33  ? 160 VAL A CG2 1 
ATOM   3354 N N   . GLU B 1 162 ? 21.444  23.112  5.102   1.00 34.33  ? 161 GLU A N   1 
ATOM   3355 C CA  . GLU B 1 162 ? 21.795  21.938  4.309   1.00 30.05  ? 161 GLU A CA  1 
ATOM   3356 C C   . GLU B 1 162 ? 21.666  20.658  5.122   1.00 34.74  ? 161 GLU A C   1 
ATOM   3357 O O   . GLU B 1 162 ? 21.158  19.648  4.622   1.00 38.30  ? 161 GLU A O   1 
ATOM   3358 C CB  . GLU B 1 162 ? 23.213  22.080  3.759   1.00 35.24  ? 161 GLU A CB  1 
ATOM   3359 C CG  . GLU B 1 162 ? 23.706  20.856  2.998   1.00 55.54  ? 161 GLU A CG  1 
ATOM   3360 C CD  . GLU B 1 162 ? 23.231  20.823  1.552   1.00 57.37  ? 161 GLU A CD  1 
ATOM   3361 O OE1 . GLU B 1 162 ? 22.367  21.649  1.179   1.00 48.16  ? 161 GLU A OE1 1 
ATOM   3362 O OE2 . GLU B 1 162 ? 23.724  19.963  0.789   1.00 63.35  ? 161 GLU A OE2 1 
ATOM   3363 N N   . LYS B 1 163 ? 22.115  20.678  6.378   1.00 37.78  ? 162 LYS A N   1 
ATOM   3364 C CA  . LYS B 1 163 ? 22.041  19.475  7.197   1.00 36.07  ? 162 LYS A CA  1 
ATOM   3365 C C   . LYS B 1 163 ? 20.596  19.054  7.443   1.00 34.54  ? 162 LYS A C   1 
ATOM   3366 O O   . LYS B 1 163 ? 20.300  17.853  7.484   1.00 30.71  ? 162 LYS A O   1 
ATOM   3367 C CB  . LYS B 1 163 ? 22.779  19.695  8.519   1.00 35.41  ? 162 LYS A CB  1 
ATOM   3368 C CG  . LYS B 1 163 ? 22.789  18.480  9.425   1.00 53.10  ? 162 LYS A CG  1 
ATOM   3369 C CD  . LYS B 1 163 ? 23.835  17.452  9.002   1.00 58.70  ? 162 LYS A CD  1 
ATOM   3370 C CE  . LYS B 1 163 ? 23.252  16.043  9.007   1.00 48.67  ? 162 LYS A CE  1 
ATOM   3371 N NZ  . LYS B 1 163 ? 24.228  15.020  9.478   1.00 53.71  ? 162 LYS A NZ  1 
ATOM   3372 N N   . ILE B 1 164 ? 19.682  20.018  7.589   1.00 33.85  ? 163 ILE A N   1 
ATOM   3373 C CA  . ILE B 1 164 ? 18.271  19.676  7.745   1.00 28.48  ? 163 ILE A CA  1 
ATOM   3374 C C   . ILE B 1 164 ? 17.717  19.083  6.451   1.00 33.92  ? 163 ILE A C   1 
ATOM   3375 O O   . ILE B 1 164 ? 16.887  18.167  6.479   1.00 27.42  ? 163 ILE A O   1 
ATOM   3376 C CB  . ILE B 1 164 ? 17.467  20.909  8.202   1.00 30.07  ? 163 ILE A CB  1 
ATOM   3377 C CG1 . ILE B 1 164 ? 17.959  21.387  9.573   1.00 27.98  ? 163 ILE A CG1 1 
ATOM   3378 C CG2 . ILE B 1 164 ? 15.970  20.596  8.249   1.00 26.12  ? 163 ILE A CG2 1 
ATOM   3379 C CD1 . ILE B 1 164 ? 17.311  20.681  10.751  1.00 14.27  ? 163 ILE A CD1 1 
ATOM   3380 N N   . LYS B 1 165 ? 18.166  19.592  5.300   1.00 32.81  ? 164 LYS A N   1 
ATOM   3381 C CA  . LYS B 1 165 ? 17.786  18.985  4.026   1.00 33.43  ? 164 LYS A CA  1 
ATOM   3382 C C   . LYS B 1 165 ? 18.227  17.528  3.971   1.00 32.60  ? 164 LYS A C   1 
ATOM   3383 O O   . LYS B 1 165 ? 17.460  16.649  3.561   1.00 31.32  ? 164 LYS A O   1 
ATOM   3384 C CB  . LYS B 1 165 ? 18.399  19.766  2.862   1.00 35.82  ? 164 LYS A CB  1 
ATOM   3385 C CG  . LYS B 1 165 ? 17.603  20.973  2.390   1.00 38.40  ? 164 LYS A CG  1 
ATOM   3386 C CD  . LYS B 1 165 ? 18.347  21.680  1.269   1.00 33.15  ? 164 LYS A CD  1 
ATOM   3387 C CE  . LYS B 1 165 ? 17.429  22.567  0.448   1.00 45.38  ? 164 LYS A CE  1 
ATOM   3388 N NZ  . LYS B 1 165 ? 18.043  23.904  0.203   1.00 49.76  ? 164 LYS A NZ  1 
ATOM   3389 N N   . GLU B 1 166 ? 19.467  17.255  4.386   1.00 28.39  ? 165 GLU A N   1 
ATOM   3390 C CA  . GLU B 1 166 ? 19.980  15.890  4.349   1.00 33.48  ? 165 GLU A CA  1 
ATOM   3391 C C   . GLU B 1 166 ? 19.242  14.989  5.331   1.00 34.81  ? 165 GLU A C   1 
ATOM   3392 O O   . GLU B 1 166 ? 18.973  13.821  5.025   1.00 35.21  ? 165 GLU A O   1 
ATOM   3393 C CB  . GLU B 1 166 ? 21.479  15.886  4.638   1.00 33.79  ? 165 GLU A CB  1 
ATOM   3394 C CG  . GLU B 1 166 ? 22.284  16.740  3.677   1.00 41.42  ? 165 GLU A CG  1 
ATOM   3395 C CD  . GLU B 1 166 ? 23.731  16.891  4.100   1.00 51.08  ? 165 GLU A CD  1 
ATOM   3396 O OE1 . GLU B 1 166 ? 24.078  16.436  5.211   1.00 54.45  ? 165 GLU A OE1 1 
ATOM   3397 O OE2 . GLU B 1 166 ? 24.520  17.467  3.323   1.00 58.77  ? 165 GLU A OE2 1 
ATOM   3398 N N   . ILE B 1 167 ? 18.908  15.508  6.516   1.00 27.39  ? 166 ILE A N   1 
ATOM   3399 C CA  . ILE B 1 167 ? 18.129  14.720  7.469   1.00 27.76  ? 166 ILE A CA  1 
ATOM   3400 C C   . ILE B 1 167 ? 16.755  14.405  6.893   1.00 30.66  ? 166 ILE A C   1 
ATOM   3401 O O   . ILE B 1 167 ? 16.242  13.289  7.044   1.00 31.55  ? 166 ILE A O   1 
ATOM   3402 C CB  . ILE B 1 167 ? 18.025  15.460  8.816   1.00 28.94  ? 166 ILE A CB  1 
ATOM   3403 C CG1 . ILE B 1 167 ? 19.368  15.432  9.543   1.00 24.43  ? 166 ILE A CG1 1 
ATOM   3404 C CG2 . ILE B 1 167 ? 16.932  14.851  9.686   1.00 17.09  ? 166 ILE A CG2 1 
ATOM   3405 C CD1 . ILE B 1 167 ? 19.493  16.478  10.616  1.00 31.18  ? 166 ILE A CD1 1 
ATOM   3406 N N   . SER B 1 168 ? 16.144  15.380  6.213   1.00 26.01  ? 167 SER A N   1 
ATOM   3407 C CA  . SER B 1 168 ? 14.814  15.169  5.653   1.00 29.10  ? 167 SER A CA  1 
ATOM   3408 C C   . SER B 1 168 ? 14.813  14.030  4.641   1.00 31.79  ? 167 SER A C   1 
ATOM   3409 O O   . SER B 1 168 ? 13.920  13.175  4.663   1.00 32.36  ? 167 SER A O   1 
ATOM   3410 C CB  . SER B 1 168 ? 14.299  16.460  5.015   1.00 31.42  ? 167 SER A CB  1 
ATOM   3411 O OG  . SER B 1 168 ? 14.391  17.549  5.919   1.00 30.46  ? 167 SER A OG  1 
ATOM   3412 N N   . VAL B 1 169 ? 15.807  13.995  3.750   1.00 29.02  ? 168 VAL A N   1 
ATOM   3413 C CA  . VAL B 1 169 ? 15.846  12.909  2.774   1.00 37.33  ? 168 VAL A CA  1 
ATOM   3414 C C   . VAL B 1 169 ? 16.221  11.598  3.452   1.00 32.50  ? 168 VAL A C   1 
ATOM   3415 O O   . VAL B 1 169 ? 15.780  10.524  3.025   1.00 34.95  ? 168 VAL A O   1 
ATOM   3416 C CB  . VAL B 1 169 ? 16.798  13.248  1.607   1.00 35.58  ? 168 VAL A CB  1 
ATOM   3417 C CG1 . VAL B 1 169 ? 16.527  14.654  1.091   1.00 29.23  ? 168 VAL A CG1 1 
ATOM   3418 C CG2 . VAL B 1 169 ? 18.253  13.103  2.017   1.00 38.66  ? 168 VAL A CG2 1 
ATOM   3419 N N   . ALA B 1 170 ? 17.013  11.659  4.525   1.00 28.41  ? 169 ALA A N   1 
ATOM   3420 C CA  . ALA B 1 170 ? 17.382  10.441  5.231   1.00 29.26  ? 169 ALA A CA  1 
ATOM   3421 C C   . ALA B 1 170 ? 16.160  9.754   5.828   1.00 33.14  ? 169 ALA A C   1 
ATOM   3422 O O   . ALA B 1 170 ? 16.097  8.519   5.855   1.00 33.34  ? 169 ALA A O   1 
ATOM   3423 C CB  . ALA B 1 170 ? 18.412  10.759  6.311   1.00 31.17  ? 169 ALA A CB  1 
ATOM   3424 N N   . ILE B 1 171 ? 15.172  10.528  6.285   1.00 25.00  ? 170 ILE A N   1 
ATOM   3425 C CA  . ILE B 1 171 ? 13.922  9.966   6.787   1.00 26.60  ? 170 ILE A CA  1 
ATOM   3426 C C   . ILE B 1 171 ? 12.854  9.872   5.701   1.00 30.05  ? 170 ILE A C   1 
ATOM   3427 O O   . ILE B 1 171 ? 11.676  9.668   6.007   1.00 27.74  ? 170 ILE A O   1 
ATOM   3428 C CB  . ILE B 1 171 ? 13.392  10.750  8.001   1.00 24.52  ? 170 ILE A CB  1 
ATOM   3429 C CG1 . ILE B 1 171 ? 12.971  12.167  7.632   1.00 26.01  ? 170 ILE A CG1 1 
ATOM   3430 C CG2 . ILE B 1 171 ? 14.431  10.829  9.122   1.00 22.83  ? 170 ILE A CG2 1 
ATOM   3431 C CD1 . ILE B 1 171 ? 12.271  12.890  8.776   1.00 22.37  ? 170 ILE A CD1 1 
ATOM   3432 N N   . GLY B 1 172 ? 13.231  10.043  4.438   1.00 27.79  ? 171 GLY A N   1 
ATOM   3433 C CA  . GLY B 1 172 ? 12.316  9.795   3.341   1.00 29.13  ? 171 GLY A CA  1 
ATOM   3434 C C   . GLY B 1 172 ? 11.398  10.937  2.971   1.00 33.61  ? 171 GLY A C   1 
ATOM   3435 O O   . GLY B 1 172 ? 10.356  10.690  2.366   1.00 32.53  ? 171 GLY A O   1 
ATOM   3436 N N   . LYS B 1 173 ? 11.766  12.180  3.282   1.00 33.07  ? 172 LYS A N   1 
ATOM   3437 C CA  . LYS B 1 173 ? 10.952  13.353  2.980   1.00 32.53  ? 172 LYS A CA  1 
ATOM   3438 C C   . LYS B 1 173 ? 11.595  14.187  1.875   1.00 30.20  ? 172 LYS A C   1 
ATOM   3439 O O   . LYS B 1 173 ? 12.761  14.001  1.515   1.00 24.77  ? 172 LYS A O   1 
ATOM   3440 C CB  . LYS B 1 173 ? 10.754  14.215  4.232   1.00 28.05  ? 172 LYS A CB  1 
ATOM   3441 C CG  . LYS B 1 173 ? 10.324  13.433  5.456   1.00 35.89  ? 172 LYS A CG  1 
ATOM   3442 C CD  . LYS B 1 173 ? 8.850   13.076  5.399   1.00 34.45  ? 172 LYS A CD  1 
ATOM   3443 C CE  . LYS B 1 173 ? 8.273   12.958  6.800   1.00 39.07  ? 172 LYS A CE  1 
ATOM   3444 N NZ  . LYS B 1 173 ? 7.205   11.924  6.861   1.00 34.11  ? 172 LYS A NZ  1 
ATOM   3445 N N   . ASN B 1 174 ? 10.811  15.130  1.347   1.00 30.11  ? 173 ASN A N   1 
ATOM   3446 C CA  . ASN B 1 174 ? 11.268  16.060  0.318   1.00 34.38  ? 173 ASN A CA  1 
ATOM   3447 C C   . ASN B 1 174 ? 11.408  17.450  0.918   1.00 28.12  ? 173 ASN A C   1 
ATOM   3448 O O   . ASN B 1 174 ? 10.399  18.150  1.100   1.00 27.05  ? 173 ASN A O   1 
ATOM   3449 C CB  . ASN B 1 174 ? 10.293  16.085  -0.861  1.00 34.66  ? 173 ASN A CB  1 
ATOM   3450 C CG  . ASN B 1 174 ? 10.136  14.731  -1.505  1.00 48.53  ? 173 ASN A CG  1 
ATOM   3451 O OD1 . ASN B 1 174 ? 9.479   13.845  -0.962  1.00 53.19  ? 173 ASN A OD1 1 
ATOM   3452 N ND2 . ASN B 1 174 ? 10.754  14.555  -2.666  1.00 55.57  ? 173 ASN A ND2 1 
ATOM   3453 N N   . PRO B 1 175 ? 12.619  17.898  1.236   1.00 25.10  ? 174 PRO A N   1 
ATOM   3454 C CA  . PRO B 1 175 ? 12.781  19.234  1.816   1.00 24.43  ? 174 PRO A CA  1 
ATOM   3455 C C   . PRO B 1 175 ? 12.687  20.318  0.755   1.00 30.57  ? 174 PRO A C   1 
ATOM   3456 O O   . PRO B 1 175 ? 13.189  20.173  -0.363  1.00 34.67  ? 174 PRO A O   1 
ATOM   3457 C CB  . PRO B 1 175 ? 14.182  19.179  2.434   1.00 29.33  ? 174 PRO A CB  1 
ATOM   3458 C CG  . PRO B 1 175 ? 14.920  18.203  1.576   1.00 25.85  ? 174 PRO A CG  1 
ATOM   3459 C CD  . PRO B 1 175 ? 13.903  17.189  1.096   1.00 28.45  ? 174 PRO A CD  1 
ATOM   3460 N N   . VAL B 1 176 ? 12.018  21.410  1.118   1.00 25.43  ? 175 VAL A N   1 
ATOM   3461 C CA  . VAL B 1 176 ? 11.902  22.596  0.277   1.00 26.84  ? 175 VAL A CA  1 
ATOM   3462 C C   . VAL B 1 176 ? 12.377  23.783  1.101   1.00 34.16  ? 175 VAL A C   1 
ATOM   3463 O O   . VAL B 1 176 ? 11.782  24.095  2.140   1.00 32.57  ? 175 VAL A O   1 
ATOM   3464 C CB  . VAL B 1 176 ? 10.463  22.820  -0.219  1.00 33.75  ? 175 VAL A CB  1 
ATOM   3465 C CG1 . VAL B 1 176 ? 10.313  24.216  -0.803  1.00 29.00  ? 175 VAL A CG1 1 
ATOM   3466 C CG2 . VAL B 1 176 ? 10.079  21.766  -1.250  1.00 19.74  ? 175 VAL A CG2 1 
ATOM   3467 N N   . GLN B 1 177 ? 13.450  24.433  0.651   1.00 32.39  ? 176 GLN A N   1 
ATOM   3468 C CA  . GLN B 1 177 ? 13.996  25.556  1.399   1.00 32.82  ? 176 GLN A CA  1 
ATOM   3469 C C   . GLN B 1 177 ? 13.089  26.774  1.287   1.00 34.06  ? 176 GLN A C   1 
ATOM   3470 O O   . GLN B 1 177 ? 12.614  27.123  0.203   1.00 40.92  ? 176 GLN A O   1 
ATOM   3471 C CB  . GLN B 1 177 ? 15.397  25.913  0.909   1.00 33.14  ? 176 GLN A CB  1 
ATOM   3472 C CG  . GLN B 1 177 ? 16.002  27.086  1.667   1.00 39.56  ? 176 GLN A CG  1 
ATOM   3473 C CD  . GLN B 1 177 ? 17.443  27.358  1.291   1.00 52.62  ? 176 GLN A CD  1 
ATOM   3474 O OE1 . GLN B 1 177 ? 18.130  26.496  0.737   1.00 46.23  ? 176 GLN A OE1 1 
ATOM   3475 N NE2 . GLN B 1 177 ? 17.911  28.566  1.590   1.00 48.84  ? 176 GLN A NE2 1 
ATOM   3476 N N   . VAL B 1 178 ? 12.856  27.425  2.421   1.00 31.51  ? 177 VAL A N   1 
ATOM   3477 C CA  . VAL B 1 178 ? 12.010  28.607  2.504   1.00 25.44  ? 177 VAL A CA  1 
ATOM   3478 C C   . VAL B 1 178 ? 12.747  29.653  3.327   1.00 34.77  ? 177 VAL A C   1 
ATOM   3479 O O   . VAL B 1 178 ? 13.167  29.375  4.457   1.00 28.48  ? 177 VAL A O   1 
ATOM   3480 C CB  . VAL B 1 178 ? 10.643  28.293  3.133   1.00 26.45  ? 177 VAL A CB  1 
ATOM   3481 C CG1 . VAL B 1 178 ? 9.868   29.579  3.402   1.00 22.96  ? 177 VAL A CG1 1 
ATOM   3482 C CG2 . VAL B 1 178 ? 9.849   27.347  2.243   1.00 27.22  ? 177 VAL A CG2 1 
ATOM   3483 N N   . ASN B 1 179 ? 12.921  30.844  2.762   1.00 30.89  ? 178 ASN A N   1 
ATOM   3484 C CA  . ASN B 1 179 ? 13.393  31.978  3.542   1.00 26.05  ? 178 ASN A CA  1 
ATOM   3485 C C   . ASN B 1 179 ? 12.214  32.567  4.298   1.00 24.22  ? 178 ASN A C   1 
ATOM   3486 O O   . ASN B 1 179 ? 11.175  32.862  3.700   1.00 24.70  ? 178 ASN A O   1 
ATOM   3487 C CB  . ASN B 1 179 ? 14.036  33.024  2.639   1.00 25.20  ? 178 ASN A CB  1 
ATOM   3488 C CG  . ASN B 1 179 ? 15.231  32.480  1.892   1.00 31.59  ? 178 ASN A CG  1 
ATOM   3489 O OD1 . ASN B 1 179 ? 16.121  31.872  2.485   1.00 35.48  ? 178 ASN A OD1 1 
ATOM   3490 N ND2 . ASN B 1 179 ? 15.252  32.681  0.581   1.00 28.57  ? 178 ASN A ND2 1 
ATOM   3491 N N   . GLU B 1 180 ? 12.380  32.736  5.607   1.00 29.03  ? 179 GLU A N   1 
ATOM   3492 C CA  . GLU B 1 180 ? 11.260  33.004  6.501   1.00 23.82  ? 179 GLU A CA  1 
ATOM   3493 C C   . GLU B 1 180 ? 10.395  34.153  6.005   1.00 31.42  ? 179 GLU A C   1 
ATOM   3494 O O   . GLU B 1 180 ? 10.884  35.262  5.768   1.00 24.87  ? 179 GLU A O   1 
ATOM   3495 C CB  . GLU B 1 180 ? 11.775  33.308  7.906   1.00 32.91  ? 179 GLU A CB  1 
ATOM   3496 C CG  . GLU B 1 180 ? 10.678  33.747  8.860   1.00 28.51  ? 179 GLU A CG  1 
ATOM   3497 C CD  . GLU B 1 180 ? 11.224  34.399  10.109  1.00 36.65  ? 179 GLU A CD  1 
ATOM   3498 O OE1 . GLU B 1 180 ? 12.401  34.144  10.446  1.00 32.14  ? 179 GLU A OE1 1 
ATOM   3499 O OE2 . GLU B 1 180 ? 10.477  35.163  10.756  1.00 38.88  ? 179 GLU A OE2 1 
ATOM   3500 N N   . ALA B 1 181 ? 9.110   33.860  5.828   1.00 23.42  ? 180 ALA A N   1 
ATOM   3501 C CA  . ALA B 1 181 ? 8.092   34.855  5.541   1.00 28.18  ? 180 ALA A CA  1 
ATOM   3502 C C   . ALA B 1 181 ? 6.770   34.315  6.064   1.00 23.12  ? 180 ALA A C   1 
ATOM   3503 O O   . ALA B 1 181 ? 6.611   33.108  6.269   1.00 24.48  ? 180 ALA A O   1 
ATOM   3504 C CB  . ALA B 1 181 ? 8.006   35.182  4.042   1.00 15.20  ? 180 ALA A CB  1 
ATOM   3505 N N   . ALA B 1 182 ? 5.825   35.224  6.289   1.00 23.14  ? 181 ALA A N   1 
ATOM   3506 C CA  . ALA B 1 182 ? 4.535   34.835  6.842   1.00 21.19  ? 181 ALA A CA  1 
ATOM   3507 C C   . ALA B 1 182 ? 3.863   33.792  5.958   1.00 25.39  ? 181 ALA A C   1 
ATOM   3508 O O   . ALA B 1 182 ? 3.759   33.963  4.739   1.00 23.99  ? 181 ALA A O   1 
ATOM   3509 C CB  . ALA B 1 182 ? 3.635   36.060  6.994   1.00 20.99  ? 181 ALA A CB  1 
ATOM   3510 N N   . GLY B 1 183 ? 3.418   32.699  6.578   1.00 20.57  ? 182 GLY A N   1 
ATOM   3511 C CA  . GLY B 1 183 ? 2.720   31.649  5.869   1.00 22.92  ? 182 GLY A CA  1 
ATOM   3512 C C   . GLY B 1 183 ? 3.595   30.724  5.053   1.00 27.92  ? 182 GLY A C   1 
ATOM   3513 O O   . GLY B 1 183 ? 3.066   29.783  4.445   1.00 24.21  ? 182 GLY A O   1 
ATOM   3514 N N   . PHE B 1 184 ? 4.910   30.955  5.029   1.00 21.69  ? 183 PHE A N   1 
ATOM   3515 C CA  . PHE B 1 184 ? 5.857   30.144  4.269   1.00 21.55  ? 183 PHE A CA  1 
ATOM   3516 C C   . PHE B 1 184 ? 5.413   30.030  2.817   1.00 25.28  ? 183 PHE A C   1 
ATOM   3517 O O   . PHE B 1 184 ? 5.268   31.046  2.132   1.00 19.89  ? 183 PHE A O   1 
ATOM   3518 C CB  . PHE B 1 184 ? 6.021   28.760  4.906   1.00 22.62  ? 183 PHE A CB  1 
ATOM   3519 C CG  . PHE B 1 184 ? 6.531   28.802  6.320   1.00 21.26  ? 183 PHE A CG  1 
ATOM   3520 C CD1 . PHE B 1 184 ? 7.233   29.906  6.787   1.00 23.45  ? 183 PHE A CD1 1 
ATOM   3521 C CD2 . PHE B 1 184 ? 6.311   27.741  7.182   1.00 25.51  ? 183 PHE A CD2 1 
ATOM   3522 C CE1 . PHE B 1 184 ? 7.696   29.955  8.090   1.00 24.73  ? 183 PHE A CE1 1 
ATOM   3523 C CE2 . PHE B 1 184 ? 6.776   27.781  8.486   1.00 24.13  ? 183 PHE A CE2 1 
ATOM   3524 C CZ  . PHE B 1 184 ? 7.469   28.892  8.939   1.00 24.34  ? 183 PHE A CZ  1 
ATOM   3525 N N   . VAL B 1 185 ? 5.194   28.809  2.334   1.00 22.34  ? 184 VAL A N   1 
ATOM   3526 C CA  . VAL B 1 185 ? 4.675   28.580  0.989   1.00 28.04  ? 184 VAL A CA  1 
ATOM   3527 C C   . VAL B 1 185 ? 3.248   28.035  1.029   1.00 30.42  ? 184 VAL A C   1 
ATOM   3528 O O   . VAL B 1 185 ? 2.324   28.656  0.500   1.00 31.28  ? 184 VAL A O   1 
ATOM   3529 C CB  . VAL B 1 185 ? 5.606   27.654  0.176   1.00 25.47  ? 184 VAL A CB  1 
ATOM   3530 C CG1 . VAL B 1 185 ? 4.924   27.242  -1.122  1.00 20.89  ? 184 VAL A CG1 1 
ATOM   3531 C CG2 . VAL B 1 185 ? 6.923   28.354  -0.116  1.00 18.91  ? 184 VAL A CG2 1 
ATOM   3532 N N   . VAL B 1 186 ? 3.048   26.875  1.660   1.00 27.57  ? 185 VAL A N   1 
ATOM   3533 C CA  . VAL B 1 186 ? 1.757   26.194  1.574   1.00 25.72  ? 185 VAL A CA  1 
ATOM   3534 C C   . VAL B 1 186 ? 0.662   27.042  2.209   1.00 26.45  ? 185 VAL A C   1 
ATOM   3535 O O   . VAL B 1 186 ? -0.359  27.341  1.580   1.00 23.76  ? 185 VAL A O   1 
ATOM   3536 C CB  . VAL B 1 186 ? 1.831   24.802  2.222   1.00 28.43  ? 185 VAL A CB  1 
ATOM   3537 C CG1 . VAL B 1 186 ? 0.512   24.068  2.032   1.00 25.17  ? 185 VAL A CG1 1 
ATOM   3538 C CG2 . VAL B 1 186 ? 2.978   24.006  1.631   1.00 22.89  ? 185 VAL A CG2 1 
ATOM   3539 N N   . ASN B 1 187 ? 0.861   27.440  3.468   1.00 23.22  ? 186 ASN A N   1 
ATOM   3540 C CA  . ASN B 1 187 ? -0.169  28.199  4.170   1.00 23.30  ? 186 ASN A CA  1 
ATOM   3541 C C   . ASN B 1 187 ? -0.420  29.548  3.508   1.00 26.75  ? 186 ASN A C   1 
ATOM   3542 O O   . ASN B 1 187 ? -1.561  30.025  3.484   1.00 20.10  ? 186 ASN A O   1 
ATOM   3543 C CB  . ASN B 1 187 ? 0.222   28.393  5.638   1.00 27.40  ? 186 ASN A CB  1 
ATOM   3544 C CG  . ASN B 1 187 ? -0.221  27.235  6.522   1.00 30.74  ? 186 ASN A CG  1 
ATOM   3545 O OD1 . ASN B 1 187 ? -1.006  26.379  6.106   1.00 33.48  ? 186 ASN A OD1 1 
ATOM   3546 N ND2 . ASN B 1 187 ? 0.282   27.207  7.750   1.00 33.44  ? 186 ASN A ND2 1 
ATOM   3547 N N   . ARG B 1 188 ? 0.623   30.174  2.961   1.00 21.25  ? 187 ARG A N   1 
ATOM   3548 C CA  . ARG B 1 188 ? 0.436   31.456  2.294   1.00 25.27  ? 187 ARG A CA  1 
ATOM   3549 C C   . ARG B 1 188 ? -0.458  31.326  1.067   1.00 27.15  ? 187 ARG A C   1 
ATOM   3550 O O   . ARG B 1 188 ? -1.201  32.259  0.746   1.00 27.68  ? 187 ARG A O   1 
ATOM   3551 C CB  . ARG B 1 188 ? 1.788   32.052  1.908   1.00 21.31  ? 187 ARG A CB  1 
ATOM   3552 C CG  . ARG B 1 188 ? 1.685   33.379  1.179   1.00 25.04  ? 187 ARG A CG  1 
ATOM   3553 C CD  . ARG B 1 188 ? 3.002   34.120  1.242   1.00 25.50  ? 187 ARG A CD  1 
ATOM   3554 N NE  . ARG B 1 188 ? 3.099   35.177  0.244   1.00 33.37  ? 187 ARG A NE  1 
ATOM   3555 C CZ  . ARG B 1 188 ? 4.190   35.899  0.028   1.00 35.02  ? 187 ARG A CZ  1 
ATOM   3556 N NH1 . ARG B 1 188 ? 5.296   35.708  0.732   1.00 23.92  ? 187 ARG A NH1 1 
ATOM   3557 N NH2 . ARG B 1 188 ? 4.171   36.839  -0.914  1.00 37.16  ? 187 ARG A NH2 1 
ATOM   3558 N N   . ILE B 1 189 ? -0.411  30.188  0.380   1.00 20.49  ? 188 ILE A N   1 
ATOM   3559 C CA  . ILE B 1 189 ? -1.228  29.999  -0.817  1.00 28.77  ? 188 ILE A CA  1 
ATOM   3560 C C   . ILE B 1 189 ? -2.555  29.329  -0.485  1.00 32.68  ? 188 ILE A C   1 
ATOM   3561 O O   . ILE B 1 189 ? -3.597  29.688  -1.040  1.00 31.43  ? 188 ILE A O   1 
ATOM   3562 C CB  . ILE B 1 189 ? -0.439  29.192  -1.868  1.00 25.52  ? 188 ILE A CB  1 
ATOM   3563 C CG1 . ILE B 1 189 ? 0.790   29.968  -2.337  1.00 28.89  ? 188 ILE A CG1 1 
ATOM   3564 C CG2 . ILE B 1 189 ? -1.318  28.840  -3.058  1.00 24.28  ? 188 ILE A CG2 1 
ATOM   3565 C CD1 . ILE B 1 189 ? 1.711   29.151  -3.220  1.00 27.75  ? 188 ILE A CD1 1 
ATOM   3566 N N   . LEU B 1 190 ? -2.534  28.369  0.440   1.00 29.71  ? 189 LEU A N   1 
ATOM   3567 C CA  . LEU B 1 190 ? -3.687  27.505  0.664   1.00 26.53  ? 189 LEU A CA  1 
ATOM   3568 C C   . LEU B 1 190 ? -4.796  28.205  1.442   1.00 25.68  ? 189 LEU A C   1 
ATOM   3569 O O   . LEU B 1 190 ? -5.972  28.086  1.085   1.00 27.74  ? 189 LEU A O   1 
ATOM   3570 C CB  . LEU B 1 190 ? -3.243  26.241  1.398   1.00 26.29  ? 189 LEU A CB  1 
ATOM   3571 C CG  . LEU B 1 190 ? -4.239  25.086  1.452   1.00 38.94  ? 189 LEU A CG  1 
ATOM   3572 C CD1 . LEU B 1 190 ? -4.454  24.518  0.055   1.00 35.48  ? 189 LEU A CD1 1 
ATOM   3573 C CD2 . LEU B 1 190 ? -3.752  24.013  2.417   1.00 28.40  ? 189 LEU A CD2 1 
ATOM   3574 N N   . ILE B 1 191 ? -4.454  28.925  2.505   1.00 20.88  ? 190 ILE A N   1 
ATOM   3575 C CA  . ILE B 1 191 ? -5.472  29.489  3.393   1.00 24.66  ? 190 ILE A CA  1 
ATOM   3576 C C   . ILE B 1 191 ? -6.192  30.671  2.743   1.00 26.14  ? 190 ILE A C   1 
ATOM   3577 O O   . ILE B 1 191 ? -7.423  30.761  2.866   1.00 23.51  ? 190 ILE A O   1 
ATOM   3578 C CB  . ILE B 1 191 ? -4.870  29.876  4.754   1.00 27.53  ? 190 ILE A CB  1 
ATOM   3579 C CG1 . ILE B 1 191 ? -4.169  28.672  5.386   1.00 21.61  ? 190 ILE A CG1 1 
ATOM   3580 C CG2 . ILE B 1 191 ? -5.952  30.385  5.687   1.00 20.22  ? 190 ILE A CG2 1 
ATOM   3581 C CD1 . ILE B 1 191 ? -5.030  27.422  5.426   1.00 21.53  ? 190 ILE A CD1 1 
ATOM   3582 N N   . PRO B 1 192 ? -5.509  31.603  2.060   1.00 26.41  ? 191 PRO A N   1 
ATOM   3583 C CA  . PRO B 1 192 ? -6.261  32.645  1.334   1.00 30.83  ? 191 PRO A CA  1 
ATOM   3584 C C   . PRO B 1 192 ? -7.244  32.081  0.321   1.00 28.87  ? 191 PRO A C   1 
ATOM   3585 O O   . PRO B 1 192 ? -8.281  32.705  0.057   1.00 23.92  ? 191 PRO A O   1 
ATOM   3586 C CB  . PRO B 1 192 ? -5.155  33.464  0.657   1.00 22.94  ? 191 PRO A CB  1 
ATOM   3587 C CG  . PRO B 1 192 ? -4.002  33.320  1.572   1.00 23.82  ? 191 PRO A CG  1 
ATOM   3588 C CD  . PRO B 1 192 ? -4.062  31.894  2.057   1.00 17.88  ? 191 PRO A CD  1 
ATOM   3589 N N   . MET B 1 193 ? -6.936  30.915  -0.252  1.00 22.46  ? 192 MET A N   1 
ATOM   3590 C CA  . MET B 1 193 ? -7.888  30.196  -1.094  1.00 26.02  ? 192 MET A CA  1 
ATOM   3591 C C   . MET B 1 193 ? -9.169  29.870  -0.332  1.00 28.85  ? 192 MET A C   1 
ATOM   3592 O O   . MET B 1 193 ? -10.277 30.127  -0.818  1.00 29.23  ? 192 MET A O   1 
ATOM   3593 C CB  . MET B 1 193 ? -7.235  28.915  -1.600  1.00 31.73  ? 192 MET A CB  1 
ATOM   3594 C CG  . MET B 1 193 ? -8.163  27.944  -2.282  1.00 45.11  ? 192 MET A CG  1 
ATOM   3595 S SD  . MET B 1 193 ? -7.239  26.552  -2.953  1.00 45.49  ? 192 MET A SD  1 
ATOM   3596 C CE  . MET B 1 193 ? -5.556  27.060  -2.605  1.00 37.78  ? 192 MET A CE  1 
ATOM   3597 N N   . ILE B 1 194 ? -9.034  29.266  0.854   1.00 27.27  ? 193 ILE A N   1 
ATOM   3598 C CA  . ILE B 1 194 ? -10.201 29.006  1.695   1.00 22.81  ? 193 ILE A CA  1 
ATOM   3599 C C   . ILE B 1 194 ? -10.902 30.312  2.033   1.00 24.26  ? 193 ILE A C   1 
ATOM   3600 O O   . ILE B 1 194 ? -12.138 30.398  2.017   1.00 18.79  ? 193 ILE A O   1 
ATOM   3601 C CB  . ILE B 1 194 ? -9.785  28.240  2.966   1.00 27.54  ? 193 ILE A CB  1 
ATOM   3602 C CG1 . ILE B 1 194 ? -9.372  26.811  2.616   1.00 25.40  ? 193 ILE A CG1 1 
ATOM   3603 C CG2 . ILE B 1 194 ? -10.909 28.232  3.995   1.00 22.11  ? 193 ILE A CG2 1 
ATOM   3604 C CD1 . ILE B 1 194 ? -8.301  26.249  3.522   1.00 24.24  ? 193 ILE A CD1 1 
ATOM   3605 N N   . ASN B 1 195 ? -10.119 31.353  2.324   1.00 23.68  ? 194 ASN A N   1 
ATOM   3606 C CA  . ASN B 1 195 ? -10.677 32.668  2.618   1.00 21.78  ? 194 ASN A CA  1 
ATOM   3607 C C   . ASN B 1 195 ? -11.469 33.216  1.434   1.00 18.92  ? 194 ASN A C   1 
ATOM   3608 O O   . ASN B 1 195 ? -12.553 33.785  1.614   1.00 22.26  ? 194 ASN A O   1 
ATOM   3609 C CB  . ASN B 1 195 ? -9.543  33.620  3.003   1.00 18.02  ? 194 ASN A CB  1 
ATOM   3610 C CG  . ASN B 1 195 ? -10.036 34.870  3.681   1.00 18.98  ? 194 ASN A CG  1 
ATOM   3611 O OD1 . ASN B 1 195 ? -10.764 34.806  4.670   1.00 21.73  ? 194 ASN A OD1 1 
ATOM   3612 N ND2 . ASN B 1 195 ? -9.630  36.025  3.161   1.00 23.02  ? 194 ASN A ND2 1 
ATOM   3613 N N   . GLU B 1 196 ? -10.947 33.048  0.214   1.00 20.56  ? 195 GLU A N   1 
ATOM   3614 C CA  . GLU B 1 196 ? -11.648 33.541  -0.970  1.00 20.90  ? 195 GLU A CA  1 
ATOM   3615 C C   . GLU B 1 196 ? -12.990 32.845  -1.151  1.00 19.01  ? 195 GLU A C   1 
ATOM   3616 O O   . GLU B 1 196 ? -14.005 33.499  -1.423  1.00 22.83  ? 195 GLU A O   1 
ATOM   3617 C CB  . GLU B 1 196 ? -10.782 33.350  -2.213  1.00 21.31  ? 195 GLU A CB  1 
ATOM   3618 C CG  . GLU B 1 196 ? -11.295 34.085  -3.453  1.00 25.91  ? 195 GLU A CG  1 
ATOM   3619 C CD  . GLU B 1 196 ? -11.250 35.597  -3.289  1.00 37.79  ? 195 GLU A CD  1 
ATOM   3620 O OE1 . GLU B 1 196 ? -10.150 36.130  -3.038  1.00 42.26  ? 195 GLU A OE1 1 
ATOM   3621 O OE2 . GLU B 1 196 ? -12.306 36.255  -3.422  1.00 36.45  ? 195 GLU A OE2 1 
ATOM   3622 N N   . ALA B 1 197 ? -13.015 31.516  -1.007  1.00 18.60  ? 196 ALA A N   1 
ATOM   3623 C CA  . ALA B 1 197 ? -14.264 30.772  -1.148  1.00 18.17  ? 196 ALA A CA  1 
ATOM   3624 C C   . ALA B 1 197 ? -15.320 31.259  -0.162  1.00 23.79  ? 196 ALA A C   1 
ATOM   3625 O O   . ALA B 1 197 ? -16.502 31.358  -0.508  1.00 26.32  ? 196 ALA A O   1 
ATOM   3626 C CB  . ALA B 1 197 ? -14.008 29.279  -0.959  1.00 12.92  ? 196 ALA A CB  1 
ATOM   3627 N N   . ALA B 1 198 ? -14.914 31.565  1.075   1.00 24.20  ? 197 ALA A N   1 
ATOM   3628 C CA  . ALA B 1 198 ? -15.859 32.113  2.042   1.00 23.40  ? 197 ALA A CA  1 
ATOM   3629 C C   . ALA B 1 198 ? -16.397 33.461  1.579   1.00 22.99  ? 197 ALA A C   1 
ATOM   3630 O O   . ALA B 1 198 ? -17.597 33.737  1.706   1.00 22.10  ? 197 ALA A O   1 
ATOM   3631 C CB  . ALA B 1 198 ? -15.195 32.243  3.413   1.00 19.78  ? 197 ALA A CB  1 
ATOM   3632 N N   . PHE B 1 199 ? -15.519 34.318  1.048   1.00 21.04  ? 198 PHE A N   1 
ATOM   3633 C CA  . PHE B 1 199 ? -15.960 35.587  0.475   1.00 20.86  ? 198 PHE A CA  1 
ATOM   3634 C C   . PHE B 1 199 ? -16.982 35.364  -0.637  1.00 24.14  ? 198 PHE A C   1 
ATOM   3635 O O   . PHE B 1 199 ? -17.985 36.084  -0.724  1.00 25.21  ? 198 PHE A O   1 
ATOM   3636 C CB  . PHE B 1 199 ? -14.754 36.363  -0.059  1.00 22.13  ? 198 PHE A CB  1 
ATOM   3637 C CG  . PHE B 1 199 ? -14.202 37.391  0.898   1.00 21.88  ? 198 PHE A CG  1 
ATOM   3638 C CD1 . PHE B 1 199 ? -14.970 38.471  1.304   1.00 17.16  ? 198 PHE A CD1 1 
ATOM   3639 C CD2 . PHE B 1 199 ? -12.899 37.290  1.365   1.00 26.01  ? 198 PHE A CD2 1 
ATOM   3640 C CE1 . PHE B 1 199 ? -14.455 39.426  2.169   1.00 27.24  ? 198 PHE A CE1 1 
ATOM   3641 C CE2 . PHE B 1 199 ? -12.375 38.242  2.232   1.00 23.36  ? 198 PHE A CE2 1 
ATOM   3642 C CZ  . PHE B 1 199 ? -13.155 39.310  2.634   1.00 21.20  ? 198 PHE A CZ  1 
ATOM   3643 N N   . ILE B 1 200 ? -16.744 34.367  -1.494  1.00 18.86  ? 199 ILE A N   1 
ATOM   3644 C CA  . ILE B 1 200 ? -17.684 34.056  -2.568  1.00 26.76  ? 199 ILE A CA  1 
ATOM   3645 C C   . ILE B 1 200 ? -19.035 33.657  -1.993  1.00 27.34  ? 199 ILE A C   1 
ATOM   3646 O O   . ILE B 1 200 ? -20.088 34.109  -2.463  1.00 21.73  ? 199 ILE A O   1 
ATOM   3647 C CB  . ILE B 1 200 ? -17.107 32.955  -3.476  1.00 29.89  ? 199 ILE A CB  1 
ATOM   3648 C CG1 . ILE B 1 200 ? -16.068 33.550  -4.424  1.00 21.53  ? 199 ILE A CG1 1 
ATOM   3649 C CG2 . ILE B 1 200 ? -18.213 32.253  -4.246  1.00 25.02  ? 199 ILE A CG2 1 
ATOM   3650 C CD1 . ILE B 1 200 ? -15.115 32.533  -4.996  1.00 22.91  ? 199 ILE A CD1 1 
ATOM   3651 N N   . LYS B 1 201 ? -19.025 32.808  -0.966  1.00 25.38  ? 200 LYS A N   1 
ATOM   3652 C CA  . LYS B 1 201 ? -20.262 32.456  -0.279  1.00 27.19  ? 200 LYS A CA  1 
ATOM   3653 C C   . LYS B 1 201 ? -20.906 33.685  0.356   1.00 24.27  ? 200 LYS A C   1 
ATOM   3654 O O   . LYS B 1 201 ? -22.106 33.930  0.183   1.00 22.41  ? 200 LYS A O   1 
ATOM   3655 C CB  . LYS B 1 201 ? -19.977 31.392  0.779   1.00 30.95  ? 200 LYS A CB  1 
ATOM   3656 C CG  . LYS B 1 201 ? -21.144 31.130  1.713   1.00 24.95  ? 200 LYS A CG  1 
ATOM   3657 C CD  . LYS B 1 201 ? -22.386 30.739  0.943   1.00 28.12  ? 200 LYS A CD  1 
ATOM   3658 C CE  . LYS B 1 201 ? -23.499 30.348  1.888   1.00 36.07  ? 200 LYS A CE  1 
ATOM   3659 N NZ  . LYS B 1 201 ? -24.810 30.783  1.350   1.00 29.34  ? 200 LYS A NZ  1 
ATOM   3660 N N   . MET B 1 202 ? -20.114 34.471  1.094   1.00 26.00  ? 201 MET A N   1 
ATOM   3661 C CA  . MET B 1 202 ? -20.649 35.637  1.794   1.00 28.04  ? 201 MET A CA  1 
ATOM   3662 C C   . MET B 1 202 ? -21.342 36.603  0.841   1.00 32.89  ? 201 MET A C   1 
ATOM   3663 O O   . MET B 1 202 ? -22.408 37.144  1.159   1.00 31.88  ? 201 MET A O   1 
ATOM   3664 C CB  . MET B 1 202 ? -19.529 36.358  2.543   1.00 26.05  ? 201 MET A CB  1 
ATOM   3665 C CG  . MET B 1 202 ? -20.004 37.575  3.328   1.00 26.21  ? 201 MET A CG  1 
ATOM   3666 S SD  . MET B 1 202 ? -18.676 38.436  4.195   1.00 41.67  ? 201 MET A SD  1 
ATOM   3667 C CE  . MET B 1 202 ? -18.214 39.671  2.983   1.00 39.89  ? 201 MET A CE  1 
ATOM   3668 N N   . GLU B 1 203 ? -20.751 36.840  -0.327  1.00 28.14  ? 202 GLU A N   1 
ATOM   3669 C CA  . GLU B 1 203 ? -21.280 37.823  -1.263  1.00 34.68  ? 202 GLU A CA  1 
ATOM   3670 C C   . GLU B 1 203 ? -22.393 37.269  -2.148  1.00 31.13  ? 202 GLU A C   1 
ATOM   3671 O O   . GLU B 1 203 ? -22.846 37.972  -3.058  1.00 29.24  ? 202 GLU A O   1 
ATOM   3672 C CB  . GLU B 1 203 ? -20.143 38.391  -2.117  1.00 28.29  ? 202 GLU A CB  1 
ATOM   3673 C CG  . GLU B 1 203 ? -19.207 39.293  -1.320  1.00 35.74  ? 202 GLU A CG  1 
ATOM   3674 C CD  . GLU B 1 203 ? -17.851 39.473  -1.970  1.00 42.03  ? 202 GLU A CD  1 
ATOM   3675 O OE1 . GLU B 1 203 ? -17.679 39.038  -3.129  1.00 34.81  ? 202 GLU A OE1 1 
ATOM   3676 O OE2 . GLU B 1 203 ? -16.954 40.048  -1.314  1.00 43.29  ? 202 GLU A OE2 1 
ATOM   3677 N N   . GLY B 1 204 ? -22.850 36.045  -1.891  1.00 24.93  ? 203 GLY A N   1 
ATOM   3678 C CA  . GLY B 1 204 ? -23.981 35.484  -2.599  1.00 32.74  ? 203 GLY A CA  1 
ATOM   3679 C C   . GLY B 1 204 ? -23.685 34.981  -3.990  1.00 35.80  ? 203 GLY A C   1 
ATOM   3680 O O   . GLY B 1 204 ? -24.623 34.733  -4.755  1.00 38.32  ? 203 GLY A O   1 
ATOM   3681 N N   . VAL B 1 205 ? -22.411 34.816  -4.341  1.00 30.97  ? 204 VAL A N   1 
ATOM   3682 C CA  . VAL B 1 205 ? -22.065 34.413  -5.698  1.00 28.62  ? 204 VAL A CA  1 
ATOM   3683 C C   . VAL B 1 205 ? -22.462 32.963  -5.947  1.00 33.12  ? 204 VAL A C   1 
ATOM   3684 O O   . VAL B 1 205 ? -22.941 32.616  -7.033  1.00 26.42  ? 204 VAL A O   1 
ATOM   3685 C CB  . VAL B 1 205 ? -20.567 34.661  -5.943  1.00 23.81  ? 204 VAL A CB  1 
ATOM   3686 C CG1 . VAL B 1 205 ? -20.131 34.065  -7.267  1.00 27.73  ? 204 VAL A CG1 1 
ATOM   3687 C CG2 . VAL B 1 205 ? -20.284 36.164  -5.902  1.00 14.09  ? 204 VAL A CG2 1 
ATOM   3688 N N   . SER B 1 206 ? -22.300 32.099  -4.948  1.00 31.95  ? 205 SER A N   1 
ATOM   3689 C CA  . SER B 1 206 ? -22.655 30.694  -5.096  1.00 27.93  ? 205 SER A CA  1 
ATOM   3690 C C   . SER B 1 206 ? -22.934 30.107  -3.714  1.00 36.49  ? 205 SER A C   1 
ATOM   3691 O O   . SER B 1 206 ? -22.817 30.789  -2.692  1.00 37.41  ? 205 SER A O   1 
ATOM   3692 C CB  . SER B 1 206 ? -21.548 29.930  -5.831  1.00 31.60  ? 205 SER A CB  1 
ATOM   3693 O OG  . SER B 1 206 ? -22.048 28.732  -6.406  1.00 38.90  ? 205 SER A OG  1 
ATOM   3694 N N   . ASP B 1 207 ? -23.314 28.831  -3.697  1.00 33.99  ? 206 ASP A N   1 
ATOM   3695 C CA  . ASP B 1 207 ? -23.619 28.087  -2.483  1.00 36.03  ? 206 ASP A CA  1 
ATOM   3696 C C   . ASP B 1 207 ? -22.428 27.229  -2.070  1.00 29.71  ? 206 ASP A C   1 
ATOM   3697 O O   . ASP B 1 207 ? -21.528 26.952  -2.867  1.00 32.70  ? 206 ASP A O   1 
ATOM   3698 C CB  . ASP B 1 207 ? -24.844 27.198  -2.693  1.00 37.52  ? 206 ASP A CB  1 
ATOM   3699 C CG  . ASP B 1 207 ? -24.649 26.209  -3.826  1.00 39.78  ? 206 ASP A CG  1 
ATOM   3700 O OD1 . ASP B 1 207 ? -24.702 26.632  -5.003  1.00 40.10  ? 206 ASP A OD1 1 
ATOM   3701 O OD2 . ASP B 1 207 ? -24.425 25.012  -3.538  1.00 37.81  ? 206 ASP A OD2 1 
ATOM   3702 N N   . ILE B 1 208 ? -22.450 26.786  -0.809  1.00 34.52  ? 207 ILE A N   1 
ATOM   3703 C CA  . ILE B 1 208 ? -21.304 26.073  -0.237  1.00 34.51  ? 207 ILE A CA  1 
ATOM   3704 C C   . ILE B 1 208 ? -20.990 24.821  -1.046  1.00 31.68  ? 207 ILE A C   1 
ATOM   3705 O O   . ILE B 1 208 ? -19.866 24.636  -1.526  1.00 32.44  ? 207 ILE A O   1 
ATOM   3706 C CB  . ILE B 1 208 ? -21.554 25.733  1.244   1.00 24.40  ? 207 ILE A CB  1 
ATOM   3707 C CG1 . ILE B 1 208 ? -21.450 26.999  2.097   1.00 32.27  ? 207 ILE A CG1 1 
ATOM   3708 C CG2 . ILE B 1 208 ? -20.573 24.678  1.729   1.00 24.82  ? 207 ILE A CG2 1 
ATOM   3709 C CD1 . ILE B 1 208 ? -22.155 26.908  3.431   1.00 29.11  ? 207 ILE A CD1 1 
ATOM   3710 N N   . ALA B 1 209 ? -21.981 23.941  -1.206  1.00 28.49  ? 208 ALA A N   1 
ATOM   3711 C CA  . ALA B 1 209 ? -21.762 22.722  -1.981  1.00 34.62  ? 208 ALA A CA  1 
ATOM   3712 C C   . ALA B 1 209 ? -21.338 23.044  -3.410  1.00 35.45  ? 208 ALA A C   1 
ATOM   3713 O O   . ALA B 1 209 ? -20.450 22.383  -3.967  1.00 31.84  ? 208 ALA A O   1 
ATOM   3714 C CB  . ALA B 1 209 ? -23.024 21.855  -1.977  1.00 30.42  ? 208 ALA A CB  1 
ATOM   3715 N N   . GLY B 1 210 ? -21.959 24.059  -4.019  1.00 29.30  ? 209 GLY A N   1 
ATOM   3716 C CA  . GLY B 1 210 ? -21.571 24.451  -5.365  1.00 26.27  ? 209 GLY A CA  1 
ATOM   3717 C C   . GLY B 1 210 ? -20.132 24.923  -5.442  1.00 30.92  ? 209 GLY A C   1 
ATOM   3718 O O   . GLY B 1 210 ? -19.386 24.524  -6.340  1.00 28.04  ? 209 GLY A O   1 
ATOM   3719 N N   . ILE B 1 211 ? -19.722 25.773  -4.496  1.00 29.48  ? 210 ILE A N   1 
ATOM   3720 C CA  . ILE B 1 211 ? -18.340 26.247  -4.456  1.00 25.17  ? 210 ILE A CA  1 
ATOM   3721 C C   . ILE B 1 211 ? -17.376 25.069  -4.386  1.00 30.09  ? 210 ILE A C   1 
ATOM   3722 O O   . ILE B 1 211 ? -16.413 24.983  -5.157  1.00 27.56  ? 210 ILE A O   1 
ATOM   3723 C CB  . ILE B 1 211 ? -18.138 27.208  -3.269  1.00 28.94  ? 210 ILE A CB  1 
ATOM   3724 C CG1 . ILE B 1 211 ? -18.849 28.538  -3.525  1.00 28.68  ? 210 ILE A CG1 1 
ATOM   3725 C CG2 . ILE B 1 211 ? -16.655 27.443  -3.019  1.00 19.79  ? 210 ILE A CG2 1 
ATOM   3726 C CD1 . ILE B 1 211 ? -19.164 29.308  -2.265  1.00 25.51  ? 210 ILE A CD1 1 
ATOM   3727 N N   . ASP B 1 212 ? -17.626 24.139  -3.465  1.00 31.10  ? 211 ASP A N   1 
ATOM   3728 C CA  . ASP B 1 212 ? -16.710 23.017  -3.284  1.00 29.93  ? 211 ASP A CA  1 
ATOM   3729 C C   . ASP B 1 212 ? -16.723 22.087  -4.489  1.00 31.56  ? 211 ASP A C   1 
ATOM   3730 O O   . ASP B 1 212 ? -15.671 21.589  -4.907  1.00 27.49  ? 211 ASP A O   1 
ATOM   3731 C CB  . ASP B 1 212 ? -17.066 22.259  -2.009  1.00 30.71  ? 211 ASP A CB  1 
ATOM   3732 C CG  . ASP B 1 212 ? -16.586 22.973  -0.766  1.00 36.76  ? 211 ASP A CG  1 
ATOM   3733 O OD1 . ASP B 1 212 ? -15.635 23.773  -0.877  1.00 36.19  ? 211 ASP A OD1 1 
ATOM   3734 O OD2 . ASP B 1 212 ? -17.167 22.751  0.314   1.00 38.73  ? 211 ASP A OD2 1 
ATOM   3735 N N   . THR B 1 213 ? -17.903 21.844  -5.064  1.00 28.89  ? 212 THR A N   1 
ATOM   3736 C CA  . THR B 1 213 ? -17.983 21.026  -6.270  1.00 29.21  ? 212 THR A CA  1 
ATOM   3737 C C   . THR B 1 213 ? -17.164 21.636  -7.403  1.00 30.01  ? 212 THR A C   1 
ATOM   3738 O O   . THR B 1 213 ? -16.427 20.928  -8.101  1.00 26.78  ? 212 THR A O   1 
ATOM   3739 C CB  . THR B 1 213 ? -19.442 20.865  -6.696  1.00 34.36  ? 212 THR A CB  1 
ATOM   3740 O OG1 . THR B 1 213 ? -20.154 20.120  -5.701  1.00 35.65  ? 212 THR A OG1 1 
ATOM   3741 C CG2 . THR B 1 213 ? -19.533 20.137  -8.023  1.00 28.69  ? 212 THR A CG2 1 
ATOM   3742 N N   . ALA B 1 214 ? -17.265 22.954  -7.585  1.00 26.60  ? 213 ALA A N   1 
ATOM   3743 C CA  . ALA B 1 214 ? -16.583 23.599  -8.700  1.00 25.92  ? 213 ALA A CA  1 
ATOM   3744 C C   . ALA B 1 214 ? -15.069 23.495  -8.578  1.00 27.18  ? 213 ALA A C   1 
ATOM   3745 O O   . ALA B 1 214 ? -14.370 23.421  -9.593  1.00 33.75  ? 213 ALA A O   1 
ATOM   3746 C CB  . ALA B 1 214 ? -17.009 25.064  -8.802  1.00 20.60  ? 213 ALA A CB  1 
ATOM   3747 N N   . MET B 1 215 ? -14.540 23.476  -7.355  1.00 30.12  ? 214 MET A N   1 
ATOM   3748 C CA  . MET B 1 215 ? -13.092 23.430  -7.197  1.00 28.75  ? 214 MET A CA  1 
ATOM   3749 C C   . MET B 1 215 ? -12.525 22.038  -7.464  1.00 34.87  ? 214 MET A C   1 
ATOM   3750 O O   . MET B 1 215 ? -11.415 21.921  -7.996  1.00 28.95  ? 214 MET A O   1 
ATOM   3751 C CB  . MET B 1 215 ? -12.701 23.906  -5.798  1.00 29.31  ? 214 MET A CB  1 
ATOM   3752 C CG  . MET B 1 215 ? -12.492 25.420  -5.668  1.00 32.59  ? 214 MET A CG  1 
ATOM   3753 S SD  . MET B 1 215 ? -12.070 26.267  -7.204  1.00 28.62  ? 214 MET A SD  1 
ATOM   3754 C CE  . MET B 1 215 ? -10.283 26.147  -7.170  1.00 27.53  ? 214 MET A CE  1 
ATOM   3755 N N   . LYS B 1 216 ? -13.257 20.975  -7.121  1.00 28.69  ? 215 LYS A N   1 
ATOM   3756 C CA  . LYS B 1 216 ? -12.730 19.638  -7.376  1.00 34.47  ? 215 LYS A CA  1 
ATOM   3757 C C   . LYS B 1 216 ? -12.941 19.218  -8.825  1.00 27.77  ? 215 LYS A C   1 
ATOM   3758 O O   . LYS B 1 216 ? -12.083 18.547  -9.406  1.00 33.74  ? 215 LYS A O   1 
ATOM   3759 C CB  . LYS B 1 216 ? -13.362 18.622  -6.424  1.00 37.52  ? 215 LYS A CB  1 
ATOM   3760 C CG  . LYS B 1 216 ? -14.864 18.731  -6.294  1.00 48.17  ? 215 LYS A CG  1 
ATOM   3761 C CD  . LYS B 1 216 ? -15.299 18.575  -4.845  1.00 43.79  ? 215 LYS A CD  1 
ATOM   3762 C CE  . LYS B 1 216 ? -14.942 17.210  -4.297  1.00 52.57  ? 215 LYS A CE  1 
ATOM   3763 N NZ  . LYS B 1 216 ? -15.965 16.759  -3.311  1.00 66.23  ? 215 LYS A NZ  1 
ATOM   3764 N N   . LEU B 1 217 ? -14.060 19.610  -9.430  1.00 31.39  ? 216 LEU A N   1 
ATOM   3765 C CA  . LEU B 1 217 ? -14.336 19.247  -10.815 1.00 37.31  ? 216 LEU A CA  1 
ATOM   3766 C C   . LEU B 1 217 ? -13.783 20.247  -11.823 1.00 33.36  ? 216 LEU A C   1 
ATOM   3767 O O   . LEU B 1 217 ? -13.596 19.887  -12.991 1.00 45.51  ? 216 LEU A O   1 
ATOM   3768 C CB  . LEU B 1 217 ? -15.844 19.092  -11.029 1.00 30.59  ? 216 LEU A CB  1 
ATOM   3769 C CG  . LEU B 1 217 ? -16.526 18.077  -10.113 1.00 34.18  ? 216 LEU A CG  1 
ATOM   3770 C CD1 . LEU B 1 217 ? -17.992 17.959  -10.451 1.00 23.70  ? 216 LEU A CD1 1 
ATOM   3771 C CD2 . LEU B 1 217 ? -15.844 16.724  -10.204 1.00 28.05  ? 216 LEU A CD2 1 
ATOM   3772 N N   . GLY B 1 218 ? -13.518 21.483  -11.406 1.00 35.40  ? 217 GLY A N   1 
ATOM   3773 C CA  . GLY B 1 218 ? -12.992 22.487  -12.309 1.00 30.20  ? 217 GLY A CA  1 
ATOM   3774 C C   . GLY B 1 218 ? -11.492 22.671  -12.206 1.00 35.90  ? 217 GLY A C   1 
ATOM   3775 O O   . GLY B 1 218 ? -10.831 22.994  -13.198 1.00 44.02  ? 217 GLY A O   1 
ATOM   3776 N N   . ALA B 1 219 ? -10.939 22.473  -11.012 1.00 29.06  ? 218 ALA A N   1 
ATOM   3777 C CA  . ALA B 1 219 ? -9.509  22.631  -10.790 1.00 41.86  ? 218 ALA A CA  1 
ATOM   3778 C C   . ALA B 1 219 ? -8.822  21.325  -10.424 1.00 40.66  ? 218 ALA A C   1 
ATOM   3779 O O   . ALA B 1 219 ? -7.621  21.335  -10.127 1.00 40.74  ? 218 ALA A O   1 
ATOM   3780 C CB  . ALA B 1 219 ? -9.251  23.675  -9.697  1.00 40.73  ? 218 ALA A CB  1 
ATOM   3781 N N   . ASN B 1 220 ? -9.556  20.210  -10.426 1.00 37.59  ? 219 ASN A N   1 
ATOM   3782 C CA  . ASN B 1 220 ? -8.997  18.888  -10.145 1.00 38.02  ? 219 ASN A CA  1 
ATOM   3783 C C   . ASN B 1 220 ? -8.430  18.810  -8.729  1.00 32.12  ? 219 ASN A C   1 
ATOM   3784 O O   . ASN B 1 220 ? -7.420  18.150  -8.480  1.00 36.43  ? 219 ASN A O   1 
ATOM   3785 C CB  . ASN B 1 220 ? -7.938  18.509  -11.183 1.00 40.84  ? 219 ASN A CB  1 
ATOM   3786 C CG  . ASN B 1 220 ? -8.432  17.465  -12.155 1.00 58.13  ? 219 ASN A CG  1 
ATOM   3787 O OD1 . ASN B 1 220 ? -8.550  16.287  -11.812 1.00 65.78  ? 219 ASN A OD1 1 
ATOM   3788 N ND2 . ASN B 1 220 ? -8.737  17.892  -13.376 1.00 52.60  ? 219 ASN A ND2 1 
ATOM   3789 N N   . HIS B 1 221 ? -9.090  19.487  -7.787  1.00 31.79  ? 220 HIS A N   1 
ATOM   3790 C CA  . HIS B 1 221 ? -8.556  19.446  -6.436  1.00 35.52  ? 220 HIS A CA  1 
ATOM   3791 C C   . HIS B 1 221 ? -9.143  18.271  -5.661  1.00 35.00  ? 220 HIS A C   1 
ATOM   3792 O O   . HIS B 1 221 ? -10.273 17.847  -5.924  1.00 32.31  ? 220 HIS A O   1 
ATOM   3793 C CB  . HIS B 1 221 ? -8.860  20.750  -5.705  1.00 37.08  ? 220 HIS A CB  1 
ATOM   3794 C CG  . HIS B 1 221 ? -8.023  21.903  -6.165  1.00 46.67  ? 220 HIS A CG  1 
ATOM   3795 N ND1 . HIS B 1 221 ? -8.334  23.214  -5.875  1.00 43.47  ? 220 HIS A ND1 1 
ATOM   3796 C CD2 . HIS B 1 221 ? -6.884  21.940  -6.898  1.00 34.56  ? 220 HIS A CD2 1 
ATOM   3797 C CE1 . HIS B 1 221 ? -7.423  24.008  -6.409  1.00 40.51  ? 220 HIS A CE1 1 
ATOM   3798 N NE2 . HIS B 1 221 ? -6.534  23.260  -7.037  1.00 40.64  ? 220 HIS A NE2 1 
ATOM   3799 N N   . PRO B 1 222 ? -8.388  17.723  -4.703  1.00 43.80  ? 221 PRO A N   1 
ATOM   3800 C CA  . PRO B 1 222 ? -8.918  16.578  -3.943  1.00 34.42  ? 221 PRO A CA  1 
ATOM   3801 C C   . PRO B 1 222 ? -10.088 16.949  -3.052  1.00 36.43  ? 221 PRO A C   1 
ATOM   3802 O O   . PRO B 1 222 ? -11.009 16.141  -2.882  1.00 37.86  ? 221 PRO A O   1 
ATOM   3803 C CB  . PRO B 1 222 ? -7.704  16.110  -3.130  1.00 31.75  ? 221 PRO A CB  1 
ATOM   3804 C CG  . PRO B 1 222 ? -6.865  17.341  -2.979  1.00 46.38  ? 221 PRO A CG  1 
ATOM   3805 C CD  . PRO B 1 222 ? -7.034  18.106  -4.263  1.00 42.34  ? 221 PRO A CD  1 
ATOM   3806 N N   . MET B 1 223 ? -10.080 18.152  -2.479  1.00 35.03  ? 222 MET A N   1 
ATOM   3807 C CA  . MET B 1 223 ? -11.147 18.626  -1.612  1.00 32.82  ? 222 MET A CA  1 
ATOM   3808 C C   . MET B 1 223 ? -11.524 20.048  -1.997  1.00 33.53  ? 222 MET A C   1 
ATOM   3809 O O   . MET B 1 223 ? -10.671 20.845  -2.397  1.00 29.33  ? 222 MET A O   1 
ATOM   3810 C CB  . MET B 1 223 ? -10.735 18.610  -0.136  1.00 31.08  ? 222 MET A CB  1 
ATOM   3811 C CG  . MET B 1 223 ? -10.967 17.298  0.594   1.00 45.89  ? 222 MET A CG  1 
ATOM   3812 S SD  . MET B 1 223 ? -10.483 17.416  2.331   1.00 45.82  ? 222 MET A SD  1 
ATOM   3813 C CE  . MET B 1 223 ? -12.043 17.851  3.095   1.00 32.08  ? 222 MET A CE  1 
ATOM   3814 N N   . GLY B 1 224 ? -12.810 20.361  -1.864  1.00 29.06  ? 223 GLY A N   1 
ATOM   3815 C CA  . GLY B 1 224 ? -13.271 21.723  -1.980  1.00 25.16  ? 223 GLY A CA  1 
ATOM   3816 C C   . GLY B 1 224 ? -12.715 22.580  -0.860  1.00 32.06  ? 223 GLY A C   1 
ATOM   3817 O O   . GLY B 1 224 ? -12.398 22.088  0.229   1.00 28.64  ? 223 GLY A O   1 
ATOM   3818 N N   . PRO B 1 225 ? -12.579 23.887  -1.107  1.00 32.28  ? 224 PRO A N   1 
ATOM   3819 C CA  . PRO B 1 225 ? -11.965 24.757  -0.093  1.00 27.76  ? 224 PRO A CA  1 
ATOM   3820 C C   . PRO B 1 225 ? -12.798 24.894  1.166   1.00 26.68  ? 224 PRO A C   1 
ATOM   3821 O O   . PRO B 1 225 ? -12.231 25.013  2.259   1.00 24.51  ? 224 PRO A O   1 
ATOM   3822 C CB  . PRO B 1 225 ? -11.819 26.098  -0.824  1.00 27.52  ? 224 PRO A CB  1 
ATOM   3823 C CG  . PRO B 1 225 ? -12.868 26.059  -1.884  1.00 28.38  ? 224 PRO A CG  1 
ATOM   3824 C CD  . PRO B 1 225 ? -12.971 24.630  -2.314  1.00 25.36  ? 224 PRO A CD  1 
ATOM   3825 N N   . LEU B 1 226 ? -14.127 24.883  1.050   1.00 24.29  ? 225 LEU A N   1 
ATOM   3826 C CA  . LEU B 1 226 ? -14.961 24.984  2.242   1.00 24.40  ? 225 LEU A CA  1 
ATOM   3827 C C   . LEU B 1 226 ? -14.935 23.689  3.049   1.00 32.63  ? 225 LEU A C   1 
ATOM   3828 O O   . LEU B 1 226 ? -14.936 23.729  4.286   1.00 35.31  ? 225 LEU A O   1 
ATOM   3829 C CB  . LEU B 1 226 ? -16.385 25.369  1.849   1.00 29.20  ? 225 LEU A CB  1 
ATOM   3830 C CG  . LEU B 1 226 ? -16.457 26.716  1.122   1.00 28.13  ? 225 LEU A CG  1 
ATOM   3831 C CD1 . LEU B 1 226 ? -17.862 27.017  0.646   1.00 28.90  ? 225 LEU A CD1 1 
ATOM   3832 C CD2 . LEU B 1 226 ? -15.942 27.830  2.024   1.00 30.35  ? 225 LEU A CD2 1 
ATOM   3833 N N   . GLU B 1 227 ? -14.906 22.529  2.380   1.00 30.17  ? 226 GLU A N   1 
ATOM   3834 C CA  . GLU B 1 227 ? -14.660 21.288  3.112   1.00 29.79  ? 226 GLU A CA  1 
ATOM   3835 C C   . GLU B 1 227 ? -13.273 21.302  3.734   1.00 31.18  ? 226 GLU A C   1 
ATOM   3836 O O   . GLU B 1 227 ? -13.087 20.846  4.869   1.00 29.35  ? 226 GLU A O   1 
ATOM   3837 C CB  . GLU B 1 227 ? -14.792 20.054  2.212   1.00 27.99  ? 226 GLU A CB  1 
ATOM   3838 C CG  . GLU B 1 227 ? -15.667 20.179  0.987   1.00 46.48  ? 226 GLU A CG  1 
ATOM   3839 C CD  . GLU B 1 227 ? -15.529 18.976  0.065   1.00 44.62  ? 226 GLU A CD  1 
ATOM   3840 O OE1 . GLU B 1 227 ? -15.854 17.853  0.504   1.00 54.84  ? 226 GLU A OE1 1 
ATOM   3841 O OE2 . GLU B 1 227 ? -15.092 19.149  -1.093  1.00 41.31  ? 226 GLU A OE2 1 
ATOM   3842 N N   . LEU B 1 228 ? -12.282 21.812  2.996   1.00 22.94  ? 227 LEU A N   1 
ATOM   3843 C CA  . LEU B 1 228 ? -10.918 21.849  3.510   1.00 28.15  ? 227 LEU A CA  1 
ATOM   3844 C C   . LEU B 1 228 ? -10.821 22.731  4.746   1.00 31.20  ? 227 LEU A C   1 
ATOM   3845 O O   . LEU B 1 228 ? -10.179 22.359  5.735   1.00 30.72  ? 227 LEU A O   1 
ATOM   3846 C CB  . LEU B 1 228 ? -9.960  22.340  2.426   1.00 22.81  ? 227 LEU A CB  1 
ATOM   3847 C CG  . LEU B 1 228 ? -8.480  22.244  2.785   1.00 27.67  ? 227 LEU A CG  1 
ATOM   3848 C CD1 . LEU B 1 228 ? -8.055  20.789  2.855   1.00 21.69  ? 227 LEU A CD1 1 
ATOM   3849 C CD2 . LEU B 1 228 ? -7.631  23.009  1.782   1.00 25.11  ? 227 LEU A CD2 1 
ATOM   3850 N N   . GLY B 1 229 ? -11.450 23.907  4.708   1.00 27.23  ? 228 GLY A N   1 
ATOM   3851 C CA  . GLY B 1 229 ? -11.464 24.760  5.883   1.00 30.45  ? 228 GLY A CA  1 
ATOM   3852 C C   . GLY B 1 229 ? -12.108 24.080  7.074   1.00 33.32  ? 228 GLY A C   1 
ATOM   3853 O O   . GLY B 1 229 ? -11.634 24.208  8.206   1.00 27.90  ? 228 GLY A O   1 
ATOM   3854 N N   . ASP B 1 230 ? -13.193 23.341  6.833   1.00 31.97  ? 229 ASP A N   1 
ATOM   3855 C CA  . ASP B 1 230 ? -13.826 22.573  7.899   1.00 32.04  ? 229 ASP A CA  1 
ATOM   3856 C C   . ASP B 1 230 ? -12.895 21.488  8.429   1.00 29.22  ? 229 ASP A C   1 
ATOM   3857 O O   . ASP B 1 230 ? -12.881 21.207  9.634   1.00 29.15  ? 229 ASP A O   1 
ATOM   3858 C CB  . ASP B 1 230 ? -15.122 21.948  7.387   1.00 35.55  ? 229 ASP A CB  1 
ATOM   3859 C CG  . ASP B 1 230 ? -16.319 22.870  7.519   1.00 41.15  ? 229 ASP A CG  1 
ATOM   3860 O OD1 . ASP B 1 230 ? -16.128 24.093  7.694   1.00 43.49  ? 229 ASP A OD1 1 
ATOM   3861 O OD2 . ASP B 1 230 ? -17.459 22.362  7.427   1.00 39.81  ? 229 ASP A OD2 1 
ATOM   3862 N N   . PHE B 1 231 ? -12.119 20.860  7.544   1.00 30.73  ? 230 PHE A N   1 
ATOM   3863 C CA  . PHE B 1 231 ? -11.205 19.809  7.981   1.00 29.92  ? 230 PHE A CA  1 
ATOM   3864 C C   . PHE B 1 231 ? -10.018 20.396  8.731   1.00 30.04  ? 230 PHE A C   1 
ATOM   3865 O O   . PHE B 1 231 ? -9.662  19.923  9.817   1.00 30.87  ? 230 PHE A O   1 
ATOM   3866 C CB  . PHE B 1 231 ? -10.733 18.981  6.784   1.00 33.85  ? 230 PHE A CB  1 
ATOM   3867 C CG  . PHE B 1 231 ? -9.777  17.875  7.149   1.00 34.72  ? 230 PHE A CG  1 
ATOM   3868 C CD1 . PHE B 1 231 ? -10.249 16.672  7.654   1.00 33.67  ? 230 PHE A CD1 1 
ATOM   3869 C CD2 . PHE B 1 231 ? -8.410  18.036  6.983   1.00 36.53  ? 230 PHE A CD2 1 
ATOM   3870 C CE1 . PHE B 1 231 ? -9.375  15.653  7.989   1.00 22.96  ? 230 PHE A CE1 1 
ATOM   3871 C CE2 . PHE B 1 231 ? -7.531  17.021  7.318   1.00 35.62  ? 230 PHE A CE2 1 
ATOM   3872 C CZ  . PHE B 1 231 ? -8.016  15.827  7.822   1.00 34.81  ? 230 PHE A CZ  1 
ATOM   3873 N N   . ILE B 1 232 ? -9.384  21.424  8.161   1.00 31.77  ? 231 ILE A N   1 
ATOM   3874 C CA  . ILE B 1 232 ? -8.291  22.098  8.856   1.00 25.62  ? 231 ILE A CA  1 
ATOM   3875 C C   . ILE B 1 232 ? -8.779  22.681  10.174  1.00 30.32  ? 231 ILE A C   1 
ATOM   3876 O O   . ILE B 1 232 ? -8.043  22.693  11.169  1.00 23.70  ? 231 ILE A O   1 
ATOM   3877 C CB  . ILE B 1 232 ? -7.677  23.183  7.949   1.00 34.71  ? 231 ILE A CB  1 
ATOM   3878 C CG1 . ILE B 1 232 ? -7.094  22.550  6.682   1.00 30.80  ? 231 ILE A CG1 1 
ATOM   3879 C CG2 . ILE B 1 232 ? -6.620  23.983  8.698   1.00 24.02  ? 231 ILE A CG2 1 
ATOM   3880 C CD1 . ILE B 1 232 ? -6.419  23.541  5.751   1.00 31.00  ? 231 ILE A CD1 1 
ATOM   3881 N N   . GLY B 1 233 ? -10.029 23.136  10.217  1.00 25.91  ? 232 GLY A N   1 
ATOM   3882 C CA  . GLY B 1 233 ? -10.547 23.821  11.384  1.00 26.75  ? 232 GLY A CA  1 
ATOM   3883 C C   . GLY B 1 233 ? -10.542 25.318  11.168  1.00 28.37  ? 232 GLY A C   1 
ATOM   3884 O O   . GLY B 1 233 ? -9.484  25.912  10.930  1.00 27.84  ? 232 GLY A O   1 
ATOM   3885 N N   . LEU B 1 234 ? -11.723 25.937  11.235  1.00 25.93  ? 233 LEU A N   1 
ATOM   3886 C CA  . LEU B 1 234 ? -11.858 27.342  10.866  1.00 26.66  ? 233 LEU A CA  1 
ATOM   3887 C C   . LEU B 1 234 ? -11.141 28.280  11.829  1.00 29.13  ? 233 LEU A C   1 
ATOM   3888 O O   . LEU B 1 234 ? -10.831 29.415  11.448  1.00 23.87  ? 233 LEU A O   1 
ATOM   3889 C CB  . LEU B 1 234 ? -13.337 27.712  10.776  1.00 20.86  ? 233 LEU A CB  1 
ATOM   3890 C CG  . LEU B 1 234 ? -14.108 26.954  9.693   1.00 24.80  ? 233 LEU A CG  1 
ATOM   3891 C CD1 . LEU B 1 234 ? -15.515 27.493  9.582   1.00 28.33  ? 233 LEU A CD1 1 
ATOM   3892 C CD2 . LEU B 1 234 ? -13.390 27.046  8.350   1.00 20.91  ? 233 LEU A CD2 1 
ATOM   3893 N N   . ASP B 1 235 ? -10.881 27.844  13.065  1.00 28.09  ? 234 ASP A N   1 
ATOM   3894 C CA  . ASP B 1 235 ? -10.092 28.669  13.972  1.00 24.38  ? 234 ASP A CA  1 
ATOM   3895 C C   . ASP B 1 235 ? -8.637  28.737  13.521  1.00 29.63  ? 234 ASP A C   1 
ATOM   3896 O O   . ASP B 1 235 ? -7.991  29.785  13.640  1.00 30.17  ? 234 ASP A O   1 
ATOM   3897 C CB  . ASP B 1 235 ? -10.203 28.135  15.402  1.00 32.32  ? 234 ASP A CB  1 
ATOM   3898 C CG  . ASP B 1 235 ? -9.957  26.635  15.494  1.00 37.80  ? 234 ASP A CG  1 
ATOM   3899 O OD1 . ASP B 1 235 ? -10.137 25.928  14.477  1.00 30.75  ? 234 ASP A OD1 1 
ATOM   3900 O OD2 . ASP B 1 235 ? -9.597  26.165  16.596  1.00 36.38  ? 234 ASP A OD2 1 
ATOM   3901 N N   . ILE B 1 236 ? -8.108  27.630  12.994  1.00 23.62  ? 235 ILE A N   1 
ATOM   3902 C CA  . ILE B 1 236 ? -6.755  27.636  12.446  1.00 23.18  ? 235 ILE A CA  1 
ATOM   3903 C C   . ILE B 1 236 ? -6.680  28.551  11.230  1.00 25.38  ? 235 ILE A C   1 
ATOM   3904 O O   . ILE B 1 236 ? -5.747  29.351  11.093  1.00 25.22  ? 235 ILE A O   1 
ATOM   3905 C CB  . ILE B 1 236 ? -6.308  26.203  12.098  1.00 33.83  ? 235 ILE A CB  1 
ATOM   3906 C CG1 . ILE B 1 236 ? -6.495  25.265  13.296  1.00 32.29  ? 235 ILE A CG1 1 
ATOM   3907 C CG2 . ILE B 1 236 ? -4.865  26.194  11.606  1.00 22.19  ? 235 ILE A CG2 1 
ATOM   3908 C CD1 . ILE B 1 236 ? -5.709  25.670  14.522  1.00 37.16  ? 235 ILE A CD1 1 
ATOM   3909 N N   . CYS B 1 237 ? -7.662  28.448  10.328  1.00 22.37  ? 236 CYS A N   1 
ATOM   3910 C CA  . CYS B 1 237 ? -7.664  29.284  9.129   1.00 24.75  ? 236 CYS A CA  1 
ATOM   3911 C C   . CYS B 1 237 ? -7.753  30.758  9.486   1.00 23.58  ? 236 CYS A C   1 
ATOM   3912 O O   . CYS B 1 237 ? -7.007  31.584  8.945   1.00 29.53  ? 236 CYS A O   1 
ATOM   3913 C CB  . CYS B 1 237 ? -8.828  28.903  8.214   1.00 21.11  ? 236 CYS A CB  1 
ATOM   3914 S SG  . CYS B 1 237 ? -8.795  27.209  7.597   1.00 32.57  ? 236 CYS A SG  1 
ATOM   3915 N N   . LEU B 1 238 ? -8.675  31.107  10.386  1.00 25.52  ? 237 LEU A N   1 
ATOM   3916 C CA  . LEU B 1 238 ? -8.791  32.489  10.835  1.00 29.48  ? 237 LEU A CA  1 
ATOM   3917 C C   . LEU B 1 238 ? -7.472  32.997  11.400  1.00 31.32  ? 237 LEU A C   1 
ATOM   3918 O O   . LEU B 1 238 ? -7.035  34.105  11.070  1.00 30.71  ? 237 LEU A O   1 
ATOM   3919 C CB  . LEU B 1 238 ? -9.901  32.606  11.879  1.00 22.10  ? 237 LEU A CB  1 
ATOM   3920 C CG  . LEU B 1 238 ? -10.215 34.032  12.320  1.00 27.49  ? 237 LEU A CG  1 
ATOM   3921 C CD1 . LEU B 1 238 ? -10.688 34.860  11.130  1.00 27.88  ? 237 LEU A CD1 1 
ATOM   3922 C CD2 . LEU B 1 238 ? -11.245 34.037  13.433  1.00 23.38  ? 237 LEU A CD2 1 
ATOM   3923 N N   . ALA B 1 239 ? -6.814  32.195  12.242  1.00 23.47  ? 238 ALA A N   1 
ATOM   3924 C CA  . ALA B 1 239 ? -5.564  32.643  12.846  1.00 27.83  ? 238 ALA A CA  1 
ATOM   3925 C C   . ALA B 1 239 ? -4.464  32.822  11.807  1.00 27.36  ? 238 ALA A C   1 
ATOM   3926 O O   . ALA B 1 239 ? -3.621  33.716  11.947  1.00 22.94  ? 238 ALA A O   1 
ATOM   3927 C CB  . ALA B 1 239 ? -5.117  31.661  13.929  1.00 19.92  ? 238 ALA A CB  1 
ATOM   3928 N N   . ILE B 1 240 ? -4.450  31.987  10.766  1.00 29.38  ? 239 ILE A N   1 
ATOM   3929 C CA  . ILE B 1 240 ? -3.433  32.125  9.728   1.00 27.32  ? 239 ILE A CA  1 
ATOM   3930 C C   . ILE B 1 240 ? -3.665  33.394  8.919   1.00 27.84  ? 239 ILE A C   1 
ATOM   3931 O O   . ILE B 1 240 ? -2.719  34.130  8.609   1.00 26.51  ? 239 ILE A O   1 
ATOM   3932 C CB  . ILE B 1 240 ? -3.409  30.876  8.829   1.00 30.99  ? 239 ILE A CB  1 
ATOM   3933 C CG1 . ILE B 1 240 ? -3.015  29.639  9.643   1.00 28.73  ? 239 ILE A CG1 1 
ATOM   3934 C CG2 . ILE B 1 240 ? -2.485  31.091  7.634   1.00 17.19  ? 239 ILE A CG2 1 
ATOM   3935 C CD1 . ILE B 1 240 ? -1.544  29.312  9.600   1.00 33.38  ? 239 ILE A CD1 1 
ATOM   3936 N N   . MET B 1 241 ? -4.922  33.665  8.555   1.00 31.57  ? 240 MET A N   1 
ATOM   3937 C CA  . MET B 1 241 ? -5.240  34.901  7.847   1.00 23.11  ? 240 MET A CA  1 
ATOM   3938 C C   . MET B 1 241 ? -4.830  36.117  8.666   1.00 27.28  ? 240 MET A C   1 
ATOM   3939 O O   . MET B 1 241 ? -4.252  37.070  8.130   1.00 25.47  ? 240 MET A O   1 
ATOM   3940 C CB  . MET B 1 241 ? -6.735  34.959  7.525   1.00 19.58  ? 240 MET A CB  1 
ATOM   3941 C CG  . MET B 1 241 ? -7.196  34.009  6.426   1.00 19.12  ? 240 MET A CG  1 
ATOM   3942 S SD  . MET B 1 241 ? -6.072  33.932  5.014   1.00 28.58  ? 240 MET A SD  1 
ATOM   3943 C CE  . MET B 1 241 ? -6.394  35.510  4.220   1.00 28.19  ? 240 MET A CE  1 
ATOM   3944 N N   . ASP B 1 242 ? -5.108  36.097  9.973   1.00 24.95  ? 241 ASP A N   1 
ATOM   3945 C CA  . ASP B 1 242 ? -4.756  37.232  10.820  1.00 26.35  ? 241 ASP A CA  1 
ATOM   3946 C C   . ASP B 1 242 ? -3.243  37.406  10.924  1.00 23.75  ? 241 ASP A C   1 
ATOM   3947 O O   . ASP B 1 242 ? -2.746  38.537  10.957  1.00 25.22  ? 241 ASP A O   1 
ATOM   3948 C CB  . ASP B 1 242 ? -5.389  37.062  12.199  1.00 27.08  ? 241 ASP A CB  1 
ATOM   3949 C CG  . ASP B 1 242 ? -6.873  37.381  12.197  1.00 32.50  ? 241 ASP A CG  1 
ATOM   3950 O OD1 . ASP B 1 242 ? -7.349  37.976  11.204  1.00 33.46  ? 241 ASP A OD1 1 
ATOM   3951 O OD2 . ASP B 1 242 ? -7.564  37.037  13.179  1.00 34.60  ? 241 ASP A OD2 1 
ATOM   3952 N N   . VAL B 1 243 ? -2.495  36.303  10.965  1.00 22.91  ? 242 VAL A N   1 
ATOM   3953 C CA  . VAL B 1 243 ? -1.037  36.395  10.977  1.00 21.79  ? 242 VAL A CA  1 
ATOM   3954 C C   . VAL B 1 243 ? -0.533  37.008  9.675   1.00 28.95  ? 242 VAL A C   1 
ATOM   3955 O O   . VAL B 1 243 ? 0.294   37.928  9.683   1.00 23.74  ? 242 VAL A O   1 
ATOM   3956 C CB  . VAL B 1 243 ? -0.414  35.010  11.232  1.00 26.67  ? 242 VAL A CB  1 
ATOM   3957 C CG1 . VAL B 1 243 ? 1.041   34.980  10.786  1.00 29.12  ? 242 VAL A CG1 1 
ATOM   3958 C CG2 . VAL B 1 243 ? -0.525  34.642  12.701  1.00 28.20  ? 242 VAL A CG2 1 
ATOM   3959 N N   . LEU B 1 244 ? -1.030  36.509  8.537   1.00 20.31  ? 243 LEU A N   1 
ATOM   3960 C CA  . LEU B 1 244 ? -0.633  37.066  7.245   1.00 22.17  ? 243 LEU A CA  1 
ATOM   3961 C C   . LEU B 1 244 ? -0.949  38.553  7.166   1.00 23.25  ? 243 LEU A C   1 
ATOM   3962 O O   . LEU B 1 244 ? -0.138  39.345  6.668   1.00 25.02  ? 243 LEU A O   1 
ATOM   3963 C CB  . LEU B 1 244 ? -1.331  36.313  6.112   1.00 22.00  ? 243 LEU A CB  1 
ATOM   3964 C CG  . LEU B 1 244 ? -0.934  34.847  5.934   1.00 23.65  ? 243 LEU A CG  1 
ATOM   3965 C CD1 . LEU B 1 244 ? -1.872  34.126  4.963   1.00 14.94  ? 243 LEU A CD1 1 
ATOM   3966 C CD2 . LEU B 1 244 ? 0.507   34.747  5.469   1.00 23.15  ? 243 LEU A CD2 1 
ATOM   3967 N N   . TYR B 1 245 ? -2.117  38.954  7.665   1.00 20.61  ? 244 TYR A N   1 
ATOM   3968 C CA  . TYR B 1 245 ? -2.486  40.361  7.636   1.00 18.23  ? 244 TYR A CA  1 
ATOM   3969 C C   . TYR B 1 245 ? -1.540  41.196  8.494   1.00 25.37  ? 244 TYR A C   1 
ATOM   3970 O O   . TYR B 1 245 ? -0.976  42.190  8.024   1.00 24.18  ? 244 TYR A O   1 
ATOM   3971 C CB  . TYR B 1 245 ? -3.936  40.525  8.094   1.00 23.36  ? 244 TYR A CB  1 
ATOM   3972 C CG  . TYR B 1 245 ? -4.432  41.954  8.057   1.00 27.62  ? 244 TYR A CG  1 
ATOM   3973 C CD1 . TYR B 1 245 ? -4.299  42.726  6.910   1.00 26.14  ? 244 TYR A CD1 1 
ATOM   3974 C CD2 . TYR B 1 245 ? -5.034  42.529  9.167   1.00 31.74  ? 244 TYR A CD2 1 
ATOM   3975 C CE1 . TYR B 1 245 ? -4.749  44.028  6.868   1.00 21.37  ? 244 TYR A CE1 1 
ATOM   3976 C CE2 . TYR B 1 245 ? -5.490  43.834  9.134   1.00 41.07  ? 244 TYR A CE2 1 
ATOM   3977 C CZ  . TYR B 1 245 ? -5.345  44.578  7.982   1.00 32.08  ? 244 TYR A CZ  1 
ATOM   3978 O OH  . TYR B 1 245 ? -5.796  45.879  7.944   1.00 42.08  ? 244 TYR A OH  1 
ATOM   3979 N N   . HIS B 1 246 ? -1.330  40.789  9.750   1.00 23.32  ? 245 HIS A N   1 
ATOM   3980 C CA  . HIS B 1 246 ? -0.542  41.607  10.668  1.00 27.32  ? 245 HIS A CA  1 
ATOM   3981 C C   . HIS B 1 246 ? 0.937   41.628  10.295  1.00 22.25  ? 245 HIS A C   1 
ATOM   3982 O O   . HIS B 1 246 ? 1.621   42.624  10.554  1.00 28.90  ? 245 HIS A O   1 
ATOM   3983 C CB  . HIS B 1 246 ? -0.723  41.114  12.106  1.00 25.29  ? 245 HIS A CB  1 
ATOM   3984 C CG  . HIS B 1 246 ? -2.096  41.351  12.659  1.00 34.81  ? 245 HIS A CG  1 
ATOM   3985 N ND1 . HIS B 1 246 ? -2.795  40.390  13.357  1.00 42.66  ? 245 HIS A ND1 1 
ATOM   3986 C CD2 . HIS B 1 246 ? -2.900  42.440  12.611  1.00 45.07  ? 245 HIS A CD2 1 
ATOM   3987 C CE1 . HIS B 1 246 ? -3.970  40.877  13.717  1.00 39.58  ? 245 HIS A CE1 1 
ATOM   3988 N NE2 . HIS B 1 246 ? -4.058  42.119  13.277  1.00 39.34  ? 245 HIS A NE2 1 
ATOM   3989 N N   . GLU B 1 247 ? 1.448   40.553  9.690   1.00 26.23  ? 246 GLU A N   1 
ATOM   3990 C CA  . GLU B 1 247 ? 2.861   40.500  9.325   1.00 29.39  ? 246 GLU A CA  1 
ATOM   3991 C C   . GLU B 1 247 ? 3.172   41.322  8.080   1.00 26.90  ? 246 GLU A C   1 
ATOM   3992 O O   . GLU B 1 247 ? 4.274   41.873  7.967   1.00 32.50  ? 246 GLU A O   1 
ATOM   3993 C CB  . GLU B 1 247 ? 3.297   39.051  9.100   1.00 21.77  ? 246 GLU A CB  1 
ATOM   3994 C CG  . GLU B 1 247 ? 3.428   38.236  10.368  1.00 27.16  ? 246 GLU A CG  1 
ATOM   3995 C CD  . GLU B 1 247 ? 4.618   38.653  11.209  1.00 32.91  ? 246 GLU A CD  1 
ATOM   3996 O OE1 . GLU B 1 247 ? 5.700   38.896  10.632  1.00 28.47  ? 246 GLU A OE1 1 
ATOM   3997 O OE2 . GLU B 1 247 ? 4.467   38.741  12.447  1.00 28.58  ? 246 GLU A OE2 1 
ATOM   3998 N N   . THR B 1 248 ? 2.234   41.408  7.136   1.00 22.49  ? 247 THR A N   1 
ATOM   3999 C CA  . THR B 1 248 ? 2.450   42.159  5.906   1.00 30.01  ? 247 THR A CA  1 
ATOM   4000 C C   . THR B 1 248 ? 1.834   43.549  5.933   1.00 29.16  ? 247 THR A C   1 
ATOM   4001 O O   . THR B 1 248 ? 2.297   44.423  5.194   1.00 28.80  ? 247 THR A O   1 
ATOM   4002 C CB  . THR B 1 248 ? 1.879   41.401  4.698   1.00 26.21  ? 247 THR A CB  1 
ATOM   4003 O OG1 . THR B 1 248 ? 0.452   41.329  4.808   1.00 23.50  ? 247 THR A OG1 1 
ATOM   4004 C CG2 . THR B 1 248 ? 2.446   39.993  4.628   1.00 23.65  ? 247 THR A CG2 1 
ATOM   4005 N N   . GLY B 1 249 ? 0.814   43.775  6.760   1.00 26.88  ? 248 GLY A N   1 
ATOM   4006 C CA  . GLY B 1 249 ? 0.090   45.028  6.719   1.00 24.41  ? 248 GLY A CA  1 
ATOM   4007 C C   . GLY B 1 249 ? -0.681  45.263  5.442   1.00 31.36  ? 248 GLY A C   1 
ATOM   4008 O O   . GLY B 1 249 ? -1.103  46.396  5.189   1.00 30.49  ? 248 GLY A O   1 
ATOM   4009 N N   . ASP B 1 250 ? -0.880  44.222  4.634   1.00 33.05  ? 249 ASP A N   1 
ATOM   4010 C CA  . ASP B 1 250 ? -1.533  44.312  3.333   1.00 25.96  ? 249 ASP A CA  1 
ATOM   4011 C C   . ASP B 1 250 ? -2.973  43.836  3.475   1.00 26.78  ? 249 ASP A C   1 
ATOM   4012 O O   . ASP B 1 250 ? -3.213  42.702  3.904   1.00 27.04  ? 249 ASP A O   1 
ATOM   4013 C CB  . ASP B 1 250 ? -0.775  43.465  2.307   1.00 23.52  ? 249 ASP A CB  1 
ATOM   4014 C CG  . ASP B 1 250 ? -1.297  43.628  0.877   1.00 33.11  ? 249 ASP A CG  1 
ATOM   4015 O OD1 . ASP B 1 250 ? -2.377  44.221  0.666   1.00 30.54  ? 249 ASP A OD1 1 
ATOM   4016 O OD2 . ASP B 1 250 ? -0.616  43.134  -0.048  1.00 33.47  ? 249 ASP A OD2 1 
ATOM   4017 N N   . SER B 1 251 ? -3.926  44.696  3.101   1.00 26.70  ? 250 SER A N   1 
ATOM   4018 C CA  . SER B 1 251 ? -5.346  44.363  3.176   1.00 28.24  ? 250 SER A CA  1 
ATOM   4019 C C   . SER B 1 251 ? -5.729  43.193  2.282   1.00 27.90  ? 250 SER A C   1 
ATOM   4020 O O   . SER B 1 251 ? -6.855  42.695  2.391   1.00 22.33  ? 250 SER A O   1 
ATOM   4021 C CB  . SER B 1 251 ? -6.195  45.579  2.800   1.00 29.13  ? 250 SER A CB  1 
ATOM   4022 O OG  . SER B 1 251 ? -6.579  46.307  3.953   1.00 48.86  ? 250 SER A OG  1 
ATOM   4023 N N   . LYS B 1 252 ? -4.828  42.755  1.400   1.00 23.95  ? 251 LYS A N   1 
ATOM   4024 C CA  . LYS B 1 252 ? -5.089  41.596  0.556   1.00 26.92  ? 251 LYS A CA  1 
ATOM   4025 C C   . LYS B 1 252 ? -5.382  40.347  1.382   1.00 25.29  ? 251 LYS A C   1 
ATOM   4026 O O   . LYS B 1 252 ? -6.091  39.446  0.920   1.00 27.13  ? 251 LYS A O   1 
ATOM   4027 C CB  . LYS B 1 252 ? -3.889  41.382  -0.374  1.00 27.76  ? 251 LYS A CB  1 
ATOM   4028 C CG  . LYS B 1 252 ? -3.752  40.002  -0.969  1.00 27.92  ? 251 LYS A CG  1 
ATOM   4029 C CD  . LYS B 1 252 ? -2.371  39.818  -1.578  1.00 29.25  ? 251 LYS A CD  1 
ATOM   4030 C CE  . LYS B 1 252 ? -2.391  38.754  -2.657  1.00 31.13  ? 251 LYS A CE  1 
ATOM   4031 N NZ  . LYS B 1 252 ? -1.123  38.723  -3.440  1.00 37.43  ? 251 LYS A NZ  1 
ATOM   4032 N N   . TYR B 1 253 ? -4.876  40.281  2.611   1.00 25.93  ? 252 TYR A N   1 
ATOM   4033 C CA  . TYR B 1 253 ? -5.031  39.103  3.452   1.00 25.86  ? 252 TYR A CA  1 
ATOM   4034 C C   . TYR B 1 253 ? -6.072  39.303  4.550   1.00 30.86  ? 252 TYR A C   1 
ATOM   4035 O O   . TYR B 1 253 ? -6.031  38.621  5.577   1.00 26.77  ? 252 TYR A O   1 
ATOM   4036 C CB  . TYR B 1 253 ? -3.682  38.701  4.052   1.00 25.64  ? 252 TYR A CB  1 
ATOM   4037 C CG  . TYR B 1 253 ? -2.615  38.471  3.006   1.00 31.47  ? 252 TYR A CG  1 
ATOM   4038 C CD1 . TYR B 1 253 ? -2.644  37.340  2.197   1.00 29.46  ? 252 TYR A CD1 1 
ATOM   4039 C CD2 . TYR B 1 253 ? -1.588  39.388  2.816   1.00 33.06  ? 252 TYR A CD2 1 
ATOM   4040 C CE1 . TYR B 1 253 ? -1.678  37.126  1.230   1.00 26.63  ? 252 TYR A CE1 1 
ATOM   4041 C CE2 . TYR B 1 253 ? -0.615  39.181  1.851   1.00 28.80  ? 252 TYR A CE2 1 
ATOM   4042 C CZ  . TYR B 1 253 ? -0.666  38.049  1.062   1.00 35.68  ? 252 TYR A CZ  1 
ATOM   4043 O OH  . TYR B 1 253 ? 0.296   37.840  0.101   1.00 30.98  ? 252 TYR A OH  1 
ATOM   4044 N N   . ARG B 1 254 ? -7.019  40.221  4.351   1.00 25.99  ? 253 ARG A N   1 
ATOM   4045 C CA  . ARG B 1 254 ? -8.058  40.422  5.352   1.00 21.44  ? 253 ARG A CA  1 
ATOM   4046 C C   . ARG B 1 254 ? -8.964  39.201  5.404   1.00 25.04  ? 253 ARG A C   1 
ATOM   4047 O O   . ARG B 1 254 ? -9.479  38.748  4.377   1.00 22.04  ? 253 ARG A O   1 
ATOM   4048 C CB  . ARG B 1 254 ? -8.872  41.688  5.066   1.00 22.78  ? 253 ARG A CB  1 
ATOM   4049 C CG  . ARG B 1 254 ? -9.569  41.762  3.708   1.00 23.15  ? 253 ARG A CG  1 
ATOM   4050 C CD  . ARG B 1 254 ? -10.247 43.124  3.529   1.00 26.19  ? 253 ARG A CD  1 
ATOM   4051 N NE  . ARG B 1 254 ? -11.116 43.181  2.360   1.00 36.16  ? 253 ARG A NE  1 
ATOM   4052 C CZ  . ARG B 1 254 ? -10.686 43.248  1.106   1.00 43.07  ? 253 ARG A CZ  1 
ATOM   4053 N NH1 . ARG B 1 254 ? -9.394  43.290  0.816   1.00 28.95  ? 253 ARG A NH1 1 
ATOM   4054 N NH2 . ARG B 1 254 ? -11.574 43.274  0.116   1.00 46.52  ? 253 ARG A NH2 1 
ATOM   4055 N N   . ALA B 1 255 ? -9.137  38.655  6.603   1.00 20.64  ? 254 ALA A N   1 
ATOM   4056 C CA  . ALA B 1 255 ? -9.964  37.472  6.771   1.00 21.80  ? 254 ALA A CA  1 
ATOM   4057 C C   . ALA B 1 255 ? -11.418 37.791  6.452   1.00 23.80  ? 254 ALA A C   1 
ATOM   4058 O O   . ALA B 1 255 ? -11.909 38.888  6.737   1.00 24.94  ? 254 ALA A O   1 
ATOM   4059 C CB  . ALA B 1 255 ? -9.843  36.937  8.196   1.00 22.59  ? 254 ALA A CB  1 
ATOM   4060 N N   . CYS B 1 256 ? -12.099 36.825  5.854   1.00 23.48  ? 255 CYS A N   1 
ATOM   4061 C CA  . CYS B 1 256 ? -13.508 36.971  5.527   1.00 29.77  ? 255 CYS A CA  1 
ATOM   4062 C C   . CYS B 1 256 ? -14.325 37.096  6.807   1.00 27.90  ? 255 CYS A C   1 
ATOM   4063 O O   . CYS B 1 256 ? -14.262 36.199  7.661   1.00 26.60  ? 255 CYS A O   1 
ATOM   4064 C CB  . CYS B 1 256 ? -13.985 35.776  4.709   1.00 22.05  ? 255 CYS A CB  1 
ATOM   4065 S SG  . CYS B 1 256 ? -15.748 35.792  4.337   1.00 26.87  ? 255 CYS A SG  1 
ATOM   4066 N N   . PRO B 1 257 ? -15.088 38.178  6.987   1.00 25.29  ? 256 PRO A N   1 
ATOM   4067 C CA  . PRO B 1 257 ? -15.885 38.324  8.217   1.00 26.29  ? 256 PRO A CA  1 
ATOM   4068 C C   . PRO B 1 257 ? -16.850 37.178  8.459   1.00 33.50  ? 256 PRO A C   1 
ATOM   4069 O O   . PRO B 1 257 ? -17.203 36.922  9.618   1.00 28.98  ? 256 PRO A O   1 
ATOM   4070 C CB  . PRO B 1 257 ? -16.631 39.646  7.995   1.00 23.71  ? 256 PRO A CB  1 
ATOM   4071 C CG  . PRO B 1 257 ? -15.773 40.400  7.024   1.00 23.47  ? 256 PRO A CG  1 
ATOM   4072 C CD  . PRO B 1 257 ? -15.176 39.364  6.120   1.00 28.00  ? 256 PRO A CD  1 
ATOM   4073 N N   . LEU B 1 258 ? -17.287 36.479  7.408   1.00 31.91  ? 257 LEU A N   1 
ATOM   4074 C CA  . LEU B 1 258 ? -18.138 35.311  7.604   1.00 30.12  ? 257 LEU A CA  1 
ATOM   4075 C C   . LEU B 1 258 ? -17.434 34.249  8.441   1.00 28.05  ? 257 LEU A C   1 
ATOM   4076 O O   . LEU B 1 258 ? -18.037 33.666  9.348   1.00 24.71  ? 257 LEU A O   1 
ATOM   4077 C CB  . LEU B 1 258 ? -18.560 34.733  6.256   1.00 25.44  ? 257 LEU A CB  1 
ATOM   4078 C CG  . LEU B 1 258 ? -19.321 33.406  6.309   1.00 21.94  ? 257 LEU A CG  1 
ATOM   4079 C CD1 . LEU B 1 258 ? -20.500 33.482  7.275   1.00 18.14  ? 257 LEU A CD1 1 
ATOM   4080 C CD2 . LEU B 1 258 ? -19.790 33.022  4.918   1.00 26.56  ? 257 LEU A CD2 1 
ATOM   4081 N N   . ILE B 1 259 ? -16.160 33.977  8.148   1.00 25.46  ? 258 ILE A N   1 
ATOM   4082 C CA  . ILE B 1 259 ? -15.426 32.990  8.934   1.00 30.38  ? 258 ILE A CA  1 
ATOM   4083 C C   . ILE B 1 259 ? -15.300 33.451  10.378  1.00 31.98  ? 258 ILE A C   1 
ATOM   4084 O O   . ILE B 1 259 ? -15.497 32.667  11.314  1.00 35.05  ? 258 ILE A O   1 
ATOM   4085 C CB  . ILE B 1 259 ? -14.047 32.712  8.312   1.00 23.75  ? 258 ILE A CB  1 
ATOM   4086 C CG1 . ILE B 1 259 ? -14.201 32.044  6.950   1.00 23.59  ? 258 ILE A CG1 1 
ATOM   4087 C CG2 . ILE B 1 259 ? -13.219 31.828  9.233   1.00 22.85  ? 258 ILE A CG2 1 
ATOM   4088 C CD1 . ILE B 1 259 ? -12.892 31.608  6.348   1.00 19.49  ? 258 ILE A CD1 1 
ATOM   4089 N N   . ARG B 1 260 ? -14.979 34.731  10.583  1.00 25.78  ? 259 ARG A N   1 
ATOM   4090 C CA  . ARG B 1 260 ? -14.837 35.240  11.943  1.00 27.94  ? 259 ARG A CA  1 
ATOM   4091 C C   . ARG B 1 260 ? -16.137 35.106  12.726  1.00 27.88  ? 259 ARG A C   1 
ATOM   4092 O O   . ARG B 1 260 ? -16.109 34.862  13.939  1.00 30.87  ? 259 ARG A O   1 
ATOM   4093 C CB  . ARG B 1 260 ? -14.370 36.697  11.917  1.00 26.58  ? 259 ARG A CB  1 
ATOM   4094 C CG  . ARG B 1 260 ? -13.665 37.138  13.193  1.00 34.57  ? 259 ARG A CG  1 
ATOM   4095 C CD  . ARG B 1 260 ? -13.315 38.622  13.169  1.00 30.03  ? 259 ARG A CD  1 
ATOM   4096 N NE  . ARG B 1 260 ? -12.334 38.965  12.142  1.00 24.41  ? 259 ARG A NE  1 
ATOM   4097 C CZ  . ARG B 1 260 ? -11.031 38.725  12.228  1.00 25.69  ? 259 ARG A CZ  1 
ATOM   4098 N NH1 . ARG B 1 260 ? -10.508 38.090  13.269  1.00 19.81  ? 259 ARG A NH1 1 
ATOM   4099 N NH2 . ARG B 1 260 ? -10.229 39.140  11.251  1.00 22.73  ? 259 ARG A NH2 1 
ATOM   4100 N N   . LYS B 1 261 ? -17.283 35.243  12.055  1.00 30.47  ? 260 LYS A N   1 
ATOM   4101 C CA  . LYS B 1 261 ? -18.555 35.060  12.745  1.00 33.99  ? 260 LYS A CA  1 
ATOM   4102 C C   . LYS B 1 261 ? -18.761 33.605  13.142  1.00 33.37  ? 260 LYS A C   1 
ATOM   4103 O O   . LYS B 1 261 ? -19.303 33.321  14.216  1.00 33.77  ? 260 LYS A O   1 
ATOM   4104 C CB  . LYS B 1 261 ? -19.713 35.535  11.870  1.00 29.59  ? 260 LYS A CB  1 
ATOM   4105 C CG  . LYS B 1 261 ? -21.047 35.549  12.599  1.00 37.91  ? 260 LYS A CG  1 
ATOM   4106 C CD  . LYS B 1 261 ? -22.212 35.530  11.630  1.00 40.57  ? 260 LYS A CD  1 
ATOM   4107 C CE  . LYS B 1 261 ? -22.136 36.691  10.661  1.00 34.83  ? 260 LYS A CE  1 
ATOM   4108 N NZ  . LYS B 1 261 ? -23.440 36.921  9.979   1.00 28.37  ? 260 LYS A NZ  1 
ATOM   4109 N N   . MET B 1 262 ? -18.333 32.671  12.291  1.00 24.48  ? 261 MET A N   1 
ATOM   4110 C CA  . MET B 1 262 ? -18.542 31.258  12.589  1.00 33.18  ? 261 MET A CA  1 
ATOM   4111 C C   . MET B 1 262 ? -17.624 30.796  13.712  1.00 30.19  ? 261 MET A C   1 
ATOM   4112 O O   . MET B 1 262 ? -18.039 30.023  14.584  1.00 28.79  ? 261 MET A O   1 
ATOM   4113 C CB  . MET B 1 262 ? -18.318 30.419  11.332  1.00 24.94  ? 261 MET A CB  1 
ATOM   4114 C CG  . MET B 1 262 ? -19.184 30.843  10.155  1.00 28.00  ? 261 MET A CG  1 
ATOM   4115 S SD  . MET B 1 262 ? -18.711 30.031  8.616   1.00 36.01  ? 261 MET A SD  1 
ATOM   4116 C CE  . MET B 1 262 ? -18.923 28.316  9.075   1.00 32.71  ? 261 MET A CE  1 
ATOM   4117 N N   . VAL B 1 263 ? -16.370 31.254  13.700  1.00 26.07  ? 262 VAL A N   1 
ATOM   4118 C CA  . VAL B 1 263 ? -15.440 30.920  14.773  1.00 29.18  ? 262 VAL A CA  1 
ATOM   4119 C C   . VAL B 1 263 ? -15.964 31.439  16.107  1.00 29.25  ? 262 VAL A C   1 
ATOM   4120 O O   . VAL B 1 263 ? -15.815 30.786  17.148  1.00 36.25  ? 262 VAL A O   1 
ATOM   4121 C CB  . VAL B 1 263 ? -14.039 31.474  14.448  1.00 29.31  ? 262 VAL A CB  1 
ATOM   4122 C CG1 . VAL B 1 263 ? -13.068 31.242  15.606  1.00 24.52  ? 262 VAL A CG1 1 
ATOM   4123 C CG2 . VAL B 1 263 ? -13.511 30.845  13.180  1.00 23.30  ? 262 VAL A CG2 1 
ATOM   4124 N N   . ARG B 1 264 ? -16.617 32.604  16.091  1.00 27.93  ? 263 ARG A N   1 
ATOM   4125 C CA  . ARG B 1 264 ? -17.146 33.174  17.325  1.00 26.42  ? 263 ARG A CA  1 
ATOM   4126 C C   . ARG B 1 264 ? -18.316 32.363  17.874  1.00 30.87  ? 263 ARG A C   1 
ATOM   4127 O O   . ARG B 1 264 ? -18.574 32.393  19.083  1.00 30.53  ? 263 ARG A O   1 
ATOM   4128 C CB  . ARG B 1 264 ? -17.567 34.624  17.091  1.00 26.09  ? 263 ARG A CB  1 
ATOM   4129 C CG  . ARG B 1 264 ? -16.449 35.626  17.303  1.00 19.54  ? 263 ARG A CG  1 
ATOM   4130 C CD  . ARG B 1 264 ? -16.750 36.931  16.597  1.00 21.59  ? 263 ARG A CD  1 
ATOM   4131 N NE  . ARG B 1 264 ? -15.715 37.931  16.828  1.00 23.53  ? 263 ARG A NE  1 
ATOM   4132 C CZ  . ARG B 1 264 ? -15.605 39.062  16.144  1.00 30.66  ? 263 ARG A CZ  1 
ATOM   4133 N NH1 . ARG B 1 264 ? -16.453 39.369  15.177  1.00 27.69  ? 263 ARG A NH1 1 
ATOM   4134 N NH2 . ARG B 1 264 ? -14.617 39.903  16.433  1.00 28.32  ? 263 ARG A NH2 1 
ATOM   4135 N N   . GLY B 1 265 ? -19.032 31.644  17.016  1.00 24.42  ? 264 GLY A N   1 
ATOM   4136 C CA  . GLY B 1 265 ? -20.134 30.818  17.458  1.00 31.16  ? 264 GLY A CA  1 
ATOM   4137 C C   . GLY B 1 265 ? -19.777 29.390  17.797  1.00 32.18  ? 264 GLY A C   1 
ATOM   4138 O O   . GLY B 1 265 ? -20.669 28.593  18.108  1.00 37.44  ? 264 GLY A O   1 
ATOM   4139 N N   . GLY B 1 266 ? -18.495 29.038  17.753  1.00 25.64  ? 265 GLY A N   1 
ATOM   4140 C CA  . GLY B 1 266 ? -18.083 27.673  17.996  1.00 35.38  ? 265 GLY A CA  1 
ATOM   4141 C C   . GLY B 1 266 ? -18.235 26.745  16.814  1.00 37.84  ? 265 GLY A C   1 
ATOM   4142 O O   . GLY B 1 266 ? -18.079 25.530  16.975  1.00 38.66  ? 265 GLY A O   1 
ATOM   4143 N N   . ASN B 1 267 ? -18.538 27.275  15.629  1.00 30.60  ? 266 ASN A N   1 
ATOM   4144 C CA  . ASN B 1 267 ? -18.706 26.449  14.437  1.00 32.98  ? 266 ASN A CA  1 
ATOM   4145 C C   . ASN B 1 267 ? -17.360 26.366  13.725  1.00 32.66  ? 266 ASN A C   1 
ATOM   4146 O O   . ASN B 1 267 ? -17.088 27.057  12.742  1.00 36.50  ? 266 ASN A O   1 
ATOM   4147 C CB  . ASN B 1 267 ? -19.799 27.017  13.544  1.00 33.84  ? 266 ASN A CB  1 
ATOM   4148 C CG  . ASN B 1 267 ? -21.155 27.005  14.218  1.00 37.17  ? 266 ASN A CG  1 
ATOM   4149 O OD1 . ASN B 1 267 ? -21.550 26.005  14.821  1.00 38.99  ? 266 ASN A OD1 1 
ATOM   4150 N ND2 . ASN B 1 267 ? -21.870 28.120  14.135  1.00 39.79  ? 266 ASN A ND2 1 
ATOM   4151 N N   . LEU B 1 268 ? -16.504 25.487  14.243  1.00 27.12  ? 267 LEU A N   1 
ATOM   4152 C CA  . LEU B 1 268 ? -15.126 25.394  13.782  1.00 31.41  ? 267 LEU A CA  1 
ATOM   4153 C C   . LEU B 1 268 ? -14.914 24.346  12.702  1.00 22.87  ? 267 LEU A C   1 
ATOM   4154 O O   . LEU B 1 268 ? -13.818 24.287  12.135  1.00 29.91  ? 267 LEU A O   1 
ATOM   4155 C CB  . LEU B 1 268 ? -14.198 25.094  14.960  1.00 28.84  ? 267 LEU A CB  1 
ATOM   4156 C CG  . LEU B 1 268 ? -14.351 26.053  16.136  1.00 32.00  ? 267 LEU A CG  1 
ATOM   4157 C CD1 . LEU B 1 268 ? -13.324 25.741  17.215  1.00 26.53  ? 267 LEU A CD1 1 
ATOM   4158 C CD2 . LEU B 1 268 ? -14.221 27.489  15.652  1.00 31.57  ? 267 LEU A CD2 1 
ATOM   4159 N N   . GLY B 1 269 ? -15.914 23.519  12.409  1.00 29.32  ? 268 GLY A N   1 
ATOM   4160 C CA  . GLY B 1 269 ? -15.755 22.491  11.398  1.00 33.76  ? 268 GLY A CA  1 
ATOM   4161 C C   . GLY B 1 269 ? -15.908 21.073  11.916  1.00 36.68  ? 268 GLY A C   1 
ATOM   4162 O O   . GLY B 1 269 ? -16.833 20.779  12.677  1.00 37.75  ? 268 GLY A O   1 
ATOM   4163 N N   . CYS B 1 270 ? -15.002 20.181  11.502  1.00 37.90  ? 269 CYS A N   1 
ATOM   4164 C CA  . CYS B 1 270 ? -15.087 18.787  11.927  1.00 33.42  ? 269 CYS A CA  1 
ATOM   4165 C C   . CYS B 1 270 ? -14.910 18.649  13.432  1.00 40.06  ? 269 CYS A C   1 
ATOM   4166 O O   . CYS B 1 270 ? -15.634 17.885  14.081  1.00 42.48  ? 269 CYS A O   1 
ATOM   4167 C CB  . CYS B 1 270 ? -14.036 17.949  11.203  1.00 30.61  ? 269 CYS A CB  1 
ATOM   4168 S SG  . CYS B 1 270 ? -14.221 17.894  9.419   1.00 38.01  ? 269 CYS A SG  1 
ATOM   4169 N N   . LYS B 1 271 ? -13.953 19.382  14.006  1.00 43.79  ? 270 LYS A N   1 
ATOM   4170 C CA  . LYS B 1 271 ? -13.622 19.209  15.415  1.00 37.36  ? 270 LYS A CA  1 
ATOM   4171 C C   . LYS B 1 271 ? -14.793 19.538  16.331  1.00 39.89  ? 270 LYS A C   1 
ATOM   4172 O O   . LYS B 1 271 ? -14.801 19.097  17.485  1.00 40.36  ? 270 LYS A O   1 
ATOM   4173 C CB  . LYS B 1 271 ? -12.405 20.067  15.776  1.00 36.76  ? 270 LYS A CB  1 
ATOM   4174 C CG  . LYS B 1 271 ? -12.737 21.516  16.086  1.00 48.29  ? 270 LYS A CG  1 
ATOM   4175 C CD  . LYS B 1 271 ? -11.653 22.464  15.593  1.00 48.66  ? 270 LYS A CD  1 
ATOM   4176 C CE  . LYS B 1 271 ? -10.282 22.048  16.096  1.00 46.95  ? 270 LYS A CE  1 
ATOM   4177 N NZ  . LYS B 1 271 ? -9.392  23.226  16.262  1.00 40.15  ? 270 LYS A NZ  1 
ATOM   4178 N N   . THR B 1 272 ? -15.782 20.294  15.845  1.00 39.01  ? 271 THR A N   1 
ATOM   4179 C CA  . THR B 1 272 ? -16.992 20.581  16.605  1.00 28.90  ? 271 THR A CA  1 
ATOM   4180 C C   . THR B 1 272 ? -18.252 20.031  15.950  1.00 41.24  ? 271 THR A C   1 
ATOM   4181 O O   . THR B 1 272 ? -19.343 20.205  16.505  1.00 35.58  ? 271 THR A O   1 
ATOM   4182 C CB  . THR B 1 272 ? -17.154 22.095  16.820  1.00 33.69  ? 271 THR A CB  1 
ATOM   4183 O OG1 . THR B 1 272 ? -17.393 22.743  15.562  1.00 38.24  ? 271 THR A OG1 1 
ATOM   4184 C CG2 . THR B 1 272 ? -15.910 22.685  17.472  1.00 31.82  ? 271 THR A CG2 1 
ATOM   4185 N N   . GLY B 1 273 ? -18.140 19.378  14.792  1.00 33.88  ? 272 GLY A N   1 
ATOM   4186 C CA  . GLY B 1 273 ? -19.285 18.792  14.130  1.00 33.00  ? 272 GLY A CA  1 
ATOM   4187 C C   . GLY B 1 273 ? -20.111 19.744  13.295  1.00 39.82  ? 272 GLY A C   1 
ATOM   4188 O O   . GLY B 1 273 ? -21.133 19.325  12.737  1.00 31.53  ? 272 GLY A O   1 
ATOM   4189 N N   . LYS B 1 274 ? -19.709 21.007  13.182  1.00 42.51  ? 273 LYS A N   1 
ATOM   4190 C CA  . LYS B 1 274 ? -20.470 21.964  12.384  1.00 31.54  ? 273 LYS A CA  1 
ATOM   4191 C C   . LYS B 1 274 ? -19.548 23.097  11.969  1.00 35.09  ? 273 LYS A C   1 
ATOM   4192 O O   . LYS B 1 274 ? -18.935 23.744  12.825  1.00 31.89  ? 273 LYS A O   1 
ATOM   4193 C CB  . LYS B 1 274 ? -21.665 22.499  13.169  1.00 32.64  ? 273 LYS A CB  1 
ATOM   4194 C CG  . LYS B 1 274 ? -22.477 23.552  12.434  1.00 24.98  ? 273 LYS A CG  1 
ATOM   4195 C CD  . LYS B 1 274 ? -23.683 23.957  13.264  1.00 38.97  ? 273 LYS A CD  1 
ATOM   4196 C CE  . LYS B 1 274 ? -24.783 24.550  12.407  1.00 42.31  ? 273 LYS A CE  1 
ATOM   4197 N NZ  . LYS B 1 274 ? -25.378 25.749  13.062  1.00 56.88  ? 273 LYS A NZ  1 
ATOM   4198 N N   . GLY B 1 275 ? -19.439 23.322  10.663  1.00 40.22  ? 274 GLY A N   1 
ATOM   4199 C CA  . GLY B 1 275 ? -18.765 24.487  10.125  1.00 30.19  ? 274 GLY A CA  1 
ATOM   4200 C C   . GLY B 1 275 ? -19.556 25.018  8.949   1.00 33.82  ? 274 GLY A C   1 
ATOM   4201 O O   . GLY B 1 275 ? -20.682 25.498  9.117   1.00 31.52  ? 274 GLY A O   1 
ATOM   4202 N N   . PHE B 1 276 ? -18.983 24.936  7.747   1.00 30.55  ? 275 PHE A N   1 
ATOM   4203 C CA  . PHE B 1 276 ? -19.789 25.126  6.550   1.00 35.79  ? 275 PHE A CA  1 
ATOM   4204 C C   . PHE B 1 276 ? -20.691 23.928  6.299   1.00 34.60  ? 275 PHE A C   1 
ATOM   4205 O O   . PHE B 1 276 ? -21.699 24.056  5.596   1.00 37.76  ? 275 PHE A O   1 
ATOM   4206 C CB  . PHE B 1 276 ? -18.886 25.383  5.341   1.00 24.57  ? 275 PHE A CB  1 
ATOM   4207 C CG  . PHE B 1 276 ? -18.137 26.684  5.412   1.00 28.92  ? 275 PHE A CG  1 
ATOM   4208 C CD1 . PHE B 1 276 ? -18.792 27.889  5.196   1.00 25.62  ? 275 PHE A CD1 1 
ATOM   4209 C CD2 . PHE B 1 276 ? -16.782 26.705  5.702   1.00 23.66  ? 275 PHE A CD2 1 
ATOM   4210 C CE1 . PHE B 1 276 ? -18.106 29.091  5.264   1.00 31.13  ? 275 PHE A CE1 1 
ATOM   4211 C CE2 . PHE B 1 276 ? -16.089 27.905  5.770   1.00 25.27  ? 275 PHE A CE2 1 
ATOM   4212 C CZ  . PHE B 1 276 ? -16.752 29.098  5.549   1.00 22.84  ? 275 PHE A CZ  1 
ATOM   4213 N N   . TYR B 1 277 ? -20.355 22.777  6.876   1.00 30.42  ? 276 TYR A N   1 
ATOM   4214 C CA  . TYR B 1 277 ? -21.140 21.559  6.774   1.00 33.40  ? 276 TYR A CA  1 
ATOM   4215 C C   . TYR B 1 277 ? -21.522 21.071  8.164   1.00 38.97  ? 276 TYR A C   1 
ATOM   4216 O O   . TYR B 1 277 ? -20.761 21.227  9.125   1.00 33.38  ? 276 TYR A O   1 
ATOM   4217 C CB  . TYR B 1 277 ? -20.362 20.454  6.054   1.00 34.85  ? 276 TYR A CB  1 
ATOM   4218 C CG  . TYR B 1 277 ? -20.085 20.735  4.599   1.00 33.81  ? 276 TYR A CG  1 
ATOM   4219 C CD1 . TYR B 1 277 ? -21.005 20.382  3.618   1.00 32.81  ? 276 TYR A CD1 1 
ATOM   4220 C CD2 . TYR B 1 277 ? -18.902 21.347  4.204   1.00 32.79  ? 276 TYR A CD2 1 
ATOM   4221 C CE1 . TYR B 1 277 ? -20.755 20.633  2.284   1.00 35.09  ? 276 TYR A CE1 1 
ATOM   4222 C CE2 . TYR B 1 277 ? -18.642 21.604  2.870   1.00 30.38  ? 276 TYR A CE2 1 
ATOM   4223 C CZ  . TYR B 1 277 ? -19.571 21.243  1.914   1.00 33.10  ? 276 TYR A CZ  1 
ATOM   4224 O OH  . TYR B 1 277 ? -19.320 21.494  0.585   1.00 39.25  ? 276 TYR A OH  1 
ATOM   4225 N N   . VAL B 1 278 ? -22.711 20.486  8.266   1.00 39.04  ? 277 VAL A N   1 
ATOM   4226 C CA  . VAL B 1 278 ? -23.098 19.724  9.446   1.00 34.06  ? 277 VAL A CA  1 
ATOM   4227 C C   . VAL B 1 278 ? -22.698 18.275  9.213   1.00 39.30  ? 277 VAL A C   1 
ATOM   4228 O O   . VAL B 1 278 ? -23.003 17.700  8.162   1.00 37.92  ? 277 VAL A O   1 
ATOM   4229 C CB  . VAL B 1 278 ? -24.605 19.844  9.720   1.00 35.84  ? 277 VAL A CB  1 
ATOM   4230 C CG1 . VAL B 1 278 ? -25.002 18.920  10.862  1.00 33.02  ? 277 VAL A CG1 1 
ATOM   4231 C CG2 . VAL B 1 278 ? -24.978 21.283  10.037  1.00 43.57  ? 277 VAL A CG2 1 
ATOM   4232 N N   . TYR B 1 279 ? -22.010 17.685  10.186  1.00 45.92  ? 278 TYR A N   1 
ATOM   4233 C CA  . TYR B 1 279 ? -21.494 16.322  10.072  1.00 43.79  ? 278 TYR A CA  1 
ATOM   4234 C C   . TYR B 1 279 ? -22.404 15.399  10.875  1.00 44.75  ? 278 TYR A C   1 
ATOM   4235 O O   . TYR B 1 279 ? -22.323 15.340  12.104  1.00 51.08  ? 278 TYR A O   1 
ATOM   4236 C CB  . TYR B 1 279 ? -20.045 16.269  10.540  1.00 36.07  ? 278 TYR A CB  1 
ATOM   4237 C CG  . TYR B 1 279 ? -19.149 17.101  9.658   1.00 40.58  ? 278 TYR A CG  1 
ATOM   4238 C CD1 . TYR B 1 279 ? -18.936 18.451  9.921   1.00 42.27  ? 278 TYR A CD1 1 
ATOM   4239 C CD2 . TYR B 1 279 ? -18.545 16.548  8.540   1.00 42.99  ? 278 TYR A CD2 1 
ATOM   4240 C CE1 . TYR B 1 279 ? -18.129 19.218  9.100   1.00 40.10  ? 278 TYR A CE1 1 
ATOM   4241 C CE2 . TYR B 1 279 ? -17.741 17.302  7.717   1.00 34.41  ? 278 TYR A CE2 1 
ATOM   4242 C CZ  . TYR B 1 279 ? -17.535 18.633  7.999   1.00 43.59  ? 278 TYR A CZ  1 
ATOM   4243 O OH  . TYR B 1 279 ? -16.731 19.372  7.164   1.00 37.67  ? 278 TYR A OH  1 
ATOM   4244 N N   . ASN B 1 280 ? -23.243 14.677  10.140  1.00 52.13  ? 279 ASN A N   1 
ATOM   4245 C CA  . ASN B 1 280 ? -24.275 13.828  10.776  1.00 54.60  ? 279 ASN A CA  1 
ATOM   4246 C C   . ASN B 1 280 ? -23.709 12.508  11.311  1.00 66.05  ? 279 ASN A C   1 
ATOM   4247 O O   . ASN B 1 280 ? -22.603 12.119  10.897  1.00 51.24  ? 279 ASN A O   1 
ATOM   4248 C CB  . ASN B 1 280 ? -25.421 13.596  9.794   1.00 57.65  ? 279 ASN A CB  1 
ATOM   4249 C CG  . ASN B 1 280 ? -25.626 14.735  8.819   1.00 54.51  ? 279 ASN A CG  1 
ATOM   4250 O OD1 . ASN B 1 280 ? -25.126 14.695  7.699   1.00 53.10  ? 279 ASN A OD1 1 
ATOM   4251 N ND2 . ASN B 1 280 ? -26.376 15.744  9.227   1.00 37.57  ? 279 ASN A ND2 1 
ATOM   4252 N N   . ALA B 1 281 ? -24.476 11.837  12.179  1.00 69.03  ? 280 ALA A N   1 
ATOM   4253 C CA  . ALA B 1 281 ? -24.046 10.569  12.816  1.00 64.17  ? 280 ALA A CA  1 
ATOM   4254 C C   . ALA B 1 281 ? -23.690 9.491   11.791  1.00 69.40  ? 280 ALA A C   1 
ATOM   4255 O O   . ALA B 1 281 ? -22.864 8.631   12.128  1.00 66.93  ? 280 ALA A O   1 
ATOM   4256 C CB  . ALA B 1 281 ? -25.147 10.098  13.722  1.00 73.08  ? 280 ALA A CB  1 
ATOM   4257 N N   . ASP B 1 282 ? -24.320 9.507   10.623  1.00 64.35  ? 281 ASP A N   1 
ATOM   4258 C CA  . ASP B 1 282 ? -23.974 8.553   9.547   1.00 56.38  ? 281 ASP A CA  1 
ATOM   4259 C C   . ASP B 1 282 ? -22.562 8.849   9.050   1.00 67.18  ? 281 ASP A C   1 
ATOM   4260 O O   . ASP B 1 282 ? -21.596 8.642   9.791   1.00 77.65  ? 281 ASP A O   1 
ATOM   4261 C CB  . ASP B 1 282 ? -24.959 8.666   8.388   1.00 55.42  ? 281 ASP A CB  1 
ATOM   4262 C CG  . ASP B 1 282 ? -25.834 9.907   8.415   1.00 69.27  ? 281 ASP A CG  1 
ATOM   4263 O OD1 . ASP B 1 282 ? -26.341 10.258  9.497   1.00 73.54  ? 281 ASP A OD1 1 
ATOM   4264 O OD2 . ASP B 1 282 ? -26.026 10.498  7.344   1.00 76.84  ? 281 ASP A OD2 1 
ATOM   4265 N N   . ARG B 1 283 ? -22.445 9.280   7.805   1.00 73.88  ? 282 ARG A N   1 
ATOM   4266 C CA  . ARG B 1 283 ? -21.120 9.674   7.272   1.00 78.71  ? 282 ARG A CA  1 
ATOM   4267 C C   . ARG B 1 283 ? -21.337 10.868  6.355   1.00 59.74  ? 282 ARG A C   1 
ATOM   4268 O O   . ARG B 1 283 ? -20.365 11.547  6.035   1.00 73.96  ? 282 ARG A O   1 
ATOM   4269 C CB  . ARG B 1 283 ? -20.489 8.536   6.473   1.00 92.02  ? 282 ARG A CB  1 
ATOM   4270 C CG  . ARG B 1 283 ? -19.835 7.448   7.312   1.00 99.57  ? 282 ARG A CG  1 
ATOM   4271 C CD  . ARG B 1 283 ? -20.208 6.063   6.812   1.00 96.28  ? 282 ARG A CD  1 
ATOM   4272 N NE  . ARG B 1 283 ? -20.134 5.051   7.854   1.00 82.22  ? 282 ARG A NE  1 
ATOM   4273 C CZ  . ARG B 1 283 ? -21.176 4.374   8.319   1.00 89.99  ? 282 ARG A CZ  1 
ATOM   4274 N NH1 . ARG B 1 283 ? -22.392 4.879   8.224   1.00 85.29  ? 282 ARG A NH1 1 
ATOM   4275 N NH2 . ARG B 1 283 ? -20.997 3.191   8.880   1.00 95.43  ? 282 ARG A NH2 1 
ATOM   4276 N N   . THR B 1 284 ? -22.582 11.089  5.958   1.00 54.77  ? 283 THR A N   1 
ATOM   4277 C CA  . THR B 1 284 ? -22.871 12.223  5.099   1.00 60.16  ? 283 THR A CA  1 
ATOM   4278 C C   . THR B 1 284 ? -22.569 13.533  5.821   1.00 57.32  ? 283 THR A C   1 
ATOM   4279 O O   . THR B 1 284 ? -22.503 13.601  7.053   1.00 42.71  ? 283 THR A O   1 
ATOM   4280 C CB  . THR B 1 284 ? -24.335 12.209  4.656   1.00 62.34  ? 283 THR A CB  1 
ATOM   4281 O OG1 . THR B 1 284 ? -25.183 12.206  5.811   1.00 61.64  ? 283 THR A OG1 1 
ATOM   4282 C CG2 . THR B 1 284 ? -24.628 10.975  3.815   1.00 59.06  ? 283 THR A CG2 1 
ATOM   4283 N N   . LYS B 1 285 ? -22.371 14.583  5.030   1.00 51.13  ? 284 LYS A N   1 
ATOM   4284 C CA  . LYS B 1 285 ? -22.227 15.935  5.544   1.00 48.08  ? 284 LYS A CA  1 
ATOM   4285 C C   . LYS B 1 285 ? -23.151 16.851  4.755   1.00 37.75  ? 284 LYS A C   1 
ATOM   4286 O O   . LYS B 1 285 ? -23.271 16.726  3.532   1.00 43.31  ? 284 LYS A O   1 
ATOM   4287 C CB  . LYS B 1 285 ? -20.759 16.411  5.482   1.00 41.30  ? 284 LYS A CB  1 
ATOM   4288 C CG  . LYS B 1 285 ? -20.271 16.878  4.124   1.00 37.41  ? 284 LYS A CG  1 
ATOM   4289 C CD  . LYS B 1 285 ? -18.790 17.222  4.165   1.00 32.53  ? 284 LYS A CD  1 
ATOM   4290 C CE  . LYS B 1 285 ? -18.177 17.235  2.769   1.00 43.03  ? 284 LYS A CE  1 
ATOM   4291 N NZ  . LYS B 1 285 ? -18.595 16.060  1.951   1.00 33.73  ? 284 LYS A NZ  1 
ATOM   4292 N N   . THR B 1 286 ? -23.823 17.754  5.466   1.00 33.49  ? 285 THR A N   1 
ATOM   4293 C CA  . THR B 1 286 ? -24.878 18.586  4.898   1.00 37.87  ? 285 THR A CA  1 
ATOM   4294 C C   . THR B 1 286 ? -24.479 20.053  4.968   1.00 34.57  ? 285 THR A C   1 
ATOM   4295 O O   . THR B 1 286 ? -24.201 20.563  6.068   1.00 28.93  ? 285 THR A O   1 
ATOM   4296 C CB  . THR B 1 286 ? -26.200 18.362  5.640   1.00 38.28  ? 285 THR A CB  1 
ATOM   4297 O OG1 . THR B 1 286 ? -26.546 16.972  5.597   1.00 42.72  ? 285 THR A OG1 1 
ATOM   4298 C CG2 . THR B 1 286 ? -27.317 19.179  5.007   1.00 28.60  ? 285 THR A CG2 1 
ATOM   4299 N N   . PRO B 1 287 ? -24.439 20.769  3.847   1.00 40.43  ? 286 PRO A N   1 
ATOM   4300 C CA  . PRO B 1 287 ? -24.079 22.189  3.899   1.00 34.52  ? 286 PRO A CA  1 
ATOM   4301 C C   . PRO B 1 287 ? -25.132 22.996  4.642   1.00 38.83  ? 286 PRO A C   1 
ATOM   4302 O O   . PRO B 1 287 ? -26.335 22.764  4.506   1.00 40.46  ? 286 PRO A O   1 
ATOM   4303 C CB  . PRO B 1 287 ? -23.990 22.592  2.423   1.00 33.87  ? 286 PRO A CB  1 
ATOM   4304 C CG  . PRO B 1 287 ? -24.762 21.556  1.685   1.00 31.07  ? 286 PRO A CG  1 
ATOM   4305 C CD  . PRO B 1 287 ? -24.622 20.288  2.468   1.00 33.32  ? 286 PRO A CD  1 
ATOM   4306 N N   . VAL B 1 288 ? -24.664 23.961  5.431   1.00 26.74  ? 287 VAL A N   1 
ATOM   4307 C CA  . VAL B 1 288 ? -25.540 24.767  6.274   1.00 32.37  ? 287 VAL A CA  1 
ATOM   4308 C C   . VAL B 1 288 ? -26.380 25.718  5.424   1.00 41.73  ? 287 VAL A C   1 
ATOM   4309 O O   . VAL B 1 288 ? -27.241 26.431  5.952   1.00 39.00  ? 287 VAL A O   1 
ATOM   4310 C CB  . VAL B 1 288 ? -24.735 25.540  7.341   1.00 34.55  ? 287 VAL A CB  1 
ATOM   4311 C CG1 . VAL B 1 288 ? -23.807 24.605  8.103   1.00 35.93  ? 287 VAL A CG1 1 
ATOM   4312 C CG2 . VAL B 1 288 ? -23.948 26.686  6.718   1.00 30.62  ? 287 VAL A CG2 1 
ATOM   4313 N N   . ASP B 1 289 ? -26.135 25.738  4.110   1.00 40.45  ? 288 ASP A N   1 
ATOM   4314 C CA  . ASP B 1 289 ? -26.945 26.518  3.167   1.00 35.28  ? 288 ASP A CA  1 
ATOM   4315 C C   . ASP B 1 289 ? -28.423 26.239  3.355   1.00 39.56  ? 288 ASP A C   1 
ATOM   4316 O O   . ASP B 1 289 ? -28.963 25.358  2.689   1.00 38.53  ? 288 ASP A O   1 
ATOM   4317 C CB  . ASP B 1 289 ? -26.575 26.200  1.718   1.00 37.74  ? 288 ASP A CB  1 
ATOM   4318 C CG  . ASP B 1 289 ? -25.496 27.098  1.181   1.00 36.28  ? 288 ASP A CG  1 
ATOM   4319 O OD1 . ASP B 1 289 ? -25.759 28.301  1.030   1.00 40.49  ? 288 ASP A OD1 1 
ATOM   4320 O OD2 . ASP B 1 289 ? -24.409 26.605  0.862   1.00 44.97  ? 288 ASP A OD2 1 
ATOM   4321 N N   . MET C 1 2   ? 33.492  57.982  -31.081 1.00 53.19  ? 1   MET B N   1 
ATOM   4322 C CA  . MET C 1 2   ? 32.165  57.386  -31.188 1.00 48.09  ? 1   MET B CA  1 
ATOM   4323 C C   . MET C 1 2   ? 31.117  58.428  -31.582 1.00 51.95  ? 1   MET B C   1 
ATOM   4324 O O   . MET C 1 2   ? 31.196  59.590  -31.180 1.00 58.59  ? 1   MET B O   1 
ATOM   4325 C CB  . MET C 1 2   ? 31.774  56.714  -29.866 1.00 49.11  ? 1   MET B CB  1 
ATOM   4326 C CG  . MET C 1 2   ? 30.333  56.207  -29.812 1.00 55.05  ? 1   MET B CG  1 
ATOM   4327 S SD  . MET C 1 2   ? 30.032  54.909  -28.590 1.00 78.79  ? 1   MET B SD  1 
ATOM   4328 C CE  . MET C 1 2   ? 31.528  54.983  -27.605 1.00 43.56  ? 1   MET B CE  1 
ATOM   4329 N N   . LYS C 1 3   ? 30.144  58.000  -32.384 1.00 52.72  ? 2   LYS B N   1 
ATOM   4330 C CA  . LYS C 1 3   ? 29.017  58.832  -32.789 1.00 51.79  ? 2   LYS B CA  1 
ATOM   4331 C C   . LYS C 1 3   ? 27.774  58.389  -32.028 1.00 55.23  ? 2   LYS B C   1 
ATOM   4332 O O   . LYS C 1 3   ? 27.452  57.196  -31.996 1.00 56.05  ? 2   LYS B O   1 
ATOM   4333 C CB  . LYS C 1 3   ? 28.785  58.735  -34.299 1.00 59.89  ? 2   LYS B CB  1 
ATOM   4334 C CG  . LYS C 1 3   ? 27.576  59.519  -34.816 1.00 66.19  ? 2   LYS B CG  1 
ATOM   4335 C CD  . LYS C 1 3   ? 27.579  60.975  -34.353 1.00 62.58  ? 2   LYS B CD  1 
ATOM   4336 C CE  . LYS C 1 3   ? 28.028  61.913  -35.469 1.00 69.80  ? 2   LYS B CE  1 
ATOM   4337 N NZ  . LYS C 1 3   ? 27.831  63.350  -35.120 1.00 67.67  ? 2   LYS B NZ  1 
ATOM   4338 N N   . ILE C 1 4   ? 27.081  59.348  -31.415 1.00 49.72  ? 3   ILE B N   1 
ATOM   4339 C CA  . ILE C 1 4   ? 25.937  59.076  -30.553 1.00 43.38  ? 3   ILE B CA  1 
ATOM   4340 C C   . ILE C 1 4   ? 24.759  59.914  -31.023 1.00 48.42  ? 3   ILE B C   1 
ATOM   4341 O O   . ILE C 1 4   ? 24.916  61.098  -31.338 1.00 50.90  ? 3   ILE B O   1 
ATOM   4342 C CB  . ILE C 1 4   ? 26.258  59.376  -29.072 1.00 41.10  ? 3   ILE B CB  1 
ATOM   4343 C CG1 . ILE C 1 4   ? 27.292  58.386  -28.543 1.00 41.15  ? 3   ILE B CG1 1 
ATOM   4344 C CG2 . ILE C 1 4   ? 24.998  59.334  -28.218 1.00 37.40  ? 3   ILE B CG2 1 
ATOM   4345 C CD1 . ILE C 1 4   ? 28.617  59.026  -28.198 1.00 48.23  ? 3   ILE B CD1 1 
ATOM   4346 N N   . GLY C 1 5   ? 23.579  59.300  -31.069 1.00 49.97  ? 4   GLY B N   1 
ATOM   4347 C CA  . GLY C 1 5   ? 22.378  60.013  -31.448 1.00 40.37  ? 4   GLY B CA  1 
ATOM   4348 C C   . GLY C 1 5   ? 21.391  60.148  -30.310 1.00 38.33  ? 4   GLY B C   1 
ATOM   4349 O O   . GLY C 1 5   ? 20.914  59.147  -29.770 1.00 43.81  ? 4   GLY B O   1 
ATOM   4350 N N   . VAL C 1 6   ? 21.073  61.383  -29.940 1.00 35.28  ? 5   VAL B N   1 
ATOM   4351 C CA  . VAL C 1 6   ? 20.151  61.670  -28.850 1.00 33.29  ? 5   VAL B CA  1 
ATOM   4352 C C   . VAL C 1 6   ? 18.812  62.069  -29.449 1.00 46.52  ? 5   VAL B C   1 
ATOM   4353 O O   . VAL C 1 6   ? 18.738  63.001  -30.259 1.00 46.55  ? 5   VAL B O   1 
ATOM   4354 C CB  . VAL C 1 6   ? 20.698  62.770  -27.928 1.00 30.96  ? 5   VAL B CB  1 
ATOM   4355 C CG1 . VAL C 1 6   ? 19.723  63.039  -26.795 1.00 29.30  ? 5   VAL B CG1 1 
ATOM   4356 C CG2 . VAL C 1 6   ? 22.061  62.364  -27.385 1.00 25.35  ? 5   VAL B CG2 1 
ATOM   4357 N N   . ILE C 1 7   ? 17.752  61.372  -29.049 1.00 43.40  ? 6   ILE B N   1 
ATOM   4358 C CA  . ILE C 1 7   ? 16.411  61.586  -29.585 1.00 44.24  ? 6   ILE B CA  1 
ATOM   4359 C C   . ILE C 1 7   ? 15.617  62.328  -28.519 1.00 44.09  ? 6   ILE B C   1 
ATOM   4360 O O   . ILE C 1 7   ? 15.247  61.751  -27.489 1.00 53.72  ? 6   ILE B O   1 
ATOM   4361 C CB  . ILE C 1 7   ? 15.725  60.270  -29.989 1.00 46.50  ? 6   ILE B CB  1 
ATOM   4362 C CG1 . ILE C 1 7   ? 16.213  59.769  -31.357 1.00 37.57  ? 6   ILE B CG1 1 
ATOM   4363 C CG2 . ILE C 1 7   ? 14.211  60.449  -30.048 1.00 49.61  ? 6   ILE B CG2 1 
ATOM   4364 C CD1 . ILE C 1 7   ? 17.700  59.549  -31.488 1.00 32.84  ? 6   ILE B CD1 1 
ATOM   4365 N N   . GLY C 1 8   ? 15.362  63.611  -28.761 1.00 45.18  ? 7   GLY B N   1 
ATOM   4366 C CA  . GLY C 1 8   ? 14.759  64.477  -27.769 1.00 43.03  ? 7   GLY B CA  1 
ATOM   4367 C C   . GLY C 1 8   ? 15.679  65.642  -27.480 1.00 54.82  ? 7   GLY B C   1 
ATOM   4368 O O   . GLY C 1 8   ? 16.896  65.458  -27.380 1.00 57.96  ? 7   GLY B O   1 
ATOM   4369 N N   . ALA C 1 9   ? 15.124  66.850  -27.364 1.00 54.45  ? 8   ALA B N   1 
ATOM   4370 C CA  . ALA C 1 9   ? 15.937  68.038  -27.137 1.00 46.21  ? 8   ALA B CA  1 
ATOM   4371 C C   . ALA C 1 9   ? 15.450  68.840  -25.937 1.00 47.26  ? 8   ALA B C   1 
ATOM   4372 O O   . ALA C 1 9   ? 15.707  70.045  -25.860 1.00 57.05  ? 8   ALA B O   1 
ATOM   4373 C CB  . ALA C 1 9   ? 15.975  68.919  -28.386 1.00 42.78  ? 8   ALA B CB  1 
ATOM   4374 N N   . GLY C 1 10  ? 14.757  68.199  -25.003 1.00 45.21  ? 9   GLY B N   1 
ATOM   4375 C CA  . GLY C 1 10  ? 14.328  68.849  -23.784 1.00 45.84  ? 9   GLY B CA  1 
ATOM   4376 C C   . GLY C 1 10  ? 15.456  68.946  -22.777 1.00 51.43  ? 9   GLY B C   1 
ATOM   4377 O O   . GLY C 1 10  ? 16.641  68.885  -23.116 1.00 45.52  ? 9   GLY B O   1 
ATOM   4378 N N   . THR C 1 11  ? 15.072  69.085  -21.505 1.00 43.19  ? 10  THR B N   1 
ATOM   4379 C CA  . THR C 1 11  ? 16.065  69.239  -20.447 1.00 46.99  ? 10  THR B CA  1 
ATOM   4380 C C   . THR C 1 11  ? 17.031  68.059  -20.409 1.00 51.48  ? 10  THR B C   1 
ATOM   4381 O O   . THR C 1 11  ? 18.222  68.233  -20.126 1.00 54.58  ? 10  THR B O   1 
ATOM   4382 C CB  . THR C 1 11  ? 15.374  69.403  -19.093 1.00 48.72  ? 10  THR B CB  1 
ATOM   4383 O OG1 . THR C 1 11  ? 14.365  68.397  -18.944 1.00 61.82  ? 10  THR B OG1 1 
ATOM   4384 C CG2 . THR C 1 11  ? 14.725  70.773  -18.988 1.00 47.92  ? 10  THR B CG2 1 
ATOM   4385 N N   . MET C 1 12  ? 16.545  66.854  -20.702 1.00 42.27  ? 11  MET B N   1 
ATOM   4386 C CA  . MET C 1 12  ? 17.403  65.681  -20.591 1.00 42.35  ? 11  MET B CA  1 
ATOM   4387 C C   . MET C 1 12  ? 18.091  65.315  -21.900 1.00 36.87  ? 11  MET B C   1 
ATOM   4388 O O   . MET C 1 12  ? 19.237  64.855  -21.880 1.00 34.75  ? 11  MET B O   1 
ATOM   4389 C CB  . MET C 1 12  ? 16.605  64.488  -20.072 1.00 42.78  ? 11  MET B CB  1 
ATOM   4390 C CG  . MET C 1 12  ? 16.164  64.652  -18.641 1.00 51.18  ? 11  MET B CG  1 
ATOM   4391 S SD  . MET C 1 12  ? 17.554  64.478  -17.500 1.00 57.01  ? 11  MET B SD  1 
ATOM   4392 C CE  . MET C 1 12  ? 18.439  63.098  -18.227 1.00 37.75  ? 11  MET B CE  1 
ATOM   4393 N N   . GLY C 1 13  ? 17.421  65.490  -23.039 1.00 36.75  ? 12  GLY B N   1 
ATOM   4394 C CA  . GLY C 1 13  ? 18.114  65.339  -24.308 1.00 39.63  ? 12  GLY B CA  1 
ATOM   4395 C C   . GLY C 1 13  ? 19.305  66.272  -24.418 1.00 45.92  ? 12  GLY B C   1 
ATOM   4396 O O   . GLY C 1 13  ? 20.349  65.904  -24.965 1.00 35.26  ? 12  GLY B O   1 
ATOM   4397 N N   . GLN C 1 14  ? 19.170  67.488  -23.879 1.00 42.37  ? 13  GLN B N   1 
ATOM   4398 C CA  . GLN C 1 14  ? 20.280  68.435  -23.857 1.00 41.53  ? 13  GLN B CA  1 
ATOM   4399 C C   . GLN C 1 14  ? 21.401  67.951  -22.944 1.00 40.38  ? 13  GLN B C   1 
ATOM   4400 O O   . GLN C 1 14  ? 22.578  67.958  -23.327 1.00 33.69  ? 13  GLN B O   1 
ATOM   4401 C CB  . GLN C 1 14  ? 19.781  69.806  -23.400 1.00 48.67  ? 13  GLN B CB  1 
ATOM   4402 C CG  . GLN C 1 14  ? 19.035  70.614  -24.451 1.00 40.74  ? 13  GLN B CG  1 
ATOM   4403 C CD  . GLN C 1 14  ? 18.125  71.658  -23.827 1.00 51.25  ? 13  GLN B CD  1 
ATOM   4404 O OE1 . GLN C 1 14  ? 18.359  72.116  -22.706 1.00 55.01  ? 13  GLN B OE1 1 
ATOM   4405 N NE2 . GLN C 1 14  ? 17.075  72.033  -24.548 1.00 54.35  ? 13  GLN B NE2 1 
ATOM   4406 N N   . GLY C 1 15  ? 21.054  67.538  -21.725 1.00 31.98  ? 14  GLY B N   1 
ATOM   4407 C CA  . GLY C 1 15  ? 22.074  67.102  -20.787 1.00 35.28  ? 14  GLY B CA  1 
ATOM   4408 C C   . GLY C 1 15  ? 22.793  65.845  -21.237 1.00 32.78  ? 14  GLY B C   1 
ATOM   4409 O O   . GLY C 1 15  ? 24.005  65.709  -21.041 1.00 28.81  ? 14  GLY B O   1 
ATOM   4410 N N   . ILE C 1 16  ? 22.059  64.900  -21.831 1.00 29.29  ? 15  ILE B N   1 
ATOM   4411 C CA  . ILE C 1 16  ? 22.698  63.687  -22.334 1.00 29.62  ? 15  ILE B CA  1 
ATOM   4412 C C   . ILE C 1 16  ? 23.662  64.029  -23.462 1.00 28.88  ? 15  ILE B C   1 
ATOM   4413 O O   . ILE C 1 16  ? 24.764  63.474  -23.548 1.00 31.76  ? 15  ILE B O   1 
ATOM   4414 C CB  . ILE C 1 16  ? 21.634  62.663  -22.771 1.00 32.27  ? 15  ILE B CB  1 
ATOM   4415 C CG1 . ILE C 1 16  ? 20.810  62.210  -21.560 1.00 33.57  ? 15  ILE B CG1 1 
ATOM   4416 C CG2 . ILE C 1 16  ? 22.284  61.467  -23.455 1.00 23.21  ? 15  ILE B CG2 1 
ATOM   4417 C CD1 . ILE C 1 16  ? 19.592  61.374  -21.918 1.00 34.54  ? 15  ILE B CD1 1 
ATOM   4418 N N   . ALA C 1 17  ? 23.271  64.965  -24.332 1.00 33.37  ? 16  ALA B N   1 
ATOM   4419 C CA  . ALA C 1 17  ? 24.172  65.428  -25.383 1.00 35.28  ? 16  ALA B CA  1 
ATOM   4420 C C   . ALA C 1 17  ? 25.447  66.017  -24.790 1.00 31.01  ? 16  ALA B C   1 
ATOM   4421 O O   . ALA C 1 17  ? 26.559  65.691  -25.227 1.00 27.40  ? 16  ALA B O   1 
ATOM   4422 C CB  . ALA C 1 17  ? 23.460  66.454  -26.264 1.00 35.50  ? 16  ALA B CB  1 
ATOM   4423 N N   . LYS C 1 18  ? 25.301  66.891  -23.789 1.00 26.82  ? 17  LYS B N   1 
ATOM   4424 C CA  . LYS C 1 18  ? 26.465  67.465  -23.121 1.00 25.42  ? 17  LYS B CA  1 
ATOM   4425 C C   . LYS C 1 18  ? 27.331  66.381  -22.497 1.00 33.81  ? 17  LYS B C   1 
ATOM   4426 O O   . LYS C 1 18  ? 28.565  66.429  -22.590 1.00 29.98  ? 17  LYS B O   1 
ATOM   4427 C CB  . LYS C 1 18  ? 26.021  68.455  -22.043 1.00 27.90  ? 17  LYS B CB  1 
ATOM   4428 C CG  . LYS C 1 18  ? 25.543  69.797  -22.562 1.00 36.44  ? 17  LYS B CG  1 
ATOM   4429 C CD  . LYS C 1 18  ? 24.350  70.298  -21.744 1.00 39.51  ? 17  LYS B CD  1 
ATOM   4430 C CE  . LYS C 1 18  ? 24.780  71.198  -20.600 1.00 35.63  ? 17  LYS B CE  1 
ATOM   4431 N NZ  . LYS C 1 18  ? 23.610  71.678  -19.816 1.00 39.87  ? 17  LYS B NZ  1 
ATOM   4432 N N   . ALA C 1 19  ? 26.698  65.397  -21.848 1.00 26.68  ? 18  ALA B N   1 
ATOM   4433 C CA  . ALA C 1 19  ? 27.441  64.343  -21.167 1.00 23.96  ? 18  ALA B CA  1 
ATOM   4434 C C   . ALA C 1 19  ? 28.366  63.599  -22.119 1.00 32.32  ? 18  ALA B C   1 
ATOM   4435 O O   . ALA C 1 19  ? 29.467  63.197  -21.726 1.00 29.20  ? 18  ALA B O   1 
ATOM   4436 C CB  . ALA C 1 19  ? 26.472  63.367  -20.499 1.00 24.63  ? 18  ALA B CB  1 
ATOM   4437 N N   . PHE C 1 20  ? 27.942  63.412  -23.371 1.00 31.44  ? 19  PHE B N   1 
ATOM   4438 C CA  . PHE C 1 20  ? 28.789  62.741  -24.350 1.00 34.57  ? 19  PHE B CA  1 
ATOM   4439 C C   . PHE C 1 20  ? 29.772  63.709  -24.998 1.00 38.34  ? 19  PHE B C   1 
ATOM   4440 O O   . PHE C 1 20  ? 30.946  63.370  -25.187 1.00 37.14  ? 19  PHE B O   1 
ATOM   4441 C CB  . PHE C 1 20  ? 27.923  62.076  -25.416 1.00 35.61  ? 19  PHE B CB  1 
ATOM   4442 C CG  . PHE C 1 20  ? 27.322  60.775  -24.980 1.00 30.86  ? 19  PHE B CG  1 
ATOM   4443 C CD1 . PHE C 1 20  ? 28.118  59.666  -24.763 1.00 33.66  ? 19  PHE B CD1 1 
ATOM   4444 C CD2 . PHE C 1 20  ? 25.959  60.667  -24.771 1.00 27.59  ? 19  PHE B CD2 1 
ATOM   4445 C CE1 . PHE C 1 20  ? 27.563  58.464  -24.361 1.00 29.27  ? 19  PHE B CE1 1 
ATOM   4446 C CE2 . PHE C 1 20  ? 25.399  59.471  -24.365 1.00 29.95  ? 19  PHE B CE2 1 
ATOM   4447 C CZ  . PHE C 1 20  ? 26.203  58.368  -24.163 1.00 28.75  ? 19  PHE B CZ  1 
ATOM   4448 N N   . ALA C 1 21  ? 29.317  64.918  -25.335 1.00 35.48  ? 20  ALA B N   1 
ATOM   4449 C CA  . ALA C 1 21  ? 30.166  65.862  -26.052 1.00 35.80  ? 20  ALA B CA  1 
ATOM   4450 C C   . ALA C 1 21  ? 31.278  66.438  -25.183 1.00 41.24  ? 20  ALA B C   1 
ATOM   4451 O O   . ALA C 1 21  ? 32.285  66.905  -25.726 1.00 31.04  ? 20  ALA B O   1 
ATOM   4452 C CB  . ALA C 1 21  ? 29.320  66.998  -26.627 1.00 31.20  ? 20  ALA B CB  1 
ATOM   4453 N N   . GLN C 1 22  ? 31.128  66.431  -23.858 1.00 29.56  ? 21  GLN B N   1 
ATOM   4454 C CA  . GLN C 1 22  ? 32.178  66.974  -23.002 1.00 34.64  ? 21  GLN B CA  1 
ATOM   4455 C C   . GLN C 1 22  ? 33.345  66.012  -22.826 1.00 37.77  ? 21  GLN B C   1 
ATOM   4456 O O   . GLN C 1 22  ? 34.338  66.372  -22.181 1.00 42.52  ? 21  GLN B O   1 
ATOM   4457 C CB  . GLN C 1 22  ? 31.607  67.370  -21.632 1.00 33.96  ? 21  GLN B CB  1 
ATOM   4458 C CG  . GLN C 1 22  ? 31.154  66.211  -20.754 1.00 33.67  ? 21  GLN B CG  1 
ATOM   4459 C CD  . GLN C 1 22  ? 30.459  66.673  -19.481 1.00 34.44  ? 21  GLN B CD  1 
ATOM   4460 O OE1 . GLN C 1 22  ? 30.232  67.870  -19.274 1.00 35.21  ? 21  GLN B OE1 1 
ATOM   4461 N NE2 . GLN C 1 22  ? 30.109  65.721  -18.624 1.00 26.70  ? 21  GLN B NE2 1 
ATOM   4462 N N   . VAL C 1 23  ? 33.245  64.806  -23.377 1.00 45.34  ? 22  VAL B N   1 
ATOM   4463 C CA  . VAL C 1 23  ? 34.326  63.832  -23.366 1.00 46.36  ? 22  VAL B CA  1 
ATOM   4464 C C   . VAL C 1 23  ? 34.918  63.797  -24.761 1.00 47.03  ? 22  VAL B C   1 
ATOM   4465 O O   . VAL C 1 23  ? 34.184  63.727  -25.755 1.00 49.27  ? 22  VAL B O   1 
ATOM   4466 C CB  . VAL C 1 23  ? 33.829  62.443  -22.932 1.00 39.50  ? 22  VAL B CB  1 
ATOM   4467 C CG1 . VAL C 1 23  ? 35.001  61.483  -22.741 1.00 37.95  ? 22  VAL B CG1 1 
ATOM   4468 C CG2 . VAL C 1 23  ? 33.014  62.560  -21.657 1.00 36.86  ? 22  VAL B CG2 1 
ATOM   4469 N N   . GLU C 1 24  ? 36.241  63.871  -24.836 1.00 52.27  ? 23  GLU B N   1 
ATOM   4470 C CA  . GLU C 1 24  ? 36.898  64.023  -26.125 1.00 57.56  ? 23  GLU B CA  1 
ATOM   4471 C C   . GLU C 1 24  ? 36.614  62.847  -27.051 1.00 59.24  ? 23  GLU B C   1 
ATOM   4472 O O   . GLU C 1 24  ? 36.447  61.706  -26.611 1.00 63.64  ? 23  GLU B O   1 
ATOM   4473 C CB  . GLU C 1 24  ? 38.408  64.193  -25.937 1.00 57.14  ? 23  GLU B CB  1 
ATOM   4474 C CG  . GLU C 1 24  ? 39.276  62.901  -25.970 1.00 73.61  ? 23  GLU B CG  1 
ATOM   4475 C CD  . GLU C 1 24  ? 39.017  61.891  -24.844 1.00 83.08  ? 23  GLU B CD  1 
ATOM   4476 O OE1 . GLU C 1 24  ? 39.935  61.085  -24.590 1.00 79.44  ? 23  GLU B OE1 1 
ATOM   4477 O OE2 . GLU C 1 24  ? 37.964  61.912  -24.172 1.00 76.43  ? 23  GLU B OE2 1 
ATOM   4478 N N   . GLY C 1 25  ? 36.554  63.137  -28.349 1.00 53.46  ? 24  GLY B N   1 
ATOM   4479 C CA  . GLY C 1 25  ? 36.408  62.109  -29.357 1.00 53.39  ? 24  GLY B CA  1 
ATOM   4480 C C   . GLY C 1 25  ? 35.005  61.591  -29.575 1.00 62.30  ? 24  GLY B C   1 
ATOM   4481 O O   . GLY C 1 25  ? 34.834  60.619  -30.321 1.00 68.14  ? 24  GLY B O   1 
ATOM   4482 N N   . ASN C 1 26  ? 33.996  62.191  -28.949 1.00 59.70  ? 25  ASN B N   1 
ATOM   4483 C CA  . ASN C 1 26  ? 32.605  61.833  -29.186 1.00 50.26  ? 25  ASN B CA  1 
ATOM   4484 C C   . ASN C 1 26  ? 31.925  62.898  -30.036 1.00 49.82  ? 25  ASN B C   1 
ATOM   4485 O O   . ASN C 1 26  ? 32.332  64.063  -30.060 1.00 56.98  ? 25  ASN B O   1 
ATOM   4486 C CB  . ASN C 1 26  ? 31.838  61.651  -27.870 1.00 38.35  ? 25  ASN B CB  1 
ATOM   4487 C CG  . ASN C 1 26  ? 32.331  60.463  -27.066 1.00 46.65  ? 25  ASN B CG  1 
ATOM   4488 O OD1 . ASN C 1 26  ? 32.528  59.373  -27.605 1.00 51.43  ? 25  ASN B OD1 1 
ATOM   4489 N ND2 . ASN C 1 26  ? 32.518  60.664  -25.766 1.00 47.86  ? 25  ASN B ND2 1 
ATOM   4490 N N   . THR C 1 27  ? 30.878  62.478  -30.741 1.00 41.98  ? 26  THR B N   1 
ATOM   4491 C CA  . THR C 1 27  ? 30.077  63.372  -31.564 1.00 52.89  ? 26  THR B CA  1 
ATOM   4492 C C   . THR C 1 27  ? 28.609  63.019  -31.374 1.00 48.15  ? 26  THR B C   1 
ATOM   4493 O O   . THR C 1 27  ? 28.251  61.839  -31.320 1.00 48.88  ? 26  THR B O   1 
ATOM   4494 C CB  . THR C 1 27  ? 30.475  63.281  -33.045 1.00 54.13  ? 26  THR B CB  1 
ATOM   4495 O OG1 . THR C 1 27  ? 30.810  61.926  -33.372 1.00 54.56  ? 26  THR B OG1 1 
ATOM   4496 C CG2 . THR C 1 27  ? 31.680  64.170  -33.323 1.00 42.28  ? 26  THR B CG2 1 
ATOM   4497 N N   . VAL C 1 28  ? 27.766  64.043  -31.261 1.00 38.95  ? 27  VAL B N   1 
ATOM   4498 C CA  . VAL C 1 28  ? 26.375  63.881  -30.860 1.00 44.03  ? 27  VAL B CA  1 
ATOM   4499 C C   . VAL C 1 28  ? 25.474  64.475  -31.932 1.00 52.30  ? 27  VAL B C   1 
ATOM   4500 O O   . VAL C 1 28  ? 25.796  65.509  -32.527 1.00 53.93  ? 27  VAL B O   1 
ATOM   4501 C CB  . VAL C 1 28  ? 26.100  64.538  -29.490 1.00 44.95  ? 27  VAL B CB  1 
ATOM   4502 C CG1 . VAL C 1 28  ? 24.641  64.375  -29.093 1.00 42.94  ? 27  VAL B CG1 1 
ATOM   4503 C CG2 . VAL C 1 28  ? 27.014  63.948  -28.423 1.00 35.24  ? 27  VAL B CG2 1 
ATOM   4504 N N   . ALA C 1 29  ? 24.343  63.813  -32.174 1.00 51.17  ? 28  ALA B N   1 
ATOM   4505 C CA  . ALA C 1 29  ? 23.303  64.293  -33.076 1.00 48.78  ? 28  ALA B CA  1 
ATOM   4506 C C   . ALA C 1 29  ? 22.045  64.545  -32.254 1.00 54.23  ? 28  ALA B C   1 
ATOM   4507 O O   . ALA C 1 29  ? 21.393  63.596  -31.803 1.00 55.55  ? 28  ALA B O   1 
ATOM   4508 C CB  . ALA C 1 29  ? 23.036  63.285  -34.194 1.00 59.39  ? 28  ALA B CB  1 
ATOM   4509 N N   . LEU C 1 30  ? 21.708  65.815  -32.053 1.00 52.91  ? 29  LEU B N   1 
ATOM   4510 C CA  . LEU C 1 30  ? 20.505  66.187  -31.325 1.00 50.91  ? 29  LEU B CA  1 
ATOM   4511 C C   . LEU C 1 30  ? 19.303  66.205  -32.262 1.00 64.59  ? 29  LEU B C   1 
ATOM   4512 O O   . LEU C 1 30  ? 19.413  66.609  -33.423 1.00 68.87  ? 29  LEU B O   1 
ATOM   4513 C CB  . LEU C 1 30  ? 20.680  67.553  -30.664 1.00 42.44  ? 29  LEU B CB  1 
ATOM   4514 C CG  . LEU C 1 30  ? 19.800  67.813  -29.445 1.00 46.28  ? 29  LEU B CG  1 
ATOM   4515 C CD1 . LEU C 1 30  ? 20.061  66.770  -28.376 1.00 42.49  ? 29  LEU B CD1 1 
ATOM   4516 C CD2 . LEU C 1 30  ? 20.045  69.210  -28.912 1.00 46.02  ? 29  LEU B CD2 1 
ATOM   4517 N N   . CYS C 1 31  ? 18.152  65.768  -31.749 1.00 61.34  ? 30  CYS B N   1 
ATOM   4518 C CA  . CYS C 1 31  ? 16.944  65.619  -32.548 1.00 51.38  ? 30  CYS B CA  1 
ATOM   4519 C C   . CYS C 1 31  ? 15.726  65.962  -31.701 1.00 61.44  ? 30  CYS B C   1 
ATOM   4520 O O   . CYS C 1 31  ? 15.755  65.835  -30.475 1.00 67.36  ? 30  CYS B O   1 
ATOM   4521 C CB  . CYS C 1 31  ? 16.806  64.194  -33.085 1.00 39.23  ? 30  CYS B CB  1 
ATOM   4522 S SG  . CYS C 1 31  ? 18.271  63.555  -33.929 1.00 57.51  ? 30  CYS B SG  1 
ATOM   4523 N N   . ASP C 1 32  ? 14.654  66.392  -32.363 1.00 57.11  ? 31  ASP B N   1 
ATOM   4524 C CA  . ASP C 1 32  ? 13.391  66.687  -31.686 1.00 55.00  ? 31  ASP B CA  1 
ATOM   4525 C C   . ASP C 1 32  ? 12.264  66.624  -32.712 1.00 67.58  ? 31  ASP B C   1 
ATOM   4526 O O   . ASP C 1 32  ? 12.454  66.157  -33.840 1.00 66.89  ? 31  ASP B O   1 
ATOM   4527 C CB  . ASP C 1 32  ? 13.440  68.047  -30.980 1.00 57.29  ? 31  ASP B CB  1 
ATOM   4528 C CG  . ASP C 1 32  ? 12.675  68.047  -29.665 1.00 67.59  ? 31  ASP B CG  1 
ATOM   4529 O OD1 . ASP C 1 32  ? 12.494  69.127  -29.060 1.00 67.07  ? 31  ASP B OD1 1 
ATOM   4530 O OD2 . ASP C 1 32  ? 12.251  66.957  -29.237 1.00 67.26  ? 31  ASP B OD2 1 
ATOM   4531 N N   . ILE C 1 33  ? 11.080  67.098  -32.318 1.00 71.71  ? 32  ILE B N   1 
ATOM   4532 C CA  . ILE C 1 33  ? 9.941   67.115  -33.233 1.00 79.54  ? 32  ILE B CA  1 
ATOM   4533 C C   . ILE C 1 33  ? 10.116  68.216  -34.273 1.00 79.98  ? 32  ILE B C   1 
ATOM   4534 O O   . ILE C 1 33  ? 10.233  67.951  -35.475 1.00 81.91  ? 32  ILE B O   1 
ATOM   4535 C CB  . ILE C 1 33  ? 8.625   67.279  -32.453 1.00 74.13  ? 32  ILE B CB  1 
ATOM   4536 C CG1 . ILE C 1 33  ? 8.404   66.082  -31.526 1.00 66.53  ? 32  ILE B CG1 1 
ATOM   4537 C CG2 . ILE C 1 33  ? 7.454   67.447  -33.410 1.00 64.13  ? 32  ILE B CG2 1 
ATOM   4538 C CD1 . ILE C 1 33  ? 7.556   66.391  -30.310 1.00 56.20  ? 32  ILE B CD1 1 
ATOM   4539 N N   . LYS C 1 34  ? 10.137  69.467  -33.822 1.00 75.80  ? 33  LYS B N   1 
ATOM   4540 C CA  . LYS C 1 34  ? 10.376  70.606  -34.696 1.00 76.54  ? 33  LYS B CA  1 
ATOM   4541 C C   . LYS C 1 34  ? 11.866  70.917  -34.727 1.00 74.91  ? 33  LYS B C   1 
ATOM   4542 O O   . LYS C 1 34  ? 12.517  70.962  -33.677 1.00 67.33  ? 33  LYS B O   1 
ATOM   4543 C CB  . LYS C 1 34  ? 9.593   71.831  -34.220 1.00 69.86  ? 33  LYS B CB  1 
ATOM   4544 C CG  . LYS C 1 34  ? 8.092   71.741  -34.443 1.00 74.88  ? 33  LYS B CG  1 
ATOM   4545 C CD  . LYS C 1 34  ? 7.502   73.105  -34.779 1.00 75.32  ? 33  LYS B CD  1 
ATOM   4546 C CE  . LYS C 1 34  ? 6.678   73.062  -36.062 1.00 76.05  ? 33  LYS B CE  1 
ATOM   4547 N NZ  . LYS C 1 34  ? 7.523   73.051  -37.292 1.00 62.02  ? 33  LYS B NZ  1 
ATOM   4548 N N   . GLN C 1 35  ? 12.403  71.123  -35.935 1.00 75.35  ? 34  GLN B N   1 
ATOM   4549 C CA  . GLN C 1 35  ? 13.787  71.570  -36.060 1.00 67.78  ? 34  GLN B CA  1 
ATOM   4550 C C   . GLN C 1 35  ? 14.020  72.848  -35.265 1.00 60.41  ? 34  GLN B C   1 
ATOM   4551 O O   . GLN C 1 35  ? 15.098  73.045  -34.693 1.00 56.65  ? 34  GLN B O   1 
ATOM   4552 C CB  . GLN C 1 35  ? 14.140  71.784  -37.529 1.00 53.83  ? 34  GLN B CB  1 
ATOM   4553 C CG  . GLN C 1 35  ? 15.575  72.215  -37.756 1.00 61.65  ? 34  GLN B CG  1 
ATOM   4554 C CD  . GLN C 1 35  ? 16.446  71.087  -38.259 1.00 57.59  ? 34  GLN B CD  1 
ATOM   4555 O OE1 . GLN C 1 35  ? 16.169  70.486  -39.297 1.00 51.27  ? 34  GLN B OE1 1 
ATOM   4556 N NE2 . GLN C 1 35  ? 17.510  70.791  -37.525 1.00 68.85  ? 34  GLN B NE2 1 
ATOM   4557 N N   . GLU C 1 36  ? 13.015  73.724  -35.218 1.00 70.43  ? 35  GLU B N   1 
ATOM   4558 C CA  . GLU C 1 36  ? 13.085  74.906  -34.365 1.00 76.85  ? 35  GLU B CA  1 
ATOM   4559 C C   . GLU C 1 36  ? 13.325  74.523  -32.909 1.00 75.41  ? 35  GLU B C   1 
ATOM   4560 O O   . GLU C 1 36  ? 14.121  75.166  -32.214 1.00 72.33  ? 35  GLU B O   1 
ATOM   4561 C CB  . GLU C 1 36  ? 11.797  75.718  -34.497 1.00 81.12  ? 35  GLU B CB  1 
ATOM   4562 C CG  . GLU C 1 36  ? 11.990  77.224  -34.541 1.00 87.24  ? 35  GLU B CG  1 
ATOM   4563 C CD  . GLU C 1 36  ? 10.758  77.946  -35.056 1.00 96.21  ? 35  GLU B CD  1 
ATOM   4564 O OE1 . GLU C 1 36  ? 10.589  79.143  -34.740 1.00 96.56  ? 35  GLU B OE1 1 
ATOM   4565 O OE2 . GLU C 1 36  ? 9.957   77.311  -35.776 1.00 96.24  ? 35  GLU B OE2 1 
ATOM   4566 N N   . TRP C 1 37  ? 12.647  73.474  -32.431 1.00 78.51  ? 36  TRP B N   1 
ATOM   4567 C CA  . TRP C 1 37  ? 12.857  73.027  -31.057 1.00 80.09  ? 36  TRP B CA  1 
ATOM   4568 C C   . TRP C 1 37  ? 14.195  72.311  -30.911 1.00 70.90  ? 36  TRP B C   1 
ATOM   4569 O O   . TRP C 1 37  ? 14.851  72.417  -29.869 1.00 67.95  ? 36  TRP B O   1 
ATOM   4570 C CB  . TRP C 1 37  ? 11.712  72.116  -30.610 1.00 73.81  ? 36  TRP B CB  1 
ATOM   4571 C CG  . TRP C 1 37  ? 10.347  72.728  -30.733 1.00 84.72  ? 36  TRP B CG  1 
ATOM   4572 C CD1 . TRP C 1 37  ? 10.049  74.041  -30.962 1.00 88.21  ? 36  TRP B CD1 1 
ATOM   4573 C CD2 . TRP C 1 37  ? 9.092   72.043  -30.640 1.00 87.47  ? 36  TRP B CD2 1 
ATOM   4574 N NE1 . TRP C 1 37  ? 8.686   74.216  -31.016 1.00 81.32  ? 36  TRP B NE1 1 
ATOM   4575 C CE2 . TRP C 1 37  ? 8.076   73.005  -30.821 1.00 86.08  ? 36  TRP B CE2 1 
ATOM   4576 C CE3 . TRP C 1 37  ? 8.728   70.710  -30.421 1.00 80.32  ? 36  TRP B CE3 1 
ATOM   4577 C CZ2 . TRP C 1 37  ? 6.722   72.676  -30.789 1.00 77.65  ? 36  TRP B CZ2 1 
ATOM   4578 C CZ3 . TRP C 1 37  ? 7.384   70.386  -30.389 1.00 80.49  ? 36  TRP B CZ3 1 
ATOM   4579 C CH2 . TRP C 1 37  ? 6.397   71.365  -30.572 1.00 78.52  ? 36  TRP B CH2 1 
ATOM   4580 N N   . ALA C 1 38  ? 14.612  71.571  -31.943 1.00 58.82  ? 37  ALA B N   1 
ATOM   4581 C CA  . ALA C 1 38  ? 15.932  70.950  -31.916 1.00 58.59  ? 37  ALA B CA  1 
ATOM   4582 C C   . ALA C 1 38  ? 17.032  72.000  -31.995 1.00 71.34  ? 37  ALA B C   1 
ATOM   4583 O O   . ALA C 1 38  ? 18.093  71.847  -31.377 1.00 67.49  ? 37  ALA B O   1 
ATOM   4584 C CB  . ALA C 1 38  ? 16.065  69.947  -33.058 1.00 52.35  ? 37  ALA B CB  1 
ATOM   4585 N N   . GLU C 1 39  ? 16.797  73.072  -32.754 1.00 72.27  ? 38  GLU B N   1 
ATOM   4586 C CA  . GLU C 1 39  ? 17.755  74.171  -32.792 1.00 63.19  ? 38  GLU B CA  1 
ATOM   4587 C C   . GLU C 1 39  ? 17.715  74.972  -31.498 1.00 57.72  ? 38  GLU B C   1 
ATOM   4588 O O   . GLU C 1 39  ? 18.749  75.471  -31.040 1.00 64.78  ? 38  GLU B O   1 
ATOM   4589 C CB  . GLU C 1 39  ? 17.476  75.066  -33.997 1.00 73.86  ? 38  GLU B CB  1 
ATOM   4590 C CG  . GLU C 1 39  ? 18.034  74.517  -35.300 1.00 72.74  ? 38  GLU B CG  1 
ATOM   4591 C CD  . GLU C 1 39  ? 17.715  75.401  -36.489 1.00 77.21  ? 38  GLU B CD  1 
ATOM   4592 O OE1 . GLU C 1 39  ? 17.339  76.575  -36.275 1.00 74.22  ? 38  GLU B OE1 1 
ATOM   4593 O OE2 . GLU C 1 39  ? 17.832  74.916  -37.637 1.00 69.39  ? 38  GLU B OE2 1 
ATOM   4594 N N   . ASN C 1 40  ? 16.529  75.104  -30.894 1.00 54.26  ? 39  ASN B N   1 
ATOM   4595 C CA  . ASN C 1 40  ? 16.438  75.685  -29.557 1.00 69.45  ? 39  ASN B CA  1 
ATOM   4596 C C   . ASN C 1 40  ? 17.241  74.877  -28.546 1.00 70.65  ? 39  ASN B C   1 
ATOM   4597 O O   . ASN C 1 40  ? 17.695  75.423  -27.533 1.00 73.27  ? 39  ASN B O   1 
ATOM   4598 C CB  . ASN C 1 40  ? 14.975  75.772  -29.107 1.00 64.53  ? 39  ASN B CB  1 
ATOM   4599 C CG  . ASN C 1 40  ? 14.264  77.011  -29.630 1.00 78.88  ? 39  ASN B CG  1 
ATOM   4600 O OD1 . ASN C 1 40  ? 14.897  77.966  -30.083 1.00 85.14  ? 39  ASN B OD1 1 
ATOM   4601 N ND2 . ASN C 1 40  ? 12.937  77.000  -29.560 1.00 77.83  ? 39  ASN B ND2 1 
ATOM   4602 N N   . GLY C 1 41  ? 17.418  73.580  -28.800 1.00 67.77  ? 40  GLY B N   1 
ATOM   4603 C CA  . GLY C 1 41  ? 18.224  72.728  -27.949 1.00 64.71  ? 40  GLY B CA  1 
ATOM   4604 C C   . GLY C 1 41  ? 19.687  73.119  -27.945 1.00 52.18  ? 40  GLY B C   1 
ATOM   4605 O O   . GLY C 1 41  ? 20.226  73.488  -26.897 1.00 51.64  ? 40  GLY B O   1 
ATOM   4606 N N   . LEU C 1 42  ? 20.339  73.047  -29.111 1.00 52.30  ? 41  LEU B N   1 
ATOM   4607 C CA  . LEU C 1 42  ? 21.726  73.489  -29.215 1.00 50.57  ? 41  LEU B CA  1 
ATOM   4608 C C   . LEU C 1 42  ? 21.883  74.962  -28.872 1.00 55.11  ? 41  LEU B C   1 
ATOM   4609 O O   . LEU C 1 42  ? 22.982  75.388  -28.503 1.00 62.05  ? 41  LEU B O   1 
ATOM   4610 C CB  . LEU C 1 42  ? 22.268  73.222  -30.619 1.00 45.75  ? 41  LEU B CB  1 
ATOM   4611 C CG  . LEU C 1 42  ? 23.784  73.374  -30.769 1.00 54.45  ? 41  LEU B CG  1 
ATOM   4612 C CD1 . LEU C 1 42  ? 24.507  72.516  -29.746 1.00 52.12  ? 41  LEU B CD1 1 
ATOM   4613 C CD2 . LEU C 1 42  ? 24.245  73.038  -32.179 1.00 60.72  ? 41  LEU B CD2 1 
ATOM   4614 N N   . ALA C 1 43  ? 20.809  75.746  -28.977 1.00 57.54  ? 42  ALA B N   1 
ATOM   4615 C CA  . ALA C 1 43  ? 20.863  77.141  -28.555 1.00 58.72  ? 42  ALA B CA  1 
ATOM   4616 C C   . ALA C 1 43  ? 20.967  77.249  -27.039 1.00 56.10  ? 42  ALA B C   1 
ATOM   4617 O O   . ALA C 1 43  ? 21.871  77.912  -26.515 1.00 57.21  ? 42  ALA B O   1 
ATOM   4618 C CB  . ALA C 1 43  ? 19.635  77.892  -29.069 1.00 65.18  ? 42  ALA B CB  1 
ATOM   4619 N N   . LYS C 1 44  ? 20.052  76.599  -26.315 1.00 52.95  ? 43  LYS B N   1 
ATOM   4620 C CA  . LYS C 1 44  ? 20.094  76.640  -24.857 1.00 58.73  ? 43  LYS B CA  1 
ATOM   4621 C C   . LYS C 1 44  ? 21.366  76.011  -24.305 1.00 56.32  ? 43  LYS B C   1 
ATOM   4622 O O   . LYS C 1 44  ? 21.753  76.312  -23.170 1.00 47.78  ? 43  LYS B O   1 
ATOM   4623 C CB  . LYS C 1 44  ? 18.865  75.940  -24.273 1.00 50.51  ? 43  LYS B CB  1 
ATOM   4624 C CG  . LYS C 1 44  ? 18.137  76.746  -23.210 1.00 53.71  ? 43  LYS B CG  1 
ATOM   4625 C CD  . LYS C 1 44  ? 17.973  75.952  -21.923 1.00 52.70  ? 43  LYS B CD  1 
ATOM   4626 C CE  . LYS C 1 44  ? 18.074  76.856  -20.702 1.00 56.29  ? 43  LYS B CE  1 
ATOM   4627 N NZ  . LYS C 1 44  ? 16.854  76.789  -19.845 1.00 68.59  ? 43  LYS B NZ  1 
ATOM   4628 N N   . ILE C 1 45  ? 22.022  75.149  -25.082 1.00 54.45  ? 44  ILE B N   1 
ATOM   4629 C CA  . ILE C 1 45  ? 23.295  74.578  -24.659 1.00 53.70  ? 44  ILE B CA  1 
ATOM   4630 C C   . ILE C 1 45  ? 24.413  75.598  -24.814 1.00 56.11  ? 44  ILE B C   1 
ATOM   4631 O O   . ILE C 1 45  ? 25.184  75.841  -23.878 1.00 52.26  ? 44  ILE B O   1 
ATOM   4632 C CB  . ILE C 1 45  ? 23.589  73.288  -25.446 1.00 46.89  ? 44  ILE B CB  1 
ATOM   4633 C CG1 . ILE C 1 45  ? 22.631  72.176  -25.015 1.00 46.29  ? 44  ILE B CG1 1 
ATOM   4634 C CG2 . ILE C 1 45  ? 25.034  72.857  -25.250 1.00 42.25  ? 44  ILE B CG2 1 
ATOM   4635 C CD1 . ILE C 1 45  ? 22.155  72.307  -23.582 1.00 55.67  ? 44  ILE B CD1 1 
ATOM   4636 N N   . LYS C 1 46  ? 24.515  76.212  -26.000 1.00 50.26  ? 45  LYS B N   1 
ATOM   4637 C CA  . LYS C 1 46  ? 25.460  77.308  -26.194 1.00 51.51  ? 45  LYS B CA  1 
ATOM   4638 C C   . LYS C 1 46  ? 25.247  78.402  -25.157 1.00 49.20  ? 45  LYS B C   1 
ATOM   4639 O O   . LYS C 1 46  ? 26.208  79.012  -24.675 1.00 54.38  ? 45  LYS B O   1 
ATOM   4640 C CB  . LYS C 1 46  ? 25.313  77.895  -27.598 1.00 46.19  ? 45  LYS B CB  1 
ATOM   4641 C CG  . LYS C 1 46  ? 25.741  76.991  -28.734 1.00 52.66  ? 45  LYS B CG  1 
ATOM   4642 C CD  . LYS C 1 46  ? 25.224  77.543  -30.057 1.00 51.95  ? 45  LYS B CD  1 
ATOM   4643 C CE  . LYS C 1 46  ? 25.792  76.792  -31.250 1.00 59.15  ? 45  LYS B CE  1 
ATOM   4644 N NZ  . LYS C 1 46  ? 25.204  77.274  -32.535 1.00 50.00  ? 45  LYS B NZ  1 
ATOM   4645 N N   . LYS C 1 47  ? 23.986  78.658  -24.803 1.00 52.19  ? 46  LYS B N   1 
ATOM   4646 C CA  . LYS C 1 47  ? 23.667  79.715  -23.849 1.00 52.59  ? 46  LYS B CA  1 
ATOM   4647 C C   . LYS C 1 47  ? 24.242  79.406  -22.473 1.00 52.92  ? 46  LYS B C   1 
ATOM   4648 O O   . LYS C 1 47  ? 24.861  80.267  -21.840 1.00 52.96  ? 46  LYS B O   1 
ATOM   4649 C CB  . LYS C 1 47  ? 22.150  79.899  -23.775 1.00 57.33  ? 46  LYS B CB  1 
ATOM   4650 C CG  . LYS C 1 47  ? 21.694  81.258  -23.277 1.00 61.32  ? 46  LYS B CG  1 
ATOM   4651 C CD  . LYS C 1 47  ? 20.219  81.224  -22.880 1.00 64.45  ? 46  LYS B CD  1 
ATOM   4652 C CE  . LYS C 1 47  ? 20.044  80.840  -21.410 1.00 71.54  ? 46  LYS B CE  1 
ATOM   4653 N NZ  . LYS C 1 47  ? 18.792  80.077  -21.124 1.00 60.83  ? 46  LYS B NZ  1 
ATOM   4654 N N   . GLY C 1 48  ? 24.053  78.175  -21.996 1.00 51.11  ? 47  GLY B N   1 
ATOM   4655 C CA  . GLY C 1 48  ? 24.535  77.819  -20.673 1.00 51.11  ? 47  GLY B CA  1 
ATOM   4656 C C   . GLY C 1 48  ? 26.045  77.771  -20.565 1.00 46.28  ? 47  GLY B C   1 
ATOM   4657 O O   . GLY C 1 48  ? 26.604  78.081  -19.510 1.00 50.90  ? 47  GLY B O   1 
ATOM   4658 N N   . TYR C 1 49  ? 26.725  77.384  -21.644 1.00 45.89  ? 48  TYR B N   1 
ATOM   4659 C CA  . TYR C 1 49  ? 28.183  77.364  -21.620 1.00 47.59  ? 48  TYR B CA  1 
ATOM   4660 C C   . TYR C 1 49  ? 28.761  78.772  -21.649 1.00 49.26  ? 48  TYR B C   1 
ATOM   4661 O O   . TYR C 1 49  ? 29.858  78.999  -21.124 1.00 49.57  ? 48  TYR B O   1 
ATOM   4662 C CB  . TYR C 1 49  ? 28.712  76.537  -22.789 1.00 40.31  ? 48  TYR B CB  1 
ATOM   4663 C CG  . TYR C 1 49  ? 28.675  75.058  -22.509 1.00 46.23  ? 48  TYR B CG  1 
ATOM   4664 C CD1 . TYR C 1 49  ? 29.553  74.480  -21.601 1.00 47.60  ? 48  TYR B CD1 1 
ATOM   4665 C CD2 . TYR C 1 49  ? 27.736  74.245  -23.120 1.00 36.77  ? 48  TYR B CD2 1 
ATOM   4666 C CE1 . TYR C 1 49  ? 29.513  73.128  -21.331 1.00 40.53  ? 48  TYR B CE1 1 
ATOM   4667 C CE2 . TYR C 1 49  ? 27.681  72.899  -22.850 1.00 43.60  ? 48  TYR B CE2 1 
ATOM   4668 C CZ  . TYR C 1 49  ? 28.575  72.341  -21.962 1.00 42.76  ? 48  TYR B CZ  1 
ATOM   4669 O OH  . TYR C 1 49  ? 28.523  70.992  -21.700 1.00 39.52  ? 48  TYR B OH  1 
ATOM   4670 N N   . GLU C 1 50  ? 28.038  79.725  -22.243 1.00 45.39  ? 49  GLU B N   1 
ATOM   4671 C CA  . GLU C 1 50  ? 28.467  81.120  -22.206 1.00 44.63  ? 49  GLU B CA  1 
ATOM   4672 C C   . GLU C 1 50  ? 28.512  81.639  -20.774 1.00 41.48  ? 49  GLU B C   1 
ATOM   4673 O O   . GLU C 1 50  ? 29.496  82.260  -20.356 1.00 45.37  ? 49  GLU B O   1 
ATOM   4674 C CB  . GLU C 1 50  ? 27.534  81.979  -23.063 1.00 49.19  ? 49  GLU B CB  1 
ATOM   4675 C CG  . GLU C 1 50  ? 28.022  82.214  -24.488 1.00 56.12  ? 49  GLU B CG  1 
ATOM   4676 C CD  . GLU C 1 50  ? 27.053  83.057  -25.310 1.00 75.07  ? 49  GLU B CD  1 
ATOM   4677 O OE1 . GLU C 1 50  ? 26.608  84.116  -24.814 1.00 75.60  ? 49  GLU B OE1 1 
ATOM   4678 O OE2 . GLU C 1 50  ? 26.736  82.659  -26.453 1.00 69.25  ? 49  GLU B OE2 1 
ATOM   4679 N N   . LYS C 1 51  ? 27.452  81.386  -20.000 1.00 35.79  ? 50  LYS B N   1 
ATOM   4680 C CA  . LYS C 1 51  ? 27.436  81.824  -18.607 1.00 52.97  ? 50  LYS B CA  1 
ATOM   4681 C C   . LYS C 1 51  ? 28.518  81.136  -17.788 1.00 47.00  ? 50  LYS B C   1 
ATOM   4682 O O   . LYS C 1 51  ? 29.087  81.747  -16.876 1.00 54.29  ? 50  LYS B O   1 
ATOM   4683 C CB  . LYS C 1 51  ? 26.064  81.568  -17.981 1.00 58.08  ? 50  LYS B CB  1 
ATOM   4684 C CG  . LYS C 1 51  ? 24.923  81.538  -18.976 1.00 59.84  ? 50  LYS B CG  1 
ATOM   4685 C CD  . LYS C 1 51  ? 23.762  82.401  -18.519 1.00 64.02  ? 50  LYS B CD  1 
ATOM   4686 C CE  . LYS C 1 51  ? 22.630  82.355  -19.532 1.00 63.45  ? 50  LYS B CE  1 
ATOM   4687 N NZ  . LYS C 1 51  ? 21.325  82.782  -18.956 1.00 66.26  ? 50  LYS B NZ  1 
ATOM   4688 N N   . LEU C 1 52  ? 28.815  79.870  -18.090 1.00 43.76  ? 51  LEU B N   1 
ATOM   4689 C CA  . LEU C 1 52  ? 29.862  79.168  -17.355 1.00 50.32  ? 51  LEU B CA  1 
ATOM   4690 C C   . LEU C 1 52  ? 31.241  79.701  -17.718 1.00 51.78  ? 51  LEU B C   1 
ATOM   4691 O O   . LEU C 1 52  ? 32.115  79.815  -16.851 1.00 48.06  ? 51  LEU B O   1 
ATOM   4692 C CB  . LEU C 1 52  ? 29.780  77.666  -17.625 1.00 48.79  ? 51  LEU B CB  1 
ATOM   4693 C CG  . LEU C 1 52  ? 28.738  76.886  -16.823 1.00 57.51  ? 51  LEU B CG  1 
ATOM   4694 C CD1 . LEU C 1 52  ? 28.431  75.568  -17.511 1.00 57.02  ? 51  LEU B CD1 1 
ATOM   4695 C CD2 . LEU C 1 52  ? 29.222  76.654  -15.400 1.00 48.45  ? 51  LEU B CD2 1 
ATOM   4696 N N   . VAL C 1 53  ? 31.454  80.024  -18.997 1.00 46.34  ? 52  VAL B N   1 
ATOM   4697 C CA  . VAL C 1 53  ? 32.729  80.597  -19.418 1.00 45.49  ? 52  VAL B CA  1 
ATOM   4698 C C   . VAL C 1 53  ? 32.924  81.971  -18.791 1.00 41.97  ? 52  VAL B C   1 
ATOM   4699 O O   . VAL C 1 53  ? 34.007  82.289  -18.284 1.00 47.97  ? 52  VAL B O   1 
ATOM   4700 C CB  . VAL C 1 53  ? 32.807  80.654  -20.956 1.00 44.43  ? 52  VAL B CB  1 
ATOM   4701 C CG1 . VAL C 1 53  ? 33.898  81.611  -21.401 1.00 40.42  ? 52  VAL B CG1 1 
ATOM   4702 C CG2 . VAL C 1 53  ? 33.047  79.262  -21.530 1.00 34.07  ? 52  VAL B CG2 1 
ATOM   4703 N N   . ALA C 1 54  ? 31.876  82.799  -18.799 1.00 43.59  ? 53  ALA B N   1 
ATOM   4704 C CA  . ALA C 1 54  ? 31.945  84.101  -18.143 1.00 49.94  ? 53  ALA B CA  1 
ATOM   4705 C C   . ALA C 1 54  ? 32.266  83.957  -16.659 1.00 55.40  ? 53  ALA B C   1 
ATOM   4706 O O   . ALA C 1 54  ? 33.036  84.748  -16.103 1.00 58.43  ? 53  ALA B O   1 
ATOM   4707 C CB  . ALA C 1 54  ? 30.631  84.856  -18.339 1.00 45.19  ? 53  ALA B CB  1 
ATOM   4708 N N   . LYS C 1 55  ? 31.693  82.950  -16.005 1.00 59.56  ? 54  LYS B N   1 
ATOM   4709 C CA  . LYS C 1 55  ? 31.991  82.662  -14.607 1.00 51.97  ? 54  LYS B CA  1 
ATOM   4710 C C   . LYS C 1 55  ? 33.337  81.963  -14.421 1.00 56.81  ? 54  LYS B C   1 
ATOM   4711 O O   . LYS C 1 55  ? 33.651  81.535  -13.304 1.00 60.46  ? 54  LYS B O   1 
ATOM   4712 C CB  . LYS C 1 55  ? 30.871  81.812  -14.000 1.00 52.07  ? 54  LYS B CB  1 
ATOM   4713 C CG  . LYS C 1 55  ? 29.893  82.589  -13.127 1.00 63.84  ? 54  LYS B CG  1 
ATOM   4714 C CD  . LYS C 1 55  ? 29.036  81.653  -12.285 1.00 65.84  ? 54  LYS B CD  1 
ATOM   4715 C CE  . LYS C 1 55  ? 29.891  80.709  -11.453 1.00 63.70  ? 54  LYS B CE  1 
ATOM   4716 N NZ  . LYS C 1 55  ? 29.045  79.734  -10.717 1.00 68.81  ? 54  LYS B NZ  1 
ATOM   4717 N N   . GLY C 1 56  ? 34.131  81.838  -15.484 1.00 51.88  ? 55  GLY B N   1 
ATOM   4718 C CA  . GLY C 1 56  ? 35.433  81.211  -15.411 1.00 48.65  ? 55  GLY B CA  1 
ATOM   4719 C C   . GLY C 1 56  ? 35.428  79.726  -15.130 1.00 49.04  ? 55  GLY B C   1 
ATOM   4720 O O   . GLY C 1 56  ? 36.507  79.145  -14.968 1.00 51.86  ? 55  GLY B O   1 
ATOM   4721 N N   . LYS C 1 57  ? 34.260  79.088  -15.071 1.00 53.14  ? 56  LYS B N   1 
ATOM   4722 C CA  . LYS C 1 57  ? 34.196  77.670  -14.741 1.00 54.46  ? 56  LYS B CA  1 
ATOM   4723 C C   . LYS C 1 57  ? 34.616  76.770  -15.896 1.00 54.97  ? 56  LYS B C   1 
ATOM   4724 O O   . LYS C 1 57  ? 34.991  75.616  -15.660 1.00 54.57  ? 56  LYS B O   1 
ATOM   4725 C CB  . LYS C 1 57  ? 32.781  77.307  -14.292 1.00 53.66  ? 56  LYS B CB  1 
ATOM   4726 C CG  . LYS C 1 57  ? 32.428  77.854  -12.926 1.00 50.94  ? 56  LYS B CG  1 
ATOM   4727 C CD  . LYS C 1 57  ? 33.371  77.305  -11.875 1.00 57.05  ? 56  LYS B CD  1 
ATOM   4728 C CE  . LYS C 1 57  ? 33.421  78.194  -10.651 1.00 63.40  ? 56  LYS B CE  1 
ATOM   4729 N NZ  . LYS C 1 57  ? 33.388  77.375  -9.405  1.00 68.72  ? 56  LYS B NZ  1 
ATOM   4730 N N   . ILE C 1 58  ? 34.555  77.262  -17.130 1.00 47.54  ? 57  ILE B N   1 
ATOM   4731 C CA  . ILE C 1 58  ? 34.967  76.491  -18.300 1.00 44.52  ? 57  ILE B CA  1 
ATOM   4732 C C   . ILE C 1 58  ? 35.912  77.333  -19.149 1.00 47.00  ? 57  ILE B C   1 
ATOM   4733 O O   . ILE C 1 58  ? 35.705  78.547  -19.291 1.00 44.99  ? 57  ILE B O   1 
ATOM   4734 C CB  . ILE C 1 58  ? 33.754  76.033  -19.130 1.00 47.15  ? 57  ILE B CB  1 
ATOM   4735 C CG1 . ILE C 1 58  ? 32.705  75.377  -18.234 1.00 55.70  ? 57  ILE B CG1 1 
ATOM   4736 C CG2 . ILE C 1 58  ? 34.183  75.058  -20.225 1.00 39.53  ? 57  ILE B CG2 1 
ATOM   4737 C CD1 . ILE C 1 58  ? 32.885  73.889  -18.122 1.00 68.84  ? 57  ILE B CD1 1 
ATOM   4738 N N   . PRO C 1 59  ? 36.969  76.745  -19.708 1.00 46.27  ? 58  PRO B N   1 
ATOM   4739 C CA  . PRO C 1 59  ? 37.711  77.429  -20.776 1.00 44.88  ? 58  PRO B CA  1 
ATOM   4740 C C   . PRO C 1 59  ? 36.859  77.531  -22.035 1.00 46.49  ? 58  PRO B C   1 
ATOM   4741 O O   . PRO C 1 59  ? 36.224  76.557  -22.449 1.00 49.20  ? 58  PRO B O   1 
ATOM   4742 C CB  . PRO C 1 59  ? 38.935  76.527  -20.993 1.00 49.57  ? 58  PRO B CB  1 
ATOM   4743 C CG  . PRO C 1 59  ? 39.064  75.758  -19.708 1.00 43.09  ? 58  PRO B CG  1 
ATOM   4744 C CD  . PRO C 1 59  ? 37.647  75.509  -19.283 1.00 43.80  ? 58  PRO B CD  1 
ATOM   4745 N N   . GLN C 1 60  ? 36.843  78.724  -22.639 1.00 47.18  ? 59  GLN B N   1 
ATOM   4746 C CA  . GLN C 1 60  ? 36.055  78.938  -23.850 1.00 46.67  ? 59  GLN B CA  1 
ATOM   4747 C C   . GLN C 1 60  ? 36.455  77.978  -24.962 1.00 53.83  ? 59  GLN B C   1 
ATOM   4748 O O   . GLN C 1 60  ? 35.610  77.583  -25.776 1.00 45.99  ? 59  GLN B O   1 
ATOM   4749 C CB  . GLN C 1 60  ? 36.200  80.383  -24.326 1.00 52.18  ? 59  GLN B CB  1 
ATOM   4750 C CG  . GLN C 1 60  ? 35.340  80.734  -25.536 1.00 55.72  ? 59  GLN B CG  1 
ATOM   4751 C CD  . GLN C 1 60  ? 33.897  81.043  -25.172 1.00 57.84  ? 59  GLN B CD  1 
ATOM   4752 O OE1 . GLN C 1 60  ? 33.602  82.082  -24.576 1.00 59.94  ? 59  GLN B OE1 1 
ATOM   4753 N NE2 . GLN C 1 60  ? 32.990  80.141  -25.531 1.00 56.47  ? 59  GLN B NE2 1 
ATOM   4754 N N   . GLU C 1 61  ? 37.733  77.592  -25.010 1.00 58.16  ? 60  GLU B N   1 
ATOM   4755 C CA  . GLU C 1 61  ? 38.181  76.616  -25.999 1.00 56.57  ? 60  GLU B CA  1 
ATOM   4756 C C   . GLU C 1 61  ? 37.482  75.277  -25.803 1.00 57.13  ? 60  GLU B C   1 
ATOM   4757 O O   . GLU C 1 61  ? 37.105  74.614  -26.779 1.00 51.82  ? 60  GLU B O   1 
ATOM   4758 C CB  . GLU C 1 61  ? 39.696  76.445  -25.907 1.00 58.49  ? 60  GLU B CB  1 
ATOM   4759 C CG  . GLU C 1 61  ? 40.443  77.750  -25.668 1.00 75.52  ? 60  GLU B CG  1 
ATOM   4760 C CD  . GLU C 1 61  ? 41.653  77.917  -26.570 1.00 82.85  ? 60  GLU B CD  1 
ATOM   4761 O OE1 . GLU C 1 61  ? 41.496  77.838  -27.808 1.00 78.28  ? 60  GLU B OE1 1 
ATOM   4762 O OE2 . GLU C 1 61  ? 42.763  78.137  -26.039 1.00 82.52  ? 60  GLU B OE2 1 
ATOM   4763 N N   . LYS C 1 62  ? 37.298  74.864  -24.545 1.00 46.62  ? 61  LYS B N   1 
ATOM   4764 C CA  . LYS C 1 62  ? 36.621  73.602  -24.266 1.00 42.56  ? 61  LYS B CA  1 
ATOM   4765 C C   . LYS C 1 62  ? 35.151  73.670  -24.658 1.00 39.52  ? 61  LYS B C   1 
ATOM   4766 O O   . LYS C 1 62  ? 34.636  72.771  -25.332 1.00 49.01  ? 61  LYS B O   1 
ATOM   4767 C CB  . LYS C 1 62  ? 36.770  73.240  -22.787 1.00 45.55  ? 61  LYS B CB  1 
ATOM   4768 C CG  . LYS C 1 62  ? 36.446  71.783  -22.471 1.00 36.98  ? 61  LYS B CG  1 
ATOM   4769 C CD  . LYS C 1 62  ? 37.112  70.832  -23.459 1.00 47.18  ? 61  LYS B CD  1 
ATOM   4770 C CE  . LYS C 1 62  ? 36.305  69.548  -23.619 1.00 43.79  ? 61  LYS B CE  1 
ATOM   4771 N NZ  . LYS C 1 62  ? 36.304  68.722  -22.379 1.00 47.18  ? 61  LYS B NZ  1 
ATOM   4772 N N   . ALA C 1 63  ? 34.461  74.740  -24.252 1.00 31.09  ? 62  ALA B N   1 
ATOM   4773 C CA  . ALA C 1 63  ? 33.042  74.877  -24.565 1.00 35.95  ? 62  ALA B CA  1 
ATOM   4774 C C   . ALA C 1 63  ? 32.808  74.884  -26.071 1.00 45.59  ? 62  ALA B C   1 
ATOM   4775 O O   . ALA C 1 63  ? 31.936  74.168  -26.578 1.00 42.02  ? 62  ALA B O   1 
ATOM   4776 C CB  . ALA C 1 63  ? 32.484  76.149  -23.927 1.00 39.99  ? 62  ALA B CB  1 
ATOM   4777 N N   . ASP C 1 64  ? 33.583  75.690  -26.804 1.00 47.22  ? 63  ASP B N   1 
ATOM   4778 C CA  . ASP C 1 64  ? 33.453  75.718  -28.258 1.00 48.23  ? 63  ASP B CA  1 
ATOM   4779 C C   . ASP C 1 64  ? 33.724  74.352  -28.864 1.00 43.71  ? 63  ASP B C   1 
ATOM   4780 O O   . ASP C 1 64  ? 33.139  74.001  -29.895 1.00 43.55  ? 63  ASP B O   1 
ATOM   4781 C CB  . ASP C 1 64  ? 34.405  76.754  -28.857 1.00 55.83  ? 63  ASP B CB  1 
ATOM   4782 C CG  . ASP C 1 64  ? 33.892  78.172  -28.714 1.00 65.19  ? 63  ASP B CG  1 
ATOM   4783 O OD1 . ASP C 1 64  ? 34.579  79.104  -29.186 1.00 65.07  ? 63  ASP B OD1 1 
ATOM   4784 O OD2 . ASP C 1 64  ? 32.805  78.358  -28.128 1.00 68.13  ? 63  ASP B OD2 1 
ATOM   4785 N N   . ALA C 1 65  ? 34.601  73.567  -28.237 1.00 42.34  ? 64  ALA B N   1 
ATOM   4786 C CA  . ALA C 1 65  ? 34.911  72.244  -28.762 1.00 43.50  ? 64  ALA B CA  1 
ATOM   4787 C C   . ALA C 1 65  ? 33.751  71.275  -28.552 1.00 44.67  ? 64  ALA B C   1 
ATOM   4788 O O   . ALA C 1 65  ? 33.480  70.430  -29.412 1.00 46.84  ? 64  ALA B O   1 
ATOM   4789 C CB  . ALA C 1 65  ? 36.190  71.711  -28.114 1.00 35.87  ? 64  ALA B CB  1 
ATOM   4790 N N   . ILE C 1 66  ? 33.051  71.376  -27.419 1.00 41.77  ? 65  ILE B N   1 
ATOM   4791 C CA  . ILE C 1 66  ? 31.933  70.464  -27.200 1.00 47.64  ? 65  ILE B CA  1 
ATOM   4792 C C   . ILE C 1 66  ? 30.714  70.902  -28.012 1.00 45.70  ? 65  ILE B C   1 
ATOM   4793 O O   . ILE C 1 66  ? 29.963  70.056  -28.513 1.00 45.13  ? 65  ILE B O   1 
ATOM   4794 C CB  . ILE C 1 66  ? 31.606  70.334  -25.696 1.00 45.05  ? 65  ILE B CB  1 
ATOM   4795 C CG1 . ILE C 1 66  ? 30.842  71.549  -25.177 1.00 47.75  ? 65  ILE B CG1 1 
ATOM   4796 C CG2 . ILE C 1 66  ? 32.868  70.114  -24.871 1.00 42.74  ? 65  ILE B CG2 1 
ATOM   4797 C CD1 . ILE C 1 66  ? 29.359  71.303  -25.087 1.00 46.66  ? 65  ILE B CD1 1 
ATOM   4798 N N   . VAL C 1 67  ? 30.502  72.212  -28.165 1.00 46.20  ? 66  VAL B N   1 
ATOM   4799 C CA  . VAL C 1 67  ? 29.380  72.698  -28.955 1.00 48.16  ? 66  VAL B CA  1 
ATOM   4800 C C   . VAL C 1 67  ? 29.575  72.368  -30.431 1.00 52.54  ? 66  VAL B C   1 
ATOM   4801 O O   . VAL C 1 67  ? 28.592  72.210  -31.166 1.00 54.60  ? 66  VAL B O   1 
ATOM   4802 C CB  . VAL C 1 67  ? 29.197  74.205  -28.675 1.00 38.27  ? 66  VAL B CB  1 
ATOM   4803 C CG1 . VAL C 1 67  ? 28.621  74.942  -29.872 1.00 47.69  ? 66  VAL B CG1 1 
ATOM   4804 C CG2 . VAL C 1 67  ? 28.319  74.404  -27.432 1.00 40.93  ? 66  VAL B CG2 1 
ATOM   4805 N N   . ALA C 1 68  ? 30.825  72.199  -30.872 1.00 45.82  ? 67  ALA B N   1 
ATOM   4806 C CA  . ALA C 1 68  ? 31.120  71.774  -32.235 1.00 44.18  ? 67  ALA B CA  1 
ATOM   4807 C C   . ALA C 1 68  ? 30.864  70.288  -32.471 1.00 55.34  ? 67  ALA B C   1 
ATOM   4808 O O   . ALA C 1 68  ? 30.786  69.868  -33.631 1.00 48.33  ? 67  ALA B O   1 
ATOM   4809 C CB  . ALA C 1 68  ? 32.576  72.099  -32.579 1.00 39.25  ? 67  ALA B CB  1 
ATOM   4810 N N   . ALA C 1 69  ? 30.745  69.485  -31.412 1.00 45.28  ? 68  ALA B N   1 
ATOM   4811 C CA  . ALA C 1 69  ? 30.458  68.062  -31.549 1.00 38.83  ? 68  ALA B CA  1 
ATOM   4812 C C   . ALA C 1 69  ? 28.968  67.752  -31.552 1.00 49.64  ? 68  ALA B C   1 
ATOM   4813 O O   . ALA C 1 69  ? 28.591  66.607  -31.830 1.00 52.71  ? 68  ALA B O   1 
ATOM   4814 C CB  . ALA C 1 69  ? 31.134  67.268  -30.427 1.00 43.34  ? 68  ALA B CB  1 
ATOM   4815 N N   . ILE C 1 70  ? 28.121  68.729  -31.244 1.00 48.13  ? 69  ILE B N   1 
ATOM   4816 C CA  . ILE C 1 70  ? 26.675  68.550  -31.262 1.00 47.83  ? 69  ILE B CA  1 
ATOM   4817 C C   . ILE C 1 70  ? 26.128  69.152  -32.548 1.00 56.16  ? 69  ILE B C   1 
ATOM   4818 O O   . ILE C 1 70  ? 26.204  70.369  -32.763 1.00 60.65  ? 69  ILE B O   1 
ATOM   4819 C CB  . ILE C 1 70  ? 26.005  69.183  -30.036 1.00 46.27  ? 69  ILE B CB  1 
ATOM   4820 C CG1 . ILE C 1 70  ? 26.717  68.741  -28.762 1.00 40.91  ? 69  ILE B CG1 1 
ATOM   4821 C CG2 . ILE C 1 70  ? 24.527  68.808  -30.010 1.00 37.96  ? 69  ILE B CG2 1 
ATOM   4822 C CD1 . ILE C 1 70  ? 26.505  69.684  -27.618 1.00 38.98  ? 69  ILE B CD1 1 
ATOM   4823 N N   . THR C 1 71  ? 25.558  68.288  -33.382 1.00 61.13  ? 70  THR B N   1 
ATOM   4824 C CA  . THR C 1 71  ? 25.026  68.621  -34.694 1.00 55.45  ? 70  THR B CA  1 
ATOM   4825 C C   . THR C 1 71  ? 23.531  68.328  -34.728 1.00 52.76  ? 70  THR B C   1 
ATOM   4826 O O   . THR C 1 71  ? 23.126  67.159  -34.594 1.00 52.39  ? 70  THR B O   1 
ATOM   4827 C CB  . THR C 1 71  ? 25.790  67.843  -35.762 1.00 47.40  ? 70  THR B CB  1 
ATOM   4828 O OG1 . THR C 1 71  ? 25.268  66.516  -35.864 1.00 68.07  ? 70  THR B OG1 1 
ATOM   4829 C CG2 . THR C 1 71  ? 27.319  67.838  -35.440 1.00 61.53  ? 70  THR B CG2 1 
ATOM   4830 N N   . PRO C 1 72  ? 22.653  69.360  -34.813 1.00 62.36  ? 71  PRO B N   1 
ATOM   4831 C CA  . PRO C 1 72  ? 21.214  69.141  -34.729 1.00 66.24  ? 71  PRO B CA  1 
ATOM   4832 C C   . PRO C 1 72  ? 20.631  68.567  -36.026 1.00 72.70  ? 71  PRO B C   1 
ATOM   4833 O O   . PRO C 1 72  ? 20.490  69.294  -36.966 1.00 81.01  ? 71  PRO B O   1 
ATOM   4834 C CB  . PRO C 1 72  ? 20.612  70.534  -34.485 1.00 61.99  ? 71  PRO B CB  1 
ATOM   4835 C CG  . PRO C 1 72  ? 21.789  71.431  -34.230 1.00 61.79  ? 71  PRO B CG  1 
ATOM   4836 C CD  . PRO C 1 72  ? 22.914  70.797  -35.012 1.00 62.93  ? 71  PRO B CD  1 
ATOM   4837 N N   . GLY C 1 73  ? 20.296  67.278  -36.030 1.00 76.83  ? 72  GLY B N   1 
ATOM   4838 C CA  . GLY C 1 73  ? 19.649  66.668  -37.202 1.00 76.67  ? 72  GLY B CA  1 
ATOM   4839 C C   . GLY C 1 73  ? 18.211  67.136  -37.319 1.00 92.14  ? 72  GLY B C   1 
ATOM   4840 O O   . GLY C 1 73  ? 17.846  68.108  -36.636 1.00 93.52  ? 72  GLY B O   1 
ATOM   4841 N N   . LEU C 1 74  ? 17.400  66.464  -38.131 1.00 95.80  ? 73  LEU B N   1 
ATOM   4842 C CA  . LEU C 1 74  ? 16.016  66.951  -38.377 1.00 102.55 ? 73  LEU B CA  1 
ATOM   4843 C C   . LEU C 1 74  ? 15.067  65.986  -37.675 1.00 94.08  ? 73  LEU B C   1 
ATOM   4844 O O   . LEU C 1 74  ? 13.857  66.111  -37.953 1.00 86.50  ? 73  LEU B O   1 
ATOM   4845 C CB  . LEU C 1 74  ? 15.820  67.031  -39.900 1.00 98.48  ? 73  LEU B CB  1 
ATOM   4846 C CG  . LEU C 1 74  ? 15.148  65.857  -40.613 1.00 88.49  ? 73  LEU B CG  1 
ATOM   4847 C CD1 . LEU C 1 74  ? 14.744  66.248  -42.023 1.00 69.97  ? 73  LEU B CD1 1 
ATOM   4848 C CD2 . LEU C 1 74  ? 16.054  64.648  -40.655 1.00 83.83  ? 73  LEU B CD2 1 
ATOM   4849 N N   . LYS C 1 75  ? 15.591  65.193  -36.731 1.00 92.10  ? 74  LYS B N   1 
ATOM   4850 C CA  . LYS C 1 75  ? 14.881  64.082  -36.033 1.00 88.66  ? 74  LYS B CA  1 
ATOM   4851 C C   . LYS C 1 75  ? 15.610  62.844  -36.559 1.00 84.28  ? 74  LYS B C   1 
ATOM   4852 O O   . LYS C 1 75  ? 15.480  61.774  -35.937 1.00 68.32  ? 74  LYS B O   1 
ATOM   4853 C CB  . LYS C 1 75  ? 13.356  64.017  -36.188 1.00 90.65  ? 74  LYS B CB  1 
ATOM   4854 C CG  . LYS C 1 75  ? 12.822  62.884  -37.055 1.00 92.35  ? 74  LYS B CG  1 
ATOM   4855 C CD  . LYS C 1 75  ? 11.648  63.279  -37.915 1.00 84.29  ? 74  LYS B CD  1 
ATOM   4856 C CE  . LYS C 1 75  ? 11.592  62.502  -39.211 1.00 77.95  ? 74  LYS B CE  1 
ATOM   4857 N NZ  . LYS C 1 75  ? 12.175  63.271  -40.334 1.00 75.39  ? 74  LYS B NZ  1 
ATOM   4858 N N   . GLU C 1 76  ? 16.397  63.027  -37.631 1.00 80.07  ? 75  GLU B N   1 
ATOM   4859 C CA  . GLU C 1 76  ? 17.224  61.920  -38.183 1.00 86.32  ? 75  GLU B CA  1 
ATOM   4860 C C   . GLU C 1 76  ? 18.147  62.460  -39.282 1.00 90.61  ? 75  GLU B C   1 
ATOM   4861 O O   . GLU C 1 76  ? 18.769  63.505  -39.027 1.00 80.40  ? 75  GLU B O   1 
ATOM   4862 C CB  . GLU C 1 76  ? 16.357  60.782  -38.724 1.00 83.04  ? 75  GLU B CB  1 
ATOM   4863 C CG  . GLU C 1 76  ? 15.089  61.259  -39.401 1.00 77.02  ? 75  GLU B CG  1 
ATOM   4864 C CD  . GLU C 1 76  ? 15.102  61.141  -40.912 1.00 78.67  ? 75  GLU B CD  1 
ATOM   4865 O OE1 . GLU C 1 76  ? 16.018  60.483  -41.445 1.00 79.33  ? 75  GLU B OE1 1 
ATOM   4866 O OE2 . GLU C 1 76  ? 14.200  61.715  -41.549 1.00 91.61  ? 75  GLU B OE2 1 
ATOM   4867 N N   . ASN C 1 77  ? 18.188  61.804  -40.457 1.00 96.52  ? 76  ASN B N   1 
ATOM   4868 C CA  . ASN C 1 77  ? 19.136  62.170  -41.550 1.00 88.31  ? 76  ASN B CA  1 
ATOM   4869 C C   . ASN C 1 77  ? 20.552  61.996  -41.007 1.00 90.69  ? 76  ASN B C   1 
ATOM   4870 O O   . ASN C 1 77  ? 21.395  61.435  -41.726 1.00 76.21  ? 76  ASN B O   1 
ATOM   4871 C CB  . ASN C 1 77  ? 18.915  63.582  -42.099 1.00 83.39  ? 76  ASN B CB  1 
ATOM   4872 C CG  . ASN C 1 77  ? 18.707  63.616  -43.597 1.00 90.91  ? 76  ASN B CG  1 
ATOM   4873 O OD1 . ASN C 1 77  ? 19.638  63.381  -44.362 1.00 100.62 ? 76  ASN B OD1 1 
ATOM   4874 N ND2 . ASN C 1 77  ? 17.492  63.913  -44.026 1.00 79.83  ? 76  ASN B ND2 1 
ATOM   4875 N N   . LEU C 1 78  ? 20.788  62.476  -39.778 1.00 102.05 ? 77  LEU B N   1 
ATOM   4876 C CA  . LEU C 1 78  ? 22.124  62.350  -39.135 1.00 96.66  ? 77  LEU B CA  1 
ATOM   4877 C C   . LEU C 1 78  ? 22.130  61.079  -38.288 1.00 84.94  ? 77  LEU B C   1 
ATOM   4878 O O   . LEU C 1 78  ? 23.204  60.463  -38.165 1.00 83.79  ? 77  LEU B O   1 
ATOM   4879 C CB  . LEU C 1 78  ? 22.338  63.568  -38.237 1.00 88.18  ? 77  LEU B CB  1 
ATOM   4880 C CG  . LEU C 1 78  ? 23.447  64.521  -38.667 1.00 88.23  ? 77  LEU B CG  1 
ATOM   4881 C CD1 . LEU C 1 78  ? 23.096  65.948  -38.285 1.00 82.83  ? 77  LEU B CD1 1 
ATOM   4882 C CD2 . LEU C 1 78  ? 24.775  64.110  -38.051 1.00 78.37  ? 77  LEU B CD2 1 
ATOM   4883 N N   . CYS C 1 79  ? 20.967  60.691  -37.758 1.00 76.80  ? 78  CYS B N   1 
ATOM   4884 C CA  . CYS C 1 79  ? 20.870  59.476  -36.900 1.00 93.17  ? 78  CYS B CA  1 
ATOM   4885 C C   . CYS C 1 79  ? 20.974  58.209  -37.748 1.00 83.38  ? 78  CYS B C   1 
ATOM   4886 O O   . CYS C 1 79  ? 20.172  57.304  -37.520 1.00 78.46  ? 78  CYS B O   1 
ATOM   4887 C CB  . CYS C 1 79  ? 19.552  59.419  -36.136 1.00 90.50  ? 78  CYS B CB  1 
ATOM   4888 S SG  . CYS C 1 79  ? 19.490  60.510  -34.694 1.00 135.66 ? 78  CYS B SG  1 
ATOM   4889 N N   . ALA C 1 80  ? 21.948  58.130  -38.650 1.00 84.56  ? 79  ALA B N   1 
ATOM   4890 C CA  . ALA C 1 80  ? 22.024  56.973  -39.570 1.00 71.71  ? 79  ALA B CA  1 
ATOM   4891 C C   . ALA C 1 80  ? 23.348  56.229  -39.398 1.00 68.97  ? 79  ALA B C   1 
ATOM   4892 O O   . ALA C 1 80  ? 23.367  55.016  -39.622 1.00 72.48  ? 79  ALA B O   1 
ATOM   4893 C CB  . ALA C 1 80  ? 21.848  57.479  -40.964 1.00 70.66  ? 79  ALA B CB  1 
ATOM   4894 N N   . ASP C 1 81  ? 24.409  56.932  -39.031 1.00 65.16  ? 80  ASP B N   1 
ATOM   4895 C CA  . ASP C 1 81  ? 25.702  56.310  -38.789 1.00 72.28  ? 80  ASP B CA  1 
ATOM   4896 C C   . ASP C 1 81  ? 26.025  56.203  -37.301 1.00 72.13  ? 80  ASP B C   1 
ATOM   4897 O O   . ASP C 1 81  ? 27.083  55.676  -36.940 1.00 66.33  ? 80  ASP B O   1 
ATOM   4898 C CB  . ASP C 1 81  ? 26.795  57.108  -39.524 1.00 78.28  ? 80  ASP B CB  1 
ATOM   4899 C CG  . ASP C 1 81  ? 28.176  56.481  -39.408 1.00 82.30  ? 80  ASP B CG  1 
ATOM   4900 O OD1 . ASP C 1 81  ? 29.169  57.235  -39.322 1.00 84.26  ? 80  ASP B OD1 1 
ATOM   4901 O OD2 . ASP C 1 81  ? 28.271  55.234  -39.412 1.00 84.12  ? 80  ASP B OD2 1 
ATOM   4902 N N   . CYS C 1 82  ? 25.136  56.679  -36.428 1.00 73.79  ? 81  CYS B N   1 
ATOM   4903 C CA  . CYS C 1 82  ? 25.409  56.670  -34.996 1.00 61.40  ? 81  CYS B CA  1 
ATOM   4904 C C   . CYS C 1 82  ? 25.683  55.255  -34.506 1.00 58.66  ? 81  CYS B C   1 
ATOM   4905 O O   . CYS C 1 82  ? 25.023  54.298  -34.916 1.00 64.84  ? 81  CYS B O   1 
ATOM   4906 C CB  . CYS C 1 82  ? 24.231  57.268  -34.225 1.00 64.28  ? 81  CYS B CB  1 
ATOM   4907 S SG  . CYS C 1 82  ? 23.592  58.816  -34.909 1.00 88.60  ? 81  CYS B SG  1 
ATOM   4908 N N   . ASP C 1 83  ? 26.684  55.126  -33.635 1.00 59.45  ? 82  ASP B N   1 
ATOM   4909 C CA  . ASP C 1 83  ? 26.996  53.844  -33.020 1.00 60.65  ? 82  ASP B CA  1 
ATOM   4910 C C   . ASP C 1 83  ? 26.160  53.572  -31.778 1.00 59.56  ? 82  ASP B C   1 
ATOM   4911 O O   . ASP C 1 83  ? 26.196  52.450  -31.259 1.00 60.39  ? 82  ASP B O   1 
ATOM   4912 C CB  . ASP C 1 83  ? 28.483  53.780  -32.662 1.00 66.23  ? 82  ASP B CB  1 
ATOM   4913 C CG  . ASP C 1 83  ? 29.344  54.618  -33.592 1.00 67.71  ? 82  ASP B CG  1 
ATOM   4914 O OD1 . ASP C 1 83  ? 28.919  54.867  -34.741 1.00 58.58  ? 82  ASP B OD1 1 
ATOM   4915 O OD2 . ASP C 1 83  ? 30.447  55.028  -33.169 1.00 67.44  ? 82  ASP B OD2 1 
ATOM   4916 N N   . LEU C 1 84  ? 25.417  54.564  -31.293 1.00 48.42  ? 83  LEU B N   1 
ATOM   4917 C CA  . LEU C 1 84  ? 24.570  54.406  -30.122 1.00 38.61  ? 83  LEU B CA  1 
ATOM   4918 C C   . LEU C 1 84  ? 23.419  55.396  -30.212 1.00 44.89  ? 83  LEU B C   1 
ATOM   4919 O O   . LEU C 1 84  ? 23.608  56.548  -30.613 1.00 47.27  ? 83  LEU B O   1 
ATOM   4920 C CB  . LEU C 1 84  ? 25.355  54.619  -28.821 1.00 43.59  ? 83  LEU B CB  1 
ATOM   4921 C CG  . LEU C 1 84  ? 24.534  54.861  -27.548 1.00 43.00  ? 83  LEU B CG  1 
ATOM   4922 C CD1 . LEU C 1 84  ? 24.003  53.551  -26.980 1.00 37.56  ? 83  LEU B CD1 1 
ATOM   4923 C CD2 . LEU C 1 84  ? 25.348  55.604  -26.503 1.00 36.81  ? 83  LEU B CD2 1 
ATOM   4924 N N   . ILE C 1 85  ? 22.229  54.930  -29.846 1.00 42.20  ? 84  ILE B N   1 
ATOM   4925 C CA  . ILE C 1 85  ? 21.026  55.749  -29.789 1.00 39.08  ? 84  ILE B CA  1 
ATOM   4926 C C   . ILE C 1 85  ? 20.610  55.884  -28.334 1.00 43.84  ? 84  ILE B C   1 
ATOM   4927 O O   . ILE C 1 85  ? 20.503  54.881  -27.619 1.00 38.97  ? 84  ILE B O   1 
ATOM   4928 C CB  . ILE C 1 85  ? 19.890  55.135  -30.624 1.00 47.76  ? 84  ILE B CB  1 
ATOM   4929 C CG1 . ILE C 1 85  ? 20.044  55.541  -32.076 1.00 50.07  ? 84  ILE B CG1 1 
ATOM   4930 C CG2 . ILE C 1 85  ? 18.540  55.624  -30.130 1.00 39.77  ? 84  ILE B CG2 1 
ATOM   4931 C CD1 . ILE C 1 85  ? 20.075  57.017  -32.219 1.00 48.81  ? 84  ILE B CD1 1 
ATOM   4932 N N   . VAL C 1 86  ? 20.380  57.116  -27.892 1.00 39.14  ? 85  VAL B N   1 
ATOM   4933 C CA  . VAL C 1 86  ? 19.777  57.374  -26.592 1.00 37.38  ? 85  VAL B CA  1 
ATOM   4934 C C   . VAL C 1 86  ? 18.542  58.229  -26.832 1.00 42.35  ? 85  VAL B C   1 
ATOM   4935 O O   . VAL C 1 86  ? 18.657  59.414  -27.166 1.00 41.38  ? 85  VAL B O   1 
ATOM   4936 C CB  . VAL C 1 86  ? 20.743  58.064  -25.620 1.00 30.59  ? 85  VAL B CB  1 
ATOM   4937 C CG1 . VAL C 1 86  ? 20.037  58.333  -24.302 1.00 27.74  ? 85  VAL B CG1 1 
ATOM   4938 C CG2 . VAL C 1 86  ? 21.980  57.212  -25.396 1.00 27.36  ? 85  VAL B CG2 1 
ATOM   4939 N N   . GLU C 1 87  ? 17.362  57.635  -26.669 1.00 42.48  ? 86  GLU B N   1 
ATOM   4940 C CA  . GLU C 1 87  ? 16.119  58.381  -26.785 1.00 44.98  ? 86  GLU B CA  1 
ATOM   4941 C C   . GLU C 1 87  ? 15.765  59.015  -25.448 1.00 39.70  ? 86  GLU B C   1 
ATOM   4942 O O   . GLU C 1 87  ? 15.915  58.398  -24.389 1.00 37.69  ? 86  GLU B O   1 
ATOM   4943 C CB  . GLU C 1 87  ? 14.971  57.486  -27.268 1.00 40.33  ? 86  GLU B CB  1 
ATOM   4944 C CG  . GLU C 1 87  ? 14.422  56.517  -26.228 1.00 46.30  ? 86  GLU B CG  1 
ATOM   4945 C CD  . GLU C 1 87  ? 13.301  57.108  -25.384 1.00 56.70  ? 86  GLU B CD  1 
ATOM   4946 O OE1 . GLU C 1 87  ? 12.657  58.083  -25.831 1.00 54.19  ? 86  GLU B OE1 1 
ATOM   4947 O OE2 . GLU C 1 87  ? 13.073  56.595  -24.268 1.00 51.04  ? 86  GLU B OE2 1 
ATOM   4948 N N   . ALA C 1 88  ? 15.303  60.258  -25.509 1.00 43.95  ? 87  ALA B N   1 
ATOM   4949 C CA  . ALA C 1 88  ? 14.833  60.997  -24.344 1.00 47.92  ? 87  ALA B CA  1 
ATOM   4950 C C   . ALA C 1 88  ? 13.570  61.762  -24.721 1.00 53.70  ? 87  ALA B C   1 
ATOM   4951 O O   . ALA C 1 88  ? 13.431  62.957  -24.458 1.00 44.33  ? 87  ALA B O   1 
ATOM   4952 C CB  . ALA C 1 88  ? 15.918  61.931  -23.812 1.00 46.42  ? 87  ALA B CB  1 
ATOM   4953 N N   . ALA C 1 89  ? 12.638  61.062  -25.365 1.00 54.79  ? 88  ALA B N   1 
ATOM   4954 C CA  . ALA C 1 89  ? 11.395  61.652  -25.836 1.00 52.27  ? 88  ALA B CA  1 
ATOM   4955 C C   . ALA C 1 89  ? 10.354  61.623  -24.718 1.00 62.05  ? 88  ALA B C   1 
ATOM   4956 O O   . ALA C 1 89  ? 10.669  61.380  -23.551 1.00 60.40  ? 88  ALA B O   1 
ATOM   4957 C CB  . ALA C 1 89  ? 10.912  60.925  -27.088 1.00 51.72  ? 88  ALA B CB  1 
ATOM   4958 N N   . PHE C 1 90  ? 9.093   61.865  -25.071 1.00 64.19  ? 89  PHE B N   1 
ATOM   4959 C CA  . PHE C 1 90  ? 8.029   61.958  -24.079 1.00 68.01  ? 89  PHE B CA  1 
ATOM   4960 C C   . PHE C 1 90  ? 7.788   60.604  -23.418 1.00 65.13  ? 89  PHE B C   1 
ATOM   4961 O O   . PHE C 1 90  ? 7.716   59.574  -24.096 1.00 67.66  ? 89  PHE B O   1 
ATOM   4962 C CB  . PHE C 1 90  ? 6.750   62.472  -24.743 1.00 72.19  ? 89  PHE B CB  1 
ATOM   4963 C CG  . PHE C 1 90  ? 5.573   62.568  -23.814 1.00 83.73  ? 89  PHE B CG  1 
ATOM   4964 C CD1 . PHE C 1 90  ? 5.716   63.079  -22.533 1.00 86.54  ? 89  PHE B CD1 1 
ATOM   4965 C CD2 . PHE C 1 90  ? 4.318   62.148  -24.226 1.00 90.03  ? 89  PHE B CD2 1 
ATOM   4966 C CE1 . PHE C 1 90  ? 4.629   63.165  -21.679 1.00 81.42  ? 89  PHE B CE1 1 
ATOM   4967 C CE2 . PHE C 1 90  ? 3.228   62.233  -23.379 1.00 87.76  ? 89  PHE B CE2 1 
ATOM   4968 C CZ  . PHE C 1 90  ? 3.384   62.742  -22.103 1.00 81.52  ? 89  PHE B CZ  1 
ATOM   4969 N N   . GLU C 1 91  ? 7.618   60.610  -22.091 1.00 60.79  ? 90  GLU B N   1 
ATOM   4970 C CA  . GLU C 1 91  ? 7.407   59.359  -21.314 1.00 61.89  ? 90  GLU B CA  1 
ATOM   4971 C C   . GLU C 1 91  ? 6.028   58.768  -21.621 1.00 65.07  ? 90  GLU B C   1 
ATOM   4972 O O   . GLU C 1 91  ? 5.165   58.753  -20.729 1.00 62.21  ? 90  GLU B O   1 
ATOM   4973 C CB  . GLU C 1 91  ? 7.605   59.603  -19.815 1.00 55.97  ? 90  GLU B CB  1 
ATOM   4974 C CG  . GLU C 1 91  ? 7.599   58.343  -18.958 1.00 52.56  ? 90  GLU B CG  1 
ATOM   4975 C CD  . GLU C 1 91  ? 8.915   57.596  -18.821 1.00 57.21  ? 90  GLU B CD  1 
ATOM   4976 O OE1 . GLU C 1 91  ? 9.853   57.909  -19.574 1.00 51.66  ? 90  GLU B OE1 1 
ATOM   4977 O OE2 . GLU C 1 91  ? 8.995   56.698  -17.960 1.00 42.89  ? 90  GLU B OE2 1 
ATOM   4978 N N   . ASP C 1 92  ? 5.832   58.326  -22.854 1.00 68.39  ? 91  ASP B N   1 
ATOM   4979 C CA  . ASP C 1 92  ? 4.577   57.634  -23.225 1.00 70.75  ? 91  ASP B CA  1 
ATOM   4980 C C   . ASP C 1 92  ? 5.002   56.362  -23.953 1.00 74.26  ? 91  ASP B C   1 
ATOM   4981 O O   . ASP C 1 92  ? 6.001   56.418  -24.678 1.00 69.23  ? 91  ASP B O   1 
ATOM   4982 C CB  . ASP C 1 92  ? 3.634   58.526  -24.029 1.00 77.45  ? 91  ASP B CB  1 
ATOM   4983 C CG  . ASP C 1 92  ? 2.363   57.814  -24.455 1.00 77.96  ? 91  ASP B CG  1 
ATOM   4984 O OD1 . ASP C 1 92  ? 2.166   57.646  -25.670 1.00 75.87  ? 91  ASP B OD1 1 
ATOM   4985 O OD2 . ASP C 1 92  ? 1.592   57.422  -23.564 1.00 74.20  ? 91  ASP B OD2 1 
ATOM   4986 N N   . MET C 1 93  ? 4.236   55.286  -23.820 1.00 72.75  ? 92  MET B N   1 
ATOM   4987 C CA  . MET C 1 93  ? 4.665   53.992  -24.341 1.00 73.13  ? 92  MET B CA  1 
ATOM   4988 C C   . MET C 1 93  ? 4.632   53.966  -25.867 1.00 57.97  ? 92  MET B C   1 
ATOM   4989 O O   . MET C 1 93  ? 5.668   53.784  -26.517 1.00 60.05  ? 92  MET B O   1 
ATOM   4990 C CB  . MET C 1 93  ? 3.792   52.883  -23.749 1.00 68.13  ? 92  MET B CB  1 
ATOM   4991 C CG  . MET C 1 93  ? 4.538   51.974  -22.775 1.00 64.32  ? 92  MET B CG  1 
ATOM   4992 S SD  . MET C 1 93  ? 5.945   51.035  -23.415 1.00 66.86  ? 92  MET B SD  1 
ATOM   4993 C CE  . MET C 1 93  ? 5.399   50.618  -25.061 1.00 53.34  ? 92  MET B CE  1 
ATOM   4994 N N   . LYS C 1 94  ? 3.450   54.150  -26.462 1.00 66.72  ? 93  LYS B N   1 
ATOM   4995 C CA  . LYS C 1 94  ? 3.354   54.096  -27.918 1.00 69.28  ? 93  LYS B CA  1 
ATOM   4996 C C   . LYS C 1 94  ? 4.183   55.181  -28.588 1.00 61.62  ? 93  LYS B C   1 
ATOM   4997 O O   . LYS C 1 94  ? 4.542   55.035  -29.762 1.00 61.83  ? 93  LYS B O   1 
ATOM   4998 C CB  . LYS C 1 94  ? 1.895   54.200  -28.368 1.00 68.58  ? 93  LYS B CB  1 
ATOM   4999 C CG  . LYS C 1 94  ? 1.060   55.192  -27.584 1.00 62.92  ? 93  LYS B CG  1 
ATOM   5000 C CD  . LYS C 1 94  ? -0.423  54.938  -27.801 1.00 69.42  ? 93  LYS B CD  1 
ATOM   5001 C CE  . LYS C 1 94  ? -1.223  55.215  -26.538 1.00 74.73  ? 93  LYS B CE  1 
ATOM   5002 N NZ  . LYS C 1 94  ? -1.311  54.017  -25.656 1.00 69.88  ? 93  LYS B NZ  1 
ATOM   5003 N N   . VAL C 1 95  ? 4.498   56.261  -27.868 1.00 69.74  ? 94  VAL B N   1 
ATOM   5004 C CA  . VAL C 1 95  ? 5.422   57.263  -28.389 1.00 66.55  ? 94  VAL B CA  1 
ATOM   5005 C C   . VAL C 1 95  ? 6.793   56.643  -28.630 1.00 63.22  ? 94  VAL B C   1 
ATOM   5006 O O   . VAL C 1 95  ? 7.408   56.848  -29.684 1.00 53.59  ? 94  VAL B O   1 
ATOM   5007 C CB  . VAL C 1 95  ? 5.498   58.464  -27.426 1.00 67.21  ? 94  VAL B CB  1 
ATOM   5008 C CG1 . VAL C 1 95  ? 6.779   59.256  -27.648 1.00 65.47  ? 94  VAL B CG1 1 
ATOM   5009 C CG2 . VAL C 1 95  ? 4.276   59.357  -27.591 1.00 67.76  ? 94  VAL B CG2 1 
ATOM   5010 N N   . LYS C 1 96  ? 7.280   55.853  -27.670 1.00 64.12  ? 95  LYS B N   1 
ATOM   5011 C CA  . LYS C 1 96  ? 8.620   55.282  -27.769 1.00 56.03  ? 95  LYS B CA  1 
ATOM   5012 C C   . LYS C 1 96  ? 8.684   54.112  -28.745 1.00 54.35  ? 95  LYS B C   1 
ATOM   5013 O O   . LYS C 1 96  ? 9.704   53.945  -29.423 1.00 49.86  ? 95  LYS B O   1 
ATOM   5014 C CB  . LYS C 1 96  ? 9.110   54.855  -26.384 1.00 57.69  ? 95  LYS B CB  1 
ATOM   5015 C CG  . LYS C 1 96  ? 9.124   55.987  -25.356 1.00 56.10  ? 95  LYS B CG  1 
ATOM   5016 C CD  . LYS C 1 96  ? 9.983   55.638  -24.150 1.00 59.33  ? 95  LYS B CD  1 
ATOM   5017 C CE  . LYS C 1 96  ? 9.845   56.677  -23.042 1.00 56.62  ? 95  LYS B CE  1 
ATOM   5018 N NZ  . LYS C 1 96  ? 10.692  57.882  -23.272 1.00 56.18  ? 95  LYS B NZ  1 
ATOM   5019 N N   . GLN C 1 97  ? 7.629   53.294  -28.838 1.00 60.68  ? 96  GLN B N   1 
ATOM   5020 C CA  . GLN C 1 97  ? 7.595   52.271  -29.882 1.00 60.87  ? 96  GLN B CA  1 
ATOM   5021 C C   . GLN C 1 97  ? 7.664   52.903  -31.259 1.00 56.82  ? 96  GLN B C   1 
ATOM   5022 O O   . GLN C 1 97  ? 8.493   52.519  -32.091 1.00 58.23  ? 96  GLN B O   1 
ATOM   5023 C CB  . GLN C 1 97  ? 6.330   51.420  -29.798 1.00 61.39  ? 96  GLN B CB  1 
ATOM   5024 C CG  . GLN C 1 97  ? 5.942   50.925  -28.448 1.00 60.63  ? 96  GLN B CG  1 
ATOM   5025 C CD  . GLN C 1 97  ? 5.210   49.599  -28.543 1.00 72.10  ? 96  GLN B CD  1 
ATOM   5026 O OE1 . GLN C 1 97  ? 4.424   49.243  -27.667 1.00 66.61  ? 96  GLN B OE1 1 
ATOM   5027 N NE2 . GLN C 1 97  ? 5.471   48.855  -29.613 1.00 63.49  ? 96  GLN B NE2 1 
ATOM   5028 N N   . THR C 1 98  ? 6.769   53.856  -31.525 1.00 54.46  ? 97  THR B N   1 
ATOM   5029 C CA  . THR C 1 98  ? 6.766   54.531  -32.816 1.00 65.01  ? 97  THR B CA  1 
ATOM   5030 C C   . THR C 1 98  ? 8.143   55.104  -33.129 1.00 57.02  ? 97  THR B C   1 
ATOM   5031 O O   . THR C 1 98  ? 8.718   54.811  -34.182 1.00 52.17  ? 97  THR B O   1 
ATOM   5032 C CB  . THR C 1 98  ? 5.689   55.616  -32.830 1.00 64.48  ? 97  THR B CB  1 
ATOM   5033 O OG1 . THR C 1 98  ? 5.703   56.310  -31.578 1.00 53.65  ? 97  THR B OG1 1 
ATOM   5034 C CG2 . THR C 1 98  ? 4.317   54.986  -33.021 1.00 57.83  ? 97  THR B CG2 1 
ATOM   5035 N N   . THR C 1 99  ? 8.715   55.866  -32.191 1.00 52.08  ? 98  THR B N   1 
ATOM   5036 C CA  . THR C 1 99  ? 10.036  56.458  -32.398 1.00 56.75  ? 98  THR B CA  1 
ATOM   5037 C C   . THR C 1 99  ? 11.079  55.389  -32.710 1.00 53.47  ? 98  THR B C   1 
ATOM   5038 O O   . THR C 1 99  ? 11.758  55.446  -33.742 1.00 52.08  ? 98  THR B O   1 
ATOM   5039 C CB  . THR C 1 99  ? 10.447  57.276  -31.170 1.00 58.00  ? 98  THR B CB  1 
ATOM   5040 O OG1 . THR C 1 99  ? 9.377   58.152  -30.790 1.00 64.20  ? 98  THR B OG1 1 
ATOM   5041 C CG2 . THR C 1 99  ? 11.685  58.103  -31.476 1.00 52.93  ? 98  THR B CG2 1 
ATOM   5042 N N   . PHE C 1 100 ? 11.214  54.393  -31.829 1.00 50.07  ? 99  PHE B N   1 
ATOM   5043 C CA  . PHE C 1 100 ? 12.132  53.294  -32.110 1.00 54.06  ? 99  PHE B CA  1 
ATOM   5044 C C   . PHE C 1 100 ? 11.699  52.516  -33.345 1.00 56.67  ? 99  PHE B C   1 
ATOM   5045 O O   . PHE C 1 100 ? 12.537  51.899  -34.017 1.00 53.48  ? 99  PHE B O   1 
ATOM   5046 C CB  . PHE C 1 100 ? 12.234  52.363  -30.898 1.00 47.47  ? 99  PHE B CB  1 
ATOM   5047 C CG  . PHE C 1 100 ? 13.243  52.804  -29.878 1.00 46.63  ? 99  PHE B CG  1 
ATOM   5048 C CD1 . PHE C 1 100 ? 14.581  52.929  -30.214 1.00 45.95  ? 99  PHE B CD1 1 
ATOM   5049 C CD2 . PHE C 1 100 ? 12.851  53.098  -28.582 1.00 40.54  ? 99  PHE B CD2 1 
ATOM   5050 C CE1 . PHE C 1 100 ? 15.513  53.340  -29.273 1.00 43.77  ? 99  PHE B CE1 1 
ATOM   5051 C CE2 . PHE C 1 100 ? 13.775  53.506  -27.640 1.00 43.03  ? 99  PHE B CE2 1 
ATOM   5052 C CZ  . PHE C 1 100 ? 15.109  53.629  -27.986 1.00 40.41  ? 99  PHE B CZ  1 
ATOM   5053 N N   . GLY C 1 101 ? 10.397  52.537  -33.651 1.00 60.96  ? 100 GLY B N   1 
ATOM   5054 C CA  . GLY C 1 101 ? 9.925   51.950  -34.895 1.00 56.06  ? 100 GLY B CA  1 
ATOM   5055 C C   . GLY C 1 101 ? 10.445  52.690  -36.115 1.00 61.95  ? 100 GLY B C   1 
ATOM   5056 O O   . GLY C 1 101 ? 11.052  52.089  -37.007 1.00 58.77  ? 100 GLY B O   1 
ATOM   5057 N N   . GLU C 1 102 ? 10.224  54.010  -36.173 1.00 57.49  ? 101 GLU B N   1 
ATOM   5058 C CA  . GLU C 1 102 ? 10.797  54.805  -37.255 1.00 61.96  ? 101 GLU B CA  1 
ATOM   5059 C C   . GLU C 1 102 ? 12.320  54.863  -37.202 1.00 62.81  ? 101 GLU B C   1 
ATOM   5060 O O   . GLU C 1 102 ? 12.929  55.397  -38.132 1.00 65.20  ? 101 GLU B O   1 
ATOM   5061 C CB  . GLU C 1 102 ? 10.239  56.236  -37.235 1.00 60.80  ? 101 GLU B CB  1 
ATOM   5062 C CG  . GLU C 1 102 ? 8.818   56.410  -36.707 1.00 52.23  ? 101 GLU B CG  1 
ATOM   5063 C CD  . GLU C 1 102 ? 8.527   57.851  -36.308 1.00 69.25  ? 101 GLU B CD  1 
ATOM   5064 O OE1 . GLU C 1 102 ? 7.693   58.513  -36.964 1.00 74.59  ? 101 GLU B OE1 1 
ATOM   5065 O OE2 . GLU C 1 102 ? 9.142   58.322  -35.328 1.00 70.81  ? 101 GLU B OE2 1 
ATOM   5066 N N   . LEU C 1 103 ? 12.947  54.322  -36.156 1.00 63.25  ? 102 LEU B N   1 
ATOM   5067 C CA  . LEU C 1 103 ? 14.395  54.386  -36.005 1.00 60.85  ? 102 LEU B CA  1 
ATOM   5068 C C   . LEU C 1 103 ? 15.111  53.118  -36.447 1.00 59.22  ? 102 LEU B C   1 
ATOM   5069 O O   . LEU C 1 103 ? 16.278  53.192  -36.845 1.00 49.53  ? 102 LEU B O   1 
ATOM   5070 C CB  . LEU C 1 103 ? 14.764  54.682  -34.548 1.00 64.86  ? 102 LEU B CB  1 
ATOM   5071 C CG  . LEU C 1 103 ? 14.949  56.158  -34.190 1.00 61.88  ? 102 LEU B CG  1 
ATOM   5072 C CD1 . LEU C 1 103 ? 14.741  56.377  -32.697 1.00 58.74  ? 102 LEU B CD1 1 
ATOM   5073 C CD2 . LEU C 1 103 ? 16.317  56.668  -34.628 1.00 49.51  ? 102 LEU B CD2 1 
ATOM   5074 N N   . ASP C 1 104 ? 14.452  51.957  -36.382 1.00 73.60  ? 103 ASP B N   1 
ATOM   5075 C CA  . ASP C 1 104 ? 15.091  50.716  -36.810 1.00 68.59  ? 103 ASP B CA  1 
ATOM   5076 C C   . ASP C 1 104 ? 15.446  50.731  -38.292 1.00 71.29  ? 103 ASP B C   1 
ATOM   5077 O O   . ASP C 1 104 ? 16.334  49.980  -38.714 1.00 64.58  ? 103 ASP B O   1 
ATOM   5078 C CB  . ASP C 1 104 ? 14.188  49.521  -36.505 1.00 67.05  ? 103 ASP B CB  1 
ATOM   5079 C CG  . ASP C 1 104 ? 14.975  48.260  -36.194 1.00 67.85  ? 103 ASP B CG  1 
ATOM   5080 O OD1 . ASP C 1 104 ? 16.196  48.237  -36.461 1.00 60.65  ? 103 ASP B OD1 1 
ATOM   5081 O OD2 . ASP C 1 104 ? 14.371  47.288  -35.695 1.00 70.21  ? 103 ASP B OD2 1 
ATOM   5082 N N   . LYS C 1 105 ? 14.774  51.567  -39.088 1.00 72.10  ? 104 LYS B N   1 
ATOM   5083 C CA  . LYS C 1 105 ? 15.148  51.743  -40.488 1.00 74.40  ? 104 LYS B CA  1 
ATOM   5084 C C   . LYS C 1 105 ? 16.314  52.712  -40.630 1.00 77.63  ? 104 LYS B C   1 
ATOM   5085 O O   . LYS C 1 105 ? 17.268  52.452  -41.371 1.00 77.76  ? 104 LYS B O   1 
ATOM   5086 C CB  . LYS C 1 105 ? 13.954  52.253  -41.296 1.00 68.02  ? 104 LYS B CB  1 
ATOM   5087 C CG  . LYS C 1 105 ? 12.803  51.280  -41.429 1.00 71.34  ? 104 LYS B CG  1 
ATOM   5088 C CD  . LYS C 1 105 ? 11.798  51.784  -42.455 1.00 76.73  ? 104 LYS B CD  1 
ATOM   5089 C CE  . LYS C 1 105 ? 11.834  50.946  -43.727 1.00 72.21  ? 104 LYS B CE  1 
ATOM   5090 N NZ  . LYS C 1 105 ? 10.996  51.534  -44.811 1.00 64.95  ? 104 LYS B NZ  1 
ATOM   5091 N N   . ILE C 1 106 ? 16.121  53.890  -40.043 1.00 68.81  ? 105 ILE B N   1 
ATOM   5092 C CA  . ILE C 1 106 ? 17.088  54.998  -40.268 1.00 66.88  ? 105 ILE B CA  1 
ATOM   5093 C C   . ILE C 1 106 ? 18.500  54.625  -39.848 1.00 65.52  ? 105 ILE B C   1 
ATOM   5094 O O   . ILE C 1 106 ? 19.413  54.892  -40.627 1.00 82.31  ? 105 ILE B O   1 
ATOM   5095 C CB  . ILE C 1 106 ? 16.583  56.266  -39.551 1.00 65.22  ? 105 ILE B CB  1 
ATOM   5096 C CG1 . ILE C 1 106 ? 15.183  56.645  -40.035 1.00 60.17  ? 105 ILE B CG1 1 
ATOM   5097 C CG2 . ILE C 1 106 ? 17.564  57.414  -39.712 1.00 70.51  ? 105 ILE B CG2 1 
ATOM   5098 C CD1 . ILE C 1 106 ? 14.554  57.772  -39.263 1.00 64.16  ? 105 ILE B CD1 1 
ATOM   5099 N N   . CYS C 1 107 ? 18.665  53.998  -38.694 1.00 73.82  ? 106 CYS B N   1 
ATOM   5100 C CA  . CYS C 1 107 ? 20.054  53.803  -38.201 1.00 79.02  ? 106 CYS B CA  1 
ATOM   5101 C C   . CYS C 1 107 ? 20.736  52.596  -38.842 1.00 60.88  ? 106 CYS B C   1 
ATOM   5102 O O   . CYS C 1 107 ? 20.052  51.767  -39.445 1.00 54.04  ? 106 CYS B O   1 
ATOM   5103 C CB  . CYS C 1 107 ? 20.100  53.731  -36.678 1.00 63.09  ? 106 CYS B CB  1 
ATOM   5104 S SG  . CYS C 1 107 ? 18.775  54.694  -35.912 1.00 79.26  ? 106 CYS B SG  1 
ATOM   5105 N N   . LYS C 1 108 ? 22.051  52.546  -38.689 1.00 65.90  ? 107 LYS B N   1 
ATOM   5106 C CA  . LYS C 1 108 ? 22.858  51.439  -39.251 1.00 62.19  ? 107 LYS B CA  1 
ATOM   5107 C C   . LYS C 1 108 ? 22.455  50.116  -38.624 1.00 54.91  ? 107 LYS B C   1 
ATOM   5108 O O   . LYS C 1 108 ? 22.084  50.101  -37.451 1.00 55.49  ? 107 LYS B O   1 
ATOM   5109 C CB  . LYS C 1 108 ? 24.333  51.743  -38.987 1.00 30.00  ? 107 LYS B CB  1 
ATOM   5110 C CG  . LYS C 1 108 ? 25.224  50.560  -38.643 1.00 30.00  ? 107 LYS B CG  1 
ATOM   5111 C CD  . LYS C 1 108 ? 26.646  50.978  -38.360 1.00 30.00  ? 107 LYS B CD  1 
ATOM   5112 C CE  . LYS C 1 108 ? 26.741  52.377  -37.789 1.00 30.00  ? 107 LYS B CE  1 
ATOM   5113 N NZ  . LYS C 1 108 ? 27.585  52.416  -36.572 1.00 30.00  ? 107 LYS B NZ  1 
ATOM   5114 N N   . PRO C 1 109 ? 22.475  49.018  -39.394 1.00 68.26  ? 108 PRO B N   1 
ATOM   5115 C CA  . PRO C 1 109 ? 22.218  47.696  -38.845 1.00 69.71  ? 108 PRO B CA  1 
ATOM   5116 C C   . PRO C 1 109 ? 22.924  47.428  -37.503 1.00 78.96  ? 108 PRO B C   1 
ATOM   5117 O O   . PRO C 1 109 ? 22.233  47.077  -36.568 1.00 76.91  ? 108 PRO B O   1 
ATOM   5118 C CB  . PRO C 1 109 ? 22.825  46.829  -39.944 1.00 52.44  ? 108 PRO B CB  1 
ATOM   5119 C CG  . PRO C 1 109 ? 22.453  47.554  -41.203 1.00 61.63  ? 108 PRO B CG  1 
ATOM   5120 C CD  . PRO C 1 109 ? 22.673  49.005  -40.843 1.00 71.77  ? 108 PRO B CD  1 
ATOM   5121 N N   . GLU C 1 110 ? 24.247  47.590  -37.419 1.00 64.95  ? 109 GLU B N   1 
ATOM   5122 C CA  . GLU C 1 110 ? 24.887  47.383  -36.099 1.00 67.52  ? 109 GLU B CA  1 
ATOM   5123 C C   . GLU C 1 110 ? 24.969  48.714  -35.358 1.00 71.36  ? 109 GLU B C   1 
ATOM   5124 O O   . GLU C 1 110 ? 25.931  49.453  -35.592 1.00 83.12  ? 109 GLU B O   1 
ATOM   5125 C CB  . GLU C 1 110 ? 26.297  46.821  -36.226 1.00 70.05  ? 109 GLU B CB  1 
ATOM   5126 C CG  . GLU C 1 110 ? 26.779  46.152  -34.953 1.00 81.18  ? 109 GLU B CG  1 
ATOM   5127 C CD  . GLU C 1 110 ? 26.852  44.635  -35.007 1.00 93.60  ? 109 GLU B CD  1 
ATOM   5128 O OE1 . GLU C 1 110 ? 27.632  44.112  -35.827 1.00 85.82  ? 109 GLU B OE1 1 
ATOM   5129 O OE2 . GLU C 1 110 ? 26.132  43.981  -34.227 1.00 84.94  ? 109 GLU B OE2 1 
ATOM   5130 N N   . CYS C 1 111 ? 24.023  48.972  -34.466 1.00 61.89  ? 110 CYS B N   1 
ATOM   5131 C CA  . CYS C 1 111 ? 24.079  50.195  -33.675 1.00 64.41  ? 110 CYS B CA  1 
ATOM   5132 C C   . CYS C 1 111 ? 23.184  49.999  -32.458 1.00 70.94  ? 110 CYS B C   1 
ATOM   5133 O O   . CYS C 1 111 ? 22.050  49.525  -32.592 1.00 65.18  ? 110 CYS B O   1 
ATOM   5134 C CB  . CYS C 1 111 ? 23.634  51.412  -34.501 1.00 64.02  ? 110 CYS B CB  1 
ATOM   5135 S SG  . CYS C 1 111 ? 22.626  52.644  -33.622 1.00 61.77  ? 110 CYS B SG  1 
ATOM   5136 N N   . ILE C 1 112 ? 23.692  50.354  -31.279 1.00 64.78  ? 111 ILE B N   1 
ATOM   5137 C CA  . ILE C 1 112 ? 23.020  50.024  -30.027 1.00 53.97  ? 111 ILE B CA  1 
ATOM   5138 C C   . ILE C 1 112 ? 21.875  50.993  -29.770 1.00 48.73  ? 111 ILE B C   1 
ATOM   5139 O O   . ILE C 1 112 ? 22.019  52.213  -29.920 1.00 51.69  ? 111 ILE B O   1 
ATOM   5140 C CB  . ILE C 1 112 ? 24.024  50.025  -28.864 1.00 55.41  ? 111 ILE B CB  1 
ATOM   5141 C CG1 . ILE C 1 112 ? 25.196  49.103  -29.198 1.00 50.70  ? 111 ILE B CG1 1 
ATOM   5142 C CG2 . ILE C 1 112 ? 23.343  49.600  -27.569 1.00 43.36  ? 111 ILE B CG2 1 
ATOM   5143 C CD1 . ILE C 1 112 ? 26.043  48.755  -28.015 1.00 42.37  ? 111 ILE B CD1 1 
ATOM   5144 N N   . PHE C 1 113 ? 20.732  50.445  -29.370 1.00 40.70  ? 112 PHE B N   1 
ATOM   5145 C CA  . PHE C 1 113 ? 19.536  51.219  -29.062 1.00 48.85  ? 112 PHE B CA  1 
ATOM   5146 C C   . PHE C 1 113 ? 19.360  51.264  -27.549 1.00 43.80  ? 112 PHE B C   1 
ATOM   5147 O O   . PHE C 1 113 ? 19.201  50.219  -26.908 1.00 35.79  ? 112 PHE B O   1 
ATOM   5148 C CB  . PHE C 1 113 ? 18.300  50.610  -29.726 1.00 52.30  ? 112 PHE B CB  1 
ATOM   5149 C CG  . PHE C 1 113 ? 18.163  50.942  -31.185 1.00 55.33  ? 112 PHE B CG  1 
ATOM   5150 C CD1 . PHE C 1 113 ? 19.221  51.494  -31.892 1.00 57.29  ? 112 PHE B CD1 1 
ATOM   5151 C CD2 . PHE C 1 113 ? 16.972  50.700  -31.851 1.00 55.96  ? 112 PHE B CD2 1 
ATOM   5152 C CE1 . PHE C 1 113 ? 19.092  51.796  -33.234 1.00 61.75  ? 112 PHE B CE1 1 
ATOM   5153 C CE2 . PHE C 1 113 ? 16.837  51.000  -33.192 1.00 51.88  ? 112 PHE B CE2 1 
ATOM   5154 C CZ  . PHE C 1 113 ? 17.898  51.549  -33.884 1.00 59.35  ? 112 PHE B CZ  1 
ATOM   5155 N N   . ALA C 1 114 ? 19.384  52.469  -26.985 1.00 33.95  ? 113 ALA B N   1 
ATOM   5156 C CA  . ALA C 1 114 ? 19.223  52.670  -25.554 1.00 30.95  ? 113 ALA B CA  1 
ATOM   5157 C C   . ALA C 1 114 ? 18.127  53.694  -25.304 1.00 34.32  ? 113 ALA B C   1 
ATOM   5158 O O   . ALA C 1 114 ? 18.002  54.677  -26.041 1.00 36.47  ? 113 ALA B O   1 
ATOM   5159 C CB  . ALA C 1 114 ? 20.529  53.130  -24.900 1.00 28.10  ? 113 ALA B CB  1 
ATOM   5160 N N   . SER C 1 115 ? 17.332  53.460  -24.262 1.00 32.65  ? 114 SER B N   1 
ATOM   5161 C CA  . SER C 1 115 ? 16.250  54.359  -23.890 1.00 34.70  ? 114 SER B CA  1 
ATOM   5162 C C   . SER C 1 115 ? 16.540  54.975  -22.530 1.00 26.96  ? 114 SER B C   1 
ATOM   5163 O O   . SER C 1 115 ? 16.961  54.274  -21.602 1.00 22.84  ? 114 SER B O   1 
ATOM   5164 C CB  . SER C 1 115 ? 14.904  53.631  -23.861 1.00 30.64  ? 114 SER B CB  1 
ATOM   5165 O OG  . SER C 1 115 ? 13.944  54.381  -23.131 1.00 34.23  ? 114 SER B OG  1 
ATOM   5166 N N   . ASN C 1 116 ? 16.313  56.285  -22.421 1.00 25.83  ? 115 ASN B N   1 
ATOM   5167 C CA  . ASN C 1 116 ? 16.418  57.019  -21.166 1.00 26.25  ? 115 ASN B CA  1 
ATOM   5168 C C   . ASN C 1 116 ? 15.080  57.088  -20.429 1.00 31.27  ? 115 ASN B C   1 
ATOM   5169 O O   . ASN C 1 116 ? 14.794  58.078  -19.743 1.00 37.89  ? 115 ASN B O   1 
ATOM   5170 C CB  . ASN C 1 116 ? 16.978  58.420  -21.443 1.00 24.61  ? 115 ASN B CB  1 
ATOM   5171 C CG  . ASN C 1 116 ? 17.211  59.241  -20.176 1.00 32.44  ? 115 ASN B CG  1 
ATOM   5172 O OD1 . ASN C 1 116 ? 17.879  58.804  -19.235 1.00 31.10  ? 115 ASN B OD1 1 
ATOM   5173 N ND2 . ASN C 1 116 ? 16.648  60.440  -20.154 1.00 28.08  ? 115 ASN B ND2 1 
ATOM   5174 N N   . THR C 1 117 ? 14.242  56.063  -20.557 1.00 33.18  ? 116 THR B N   1 
ATOM   5175 C CA  . THR C 1 117 ? 12.935  56.103  -19.918 1.00 37.22  ? 116 THR B CA  1 
ATOM   5176 C C   . THR C 1 117 ? 13.075  56.081  -18.398 1.00 40.37  ? 116 THR B C   1 
ATOM   5177 O O   . THR C 1 117 ? 14.028  55.525  -17.842 1.00 36.75  ? 116 THR B O   1 
ATOM   5178 C CB  . THR C 1 117 ? 12.061  54.942  -20.397 1.00 42.35  ? 116 THR B CB  1 
ATOM   5179 O OG1 . THR C 1 117 ? 10.688  55.227  -20.101 1.00 43.57  ? 116 THR B OG1 1 
ATOM   5180 C CG2 . THR C 1 117 ? 12.465  53.636  -19.732 1.00 34.01  ? 116 THR B CG2 1 
ATOM   5181 N N   . ALA C 1 118 ? 12.125  56.714  -17.711 1.00 42.37  ? 117 ALA B N   1 
ATOM   5182 C CA  . ALA C 1 118 ? 12.212  56.858  -16.241 1.00 31.35  ? 117 ALA B CA  1 
ATOM   5183 C C   . ALA C 1 118 ? 11.624  55.660  -15.490 1.00 40.78  ? 117 ALA B C   1 
ATOM   5184 O O   . ALA C 1 118 ? 12.118  55.376  -14.388 1.00 31.21  ? 117 ALA B O   1 
ATOM   5185 C CB  . ALA C 1 118 ? 11.483  58.109  -15.870 1.00 32.48  ? 117 ALA B CB  1 
ATOM   5186 N N   . SER C 1 119 ? 10.598  55.012  -16.043 1.00 35.20  ? 118 SER B N   1 
ATOM   5187 C CA  . SER C 1 119 ? 9.907   53.933  -15.299 1.00 37.13  ? 118 SER B CA  1 
ATOM   5188 C C   . SER C 1 119 ? 9.251   52.923  -16.238 1.00 48.75  ? 118 SER B C   1 
ATOM   5189 O O   . SER C 1 119 ? 8.793   51.891  -15.735 1.00 47.94  ? 118 SER B O   1 
ATOM   5190 C CB  . SER C 1 119 ? 8.862   54.539  -14.430 1.00 45.88  ? 118 SER B CB  1 
ATOM   5191 O OG  . SER C 1 119 ? 7.969   55.329  -15.200 1.00 51.16  ? 118 SER B OG  1 
ATOM   5192 N N   . LEU C 1 120 ? 9.196   53.214  -17.538 1.00 46.22  ? 119 LEU B N   1 
ATOM   5193 C CA  . LEU C 1 120 ? 8.465   52.320  -18.474 1.00 46.58  ? 119 LEU B CA  1 
ATOM   5194 C C   . LEU C 1 120 ? 9.208   50.997  -18.693 1.00 44.15  ? 119 LEU B C   1 
ATOM   5195 O O   . LEU C 1 120 ? 10.428  50.961  -18.504 1.00 41.86  ? 119 LEU B O   1 
ATOM   5196 C CB  . LEU C 1 120 ? 8.230   53.054  -19.795 1.00 40.30  ? 119 LEU B CB  1 
ATOM   5197 C CG  . LEU C 1 120 ? 7.329   54.281  -19.711 1.00 47.28  ? 119 LEU B CG  1 
ATOM   5198 C CD1 . LEU C 1 120 ? 6.987   54.793  -21.100 1.00 46.46  ? 119 LEU B CD1 1 
ATOM   5199 C CD2 . LEU C 1 120 ? 6.066   53.961  -18.934 1.00 35.82  ? 119 LEU B CD2 1 
ATOM   5200 N N   . SER C 1 121 ? 8.472   49.961  -19.100 1.00 45.36  ? 120 SER B N   1 
ATOM   5201 C CA  . SER C 1 121 ? 9.077   48.635  -19.378 1.00 46.00  ? 120 SER B CA  1 
ATOM   5202 C C   . SER C 1 121 ? 10.054  48.697  -20.547 1.00 42.77  ? 120 SER B C   1 
ATOM   5203 O O   . SER C 1 121 ? 9.631   49.040  -21.650 1.00 37.69  ? 120 SER B O   1 
ATOM   5204 C CB  . SER C 1 121 ? 8.041   47.587  -19.652 1.00 44.23  ? 120 SER B CB  1 
ATOM   5205 O OG  . SER C 1 121 ? 8.611   46.474  -20.314 1.00 39.51  ? 120 SER B OG  1 
ATOM   5206 N N   . ILE C 1 122 ? 11.307  48.352  -20.286 1.00 39.14  ? 121 ILE B N   1 
ATOM   5207 C CA  . ILE C 1 122 ? 12.285  48.249  -21.366 1.00 42.08  ? 121 ILE B CA  1 
ATOM   5208 C C   . ILE C 1 122 ? 11.873  47.167  -22.355 1.00 34.78  ? 121 ILE B C   1 
ATOM   5209 O O   . ILE C 1 122 ? 12.020  47.326  -23.572 1.00 34.33  ? 121 ILE B O   1 
ATOM   5210 C CB  . ILE C 1 122 ? 13.686  47.979  -20.783 1.00 40.10  ? 121 ILE B CB  1 
ATOM   5211 C CG1 . ILE C 1 122 ? 14.171  49.181  -19.972 1.00 37.00  ? 121 ILE B CG1 1 
ATOM   5212 C CG2 . ILE C 1 122 ? 14.678  47.645  -21.881 1.00 34.28  ? 121 ILE B CG2 1 
ATOM   5213 C CD1 . ILE C 1 122 ? 13.958  50.501  -20.669 1.00 36.80  ? 121 ILE B CD1 1 
ATOM   5214 N N   . THR C 1 123 ? 11.338  46.054  -21.844 1.00 41.30  ? 122 THR B N   1 
ATOM   5215 C CA  . THR C 1 123 ? 10.973  44.930  -22.701 1.00 37.88  ? 122 THR B CA  1 
ATOM   5216 C C   . THR C 1 123 ? 9.870   45.309  -23.683 1.00 40.00  ? 122 THR B C   1 
ATOM   5217 O O   . THR C 1 123 ? 9.949   44.983  -24.874 1.00 37.57  ? 122 THR B O   1 
ATOM   5218 C CB  . THR C 1 123 ? 10.539  43.744  -21.836 1.00 39.81  ? 122 THR B CB  1 
ATOM   5219 O OG1 . THR C 1 123 ? 11.633  43.329  -21.009 1.00 42.98  ? 122 THR B OG1 1 
ATOM   5220 C CG2 . THR C 1 123 ? 10.098  42.576  -22.700 1.00 42.05  ? 122 THR B CG2 1 
ATOM   5221 N N   . GLU C 1 124 ? 8.836   46.005  -23.207 1.00 41.64  ? 123 GLU B N   1 
ATOM   5222 C CA  . GLU C 1 124 ? 7.715   46.335  -24.081 1.00 50.45  ? 123 GLU B CA  1 
ATOM   5223 C C   . GLU C 1 124 ? 8.071   47.431  -25.077 1.00 49.84  ? 123 GLU B C   1 
ATOM   5224 O O   . GLU C 1 124 ? 7.547   47.434  -26.198 1.00 52.17  ? 123 GLU B O   1 
ATOM   5225 C CB  . GLU C 1 124 ? 6.499   46.752  -23.253 1.00 48.12  ? 123 GLU B CB  1 
ATOM   5226 C CG  . GLU C 1 124 ? 5.176   46.326  -23.866 1.00 58.10  ? 123 GLU B CG  1 
ATOM   5227 C CD  . GLU C 1 124 ? 4.059   47.307  -23.580 1.00 64.47  ? 123 GLU B CD  1 
ATOM   5228 O OE1 . GLU C 1 124 ? 4.057   47.902  -22.480 1.00 66.02  ? 123 GLU B OE1 1 
ATOM   5229 O OE2 . GLU C 1 124 ? 3.189   47.489  -24.459 1.00 62.50  ? 123 GLU B OE2 1 
ATOM   5230 N N   . ILE C 1 125 ? 8.943   48.369  -24.691 1.00 44.12  ? 124 ILE B N   1 
ATOM   5231 C CA  . ILE C 1 125 ? 9.360   49.421  -25.615 1.00 48.89  ? 124 ILE B CA  1 
ATOM   5232 C C   . ILE C 1 125 ? 9.979   48.808  -26.866 1.00 44.80  ? 124 ILE B C   1 
ATOM   5233 O O   . ILE C 1 125 ? 9.606   49.148  -27.996 1.00 51.70  ? 124 ILE B O   1 
ATOM   5234 C CB  . ILE C 1 125 ? 10.328  50.401  -24.924 1.00 43.88  ? 124 ILE B CB  1 
ATOM   5235 C CG1 . ILE C 1 125 ? 9.554   51.427  -24.093 1.00 49.31  ? 124 ILE B CG1 1 
ATOM   5236 C CG2 . ILE C 1 125 ? 11.185  51.123  -25.945 1.00 38.51  ? 124 ILE B CG2 1 
ATOM   5237 C CD1 . ILE C 1 125 ? 10.303  51.923  -22.871 1.00 45.94  ? 124 ILE B CD1 1 
ATOM   5238 N N   . GLY C 1 126 ? 10.916  47.881  -26.685 1.00 40.85  ? 125 GLY B N   1 
ATOM   5239 C CA  . GLY C 1 126 ? 11.544  47.226  -27.816 1.00 46.19  ? 125 GLY B CA  1 
ATOM   5240 C C   . GLY C 1 126 ? 11.003  45.833  -28.058 1.00 57.45  ? 125 GLY B C   1 
ATOM   5241 O O   . GLY C 1 126 ? 11.507  44.859  -27.493 1.00 73.28  ? 125 GLY B O   1 
ATOM   5242 N N   . LYS C 1 127 ? 9.972   45.723  -28.894 1.00 60.88  ? 126 LYS B N   1 
ATOM   5243 C CA  . LYS C 1 127 ? 9.329   44.441  -29.165 1.00 57.43  ? 126 LYS B CA  1 
ATOM   5244 C C   . LYS C 1 127 ? 9.515   44.004  -30.611 1.00 72.10  ? 126 LYS B C   1 
ATOM   5245 O O   . LYS C 1 127 ? 10.173  42.989  -30.862 1.00 77.80  ? 126 LYS B O   1 
ATOM   5246 C CB  . LYS C 1 127 ? 7.841   44.519  -28.807 1.00 55.18  ? 126 LYS B CB  1 
ATOM   5247 C CG  . LYS C 1 127 ? 7.362   43.372  -27.936 1.00 58.07  ? 126 LYS B CG  1 
ATOM   5248 C CD  . LYS C 1 127 ? 6.149   43.771  -27.113 1.00 57.29  ? 126 LYS B CD  1 
ATOM   5249 C CE  . LYS C 1 127 ? 5.010   44.245  -28.000 1.00 65.66  ? 126 LYS B CE  1 
ATOM   5250 N NZ  . LYS C 1 127 ? 3.737   44.381  -27.239 1.00 61.75  ? 126 LYS B NZ  1 
ATOM   5251 N N   . GLY C 1 128 ? 8.957   44.736  -31.570 1.00 63.18  ? 127 GLY B N   1 
ATOM   5252 C CA  . GLY C 1 128 ? 9.140   44.388  -32.962 1.00 67.35  ? 127 GLY B CA  1 
ATOM   5253 C C   . GLY C 1 128 ? 10.494  44.717  -33.536 1.00 70.83  ? 127 GLY B C   1 
ATOM   5254 O O   . GLY C 1 128 ? 10.722  44.504  -34.730 1.00 84.13  ? 127 GLY B O   1 
ATOM   5255 N N   . LEU C 1 129 ? 11.408  45.220  -32.713 1.00 70.84  ? 128 LEU B N   1 
ATOM   5256 C CA  . LEU C 1 129 ? 12.695  45.690  -33.197 1.00 70.11  ? 128 LEU B CA  1 
ATOM   5257 C C   . LEU C 1 129 ? 13.537  44.534  -33.726 1.00 66.43  ? 128 LEU B C   1 
ATOM   5258 O O   . LEU C 1 129 ? 13.321  43.364  -33.398 1.00 59.08  ? 128 LEU B O   1 
ATOM   5259 C CB  . LEU C 1 129 ? 13.455  46.415  -32.085 1.00 66.34  ? 128 LEU B CB  1 
ATOM   5260 C CG  . LEU C 1 129 ? 12.747  47.550  -31.340 1.00 62.73  ? 128 LEU B CG  1 
ATOM   5261 C CD1 . LEU C 1 129 ? 13.775  48.456  -30.683 1.00 59.43  ? 128 LEU B CD1 1 
ATOM   5262 C CD2 . LEU C 1 129 ? 11.843  48.356  -32.263 1.00 59.14  ? 128 LEU B CD2 1 
ATOM   5263 N N   . SER C 1 130 ? 14.508  44.886  -34.567 1.00 71.67  ? 129 SER B N   1 
ATOM   5264 C CA  . SER C 1 130 ? 15.460  43.930  -35.114 1.00 67.70  ? 129 SER B CA  1 
ATOM   5265 C C   . SER C 1 130 ? 16.673  43.727  -34.221 1.00 62.36  ? 129 SER B C   1 
ATOM   5266 O O   . SER C 1 130 ? 17.353  42.701  -34.342 1.00 65.08  ? 129 SER B O   1 
ATOM   5267 C CB  . SER C 1 130 ? 15.921  44.391  -36.501 1.00 78.79  ? 129 SER B CB  1 
ATOM   5268 O OG  . SER C 1 130 ? 17.333  44.328  -36.621 1.00 67.21  ? 129 SER B OG  1 
ATOM   5269 N N   . ARG C 1 131 ? 16.959  44.673  -33.338 1.00 66.17  ? 130 ARG B N   1 
ATOM   5270 C CA  . ARG C 1 131 ? 18.102  44.628  -32.445 1.00 58.26  ? 130 ARG B CA  1 
ATOM   5271 C C   . ARG C 1 131 ? 17.632  44.687  -30.999 1.00 50.56  ? 130 ARG B C   1 
ATOM   5272 O O   . ARG C 1 131 ? 16.491  45.074  -30.722 1.00 48.20  ? 130 ARG B O   1 
ATOM   5273 C CB  . ARG C 1 131 ? 19.054  45.799  -32.722 1.00 58.35  ? 130 ARG B CB  1 
ATOM   5274 C CG  . ARG C 1 131 ? 18.393  47.152  -32.575 1.00 57.98  ? 130 ARG B CG  1 
ATOM   5275 C CD  . ARG C 1 131 ? 19.099  48.191  -33.410 1.00 57.48  ? 130 ARG B CD  1 
ATOM   5276 N NE  . ARG C 1 131 ? 18.569  48.236  -34.766 1.00 62.75  ? 130 ARG B NE  1 
ATOM   5277 C CZ  . ARG C 1 131 ? 19.294  48.514  -35.840 1.00 65.11  ? 130 ARG B CZ  1 
ATOM   5278 N NH1 . ARG C 1 131 ? 20.585  48.787  -35.749 1.00 65.32  ? 130 ARG B NH1 1 
ATOM   5279 N NH2 . ARG C 1 131 ? 18.708  48.520  -37.035 1.00 66.12  ? 130 ARG B NH2 1 
ATOM   5280 N N   . PRO C 1 132 ? 18.481  44.292  -30.052 1.00 46.06  ? 131 PRO B N   1 
ATOM   5281 C CA  . PRO C 1 132 ? 18.129  44.444  -28.637 1.00 48.50  ? 131 PRO B CA  1 
ATOM   5282 C C   . PRO C 1 132 ? 17.832  45.895  -28.284 1.00 50.70  ? 131 PRO B C   1 
ATOM   5283 O O   . PRO C 1 132 ? 18.227  46.833  -28.980 1.00 46.48  ? 131 PRO B O   1 
ATOM   5284 C CB  . PRO C 1 132 ? 19.374  43.946  -27.894 1.00 51.01  ? 131 PRO B CB  1 
ATOM   5285 C CG  . PRO C 1 132 ? 20.197  43.210  -28.893 1.00 53.82  ? 131 PRO B CG  1 
ATOM   5286 C CD  . PRO C 1 132 ? 19.646  43.415  -30.264 1.00 48.37  ? 131 PRO B CD  1 
ATOM   5287 N N   . LEU C 1 133 ? 17.118  46.067  -27.174 1.00 47.22  ? 132 LEU B N   1 
ATOM   5288 C CA  . LEU C 1 133 ? 16.825  47.378  -26.612 1.00 41.64  ? 132 LEU B CA  1 
ATOM   5289 C C   . LEU C 1 133 ? 17.243  47.363  -25.152 1.00 36.61  ? 132 LEU B C   1 
ATOM   5290 O O   . LEU C 1 133 ? 16.814  46.490  -24.391 1.00 39.30  ? 132 LEU B O   1 
ATOM   5291 C CB  . LEU C 1 133 ? 15.335  47.729  -26.756 1.00 38.11  ? 132 LEU B CB  1 
ATOM   5292 C CG  . LEU C 1 133 ? 14.835  49.158  -26.501 1.00 40.02  ? 132 LEU B CG  1 
ATOM   5293 C CD1 . LEU C 1 133 ? 14.602  49.438  -25.016 1.00 40.82  ? 132 LEU B CD1 1 
ATOM   5294 C CD2 . LEU C 1 133 ? 15.790  50.178  -27.084 1.00 39.14  ? 132 LEU B CD2 1 
ATOM   5295 N N   . VAL C 1 134 ? 18.088  48.315  -24.768 1.00 30.30  ? 133 VAL B N   1 
ATOM   5296 C CA  . VAL C 1 134 ? 18.625  48.377  -23.417 1.00 32.39  ? 133 VAL B CA  1 
ATOM   5297 C C   . VAL C 1 134 ? 18.254  49.719  -22.799 1.00 29.63  ? 133 VAL B C   1 
ATOM   5298 O O   . VAL C 1 134 ? 17.985  50.703  -23.489 1.00 32.59  ? 133 VAL B O   1 
ATOM   5299 C CB  . VAL C 1 134 ? 20.154  48.162  -23.401 1.00 32.78  ? 133 VAL B CB  1 
ATOM   5300 C CG1 . VAL C 1 134 ? 20.874  49.433  -23.811 1.00 31.30  ? 133 VAL B CG1 1 
ATOM   5301 C CG2 . VAL C 1 134 ? 20.623  47.683  -22.032 1.00 32.60  ? 133 VAL B CG2 1 
ATOM   5302 N N   . GLY C 1 135 ? 18.222  49.745  -21.465 1.00 26.78  ? 134 GLY B N   1 
ATOM   5303 C CA  . GLY C 1 135 ? 17.946  50.963  -20.726 1.00 27.86  ? 134 GLY B CA  1 
ATOM   5304 C C   . GLY C 1 135 ? 19.241  51.615  -20.272 1.00 32.65  ? 134 GLY B C   1 
ATOM   5305 O O   . GLY C 1 135 ? 20.100  50.965  -19.673 1.00 26.24  ? 134 GLY B O   1 
ATOM   5306 N N   . MET C 1 136 ? 19.369  52.907  -20.575 1.00 25.22  ? 135 MET B N   1 
ATOM   5307 C CA  . MET C 1 136 ? 20.522  53.709  -20.161 1.00 27.59  ? 135 MET B CA  1 
ATOM   5308 C C   . MET C 1 136 ? 19.959  54.983  -19.548 1.00 26.21  ? 135 MET B C   1 
ATOM   5309 O O   . MET C 1 136 ? 19.702  55.959  -20.257 1.00 29.74  ? 135 MET B O   1 
ATOM   5310 C CB  . MET C 1 136 ? 21.448  54.016  -21.324 1.00 23.59  ? 135 MET B CB  1 
ATOM   5311 C CG  . MET C 1 136 ? 22.831  54.432  -20.885 1.00 23.09  ? 135 MET B CG  1 
ATOM   5312 S SD  . MET C 1 136 ? 23.875  54.912  -22.264 1.00 28.37  ? 135 MET B SD  1 
ATOM   5313 C CE  . MET C 1 136 ? 25.239  55.678  -21.384 1.00 23.51  ? 135 MET B CE  1 
ATOM   5314 N N   . HIS C 1 137 ? 19.783  54.974  -18.234 1.00 27.34  ? 136 HIS B N   1 
ATOM   5315 C CA  . HIS C 1 137 ? 19.041  56.015  -17.539 1.00 27.69  ? 136 HIS B CA  1 
ATOM   5316 C C   . HIS C 1 137 ? 20.004  57.057  -16.980 1.00 26.06  ? 136 HIS B C   1 
ATOM   5317 O O   . HIS C 1 137 ? 20.832  56.744  -16.120 1.00 26.47  ? 136 HIS B O   1 
ATOM   5318 C CB  . HIS C 1 137 ? 18.195  55.398  -16.428 1.00 30.63  ? 136 HIS B CB  1 
ATOM   5319 C CG  . HIS C 1 137 ? 17.241  56.357  -15.794 1.00 34.94  ? 136 HIS B CG  1 
ATOM   5320 N ND1 . HIS C 1 137 ? 16.800  56.215  -14.496 1.00 27.61  ? 136 HIS B ND1 1 
ATOM   5321 C CD2 . HIS C 1 137 ? 16.647  57.473  -16.276 1.00 35.70  ? 136 HIS B CD2 1 
ATOM   5322 C CE1 . HIS C 1 137 ? 15.975  57.205  -14.205 1.00 33.43  ? 136 HIS B CE1 1 
ATOM   5323 N NE2 . HIS C 1 137 ? 15.864  57.982  -15.268 1.00 37.88  ? 136 HIS B NE2 1 
ATOM   5324 N N   . PHE C 1 138 ? 19.898  58.285  -17.481 1.00 31.35  ? 137 PHE B N   1 
ATOM   5325 C CA  . PHE C 1 138 ? 20.650  59.418  -16.961 1.00 27.48  ? 137 PHE B CA  1 
ATOM   5326 C C   . PHE C 1 138 ? 19.838  60.122  -15.878 1.00 32.46  ? 137 PHE B C   1 
ATOM   5327 O O   . PHE C 1 138 ? 18.672  59.806  -15.634 1.00 32.42  ? 137 PHE B O   1 
ATOM   5328 C CB  . PHE C 1 138 ? 20.994  60.406  -18.075 1.00 29.38  ? 137 PHE B CB  1 
ATOM   5329 C CG  . PHE C 1 138 ? 22.022  59.902  -19.045 1.00 32.46  ? 137 PHE B CG  1 
ATOM   5330 C CD1 . PHE C 1 138 ? 21.691  58.943  -19.990 1.00 26.33  ? 137 PHE B CD1 1 
ATOM   5331 C CD2 . PHE C 1 138 ? 23.314  60.406  -19.027 1.00 30.28  ? 137 PHE B CD2 1 
ATOM   5332 C CE1 . PHE C 1 138 ? 22.634  58.484  -20.892 1.00 25.37  ? 137 PHE B CE1 1 
ATOM   5333 C CE2 . PHE C 1 138 ? 24.261  59.956  -19.929 1.00 27.13  ? 137 PHE B CE2 1 
ATOM   5334 C CZ  . PHE C 1 138 ? 23.920  58.993  -20.863 1.00 22.76  ? 137 PHE B CZ  1 
ATOM   5335 N N   . PHE C 1 139 ? 20.461  61.109  -15.235 1.00 30.70  ? 138 PHE B N   1 
ATOM   5336 C CA  . PHE C 1 139 ? 19.821  61.801  -14.123 1.00 32.14  ? 138 PHE B CA  1 
ATOM   5337 C C   . PHE C 1 139 ? 20.086  63.294  -14.211 1.00 30.35  ? 138 PHE B C   1 
ATOM   5338 O O   . PHE C 1 139 ? 21.227  63.714  -14.417 1.00 31.63  ? 138 PHE B O   1 
ATOM   5339 C CB  . PHE C 1 139 ? 20.314  61.243  -12.786 1.00 29.68  ? 138 PHE B CB  1 
ATOM   5340 C CG  . PHE C 1 139 ? 19.847  59.851  -12.523 1.00 28.37  ? 138 PHE B CG  1 
ATOM   5341 C CD1 . PHE C 1 139 ? 18.666  59.622  -11.840 1.00 26.80  ? 138 PHE B CD1 1 
ATOM   5342 C CD2 . PHE C 1 139 ? 20.569  58.767  -12.994 1.00 23.28  ? 138 PHE B CD2 1 
ATOM   5343 C CE1 . PHE C 1 139 ? 18.224  58.336  -11.612 1.00 33.06  ? 138 PHE B CE1 1 
ATOM   5344 C CE2 . PHE C 1 139 ? 20.131  57.481  -12.772 1.00 30.94  ? 138 PHE B CE2 1 
ATOM   5345 C CZ  . PHE C 1 139 ? 18.956  57.263  -12.078 1.00 34.95  ? 138 PHE B CZ  1 
ATOM   5346 N N   . ASN C 1 140 ? 19.029  64.080  -14.041 1.00 26.52  ? 139 ASN B N   1 
ATOM   5347 C CA  . ASN C 1 140 ? 19.114  65.532  -14.181 1.00 29.49  ? 139 ASN B CA  1 
ATOM   5348 C C   . ASN C 1 140 ? 19.983  66.133  -13.081 1.00 34.69  ? 139 ASN B C   1 
ATOM   5349 O O   . ASN C 1 140 ? 19.713  65.909  -11.895 1.00 34.89  ? 139 ASN B O   1 
ATOM   5350 C CB  . ASN C 1 140 ? 17.708  66.125  -14.125 1.00 40.98  ? 139 ASN B CB  1 
ATOM   5351 C CG  . ASN C 1 140 ? 17.641  67.541  -14.658 1.00 38.53  ? 139 ASN B CG  1 
ATOM   5352 O OD1 . ASN C 1 140 ? 18.662  68.164  -14.941 1.00 37.10  ? 139 ASN B OD1 1 
ATOM   5353 N ND2 . ASN C 1 140 ? 16.427  68.061  -14.792 1.00 34.07  ? 139 ASN B ND2 1 
ATOM   5354 N N   . PRO C 1 141 ? 21.027  66.909  -13.420 1.00 33.89  ? 140 PRO B N   1 
ATOM   5355 C CA  . PRO C 1 141 ? 21.547  67.230  -14.762 1.00 34.66  ? 140 PRO B CA  1 
ATOM   5356 C C   . PRO C 1 141 ? 22.503  66.161  -15.292 1.00 32.00  ? 140 PRO B C   1 
ATOM   5357 O O   . PRO C 1 141 ? 23.434  65.741  -14.608 1.00 32.29  ? 140 PRO B O   1 
ATOM   5358 C CB  . PRO C 1 141 ? 22.241  68.578  -14.532 1.00 29.00  ? 140 PRO B CB  1 
ATOM   5359 C CG  . PRO C 1 141 ? 22.766  68.465  -13.130 1.00 36.59  ? 140 PRO B CG  1 
ATOM   5360 C CD  . PRO C 1 141 ? 21.698  67.708  -12.376 1.00 37.06  ? 140 PRO B CD  1 
ATOM   5361 N N   . ALA C 1 142 ? 22.290  65.712  -16.531 1.00 28.52  ? 141 ALA B N   1 
ATOM   5362 C CA  . ALA C 1 142 ? 22.963  64.511  -17.019 1.00 27.49  ? 141 ALA B CA  1 
ATOM   5363 C C   . ALA C 1 142 ? 24.462  64.714  -17.188 1.00 26.96  ? 141 ALA B C   1 
ATOM   5364 O O   . ALA C 1 142 ? 25.224  63.742  -17.142 1.00 27.81  ? 141 ALA B O   1 
ATOM   5365 C CB  . ALA C 1 142 ? 22.340  64.059  -18.338 1.00 22.80  ? 141 ALA B CB  1 
ATOM   5366 N N   . ASP C 1 143 ? 24.907  65.951  -17.390 1.00 34.60  ? 142 ASP B N   1 
ATOM   5367 C CA  . ASP C 1 143 ? 26.333  66.209  -17.533 1.00 36.17  ? 142 ASP B CA  1 
ATOM   5368 C C   . ASP C 1 143 ? 27.067  66.192  -16.197 1.00 34.98  ? 142 ASP B C   1 
ATOM   5369 O O   . ASP C 1 143 ? 28.300  66.104  -16.183 1.00 35.99  ? 142 ASP B O   1 
ATOM   5370 C CB  . ASP C 1 143 ? 26.552  67.554  -18.226 1.00 28.18  ? 142 ASP B CB  1 
ATOM   5371 C CG  . ASP C 1 143 ? 25.636  68.636  -17.692 1.00 42.85  ? 142 ASP B CG  1 
ATOM   5372 O OD1 . ASP C 1 143 ? 24.432  68.355  -17.503 1.00 40.22  ? 142 ASP B OD1 1 
ATOM   5373 O OD2 . ASP C 1 143 ? 26.116  69.767  -17.458 1.00 53.51  ? 142 ASP B OD2 1 
ATOM   5374 N N   . ARG C 1 144 ? 26.338  66.253  -15.081 1.00 29.12  ? 143 ARG B N   1 
ATOM   5375 C CA  . ARG C 1 144 ? 26.922  66.351  -13.749 1.00 36.12  ? 143 ARG B CA  1 
ATOM   5376 C C   . ARG C 1 144 ? 26.681  65.117  -12.894 1.00 28.27  ? 143 ARG B C   1 
ATOM   5377 O O   . ARG C 1 144 ? 27.617  64.612  -12.270 1.00 28.92  ? 143 ARG B O   1 
ATOM   5378 C CB  . ARG C 1 144 ? 26.373  67.590  -13.029 1.00 30.99  ? 143 ARG B CB  1 
ATOM   5379 C CG  . ARG C 1 144 ? 26.596  68.889  -13.782 1.00 39.19  ? 143 ARG B CG  1 
ATOM   5380 C CD  . ARG C 1 144 ? 27.565  69.789  -13.035 1.00 50.35  ? 143 ARG B CD  1 
ATOM   5381 N NE  . ARG C 1 144 ? 28.945  69.578  -13.459 1.00 50.33  ? 143 ARG B NE  1 
ATOM   5382 C CZ  . ARG C 1 144 ? 30.009  69.924  -12.746 1.00 53.94  ? 143 ARG B CZ  1 
ATOM   5383 N NH1 . ARG C 1 144 ? 29.890  70.499  -11.559 1.00 55.85  ? 143 ARG B NH1 1 
ATOM   5384 N NH2 . ARG C 1 144 ? 31.223  69.686  -13.236 1.00 54.18  ? 143 ARG B NH2 1 
ATOM   5385 N N   . MET C 1 145 ? 25.446  64.620  -12.839 1.00 32.72  ? 144 MET B N   1 
ATOM   5386 C CA  . MET C 1 145 ? 25.154  63.431  -12.046 1.00 25.26  ? 144 MET B CA  1 
ATOM   5387 C C   . MET C 1 145 ? 25.936  62.234  -12.577 1.00 28.02  ? 144 MET B C   1 
ATOM   5388 O O   . MET C 1 145 ? 25.892  61.927  -13.773 1.00 25.63  ? 144 MET B O   1 
ATOM   5389 C CB  . MET C 1 145 ? 23.653  63.138  -12.061 1.00 28.94  ? 144 MET B CB  1 
ATOM   5390 C CG  . MET C 1 145 ? 22.762  64.309  -11.640 1.00 29.40  ? 144 MET B CG  1 
ATOM   5391 S SD  . MET C 1 145 ? 23.239  65.113  -10.092 1.00 34.25  ? 144 MET B SD  1 
ATOM   5392 C CE  . MET C 1 145 ? 22.979  63.781  -8.922  1.00 33.48  ? 144 MET B CE  1 
ATOM   5393 N N   . LYS C 1 146 ? 26.644  61.548  -11.677 1.00 28.41  ? 145 LYS B N   1 
ATOM   5394 C CA  . LYS C 1 146 ? 27.586  60.505  -12.065 1.00 32.53  ? 145 LYS B CA  1 
ATOM   5395 C C   . LYS C 1 146 ? 26.937  59.145  -12.285 1.00 28.57  ? 145 LYS B C   1 
ATOM   5396 O O   . LYS C 1 146 ? 27.614  58.233  -12.773 1.00 31.40  ? 145 LYS B O   1 
ATOM   5397 C CB  . LYS C 1 146 ? 28.684  60.361  -11.002 1.00 26.50  ? 145 LYS B CB  1 
ATOM   5398 C CG  . LYS C 1 146 ? 29.445  61.645  -10.683 1.00 30.85  ? 145 LYS B CG  1 
ATOM   5399 C CD  . LYS C 1 146 ? 30.140  62.214  -11.914 1.00 49.03  ? 145 LYS B CD  1 
ATOM   5400 C CE  . LYS C 1 146 ? 31.210  63.229  -11.526 1.00 50.36  ? 145 LYS B CE  1 
ATOM   5401 N NZ  . LYS C 1 146 ? 30.916  64.588  -12.070 1.00 56.44  ? 145 LYS B NZ  1 
ATOM   5402 N N   . LEU C 1 147 ? 25.665  58.974  -11.939 1.00 26.02  ? 146 LEU B N   1 
ATOM   5403 C CA  . LEU C 1 147 ? 25.038  57.660  -11.987 1.00 29.80  ? 146 LEU B CA  1 
ATOM   5404 C C   . LEU C 1 147 ? 24.427  57.384  -13.357 1.00 24.24  ? 146 LEU B C   1 
ATOM   5405 O O   . LEU C 1 147 ? 23.899  58.285  -14.014 1.00 23.15  ? 146 LEU B O   1 
ATOM   5406 C CB  . LEU C 1 147 ? 23.965  57.536  -10.902 1.00 20.34  ? 146 LEU B CB  1 
ATOM   5407 C CG  . LEU C 1 147 ? 23.090  56.278  -10.943 1.00 26.47  ? 146 LEU B CG  1 
ATOM   5408 C CD1 . LEU C 1 147 ? 23.917  55.030  -10.686 1.00 18.42  ? 146 LEU B CD1 1 
ATOM   5409 C CD2 . LEU C 1 147 ? 21.939  56.374  -9.949  1.00 22.40  ? 146 LEU B CD2 1 
ATOM   5410 N N   . ILE C 1 148 ? 24.522  56.127  -13.786 1.00 20.16  ? 147 ILE B N   1 
ATOM   5411 C CA  . ILE C 1 148 ? 23.779  55.604  -14.924 1.00 26.09  ? 147 ILE B CA  1 
ATOM   5412 C C   . ILE C 1 148 ? 23.164  54.282  -14.493 1.00 27.74  ? 147 ILE B C   1 
ATOM   5413 O O   . ILE C 1 148 ? 23.883  53.371  -14.068 1.00 34.11  ? 147 ILE B O   1 
ATOM   5414 C CB  . ILE C 1 148 ? 24.666  55.397  -16.163 1.00 30.37  ? 147 ILE B CB  1 
ATOM   5415 C CG1 . ILE C 1 148 ? 25.363  56.700  -16.556 1.00 24.77  ? 147 ILE B CG1 1 
ATOM   5416 C CG2 . ILE C 1 148 ? 23.844  54.819  -17.317 1.00 20.29  ? 147 ILE B CG2 1 
ATOM   5417 C CD1 . ILE C 1 148 ? 24.608  57.508  -17.572 1.00 25.76  ? 147 ILE B CD1 1 
ATOM   5418 N N   . GLU C 1 149 ? 21.845  54.174  -14.597 1.00 27.39  ? 148 GLU B N   1 
ATOM   5419 C CA  . GLU C 1 149 ? 21.160  52.908  -14.371 1.00 28.33  ? 148 GLU B CA  1 
ATOM   5420 C C   . GLU C 1 149 ? 21.129  52.128  -15.682 1.00 29.36  ? 148 GLU B C   1 
ATOM   5421 O O   . GLU C 1 149 ? 20.670  52.646  -16.707 1.00 27.80  ? 148 GLU B O   1 
ATOM   5422 C CB  . GLU C 1 149 ? 19.747  53.138  -13.835 1.00 27.98  ? 148 GLU B CB  1 
ATOM   5423 C CG  . GLU C 1 149 ? 19.692  53.467  -12.344 1.00 28.72  ? 148 GLU B CG  1 
ATOM   5424 C CD  . GLU C 1 149 ? 18.271  53.682  -11.833 1.00 34.05  ? 148 GLU B CD  1 
ATOM   5425 O OE1 . GLU C 1 149 ? 17.435  54.224  -12.592 1.00 31.28  ? 148 GLU B OE1 1 
ATOM   5426 O OE2 . GLU C 1 149 ? 17.991  53.305  -10.670 1.00 31.33  ? 148 GLU B OE2 1 
ATOM   5427 N N   . VAL C 1 150 ? 21.630  50.894  -15.651 1.00 22.34  ? 149 VAL B N   1 
ATOM   5428 C CA  . VAL C 1 150 ? 21.662  50.013  -16.814 1.00 28.21  ? 149 VAL B CA  1 
ATOM   5429 C C   . VAL C 1 150 ? 20.590  48.951  -16.614 1.00 31.43  ? 149 VAL B C   1 
ATOM   5430 O O   . VAL C 1 150 ? 20.712  48.089  -15.734 1.00 27.80  ? 149 VAL B O   1 
ATOM   5431 C CB  . VAL C 1 150 ? 23.043  49.375  -17.009 1.00 33.85  ? 149 VAL B CB  1 
ATOM   5432 C CG1 . VAL C 1 150 ? 23.118  48.686  -18.362 1.00 31.51  ? 149 VAL B CG1 1 
ATOM   5433 C CG2 . VAL C 1 150 ? 24.137  50.424  -16.873 1.00 23.13  ? 149 VAL B CG2 1 
ATOM   5434 N N   . ILE C 1 151 ? 19.546  49.002  -17.436 1.00 26.75  ? 150 ILE B N   1 
ATOM   5435 C CA  . ILE C 1 151 ? 18.381  48.134  -17.304 1.00 25.56  ? 150 ILE B CA  1 
ATOM   5436 C C   . ILE C 1 151 ? 18.296  47.240  -18.531 1.00 34.88  ? 150 ILE B C   1 
ATOM   5437 O O   . ILE C 1 151 ? 18.333  47.729  -19.667 1.00 36.87  ? 150 ILE B O   1 
ATOM   5438 C CB  . ILE C 1 151 ? 17.086  48.949  -17.137 1.00 28.93  ? 150 ILE B CB  1 
ATOM   5439 C CG1 . ILE C 1 151 ? 17.243  49.978  -16.017 1.00 32.36  ? 150 ILE B CG1 1 
ATOM   5440 C CG2 . ILE C 1 151 ? 15.902  48.023  -16.884 1.00 31.74  ? 150 ILE B CG2 1 
ATOM   5441 C CD1 . ILE C 1 151 ? 17.467  51.384  -16.510 1.00 35.08  ? 150 ILE B CD1 1 
ATOM   5442 N N   . ALA C 1 152 ? 18.164  45.939  -18.304 1.00 44.18  ? 151 ALA B N   1 
ATOM   5443 C CA  . ALA C 1 152 ? 18.053  44.966  -19.380 1.00 48.97  ? 151 ALA B CA  1 
ATOM   5444 C C   . ALA C 1 152 ? 16.641  44.403  -19.432 1.00 46.62  ? 151 ALA B C   1 
ATOM   5445 O O   . ALA C 1 152 ? 16.025  44.146  -18.392 1.00 46.33  ? 151 ALA B O   1 
ATOM   5446 C CB  . ALA C 1 152 ? 19.059  43.827  -19.197 1.00 44.06  ? 151 ALA B CB  1 
ATOM   5447 N N   . GLY C 1 153 ? 16.126  44.227  -20.647 1.00 48.90  ? 152 GLY B N   1 
ATOM   5448 C CA  . GLY C 1 153 ? 14.887  43.505  -20.825 1.00 49.20  ? 152 GLY B CA  1 
ATOM   5449 C C   . GLY C 1 153 ? 15.109  42.007  -20.770 1.00 59.55  ? 152 GLY B C   1 
ATOM   5450 O O   . GLY C 1 153 ? 16.241  41.522  -20.728 1.00 53.98  ? 152 GLY B O   1 
ATOM   5451 N N   . CYS C 1 154 ? 13.999  41.263  -20.761 1.00 58.41  ? 153 CYS B N   1 
ATOM   5452 C CA  . CYS C 1 154 ? 14.101  39.807  -20.778 1.00 59.34  ? 153 CYS B CA  1 
ATOM   5453 C C   . CYS C 1 154 ? 14.880  39.321  -21.990 1.00 61.71  ? 153 CYS B C   1 
ATOM   5454 O O   . CYS C 1 154 ? 15.600  38.319  -21.909 1.00 69.94  ? 153 CYS B O   1 
ATOM   5455 C CB  . CYS C 1 154 ? 12.711  39.173  -20.765 1.00 58.37  ? 153 CYS B CB  1 
ATOM   5456 S SG  . CYS C 1 154 ? 11.556  39.923  -19.613 1.00 69.08  ? 153 CYS B SG  1 
ATOM   5457 N N   . ASN C 1 155 ? 14.754  40.021  -23.115 1.00 52.24  ? 154 ASN B N   1 
ATOM   5458 C CA  . ASN C 1 155 ? 15.423  39.633  -24.347 1.00 55.08  ? 154 ASN B CA  1 
ATOM   5459 C C   . ASN C 1 155 ? 16.541  40.615  -24.676 1.00 61.83  ? 154 ASN B C   1 
ATOM   5460 O O   . ASN C 1 155 ? 16.610  41.136  -25.794 1.00 58.14  ? 154 ASN B O   1 
ATOM   5461 C CB  . ASN C 1 155 ? 14.411  39.556  -25.493 1.00 68.96  ? 154 ASN B CB  1 
ATOM   5462 C CG  . ASN C 1 155 ? 13.065  38.998  -25.050 1.00 68.22  ? 154 ASN B CG  1 
ATOM   5463 O OD1 . ASN C 1 155 ? 12.969  38.289  -24.048 1.00 60.71  ? 154 ASN B OD1 1 
ATOM   5464 N ND2 . ASN C 1 155 ? 12.015  39.325  -25.797 1.00 57.66  ? 154 ASN B ND2 1 
ATOM   5465 N N   . THR C 1 156 ? 17.415  40.877  -23.707 1.00 58.28  ? 155 THR B N   1 
ATOM   5466 C CA  . THR C 1 156 ? 18.550  41.776  -23.883 1.00 53.01  ? 155 THR B CA  1 
ATOM   5467 C C   . THR C 1 156 ? 19.832  41.012  -23.578 1.00 46.91  ? 155 THR B C   1 
ATOM   5468 O O   . THR C 1 156 ? 20.026  40.576  -22.430 1.00 40.35  ? 155 THR B O   1 
ATOM   5469 C CB  . THR C 1 156 ? 18.428  43.005  -22.973 1.00 58.20  ? 155 THR B CB  1 
ATOM   5470 O OG1 . THR C 1 156 ? 17.242  43.737  -23.310 1.00 53.53  ? 155 THR B OG1 1 
ATOM   5471 C CG2 . THR C 1 156 ? 19.636  43.918  -23.135 1.00 48.11  ? 155 THR B CG2 1 
ATOM   5472 N N   . PRO C 1 157 ? 20.725  40.820  -24.547 1.00 50.88  ? 156 PRO B N   1 
ATOM   5473 C CA  . PRO C 1 157 ? 21.925  40.010  -24.304 1.00 51.33  ? 156 PRO B CA  1 
ATOM   5474 C C   . PRO C 1 157 ? 22.895  40.708  -23.362 1.00 62.69  ? 156 PRO B C   1 
ATOM   5475 O O   . PRO C 1 157 ? 22.810  41.908  -23.093 1.00 59.98  ? 156 PRO B O   1 
ATOM   5476 C CB  . PRO C 1 157 ? 22.541  39.833  -25.698 1.00 53.65  ? 156 PRO B CB  1 
ATOM   5477 C CG  . PRO C 1 157 ? 21.501  40.304  -26.669 1.00 49.41  ? 156 PRO B CG  1 
ATOM   5478 C CD  . PRO C 1 157 ? 20.646  41.288  -25.938 1.00 49.27  ? 156 PRO B CD  1 
ATOM   5479 N N   . ALA C 1 158 ? 23.843  39.916  -22.856 1.00 61.02  ? 157 ALA B N   1 
ATOM   5480 C CA  . ALA C 1 158 ? 24.852  40.461  -21.957 1.00 54.86  ? 157 ALA B CA  1 
ATOM   5481 C C   . ALA C 1 158 ? 25.851  41.343  -22.697 1.00 60.46  ? 157 ALA B C   1 
ATOM   5482 O O   . ALA C 1 158 ? 26.394  42.283  -22.108 1.00 60.55  ? 157 ALA B O   1 
ATOM   5483 C CB  . ALA C 1 158 ? 25.576  39.327  -21.232 1.00 60.47  ? 157 ALA B CB  1 
ATOM   5484 N N   . GLU C 1 159 ? 26.103  41.063  -23.981 1.00 63.04  ? 158 GLU B N   1 
ATOM   5485 C CA  . GLU C 1 159 ? 27.043  41.879  -24.745 1.00 71.89  ? 158 GLU B CA  1 
ATOM   5486 C C   . GLU C 1 159 ? 26.578  43.325  -24.843 1.00 66.46  ? 158 GLU B C   1 
ATOM   5487 O O   . GLU C 1 159 ? 27.407  44.242  -24.892 1.00 64.58  ? 158 GLU B O   1 
ATOM   5488 C CB  . GLU C 1 159 ? 27.245  41.294  -26.146 1.00 69.03  ? 158 GLU B CB  1 
ATOM   5489 C CG  . GLU C 1 159 ? 28.477  41.829  -26.873 1.00 73.13  ? 158 GLU B CG  1 
ATOM   5490 C CD  . GLU C 1 159 ? 28.960  40.899  -27.975 1.00 88.77  ? 158 GLU B CD  1 
ATOM   5491 O OE1 . GLU C 1 159 ? 28.348  39.825  -28.158 1.00 82.81  ? 158 GLU B OE1 1 
ATOM   5492 O OE2 . GLU C 1 159 ? 29.949  41.242  -28.661 1.00 79.78  ? 158 GLU B OE2 1 
ATOM   5493 N N   . THR C 1 160 ? 25.264  43.551  -24.871 1.00 60.31  ? 159 THR B N   1 
ATOM   5494 C CA  . THR C 1 160 ? 24.753  44.915  -24.935 1.00 64.63  ? 159 THR B CA  1 
ATOM   5495 C C   . THR C 1 160 ? 24.741  45.571  -23.558 1.00 54.51  ? 159 THR B C   1 
ATOM   5496 O O   . THR C 1 160 ? 25.030  46.767  -23.437 1.00 47.28  ? 159 THR B O   1 
ATOM   5497 C CB  . THR C 1 160 ? 23.355  44.924  -25.549 1.00 51.74  ? 159 THR B CB  1 
ATOM   5498 O OG1 . THR C 1 160 ? 22.628  43.779  -25.092 1.00 59.29  ? 159 THR B OG1 1 
ATOM   5499 C CG2 . THR C 1 160 ? 23.446  44.883  -27.066 1.00 44.17  ? 159 THR B CG2 1 
ATOM   5500 N N   . VAL C 1 161 ? 24.421  44.807  -22.512 1.00 53.13  ? 160 VAL B N   1 
ATOM   5501 C CA  . VAL C 1 161 ? 24.470  45.350  -21.157 1.00 50.77  ? 160 VAL B CA  1 
ATOM   5502 C C   . VAL C 1 161 ? 25.899  45.726  -20.787 1.00 53.71  ? 160 VAL B C   1 
ATOM   5503 O O   . VAL C 1 161 ? 26.137  46.725  -20.097 1.00 55.48  ? 160 VAL B O   1 
ATOM   5504 C CB  . VAL C 1 161 ? 23.873  44.346  -20.153 1.00 47.27  ? 160 VAL B CB  1 
ATOM   5505 C CG1 . VAL C 1 161 ? 23.921  44.911  -18.739 1.00 39.50  ? 160 VAL B CG1 1 
ATOM   5506 C CG2 . VAL C 1 161 ? 22.447  43.991  -20.544 1.00 50.55  ? 160 VAL B CG2 1 
ATOM   5507 N N   . GLU C 1 162 ? 26.872  44.936  -21.246 1.00 56.69  ? 161 GLU B N   1 
ATOM   5508 C CA  . GLU C 1 162 ? 28.269  45.230  -20.942 1.00 53.99  ? 161 GLU B CA  1 
ATOM   5509 C C   . GLU C 1 162 ? 28.763  46.432  -21.737 1.00 46.06  ? 161 GLU B C   1 
ATOM   5510 O O   . GLU C 1 162 ? 29.422  47.320  -21.186 1.00 44.24  ? 161 GLU B O   1 
ATOM   5511 C CB  . GLU C 1 162 ? 29.139  44.003  -21.218 1.00 53.53  ? 161 GLU B CB  1 
ATOM   5512 C CG  . GLU C 1 162 ? 30.427  43.952  -20.401 1.00 55.07  ? 161 GLU B CG  1 
ATOM   5513 C CD  . GLU C 1 162 ? 30.195  44.132  -18.905 1.00 69.79  ? 161 GLU B CD  1 
ATOM   5514 O OE1 . GLU C 1 162 ? 29.231  43.545  -18.361 1.00 58.70  ? 161 GLU B OE1 1 
ATOM   5515 O OE2 . GLU C 1 162 ? 30.984  44.866  -18.271 1.00 68.08  ? 161 GLU B OE2 1 
ATOM   5516 N N   . LYS C 1 163 ? 28.454  46.478  -23.037 1.00 45.76  ? 162 LYS B N   1 
ATOM   5517 C CA  . LYS C 1 163 ? 28.879  47.605  -23.864 1.00 46.17  ? 162 LYS B CA  1 
ATOM   5518 C C   . LYS C 1 163 ? 28.357  48.925  -23.307 1.00 48.99  ? 162 LYS B C   1 
ATOM   5519 O O   . LYS C 1 163 ? 29.060  49.943  -23.333 1.00 39.47  ? 162 LYS B O   1 
ATOM   5520 C CB  . LYS C 1 163 ? 28.413  47.396  -25.306 1.00 44.56  ? 162 LYS B CB  1 
ATOM   5521 C CG  . LYS C 1 163 ? 29.004  48.370  -26.331 1.00 64.42  ? 162 LYS B CG  1 
ATOM   5522 C CD  . LYS C 1 163 ? 30.483  48.659  -26.116 1.00 59.64  ? 162 LYS B CD  1 
ATOM   5523 C CE  . LYS C 1 163 ? 30.938  49.829  -26.987 1.00 51.30  ? 162 LYS B CE  1 
ATOM   5524 N NZ  . LYS C 1 163 ? 32.341  50.248  -26.702 1.00 46.07  ? 162 LYS B NZ  1 
ATOM   5525 N N   . ILE C 1 164 ? 27.130  48.923  -22.783 1.00 51.88  ? 163 ILE B N   1 
ATOM   5526 C CA  . ILE C 1 164 ? 26.604  50.108  -22.114 1.00 42.96  ? 163 ILE B CA  1 
ATOM   5527 C C   . ILE C 1 164 ? 27.417  50.416  -20.863 1.00 35.72  ? 163 ILE B C   1 
ATOM   5528 O O   . ILE C 1 164 ? 27.688  51.583  -20.553 1.00 31.75  ? 163 ILE B O   1 
ATOM   5529 C CB  . ILE C 1 164 ? 25.110  49.917  -21.793 1.00 35.91  ? 163 ILE B CB  1 
ATOM   5530 C CG1 . ILE C 1 164 ? 24.293  49.908  -23.086 1.00 36.01  ? 163 ILE B CG1 1 
ATOM   5531 C CG2 . ILE C 1 164 ? 24.615  50.995  -20.829 1.00 33.47  ? 163 ILE B CG2 1 
ATOM   5532 C CD1 . ILE C 1 164 ? 24.070  51.276  -23.690 1.00 29.61  ? 163 ILE B CD1 1 
ATOM   5533 N N   . LYS C 1 165 ? 27.829  49.378  -20.133 1.00 43.42  ? 164 LYS B N   1 
ATOM   5534 C CA  . LYS C 1 165 ? 28.637  49.591  -18.938 1.00 36.84  ? 164 LYS B CA  1 
ATOM   5535 C C   . LYS C 1 165 ? 29.992  50.199  -19.283 1.00 42.04  ? 164 LYS B C   1 
ATOM   5536 O O   . LYS C 1 165 ? 30.510  51.031  -18.529 1.00 39.32  ? 164 LYS B O   1 
ATOM   5537 C CB  . LYS C 1 165 ? 28.813  48.273  -18.184 1.00 47.95  ? 164 LYS B CB  1 
ATOM   5538 C CG  . LYS C 1 165 ? 27.714  47.980  -17.178 1.00 44.10  ? 164 LYS B CG  1 
ATOM   5539 C CD  . LYS C 1 165 ? 28.145  46.919  -16.183 1.00 41.88  ? 164 LYS B CD  1 
ATOM   5540 C CE  . LYS C 1 165 ? 27.103  45.820  -16.063 1.00 52.90  ? 164 LYS B CE  1 
ATOM   5541 N NZ  . LYS C 1 165 ? 27.381  44.922  -14.907 1.00 57.69  ? 164 LYS B NZ  1 
ATOM   5542 N N   . GLU C 1 166 ? 30.583  49.800  -20.416 1.00 39.64  ? 165 GLU B N   1 
ATOM   5543 C CA  . GLU C 1 166 ? 31.881  50.354  -20.799 1.00 43.34  ? 165 GLU B CA  1 
ATOM   5544 C C   . GLU C 1 166 ? 31.743  51.792  -21.278 1.00 45.84  ? 165 GLU B C   1 
ATOM   5545 O O   . GLU C 1 166 ? 32.539  52.662  -20.903 1.00 45.91  ? 165 GLU B O   1 
ATOM   5546 C CB  . GLU C 1 166 ? 32.540  49.498  -21.882 1.00 44.60  ? 165 GLU B CB  1 
ATOM   5547 C CG  . GLU C 1 166 ? 32.325  48.002  -21.743 1.00 55.98  ? 165 GLU B CG  1 
ATOM   5548 C CD  . GLU C 1 166 ? 32.886  47.225  -22.920 1.00 65.56  ? 165 GLU B CD  1 
ATOM   5549 O OE1 . GLU C 1 166 ? 32.673  47.654  -24.077 1.00 61.67  ? 165 GLU B OE1 1 
ATOM   5550 O OE2 . GLU C 1 166 ? 33.536  46.184  -22.689 1.00 64.65  ? 165 GLU B OE2 1 
ATOM   5551 N N   . ILE C 1 167 ? 30.746  52.055  -22.124 1.00 39.62  ? 166 ILE B N   1 
ATOM   5552 C CA  . ILE C 1 167 ? 30.493  53.417  -22.587 1.00 38.33  ? 166 ILE B CA  1 
ATOM   5553 C C   . ILE C 1 167 ? 30.253  54.345  -21.403 1.00 36.66  ? 166 ILE B C   1 
ATOM   5554 O O   . ILE C 1 167 ? 30.686  55.504  -21.405 1.00 34.75  ? 166 ILE B O   1 
ATOM   5555 C CB  . ILE C 1 167 ? 29.312  53.426  -23.575 1.00 36.64  ? 166 ILE B CB  1 
ATOM   5556 C CG1 . ILE C 1 167 ? 29.695  52.693  -24.863 1.00 44.20  ? 166 ILE B CG1 1 
ATOM   5557 C CG2 . ILE C 1 167 ? 28.864  54.845  -23.880 1.00 35.97  ? 166 ILE B CG2 1 
ATOM   5558 C CD1 . ILE C 1 167 ? 28.523  52.417  -25.775 1.00 44.38  ? 166 ILE B CD1 1 
ATOM   5559 N N   . SER C 1 168 ? 29.585  53.842  -20.361 1.00 38.88  ? 167 SER B N   1 
ATOM   5560 C CA  . SER C 1 168 ? 29.312  54.663  -19.184 1.00 29.37  ? 167 SER B CA  1 
ATOM   5561 C C   . SER C 1 168 ? 30.601  55.093  -18.495 1.00 32.90  ? 167 SER B C   1 
ATOM   5562 O O   . SER C 1 168 ? 30.785  56.276  -18.185 1.00 28.86  ? 167 SER B O   1 
ATOM   5563 C CB  . SER C 1 168 ? 28.411  53.907  -18.207 1.00 35.76  ? 167 SER B CB  1 
ATOM   5564 O OG  . SER C 1 168 ? 27.106  53.736  -18.731 1.00 32.29  ? 167 SER B OG  1 
ATOM   5565 N N   . VAL C 1 169 ? 31.504  54.143  -18.232 1.00 35.56  ? 168 VAL B N   1 
ATOM   5566 C CA  . VAL C 1 169 ? 32.756  54.501  -17.568 1.00 37.30  ? 168 VAL B CA  1 
ATOM   5567 C C   . VAL C 1 169 ? 33.652  55.301  -18.505 1.00 36.14  ? 168 VAL B C   1 
ATOM   5568 O O   . VAL C 1 169 ? 34.462  56.120  -18.051 1.00 36.38  ? 168 VAL B O   1 
ATOM   5569 C CB  . VAL C 1 169 ? 33.475  53.247  -17.026 1.00 41.32  ? 168 VAL B CB  1 
ATOM   5570 C CG1 . VAL C 1 169 ? 32.492  52.316  -16.328 1.00 32.91  ? 168 VAL B CG1 1 
ATOM   5571 C CG2 . VAL C 1 169 ? 34.211  52.512  -18.137 1.00 44.04  ? 168 VAL B CG2 1 
ATOM   5572 N N   . ALA C 1 170 ? 33.512  55.100  -19.818 1.00 33.88  ? 169 ALA B N   1 
ATOM   5573 C CA  . ALA C 1 170 ? 34.310  55.843  -20.783 1.00 38.34  ? 169 ALA B CA  1 
ATOM   5574 C C   . ALA C 1 170 ? 33.979  57.329  -20.788 1.00 40.63  ? 169 ALA B C   1 
ATOM   5575 O O   . ALA C 1 170 ? 34.813  58.132  -21.219 1.00 40.94  ? 169 ALA B O   1 
ATOM   5576 C CB  . ALA C 1 170 ? 34.113  55.263  -22.185 1.00 39.43  ? 169 ALA B CB  1 
ATOM   5577 N N   . ILE C 1 171 ? 32.790  57.711  -20.329 1.00 32.93  ? 170 ILE B N   1 
ATOM   5578 C CA  . ILE C 1 171 ? 32.412  59.113  -20.233 1.00 35.73  ? 170 ILE B CA  1 
ATOM   5579 C C   . ILE C 1 171 ? 32.390  59.580  -18.778 1.00 32.34  ? 170 ILE B C   1 
ATOM   5580 O O   . ILE C 1 171 ? 31.795  60.608  -18.465 1.00 34.05  ? 170 ILE B O   1 
ATOM   5581 C CB  . ILE C 1 171 ? 31.070  59.387  -20.934 1.00 30.45  ? 170 ILE B CB  1 
ATOM   5582 C CG1 . ILE C 1 171 ? 29.957  58.519  -20.348 1.00 37.76  ? 170 ILE B CG1 1 
ATOM   5583 C CG2 . ILE C 1 171 ? 31.190  59.134  -22.427 1.00 35.34  ? 170 ILE B CG2 1 
ATOM   5584 C CD1 . ILE C 1 171 ? 28.575  58.928  -20.810 1.00 34.84  ? 170 ILE B CD1 1 
ATOM   5585 N N   . GLY C 1 172 ? 33.036  58.833  -17.885 1.00 26.79  ? 171 GLY B N   1 
ATOM   5586 C CA  . GLY C 1 172 ? 33.221  59.286  -16.522 1.00 21.11  ? 171 GLY B CA  1 
ATOM   5587 C C   . GLY C 1 172 ? 32.046  59.056  -15.606 1.00 27.89  ? 171 GLY B C   1 
ATOM   5588 O O   . GLY C 1 172 ? 31.962  59.695  -14.553 1.00 27.58  ? 171 GLY B O   1 
ATOM   5589 N N   . LYS C 1 173 ? 31.132  58.169  -15.975 1.00 33.76  ? 172 LYS B N   1 
ATOM   5590 C CA  . LYS C 1 173 ? 29.971  57.849  -15.164 1.00 32.56  ? 172 LYS B CA  1 
ATOM   5591 C C   . LYS C 1 173 ? 30.188  56.528  -14.432 1.00 34.59  ? 172 LYS B C   1 
ATOM   5592 O O   . LYS C 1 173 ? 31.133  55.783  -14.702 1.00 40.28  ? 172 LYS B O   1 
ATOM   5593 C CB  . LYS C 1 173 ? 28.714  57.783  -16.035 1.00 31.09  ? 172 LYS B CB  1 
ATOM   5594 C CG  . LYS C 1 173 ? 28.452  59.038  -16.852 1.00 29.76  ? 172 LYS B CG  1 
ATOM   5595 C CD  . LYS C 1 173 ? 28.115  60.215  -15.963 1.00 31.84  ? 172 LYS B CD  1 
ATOM   5596 C CE  . LYS C 1 173 ? 27.267  61.239  -16.700 1.00 26.80  ? 172 LYS B CE  1 
ATOM   5597 N NZ  . LYS C 1 173 ? 27.490  62.612  -16.164 1.00 31.28  ? 172 LYS B NZ  1 
ATOM   5598 N N   . ASN C 1 174 ? 29.293  56.245  -13.491 1.00 32.36  ? 173 ASN B N   1 
ATOM   5599 C CA  . ASN C 1 174 ? 29.342  55.020  -12.692 1.00 28.26  ? 173 ASN B CA  1 
ATOM   5600 C C   . ASN C 1 174 ? 28.101  54.188  -12.978 1.00 32.10  ? 173 ASN B C   1 
ATOM   5601 O O   . ASN C 1 174 ? 27.019  54.477  -12.436 1.00 28.26  ? 173 ASN B O   1 
ATOM   5602 C CB  . ASN C 1 174 ? 29.441  55.345  -11.203 1.00 31.71  ? 173 ASN B CB  1 
ATOM   5603 C CG  . ASN C 1 174 ? 30.750  56.026  -10.839 1.00 40.63  ? 173 ASN B CG  1 
ATOM   5604 O OD1 . ASN C 1 174 ? 31.733  55.364  -10.502 1.00 48.61  ? 173 ASN B OD1 1 
ATOM   5605 N ND2 . ASN C 1 174 ? 30.768  57.354  -10.907 1.00 46.26  ? 173 ASN B ND2 1 
ATOM   5606 N N   . PRO C 1 175 ? 28.196  53.154  -13.816 1.00 32.03  ? 174 PRO B N   1 
ATOM   5607 C CA  . PRO C 1 175 ? 27.001  52.375  -14.171 1.00 34.44  ? 174 PRO B CA  1 
ATOM   5608 C C   . PRO C 1 175 ? 26.651  51.359  -13.091 1.00 36.12  ? 174 PRO B C   1 
ATOM   5609 O O   . PRO C 1 175 ? 27.507  50.602  -12.625 1.00 37.02  ? 174 PRO B O   1 
ATOM   5610 C CB  . PRO C 1 175 ? 27.401  51.684  -15.481 1.00 26.00  ? 174 PRO B CB  1 
ATOM   5611 C CG  . PRO C 1 175 ? 28.887  51.567  -15.401 1.00 32.94  ? 174 PRO B CG  1 
ATOM   5612 C CD  . PRO C 1 175 ? 29.389  52.726  -14.567 1.00 28.16  ? 174 PRO B CD  1 
ATOM   5613 N N   . VAL C 1 176 ? 25.381  51.353  -12.696 1.00 28.00  ? 175 VAL B N   1 
ATOM   5614 C CA  . VAL C 1 176 ? 24.829  50.360  -11.784 1.00 24.35  ? 175 VAL B CA  1 
ATOM   5615 C C   . VAL C 1 176 ? 23.750  49.605  -12.541 1.00 28.74  ? 175 VAL B C   1 
ATOM   5616 O O   . VAL C 1 176 ? 22.785  50.213  -13.022 1.00 32.65  ? 175 VAL B O   1 
ATOM   5617 C CB  . VAL C 1 176 ? 24.255  51.003  -10.511 1.00 35.48  ? 175 VAL B CB  1 
ATOM   5618 C CG1 . VAL C 1 176 ? 23.578  49.948  -9.649  1.00 31.15  ? 175 VAL B CG1 1 
ATOM   5619 C CG2 . VAL C 1 176 ? 25.349  51.712  -9.730  1.00 29.35  ? 175 VAL B CG2 1 
ATOM   5620 N N   . GLN C 1 177 ? 23.911  48.289  -12.656 1.00 29.79  ? 176 GLN B N   1 
ATOM   5621 C CA  . GLN C 1 177 ? 22.911  47.479  -13.336 1.00 28.84  ? 176 GLN B CA  1 
ATOM   5622 C C   . GLN C 1 177 ? 21.729  47.211  -12.417 1.00 35.13  ? 176 GLN B C   1 
ATOM   5623 O O   . GLN C 1 177 ? 21.888  47.023  -11.207 1.00 41.75  ? 176 GLN B O   1 
ATOM   5624 C CB  . GLN C 1 177 ? 23.505  46.158  -13.820 1.00 36.28  ? 176 GLN B CB  1 
ATOM   5625 C CG  . GLN C 1 177 ? 22.669  45.505  -14.909 1.00 38.05  ? 176 GLN B CG  1 
ATOM   5626 C CD  . GLN C 1 177 ? 23.239  44.185  -15.378 1.00 48.32  ? 176 GLN B CD  1 
ATOM   5627 O OE1 . GLN C 1 177 ? 24.427  43.912  -15.208 1.00 56.96  ? 176 GLN B OE1 1 
ATOM   5628 N NE2 . GLN C 1 177 ? 22.393  43.361  -15.986 1.00 36.01  ? 176 GLN B NE2 1 
ATOM   5629 N N   . VAL C 1 178 ? 20.537  47.196  -13.003 1.00 24.58  ? 177 VAL B N   1 
ATOM   5630 C CA  . VAL C 1 178 ? 19.287  47.112  -12.260 1.00 26.29  ? 177 VAL B CA  1 
ATOM   5631 C C   . VAL C 1 178 ? 18.327  46.234  -13.051 1.00 31.35  ? 177 VAL B C   1 
ATOM   5632 O O   . VAL C 1 178 ? 18.203  46.383  -14.271 1.00 36.01  ? 177 VAL B O   1 
ATOM   5633 C CB  . VAL C 1 178 ? 18.687  48.514  -12.022 1.00 25.78  ? 177 VAL B CB  1 
ATOM   5634 C CG1 . VAL C 1 178 ? 17.216  48.429  -11.659 1.00 41.38  ? 177 VAL B CG1 1 
ATOM   5635 C CG2 . VAL C 1 178 ? 19.472  49.256  -10.948 1.00 33.98  ? 177 VAL B CG2 1 
ATOM   5636 N N   . ASN C 1 179 ? 17.661  45.310  -12.366 1.00 31.48  ? 178 ASN B N   1 
ATOM   5637 C CA  . ASN C 1 179 ? 16.681  44.464  -13.027 1.00 30.68  ? 178 ASN B CA  1 
ATOM   5638 C C   . ASN C 1 179 ? 15.418  45.259  -13.343 1.00 36.10  ? 178 ASN B C   1 
ATOM   5639 O O   . ASN C 1 179 ? 15.090  46.241  -12.670 1.00 28.87  ? 178 ASN B O   1 
ATOM   5640 C CB  . ASN C 1 179 ? 16.342  43.258  -12.152 1.00 30.15  ? 178 ASN B CB  1 
ATOM   5641 C CG  . ASN C 1 179 ? 17.414  42.190  -12.198 1.00 33.49  ? 178 ASN B CG  1 
ATOM   5642 O OD1 . ASN C 1 179 ? 18.367  42.282  -12.973 1.00 39.05  ? 178 ASN B OD1 1 
ATOM   5643 N ND2 . ASN C 1 179 ? 17.267  41.169  -11.361 1.00 55.27  ? 178 ASN B ND2 1 
ATOM   5644 N N   . GLU C 1 180 ? 14.705  44.816  -14.376 1.00 31.66  ? 179 GLU B N   1 
ATOM   5645 C CA  . GLU C 1 180 ? 13.551  45.550  -14.885 1.00 28.61  ? 179 GLU B CA  1 
ATOM   5646 C C   . GLU C 1 180 ? 12.406  45.522  -13.879 1.00 34.79  ? 179 GLU B C   1 
ATOM   5647 O O   . GLU C 1 180 ? 11.890  44.453  -13.538 1.00 40.08  ? 179 GLU B O   1 
ATOM   5648 C CB  . GLU C 1 180 ? 13.100  44.956  -16.215 1.00 30.70  ? 179 GLU B CB  1 
ATOM   5649 C CG  . GLU C 1 180 ? 12.678  45.982  -17.251 1.00 49.28  ? 179 GLU B CG  1 
ATOM   5650 C CD  . GLU C 1 180 ? 11.712  45.411  -18.273 1.00 41.35  ? 179 GLU B CD  1 
ATOM   5651 O OE1 . GLU C 1 180 ? 11.863  44.228  -18.643 1.00 51.05  ? 179 GLU B OE1 1 
ATOM   5652 O OE2 . GLU C 1 180 ? 10.807  46.146  -18.713 1.00 45.53  ? 179 GLU B OE2 1 
ATOM   5653 N N   . ALA C 1 181 ? 12.008  46.702  -13.413 1.00 27.53  ? 180 ALA B N   1 
ATOM   5654 C CA  . ALA C 1 181 ? 10.847  46.860  -12.548 1.00 24.09  ? 180 ALA B CA  1 
ATOM   5655 C C   . ALA C 1 181 ? 10.433  48.321  -12.601 1.00 27.47  ? 180 ALA B C   1 
ATOM   5656 O O   . ALA C 1 181 ? 11.238  49.199  -12.925 1.00 26.89  ? 180 ALA B O   1 
ATOM   5657 C CB  . ALA C 1 181 ? 11.136  46.417  -11.108 1.00 21.34  ? 180 ALA B CB  1 
ATOM   5658 N N   . ALA C 1 182 ? 9.164   48.570  -12.291 1.00 21.83  ? 181 ALA B N   1 
ATOM   5659 C CA  . ALA C 1 182 ? 8.625   49.922  -12.375 1.00 26.83  ? 181 ALA B CA  1 
ATOM   5660 C C   . ALA C 1 182 ? 9.438   50.881  -11.511 1.00 33.41  ? 181 ALA B C   1 
ATOM   5661 O O   . ALA C 1 182 ? 9.527   50.715  -10.289 1.00 25.66  ? 181 ALA B O   1 
ATOM   5662 C CB  . ALA C 1 182 ? 7.160   49.930  -11.948 1.00 20.48  ? 181 ALA B CB  1 
ATOM   5663 N N   . GLY C 1 183 ? 10.046  51.877  -12.156 1.00 25.15  ? 182 GLY B N   1 
ATOM   5664 C CA  . GLY C 1 183 ? 10.815  52.888  -11.469 1.00 24.77  ? 182 GLY B CA  1 
ATOM   5665 C C   . GLY C 1 183 ? 12.257  52.525  -11.199 1.00 28.00  ? 182 GLY B C   1 
ATOM   5666 O O   . GLY C 1 183 ? 13.011  53.380  -10.713 1.00 23.33  ? 182 GLY B O   1 
ATOM   5667 N N   . PHE C 1 184 ? 12.662  51.289  -11.503 1.00 20.40  ? 183 PHE B N   1 
ATOM   5668 C CA  . PHE C 1 184 ? 14.012  50.809  -11.232 1.00 22.11  ? 183 PHE B CA  1 
ATOM   5669 C C   . PHE C 1 184 ? 14.345  51.044  -9.763  1.00 26.94  ? 183 PHE B C   1 
ATOM   5670 O O   . PHE C 1 184 ? 13.607  50.586  -8.885  1.00 28.99  ? 183 PHE B O   1 
ATOM   5671 C CB  . PHE C 1 184 ? 15.010  51.481  -12.179 1.00 23.15  ? 183 PHE B CB  1 
ATOM   5672 C CG  . PHE C 1 184 ? 14.503  51.596  -13.589 1.00 27.30  ? 183 PHE B CG  1 
ATOM   5673 C CD1 . PHE C 1 184 ? 14.100  50.468  -14.283 1.00 28.74  ? 183 PHE B CD1 1 
ATOM   5674 C CD2 . PHE C 1 184 ? 14.398  52.830  -14.209 1.00 31.66  ? 183 PHE B CD2 1 
ATOM   5675 C CE1 . PHE C 1 184 ? 13.620  50.564  -15.577 1.00 30.46  ? 183 PHE B CE1 1 
ATOM   5676 C CE2 . PHE C 1 184 ? 13.913  52.933  -15.498 1.00 28.16  ? 183 PHE B CE2 1 
ATOM   5677 C CZ  . PHE C 1 184 ? 13.525  51.799  -16.184 1.00 30.91  ? 183 PHE B CZ  1 
ATOM   5678 N N   . VAL C 1 185 ? 15.423  51.767  -9.474  1.00 25.36  ? 184 VAL B N   1 
ATOM   5679 C CA  . VAL C 1 185 ? 15.847  52.023  -8.098  1.00 29.93  ? 184 VAL B CA  1 
ATOM   5680 C C   . VAL C 1 185 ? 15.587  53.471  -7.695  1.00 25.85  ? 184 VAL B C   1 
ATOM   5681 O O   . VAL C 1 185 ? 14.810  53.736  -6.776  1.00 29.67  ? 184 VAL B O   1 
ATOM   5682 C CB  . VAL C 1 185 ? 17.330  51.644  -7.889  1.00 27.57  ? 184 VAL B CB  1 
ATOM   5683 C CG1 . VAL C 1 185 ? 17.829  52.194  -6.559  1.00 20.11  ? 184 VAL B CG1 1 
ATOM   5684 C CG2 . VAL C 1 185 ? 17.509  50.139  -7.957  1.00 26.13  ? 184 VAL B CG2 1 
ATOM   5685 N N   . VAL C 1 186 ? 16.231  54.424  -8.372  1.00 22.79  ? 185 VAL B N   1 
ATOM   5686 C CA  . VAL C 1 186 ? 16.242  55.803  -7.889  1.00 23.61  ? 185 VAL B CA  1 
ATOM   5687 C C   . VAL C 1 186 ? 14.847  56.412  -7.954  1.00 27.89  ? 185 VAL B C   1 
ATOM   5688 O O   . VAL C 1 186 ? 14.339  56.941  -6.957  1.00 23.96  ? 185 VAL B O   1 
ATOM   5689 C CB  . VAL C 1 186 ? 17.257  56.645  -8.680  1.00 22.94  ? 185 VAL B CB  1 
ATOM   5690 C CG1 . VAL C 1 186 ? 17.177  58.098  -8.240  1.00 23.83  ? 185 VAL B CG1 1 
ATOM   5691 C CG2 . VAL C 1 186 ? 18.663  56.101  -8.484  1.00 21.20  ? 185 VAL B CG2 1 
ATOM   5692 N N   . ASN C 1 187 ? 14.211  56.353  -9.129  1.00 22.22  ? 186 ASN B N   1 
ATOM   5693 C CA  . ASN C 1 187 ? 12.896  56.964  -9.291  1.00 22.90  ? 186 ASN B CA  1 
ATOM   5694 C C   . ASN C 1 187 ? 11.862  56.315  -8.382  1.00 21.42  ? 186 ASN B C   1 
ATOM   5695 O O   . ASN C 1 187 ? 10.994  57.002  -7.833  1.00 24.03  ? 186 ASN B O   1 
ATOM   5696 C CB  . ASN C 1 187 ? 12.446  56.874  -10.748 1.00 22.55  ? 186 ASN B CB  1 
ATOM   5697 C CG  . ASN C 1 187 ? 13.006  57.995  -11.602 1.00 29.13  ? 186 ASN B CG  1 
ATOM   5698 O OD1 . ASN C 1 187 ? 13.460  59.019  -11.089 1.00 27.07  ? 186 ASN B OD1 1 
ATOM   5699 N ND2 . ASN C 1 187 ? 12.970  57.808  -12.913 1.00 22.75  ? 186 ASN B ND2 1 
ATOM   5700 N N   . ARG C 1 188 ? 11.934  54.992  -8.215  1.00 18.43  ? 187 ARG B N   1 
ATOM   5701 C CA  . ARG C 1 188 ? 10.997  54.315  -7.325  1.00 21.09  ? 187 ARG B CA  1 
ATOM   5702 C C   . ARG C 1 188 ? 11.127  54.825  -5.896  1.00 25.85  ? 187 ARG B C   1 
ATOM   5703 O O   . ARG C 1 188 ? 10.143  54.854  -5.148  1.00 22.78  ? 187 ARG B O   1 
ATOM   5704 C CB  . ARG C 1 188 ? 11.229  52.807  -7.379  1.00 26.31  ? 187 ARG B CB  1 
ATOM   5705 C CG  . ARG C 1 188 ? 10.428  52.007  -6.368  1.00 24.80  ? 187 ARG B CG  1 
ATOM   5706 C CD  . ARG C 1 188 ? 10.194  50.597  -6.870  1.00 28.79  ? 187 ARG B CD  1 
ATOM   5707 N NE  . ARG C 1 188 ? 9.776   49.704  -5.799  1.00 35.30  ? 187 ARG B NE  1 
ATOM   5708 C CZ  . ARG C 1 188 ? 9.882   48.383  -5.841  1.00 37.54  ? 187 ARG B CZ  1 
ATOM   5709 N NH1 . ARG C 1 188 ? 10.387  47.763  -6.896  1.00 28.32  ? 187 ARG B NH1 1 
ATOM   5710 N NH2 . ARG C 1 188 ? 9.475   47.666  -4.797  1.00 29.89  ? 187 ARG B NH2 1 
ATOM   5711 N N   . ILE C 1 189 ? 12.327  55.241  -5.508  1.00 25.19  ? 188 ILE B N   1 
ATOM   5712 C CA  . ILE C 1 189 ? 12.570  55.768  -4.173  1.00 22.78  ? 188 ILE B CA  1 
ATOM   5713 C C   . ILE C 1 189 ? 12.337  57.272  -4.119  1.00 27.02  ? 188 ILE B C   1 
ATOM   5714 O O   . ILE C 1 189 ? 11.737  57.784  -3.171  1.00 28.15  ? 188 ILE B O   1 
ATOM   5715 C CB  . ILE C 1 189 ? 14.005  55.406  -3.741  1.00 24.77  ? 188 ILE B CB  1 
ATOM   5716 C CG1 . ILE C 1 189 ? 14.130  53.912  -3.435  1.00 23.40  ? 188 ILE B CG1 1 
ATOM   5717 C CG2 . ILE C 1 189 ? 14.418  56.212  -2.542  1.00 26.36  ? 188 ILE B CG2 1 
ATOM   5718 C CD1 . ILE C 1 189 ? 15.559  53.472  -3.148  1.00 22.12  ? 188 ILE B CD1 1 
ATOM   5719 N N   . LEU C 1 190 ? 12.790  57.996  -5.143  1.00 29.14  ? 189 LEU B N   1 
ATOM   5720 C CA  . LEU C 1 190 ? 12.852  59.450  -5.061  1.00 23.38  ? 189 LEU B CA  1 
ATOM   5721 C C   . LEU C 1 190 ? 11.498  60.105  -5.331  1.00 31.04  ? 189 LEU B C   1 
ATOM   5722 O O   . LEU C 1 190 ? 11.148  61.092  -4.675  1.00 23.17  ? 189 LEU B O   1 
ATOM   5723 C CB  . LEU C 1 190 ? 13.908  59.972  -6.038  1.00 21.85  ? 189 LEU B CB  1 
ATOM   5724 C CG  . LEU C 1 190 ? 14.326  61.433  -5.909  1.00 27.24  ? 189 LEU B CG  1 
ATOM   5725 C CD1 . LEU C 1 190 ? 15.141  61.643  -4.641  1.00 42.87  ? 189 LEU B CD1 1 
ATOM   5726 C CD2 . LEU C 1 190 ? 15.114  61.862  -7.134  1.00 39.05  ? 189 LEU B CD2 1 
ATOM   5727 N N   . ILE C 1 191 ? 10.722  59.583  -6.278  1.00 21.23  ? 190 ILE B N   1 
ATOM   5728 C CA  . ILE C 1 191 ? 9.493   60.263  -6.695  1.00 25.11  ? 190 ILE B CA  1 
ATOM   5729 C C   . ILE C 1 191 ? 8.378   60.128  -5.659  1.00 21.76  ? 190 ILE B C   1 
ATOM   5730 O O   . ILE C 1 191 ? 7.665   61.114  -5.424  1.00 24.77  ? 190 ILE B O   1 
ATOM   5731 C CB  . ILE C 1 191 ? 9.015   59.777  -8.072  1.00 20.90  ? 190 ILE B CB  1 
ATOM   5732 C CG1 . ILE C 1 191 ? 10.173  59.778  -9.067  1.00 21.93  ? 190 ILE B CG1 1 
ATOM   5733 C CG2 . ILE C 1 191 ? 7.914   60.692  -8.594  1.00 13.10  ? 190 ILE B CG2 1 
ATOM   5734 C CD1 . ILE C 1 191 ? 10.848  61.123  -9.208  1.00 23.65  ? 190 ILE B CD1 1 
ATOM   5735 N N   . PRO C 1 192 ? 8.156   58.965  -5.028  1.00 15.52  ? 191 PRO B N   1 
ATOM   5736 C CA  . PRO C 1 192 ? 7.179   58.941  -3.926  1.00 26.03  ? 191 PRO B CA  1 
ATOM   5737 C C   . PRO C 1 192 ? 7.579   59.847  -2.780  1.00 21.68  ? 191 PRO B C   1 
ATOM   5738 O O   . PRO C 1 192 ? 6.709   60.414  -2.107  1.00 19.28  ? 191 PRO B O   1 
ATOM   5739 C CB  . PRO C 1 192 ? 7.154   57.464  -3.506  1.00 18.44  ? 191 PRO B CB  1 
ATOM   5740 C CG  . PRO C 1 192 ? 7.588   56.729  -4.726  1.00 18.92  ? 191 PRO B CG  1 
ATOM   5741 C CD  . PRO C 1 192 ? 8.640   57.606  -5.335  1.00 15.40  ? 191 PRO B CD  1 
ATOM   5742 N N   . MET C 1 193 ? 8.882   60.004  -2.548  1.00 18.71  ? 192 MET B N   1 
ATOM   5743 C CA  . MET C 1 193 ? 9.371   60.997  -1.599  1.00 21.21  ? 192 MET B CA  1 
ATOM   5744 C C   . MET C 1 193 ? 8.822   62.380  -1.937  1.00 26.53  ? 192 MET B C   1 
ATOM   5745 O O   . MET C 1 193 ? 8.291   63.086  -1.070  1.00 24.20  ? 192 MET B O   1 
ATOM   5746 C CB  . MET C 1 193 ? 10.902  60.983  -1.618  1.00 27.17  ? 192 MET B CB  1 
ATOM   5747 C CG  . MET C 1 193 ? 11.581  61.719  -0.499  1.00 38.69  ? 192 MET B CG  1 
ATOM   5748 S SD  . MET C 1 193 ? 13.196  62.343  -0.989  1.00 60.18  ? 192 MET B SD  1 
ATOM   5749 C CE  . MET C 1 193 ? 12.762  63.305  -2.441  1.00 29.79  ? 192 MET B CE  1 
ATOM   5750 N N   . ILE C 1 194 ? 8.921   62.774  -3.211  1.00 25.35  ? 193 ILE B N   1 
ATOM   5751 C CA  . ILE C 1 194 ? 8.316   64.028  -3.655  1.00 23.60  ? 193 ILE B CA  1 
ATOM   5752 C C   . ILE C 1 194 ? 6.805   63.972  -3.488  1.00 20.68  ? 193 ILE B C   1 
ATOM   5753 O O   . ILE C 1 194 ? 6.180   64.923  -3.002  1.00 22.75  ? 193 ILE B O   1 
ATOM   5754 C CB  . ILE C 1 194 ? 8.707   64.327  -5.115  1.00 23.93  ? 193 ILE B CB  1 
ATOM   5755 C CG1 . ILE C 1 194 ? 10.218  64.537  -5.239  1.00 23.02  ? 193 ILE B CG1 1 
ATOM   5756 C CG2 . ILE C 1 194 ? 7.947   65.537  -5.636  1.00 15.59  ? 193 ILE B CG2 1 
ATOM   5757 C CD1 . ILE C 1 194 ? 10.715  64.544  -6.673  1.00 21.48  ? 193 ILE B CD1 1 
ATOM   5758 N N   . ASN C 1 195 ? 6.197   62.854  -3.890  1.00 25.16  ? 194 ASN B N   1 
ATOM   5759 C CA  . ASN C 1 195 ? 4.756   62.690  -3.742  1.00 21.34  ? 194 ASN B CA  1 
ATOM   5760 C C   . ASN C 1 195 ? 4.328   62.837  -2.288  1.00 19.20  ? 194 ASN B C   1 
ATOM   5761 O O   . ASN C 1 195 ? 3.345   63.526  -1.990  1.00 20.15  ? 194 ASN B O   1 
ATOM   5762 C CB  . ASN C 1 195 ? 4.334   61.329  -4.292  1.00 19.74  ? 194 ASN B CB  1 
ATOM   5763 C CG  . ASN C 1 195 ? 2.842   61.222  -4.486  1.00 21.53  ? 194 ASN B CG  1 
ATOM   5764 O OD1 . ASN C 1 195 ? 2.238   62.038  -5.180  1.00 25.19  ? 194 ASN B OD1 1 
ATOM   5765 N ND2 . ASN C 1 195 ? 2.234   60.213  -3.872  1.00 28.96  ? 194 ASN B ND2 1 
ATOM   5766 N N   . GLU C 1 196 ? 5.058   62.199  -1.370  1.00 14.34  ? 195 GLU B N   1 
ATOM   5767 C CA  . GLU C 1 196 ? 4.760   62.353  0.050   1.00 20.41  ? 195 GLU B CA  1 
ATOM   5768 C C   . GLU C 1 196 ? 4.844   63.811  0.478   1.00 20.65  ? 195 GLU B C   1 
ATOM   5769 O O   . GLU C 1 196 ? 3.991   64.295  1.229   1.00 17.31  ? 195 GLU B O   1 
ATOM   5770 C CB  . GLU C 1 196 ? 5.719   61.509  0.885   1.00 16.32  ? 195 GLU B CB  1 
ATOM   5771 C CG  . GLU C 1 196 ? 5.306   61.378  2.337   1.00 23.89  ? 195 GLU B CG  1 
ATOM   5772 C CD  . GLU C 1 196 ? 3.997   60.631  2.484   1.00 39.64  ? 195 GLU B CD  1 
ATOM   5773 O OE1 . GLU C 1 196 ? 3.730   59.752  1.637   1.00 31.24  ? 195 GLU B OE1 1 
ATOM   5774 O OE2 . GLU C 1 196 ? 3.246   60.910  3.445   1.00 34.93  ? 195 GLU B OE2 1 
ATOM   5775 N N   . ALA C 1 197 ? 5.865   64.528  0.004   1.00 21.94  ? 196 ALA B N   1 
ATOM   5776 C CA  . ALA C 1 197 ? 6.022   65.927  0.385   1.00 17.20  ? 196 ALA B CA  1 
ATOM   5777 C C   . ALA C 1 197 ? 4.808   66.753  -0.018  1.00 18.45  ? 196 ALA B C   1 
ATOM   5778 O O   . ALA C 1 197 ? 4.396   67.661  0.712   1.00 18.68  ? 196 ALA B O   1 
ATOM   5779 C CB  . ALA C 1 197 ? 7.291   66.497  -0.241  1.00 18.89  ? 196 ALA B CB  1 
ATOM   5780 N N   . ALA C 1 198 ? 4.215   66.452  -1.175  1.00 25.29  ? 197 ALA B N   1 
ATOM   5781 C CA  . ALA C 1 198 ? 3.027   67.188  -1.592  1.00 27.05  ? 197 ALA B CA  1 
ATOM   5782 C C   . ALA C 1 198 ? 1.836   66.851  -0.704  1.00 24.20  ? 197 ALA B C   1 
ATOM   5783 O O   . ALA C 1 198 ? 1.057   67.738  -0.340  1.00 23.20  ? 197 ALA B O   1 
ATOM   5784 C CB  . ALA C 1 198 ? 2.710   66.897  -3.057  1.00 20.47  ? 197 ALA B CB  1 
ATOM   5785 N N   . PHE C 1 199 ? 1.683   65.571  -0.349  1.00 21.77  ? 198 PHE B N   1 
ATOM   5786 C CA  . PHE C 1 199 ? 0.639   65.171  0.591   1.00 21.78  ? 198 PHE B CA  1 
ATOM   5787 C C   . PHE C 1 199 ? 0.766   65.924  1.909   1.00 25.73  ? 198 PHE B C   1 
ATOM   5788 O O   . PHE C 1 199 ? -0.242  66.331  2.501   1.00 25.86  ? 198 PHE B O   1 
ATOM   5789 C CB  . PHE C 1 199 ? 0.708   63.664  0.840   1.00 17.64  ? 198 PHE B CB  1 
ATOM   5790 C CG  . PHE C 1 199 ? -0.204  62.861  -0.038  1.00 20.39  ? 198 PHE B CG  1 
ATOM   5791 C CD1 . PHE C 1 199 ? -1.576  63.050  0.006   1.00 27.19  ? 198 PHE B CD1 1 
ATOM   5792 C CD2 . PHE C 1 199 ? 0.312   61.918  -0.915  1.00 17.44  ? 198 PHE B CD2 1 
ATOM   5793 C CE1 . PHE C 1 199 ? -2.418  62.305  -0.806  1.00 23.74  ? 198 PHE B CE1 1 
ATOM   5794 C CE2 . PHE C 1 199 ? -0.524  61.170  -1.725  1.00 15.31  ? 198 PHE B CE2 1 
ATOM   5795 C CZ  . PHE C 1 199 ? -1.890  61.366  -1.672  1.00 19.53  ? 198 PHE B CZ  1 
ATOM   5796 N N   . ILE C 1 200 ? 1.999   66.114  2.386   1.00 22.66  ? 199 ILE B N   1 
ATOM   5797 C CA  . ILE C 1 200 ? 2.207   66.811  3.653   1.00 27.90  ? 199 ILE B CA  1 
ATOM   5798 C C   . ILE C 1 200 ? 1.737   68.256  3.544   1.00 24.89  ? 199 ILE B C   1 
ATOM   5799 O O   . ILE C 1 200 ? 1.108   68.794  4.464   1.00 27.72  ? 199 ILE B O   1 
ATOM   5800 C CB  . ILE C 1 200 ? 3.685   66.712  4.077   1.00 26.88  ? 199 ILE B CB  1 
ATOM   5801 C CG1 . ILE C 1 200 ? 3.971   65.327  4.657   1.00 24.02  ? 199 ILE B CG1 1 
ATOM   5802 C CG2 . ILE C 1 200 ? 4.036   67.778  5.105   1.00 24.33  ? 199 ILE B CG2 1 
ATOM   5803 C CD1 . ILE C 1 200 ? 5.440   65.016  4.774   1.00 22.46  ? 199 ILE B CD1 1 
ATOM   5804 N N   . LYS C 1 201 ? 2.014   68.901  2.408   1.00 22.44  ? 200 LYS B N   1 
ATOM   5805 C CA  . LYS C 1 201 ? 1.517   70.255  2.192   1.00 25.19  ? 200 LYS B CA  1 
ATOM   5806 C C   . LYS C 1 201 ? -0.002  70.268  2.089   1.00 24.72  ? 200 LYS B C   1 
ATOM   5807 O O   . LYS C 1 201 ? -0.668  71.110  2.704   1.00 23.61  ? 200 LYS B O   1 
ATOM   5808 C CB  . LYS C 1 201 ? 2.153   70.847  0.932   1.00 27.24  ? 200 LYS B CB  1 
ATOM   5809 C CG  . LYS C 1 201 ? 1.429   72.059  0.371   1.00 25.98  ? 200 LYS B CG  1 
ATOM   5810 C CD  . LYS C 1 201 ? 1.677   73.287  1.236   1.00 34.19  ? 200 LYS B CD  1 
ATOM   5811 C CE  . LYS C 1 201 ? 0.736   74.423  0.869   1.00 31.20  ? 200 LYS B CE  1 
ATOM   5812 N NZ  . LYS C 1 201 ? 0.592   75.389  1.998   1.00 36.38  ? 200 LYS B NZ  1 
ATOM   5813 N N   . MET C 1 202 ? -0.568  69.319  1.340   1.00 26.39  ? 201 MET B N   1 
ATOM   5814 C CA  . MET C 1 202 ? -2.009  69.299  1.119   1.00 28.26  ? 201 MET B CA  1 
ATOM   5815 C C   . MET C 1 202 ? -2.771  69.101  2.426   1.00 22.24  ? 201 MET B C   1 
ATOM   5816 O O   . MET C 1 202 ? -3.826  69.710  2.637   1.00 27.63  ? 201 MET B O   1 
ATOM   5817 C CB  . MET C 1 202 ? -2.355  68.204  0.110   1.00 22.36  ? 201 MET B CB  1 
ATOM   5818 C CG  . MET C 1 202 ? -3.839  67.990  -0.111  1.00 27.96  ? 201 MET B CG  1 
ATOM   5819 S SD  . MET C 1 202 ? -4.130  66.646  -1.280  1.00 44.12  ? 201 MET B SD  1 
ATOM   5820 C CE  . MET C 1 202 ? -4.536  65.321  -0.150  1.00 35.94  ? 201 MET B CE  1 
ATOM   5821 N N   . GLU C 1 203 ? -2.249  68.271  3.322   1.00 27.92  ? 202 GLU B N   1 
ATOM   5822 C CA  . GLU C 1 203 ? -2.882  68.059  4.616   1.00 28.57  ? 202 GLU B CA  1 
ATOM   5823 C C   . GLU C 1 203 ? -2.485  69.104  5.650   1.00 27.24  ? 202 GLU B C   1 
ATOM   5824 O O   . GLU C 1 203 ? -2.900  68.996  6.809   1.00 37.48  ? 202 GLU B O   1 
ATOM   5825 C CB  . GLU C 1 203 ? -2.561  66.656  5.128   1.00 22.01  ? 202 GLU B CB  1 
ATOM   5826 C CG  . GLU C 1 203 ? -3.226  65.574  4.301   1.00 32.23  ? 202 GLU B CG  1 
ATOM   5827 C CD  . GLU C 1 203 ? -2.539  64.240  4.429   1.00 42.52  ? 202 GLU B CD  1 
ATOM   5828 O OE1 . GLU C 1 203 ? -1.778  64.056  5.404   1.00 32.23  ? 202 GLU B OE1 1 
ATOM   5829 O OE2 . GLU C 1 203 ? -2.754  63.379  3.548   1.00 51.22  ? 202 GLU B OE2 1 
ATOM   5830 N N   . GLY C 1 204 ? -1.699  70.107  5.262   1.00 27.90  ? 203 GLY B N   1 
ATOM   5831 C CA  . GLY C 1 204 ? -1.441  71.237  6.131   1.00 23.66  ? 203 GLY B CA  1 
ATOM   5832 C C   . GLY C 1 204 ? -0.484  70.979  7.269   1.00 29.28  ? 203 GLY B C   1 
ATOM   5833 O O   . GLY C 1 204 ? -0.481  71.738  8.242   1.00 29.27  ? 203 GLY B O   1 
ATOM   5834 N N   . VAL C 1 205 ? 0.335   69.930  7.180   1.00 30.38  ? 204 VAL B N   1 
ATOM   5835 C CA  . VAL C 1 205 ? 1.296   69.652  8.243   1.00 26.28  ? 204 VAL B CA  1 
ATOM   5836 C C   . VAL C 1 205 ? 2.339   70.758  8.322   1.00 28.35  ? 204 VAL B C   1 
ATOM   5837 O O   . VAL C 1 205 ? 2.802   71.120  9.411   1.00 33.28  ? 204 VAL B O   1 
ATOM   5838 C CB  . VAL C 1 205 ? 1.942   68.273  8.024   1.00 28.25  ? 204 VAL B CB  1 
ATOM   5839 C CG1 . VAL C 1 205 ? 2.885   67.944  9.165   1.00 21.72  ? 204 VAL B CG1 1 
ATOM   5840 C CG2 . VAL C 1 205 ? 0.868   67.204  7.890   1.00 26.98  ? 204 VAL B CG2 1 
ATOM   5841 N N   . SER C 1 206 ? 2.719   71.315  7.176   1.00 30.50  ? 205 SER B N   1 
ATOM   5842 C CA  . SER C 1 206 ? 3.672   72.413  7.109   1.00 31.01  ? 205 SER B CA  1 
ATOM   5843 C C   . SER C 1 206 ? 3.474   73.113  5.772   1.00 25.49  ? 205 SER B C   1 
ATOM   5844 O O   . SER C 1 206 ? 2.751   72.629  4.899   1.00 29.22  ? 205 SER B O   1 
ATOM   5845 C CB  . SER C 1 206 ? 5.115   71.919  7.273   1.00 32.14  ? 205 SER B CB  1 
ATOM   5846 O OG  . SER C 1 206 ? 6.041   72.996  7.278   1.00 29.89  ? 205 SER B OG  1 
ATOM   5847 N N   . ASP C 1 207 ? 4.116   74.269  5.626   1.00 26.66  ? 206 ASP B N   1 
ATOM   5848 C CA  . ASP C 1 207 ? 4.051   75.020  4.384   1.00 37.60  ? 206 ASP B CA  1 
ATOM   5849 C C   . ASP C 1 207 ? 5.182   74.582  3.452   1.00 30.96  ? 206 ASP B C   1 
ATOM   5850 O O   . ASP C 1 207 ? 6.044   73.776  3.815   1.00 31.40  ? 206 ASP B O   1 
ATOM   5851 C CB  . ASP C 1 207 ? 4.096   76.523  4.663   1.00 34.67  ? 206 ASP B CB  1 
ATOM   5852 C CG  . ASP C 1 207 ? 5.384   76.958  5.341   1.00 41.88  ? 206 ASP B CG  1 
ATOM   5853 O OD1 . ASP C 1 207 ? 6.107   76.092  5.880   1.00 48.17  ? 206 ASP B OD1 1 
ATOM   5854 O OD2 . ASP C 1 207 ? 5.677   78.173  5.329   1.00 48.79  ? 206 ASP B OD2 1 
ATOM   5855 N N   . ILE C 1 208 ? 5.183   75.121  2.231   1.00 24.56  ? 207 ILE B N   1 
ATOM   5856 C CA  . ILE C 1 208 ? 6.147   74.678  1.226   1.00 25.38  ? 207 ILE B CA  1 
ATOM   5857 C C   . ILE C 1 208 ? 7.572   74.963  1.690   1.00 32.53  ? 207 ILE B C   1 
ATOM   5858 O O   . ILE C 1 208 ? 8.447   74.089  1.638   1.00 27.48  ? 207 ILE B O   1 
ATOM   5859 C CB  . ILE C 1 208 ? 5.848   75.335  -0.133  1.00 28.11  ? 207 ILE B CB  1 
ATOM   5860 C CG1 . ILE C 1 208 ? 4.592   74.717  -0.751  1.00 28.74  ? 207 ILE B CG1 1 
ATOM   5861 C CG2 . ILE C 1 208 ? 7.039   75.191  -1.070  1.00 26.93  ? 207 ILE B CG2 1 
ATOM   5862 C CD1 . ILE C 1 208 ? 4.057   75.466  -1.948  1.00 30.90  ? 207 ILE B CD1 1 
ATOM   5863 N N   . ALA C 1 209 ? 7.822   76.186  2.167   1.00 32.29  ? 208 ALA B N   1 
ATOM   5864 C CA  . ALA C 1 209 ? 9.152   76.532  2.662   1.00 26.62  ? 208 ALA B CA  1 
ATOM   5865 C C   . ALA C 1 209 ? 9.588   75.585  3.772   1.00 27.21  ? 208 ALA B C   1 
ATOM   5866 O O   . ALA C 1 209 ? 10.690  75.028  3.727   1.00 28.59  ? 208 ALA B O   1 
ATOM   5867 C CB  . ALA C 1 209 ? 9.175   77.980  3.151   1.00 28.02  ? 208 ALA B CB  1 
ATOM   5868 N N   . GLY C 1 210 ? 8.726   75.374  4.770   1.00 25.60  ? 209 GLY B N   1 
ATOM   5869 C CA  . GLY C 1 210 ? 9.107   74.539  5.898   1.00 24.44  ? 209 GLY B CA  1 
ATOM   5870 C C   . GLY C 1 210 ? 9.501   73.134  5.484   1.00 30.11  ? 209 GLY B C   1 
ATOM   5871 O O   . GLY C 1 210 ? 10.508  72.596  5.954   1.00 22.74  ? 209 GLY B O   1 
ATOM   5872 N N   . ILE C 1 211 ? 8.718   72.527  4.588   1.00 20.38  ? 210 ILE B N   1 
ATOM   5873 C CA  . ILE C 1 211 ? 8.988   71.161  4.151   1.00 22.22  ? 210 ILE B CA  1 
ATOM   5874 C C   . ILE C 1 211 ? 10.360  71.064  3.497   1.00 24.55  ? 210 ILE B C   1 
ATOM   5875 O O   . ILE C 1 211 ? 11.126  70.130  3.761   1.00 23.35  ? 210 ILE B O   1 
ATOM   5876 C CB  . ILE C 1 211 ? 7.873   70.688  3.202   1.00 22.38  ? 210 ILE B CB  1 
ATOM   5877 C CG1 . ILE C 1 211 ? 6.561   70.519  3.973   1.00 25.91  ? 210 ILE B CG1 1 
ATOM   5878 C CG2 . ILE C 1 211 ? 8.275   69.404  2.498   1.00 22.03  ? 210 ILE B CG2 1 
ATOM   5879 C CD1 . ILE C 1 211 ? 5.325   70.641  3.110   1.00 27.91  ? 210 ILE B CD1 1 
ATOM   5880 N N   . ASP C 1 212 ? 10.704  72.035  2.651   1.00 21.41  ? 211 ASP B N   1 
ATOM   5881 C CA  . ASP C 1 212 ? 11.956  71.943  1.909   1.00 28.87  ? 211 ASP B CA  1 
ATOM   5882 C C   . ASP C 1 212 ? 13.172  72.238  2.788   1.00 24.21  ? 211 ASP B C   1 
ATOM   5883 O O   . ASP C 1 212 ? 14.208  71.582  2.641   1.00 28.87  ? 211 ASP B O   1 
ATOM   5884 C CB  . ASP C 1 212 ? 11.913  72.875  0.696   1.00 26.09  ? 211 ASP B CB  1 
ATOM   5885 C CG  . ASP C 1 212 ? 11.177  72.256  -0.483  1.00 31.22  ? 211 ASP B CG  1 
ATOM   5886 O OD1 . ASP C 1 212 ? 10.831  71.056  -0.410  1.00 30.30  ? 211 ASP B OD1 1 
ATOM   5887 O OD2 . ASP C 1 212 ? 10.935  72.968  -1.479  1.00 31.74  ? 211 ASP B OD2 1 
ATOM   5888 N N   . THR C 1 213 ? 13.083  73.207  3.706   1.00 25.54  ? 212 THR B N   1 
ATOM   5889 C CA  . THR C 1 213 ? 14.220  73.419  4.601   1.00 31.74  ? 212 THR B CA  1 
ATOM   5890 C C   . THR C 1 213 ? 14.347  72.291  5.611   1.00 26.41  ? 212 THR B C   1 
ATOM   5891 O O   . THR C 1 213 ? 15.452  72.012  6.085   1.00 32.83  ? 212 THR B O   1 
ATOM   5892 C CB  . THR C 1 213 ? 14.132  74.761  5.338   1.00 23.55  ? 212 THR B CB  1 
ATOM   5893 O OG1 . THR C 1 213 ? 13.451  74.590  6.587   1.00 46.81  ? 212 THR B OG1 1 
ATOM   5894 C CG2 . THR C 1 213 ? 13.451  75.824  4.498   1.00 22.64  ? 212 THR B CG2 1 
ATOM   5895 N N   . ALA C 1 214 ? 13.237  71.633  5.947   1.00 25.91  ? 213 ALA B N   1 
ATOM   5896 C CA  . ALA C 1 214 ? 13.306  70.483  6.840   1.00 28.33  ? 213 ALA B CA  1 
ATOM   5897 C C   . ALA C 1 214 ? 14.134  69.365  6.219   1.00 21.09  ? 213 ALA B C   1 
ATOM   5898 O O   . ALA C 1 214 ? 15.035  68.811  6.859   1.00 24.54  ? 213 ALA B O   1 
ATOM   5899 C CB  . ALA C 1 214 ? 11.899  69.992  7.181   1.00 19.80  ? 213 ALA B CB  1 
ATOM   5900 N N   . MET C 1 215 ? 13.858  69.031  4.961   1.00 22.81  ? 214 MET B N   1 
ATOM   5901 C CA  . MET C 1 215 ? 14.605  67.954  4.330   1.00 25.06  ? 214 MET B CA  1 
ATOM   5902 C C   . MET C 1 215 ? 16.031  68.359  3.986   1.00 25.74  ? 214 MET B C   1 
ATOM   5903 O O   . MET C 1 215 ? 16.908  67.490  3.925   1.00 30.71  ? 214 MET B O   1 
ATOM   5904 C CB  . MET C 1 215 ? 13.863  67.472  3.087   1.00 26.28  ? 214 MET B CB  1 
ATOM   5905 C CG  . MET C 1 215 ? 12.486  66.926  3.422   1.00 22.95  ? 214 MET B CG  1 
ATOM   5906 S SD  . MET C 1 215 ? 12.521  65.444  4.450   1.00 35.73  ? 214 MET B SD  1 
ATOM   5907 C CE  . MET C 1 215 ? 13.908  64.556  3.740   1.00 33.69  ? 214 MET B CE  1 
ATOM   5908 N N   . LYS C 1 216 ? 16.290  69.651  3.779   1.00 22.69  ? 215 LYS B N   1 
ATOM   5909 C CA  . LYS C 1 216 ? 17.660  70.083  3.521   1.00 23.16  ? 215 LYS B CA  1 
ATOM   5910 C C   . LYS C 1 216 ? 18.478  70.136  4.804   1.00 31.59  ? 215 LYS B C   1 
ATOM   5911 O O   . LYS C 1 216 ? 19.612  69.642  4.840   1.00 33.74  ? 215 LYS B O   1 
ATOM   5912 C CB  . LYS C 1 216 ? 17.663  71.442  2.821   1.00 24.09  ? 215 LYS B CB  1 
ATOM   5913 C CG  . LYS C 1 216 ? 17.468  71.339  1.311   1.00 31.43  ? 215 LYS B CG  1 
ATOM   5914 C CD  . LYS C 1 216 ? 17.868  72.620  0.590   1.00 33.48  ? 215 LYS B CD  1 
ATOM   5915 C CE  . LYS C 1 216 ? 17.023  73.802  1.033   1.00 29.43  ? 215 LYS B CE  1 
ATOM   5916 N NZ  . LYS C 1 216 ? 16.956  74.848  -0.030  1.00 48.27  ? 215 LYS B NZ  1 
ATOM   5917 N N   . LEU C 1 217 ? 17.919  70.708  5.870   1.00 26.87  ? 216 LEU B N   1 
ATOM   5918 C CA  . LEU C 1 217 ? 18.633  70.833  7.133   1.00 30.32  ? 216 LEU B CA  1 
ATOM   5919 C C   . LEU C 1 217 ? 18.495  69.611  8.035   1.00 25.10  ? 216 LEU B C   1 
ATOM   5920 O O   . LEU C 1 217 ? 19.237  69.504  9.017   1.00 28.33  ? 216 LEU B O   1 
ATOM   5921 C CB  . LEU C 1 217 ? 18.158  72.086  7.879   1.00 29.59  ? 216 LEU B CB  1 
ATOM   5922 C CG  . LEU C 1 217 ? 18.390  73.397  7.123   1.00 30.35  ? 216 LEU B CG  1 
ATOM   5923 C CD1 . LEU C 1 217 ? 18.165  74.607  8.017   1.00 24.94  ? 216 LEU B CD1 1 
ATOM   5924 C CD2 . LEU C 1 217 ? 19.787  73.422  6.519   1.00 25.70  ? 216 LEU B CD2 1 
ATOM   5925 N N   . GLY C 1 218 ? 17.588  68.685  7.727   1.00 34.38  ? 217 GLY B N   1 
ATOM   5926 C CA  . GLY C 1 218 ? 17.391  67.515  8.566   1.00 26.52  ? 217 GLY B CA  1 
ATOM   5927 C C   . GLY C 1 218 ? 17.922  66.219  7.984   1.00 32.88  ? 217 GLY B C   1 
ATOM   5928 O O   . GLY C 1 218 ? 18.259  65.289  8.726   1.00 26.47  ? 217 GLY B O   1 
ATOM   5929 N N   . ALA C 1 219 ? 17.994  66.134  6.655   1.00 23.71  ? 218 ALA B N   1 
ATOM   5930 C CA  . ALA C 1 219 ? 18.528  64.955  5.984   1.00 22.29  ? 218 ALA B CA  1 
ATOM   5931 C C   . ALA C 1 219 ? 19.718  65.291  5.095   1.00 28.25  ? 218 ALA B C   1 
ATOM   5932 O O   . ALA C 1 219 ? 20.219  64.407  4.385   1.00 25.53  ? 218 ALA B O   1 
ATOM   5933 C CB  . ALA C 1 219 ? 17.435  64.261  5.164   1.00 23.15  ? 218 ALA B CB  1 
ATOM   5934 N N   . ASN C 1 220 ? 20.181  66.543  5.117   1.00 28.72  ? 219 ASN B N   1 
ATOM   5935 C CA  . ASN C 1 220 ? 21.314  66.992  4.309   1.00 27.04  ? 219 ASN B CA  1 
ATOM   5936 C C   . ASN C 1 220 ? 21.071  66.756  2.823   1.00 29.55  ? 219 ASN B C   1 
ATOM   5937 O O   . ASN C 1 220 ? 22.000  66.460  2.069   1.00 31.70  ? 219 ASN B O   1 
ATOM   5938 C CB  . ASN C 1 220 ? 22.619  66.326  4.754   1.00 26.65  ? 219 ASN B CB  1 
ATOM   5939 C CG  . ASN C 1 220 ? 23.239  67.012  5.957   1.00 35.77  ? 219 ASN B CG  1 
ATOM   5940 O OD1 . ASN C 1 220 ? 22.895  68.148  6.284   1.00 35.42  ? 219 ASN B OD1 1 
ATOM   5941 N ND2 . ASN C 1 220 ? 24.150  66.318  6.631   1.00 43.22  ? 219 ASN B ND2 1 
ATOM   5942 N N   . HIS C 1 221 ? 19.820  66.877  2.400   1.00 34.73  ? 220 HIS B N   1 
ATOM   5943 C CA  . HIS C 1 221 ? 19.502  66.761  0.986   1.00 36.03  ? 220 HIS B CA  1 
ATOM   5944 C C   . HIS C 1 221 ? 19.875  68.052  0.265   1.00 35.81  ? 220 HIS B C   1 
ATOM   5945 O O   . HIS C 1 221 ? 19.717  69.141  0.824   1.00 32.12  ? 220 HIS B O   1 
ATOM   5946 C CB  . HIS C 1 221 ? 18.017  66.466  0.783   1.00 30.43  ? 220 HIS B CB  1 
ATOM   5947 C CG  . HIS C 1 221 ? 17.633  65.057  1.106   1.00 32.37  ? 220 HIS B CG  1 
ATOM   5948 N ND1 . HIS C 1 221 ? 16.334  64.603  1.029   1.00 26.99  ? 220 HIS B ND1 1 
ATOM   5949 C CD2 . HIS C 1 221 ? 18.377  64.002  1.513   1.00 29.05  ? 220 HIS B CD2 1 
ATOM   5950 C CE1 . HIS C 1 221 ? 16.295  63.328  1.371   1.00 33.86  ? 220 HIS B CE1 1 
ATOM   5951 N NE2 . HIS C 1 221 ? 17.523  62.938  1.668   1.00 32.38  ? 220 HIS B NE2 1 
ATOM   5952 N N   . PRO C 1 222 ? 20.372  67.960  -0.969  1.00 33.77  ? 221 PRO B N   1 
ATOM   5953 C CA  . PRO C 1 222 ? 20.774  69.185  -1.673  1.00 29.60  ? 221 PRO B CA  1 
ATOM   5954 C C   . PRO C 1 222 ? 19.596  70.065  -2.049  1.00 31.57  ? 221 PRO B C   1 
ATOM   5955 O O   . PRO C 1 222 ? 19.718  71.296  -2.007  1.00 25.88  ? 221 PRO B O   1 
ATOM   5956 C CB  . PRO C 1 222 ? 21.512  68.651  -2.908  1.00 31.18  ? 221 PRO B CB  1 
ATOM   5957 C CG  . PRO C 1 222 ? 20.917  67.301  -3.150  1.00 27.25  ? 221 PRO B CG  1 
ATOM   5958 C CD  . PRO C 1 222 ? 20.526  66.752  -1.802  1.00 32.03  ? 221 PRO B CD  1 
ATOM   5959 N N   . MET C 1 223 ? 18.456  69.476  -2.402  1.00 31.82  ? 222 MET B N   1 
ATOM   5960 C CA  . MET C 1 223 ? 17.238  70.221  -2.683  1.00 30.23  ? 222 MET B CA  1 
ATOM   5961 C C   . MET C 1 223 ? 16.091  69.622  -1.883  1.00 31.65  ? 222 MET B C   1 
ATOM   5962 O O   . MET C 1 223 ? 16.017  68.402  -1.709  1.00 27.68  ? 222 MET B O   1 
ATOM   5963 C CB  . MET C 1 223 ? 16.902  70.208  -4.184  1.00 27.60  ? 222 MET B CB  1 
ATOM   5964 C CG  . MET C 1 223 ? 17.854  71.033  -5.044  1.00 26.84  ? 222 MET B CG  1 
ATOM   5965 S SD  . MET C 1 223 ? 17.486  71.005  -6.818  1.00 37.15  ? 222 MET B SD  1 
ATOM   5966 C CE  . MET C 1 223 ? 16.802  69.383  -6.977  1.00 28.59  ? 222 MET B CE  1 
ATOM   5967 N N   . GLY C 1 224 ? 15.209  70.483  -1.381  1.00 34.65  ? 223 GLY B N   1 
ATOM   5968 C CA  . GLY C 1 224 ? 13.977  70.033  -0.779  1.00 26.20  ? 223 GLY B CA  1 
ATOM   5969 C C   . GLY C 1 224 ? 13.167  69.230  -1.780  1.00 33.78  ? 223 GLY B C   1 
ATOM   5970 O O   . GLY C 1 224 ? 13.308  69.393  -2.997  1.00 23.88  ? 223 GLY B O   1 
ATOM   5971 N N   . PRO C 1 225 ? 12.311  68.332  -1.289  1.00 30.52  ? 224 PRO B N   1 
ATOM   5972 C CA  . PRO C 1 225 ? 11.535  67.493  -2.217  1.00 22.31  ? 224 PRO B CA  1 
ATOM   5973 C C   . PRO C 1 225 ? 10.608  68.295  -3.108  1.00 22.23  ? 224 PRO B C   1 
ATOM   5974 O O   . PRO C 1 225 ? 10.298  67.853  -4.222  1.00 21.66  ? 224 PRO B O   1 
ATOM   5975 C CB  . PRO C 1 225 ? 10.757  66.559  -1.280  1.00 22.71  ? 224 PRO B CB  1 
ATOM   5976 C CG  . PRO C 1 225 ? 10.697  67.300  0.020   1.00 24.93  ? 224 PRO B CG  1 
ATOM   5977 C CD  . PRO C 1 225 ? 11.975  68.066  0.117   1.00 26.54  ? 224 PRO B CD  1 
ATOM   5978 N N   . LEU C 1 226 ? 10.166  69.472  -2.661  1.00 23.07  ? 225 LEU B N   1 
ATOM   5979 C CA  . LEU C 1 226 ? 9.296   70.284  -3.500  1.00 24.30  ? 225 LEU B CA  1 
ATOM   5980 C C   . LEU C 1 226 ? 10.093  71.066  -4.544  1.00 30.83  ? 225 LEU B C   1 
ATOM   5981 O O   . LEU C 1 226 ? 9.642   71.192  -5.689  1.00 31.14  ? 225 LEU B O   1 
ATOM   5982 C CB  . LEU C 1 226 ? 8.445   71.205  -2.626  1.00 23.04  ? 225 LEU B CB  1 
ATOM   5983 C CG  . LEU C 1 226 ? 7.510   70.433  -1.686  1.00 22.09  ? 225 LEU B CG  1 
ATOM   5984 C CD1 . LEU C 1 226 ? 6.615   71.361  -0.889  1.00 20.25  ? 225 LEU B CD1 1 
ATOM   5985 C CD2 . LEU C 1 226 ? 6.671   69.421  -2.460  1.00 25.93  ? 225 LEU B CD2 1 
ATOM   5986 N N   . GLU C 1 227 ? 11.276  71.587  -4.189  1.00 25.51  ? 226 GLU B N   1 
ATOM   5987 C CA  . GLU C 1 227 ? 12.162  72.132  -5.219  1.00 32.66  ? 226 GLU B CA  1 
ATOM   5988 C C   . GLU C 1 227 ? 12.512  71.062  -6.240  1.00 21.16  ? 226 GLU B C   1 
ATOM   5989 O O   . GLU C 1 227 ? 12.496  71.310  -7.451  1.00 30.27  ? 226 GLU B O   1 
ATOM   5990 C CB  . GLU C 1 227 ? 13.463  72.692  -4.630  1.00 28.31  ? 226 GLU B CB  1 
ATOM   5991 C CG  . GLU C 1 227 ? 13.455  73.169  -3.205  1.00 42.51  ? 226 GLU B CG  1 
ATOM   5992 C CD  . GLU C 1 227 ? 14.866  73.469  -2.713  1.00 49.91  ? 226 GLU B CD  1 
ATOM   5993 O OE1 . GLU C 1 227 ? 15.472  74.451  -3.194  1.00 49.70  ? 226 GLU B OE1 1 
ATOM   5994 O OE2 . GLU C 1 227 ? 15.373  72.721  -1.853  1.00 51.22  ? 226 GLU B OE2 1 
ATOM   5995 N N   . LEU C 1 228 ? 12.866  69.869  -5.758  1.00 19.64  ? 227 LEU B N   1 
ATOM   5996 C CA  . LEU C 1 228 ? 13.253  68.786  -6.652  1.00 22.97  ? 227 LEU B CA  1 
ATOM   5997 C C   . LEU C 1 228 ? 12.107  68.400  -7.575  1.00 21.70  ? 227 LEU B C   1 
ATOM   5998 O O   . LEU C 1 228 ? 12.337  68.050  -8.737  1.00 27.93  ? 227 LEU B O   1 
ATOM   5999 C CB  . LEU C 1 228 ? 13.729  67.590  -5.828  1.00 19.97  ? 227 LEU B CB  1 
ATOM   6000 C CG  . LEU C 1 228 ? 14.111  66.277  -6.505  1.00 26.62  ? 227 LEU B CG  1 
ATOM   6001 C CD1 . LEU C 1 228 ? 15.172  66.486  -7.567  1.00 29.00  ? 227 LEU B CD1 1 
ATOM   6002 C CD2 . LEU C 1 228 ? 14.604  65.297  -5.452  1.00 27.43  ? 227 LEU B CD2 1 
ATOM   6003 N N   . GLY C 1 229 ? 10.871  68.472  -7.081  1.00 22.78  ? 228 GLY B N   1 
ATOM   6004 C CA  . GLY C 1 229 ? 9.731   68.268  -7.957  1.00 22.98  ? 228 GLY B CA  1 
ATOM   6005 C C   . GLY C 1 229 ? 9.673   69.294  -9.072  1.00 32.93  ? 228 GLY B C   1 
ATOM   6006 O O   . GLY C 1 229 ? 9.477   68.950  -10.243 1.00 22.50  ? 228 GLY B O   1 
ATOM   6007 N N   . ASP C 1 230 ? 9.841   70.575  -8.722  1.00 25.60  ? 229 ASP B N   1 
ATOM   6008 C CA  . ASP C 1 230 ? 9.865   71.623  -9.737  1.00 24.97  ? 229 ASP B CA  1 
ATOM   6009 C C   . ASP C 1 230 ? 11.037  71.436  -10.689 1.00 28.58  ? 229 ASP B C   1 
ATOM   6010 O O   . ASP C 1 230 ? 10.897  71.622  -11.904 1.00 26.92  ? 229 ASP B O   1 
ATOM   6011 C CB  . ASP C 1 230 ? 9.949   72.999  -9.078  1.00 30.03  ? 229 ASP B CB  1 
ATOM   6012 C CG  . ASP C 1 230 ? 8.648   73.426  -8.417  1.00 30.42  ? 229 ASP B CG  1 
ATOM   6013 O OD1 . ASP C 1 230 ? 7.602   72.783  -8.653  1.00 34.03  ? 229 ASP B OD1 1 
ATOM   6014 O OD2 . ASP C 1 230 ? 8.676   74.417  -7.657  1.00 29.15  ? 229 ASP B OD2 1 
ATOM   6015 N N   . PHE C 1 231 ? 12.205  71.070  -10.149 1.00 25.16  ? 230 PHE B N   1 
ATOM   6016 C CA  . PHE C 1 231 ? 13.402  70.904  -10.969 1.00 23.38  ? 230 PHE B CA  1 
ATOM   6017 C C   . PHE C 1 231 ? 13.245  69.754  -11.959 1.00 29.92  ? 230 PHE B C   1 
ATOM   6018 O O   . PHE C 1 231 ? 13.593  69.892  -13.138 1.00 24.44  ? 230 PHE B O   1 
ATOM   6019 C CB  . PHE C 1 231 ? 14.613  70.687  -10.059 1.00 24.82  ? 230 PHE B CB  1 
ATOM   6020 C CG  . PHE C 1 231 ? 15.914  70.516  -10.795 1.00 31.00  ? 230 PHE B CG  1 
ATOM   6021 C CD1 . PHE C 1 231 ? 16.463  71.567  -11.511 1.00 30.30  ? 230 PHE B CD1 1 
ATOM   6022 C CD2 . PHE C 1 231 ? 16.602  69.312  -10.746 1.00 31.21  ? 230 PHE B CD2 1 
ATOM   6023 C CE1 . PHE C 1 231 ? 17.663  71.415  -12.182 1.00 32.97  ? 230 PHE B CE1 1 
ATOM   6024 C CE2 . PHE C 1 231 ? 17.802  69.156  -11.415 1.00 32.69  ? 230 PHE B CE2 1 
ATOM   6025 C CZ  . PHE C 1 231 ? 18.332  70.209  -12.134 1.00 31.01  ? 230 PHE B CZ  1 
ATOM   6026 N N   . ILE C 1 232 ? 12.714  68.617  -11.503 1.00 28.44  ? 231 ILE B N   1 
ATOM   6027 C CA  . ILE C 1 232 ? 12.521  67.469  -12.386 1.00 28.16  ? 231 ILE B CA  1 
ATOM   6028 C C   . ILE C 1 232 ? 11.463  67.775  -13.440 1.00 27.22  ? 231 ILE B C   1 
ATOM   6029 O O   . ILE C 1 232 ? 11.559  67.325  -14.589 1.00 30.67  ? 231 ILE B O   1 
ATOM   6030 C CB  . ILE C 1 232 ? 12.140  66.223  -11.561 1.00 31.47  ? 231 ILE B CB  1 
ATOM   6031 C CG1 . ILE C 1 232 ? 13.332  65.708  -10.754 1.00 33.60  ? 231 ILE B CG1 1 
ATOM   6032 C CG2 . ILE C 1 232 ? 11.600  65.115  -12.455 1.00 29.07  ? 231 ILE B CG2 1 
ATOM   6033 C CD1 . ILE C 1 232 ? 12.947  64.669  -9.727  1.00 20.47  ? 231 ILE B CD1 1 
ATOM   6034 N N   . GLY C 1 233 ? 10.446  68.548  -13.070 1.00 20.80  ? 232 GLY B N   1 
ATOM   6035 C CA  . GLY C 1 233 ? 9.259   68.701  -13.885 1.00 25.24  ? 232 GLY B CA  1 
ATOM   6036 C C   . GLY C 1 233 ? 8.098   67.941  -13.275 1.00 28.70  ? 232 GLY B C   1 
ATOM   6037 O O   . GLY C 1 233 ? 8.118   66.707  -13.220 1.00 26.35  ? 232 GLY B O   1 
ATOM   6038 N N   . LEU C 1 234 ? 7.082   68.663  -12.799 1.00 24.77  ? 233 LEU B N   1 
ATOM   6039 C CA  . LEU C 1 234 ? 5.986   68.002  -12.099 1.00 21.53  ? 233 LEU B CA  1 
ATOM   6040 C C   . LEU C 1 234 ? 5.196   67.086  -13.021 1.00 24.64  ? 233 LEU B C   1 
ATOM   6041 O O   . LEU C 1 234 ? 4.624   66.092  -12.559 1.00 26.39  ? 233 LEU B O   1 
ATOM   6042 C CB  . LEU C 1 234 ? 5.074   69.042  -11.460 1.00 23.35  ? 233 LEU B CB  1 
ATOM   6043 C CG  . LEU C 1 234 ? 5.755   69.752  -10.292 1.00 24.16  ? 233 LEU B CG  1 
ATOM   6044 C CD1 . LEU C 1 234 ? 4.802   70.709  -9.623  1.00 19.87  ? 233 LEU B CD1 1 
ATOM   6045 C CD2 . LEU C 1 234 ? 6.289   68.737  -9.299  1.00 22.38  ? 233 LEU B CD2 1 
ATOM   6046 N N   . ASP C 1 235 ? 5.155   67.395  -14.318 1.00 30.37  ? 234 ASP B N   1 
ATOM   6047 C CA  . ASP C 1 235 ? 4.537   66.473  -15.266 1.00 27.44  ? 234 ASP B CA  1 
ATOM   6048 C C   . ASP C 1 235 ? 5.264   65.134  -15.273 1.00 22.45  ? 234 ASP B C   1 
ATOM   6049 O O   . ASP C 1 235 ? 4.633   64.077  -15.388 1.00 25.36  ? 234 ASP B O   1 
ATOM   6050 C CB  . ASP C 1 235 ? 4.521   67.090  -16.665 1.00 20.86  ? 234 ASP B CB  1 
ATOM   6051 C CG  . ASP C 1 235 ? 5.899   67.524  -17.128 1.00 34.16  ? 234 ASP B CG  1 
ATOM   6052 O OD1 . ASP C 1 235 ? 6.724   67.918  -16.273 1.00 27.91  ? 234 ASP B OD1 1 
ATOM   6053 O OD2 . ASP C 1 235 ? 6.157   67.471  -18.348 1.00 38.01  ? 234 ASP B OD2 1 
ATOM   6054 N N   . ILE C 1 236 ? 6.592   65.161  -15.130 1.00 26.38  ? 235 ILE B N   1 
ATOM   6055 C CA  . ILE C 1 236 ? 7.370   63.926  -15.097 1.00 27.17  ? 235 ILE B CA  1 
ATOM   6056 C C   . ILE C 1 236 ? 7.086   63.151  -13.818 1.00 24.18  ? 235 ILE B C   1 
ATOM   6057 O O   . ILE C 1 236 ? 6.918   61.925  -13.841 1.00 20.55  ? 235 ILE B O   1 
ATOM   6058 C CB  . ILE C 1 236 ? 8.871   64.241  -15.242 1.00 29.21  ? 235 ILE B CB  1 
ATOM   6059 C CG1 . ILE C 1 236 ? 9.127   65.078  -16.497 1.00 36.45  ? 235 ILE B CG1 1 
ATOM   6060 C CG2 . ILE C 1 236 ? 9.687   62.959  -15.263 1.00 31.25  ? 235 ILE B CG2 1 
ATOM   6061 C CD1 . ILE C 1 236 ? 8.997   64.300  -17.788 1.00 37.28  ? 235 ILE B CD1 1 
ATOM   6062 N N   . CYS C 1 237 ? 7.037   63.849  -12.682 1.00 19.82  ? 236 CYS B N   1 
ATOM   6063 C CA  . CYS C 1 237 ? 6.746   63.181  -11.419 1.00 21.69  ? 236 CYS B CA  1 
ATOM   6064 C C   . CYS C 1 237 ? 5.369   62.533  -11.445 1.00 22.53  ? 236 CYS B C   1 
ATOM   6065 O O   . CYS C 1 237 ? 5.208   61.383  -11.021 1.00 25.89  ? 236 CYS B O   1 
ATOM   6066 C CB  . CYS C 1 237 ? 6.849   64.175  -10.263 1.00 19.26  ? 236 CYS B CB  1 
ATOM   6067 S SG  . CYS C 1 237 ? 8.455   64.973  -10.125 1.00 25.82  ? 236 CYS B SG  1 
ATOM   6068 N N   . LEU C 1 238 ? 4.363   63.254  -11.949 1.00 22.78  ? 237 LEU B N   1 
ATOM   6069 C CA  . LEU C 1 238 ? 3.025   62.683  -12.053 1.00 21.68  ? 237 LEU B CA  1 
ATOM   6070 C C   . LEU C 1 238 ? 3.032   61.430  -12.920 1.00 24.46  ? 237 LEU B C   1 
ATOM   6071 O O   . LEU C 1 238 ? 2.453   60.402  -12.549 1.00 24.22  ? 237 LEU B O   1 
ATOM   6072 C CB  . LEU C 1 238 ? 2.054   63.721  -12.615 1.00 23.43  ? 237 LEU B CB  1 
ATOM   6073 C CG  . LEU C 1 238 ? 0.603   63.269  -12.778 1.00 29.74  ? 237 LEU B CG  1 
ATOM   6074 C CD1 . LEU C 1 238 ? -0.023  62.993  -11.414 1.00 16.17  ? 237 LEU B CD1 1 
ATOM   6075 C CD2 . LEU C 1 238 ? -0.210  64.306  -13.547 1.00 16.39  ? 237 LEU B CD2 1 
ATOM   6076 N N   . ALA C 1 239 ? 3.700   61.494  -14.076 1.00 27.81  ? 238 ALA B N   1 
ATOM   6077 C CA  . ALA C 1 239 ? 3.730   60.346  -14.978 1.00 19.82  ? 238 ALA B CA  1 
ATOM   6078 C C   . ALA C 1 239 ? 4.376   59.139  -14.312 1.00 21.30  ? 238 ALA B C   1 
ATOM   6079 O O   . ALA C 1 239 ? 3.933   58.002  -14.511 1.00 24.67  ? 238 ALA B O   1 
ATOM   6080 C CB  . ALA C 1 239 ? 4.466   60.706  -16.269 1.00 22.03  ? 238 ALA B CB  1 
ATOM   6081 N N   . ILE C 1 240 ? 5.410   59.368  -13.499 1.00 20.75  ? 239 ILE B N   1 
ATOM   6082 C CA  . ILE C 1 240 ? 6.098   58.264  -12.836 1.00 19.93  ? 239 ILE B CA  1 
ATOM   6083 C C   . ILE C 1 240 ? 5.219   57.646  -11.751 1.00 19.61  ? 239 ILE B C   1 
ATOM   6084 O O   . ILE C 1 240 ? 5.125   56.417  -11.642 1.00 21.33  ? 239 ILE B O   1 
ATOM   6085 C CB  . ILE C 1 240 ? 7.449   58.742  -12.277 1.00 21.14  ? 239 ILE B CB  1 
ATOM   6086 C CG1 . ILE C 1 240 ? 8.441   58.949  -13.428 1.00 19.32  ? 239 ILE B CG1 1 
ATOM   6087 C CG2 . ILE C 1 240 ? 7.984   57.743  -11.251 1.00 10.19  ? 239 ILE B CG2 1 
ATOM   6088 C CD1 . ILE C 1 240 ? 9.622   59.825  -13.086 1.00 17.93  ? 239 ILE B CD1 1 
ATOM   6089 N N   . MET C 1 241 ? 4.573   58.475  -10.925 1.00 21.03  ? 240 MET B N   1 
ATOM   6090 C CA  . MET C 1 241 ? 3.639   57.937  -9.937  1.00 24.00  ? 240 MET B CA  1 
ATOM   6091 C C   . MET C 1 241 ? 2.527   57.143  -10.606 1.00 22.42  ? 240 MET B C   1 
ATOM   6092 O O   . MET C 1 241 ? 2.121   56.088  -10.103 1.00 26.27  ? 240 MET B O   1 
ATOM   6093 C CB  . MET C 1 241 ? 3.050   59.060  -9.080  1.00 20.89  ? 240 MET B CB  1 
ATOM   6094 C CG  . MET C 1 241 ? 4.053   59.804  -8.206  1.00 20.96  ? 240 MET B CG  1 
ATOM   6095 S SD  . MET C 1 241 ? 5.104   58.718  -7.218  1.00 28.35  ? 240 MET B SD  1 
ATOM   6096 C CE  . MET C 1 241 ? 3.899   57.867  -6.206  1.00 20.01  ? 240 MET B CE  1 
ATOM   6097 N N   . ASP C 1 242 ? 2.032   57.623  -11.749 1.00 20.52  ? 241 ASP B N   1 
ATOM   6098 C CA  . ASP C 1 242 ? 0.962   56.906  -12.434 1.00 25.74  ? 241 ASP B CA  1 
ATOM   6099 C C   . ASP C 1 242 ? 1.456   55.570  -12.975 1.00 27.47  ? 241 ASP B C   1 
ATOM   6100 O O   . ASP C 1 242 ? 0.743   54.563  -12.896 1.00 24.89  ? 241 ASP B O   1 
ATOM   6101 C CB  . ASP C 1 242 ? 0.378   57.761  -13.559 1.00 22.28  ? 241 ASP B CB  1 
ATOM   6102 C CG  . ASP C 1 242 ? -0.582  58.823  -13.051 1.00 29.02  ? 241 ASP B CG  1 
ATOM   6103 O OD1 . ASP C 1 242 ? -1.073  58.698  -11.903 1.00 26.07  ? 241 ASP B OD1 1 
ATOM   6104 O OD2 . ASP C 1 242 ? -0.868  59.774  -13.814 1.00 31.83  ? 241 ASP B OD2 1 
ATOM   6105 N N   . VAL C 1 243 ? 2.674   55.538  -13.528 1.00 17.69  ? 242 VAL B N   1 
ATOM   6106 C CA  . VAL C 1 243 ? 3.249   54.267  -13.964 1.00 25.85  ? 242 VAL B CA  1 
ATOM   6107 C C   . VAL C 1 243 ? 3.435   53.338  -12.774 1.00 18.07  ? 242 VAL B C   1 
ATOM   6108 O O   . VAL C 1 243 ? 3.142   52.139  -12.853 1.00 23.33  ? 242 VAL B O   1 
ATOM   6109 C CB  . VAL C 1 243 ? 4.579   54.492  -14.708 1.00 27.05  ? 242 VAL B CB  1 
ATOM   6110 C CG1 . VAL C 1 243 ? 5.248   53.156  -14.991 1.00 26.71  ? 242 VAL B CG1 1 
ATOM   6111 C CG2 . VAL C 1 243 ? 4.350   55.251  -15.999 1.00 26.72  ? 242 VAL B CG2 1 
ATOM   6112 N N   . LEU C 1 244 ? 3.923   53.874  -11.653 1.00 19.47  ? 243 LEU B N   1 
ATOM   6113 C CA  . LEU C 1 244 ? 4.074   53.060  -10.452 1.00 19.84  ? 243 LEU B CA  1 
ATOM   6114 C C   . LEU C 1 244 ? 2.735   52.475  -10.023 1.00 18.86  ? 243 LEU B C   1 
ATOM   6115 O O   . LEU C 1 244 ? 2.620   51.270  -9.774  1.00 18.54  ? 243 LEU B O   1 
ATOM   6116 C CB  . LEU C 1 244 ? 4.691   53.892  -9.325  1.00 21.38  ? 243 LEU B CB  1 
ATOM   6117 C CG  . LEU C 1 244 ? 6.183   54.207  -9.478  1.00 24.79  ? 243 LEU B CG  1 
ATOM   6118 C CD1 . LEU C 1 244 ? 6.687   55.081  -8.331  1.00 17.62  ? 243 LEU B CD1 1 
ATOM   6119 C CD2 . LEU C 1 244 ? 6.999   52.925  -9.572  1.00 19.37  ? 243 LEU B CD2 1 
ATOM   6120 N N   . TYR C 1 245 ? 1.700   53.317  -9.965  1.00 25.30  ? 244 TYR B N   1 
ATOM   6121 C CA  . TYR C 1 245 ? 0.390   52.856  -9.517  1.00 26.31  ? 244 TYR B CA  1 
ATOM   6122 C C   . TYR C 1 245 ? -0.174  51.795  -10.454 1.00 23.02  ? 244 TYR B C   1 
ATOM   6123 O O   . TYR C 1 245 ? -0.701  50.772  -10.003 1.00 21.22  ? 244 TYR B O   1 
ATOM   6124 C CB  . TYR C 1 245 ? -0.562  54.048  -9.406  1.00 22.91  ? 244 TYR B CB  1 
ATOM   6125 C CG  . TYR C 1 245 ? -1.993  53.689  -9.070  1.00 28.74  ? 244 TYR B CG  1 
ATOM   6126 C CD1 . TYR C 1 245 ? -2.311  53.059  -7.869  1.00 33.41  ? 244 TYR B CD1 1 
ATOM   6127 C CD2 . TYR C 1 245 ? -3.027  53.992  -9.949  1.00 24.88  ? 244 TYR B CD2 1 
ATOM   6128 C CE1 . TYR C 1 245 ? -3.618  52.734  -7.556  1.00 25.98  ? 244 TYR B CE1 1 
ATOM   6129 C CE2 . TYR C 1 245 ? -4.336  53.673  -9.646  1.00 32.12  ? 244 TYR B CE2 1 
ATOM   6130 C CZ  . TYR C 1 245 ? -4.627  53.046  -8.448  1.00 39.61  ? 244 TYR B CZ  1 
ATOM   6131 O OH  . TYR C 1 245 ? -5.932  52.731  -8.149  1.00 34.52  ? 244 TYR B OH  1 
ATOM   6132 N N   . HIS C 1 246 ? -0.054  52.007  -11.763 1.00 28.51  ? 245 HIS B N   1 
ATOM   6133 C CA  . HIS C 1 246 ? -0.644  51.071  -12.712 1.00 20.43  ? 245 HIS B CA  1 
ATOM   6134 C C   . HIS C 1 246 ? 0.157   49.781  -12.830 1.00 22.09  ? 245 HIS B C   1 
ATOM   6135 O O   . HIS C 1 246 ? -0.432  48.714  -13.035 1.00 23.22  ? 245 HIS B O   1 
ATOM   6136 C CB  . HIS C 1 246 ? -0.793  51.748  -14.073 1.00 20.85  ? 245 HIS B CB  1 
ATOM   6137 C CG  . HIS C 1 246 ? -1.800  52.857  -14.073 1.00 36.19  ? 245 HIS B CG  1 
ATOM   6138 N ND1 . HIS C 1 246 ? -1.538  54.105  -14.595 1.00 33.16  ? 245 HIS B ND1 1 
ATOM   6139 C CD2 . HIS C 1 246 ? -3.065  52.909  -13.591 1.00 28.94  ? 245 HIS B CD2 1 
ATOM   6140 C CE1 . HIS C 1 246 ? -2.601  54.875  -14.444 1.00 33.45  ? 245 HIS B CE1 1 
ATOM   6141 N NE2 . HIS C 1 246 ? -3.541  54.174  -13.837 1.00 36.81  ? 245 HIS B NE2 1 
ATOM   6142 N N   . GLU C 1 247 ? 1.485   49.848  -12.684 1.00 19.25  ? 246 GLU B N   1 
ATOM   6143 C CA  . GLU C 1 247 ? 2.301   48.644  -12.819 1.00 22.59  ? 246 GLU B CA  1 
ATOM   6144 C C   . GLU C 1 247 ? 2.126   47.711  -11.629 1.00 25.64  ? 246 GLU B C   1 
ATOM   6145 O O   . GLU C 1 247 ? 2.058   46.487  -11.797 1.00 26.44  ? 246 GLU B O   1 
ATOM   6146 C CB  . GLU C 1 247 ? 3.774   49.015  -12.981 1.00 24.15  ? 246 GLU B CB  1 
ATOM   6147 C CG  . GLU C 1 247 ? 4.130   49.515  -14.365 1.00 38.58  ? 246 GLU B CG  1 
ATOM   6148 C CD  . GLU C 1 247 ? 4.169   48.396  -15.392 1.00 46.48  ? 246 GLU B CD  1 
ATOM   6149 O OE1 . GLU C 1 247 ? 4.349   47.221  -14.993 1.00 36.25  ? 246 GLU B OE1 1 
ATOM   6150 O OE2 . GLU C 1 247 ? 4.015   48.694  -16.598 1.00 46.81  ? 246 GLU B OE2 1 
ATOM   6151 N N   . THR C 1 248 ? 2.068   48.261  -10.418 1.00 20.58  ? 247 THR B N   1 
ATOM   6152 C CA  . THR C 1 248 ? 1.931   47.425  -9.235  1.00 23.86  ? 247 THR B CA  1 
ATOM   6153 C C   . THR C 1 248 ? 0.484   47.182  -8.842  1.00 17.73  ? 247 THR B C   1 
ATOM   6154 O O   . THR C 1 248 ? 0.198   46.168  -8.197  1.00 20.87  ? 247 THR B O   1 
ATOM   6155 C CB  . THR C 1 248 ? 2.674   48.052  -8.054  1.00 20.12  ? 247 THR B CB  1 
ATOM   6156 O OG1 . THR C 1 248 ? 2.046   49.294  -7.708  1.00 17.20  ? 247 THR B OG1 1 
ATOM   6157 C CG2 . THR C 1 248 ? 4.130   48.304  -8.421  1.00 22.05  ? 247 THR B CG2 1 
ATOM   6158 N N   . GLY C 1 249 ? -0.432  48.065  -9.234  1.00 22.40  ? 248 GLY B N   1 
ATOM   6159 C CA  . GLY C 1 249 ? -1.793  47.991  -8.748  1.00 22.66  ? 248 GLY B CA  1 
ATOM   6160 C C   . GLY C 1 249 ? -1.947  48.325  -7.283  1.00 27.37  ? 248 GLY B C   1 
ATOM   6161 O O   . GLY C 1 249 ? -3.008  48.058  -6.710  1.00 26.12  ? 248 GLY B O   1 
ATOM   6162 N N   . ASP C 1 250 ? -0.924  48.917  -6.666  1.00 25.47  ? 249 ASP B N   1 
ATOM   6163 C CA  . ASP C 1 250 ? -0.887  49.172  -5.231  1.00 23.90  ? 249 ASP B CA  1 
ATOM   6164 C C   . ASP C 1 250 ? -1.190  50.640  -4.964  1.00 24.32  ? 249 ASP B C   1 
ATOM   6165 O O   . ASP C 1 250 ? -0.454  51.519  -5.423  1.00 26.26  ? 249 ASP B O   1 
ATOM   6166 C CB  . ASP C 1 250 ? 0.485   48.798  -4.665  1.00 24.92  ? 249 ASP B CB  1 
ATOM   6167 C CG  . ASP C 1 250 ? 0.514   48.776  -3.141  1.00 35.28  ? 249 ASP B CG  1 
ATOM   6168 O OD1 . ASP C 1 250 ? -0.420  49.311  -2.506  1.00 28.68  ? 249 ASP B OD1 1 
ATOM   6169 O OD2 . ASP C 1 250 ? 1.487   48.226  -2.578  1.00 32.69  ? 249 ASP B OD2 1 
ATOM   6170 N N   . SER C 1 251 ? -2.252  50.899  -4.192  1.00 25.45  ? 250 SER B N   1 
ATOM   6171 C CA  . SER C 1 251 ? -2.634  52.264  -3.836  1.00 23.57  ? 250 SER B CA  1 
ATOM   6172 C C   . SER C 1 251 ? -1.552  52.993  -3.053  1.00 27.98  ? 250 SER B C   1 
ATOM   6173 O O   . SER C 1 251 ? -1.676  54.204  -2.836  1.00 22.27  ? 250 SER B O   1 
ATOM   6174 C CB  . SER C 1 251 ? -3.931  52.258  -3.021  1.00 29.81  ? 250 SER B CB  1 
ATOM   6175 O OG  . SER C 1 251 ? -5.041  51.907  -3.828  1.00 41.21  ? 250 SER B OG  1 
ATOM   6176 N N   . LYS C 1 252 ? -0.505  52.285  -2.623  1.00 23.98  ? 251 LYS B N   1 
ATOM   6177 C CA  . LYS C 1 252 ? 0.629   52.929  -1.970  1.00 20.75  ? 251 LYS B CA  1 
ATOM   6178 C C   . LYS C 1 252 ? 1.254   54.004  -2.856  1.00 27.96  ? 251 LYS B C   1 
ATOM   6179 O O   . LYS C 1 252 ? 1.806   54.989  -2.348  1.00 29.48  ? 251 LYS B O   1 
ATOM   6180 C CB  . LYS C 1 252 ? 1.654   51.856  -1.592  1.00 24.14  ? 251 LYS B CB  1 
ATOM   6181 C CG  . LYS C 1 252 ? 3.069   52.341  -1.402  1.00 31.97  ? 251 LYS B CG  1 
ATOM   6182 C CD  . LYS C 1 252 ? 3.988   51.196  -1.014  1.00 27.85  ? 251 LYS B CD  1 
ATOM   6183 C CE  . LYS C 1 252 ? 5.393   51.709  -0.760  1.00 26.11  ? 251 LYS B CE  1 
ATOM   6184 N NZ  . LYS C 1 252 ? 6.179   50.793  0.106   1.00 26.22  ? 251 LYS B NZ  1 
ATOM   6185 N N   . TYR C 1 253 ? 1.149   53.852  -4.177  1.00 28.57  ? 252 TYR B N   1 
ATOM   6186 C CA  . TYR C 1 253 ? 1.778   54.755  -5.133  1.00 33.50  ? 252 TYR B CA  1 
ATOM   6187 C C   . TYR C 1 253 ? 0.789   55.713  -5.790  1.00 24.19  ? 252 TYR B C   1 
ATOM   6188 O O   . TYR C 1 253 ? 1.102   56.287  -6.836  1.00 24.74  ? 252 TYR B O   1 
ATOM   6189 C CB  . TYR C 1 253 ? 2.517   53.949  -6.204  1.00 25.07  ? 252 TYR B CB  1 
ATOM   6190 C CG  . TYR C 1 253 ? 3.568   53.038  -5.631  1.00 24.45  ? 252 TYR B CG  1 
ATOM   6191 C CD1 . TYR C 1 253 ? 4.719   53.560  -5.060  1.00 24.88  ? 252 TYR B CD1 1 
ATOM   6192 C CD2 . TYR C 1 253 ? 3.404   51.659  -5.641  1.00 24.43  ? 252 TYR B CD2 1 
ATOM   6193 C CE1 . TYR C 1 253 ? 5.685   52.738  -4.521  1.00 24.94  ? 252 TYR B CE1 1 
ATOM   6194 C CE2 . TYR C 1 253 ? 4.365   50.826  -5.102  1.00 26.49  ? 252 TYR B CE2 1 
ATOM   6195 C CZ  . TYR C 1 253 ? 5.505   51.373  -4.544  1.00 24.18  ? 252 TYR B CZ  1 
ATOM   6196 O OH  . TYR C 1 253 ? 6.470   50.559  -4.003  1.00 27.15  ? 252 TYR B OH  1 
ATOM   6197 N N   . ARG C 1 254 ? -0.391  55.908  -5.198  1.00 25.58  ? 253 ARG B N   1 
ATOM   6198 C CA  . ARG C 1 254 ? -1.369  56.811  -5.791  1.00 25.94  ? 253 ARG B CA  1 
ATOM   6199 C C   . ARG C 1 254 ? -0.838  58.239  -5.790  1.00 25.40  ? 253 ARG B C   1 
ATOM   6200 O O   . ARG C 1 254 ? -0.351  58.735  -4.770  1.00 23.26  ? 253 ARG B O   1 
ATOM   6201 C CB  . ARG C 1 254 ? -2.706  56.734  -5.047  1.00 25.12  ? 253 ARG B CB  1 
ATOM   6202 C CG  . ARG C 1 254 ? -2.662  57.078  -3.560  1.00 21.20  ? 253 ARG B CG  1 
ATOM   6203 C CD  . ARG C 1 254 ? -3.983  56.713  -2.887  1.00 20.49  ? 253 ARG B CD  1 
ATOM   6204 N NE  . ARG C 1 254 ? -4.128  57.315  -1.566  1.00 35.80  ? 253 ARG B NE  1 
ATOM   6205 C CZ  . ARG C 1 254 ? -3.566  56.838  -0.463  1.00 38.48  ? 253 ARG B CZ  1 
ATOM   6206 N NH1 . ARG C 1 254 ? -2.818  55.744  -0.483  1.00 29.98  ? 253 ARG B NH1 1 
ATOM   6207 N NH2 . ARG C 1 254 ? -3.758  57.473  0.689   1.00 47.58  ? 253 ARG B NH2 1 
ATOM   6208 N N   . ALA C 1 255 ? -0.920  58.890  -6.946  1.00 25.17  ? 254 ALA B N   1 
ATOM   6209 C CA  . ALA C 1 255 ? -0.392  60.239  -7.087  1.00 22.77  ? 254 ALA B CA  1 
ATOM   6210 C C   . ALA C 1 255 ? -1.161  61.215  -6.207  1.00 24.58  ? 254 ALA B C   1 
ATOM   6211 O O   . ALA C 1 255 ? -2.386  61.122  -6.069  1.00 20.75  ? 254 ALA B O   1 
ATOM   6212 C CB  . ALA C 1 255 ? -0.458  60.681  -8.550  1.00 18.16  ? 254 ALA B CB  1 
ATOM   6213 N N   . CYS C 1 256 ? -0.432  62.154  -5.608  1.00 20.04  ? 255 CYS B N   1 
ATOM   6214 C CA  . CYS C 1 256 ? -1.059  63.140  -4.739  1.00 23.59  ? 255 CYS B CA  1 
ATOM   6215 C C   . CYS C 1 256 ? -1.950  64.058  -5.565  1.00 25.25  ? 255 CYS B C   1 
ATOM   6216 O O   . CYS C 1 256 ? -1.487  64.630  -6.559  1.00 24.11  ? 255 CYS B O   1 
ATOM   6217 C CB  . CYS C 1 256 ? -0.008  63.962  -4.002  1.00 22.22  ? 255 CYS B CB  1 
ATOM   6218 S SG  . CYS C 1 256 ? -0.688  65.389  -3.115  1.00 23.30  ? 255 CYS B SG  1 
ATOM   6219 N N   . PRO C 1 257 ? -3.220  64.227  -5.193  1.00 29.66  ? 256 PRO B N   1 
ATOM   6220 C CA  . PRO C 1 257 ? -4.124  65.050  -6.015  1.00 27.05  ? 256 PRO B CA  1 
ATOM   6221 C C   . PRO C 1 257 ? -3.670  66.491  -6.167  1.00 27.87  ? 256 PRO B C   1 
ATOM   6222 O O   . PRO C 1 257 ? -4.050  67.143  -7.149  1.00 24.37  ? 256 PRO B O   1 
ATOM   6223 C CB  . PRO C 1 257 ? -5.463  64.957  -5.269  1.00 27.13  ? 256 PRO B CB  1 
ATOM   6224 C CG  . PRO C 1 257 ? -5.361  63.699  -4.449  1.00 30.17  ? 256 PRO B CG  1 
ATOM   6225 C CD  . PRO C 1 257 ? -3.911  63.610  -4.049  1.00 29.68  ? 256 PRO B CD  1 
ATOM   6226 N N   . LEU C 1 258 ? -2.861  67.008  -5.240  1.00 24.29  ? 257 LEU B N   1 
ATOM   6227 C CA  . LEU C 1 258 ? -2.346  68.365  -5.392  1.00 22.94  ? 257 LEU B CA  1 
ATOM   6228 C C   . LEU C 1 258 ? -1.407  68.471  -6.588  1.00 28.62  ? 257 LEU B C   1 
ATOM   6229 O O   . LEU C 1 258 ? -1.401  69.489  -7.288  1.00 21.37  ? 257 LEU B O   1 
ATOM   6230 C CB  . LEU C 1 258 ? -1.637  68.804  -4.112  1.00 26.62  ? 257 LEU B CB  1 
ATOM   6231 C CG  . LEU C 1 258 ? -0.912  70.149  -4.152  1.00 24.14  ? 257 LEU B CG  1 
ATOM   6232 C CD1 . LEU C 1 258 ? -1.858  71.261  -4.592  1.00 17.37  ? 257 LEU B CD1 1 
ATOM   6233 C CD2 . LEU C 1 258 ? -0.318  70.458  -2.784  1.00 25.38  ? 257 LEU B CD2 1 
ATOM   6234 N N   . ILE C 1 259 ? -0.607  67.433  -6.844  1.00 20.03  ? 258 ILE B N   1 
ATOM   6235 C CA  . ILE C 1 259 ? 0.283   67.473  -8.000  1.00 23.46  ? 258 ILE B CA  1 
ATOM   6236 C C   . ILE C 1 259 ? -0.516  67.347  -9.290  1.00 23.35  ? 258 ILE B C   1 
ATOM   6237 O O   . ILE C 1 259 ? -0.252  68.053  -10.270 1.00 24.64  ? 258 ILE B O   1 
ATOM   6238 C CB  . ILE C 1 259 ? 1.360   66.379  -7.893  1.00 28.51  ? 258 ILE B CB  1 
ATOM   6239 C CG1 . ILE C 1 259 ? 2.331   66.693  -6.754  1.00 12.09  ? 258 ILE B CG1 1 
ATOM   6240 C CG2 . ILE C 1 259 ? 2.112   66.247  -9.212  1.00 14.11  ? 258 ILE B CG2 1 
ATOM   6241 C CD1 . ILE C 1 259 ? 3.189   65.514  -6.354  1.00 15.38  ? 258 ILE B CD1 1 
ATOM   6242 N N   . ARG C 1 260 ? -1.506  66.451  -9.313  1.00 25.47  ? 259 ARG B N   1 
ATOM   6243 C CA  . ARG C 1 260 ? -2.333  66.306  -10.505 1.00 28.45  ? 259 ARG B CA  1 
ATOM   6244 C C   . ARG C 1 260 ? -3.075  67.598  -10.828 1.00 28.01  ? 259 ARG B C   1 
ATOM   6245 O O   . ARG C 1 260 ? -3.236  67.941  -12.004 1.00 28.07  ? 259 ARG B O   1 
ATOM   6246 C CB  . ARG C 1 260 ? -3.314  65.142  -10.334 1.00 19.86  ? 259 ARG B CB  1 
ATOM   6247 C CG  . ARG C 1 260 ? -3.789  64.556  -11.663 1.00 24.85  ? 259 ARG B CG  1 
ATOM   6248 C CD  . ARG C 1 260 ? -4.804  63.431  -11.493 1.00 24.56  ? 259 ARG B CD  1 
ATOM   6249 N NE  . ARG C 1 260 ? -4.223  62.230  -10.904 1.00 30.74  ? 259 ARG B NE  1 
ATOM   6250 C CZ  . ARG C 1 260 ? -3.447  61.374  -11.555 1.00 27.66  ? 259 ARG B CZ  1 
ATOM   6251 N NH1 . ARG C 1 260 ? -3.117  61.564  -12.823 1.00 29.24  ? 259 ARG B NH1 1 
ATOM   6252 N NH2 . ARG C 1 260 ? -2.983  60.303  -10.915 1.00 26.45  ? 259 ARG B NH2 1 
ATOM   6253 N N   . LYS C 1 261 ? -3.506  68.338  -9.803  1.00 29.74  ? 260 LYS B N   1 
ATOM   6254 C CA  . LYS C 1 261 ? -4.144  69.632  -10.033 1.00 26.11  ? 260 LYS B CA  1 
ATOM   6255 C C   . LYS C 1 261 ? -3.159  70.640  -10.614 1.00 32.84  ? 260 LYS B C   1 
ATOM   6256 O O   . LYS C 1 261 ? -3.521  71.443  -11.483 1.00 27.92  ? 260 LYS B O   1 
ATOM   6257 C CB  . LYS C 1 261 ? -4.740  70.159  -8.726  1.00 31.06  ? 260 LYS B CB  1 
ATOM   6258 C CG  . LYS C 1 261 ? -5.392  71.533  -8.834  1.00 34.31  ? 260 LYS B CG  1 
ATOM   6259 C CD  . LYS C 1 261 ? -5.515  72.193  -7.466  1.00 31.73  ? 260 LYS B CD  1 
ATOM   6260 C CE  . LYS C 1 261 ? -6.656  71.594  -6.672  1.00 34.47  ? 260 LYS B CE  1 
ATOM   6261 N NZ  . LYS C 1 261 ? -6.729  72.117  -5.276  1.00 27.44  ? 260 LYS B NZ  1 
ATOM   6262 N N   . MET C 1 262 ? -1.908  70.611  -10.151 1.00 24.91  ? 261 MET B N   1 
ATOM   6263 C CA  . MET C 1 262 ? -0.924  71.579  -10.623 1.00 27.20  ? 261 MET B CA  1 
ATOM   6264 C C   . MET C 1 262 ? -0.512  71.292  -12.061 1.00 26.57  ? 261 MET B C   1 
ATOM   6265 O O   . MET C 1 262 ? -0.303  72.221  -12.851 1.00 28.88  ? 261 MET B O   1 
ATOM   6266 C CB  . MET C 1 262 ? 0.293   71.560  -9.706  1.00 22.34  ? 261 MET B CB  1 
ATOM   6267 C CG  . MET C 1 262 ? 0.039   72.198  -8.362  1.00 30.74  ? 261 MET B CG  1 
ATOM   6268 S SD  . MET C 1 262 ? 1.287   71.726  -7.160  1.00 31.02  ? 261 MET B SD  1 
ATOM   6269 C CE  . MET C 1 262 ? 2.659   72.747  -7.681  1.00 32.56  ? 261 MET B CE  1 
ATOM   6270 N N   . VAL C 1 263 ? -0.379  70.010  -12.412 1.00 19.04  ? 262 VAL B N   1 
ATOM   6271 C CA  . VAL C 1 263 ? -0.019  69.640  -13.776 1.00 29.63  ? 262 VAL B CA  1 
ATOM   6272 C C   . VAL C 1 263 ? -1.145  69.996  -14.738 1.00 24.06  ? 262 VAL B C   1 
ATOM   6273 O O   . VAL C 1 263 ? -0.898  70.428  -15.870 1.00 27.90  ? 262 VAL B O   1 
ATOM   6274 C CB  . VAL C 1 263 ? 0.340   68.145  -13.839 1.00 22.63  ? 262 VAL B CB  1 
ATOM   6275 C CG1 . VAL C 1 263 ? 0.317   67.637  -15.274 1.00 22.82  ? 262 VAL B CG1 1 
ATOM   6276 C CG2 . VAL C 1 263 ? 1.704   67.913  -13.206 1.00 23.49  ? 262 VAL B CG2 1 
ATOM   6277 N N   . ARG C 1 264 ? -2.396  69.836  -14.302 1.00 26.45  ? 263 ARG B N   1 
ATOM   6278 C CA  . ARG C 1 264 ? -3.527  70.196  -15.148 1.00 28.12  ? 263 ARG B CA  1 
ATOM   6279 C C   . ARG C 1 264 ? -3.577  71.692  -15.426 1.00 31.52  ? 263 ARG B C   1 
ATOM   6280 O O   . ARG C 1 264 ? -4.190  72.107  -16.414 1.00 36.84  ? 263 ARG B O   1 
ATOM   6281 C CB  . ARG C 1 264 ? -4.836  69.738  -14.503 1.00 27.27  ? 263 ARG B CB  1 
ATOM   6282 C CG  . ARG C 1 264 ? -5.317  68.366  -14.951 1.00 24.11  ? 263 ARG B CG  1 
ATOM   6283 C CD  . ARG C 1 264 ? -5.986  67.625  -13.802 1.00 25.71  ? 263 ARG B CD  1 
ATOM   6284 N NE  . ARG C 1 264 ? -6.563  66.350  -14.218 1.00 22.98  ? 263 ARG B NE  1 
ATOM   6285 C CZ  . ARG C 1 264 ? -7.327  65.591  -13.443 1.00 22.08  ? 263 ARG B CZ  1 
ATOM   6286 N NH1 . ARG C 1 264 ? -7.633  65.952  -12.207 1.00 26.92  ? 263 ARG B NH1 1 
ATOM   6287 N NH2 . ARG C 1 264 ? -7.800  64.443  -13.921 1.00 16.11  ? 263 ARG B NH2 1 
ATOM   6288 N N   . GLY C 1 265 ? -2.943  72.507  -14.586 1.00 21.50  ? 264 GLY B N   1 
ATOM   6289 C CA  . GLY C 1 265 ? -2.882  73.937  -14.789 1.00 32.74  ? 264 GLY B CA  1 
ATOM   6290 C C   . GLY C 1 265 ? -1.642  74.452  -15.481 1.00 31.62  ? 264 GLY B C   1 
ATOM   6291 O O   . GLY C 1 265 ? -1.531  75.662  -15.698 1.00 30.96  ? 264 GLY B O   1 
ATOM   6292 N N   . GLY C 1 266 ? -0.704  73.577  -15.836 1.00 29.00  ? 265 GLY B N   1 
ATOM   6293 C CA  . GLY C 1 266 ? 0.535   74.007  -16.447 1.00 21.88  ? 265 GLY B CA  1 
ATOM   6294 C C   . GLY C 1 266 ? 1.597   74.478  -15.481 1.00 29.56  ? 265 GLY B C   1 
ATOM   6295 O O   . GLY C 1 266 ? 2.640   74.970  -15.929 1.00 31.05  ? 265 GLY B O   1 
ATOM   6296 N N   . ASN C 1 267 ? 1.368   74.346  -14.171 1.00 27.61  ? 266 ASN B N   1 
ATOM   6297 C CA  . ASN C 1 267 ? 2.349   74.719  -13.150 1.00 28.01  ? 266 ASN B CA  1 
ATOM   6298 C C   . ASN C 1 267 ? 3.335   73.563  -12.990 1.00 33.55  ? 266 ASN B C   1 
ATOM   6299 O O   . ASN C 1 267 ? 3.291   72.784  -12.034 1.00 27.00  ? 266 ASN B O   1 
ATOM   6300 C CB  . ASN C 1 267 ? 1.661   75.050  -11.830 1.00 32.27  ? 266 ASN B CB  1 
ATOM   6301 C CG  . ASN C 1 267 ? 0.615   76.148  -11.966 1.00 32.76  ? 266 ASN B CG  1 
ATOM   6302 O OD1 . ASN C 1 267 ? 0.009   76.325  -13.021 1.00 40.52  ? 266 ASN B OD1 1 
ATOM   6303 N ND2 . ASN C 1 267 ? 0.392   76.881  -10.884 1.00 43.78  ? 266 ASN B ND2 1 
ATOM   6304 N N   . LEU C 1 268 ? 4.253   73.459  -13.949 1.00 32.75  ? 267 LEU B N   1 
ATOM   6305 C CA  . LEU C 1 268 ? 5.130   72.299  -14.034 1.00 31.28  ? 267 LEU B CA  1 
ATOM   6306 C C   . LEU C 1 268 ? 6.444   72.464  -13.283 1.00 29.99  ? 267 LEU B C   1 
ATOM   6307 O O   . LEU C 1 268 ? 7.164   71.485  -13.106 1.00 26.09  ? 267 LEU B O   1 
ATOM   6308 C CB  . LEU C 1 268 ? 5.421   71.972  -15.501 1.00 30.74  ? 267 LEU B CB  1 
ATOM   6309 C CG  . LEU C 1 268 ? 4.167   71.768  -16.354 1.00 30.11  ? 267 LEU B CG  1 
ATOM   6310 C CD1 . LEU C 1 268 ? 4.532   71.299  -17.749 1.00 32.96  ? 267 LEU B CD1 1 
ATOM   6311 C CD2 . LEU C 1 268 ? 3.229   70.777  -15.677 1.00 29.95  ? 267 LEU B CD2 1 
ATOM   6312 N N   . GLY C 1 269 ? 6.776   73.681  -12.825 1.00 29.93  ? 268 GLY B N   1 
ATOM   6313 C CA  . GLY C 1 269 ? 8.000   73.934  -12.096 1.00 30.01  ? 268 GLY B CA  1 
ATOM   6314 C C   . GLY C 1 269 ? 8.902   74.891  -12.856 1.00 31.77  ? 268 GLY B C   1 
ATOM   6315 O O   . GLY C 1 269 ? 8.430   75.896  -13.415 1.00 28.63  ? 268 GLY B O   1 
ATOM   6316 N N   . CYS C 1 270 ? 10.195  74.580  -12.870 1.00 28.84  ? 269 CYS B N   1 
ATOM   6317 C CA  . CYS C 1 270 ? 11.178  75.452  -13.503 1.00 34.23  ? 269 CYS B CA  1 
ATOM   6318 C C   . CYS C 1 270 ? 10.870  75.662  -14.979 1.00 36.95  ? 269 CYS B C   1 
ATOM   6319 O O   . CYS C 1 270 ? 11.015  76.776  -15.493 1.00 42.96  ? 269 CYS B O   1 
ATOM   6320 C CB  . CYS C 1 270 ? 12.585  74.865  -13.336 1.00 32.42  ? 269 CYS B CB  1 
ATOM   6321 S SG  . CYS C 1 270 ? 13.131  74.688  -11.621 1.00 37.85  ? 269 CYS B SG  1 
ATOM   6322 N N   . LYS C 1 271 ? 10.440  74.609  -15.677 1.00 27.87  ? 270 LYS B N   1 
ATOM   6323 C CA  . LYS C 1 271 ? 10.272  74.704  -17.123 1.00 29.95  ? 270 LYS B CA  1 
ATOM   6324 C C   . LYS C 1 271 ? 9.083   75.564  -17.535 1.00 32.13  ? 270 LYS B C   1 
ATOM   6325 O O   . LYS C 1 271 ? 8.973   75.904  -18.717 1.00 29.17  ? 270 LYS B O   1 
ATOM   6326 C CB  . LYS C 1 271 ? 10.159  73.303  -17.729 1.00 28.75  ? 270 LYS B CB  1 
ATOM   6327 C CG  . LYS C 1 271 ? 8.985   72.480  -17.240 1.00 32.93  ? 270 LYS B CG  1 
ATOM   6328 C CD  . LYS C 1 271 ? 9.270   71.007  -17.461 1.00 34.88  ? 270 LYS B CD  1 
ATOM   6329 C CE  . LYS C 1 271 ? 8.077   70.274  -18.025 1.00 42.03  ? 270 LYS B CE  1 
ATOM   6330 N NZ  . LYS C 1 271 ? 8.470   68.916  -18.498 1.00 41.46  ? 270 LYS B NZ  1 
ATOM   6331 N N   . THR C 1 272 ? 8.197   75.927  -16.605 1.00 33.29  ? 271 THR B N   1 
ATOM   6332 C CA  . THR C 1 272 ? 7.148   76.907  -16.868 1.00 30.05  ? 271 THR B CA  1 
ATOM   6333 C C   . THR C 1 272 ? 7.226   78.099  -15.923 1.00 34.96  ? 271 THR B C   1 
ATOM   6334 O O   . THR C 1 272 ? 6.274   78.887  -15.858 1.00 35.22  ? 271 THR B O   1 
ATOM   6335 C CB  . THR C 1 272 ? 5.754   76.273  -16.772 1.00 33.06  ? 271 THR B CB  1 
ATOM   6336 O OG1 . THR C 1 272 ? 5.458   75.957  -15.404 1.00 35.66  ? 271 THR B OG1 1 
ATOM   6337 C CG2 . THR C 1 272 ? 5.665   75.012  -17.624 1.00 21.80  ? 271 THR B CG2 1 
ATOM   6338 N N   . GLY C 1 273 ? 8.324   78.247  -15.181 1.00 32.95  ? 272 GLY B N   1 
ATOM   6339 C CA  . GLY C 1 273 ? 8.486   79.341  -14.246 1.00 36.48  ? 272 GLY B CA  1 
ATOM   6340 C C   . GLY C 1 273 ? 7.628   79.271  -13.004 1.00 35.27  ? 272 GLY B C   1 
ATOM   6341 O O   . GLY C 1 273 ? 7.828   80.083  -12.090 1.00 35.33  ? 272 GLY B O   1 
ATOM   6342 N N   . LYS C 1 274 ? 6.683   78.334  -12.931 1.00 34.19  ? 273 LYS B N   1 
ATOM   6343 C CA  . LYS C 1 274 ? 5.800   78.203  -11.781 1.00 36.52  ? 273 LYS B CA  1 
ATOM   6344 C C   . LYS C 1 274 ? 5.543   76.733  -11.496 1.00 38.33  ? 273 LYS B C   1 
ATOM   6345 O O   . LYS C 1 274 ? 5.140   75.984  -12.392 1.00 31.27  ? 273 LYS B O   1 
ATOM   6346 C CB  . LYS C 1 274 ? 4.466   78.922  -12.013 1.00 33.91  ? 273 LYS B CB  1 
ATOM   6347 C CG  . LYS C 1 274 ? 3.565   78.937  -10.793 1.00 32.95  ? 273 LYS B CG  1 
ATOM   6348 C CD  . LYS C 1 274 ? 2.600   80.104  -10.835 1.00 38.59  ? 273 LYS B CD  1 
ATOM   6349 C CE  . LYS C 1 274 ? 1.420   79.871  -9.906  1.00 37.83  ? 273 LYS B CE  1 
ATOM   6350 N NZ  . LYS C 1 274 ? 0.139   80.345  -10.501 1.00 45.46  ? 273 LYS B NZ  1 
ATOM   6351 N N   . GLY C 1 275 ? 5.782   76.334  -10.250 1.00 32.74  ? 274 GLY B N   1 
ATOM   6352 C CA  . GLY C 1 275 ? 5.396   75.031  -9.745  1.00 28.86  ? 274 GLY B CA  1 
ATOM   6353 C C   . GLY C 1 275 ? 4.992   75.164  -8.291  1.00 32.69  ? 274 GLY B C   1 
ATOM   6354 O O   . GLY C 1 275 ? 4.026   75.867  -7.977  1.00 31.02  ? 274 GLY B O   1 
ATOM   6355 N N   . PHE C 1 276 ? 5.722   74.502  -7.390  1.00 32.91  ? 275 PHE B N   1 
ATOM   6356 C CA  . PHE C 1 276 ? 5.580   74.805  -5.970  1.00 32.68  ? 275 PHE B CA  1 
ATOM   6357 C C   . PHE C 1 276 ? 6.219   76.140  -5.619  1.00 29.35  ? 275 PHE B C   1 
ATOM   6358 O O   . PHE C 1 276 ? 5.882   76.725  -4.584  1.00 34.88  ? 275 PHE B O   1 
ATOM   6359 C CB  . PHE C 1 276 ? 6.190   73.689  -5.120  1.00 28.94  ? 275 PHE B CB  1 
ATOM   6360 C CG  . PHE C 1 276 ? 5.333   72.457  -5.036  1.00 30.82  ? 275 PHE B CG  1 
ATOM   6361 C CD1 . PHE C 1 276 ? 4.191   72.446  -4.253  1.00 31.70  ? 275 PHE B CD1 1 
ATOM   6362 C CD2 . PHE C 1 276 ? 5.665   71.315  -5.747  1.00 27.16  ? 275 PHE B CD2 1 
ATOM   6363 C CE1 . PHE C 1 276 ? 3.399   71.317  -4.175  1.00 26.38  ? 275 PHE B CE1 1 
ATOM   6364 C CE2 . PHE C 1 276 ? 4.880   70.185  -5.673  1.00 29.30  ? 275 PHE B CE2 1 
ATOM   6365 C CZ  . PHE C 1 276 ? 3.743   70.185  -4.885  1.00 29.72  ? 275 PHE B CZ  1 
ATOM   6366 N N   . TYR C 1 277 ? 7.134   76.622  -6.457  1.00 32.34  ? 276 TYR B N   1 
ATOM   6367 C CA  . TYR C 1 277 ? 7.718   77.949  -6.349  1.00 34.13  ? 276 TYR B CA  1 
ATOM   6368 C C   . TYR C 1 277 ? 7.441   78.730  -7.626  1.00 36.65  ? 276 TYR B C   1 
ATOM   6369 O O   . TYR C 1 277 ? 7.238   78.153  -8.699  1.00 31.51  ? 276 TYR B O   1 
ATOM   6370 C CB  . TYR C 1 277 ? 9.236   77.886  -6.121  1.00 31.69  ? 276 TYR B CB  1 
ATOM   6371 C CG  . TYR C 1 277 ? 9.658   77.250  -4.818  1.00 38.81  ? 276 TYR B CG  1 
ATOM   6372 C CD1 . TYR C 1 277 ? 9.766   75.870  -4.700  1.00 32.38  ? 276 TYR B CD1 1 
ATOM   6373 C CD2 . TYR C 1 277 ? 9.969   78.030  -3.710  1.00 33.04  ? 276 TYR B CD2 1 
ATOM   6374 C CE1 . TYR C 1 277 ? 10.158  75.284  -3.512  1.00 30.27  ? 276 TYR B CE1 1 
ATOM   6375 C CE2 . TYR C 1 277 ? 10.362  77.453  -2.520  1.00 27.41  ? 276 TYR B CE2 1 
ATOM   6376 C CZ  . TYR C 1 277 ? 10.456  76.079  -2.427  1.00 30.48  ? 276 TYR B CZ  1 
ATOM   6377 O OH  . TYR C 1 277 ? 10.849  75.499  -1.246  1.00 35.48  ? 276 TYR B OH  1 
ATOM   6378 N N   . VAL C 1 278 ? 7.433   80.057  -7.501  1.00 40.92  ? 277 VAL B N   1 
ATOM   6379 C CA  . VAL C 1 278 ? 7.470   80.956  -8.650  1.00 35.53  ? 277 VAL B CA  1 
ATOM   6380 C C   . VAL C 1 278 ? 8.909   81.410  -8.829  1.00 35.02  ? 277 VAL B C   1 
ATOM   6381 O O   . VAL C 1 278 ? 9.550   81.857  -7.869  1.00 38.12  ? 277 VAL B O   1 
ATOM   6382 C CB  . VAL C 1 278 ? 6.529   82.159  -8.463  1.00 31.41  ? 277 VAL B CB  1 
ATOM   6383 C CG1 . VAL C 1 278 ? 6.843   83.239  -9.489  1.00 33.60  ? 277 VAL B CG1 1 
ATOM   6384 C CG2 . VAL C 1 278 ? 5.073   81.724  -8.571  1.00 30.81  ? 277 VAL B CG2 1 
ATOM   6385 N N   . TYR C 1 279 ? 9.423   81.287  -10.051 1.00 36.10  ? 278 TYR B N   1 
ATOM   6386 C CA  . TYR C 1 279 ? 10.826  81.559  -10.351 1.00 38.51  ? 278 TYR B CA  1 
ATOM   6387 C C   . TYR C 1 279 ? 10.939  82.938  -10.989 1.00 43.54  ? 278 TYR B C   1 
ATOM   6388 O O   . TYR C 1 279 ? 10.509  83.141  -12.129 1.00 47.17  ? 278 TYR B O   1 
ATOM   6389 C CB  . TYR C 1 279 ? 11.392  80.465  -11.252 1.00 34.21  ? 278 TYR B CB  1 
ATOM   6390 C CG  . TYR C 1 279 ? 11.433  79.141  -10.537 1.00 38.21  ? 278 TYR B CG  1 
ATOM   6391 C CD1 . TYR C 1 279 ? 12.526  78.792  -9.758  1.00 33.86  ? 278 TYR B CD1 1 
ATOM   6392 C CD2 . TYR C 1 279 ? 10.356  78.265  -10.593 1.00 35.89  ? 278 TYR B CD2 1 
ATOM   6393 C CE1 . TYR C 1 279 ? 12.562  77.596  -9.081  1.00 34.15  ? 278 TYR B CE1 1 
ATOM   6394 C CE2 . TYR C 1 279 ? 10.380  77.065  -9.916  1.00 31.12  ? 278 TYR B CE2 1 
ATOM   6395 C CZ  . TYR C 1 279 ? 11.486  76.736  -9.163  1.00 40.06  ? 278 TYR B CZ  1 
ATOM   6396 O OH  . TYR C 1 279 ? 11.523  75.543  -8.483  1.00 41.57  ? 278 TYR B OH  1 
ATOM   6397 N N   . ASN C 1 280 ? 11.522  83.878  -10.251 1.00 45.53  ? 279 ASN B N   1 
ATOM   6398 C CA  . ASN C 1 280 ? 11.585  85.273  -10.656 1.00 45.04  ? 279 ASN B CA  1 
ATOM   6399 C C   . ASN C 1 280 ? 12.882  85.575  -11.401 1.00 53.32  ? 279 ASN B C   1 
ATOM   6400 O O   . ASN C 1 280 ? 13.883  84.863  -11.278 1.00 54.01  ? 279 ASN B O   1 
ATOM   6401 C CB  . ASN C 1 280 ? 11.455  86.189  -9.438  1.00 49.50  ? 279 ASN B CB  1 
ATOM   6402 C CG  . ASN C 1 280 ? 10.432  85.684  -8.433  1.00 47.42  ? 279 ASN B CG  1 
ATOM   6403 O OD1 . ASN C 1 280 ? 9.247   85.566  -8.746  1.00 42.21  ? 279 ASN B OD1 1 
ATOM   6404 N ND2 . ASN C 1 280 ? 10.887  85.389  -7.218  1.00 43.14  ? 279 ASN B ND2 1 
ATOM   6405 N N   . ALA C 1 281 ? 12.871  86.672  -12.154 1.00 52.36  ? 280 ALA B N   1 
ATOM   6406 C CA  . ALA C 1 281 ? 14.047  87.045  -12.969 1.00 52.97  ? 280 ALA B CA  1 
ATOM   6407 C C   . ALA C 1 281 ? 15.262  87.364  -12.091 1.00 62.71  ? 280 ALA B C   1 
ATOM   6408 O O   . ALA C 1 281 ? 16.386  87.292  -12.606 1.00 58.04  ? 280 ALA B O   1 
ATOM   6409 C CB  . ALA C 1 281 ? 13.673  88.213  -13.827 1.00 46.89  ? 280 ALA B CB  1 
ATOM   6410 N N   . ASP C 1 282 ? 15.043  87.687  -10.816 1.00 61.21  ? 281 ASP B N   1 
ATOM   6411 C CA  . ASP C 1 282 ? 16.155  87.979  -9.880  1.00 57.70  ? 281 ASP B CA  1 
ATOM   6412 C C   . ASP C 1 282 ? 16.921  86.699  -9.559  1.00 66.55  ? 281 ASP B C   1 
ATOM   6413 O O   . ASP C 1 282 ? 17.834  86.789  -8.726  1.00 74.22  ? 281 ASP B O   1 
ATOM   6414 C CB  . ASP C 1 282 ? 15.630  88.573  -8.579  1.00 64.02  ? 281 ASP B CB  1 
ATOM   6415 C CG  . ASP C 1 282 ? 16.595  89.548  -7.932  1.00 86.69  ? 281 ASP B CG  1 
ATOM   6416 O OD1 . ASP C 1 282 ? 17.181  90.367  -8.670  1.00 91.17  ? 281 ASP B OD1 1 
ATOM   6417 O OD2 . ASP C 1 282 ? 16.760  89.476  -6.697  1.00 96.09  ? 281 ASP B OD2 1 
ATOM   6418 N N   . ARG C 1 283 ? 16.539  85.569  -10.158 1.00 67.47  ? 282 ARG B N   1 
ATOM   6419 C CA  . ARG C 1 283 ? 17.159  84.246  -9.865  1.00 68.82  ? 282 ARG B CA  1 
ATOM   6420 C C   . ARG C 1 283 ? 16.699  83.739  -8.489  1.00 61.60  ? 282 ARG B C   1 
ATOM   6421 O O   . ARG C 1 283 ? 17.317  82.789  -8.000  1.00 57.26  ? 282 ARG B O   1 
ATOM   6422 C CB  . ARG C 1 283 ? 18.681  84.306  -10.031 1.00 70.19  ? 282 ARG B CB  1 
ATOM   6423 C CG  . ARG C 1 283 ? 19.148  84.217  -11.475 1.00 69.87  ? 282 ARG B CG  1 
ATOM   6424 C CD  . ARG C 1 283 ? 20.523  83.590  -11.569 1.00 66.89  ? 282 ARG B CD  1 
ATOM   6425 N NE  . ARG C 1 283 ? 20.589  82.587  -12.620 1.00 79.20  ? 282 ARG B NE  1 
ATOM   6426 C CZ  . ARG C 1 283 ? 21.200  81.415  -12.501 1.00 84.37  ? 282 ARG B CZ  1 
ATOM   6427 N NH1 . ARG C 1 283 ? 21.890  81.136  -11.411 1.00 86.35  ? 282 ARG B NH1 1 
ATOM   6428 N NH2 . ARG C 1 283 ? 21.116  80.525  -13.474 1.00 78.07  ? 282 ARG B NH2 1 
ATOM   6429 N N   . THR C 1 284 ? 15.670  84.347  -7.892  1.00 59.84  ? 283 THR B N   1 
ATOM   6430 C CA  . THR C 1 284 ? 15.107  83.855  -6.645  1.00 61.51  ? 283 THR B CA  1 
ATOM   6431 C C   . THR C 1 284 ? 13.785  83.144  -6.909  1.00 54.11  ? 283 THR B C   1 
ATOM   6432 O O   . THR C 1 284 ? 13.077  83.443  -7.874  1.00 51.63  ? 283 THR B O   1 
ATOM   6433 C CB  . THR C 1 284 ? 14.870  84.994  -5.647  1.00 55.69  ? 283 THR B CB  1 
ATOM   6434 O OG1 . THR C 1 284 ? 13.850  85.871  -6.147  1.00 55.26  ? 283 THR B OG1 1 
ATOM   6435 C CG2 . THR C 1 284 ? 16.146  85.782  -5.394  1.00 59.54  ? 283 THR B CG2 1 
ATOM   6436 N N   . LYS C 1 285 ? 13.449  82.211  -6.025  1.00 47.78  ? 284 LYS B N   1 
ATOM   6437 C CA  . LYS C 1 285 ? 12.187  81.495  -6.086  1.00 43.79  ? 284 LYS B CA  1 
ATOM   6438 C C   . LYS C 1 285 ? 11.330  81.855  -4.879  1.00 39.97  ? 284 LYS B C   1 
ATOM   6439 O O   . LYS C 1 285 ? 11.845  82.140  -3.794  1.00 43.19  ? 284 LYS B O   1 
ATOM   6440 C CB  . LYS C 1 285 ? 12.412  79.980  -6.145  1.00 43.87  ? 284 LYS B CB  1 
ATOM   6441 C CG  . LYS C 1 285 ? 13.139  79.405  -4.940  1.00 45.33  ? 284 LYS B CG  1 
ATOM   6442 C CD  . LYS C 1 285 ? 13.364  77.910  -5.102  1.00 38.63  ? 284 LYS B CD  1 
ATOM   6443 C CE  . LYS C 1 285 ? 14.650  77.466  -4.428  1.00 37.27  ? 284 LYS B CE  1 
ATOM   6444 N NZ  . LYS C 1 285 ? 14.655  77.793  -2.976  1.00 44.59  ? 284 LYS B NZ  1 
ATOM   6445 N N   . THR C 1 286 ? 10.013  81.855  -5.083  1.00 41.35  ? 285 THR B N   1 
ATOM   6446 C CA  . THR C 1 286 ? 9.063   82.222  -4.042  1.00 36.25  ? 285 THR B CA  1 
ATOM   6447 C C   . THR C 1 286 ? 7.990   81.144  -3.937  1.00 37.66  ? 285 THR B C   1 
ATOM   6448 O O   . THR C 1 286 ? 7.385   80.770  -4.957  1.00 33.18  ? 285 THR B O   1 
ATOM   6449 C CB  . THR C 1 286 ? 8.418   83.585  -4.334  1.00 33.99  ? 285 THR B CB  1 
ATOM   6450 O OG1 . THR C 1 286 ? 9.400   84.620  -4.200  1.00 39.01  ? 285 THR B OG1 1 
ATOM   6451 C CG2 . THR C 1 286 ? 7.277   83.853  -3.367  1.00 33.49  ? 285 THR B CG2 1 
ATOM   6452 N N   . PRO C 1 287 ? 7.725   80.621  -2.740  1.00 40.53  ? 286 PRO B N   1 
ATOM   6453 C CA  . PRO C 1 287 ? 6.669   79.611  -2.594  1.00 36.83  ? 286 PRO B CA  1 
ATOM   6454 C C   . PRO C 1 287 ? 5.306   80.182  -2.953  1.00 32.66  ? 286 PRO B C   1 
ATOM   6455 O O   . PRO C 1 287 ? 4.979   81.320  -2.609  1.00 35.84  ? 286 PRO B O   1 
ATOM   6456 C CB  . PRO C 1 287 ? 6.746   79.230  -1.110  1.00 37.52  ? 286 PRO B CB  1 
ATOM   6457 C CG  . PRO C 1 287 ? 8.123   79.638  -0.680  1.00 35.00  ? 286 PRO B CG  1 
ATOM   6458 C CD  . PRO C 1 287 ? 8.428   80.871  -1.473  1.00 32.02  ? 286 PRO B CD  1 
ATOM   6459 N N   . VAL C 1 288 ? 4.504   79.373  -3.651  1.00 28.31  ? 287 VAL B N   1 
ATOM   6460 C CA  . VAL C 1 288 ? 3.199   79.839  -4.102  1.00 26.72  ? 287 VAL B CA  1 
ATOM   6461 C C   . VAL C 1 288 ? 2.250   80.082  -2.938  1.00 39.09  ? 287 VAL B C   1 
ATOM   6462 O O   . VAL C 1 288 ? 1.276   80.829  -3.088  1.00 40.54  ? 287 VAL B O   1 
ATOM   6463 C CB  . VAL C 1 288 ? 2.581   78.849  -5.106  1.00 25.71  ? 287 VAL B CB  1 
ATOM   6464 C CG1 . VAL C 1 288 ? 3.478   78.709  -6.330  1.00 26.03  ? 287 VAL B CG1 1 
ATOM   6465 C CG2 . VAL C 1 288 ? 2.338   77.500  -4.448  1.00 28.91  ? 287 VAL B CG2 1 
ATOM   6466 N N   . ASP C 1 289 ? 2.532   79.455  -1.791  1.00 35.90  ? 288 ASP B N   1 
ATOM   6467 C CA  . ASP C 1 289 ? 1.735   79.702  -0.560  1.00 38.55  ? 288 ASP B CA  1 
ATOM   6468 C C   . ASP C 1 289 ? 2.277   80.972  0.097   1.00 34.91  ? 288 ASP B C   1 
ATOM   6469 O O   . ASP C 1 289 ? 1.807   81.316  1.177   1.00 44.42  ? 288 ASP B O   1 
ATOM   6470 C CB  . ASP C 1 289 ? 1.740   78.492  0.380   1.00 33.25  ? 288 ASP B CB  1 
ATOM   6471 C CG  . ASP C 1 289 ? 3.108   77.958  0.760   1.00 42.01  ? 288 ASP B CG  1 
ATOM   6472 O OD1 . ASP C 1 289 ? 4.107   78.572  0.375   1.00 40.35  ? 288 ASP B OD1 1 
ATOM   6473 O OD2 . ASP C 1 289 ? 3.153   76.924  1.442   1.00 36.60  ? 288 ASP B OD2 1 
ATOM   6474 N N   . GLN C 1 290 ? 3.247   81.611  -0.545  1.00 39.97  ? 289 GLN B N   1 
ATOM   6475 C CA  . GLN C 1 290 ? 3.864   82.860  -0.027  1.00 38.24  ? 289 GLN B CA  1 
ATOM   6476 C C   . GLN C 1 290 ? 4.424   82.606  1.373   1.00 50.87  ? 289 GLN B C   1 
ATOM   6477 O O   . GLN C 1 290 ? 5.607   82.229  1.462   1.00 50.30  ? 289 GLN B O   1 
ATOM   6478 C CB  . GLN C 1 290 ? 2.864   84.017  -0.105  1.00 30.00  ? 289 GLN B CB  1 
ATOM   6479 C CG  . GLN C 1 290 ? 1.979   83.982  -1.342  1.00 30.00  ? 289 GLN B CG  1 
ATOM   6480 C CD  . GLN C 1 290 ? 2.747   84.353  -2.584  1.00 30.00  ? 289 GLN B CD  1 
ATOM   6481 O OE1 . GLN C 1 290 ? 3.883   84.812  -2.508  1.00 30.00  ? 289 GLN B OE1 1 
ATOM   6482 N NE2 . GLN C 1 290 ? 2.134   84.159  -3.741  1.00 30.00  ? 289 GLN B NE2 1 
HETATM 6483 N N1A . CAA D 2 .   ? 28.707  72.446  -15.669 1.00 62.89  ? 401 CAA B N1A 1 
HETATM 6484 C C2A . CAA D 2 .   ? 27.940  72.877  -14.677 1.00 62.11  ? 401 CAA B C2A 1 
HETATM 6485 N N3A . CAA D 2 .   ? 28.453  73.427  -13.588 1.00 50.57  ? 401 CAA B N3A 1 
HETATM 6486 C C4A . CAA D 2 .   ? 29.782  73.569  -13.454 1.00 62.91  ? 401 CAA B C4A 1 
HETATM 6487 C C5A . CAA D 2 .   ? 30.615  73.135  -14.460 1.00 58.97  ? 401 CAA B C5A 1 
HETATM 6488 C C6A . CAA D 2 .   ? 30.024  72.557  -15.595 1.00 61.35  ? 401 CAA B C6A 1 
HETATM 6489 N N6A . CAA D 2 .   ? 30.847  72.077  -16.686 1.00 63.40  ? 401 CAA B N6A 1 
HETATM 6490 N N7A . CAA D 2 .   ? 31.875  73.394  -14.073 1.00 62.51  ? 401 CAA B N7A 1 
HETATM 6491 C C8A . CAA D 2 .   ? 31.828  73.964  -12.874 1.00 73.99  ? 401 CAA B C8A 1 
HETATM 6492 N N9A . CAA D 2 .   ? 30.567  74.098  -12.496 1.00 69.79  ? 401 CAA B N9A 1 
HETATM 6493 C C1B . CAA D 2 .   ? 30.076  74.635  -11.211 1.00 76.51  ? 401 CAA B C1B 1 
HETATM 6494 C C2B . CAA D 2 .   ? 30.381  75.795  -10.788 1.00 85.06  ? 401 CAA B C2B 1 
HETATM 6495 O O2B . CAA D 2 .   ? 31.575  75.689  -9.959  1.00 94.50  ? 401 CAA B O2B 1 
HETATM 6496 C C3B . CAA D 2 .   ? 29.085  76.178  -9.760  1.00 84.48  ? 401 CAA B C3B 1 
HETATM 6497 O O3B . CAA D 2 .   ? 29.490  76.539  -8.445  1.00 94.99  ? 401 CAA B O3B 1 
HETATM 6498 P P3B . CAA D 2 .   ? 29.792  78.101  -8.024  1.00 98.08  ? 401 CAA B P3B 1 
HETATM 6499 O O7A . CAA D 2 .   ? 31.170  78.469  -8.510  1.00 84.50  ? 401 CAA B O7A 1 
HETATM 6500 O O8A . CAA D 2 .   ? 29.753  78.218  -6.520  1.00 89.76  ? 401 CAA B O8A 1 
HETATM 6501 O O9A . CAA D 2 .   ? 28.761  79.035  -8.619  1.00 78.79  ? 401 CAA B O9A 1 
HETATM 6502 C C4B . CAA D 2 .   ? 28.631  74.969  -9.688  1.00 88.75  ? 401 CAA B C4B 1 
HETATM 6503 O O4B . CAA D 2 .   ? 28.474  74.633  -11.159 1.00 82.64  ? 401 CAA B O4B 1 
HETATM 6504 C C5B . CAA D 2 .   ? 27.382  74.655  -8.844  1.00 86.60  ? 401 CAA B C5B 1 
HETATM 6505 O O5B . CAA D 2 .   ? 27.588  73.280  -8.601  1.00 89.40  ? 401 CAA B O5B 1 
HETATM 6506 P P1A . CAA D 2 .   ? 26.743  72.189  -9.513  1.00 84.88  ? 401 CAA B P1A 1 
HETATM 6507 O O1A . CAA D 2 .   ? 26.913  70.797  -8.954  1.00 73.93  ? 401 CAA B O1A 1 
HETATM 6508 O O2A . CAA D 2 .   ? 27.106  72.210  -10.979 1.00 68.84  ? 401 CAA B O2A 1 
HETATM 6509 O O3A . CAA D 2 .   ? 25.208  72.718  -9.309  1.00 90.78  ? 401 CAA B O3A 1 
HETATM 6510 P P2A . CAA D 2 .   ? 24.695  72.962  -7.768  1.00 78.43  ? 401 CAA B P2A 1 
HETATM 6511 O O4A . CAA D 2 .   ? 25.604  72.180  -6.841  1.00 37.27  ? 401 CAA B O4A 1 
HETATM 6512 O O5A . CAA D 2 .   ? 24.710  74.427  -7.396  1.00 43.25  ? 401 CAA B O5A 1 
HETATM 6513 O O6A . CAA D 2 .   ? 23.157  72.397  -7.732  1.00 70.93  ? 401 CAA B O6A 1 
HETATM 6514 C CBP . CAA D 2 .   ? 22.595  70.099  -7.453  1.00 50.48  ? 401 CAA B CBP 1 
HETATM 6515 C CCP . CAA D 2 .   ? 22.923  71.422  -6.780  1.00 56.16  ? 401 CAA B CCP 1 
HETATM 6516 C CDP . CAA D 2 .   ? 23.871  69.374  -7.882  1.00 40.40  ? 401 CAA B CDP 1 
HETATM 6517 C CEP . CAA D 2 .   ? 21.664  70.294  -8.651  1.00 39.35  ? 401 CAA B CEP 1 
HETATM 6518 C CAP . CAA D 2 .   ? 21.887  69.414  -6.293  1.00 42.63  ? 401 CAA B CAP 1 
HETATM 6519 O OAP . CAA D 2 .   ? 20.852  70.267  -5.898  1.00 46.83  ? 401 CAA B OAP 1 
HETATM 6520 C C9P . CAA D 2 .   ? 21.287  68.063  -6.632  1.00 35.32  ? 401 CAA B C9P 1 
HETATM 6521 O O9P . CAA D 2 .   ? 21.977  67.124  -6.829  1.00 33.91  ? 401 CAA B O9P 1 
HETATM 6522 N N8P . CAA D 2 .   ? 19.838  67.975  -6.669  1.00 34.55  ? 401 CAA B N8P 1 
HETATM 6523 C C7P . CAA D 2 .   ? 19.209  66.711  -6.965  1.00 35.33  ? 401 CAA B C7P 1 
HETATM 6524 C C6P . CAA D 2 .   ? 19.336  66.428  -8.452  1.00 26.57  ? 401 CAA B C6P 1 
HETATM 6525 C C5P . CAA D 2 .   ? 18.659  65.100  -8.707  1.00 30.05  ? 401 CAA B C5P 1 
HETATM 6526 O O5P . CAA D 2 .   ? 18.256  64.469  -7.787  1.00 30.77  ? 401 CAA B O5P 1 
HETATM 6527 N N4P . CAA D 2 .   ? 18.515  64.624  -10.059 1.00 34.11  ? 401 CAA B N4P 1 
HETATM 6528 C C3P . CAA D 2 .   ? 17.865  63.353  -10.258 1.00 33.18  ? 401 CAA B C3P 1 
HETATM 6529 C C2P . CAA D 2 .   ? 16.368  63.541  -10.084 1.00 29.56  ? 401 CAA B C2P 1 
HETATM 6530 S S1P . CAA D 2 .   ? 15.594  62.008  -10.636 1.00 36.61  ? 401 CAA B S1P 1 
HETATM 6531 C C1  . CAA D 2 .   ? 15.905  61.860  -12.408 1.00 40.44  ? 401 CAA B C1  1 
HETATM 6532 O O1  . CAA D 2 .   ? 16.379  62.769  -12.997 1.00 36.10  ? 401 CAA B O1  1 
HETATM 6533 C C2  . CAA D 2 .   ? 15.551  60.559  -13.116 1.00 40.42  ? 401 CAA B C2  1 
HETATM 6534 C C3  . CAA D 2 .   ? 14.148  60.577  -13.715 1.00 44.16  ? 401 CAA B C3  1 
HETATM 6535 O O3  . CAA D 2 .   ? 13.903  59.879  -14.640 1.00 45.46  ? 401 CAA B O3  1 
HETATM 6536 C C4  . CAA D 2 .   ? 13.068  61.490  -13.141 1.00 38.24  ? 401 CAA B C4  1 
HETATM 6537 P PA  . NAD E 3 .   ? 10.364  67.504  -21.360 1.00 71.65  ? 402 NAD B PA  1 
HETATM 6538 O O1A . NAD E 3 .   ? 9.020   67.881  -20.782 1.00 66.93  ? 402 NAD B O1A 1 
HETATM 6539 O O2A . NAD E 3 .   ? 11.377  68.595  -21.068 1.00 59.15  ? 402 NAD B O2A 1 
HETATM 6540 O O5B . NAD E 3 .   ? 10.218  67.296  -23.019 1.00 67.62  ? 402 NAD B O5B 1 
HETATM 6541 C C5B . NAD E 3 .   ? 10.730  66.104  -23.592 1.00 51.50  ? 402 NAD B C5B 1 
HETATM 6542 C C4B . NAD E 3 .   ? 11.378  66.494  -24.939 1.00 61.66  ? 402 NAD B C4B 1 
HETATM 6543 O O4B . NAD E 3 .   ? 11.302  65.494  -25.783 1.00 60.80  ? 402 NAD B O4B 1 
HETATM 6544 C C3B . NAD E 3 .   ? 10.534  67.659  -25.566 1.00 64.38  ? 402 NAD B C3B 1 
HETATM 6545 O O3B . NAD E 3 .   ? 11.332  68.467  -26.276 1.00 62.37  ? 402 NAD B O3B 1 
HETATM 6546 C C2B . NAD E 3 .   ? 9.553   66.906  -26.504 1.00 63.24  ? 402 NAD B C2B 1 
HETATM 6547 O O2B . NAD E 3 .   ? 9.023   67.842  -27.554 1.00 62.33  ? 402 NAD B O2B 1 
HETATM 6548 C C1B . NAD E 3 .   ? 10.359  66.014  -27.034 1.00 65.61  ? 402 NAD B C1B 1 
HETATM 6549 N N9A . NAD E 3 .   ? 9.653   64.918  -27.655 1.00 69.72  ? 402 NAD B N9A 1 
HETATM 6550 C C8A . NAD E 3 .   ? 8.472   64.428  -27.292 1.00 70.55  ? 402 NAD B C8A 1 
HETATM 6551 N N7A . NAD E 3 .   ? 8.146   63.430  -28.091 1.00 68.11  ? 402 NAD B N7A 1 
HETATM 6552 C C5A . NAD E 3 .   ? 9.128   63.268  -28.991 1.00 68.20  ? 402 NAD B C5A 1 
HETATM 6553 C C6A . NAD E 3 .   ? 9.357   62.411  -30.059 1.00 67.97  ? 402 NAD B C6A 1 
HETATM 6554 N N6A . NAD E 3 .   ? 8.372   61.383  -30.402 1.00 71.99  ? 402 NAD B N6A 1 
HETATM 6555 N N1A . NAD E 3 .   ? 10.453  62.514  -30.763 1.00 63.99  ? 402 NAD B N1A 1 
HETATM 6556 C C2A . NAD E 3 .   ? 11.343  63.448  -30.449 1.00 59.93  ? 402 NAD B C2A 1 
HETATM 6557 N N3A . NAD E 3 .   ? 11.180  64.279  -29.459 1.00 60.29  ? 402 NAD B N3A 1 
HETATM 6558 C C4A . NAD E 3 .   ? 10.092  64.224  -28.708 1.00 65.02  ? 402 NAD B C4A 1 
HETATM 6559 O O3  . NAD E 3 .   ? 10.868  66.083  -20.688 1.00 67.12  ? 402 NAD B O3  1 
HETATM 6560 P PN  . NAD E 3 .   ? 12.483  65.683  -20.490 1.00 66.58  ? 402 NAD B PN  1 
HETATM 6561 O O1N . NAD E 3 .   ? 13.025  66.408  -19.290 1.00 60.35  ? 402 NAD B O1N 1 
HETATM 6562 O O2N . NAD E 3 .   ? 13.278  66.106  -21.716 1.00 66.31  ? 402 NAD B O2N 1 
HETATM 6563 O O5D . NAD E 3 .   ? 12.612  64.014  -20.288 1.00 61.18  ? 402 NAD B O5D 1 
HETATM 6564 C C5D . NAD E 3 .   ? 12.514  63.185  -21.476 1.00 61.81  ? 402 NAD B C5D 1 
HETATM 6565 C C4D . NAD E 3 .   ? 12.717  61.660  -21.068 1.00 57.88  ? 402 NAD B C4D 1 
HETATM 6566 O O4D . NAD E 3 .   ? 13.582  61.555  -20.156 1.00 65.07  ? 402 NAD B O4D 1 
HETATM 6567 C C3D . NAD E 3 .   ? 11.373  61.084  -20.468 1.00 64.31  ? 402 NAD B C3D 1 
HETATM 6568 O O3D . NAD E 3 .   ? 11.229  59.761  -20.834 1.00 63.52  ? 402 NAD B O3D 1 
HETATM 6569 C C2D . NAD E 3 .   ? 11.580  61.186  -19.004 1.00 69.32  ? 402 NAD B C2D 1 
HETATM 6570 O O2D . NAD E 3 .   ? 10.705  60.203  -18.276 1.00 65.10  ? 402 NAD B O2D 1 
HETATM 6571 C C1D . NAD E 3 .   ? 12.852  60.861  -18.885 1.00 67.75  ? 402 NAD B C1D 1 
HETATM 6572 N N1N . NAD E 3 .   ? 13.411  61.336  -17.621 1.00 67.68  ? 402 NAD B N1N 1 
HETATM 6573 C C2N . NAD E 3 .   ? 13.274  62.834  -17.474 1.00 72.39  ? 402 NAD B C2N 1 
HETATM 6574 C C3N . NAD E 3 .   ? 13.768  63.287  -16.093 1.00 70.68  ? 402 NAD B C3N 1 
HETATM 6575 C C7N . NAD E 3 .   ? 13.700  64.824  -15.958 1.00 67.50  ? 402 NAD B C7N 1 
HETATM 6576 O O7N . NAD E 3 .   ? 13.327  65.490  -16.864 1.00 66.24  ? 402 NAD B O7N 1 
HETATM 6577 N N7N . NAD E 3 .   ? 14.103  65.492  -14.688 1.00 56.63  ? 402 NAD B N7N 1 
HETATM 6578 C C4N . NAD E 3 .   ? 15.190  62.854  -15.811 1.00 71.46  ? 402 NAD B C4N 1 
HETATM 6579 C C5N . NAD E 3 .   ? 15.733  61.609  -16.498 1.00 58.84  ? 402 NAD B C5N 1 
HETATM 6580 C C6N . NAD E 3 .   ? 14.844  60.873  -17.523 1.00 60.38  ? 402 NAD B C6N 1 
HETATM 6581 O O   . HOH F 4 .   ? -9.820  23.816  -44.003 1.00 44.88  ? 301 HOH C O   1 
HETATM 6582 O O   . HOH F 4 .   ? -21.154 32.070  -38.792 1.00 38.68  ? 302 HOH C O   1 
HETATM 6583 O O   . HOH F 4 .   ? -13.991 13.463  -27.113 1.00 37.74  ? 303 HOH C O   1 
HETATM 6584 O O   . HOH F 4 .   ? -16.903 35.788  -8.535  1.00 21.89  ? 304 HOH C O   1 
HETATM 6585 O O   . HOH F 4 .   ? -19.930 32.423  -19.311 1.00 23.85  ? 305 HOH C O   1 
HETATM 6586 O O   . HOH F 4 .   ? -22.326 34.664  -39.971 1.00 44.60  ? 306 HOH C O   1 
HETATM 6587 O O   . HOH F 4 .   ? -31.345 38.928  -22.855 1.00 32.77  ? 307 HOH C O   1 
HETATM 6588 O O   . HOH F 4 .   ? -21.750 9.310   -29.957 1.00 45.98  ? 308 HOH C O   1 
HETATM 6589 O O   . HOH F 4 .   ? -31.409 41.510  -32.969 1.00 48.43  ? 309 HOH C O   1 
HETATM 6590 O O   . HOH F 4 .   ? 3.824   23.228  -16.905 1.00 30.40  ? 310 HOH C O   1 
HETATM 6591 O O   . HOH F 4 .   ? -34.849 25.214  -26.782 1.00 38.92  ? 311 HOH C O   1 
HETATM 6592 O O   . HOH F 4 .   ? -15.555 48.359  -9.167  1.00 24.63  ? 312 HOH C O   1 
HETATM 6593 O O   . HOH F 4 .   ? -4.675  42.412  -18.713 1.00 31.25  ? 313 HOH C O   1 
HETATM 6594 O O   . HOH F 4 .   ? -2.709  40.198  -5.352  1.00 20.65  ? 314 HOH C O   1 
HETATM 6595 O O   . HOH F 4 .   ? -16.505 21.804  -18.749 1.00 28.38  ? 315 HOH C O   1 
HETATM 6596 O O   . HOH F 4 .   ? -18.747 21.643  -45.750 1.00 38.18  ? 316 HOH C O   1 
HETATM 6597 O O   . HOH F 4 .   ? -12.387 49.676  -11.007 1.00 38.93  ? 317 HOH C O   1 
HETATM 6598 O O   . HOH F 4 .   ? -22.650 27.649  -43.983 1.00 43.10  ? 318 HOH C O   1 
HETATM 6599 O O   . HOH F 4 .   ? -34.259 42.950  -23.217 1.00 42.93  ? 319 HOH C O   1 
HETATM 6600 O O   . HOH F 4 .   ? -6.980  22.288  -2.002  1.00 39.75  ? 320 HOH C O   1 
HETATM 6601 O O   . HOH F 4 .   ? -4.097  43.054  -11.690 1.00 27.24  ? 321 HOH C O   1 
HETATM 6602 O O   . HOH F 4 .   ? -20.262 37.045  -16.937 1.00 38.65  ? 322 HOH C O   1 
HETATM 6603 O O   . HOH F 4 .   ? -20.173 15.595  -22.714 1.00 32.13  ? 323 HOH C O   1 
HETATM 6604 O O   . HOH F 4 .   ? -21.571 40.894  -9.116  1.00 37.43  ? 324 HOH C O   1 
HETATM 6605 O O   . HOH F 4 .   ? -0.067  44.569  -11.303 1.00 26.89  ? 325 HOH C O   1 
HETATM 6606 O O   . HOH F 4 .   ? -18.607 42.507  -11.762 1.00 36.66  ? 326 HOH C O   1 
HETATM 6607 O O   . HOH F 4 .   ? -30.472 26.857  -40.212 1.00 38.21  ? 327 HOH C O   1 
HETATM 6608 O O   . HOH F 4 .   ? -7.688  47.202  -1.715  1.00 41.09  ? 328 HOH C O   1 
HETATM 6609 O O   . HOH F 4 .   ? 8.573   20.057  -8.591  1.00 34.39  ? 329 HOH C O   1 
HETATM 6610 O O   . HOH F 4 .   ? 0.475   27.554  -22.299 1.00 33.46  ? 330 HOH C O   1 
HETATM 6611 O O   . HOH F 4 .   ? -5.282  37.915  -4.891  1.00 24.75  ? 331 HOH C O   1 
HETATM 6612 O O   . HOH F 4 .   ? -14.454 30.608  -13.167 1.00 26.00  ? 332 HOH C O   1 
HETATM 6613 O O   . HOH F 4 .   ? -32.421 31.980  -23.731 1.00 33.46  ? 333 HOH C O   1 
HETATM 6614 O O   . HOH F 4 .   ? -1.689  24.167  -7.174  1.00 35.30  ? 334 HOH C O   1 
HETATM 6615 O O   . HOH F 4 .   ? -32.359 41.507  -30.705 1.00 44.31  ? 335 HOH C O   1 
HETATM 6616 O O   . HOH F 4 .   ? -23.104 10.651  -35.029 1.00 34.69  ? 336 HOH C O   1 
HETATM 6617 O O   . HOH F 4 .   ? 7.773   37.725  1.464   1.00 33.73  ? 337 HOH C O   1 
HETATM 6618 O O   . HOH F 4 .   ? -13.384 42.429  -2.803  1.00 38.81  ? 338 HOH C O   1 
HETATM 6619 O O   . HOH F 4 .   ? -17.970 43.018  -19.593 1.00 36.41  ? 339 HOH C O   1 
HETATM 6620 O O   . HOH F 4 .   ? -24.326 9.004   -25.235 1.00 31.82  ? 340 HOH C O   1 
HETATM 6621 O O   . HOH F 4 .   ? -29.263 41.566  -19.513 1.00 33.01  ? 341 HOH C O   1 
HETATM 6622 O O   . HOH F 4 .   ? 13.824  32.644  -5.060  1.00 34.23  ? 342 HOH C O   1 
HETATM 6623 O O   . HOH F 4 .   ? -27.263 38.013  -39.957 1.00 49.64  ? 343 HOH C O   1 
HETATM 6624 O O   . HOH F 4 .   ? -37.168 36.110  -36.540 1.00 46.96  ? 344 HOH C O   1 
HETATM 6625 O O   . HOH F 4 .   ? 3.044   38.899  -25.355 1.00 36.28  ? 345 HOH C O   1 
HETATM 6626 O O   . HOH F 4 .   ? -18.245 14.700  -20.061 1.00 36.23  ? 346 HOH C O   1 
HETATM 6627 O O   . HOH F 4 .   ? -31.350 23.845  -37.249 1.00 54.54  ? 347 HOH C O   1 
HETATM 6628 O O   . HOH F 4 .   ? 3.568   17.630  -12.256 1.00 37.39  ? 348 HOH C O   1 
HETATM 6629 O O   . HOH F 4 .   ? 2.921   40.585  -1.265  1.00 44.45  ? 349 HOH C O   1 
HETATM 6630 O O   . HOH F 4 .   ? -9.579  21.461  -25.991 1.00 48.63  ? 350 HOH C O   1 
HETATM 6631 O O   . HOH F 4 .   ? -8.308  28.934  -39.171 1.00 40.89  ? 351 HOH C O   1 
HETATM 6632 O O   . HOH F 4 .   ? 0.437   44.173  -19.086 1.00 33.84  ? 352 HOH C O   1 
HETATM 6633 O O   . HOH F 4 .   ? -17.548 46.404  -19.549 1.00 37.57  ? 353 HOH C O   1 
HETATM 6634 O O   . HOH F 4 .   ? 8.257   20.907  -10.735 1.00 38.59  ? 354 HOH C O   1 
HETATM 6635 O O   . HOH F 4 .   ? -10.386 27.924  -36.774 1.00 36.08  ? 355 HOH C O   1 
HETATM 6636 O O   . HOH F 4 .   ? -36.919 35.443  -34.302 1.00 43.28  ? 356 HOH C O   1 
HETATM 6637 O O   . HOH F 4 .   ? 10.910  37.330  1.589   1.00 41.64  ? 357 HOH C O   1 
HETATM 6638 O O   . HOH F 4 .   ? -29.714 38.403  -38.488 1.00 39.74  ? 358 HOH C O   1 
HETATM 6639 O O   . HOH F 4 .   ? -16.405 39.956  -15.638 1.00 32.78  ? 359 HOH C O   1 
HETATM 6640 O O   . HOH F 4 .   ? -31.465 21.910  -10.329 1.00 46.36  ? 360 HOH C O   1 
HETATM 6641 O O   . HOH F 4 .   ? -14.411 43.954  -24.442 1.00 29.29  ? 361 HOH C O   1 
HETATM 6642 O O   . HOH F 4 .   ? -20.620 12.033  -15.468 1.00 49.11  ? 362 HOH C O   1 
HETATM 6643 O O   . HOH F 4 .   ? -9.316  29.481  -17.360 1.00 45.27  ? 363 HOH C O   1 
HETATM 6644 O O   . HOH F 4 .   ? -18.553 39.527  -14.953 1.00 39.23  ? 364 HOH C O   1 
HETATM 6645 O O   . HOH F 4 .   ? -39.154 23.117  -31.638 1.00 45.12  ? 365 HOH C O   1 
HETATM 6646 O O   . HOH F 4 .   ? -30.178 43.291  -30.042 1.00 46.81  ? 366 HOH C O   1 
HETATM 6647 O O   . HOH F 4 .   ? -12.877 50.365  -13.567 1.00 38.20  ? 367 HOH C O   1 
HETATM 6648 O O   . HOH F 4 .   ? -2.770  45.551  -10.990 1.00 25.64  ? 368 HOH C O   1 
HETATM 6649 O O   . HOH F 4 .   ? -9.042  27.549  -15.964 1.00 44.21  ? 369 HOH C O   1 
HETATM 6650 O O   . HOH F 4 .   ? -11.979 32.256  -31.310 1.00 38.77  ? 370 HOH C O   1 
HETATM 6651 O O   . HOH F 4 .   ? -9.513  6.521   -40.684 1.00 41.00  ? 371 HOH C O   1 
HETATM 6652 O O   . HOH F 4 .   ? 10.087  41.182  -11.101 1.00 37.86  ? 372 HOH C O   1 
HETATM 6653 O O   . HOH F 4 .   ? -19.086 12.665  -20.925 1.00 43.61  ? 373 HOH C O   1 
HETATM 6654 O O   . HOH F 4 .   ? -38.815 23.231  -29.237 1.00 46.04  ? 374 HOH C O   1 
HETATM 6655 O O   . HOH F 4 .   ? -10.985 30.826  -27.788 1.00 40.58  ? 375 HOH C O   1 
HETATM 6656 O O   . HOH F 4 .   ? -3.148  20.956  5.022   1.00 40.15  ? 376 HOH C O   1 
HETATM 6657 O O   . HOH F 4 .   ? -10.277 31.476  -29.950 1.00 50.88  ? 377 HOH C O   1 
HETATM 6658 O O   . HOH F 4 .   ? 0.844   37.946  -25.056 1.00 38.13  ? 378 HOH C O   1 
HETATM 6659 O O   . HOH F 4 .   ? -9.786  30.205  -36.723 1.00 48.54  ? 379 HOH C O   1 
HETATM 6660 O O   . HOH F 4 .   ? 11.693  33.991  -11.959 1.00 35.01  ? 380 HOH C O   1 
HETATM 6661 O O   . HOH F 4 .   ? 10.135  34.206  -14.167 1.00 31.91  ? 381 HOH C O   1 
HETATM 6662 O O   . HOH F 4 .   ? -38.784 37.576  -34.625 1.00 38.36  ? 382 HOH C O   1 
HETATM 6663 O O   . HOH F 4 .   ? -0.947  39.510  -23.614 1.00 39.58  ? 383 HOH C O   1 
HETATM 6664 O O   . HOH G 4 .   ? -29.350 23.174  2.409   1.00 33.72  ? 301 HOH A O   1 
HETATM 6665 O O   . HOH G 4 .   ? 10.820  25.006  30.016  1.00 42.83  ? 302 HOH A O   1 
HETATM 6666 O O   . HOH G 4 .   ? 19.670  36.297  15.480  1.00 49.03  ? 303 HOH A O   1 
HETATM 6667 O O   . HOH G 4 .   ? 4.602   4.487   11.168  1.00 42.16  ? 304 HOH A O   1 
HETATM 6668 O O   . HOH G 4 .   ? 1.563   42.199  -0.026  1.00 43.27  ? 305 HOH A O   1 
HETATM 6669 O O   . HOH G 4 .   ? -25.617 28.769  -5.640  1.00 41.35  ? 306 HOH A O   1 
HETATM 6670 O O   . HOH G 4 .   ? -14.904 29.743  19.142  1.00 36.93  ? 307 HOH A O   1 
HETATM 6671 O O   . HOH G 4 .   ? -5.959  37.102  0.299   1.00 27.77  ? 308 HOH A O   1 
HETATM 6672 O O   . HOH G 4 .   ? 15.481  33.155  22.039  1.00 37.49  ? 309 HOH A O   1 
HETATM 6673 O O   . HOH G 4 .   ? 11.209  7.663   30.487  1.00 38.51  ? 310 HOH A O   1 
HETATM 6674 O O   . HOH G 4 .   ? -6.127  22.752  -11.526 1.00 43.59  ? 311 HOH A O   1 
HETATM 6675 O O   . HOH G 4 .   ? 5.623   33.418  2.817   1.00 25.22  ? 312 HOH A O   1 
HETATM 6676 O O   . HOH G 4 .   ? 23.795  14.663  11.909  1.00 49.37  ? 313 HOH A O   1 
HETATM 6677 O O   . HOH G 4 .   ? 6.950   39.379  8.527   1.00 33.96  ? 314 HOH A O   1 
HETATM 6678 O O   . HOH G 4 .   ? -14.907 18.494  5.693   1.00 30.57  ? 315 HOH A O   1 
HETATM 6679 O O   . HOH G 4 .   ? -4.662  23.503  -8.703  1.00 34.24  ? 316 HOH A O   1 
HETATM 6680 O O   . HOH G 4 .   ? 20.412  12.781  25.503  1.00 41.97  ? 317 HOH A O   1 
HETATM 6681 O O   . HOH G 4 .   ? -17.496 42.185  0.000   0.50 31.70  ? 318 HOH A O   1 
HETATM 6682 O O   . HOH G 4 .   ? -18.246 38.495  11.361  1.00 38.36  ? 319 HOH A O   1 
HETATM 6683 O O   . HOH G 4 .   ? -27.885 17.794  8.764   1.00 43.55  ? 320 HOH A O   1 
HETATM 6684 O O   . HOH G 4 .   ? 17.739  34.933  15.305  1.00 36.82  ? 321 HOH A O   1 
HETATM 6685 O O   . HOH G 4 .   ? 1.187   39.329  -2.413  1.00 40.27  ? 322 HOH A O   1 
HETATM 6686 O O   . HOH G 4 .   ? -24.492 24.520  -0.859  1.00 36.17  ? 323 HOH A O   1 
HETATM 6687 O O   . HOH G 4 .   ? 8.960   31.490  11.175  1.00 31.72  ? 324 HOH A O   1 
HETATM 6688 O O   . HOH G 4 .   ? -14.489 40.486  -2.030  1.00 40.13  ? 325 HOH A O   1 
HETATM 6689 O O   . HOH G 4 .   ? 1.774   14.806  12.355  1.00 38.99  ? 326 HOH A O   1 
HETATM 6690 O O   . HOH G 4 .   ? 5.990   20.972  26.140  1.00 41.20  ? 327 HOH A O   1 
HETATM 6691 O O   . HOH G 4 .   ? 14.599  3.338   22.863  1.00 35.63  ? 328 HOH A O   1 
HETATM 6692 O O   . HOH G 4 .   ? 2.956   18.124  19.751  1.00 35.61  ? 329 HOH A O   1 
HETATM 6693 O O   . HOH G 4 .   ? 25.662  23.233  25.603  1.00 32.55  ? 330 HOH A O   1 
HETATM 6694 O O   . HOH G 4 .   ? -18.652 38.357  14.074  1.00 29.57  ? 331 HOH A O   1 
HETATM 6695 O O   . HOH G 4 .   ? 0.780   11.003  12.975  1.00 42.56  ? 332 HOH A O   1 
HETATM 6696 O O   . HOH G 4 .   ? -3.516  34.986  14.321  1.00 28.34  ? 333 HOH A O   1 
HETATM 6697 O O   . HOH G 4 .   ? 3.211   26.363  5.322   1.00 22.04  ? 334 HOH A O   1 
HETATM 6698 O O   . HOH G 4 .   ? -12.100 20.754  12.579  1.00 36.69  ? 335 HOH A O   1 
HETATM 6699 O O   . HOH G 4 .   ? 14.758  6.195   22.817  1.00 35.65  ? 336 HOH A O   1 
HETATM 6700 O O   . HOH G 4 .   ? -8.256  21.583  13.636  1.00 42.29  ? 337 HOH A O   1 
HETATM 6701 O O   . HOH G 4 .   ? 10.438  37.951  5.613   1.00 35.89  ? 338 HOH A O   1 
HETATM 6702 O O   . HOH G 4 .   ? -25.377 38.971  -3.384  1.00 39.62  ? 339 HOH A O   1 
HETATM 6703 O O   . HOH G 4 .   ? -8.749  38.898  1.738   1.00 26.20  ? 340 HOH A O   1 
HETATM 6704 O O   . HOH G 4 .   ? -21.152 15.312  1.266   1.00 40.22  ? 341 HOH A O   1 
HETATM 6705 O O   . HOH G 4 .   ? -0.079  5.931   16.313  1.00 34.36  ? 342 HOH A O   1 
HETATM 6706 O O   . HOH G 4 .   ? 0.624   45.188  10.232  1.00 27.96  ? 343 HOH A O   1 
HETATM 6707 O O   . HOH G 4 .   ? 25.475  30.974  5.596   1.00 40.54  ? 344 HOH A O   1 
HETATM 6708 O O   . HOH G 4 .   ? -24.879 32.176  -1.440  1.00 28.52  ? 345 HOH A O   1 
HETATM 6709 O O   . HOH G 4 .   ? 9.689   9.532   7.962   1.00 32.20  ? 346 HOH A O   1 
HETATM 6710 O O   . HOH G 4 .   ? 12.109  12.160  32.381  1.00 32.33  ? 347 HOH A O   1 
HETATM 6711 O O   . HOH G 4 .   ? 21.376  24.434  15.530  1.00 34.45  ? 348 HOH A O   1 
HETATM 6712 O O   . HOH G 4 .   ? -9.719  23.467  -2.766  1.00 40.01  ? 349 HOH A O   1 
HETATM 6713 O O   . HOH G 4 .   ? -7.088  39.010  8.575   1.00 23.02  ? 350 HOH A O   1 
HETATM 6714 O O   . HOH G 4 .   ? -10.445 27.132  19.130  1.00 34.12  ? 351 HOH A O   1 
HETATM 6715 O O   . HOH G 4 .   ? 15.703  34.284  5.960   1.00 29.04  ? 352 HOH A O   1 
HETATM 6716 O O   . HOH G 4 .   ? -18.113 17.330  -1.166  1.00 39.20  ? 353 HOH A O   1 
HETATM 6717 O O   . HOH G 4 .   ? 3.324   35.788  14.364  1.00 33.08  ? 354 HOH A O   1 
HETATM 6718 O O   . HOH G 4 .   ? 20.618  29.865  27.727  1.00 41.43  ? 355 HOH A O   1 
HETATM 6719 O O   . HOH G 4 .   ? -2.646  37.808  14.600  1.00 31.58  ? 356 HOH A O   1 
HETATM 6720 O O   . HOH G 4 .   ? -20.684 23.852  16.509  1.00 42.91  ? 357 HOH A O   1 
HETATM 6721 O O   . HOH G 4 .   ? 5.658   16.048  6.660   1.00 35.15  ? 358 HOH A O   1 
HETATM 6722 O O   . HOH G 4 .   ? -21.761 26.494  19.771  1.00 46.85  ? 359 HOH A O   1 
HETATM 6723 O O   . HOH G 4 .   ? 1.108   18.801  24.944  1.00 46.10  ? 360 HOH A O   1 
HETATM 6724 O O   . HOH G 4 .   ? -8.498  35.812  0.479   1.00 23.46  ? 361 HOH A O   1 
HETATM 6725 O O   . HOH G 4 .   ? -25.093 24.761  -7.224  1.00 34.80  ? 362 HOH A O   1 
HETATM 6726 O O   . HOH G 4 .   ? -11.087 37.020  15.936  1.00 24.27  ? 363 HOH A O   1 
HETATM 6727 O O   . HOH G 4 .   ? -25.011 37.846  0.000   0.50 34.04  ? 364 HOH A O   1 
HETATM 6728 O O   . HOH G 4 .   ? -30.299 23.425  4.450   1.00 39.55  ? 365 HOH A O   1 
HETATM 6729 O O   . HOH G 4 .   ? -4.137  31.976  -2.805  1.00 31.60  ? 366 HOH A O   1 
HETATM 6730 O O   . HOH G 4 .   ? 4.462   32.573  9.514   1.00 36.36  ? 367 HOH A O   1 
HETATM 6731 O O   . HOH G 4 .   ? 17.942  33.678  12.737  1.00 35.78  ? 368 HOH A O   1 
HETATM 6732 O O   . HOH G 4 .   ? -13.801 17.110  -14.009 1.00 32.45  ? 369 HOH A O   1 
HETATM 6733 O O   . HOH G 4 .   ? -20.108 19.605  -1.646  1.00 36.24  ? 370 HOH A O   1 
HETATM 6734 O O   . HOH G 4 .   ? 4.329   44.931  8.095   1.00 25.15  ? 371 HOH A O   1 
HETATM 6735 O O   . HOH G 4 .   ? -0.675  8.825   11.302  1.00 40.19  ? 372 HOH A O   1 
HETATM 6736 O O   . HOH G 4 .   ? 23.950  24.131  16.726  1.00 34.25  ? 373 HOH A O   1 
HETATM 6737 O O   . HOH G 4 .   ? -2.824  36.807  -5.214  1.00 21.13  ? 374 HOH A O   1 
HETATM 6738 O O   . HOH G 4 .   ? -3.060  3.790   6.360   1.00 46.86  ? 375 HOH A O   1 
HETATM 6739 O O   . HOH G 4 .   ? 19.979  31.104  13.335  1.00 31.05  ? 376 HOH A O   1 
HETATM 6740 O O   . HOH G 4 .   ? 3.488   22.432  16.125  1.00 39.73  ? 377 HOH A O   1 
HETATM 6741 O O   . HOH G 4 .   ? 17.706  9.320   31.070  1.00 36.47  ? 378 HOH A O   1 
HETATM 6742 O O   . HOH G 4 .   ? 21.310  26.239  1.161   1.00 48.73  ? 379 HOH A O   1 
HETATM 6743 O O   . HOH G 4 .   ? -6.329  45.050  -0.443  1.00 39.68  ? 380 HOH A O   1 
HETATM 6744 O O   . HOH G 4 .   ? -23.787 1.536   8.246   1.00 33.87  ? 381 HOH A O   1 
HETATM 6745 O O   . HOH G 4 .   ? -2.196  23.280  5.891   1.00 45.21  ? 382 HOH A O   1 
HETATM 6746 O O   . HOH G 4 .   ? 3.549   22.160  25.873  1.00 41.35  ? 383 HOH A O   1 
HETATM 6747 O O   . HOH G 4 .   ? 17.795  34.053  4.452   1.00 42.16  ? 384 HOH A O   1 
HETATM 6748 O O   . HOH G 4 .   ? -0.284  19.639  18.384  1.00 46.03  ? 385 HOH A O   1 
HETATM 6749 O O   . HOH G 4 .   ? -26.237 31.847  -3.719  1.00 38.54  ? 386 HOH A O   1 
HETATM 6750 O O   . HOH G 4 .   ? -1.197  32.379  15.155  1.00 42.60  ? 387 HOH A O   1 
HETATM 6751 O O   . HOH G 4 .   ? 17.570  9.459   24.545  1.00 39.47  ? 388 HOH A O   1 
HETATM 6752 O O   . HOH G 4 .   ? 15.881  8.110   23.384  1.00 32.40  ? 389 HOH A O   1 
HETATM 6753 O O   . HOH G 4 .   ? -8.534  41.382  8.880   1.00 18.75  ? 390 HOH A O   1 
HETATM 6754 O O   . HOH G 4 .   ? 7.098   33.908  9.871   1.00 40.53  ? 391 HOH A O   1 
HETATM 6755 O O   . HOH G 4 .   ? -0.169  37.884  14.612  1.00 39.48  ? 392 HOH A O   1 
HETATM 6756 O O   . HOH G 4 .   ? 0.963   20.225  22.246  1.00 41.53  ? 393 HOH A O   1 
HETATM 6757 O O   . HOH G 4 .   ? -0.687  4.078   7.680   1.00 45.61  ? 394 HOH A O   1 
HETATM 6758 O O   . HOH G 4 .   ? -6.926  23.635  -14.038 1.00 46.57  ? 395 HOH A O   1 
HETATM 6759 O O   . HOH G 4 .   ? -29.177 23.033  7.430   1.00 41.03  ? 396 HOH A O   1 
HETATM 6760 O O   . HOH G 4 .   ? -7.527  21.810  -15.392 1.00 47.42  ? 397 HOH A O   1 
HETATM 6761 O O   . HOH G 4 .   ? -12.210 28.802  18.587  1.00 37.70  ? 398 HOH A O   1 
HETATM 6762 O O   . HOH G 4 .   ? -0.764  20.224  20.688  1.00 37.82  ? 399 HOH A O   1 
HETATM 6763 O O   . HOH G 4 .   ? -30.991 24.396  6.382   1.00 48.10  ? 400 HOH A O   1 
HETATM 6764 O O   . HOH G 4 .   ? -2.665  23.220  8.853   1.00 45.48  ? 401 HOH A O   1 
HETATM 6765 O O   . HOH G 4 .   ? -2.888  33.881  16.406  1.00 38.62  ? 402 HOH A O   1 
HETATM 6766 O O   . HOH H 4 .   ? 12.759  52.203  -38.303 1.00 63.83  ? 501 HOH B O   1 
HETATM 6767 O O   . HOH H 4 .   ? 13.293  74.172  -8.096  1.00 25.22  ? 502 HOH B O   1 
HETATM 6768 O O   . HOH H 4 .   ? 35.188  69.303  -30.604 1.00 40.56  ? 503 HOH B O   1 
HETATM 6769 O O   . HOH H 4 .   ? 0.363   74.405  4.186   1.00 43.13  ? 504 HOH B O   1 
HETATM 6770 O O   . HOH H 4 .   ? 18.087  51.638  -37.279 1.00 64.30  ? 505 HOH B O   1 
HETATM 6771 O O   . HOH H 4 .   ? 16.139  67.488  -35.012 1.00 61.79  ? 506 HOH B O   1 
HETATM 6772 O O   . HOH H 4 .   ? 3.053   46.770  -27.286 1.00 55.23  ? 507 HOH B O   1 
HETATM 6773 O O   . HOH H 4 .   ? 15.963  44.104  -26.162 1.00 40.00  ? 508 HOH B O   1 
HETATM 6774 O O   . HOH H 4 .   ? 5.711   49.980  -17.899 1.00 34.01  ? 509 HOH B O   1 
HETATM 6775 O O   . HOH H 4 .   ? 32.022  79.071  -5.909  1.00 56.88  ? 510 HOH B O   1 
HETATM 6776 O O   . HOH H 4 .   ? 28.005  42.503  -15.019 1.00 71.59  ? 511 HOH B O   1 
HETATM 6777 O O   . HOH H 4 .   ? 3.301   46.777  -3.583  1.00 35.42  ? 512 HOH B O   1 
HETATM 6778 O O   . HOH H 4 .   ? 7.052   50.047  -15.992 1.00 42.70  ? 513 HOH B O   1 
HETATM 6779 O O   . HOH H 4 .   ? -2.844  47.934  -12.546 1.00 21.55  ? 514 HOH B O   1 
HETATM 6780 O O   . HOH H 4 .   ? 11.589  49.024  -9.313  1.00 29.69  ? 515 HOH B O   1 
HETATM 6781 O O   . HOH H 4 .   ? 8.116   83.119  -13.123 1.00 38.21  ? 516 HOH B O   1 
HETATM 6782 O O   . HOH H 4 .   ? -1.554  64.659  7.917   1.00 38.75  ? 517 HOH B O   1 
HETATM 6783 O O   . HOH H 4 .   ? 5.192   50.282  2.498   1.00 30.12  ? 518 HOH B O   1 
HETATM 6784 O O   . HOH H 4 .   ? -7.149  67.874  -10.462 1.00 32.98  ? 519 HOH B O   1 
HETATM 6785 O O   . HOH H 4 .   ? 31.017  65.864  -14.380 1.00 47.04  ? 520 HOH B O   1 
HETATM 6786 O O   . HOH H 4 .   ? 21.403  70.759  2.122   1.00 39.81  ? 521 HOH B O   1 
HETATM 6787 O O   . HOH H 4 .   ? 30.138  63.088  -19.095 1.00 29.46  ? 522 HOH B O   1 
HETATM 6788 O O   . HOH H 4 .   ? 14.675  66.076  -1.588  1.00 35.06  ? 523 HOH B O   1 
HETATM 6789 O O   . HOH H 4 .   ? -0.094  70.541  -18.437 1.00 35.74  ? 524 HOH B O   1 
HETATM 6790 O O   . HOH H 4 .   ? 23.624  60.952  -14.926 1.00 30.72  ? 525 HOH B O   1 
HETATM 6791 O O   . HOH H 4 .   ? 4.205   56.282  -2.269  1.00 27.03  ? 526 HOH B O   1 
HETATM 6792 O O   . HOH H 4 .   ? 6.065   78.301  2.391   1.00 30.13  ? 527 HOH B O   1 
HETATM 6793 O O   . HOH H 4 .   ? 14.827  65.394  -23.990 1.00 41.61  ? 528 HOH B O   1 
HETATM 6794 O O   . HOH H 4 .   ? -1.091  57.380  -9.257  1.00 22.62  ? 529 HOH B O   1 
HETATM 6795 O O   . HOH H 4 .   ? 15.923  53.784  -18.882 1.00 31.37  ? 530 HOH B O   1 
HETATM 6796 O O   . HOH H 4 .   ? 15.069  55.357  -11.626 1.00 20.89  ? 531 HOH B O   1 
HETATM 6797 O O   . HOH H 4 .   ? 18.585  60.452  2.406   1.00 26.81  ? 532 HOH B O   1 
HETATM 6798 O O   . HOH H 4 .   ? 30.079  63.525  -15.581 1.00 41.95  ? 533 HOH B O   1 
HETATM 6799 O O   . HOH H 4 .   ? -0.007  59.865  -16.495 1.00 31.43  ? 534 HOH B O   1 
HETATM 6800 O O   . HOH H 4 .   ? 6.022   75.374  8.801   1.00 37.01  ? 535 HOH B O   1 
HETATM 6801 O O   . HOH H 4 .   ? 0.339   55.176  -16.429 1.00 31.48  ? 536 HOH B O   1 
HETATM 6802 O O   . HOH H 4 .   ? 8.027   52.261  1.763   1.00 23.30  ? 537 HOH B O   1 
HETATM 6803 O O   . HOH H 4 .   ? -6.790  66.913  -8.062  1.00 31.18  ? 538 HOH B O   1 
HETATM 6804 O O   . HOH H 4 .   ? 11.083  71.819  -14.793 1.00 32.50  ? 539 HOH B O   1 
HETATM 6805 O O   . HOH H 4 .   ? -4.849  71.375  4.803   1.00 27.06  ? 540 HOH B O   1 
HETATM 6806 O O   . HOH H 4 .   ? 0.496   86.072  -2.266  1.00 45.52  ? 541 HOH B O   1 
HETATM 6807 O O   . HOH H 4 .   ? 18.541  74.779  -2.551  1.00 40.96  ? 542 HOH B O   1 
HETATM 6808 O O   . HOH H 4 .   ? 19.718  66.758  -18.005 1.00 36.33  ? 543 HOH B O   1 
HETATM 6809 O O   . HOH H 4 .   ? 22.344  74.650  -20.748 1.00 47.78  ? 544 HOH B O   1 
HETATM 6810 O O   . HOH H 4 .   ? 26.977  81.422  -8.091  1.00 53.31  ? 545 HOH B O   1 
HETATM 6811 O O   . HOH H 4 .   ? -0.277  77.911  3.436   1.00 39.65  ? 546 HOH B O   1 
HETATM 6812 O O   . HOH H 4 .   ? -2.981  66.805  8.962   1.00 34.26  ? 547 HOH B O   1 
HETATM 6813 O O   . HOH H 4 .   ? 1.780   57.560  -16.693 1.00 32.06  ? 548 HOH B O   1 
HETATM 6814 O O   . HOH H 4 .   ? 19.958  61.299  4.531   1.00 28.42  ? 549 HOH B O   1 
HETATM 6815 O O   . HOH H 4 .   ? 30.347  44.814  -13.854 1.00 47.47  ? 550 HOH B O   1 
HETATM 6816 O O   . HOH H 4 .   ? 21.773  73.889  -18.310 1.00 36.92  ? 551 HOH B O   1 
HETATM 6817 O O   . HOH H 4 .   ? 20.549  69.015  -17.888 1.00 36.25  ? 552 HOH B O   1 
HETATM 6818 O O   . HOH H 4 .   ? -3.479  57.419  -8.638  1.00 24.93  ? 553 HOH B O   1 
HETATM 6819 O O   . HOH H 4 .   ? -2.029  62.315  9.137   1.00 39.83  ? 554 HOH B O   1 
HETATM 6820 O O   . HOH H 4 .   ? 5.868   55.674  0.000   0.50 24.50  ? 555 HOH B O   1 
HETATM 6821 O O   . HOH H 4 .   ? 0.397   88.440  -1.975  1.00 47.17  ? 556 HOH B O   1 
# 
