data_5IPZ
# 
_entry.id   5IPZ 
# 
_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   5IPZ         pdb_00005ipz 10.2210/pdb5ipz/pdb 
WWPDB D_1000219156 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2017-03-29 
2 'Structure model' 1 1 2017-12-06 
3 'Structure model' 1 2 2018-07-11 
4 'Structure model' 1 3 2024-01-10 
5 'Structure model' 1 4 2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 3 'Structure model' 'Data collection'        
4 3 'Structure model' 'Database references'    
5 4 'Structure model' 'Data collection'        
6 4 'Structure model' 'Database references'    
7 4 'Structure model' 'Derived calculations'   
8 4 'Structure model' 'Refinement description' 
9 5 'Structure model' 'Structure summary'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  2 'Structure model' citation                      
2  2 'Structure model' citation_author               
3  2 'Structure model' diffrn_source                 
4  3 'Structure model' citation                      
5  4 'Structure model' chem_comp_atom                
6  4 'Structure model' chem_comp_bond                
7  4 'Structure model' database_2                    
8  4 'Structure model' pdbx_initial_refinement_model 
9  4 'Structure model' struct_conn                   
10 5 'Structure model' pdbx_entry_details            
11 5 'Structure model' pdbx_modification_feature     
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                    
2  2 'Structure model' '_citation.journal_abbrev'             
3  2 'Structure model' '_citation.journal_id_ASTM'            
4  2 'Structure model' '_citation.journal_id_CSD'             
5  2 'Structure model' '_citation.journal_id_ISSN'            
6  2 'Structure model' '_citation.pdbx_database_id_DOI'       
7  2 'Structure model' '_citation.pdbx_database_id_PubMed'    
8  2 'Structure model' '_citation.title'                      
9  2 'Structure model' '_citation.year'                       
10 2 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
11 3 'Structure model' '_citation.journal_volume'             
12 3 'Structure model' '_citation.page_first'                 
13 3 'Structure model' '_citation.page_last'                  
14 3 'Structure model' '_citation.year'                       
15 4 'Structure model' '_database_2.pdbx_DOI'                 
16 4 'Structure model' '_database_2.pdbx_database_accession'  
17 4 'Structure model' '_struct_conn.pdbx_dist_value'         
18 4 'Structure model' '_struct_conn.ptnr1_auth_asym_id'      
19 4 'Structure model' '_struct_conn.ptnr1_auth_comp_id'      
20 4 'Structure model' '_struct_conn.ptnr1_auth_seq_id'       
21 4 'Structure model' '_struct_conn.ptnr1_label_asym_id'     
22 4 'Structure model' '_struct_conn.ptnr1_label_atom_id'     
23 4 'Structure model' '_struct_conn.ptnr1_label_comp_id'     
24 4 'Structure model' '_struct_conn.ptnr1_label_seq_id'      
25 4 'Structure model' '_struct_conn.ptnr2_auth_asym_id'      
26 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id'      
27 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id'       
28 4 'Structure model' '_struct_conn.ptnr2_label_asym_id'     
29 4 'Structure model' '_struct_conn.ptnr2_label_atom_id'     
30 4 'Structure model' '_struct_conn.ptnr2_label_comp_id'     
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5IPZ 
_pdbx_database_status.recvd_initial_deposition_date   2016-03-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   GW 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Eur. Biophys. J.' 
_citation.journal_id_ASTM           EBJOE8 
_citation.journal_id_CSD            0997 
_citation.journal_id_ISSN           1432-1017 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            47 
_citation.language                  ? 
_citation.page_first                271 
_citation.page_last                 290 
_citation.title                     
'Intrinsic thermodynamics of high affinity inhibitor binding to recombinant human carbonic anhydrase IV.' 
_citation.year                      2018 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1007/s00249-017-1256-0 
_citation.pdbx_database_id_PubMed   28975383 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Mickeviciute, A.'  1  ? 
primary 'Timm, D.D.'        2  ? 
primary 'Gedgaudas, M.'     3  ? 
primary 'Linkuviene, V.'    4  ? 
primary 'Chen, Z.'          5  ? 
primary 'Waheed, A.'        6  ? 
primary 'Michailoviene, V.' 7  ? 
primary 'Zubriene, A.'      8  ? 
primary 'Smirnov, A.'       9  ? 
primary 'Capkauskaite, E.'  10 ? 
primary 'Baranauskiene, L.' 11 ? 
primary 'Jachno, J.'        12 ? 
primary 'Revuckiene, J.'    13 ? 
primary 'Manakova, E.'      14 ? 
primary 'Grazulis, S.'      15 ? 
primary 'Matuliene, J.'     16 ? 
primary 'Di Cera, E.'       17 ? 
primary 'Sly, W.S.'         18 ? 
primary 'Matulis, D.'       19 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 4'                                       30495.668 4   4.2.1.1 ? 'UNP residues 19-284' ? 
2 non-polymer syn 'ZINC ION'                                                   65.409    4   ?       ? 
'5-(2-amino-1,3-thiazol-4-yl)-2-chlorobenzenesulfonamide' ? 
3 non-polymer syn '5-(2-amino-1,3-thiazol-4-yl)-2-chlorobenzene-1-sulfonamide' 289.762   3   ?       ? Zn ? 
4 water       nat water                                                        18.015    120 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase IV,Carbonic anhydrase IV,CA-IV' 
# 
_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       
;MAESHWCYEVQAESSNYPCLVPVKWGGNCQKDRQSPINIVTTKAKVDKKLGRFFFSGYDKKQTWTVQNNGHSVMMLLENK
ASISGGGLPAPYQAKQLHLHWSDLPYKGSEHSLDGEHFAMEMHIVHEKEKGTSRNVKEAQDPEDEIAVLAFLVEAGTQVN
EGFQPLVEALSNIPKPEMSTTMAESSLLDLLPKEEKLRHYFRYLGSLTTPTCDEKVVWTVFREPIQLHREQILAFSQKLY
YDKEQTVSMKDNVRPLQQLGQRTVIKS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAESHWCYEVQAESSNYPCLVPVKWGGNCQKDRQSPINIVTTKAKVDKKLGRFFFSGYDKKQTWTVQNNGHSVMMLLENK
ASISGGGLPAPYQAKQLHLHWSDLPYKGSEHSLDGEHFAMEMHIVHEKEKGTSRNVKEAQDPEDEIAVLAFLVEAGTQVN
EGFQPLVEALSNIPKPEMSTTMAESSLLDLLPKEEKLRHYFRYLGSLTTPTCDEKVVWTVFREPIQLHREQILAFSQKLY
YDKEQTVSMKDNVRPLQQLGQRTVIKS
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                   ZN  
3 '5-(2-amino-1,3-thiazol-4-yl)-2-chlorobenzene-1-sulfonamide' 6CC 
4 water                                                        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   GLU n 
1 4   SER n 
1 5   HIS n 
1 6   TRP n 
1 7   CYS n 
1 8   TYR n 
1 9   GLU n 
1 10  VAL n 
1 11  GLN n 
1 12  ALA n 
1 13  GLU n 
1 14  SER n 
1 15  SER n 
1 16  ASN n 
1 17  TYR n 
1 18  PRO n 
1 19  CYS n 
1 20  LEU n 
1 21  VAL n 
1 22  PRO n 
1 23  VAL n 
1 24  LYS n 
1 25  TRP n 
1 26  GLY n 
1 27  GLY n 
1 28  ASN n 
1 29  CYS n 
1 30  GLN n 
1 31  LYS n 
1 32  ASP n 
1 33  ARG n 
1 34  GLN n 
1 35  SER n 
1 36  PRO n 
1 37  ILE n 
1 38  ASN n 
1 39  ILE n 
1 40  VAL n 
1 41  THR n 
1 42  THR n 
1 43  LYS n 
1 44  ALA n 
1 45  LYS n 
1 46  VAL n 
1 47  ASP n 
1 48  LYS n 
1 49  LYS n 
1 50  LEU n 
1 51  GLY n 
1 52  ARG n 
1 53  PHE n 
1 54  PHE n 
1 55  PHE n 
1 56  SER n 
1 57  GLY n 
1 58  TYR n 
1 59  ASP n 
1 60  LYS n 
1 61  LYS n 
1 62  GLN n 
1 63  THR n 
1 64  TRP n 
1 65  THR n 
1 66  VAL n 
1 67  GLN n 
1 68  ASN n 
1 69  ASN n 
1 70  GLY n 
1 71  HIS n 
1 72  SER n 
1 73  VAL n 
1 74  MET n 
1 75  MET n 
1 76  LEU n 
1 77  LEU n 
1 78  GLU n 
1 79  ASN n 
1 80  LYS n 
1 81  ALA n 
1 82  SER n 
1 83  ILE n 
1 84  SER n 
1 85  GLY n 
1 86  GLY n 
1 87  GLY n 
1 88  LEU n 
1 89  PRO n 
1 90  ALA n 
1 91  PRO n 
1 92  TYR n 
1 93  GLN n 
1 94  ALA n 
1 95  LYS n 
1 96  GLN n 
1 97  LEU n 
1 98  HIS n 
1 99  LEU n 
1 100 HIS n 
1 101 TRP n 
1 102 SER n 
1 103 ASP n 
1 104 LEU n 
1 105 PRO n 
1 106 TYR n 
1 107 LYS n 
1 108 GLY n 
1 109 SER n 
1 110 GLU n 
1 111 HIS n 
1 112 SER n 
1 113 LEU n 
1 114 ASP n 
1 115 GLY n 
1 116 GLU n 
1 117 HIS n 
1 118 PHE n 
1 119 ALA n 
1 120 MET n 
1 121 GLU n 
1 122 MET n 
1 123 HIS n 
1 124 ILE n 
1 125 VAL n 
1 126 HIS n 
1 127 GLU n 
1 128 LYS n 
1 129 GLU n 
1 130 LYS n 
1 131 GLY n 
1 132 THR n 
1 133 SER n 
1 134 ARG n 
1 135 ASN n 
1 136 VAL n 
1 137 LYS n 
1 138 GLU n 
1 139 ALA n 
1 140 GLN n 
1 141 ASP n 
1 142 PRO n 
1 143 GLU n 
1 144 ASP n 
1 145 GLU n 
1 146 ILE n 
1 147 ALA n 
1 148 VAL n 
1 149 LEU n 
1 150 ALA n 
1 151 PHE n 
1 152 LEU n 
1 153 VAL n 
1 154 GLU n 
1 155 ALA n 
1 156 GLY n 
1 157 THR n 
1 158 GLN n 
1 159 VAL n 
1 160 ASN n 
1 161 GLU n 
1 162 GLY n 
1 163 PHE n 
1 164 GLN n 
1 165 PRO n 
1 166 LEU n 
1 167 VAL n 
1 168 GLU n 
1 169 ALA n 
1 170 LEU n 
1 171 SER n 
1 172 ASN n 
1 173 ILE n 
1 174 PRO n 
1 175 LYS n 
1 176 PRO n 
1 177 GLU n 
1 178 MET n 
1 179 SER n 
1 180 THR n 
1 181 THR n 
1 182 MET n 
1 183 ALA n 
1 184 GLU n 
1 185 SER n 
1 186 SER n 
1 187 LEU n 
1 188 LEU n 
1 189 ASP n 
1 190 LEU n 
1 191 LEU n 
1 192 PRO n 
1 193 LYS n 
1 194 GLU n 
1 195 GLU n 
1 196 LYS n 
1 197 LEU n 
1 198 ARG n 
1 199 HIS n 
1 200 TYR n 
1 201 PHE n 
1 202 ARG n 
1 203 TYR n 
1 204 LEU n 
1 205 GLY n 
1 206 SER n 
1 207 LEU n 
1 208 THR n 
1 209 THR n 
1 210 PRO n 
1 211 THR n 
1 212 CYS n 
1 213 ASP n 
1 214 GLU n 
1 215 LYS n 
1 216 VAL n 
1 217 VAL n 
1 218 TRP n 
1 219 THR n 
1 220 VAL n 
1 221 PHE n 
1 222 ARG n 
1 223 GLU n 
1 224 PRO n 
1 225 ILE n 
1 226 GLN n 
1 227 LEU n 
1 228 HIS n 
1 229 ARG n 
1 230 GLU n 
1 231 GLN n 
1 232 ILE n 
1 233 LEU n 
1 234 ALA n 
1 235 PHE n 
1 236 SER n 
1 237 GLN n 
1 238 LYS n 
1 239 LEU n 
1 240 TYR n 
1 241 TYR n 
1 242 ASP n 
1 243 LYS n 
1 244 GLU n 
1 245 GLN n 
1 246 THR n 
1 247 VAL n 
1 248 SER n 
1 249 MET n 
1 250 LYS n 
1 251 ASP n 
1 252 ASN n 
1 253 VAL n 
1 254 ARG n 
1 255 PRO n 
1 256 LEU n 
1 257 GLN n 
1 258 GLN n 
1 259 LEU n 
1 260 GLY n 
1 261 GLN n 
1 262 ARG n 
1 263 THR n 
1 264 VAL n 
1 265 ILE n 
1 266 LYS n 
1 267 SER 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                   267 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA4 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     511693 
_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              'Origami B (DE3)' 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET21a 
_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 
6CC non-polymer         . '5-(2-amino-1,3-thiazol-4-yl)-2-chlorobenzene-1-sulfonamide' ? 'C9 H8 Cl N3 O2 S2' 289.762 
ALA 'L-peptide linking' y ALANINE                                                      ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                                                     ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                   ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                              ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                                                     ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                    ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                              ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                                      ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                                    ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                                        ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                   ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                                      ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                                       ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                                                   ? 'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                                      ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                                                       ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                                                    ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                   ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                                     ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                                       ? 'C5 H11 N O2'       117.146 
ZN  non-polymer         . 'ZINC ION'                                                   ? 'Zn 2'              65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   SER 4   4   4   SER SER A . n 
A 1 5   HIS 5   5   5   HIS HIS A . n 
A 1 6   TRP 6   6   6   TRP TRP A . n 
A 1 7   CYS 7   7   7   CYS CYS A . n 
A 1 8   TYR 8   8   8   TYR TYR A . n 
A 1 9   GLU 9   9   9   GLU GLU A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  GLN 11  11  11  GLN GLN A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  PRO 18  18  18  PRO PRO A . n 
A 1 19  CYS 19  19  19  CYS CYS A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  PRO 22  22  22  PRO PRO A . n 
A 1 23  VAL 23  23  23  VAL VAL A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  TRP 25  25  25  TRP TRP A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  CYS 29  29  29  CYS CYS A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  GLN 34  34  34  GLN GLN A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  ASN 38  38  38  ASN ASN A . n 
A 1 39  ILE 39  39  39  ILE ILE A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  THR 42  42  42  THR THR A . n 
A 1 43  LYS 43  43  43  LYS LYS A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  LYS 49  49  49  LYS LYS A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ARG 52  52  52  ARG ARG A . n 
A 1 53  PHE 53  53  53  PHE PHE A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  PHE 55  55  55  PHE PHE A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  TYR 58  58  58  TYR TYR A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  TRP 64  64  64  TRP TRP A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  ASN 69  69  69  ASN ASN A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  MET 74  74  74  MET MET A . n 
A 1 75  MET 75  75  75  MET MET A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ASN 79  79  79  ASN ASN A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  SER 82  82  82  SER SER A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  TYR 92  92  92  TYR TYR A . n 
A 1 93  GLN 93  93  93  GLN GLN A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  LYS 95  95  95  LYS LYS A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  HIS 98  98  98  HIS HIS A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 TRP 101 101 101 TRP TRP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 PRO 105 105 105 PRO PRO A . n 
A 1 106 TYR 106 106 106 TYR TYR A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 SER 109 109 109 SER SER A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 ASP 114 114 114 ASP ASP A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 HIS 117 117 117 HIS HIS A . n 
A 1 118 PHE 118 118 118 PHE PHE A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 MET 120 120 120 MET MET A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 MET 122 122 122 MET MET A . n 
A 1 123 HIS 123 123 123 HIS HIS A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 HIS 126 126 126 HIS HIS A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 LYS 130 130 130 LYS LYS A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ARG 134 134 134 ARG ARG A . n 
A 1 135 ASN 135 135 135 ASN ASN A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 LYS 137 137 ?   ?   ?   A . n 
A 1 138 GLU 138 138 ?   ?   ?   A . n 
A 1 139 ALA 139 139 ?   ?   ?   A . n 
A 1 140 GLN 140 140 ?   ?   ?   A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 GLU 143 143 143 GLU GLU A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 PHE 151 151 151 PHE PHE A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 GLN 158 158 158 GLN GLN A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 ASN 160 160 160 ASN ASN A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 PHE 163 163 163 PHE PHE A . n 
A 1 164 GLN 164 164 164 GLN GLN A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 ASN 172 172 172 ASN ASN A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 LYS 175 175 175 LYS LYS A . n 
A 1 176 PRO 176 176 176 PRO PRO A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 MET 178 178 178 MET MET A . n 
A 1 179 SER 179 179 179 SER SER A . n 
A 1 180 THR 180 180 180 THR THR A . n 
A 1 181 THR 181 181 181 THR THR A . n 
A 1 182 MET 182 182 182 MET MET A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 PRO 192 192 192 PRO PRO A . n 
A 1 193 LYS 193 193 193 LYS LYS A . n 
A 1 194 GLU 194 194 194 GLU GLU A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 LYS 196 196 196 LYS LYS A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 ARG 198 198 198 ARG ARG A . n 
A 1 199 HIS 199 199 199 HIS HIS A . n 
A 1 200 TYR 200 200 200 TYR TYR A . n 
A 1 201 PHE 201 201 201 PHE PHE A . n 
A 1 202 ARG 202 202 202 ARG ARG A . n 
A 1 203 TYR 203 203 203 TYR TYR A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 GLY 205 205 205 GLY GLY A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 THR 208 208 208 THR THR A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 PRO 210 210 210 PRO PRO A . n 
A 1 211 THR 211 211 211 THR THR A . n 
A 1 212 CYS 212 212 212 CYS CYS A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 GLU 214 214 214 GLU GLU A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 THR 219 219 219 THR THR A . n 
A 1 220 VAL 220 220 220 VAL VAL A . n 
A 1 221 PHE 221 221 221 PHE PHE A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 PRO 224 224 224 PRO PRO A . n 
A 1 225 ILE 225 225 225 ILE ILE A . n 
A 1 226 GLN 226 226 226 GLN GLN A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 HIS 228 228 228 HIS HIS A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 GLU 230 230 230 GLU GLU A . n 
A 1 231 GLN 231 231 231 GLN GLN A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 PHE 235 235 235 PHE PHE A . n 
A 1 236 SER 236 236 236 SER SER A . n 
A 1 237 GLN 237 237 237 GLN GLN A . n 
A 1 238 LYS 238 238 238 LYS LYS A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 TYR 240 240 240 TYR TYR A . n 
A 1 241 TYR 241 241 241 TYR TYR A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 LYS 243 243 243 LYS LYS A . n 
A 1 244 GLU 244 244 244 GLU GLU A . n 
A 1 245 GLN 245 245 245 GLN GLN A . n 
A 1 246 THR 246 246 246 THR THR A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 SER 248 248 248 SER SER A . n 
A 1 249 MET 249 249 249 MET MET A . n 
A 1 250 LYS 250 250 250 LYS LYS A . n 
A 1 251 ASP 251 251 251 ASP ASP A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 VAL 253 253 253 VAL VAL A . n 
A 1 254 ARG 254 254 254 ARG ARG A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 GLN 257 257 257 GLN GLN A . n 
A 1 258 GLN 258 258 258 GLN GLN A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 GLY 260 260 260 GLY GLY A . n 
A 1 261 GLN 261 261 261 GLN GLN A . n 
A 1 262 ARG 262 262 262 ARG ARG A . n 
A 1 263 THR 263 263 263 THR THR A . n 
A 1 264 VAL 264 264 264 VAL VAL A . n 
A 1 265 ILE 265 265 265 ILE ILE A . n 
A 1 266 LYS 266 266 266 LYS LYS A . n 
A 1 267 SER 267 267 267 SER SER A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ALA 2   2   ?   ?   ?   B . n 
B 1 3   GLU 3   3   3   GLU GLU B . n 
B 1 4   SER 4   4   4   SER SER B . n 
B 1 5   HIS 5   5   5   HIS HIS B . n 
B 1 6   TRP 6   6   6   TRP TRP B . n 
B 1 7   CYS 7   7   7   CYS CYS B . n 
B 1 8   TYR 8   8   8   TYR TYR B . n 
B 1 9   GLU 9   9   9   GLU GLU B . n 
B 1 10  VAL 10  10  10  VAL VAL B . n 
B 1 11  GLN 11  11  11  GLN GLN B . n 
B 1 12  ALA 12  12  12  ALA ALA B . n 
B 1 13  GLU 13  13  13  GLU GLU B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  SER 15  15  15  SER SER B . n 
B 1 16  ASN 16  16  16  ASN ASN B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  PRO 18  18  18  PRO PRO B . n 
B 1 19  CYS 19  19  19  CYS CYS B . n 
B 1 20  LEU 20  20  20  LEU LEU B . n 
B 1 21  VAL 21  21  21  VAL VAL B . n 
B 1 22  PRO 22  22  22  PRO PRO B . n 
B 1 23  VAL 23  23  23  VAL VAL B . n 
B 1 24  LYS 24  24  24  LYS LYS B . n 
B 1 25  TRP 25  25  25  TRP TRP B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  CYS 29  29  29  CYS CYS B . n 
B 1 30  GLN 30  30  30  GLN GLN B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  ASP 32  32  32  ASP ASP B . n 
B 1 33  ARG 33  33  33  ARG ARG B . n 
B 1 34  GLN 34  34  34  GLN GLN B . n 
B 1 35  SER 35  35  35  SER SER B . n 
B 1 36  PRO 36  36  36  PRO PRO B . n 
B 1 37  ILE 37  37  37  ILE ILE B . n 
B 1 38  ASN 38  38  38  ASN ASN B . n 
B 1 39  ILE 39  39  39  ILE ILE B . n 
B 1 40  VAL 40  40  40  VAL VAL B . n 
B 1 41  THR 41  41  41  THR THR B . n 
B 1 42  THR 42  42  42  THR THR B . n 
B 1 43  LYS 43  43  43  LYS LYS B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  LYS 45  45  45  LYS LYS B . n 
B 1 46  VAL 46  46  46  VAL VAL B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  LYS 48  48  48  LYS LYS B . n 
B 1 49  LYS 49  49  49  LYS LYS B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ARG 52  52  52  ARG ARG B . n 
B 1 53  PHE 53  53  53  PHE PHE B . n 
B 1 54  PHE 54  54  54  PHE PHE B . n 
B 1 55  PHE 55  55  55  PHE PHE B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  GLY 57  57  57  GLY GLY B . n 
B 1 58  TYR 58  58  58  TYR TYR B . n 
B 1 59  ASP 59  59  59  ASP ASP B . n 
B 1 60  LYS 60  60  60  LYS LYS B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  THR 63  63  63  THR THR B . n 
B 1 64  TRP 64  64  64  TRP TRP B . n 
B 1 65  THR 65  65  65  THR THR B . n 
B 1 66  VAL 66  66  66  VAL VAL B . n 
B 1 67  GLN 67  67  67  GLN GLN B . n 
B 1 68  ASN 68  68  68  ASN ASN B . n 
B 1 69  ASN 69  69  69  ASN ASN B . n 
B 1 70  GLY 70  70  70  GLY GLY B . n 
B 1 71  HIS 71  71  71  HIS HIS B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  MET 74  74  74  MET MET B . n 
B 1 75  MET 75  75  75  MET MET B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ASN 79  79  79  ASN ASN B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  SER 82  82  82  SER SER B . n 
B 1 83  ILE 83  83  83  ILE ILE B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  GLY 87  87  87  GLY GLY B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  PRO 89  89  89  PRO PRO B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  PRO 91  91  91  PRO PRO B . n 
B 1 92  TYR 92  92  92  TYR TYR B . n 
B 1 93  GLN 93  93  93  GLN GLN B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  LYS 95  95  95  LYS LYS B . n 
B 1 96  GLN 96  96  96  GLN GLN B . n 
B 1 97  LEU 97  97  97  LEU LEU B . n 
B 1 98  HIS 98  98  98  HIS HIS B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 HIS 100 100 100 HIS HIS B . n 
B 1 101 TRP 101 101 101 TRP TRP B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 PRO 105 105 105 PRO PRO B . n 
B 1 106 TYR 106 106 106 TYR TYR B . n 
B 1 107 LYS 107 107 107 LYS LYS B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 SER 109 109 109 SER SER B . n 
B 1 110 GLU 110 110 110 GLU GLU B . n 
B 1 111 HIS 111 111 111 HIS HIS B . n 
B 1 112 SER 112 112 112 SER SER B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 ASP 114 114 114 ASP ASP B . n 
B 1 115 GLY 115 115 115 GLY GLY B . n 
B 1 116 GLU 116 116 116 GLU GLU B . n 
B 1 117 HIS 117 117 117 HIS HIS B . n 
B 1 118 PHE 118 118 118 PHE PHE B . n 
B 1 119 ALA 119 119 119 ALA ALA B . n 
B 1 120 MET 120 120 120 MET MET B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 MET 122 122 122 MET MET B . n 
B 1 123 HIS 123 123 123 HIS HIS B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 HIS 126 126 126 HIS HIS B . n 
B 1 127 GLU 127 127 127 GLU GLU B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 GLU 129 129 129 GLU GLU B . n 
B 1 130 LYS 130 130 130 LYS LYS B . n 
B 1 131 GLY 131 131 131 GLY GLY B . n 
B 1 132 THR 132 132 ?   ?   ?   B . n 
B 1 133 SER 133 133 ?   ?   ?   B . n 
B 1 134 ARG 134 134 ?   ?   ?   B . n 
B 1 135 ASN 135 135 ?   ?   ?   B . n 
B 1 136 VAL 136 136 ?   ?   ?   B . n 
B 1 137 LYS 137 137 ?   ?   ?   B . n 
B 1 138 GLU 138 138 ?   ?   ?   B . n 
B 1 139 ALA 139 139 ?   ?   ?   B . n 
B 1 140 GLN 140 140 ?   ?   ?   B . n 
B 1 141 ASP 141 141 141 ASP ASP B . n 
B 1 142 PRO 142 142 142 PRO PRO B . n 
B 1 143 GLU 143 143 143 GLU GLU B . n 
B 1 144 ASP 144 144 144 ASP ASP B . n 
B 1 145 GLU 145 145 145 GLU GLU B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 ALA 147 147 147 ALA ALA B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 LEU 149 149 149 LEU LEU B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 PHE 151 151 151 PHE PHE B . n 
B 1 152 LEU 152 152 152 LEU LEU B . n 
B 1 153 VAL 153 153 153 VAL VAL B . n 
B 1 154 GLU 154 154 154 GLU GLU B . n 
B 1 155 ALA 155 155 155 ALA ALA B . n 
B 1 156 GLY 156 156 156 GLY GLY B . n 
B 1 157 THR 157 157 157 THR THR B . n 
B 1 158 GLN 158 158 158 GLN GLN B . n 
B 1 159 VAL 159 159 159 VAL VAL B . n 
B 1 160 ASN 160 160 160 ASN ASN B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 GLY 162 162 162 GLY GLY B . n 
B 1 163 PHE 163 163 163 PHE PHE B . n 
B 1 164 GLN 164 164 164 GLN GLN B . n 
B 1 165 PRO 165 165 165 PRO PRO B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 VAL 167 167 167 VAL VAL B . n 
B 1 168 GLU 168 168 168 GLU GLU B . n 
B 1 169 ALA 169 169 169 ALA ALA B . n 
B 1 170 LEU 170 170 170 LEU LEU B . n 
B 1 171 SER 171 171 171 SER SER B . n 
B 1 172 ASN 172 172 172 ASN ASN B . n 
B 1 173 ILE 173 173 173 ILE ILE B . n 
B 1 174 PRO 174 174 174 PRO PRO B . n 
B 1 175 LYS 175 175 175 LYS LYS B . n 
B 1 176 PRO 176 176 176 PRO PRO B . n 
B 1 177 GLU 177 177 177 GLU GLU B . n 
B 1 178 MET 178 178 178 MET MET B . n 
B 1 179 SER 179 179 179 SER SER B . n 
B 1 180 THR 180 180 180 THR THR B . n 
B 1 181 THR 181 181 181 THR THR B . n 
B 1 182 MET 182 182 182 MET MET B . n 
B 1 183 ALA 183 183 183 ALA ALA B . n 
B 1 184 GLU 184 184 184 GLU GLU B . n 
B 1 185 SER 185 185 185 SER SER B . n 
B 1 186 SER 186 186 186 SER SER B . n 
B 1 187 LEU 187 187 187 LEU LEU B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 ASP 189 189 189 ASP ASP B . n 
B 1 190 LEU 190 190 190 LEU LEU B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 PRO 192 192 192 PRO PRO B . n 
B 1 193 LYS 193 193 193 LYS LYS B . n 
B 1 194 GLU 194 194 194 GLU GLU B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 LYS 196 196 196 LYS LYS B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 ARG 198 198 198 ARG ARG B . n 
B 1 199 HIS 199 199 199 HIS HIS B . n 
B 1 200 TYR 200 200 200 TYR TYR B . n 
B 1 201 PHE 201 201 201 PHE PHE B . n 
B 1 202 ARG 202 202 202 ARG ARG B . n 
B 1 203 TYR 203 203 203 TYR TYR B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 GLY 205 205 205 GLY GLY B . n 
B 1 206 SER 206 206 206 SER SER B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 THR 208 208 208 THR THR B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 PRO 210 210 210 PRO PRO B . n 
B 1 211 THR 211 211 211 THR THR B . n 
B 1 212 CYS 212 212 212 CYS CYS B . n 
B 1 213 ASP 213 213 213 ASP ASP B . n 
B 1 214 GLU 214 214 214 GLU GLU B . n 
B 1 215 LYS 215 215 215 LYS LYS B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 VAL 217 217 217 VAL VAL B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 THR 219 219 219 THR THR B . n 
B 1 220 VAL 220 220 220 VAL VAL B . n 
B 1 221 PHE 221 221 221 PHE PHE B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 GLU 223 223 223 GLU GLU B . n 
B 1 224 PRO 224 224 224 PRO PRO B . n 
B 1 225 ILE 225 225 225 ILE ILE B . n 
B 1 226 GLN 226 226 226 GLN GLN B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 HIS 228 228 228 HIS HIS B . n 
B 1 229 ARG 229 229 229 ARG ARG B . n 
B 1 230 GLU 230 230 230 GLU GLU B . n 
B 1 231 GLN 231 231 231 GLN GLN B . n 
B 1 232 ILE 232 232 232 ILE ILE B . n 
B 1 233 LEU 233 233 233 LEU LEU B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 PHE 235 235 235 PHE PHE B . n 
B 1 236 SER 236 236 236 SER SER B . n 
B 1 237 GLN 237 237 237 GLN GLN B . n 
B 1 238 LYS 238 238 238 LYS LYS B . n 
B 1 239 LEU 239 239 239 LEU LEU B . n 
B 1 240 TYR 240 240 240 TYR TYR B . n 
B 1 241 TYR 241 241 241 TYR TYR B . n 
B 1 242 ASP 242 242 242 ASP ASP B . n 
B 1 243 LYS 243 243 243 LYS LYS B . n 
B 1 244 GLU 244 244 244 GLU GLU B . n 
B 1 245 GLN 245 245 245 GLN GLN B . n 
B 1 246 THR 246 246 246 THR THR B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 SER 248 248 248 SER SER B . n 
B 1 249 MET 249 249 249 MET MET B . n 
B 1 250 LYS 250 250 250 LYS LYS B . n 
B 1 251 ASP 251 251 251 ASP ASP B . n 
B 1 252 ASN 252 252 252 ASN ASN B . n 
B 1 253 VAL 253 253 253 VAL VAL B . n 
B 1 254 ARG 254 254 254 ARG ARG B . n 
B 1 255 PRO 255 255 255 PRO PRO B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 GLN 257 257 257 GLN GLN B . n 
B 1 258 GLN 258 258 258 GLN GLN B . n 
B 1 259 LEU 259 259 259 LEU LEU B . n 
B 1 260 GLY 260 260 260 GLY GLY B . n 
B 1 261 GLN 261 261 261 GLN GLN B . n 
B 1 262 ARG 262 262 262 ARG ARG B . n 
B 1 263 THR 263 263 263 THR THR B . n 
B 1 264 VAL 264 264 264 VAL VAL B . n 
B 1 265 ILE 265 265 265 ILE ILE B . n 
B 1 266 LYS 266 266 266 LYS LYS B . n 
B 1 267 SER 267 267 267 SER SER B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   ALA 2   2   ?   ?   ?   C . n 
C 1 3   GLU 3   3   3   GLU GLU C . n 
C 1 4   SER 4   4   4   SER SER C . n 
C 1 5   HIS 5   5   5   HIS HIS C . n 
C 1 6   TRP 6   6   6   TRP TRP C . n 
C 1 7   CYS 7   7   7   CYS CYS C . n 
C 1 8   TYR 8   8   8   TYR TYR C . n 
C 1 9   GLU 9   9   9   GLU GLU C . n 
C 1 10  VAL 10  10  10  VAL VAL C . n 
C 1 11  GLN 11  11  11  GLN GLN C . n 
C 1 12  ALA 12  12  12  ALA ALA C . n 
C 1 13  GLU 13  13  13  GLU GLU C . n 
C 1 14  SER 14  14  14  SER SER C . n 
C 1 15  SER 15  15  15  SER SER C . n 
C 1 16  ASN 16  16  16  ASN ASN C . n 
C 1 17  TYR 17  17  17  TYR TYR C . n 
C 1 18  PRO 18  18  18  PRO PRO C . n 
C 1 19  CYS 19  19  19  CYS CYS C . n 
C 1 20  LEU 20  20  20  LEU LEU C . n 
C 1 21  VAL 21  21  21  VAL VAL C . n 
C 1 22  PRO 22  22  22  PRO PRO C . n 
C 1 23  VAL 23  23  23  VAL VAL C . n 
C 1 24  LYS 24  24  24  LYS LYS C . n 
C 1 25  TRP 25  25  25  TRP TRP C . n 
C 1 26  GLY 26  26  26  GLY GLY C . n 
C 1 27  GLY 27  27  27  GLY GLY C . n 
C 1 28  ASN 28  28  28  ASN ASN C . n 
C 1 29  CYS 29  29  29  CYS CYS C . n 
C 1 30  GLN 30  30  30  GLN GLN C . n 
C 1 31  LYS 31  31  31  LYS LYS C . n 
C 1 32  ASP 32  32  32  ASP ASP C . n 
C 1 33  ARG 33  33  33  ARG ARG C . n 
C 1 34  GLN 34  34  34  GLN GLN C . n 
C 1 35  SER 35  35  35  SER SER C . n 
C 1 36  PRO 36  36  36  PRO PRO C . n 
C 1 37  ILE 37  37  37  ILE ILE C . n 
C 1 38  ASN 38  38  38  ASN ASN C . n 
C 1 39  ILE 39  39  39  ILE ILE C . n 
C 1 40  VAL 40  40  40  VAL VAL C . n 
C 1 41  THR 41  41  41  THR THR C . n 
C 1 42  THR 42  42  42  THR THR C . n 
C 1 43  LYS 43  43  43  LYS LYS C . n 
C 1 44  ALA 44  44  44  ALA ALA C . n 
C 1 45  LYS 45  45  45  LYS LYS C . n 
C 1 46  VAL 46  46  46  VAL VAL C . n 
C 1 47  ASP 47  47  47  ASP ASP C . n 
C 1 48  LYS 48  48  48  LYS LYS C . n 
C 1 49  LYS 49  49  49  LYS LYS C . n 
C 1 50  LEU 50  50  50  LEU LEU C . n 
C 1 51  GLY 51  51  51  GLY GLY C . n 
C 1 52  ARG 52  52  52  ARG ARG C . n 
C 1 53  PHE 53  53  53  PHE PHE C . n 
C 1 54  PHE 54  54  54  PHE PHE C . n 
C 1 55  PHE 55  55  55  PHE PHE C . n 
C 1 56  SER 56  56  56  SER SER C . n 
C 1 57  GLY 57  57  57  GLY GLY C . n 
C 1 58  TYR 58  58  58  TYR TYR C . n 
C 1 59  ASP 59  59  59  ASP ASP C . n 
C 1 60  LYS 60  60  60  LYS LYS C . n 
C 1 61  LYS 61  61  61  LYS LYS C . n 
C 1 62  GLN 62  62  62  GLN GLN C . n 
C 1 63  THR 63  63  63  THR THR C . n 
C 1 64  TRP 64  64  64  TRP TRP C . n 
C 1 65  THR 65  65  65  THR THR C . n 
C 1 66  VAL 66  66  66  VAL VAL C . n 
C 1 67  GLN 67  67  67  GLN GLN C . n 
C 1 68  ASN 68  68  68  ASN ASN C . n 
C 1 69  ASN 69  69  69  ASN ASN C . n 
C 1 70  GLY 70  70  70  GLY GLY C . n 
C 1 71  HIS 71  71  71  HIS HIS C . n 
C 1 72  SER 72  72  72  SER SER C . n 
C 1 73  VAL 73  73  73  VAL VAL C . n 
C 1 74  MET 74  74  74  MET MET C . n 
C 1 75  MET 75  75  75  MET MET C . n 
C 1 76  LEU 76  76  76  LEU LEU C . n 
C 1 77  LEU 77  77  77  LEU LEU C . n 
C 1 78  GLU 78  78  78  GLU GLU C . n 
C 1 79  ASN 79  79  79  ASN ASN C . n 
C 1 80  LYS 80  80  80  LYS LYS C . n 
C 1 81  ALA 81  81  81  ALA ALA C . n 
C 1 82  SER 82  82  82  SER SER C . n 
C 1 83  ILE 83  83  83  ILE ILE C . n 
C 1 84  SER 84  84  84  SER SER C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  GLY 86  86  86  GLY GLY C . n 
C 1 87  GLY 87  87  87  GLY GLY C . n 
C 1 88  LEU 88  88  88  LEU LEU C . n 
C 1 89  PRO 89  89  89  PRO PRO C . n 
C 1 90  ALA 90  90  90  ALA ALA C . n 
C 1 91  PRO 91  91  91  PRO PRO C . n 
C 1 92  TYR 92  92  92  TYR TYR C . n 
C 1 93  GLN 93  93  93  GLN GLN C . n 
C 1 94  ALA 94  94  94  ALA ALA C . n 
C 1 95  LYS 95  95  95  LYS LYS C . n 
C 1 96  GLN 96  96  96  GLN GLN C . n 
C 1 97  LEU 97  97  97  LEU LEU C . n 
C 1 98  HIS 98  98  98  HIS HIS C . n 
C 1 99  LEU 99  99  99  LEU LEU C . n 
C 1 100 HIS 100 100 100 HIS HIS C . n 
C 1 101 TRP 101 101 101 TRP TRP C . n 
C 1 102 SER 102 102 102 SER SER C . n 
C 1 103 ASP 103 103 103 ASP ASP C . n 
C 1 104 LEU 104 104 104 LEU LEU C . n 
C 1 105 PRO 105 105 105 PRO PRO C . n 
C 1 106 TYR 106 106 106 TYR TYR C . n 
C 1 107 LYS 107 107 107 LYS LYS C . n 
C 1 108 GLY 108 108 108 GLY GLY C . n 
C 1 109 SER 109 109 109 SER SER C . n 
C 1 110 GLU 110 110 110 GLU GLU C . n 
C 1 111 HIS 111 111 111 HIS HIS C . n 
C 1 112 SER 112 112 112 SER SER C . n 
C 1 113 LEU 113 113 113 LEU LEU C . n 
C 1 114 ASP 114 114 114 ASP ASP C . n 
C 1 115 GLY 115 115 115 GLY GLY C . n 
C 1 116 GLU 116 116 116 GLU GLU C . n 
C 1 117 HIS 117 117 117 HIS HIS C . n 
C 1 118 PHE 118 118 118 PHE PHE C . n 
C 1 119 ALA 119 119 119 ALA ALA C . n 
C 1 120 MET 120 120 120 MET MET C . n 
C 1 121 GLU 121 121 121 GLU GLU C . n 
C 1 122 MET 122 122 122 MET MET C . n 
C 1 123 HIS 123 123 123 HIS HIS C . n 
C 1 124 ILE 124 124 124 ILE ILE C . n 
C 1 125 VAL 125 125 125 VAL VAL C . n 
C 1 126 HIS 126 126 126 HIS HIS C . n 
C 1 127 GLU 127 127 127 GLU GLU C . n 
C 1 128 LYS 128 128 128 LYS LYS C . n 
C 1 129 GLU 129 129 129 GLU GLU C . n 
C 1 130 LYS 130 130 130 LYS LYS C . n 
C 1 131 GLY 131 131 131 GLY GLY C . n 
C 1 132 THR 132 131 ?   ?   ?   C A n 
C 1 133 SER 133 131 ?   ?   ?   C B n 
C 1 134 ARG 134 131 ?   ?   ?   C C n 
C 1 135 ASN 135 131 ?   ?   ?   C D n 
C 1 136 VAL 136 131 ?   ?   ?   C E n 
C 1 137 LYS 137 131 ?   ?   ?   C F n 
C 1 138 GLU 138 131 ?   ?   ?   C G n 
C 1 139 ALA 139 131 ?   ?   ?   C H n 
C 1 140 GLN 140 131 ?   ?   ?   C I n 
C 1 141 ASP 141 131 ?   ?   ?   C J n 
C 1 142 PRO 142 140 140 PRO PRO C . n 
C 1 143 GLU 143 141 141 GLU GLU C . n 
C 1 144 ASP 144 142 142 ASP ASP C . n 
C 1 145 GLU 145 143 143 GLU GLU C . n 
C 1 146 ILE 146 144 144 ILE ILE C . n 
C 1 147 ALA 147 145 145 ALA ALA C . n 
C 1 148 VAL 148 146 146 VAL VAL C . n 
C 1 149 LEU 149 147 147 LEU LEU C . n 
C 1 150 ALA 150 148 148 ALA ALA C . n 
C 1 151 PHE 151 149 149 PHE PHE C . n 
C 1 152 LEU 152 150 150 LEU LEU C . n 
C 1 153 VAL 153 151 151 VAL VAL C . n 
C 1 154 GLU 154 152 152 GLU GLU C . n 
C 1 155 ALA 155 153 153 ALA ALA C . n 
C 1 156 GLY 156 154 154 GLY GLY C . n 
C 1 157 THR 157 155 155 THR THR C . n 
C 1 158 GLN 158 156 156 GLN GLN C . n 
C 1 159 VAL 159 157 157 VAL VAL C . n 
C 1 160 ASN 160 158 158 ASN ASN C . n 
C 1 161 GLU 161 159 159 GLU GLU C . n 
C 1 162 GLY 162 160 160 GLY GLY C . n 
C 1 163 PHE 163 161 161 PHE PHE C . n 
C 1 164 GLN 164 162 162 GLN GLN C . n 
C 1 165 PRO 165 163 163 PRO PRO C . n 
C 1 166 LEU 166 164 164 LEU LEU C . n 
C 1 167 VAL 167 165 165 VAL VAL C . n 
C 1 168 GLU 168 166 166 GLU GLU C . n 
C 1 169 ALA 169 167 167 ALA ALA C . n 
C 1 170 LEU 170 168 168 LEU LEU C . n 
C 1 171 SER 171 169 169 SER SER C . n 
C 1 172 ASN 172 170 170 ASN ASN C . n 
C 1 173 ILE 173 171 171 ILE ILE C . n 
C 1 174 PRO 174 172 172 PRO PRO C . n 
C 1 175 LYS 175 173 173 LYS LYS C . n 
C 1 176 PRO 176 174 174 PRO PRO C . n 
C 1 177 GLU 177 175 175 GLU GLU C . n 
C 1 178 MET 178 176 176 MET MET C . n 
C 1 179 SER 179 177 177 SER SER C . n 
C 1 180 THR 180 178 178 THR THR C . n 
C 1 181 THR 181 179 179 THR THR C . n 
C 1 182 MET 182 180 180 MET MET C . n 
C 1 183 ALA 183 181 181 ALA ALA C . n 
C 1 184 GLU 184 182 182 GLU GLU C . n 
C 1 185 SER 185 183 183 SER SER C . n 
C 1 186 SER 186 184 184 SER SER C . n 
C 1 187 LEU 187 185 185 LEU LEU C . n 
C 1 188 LEU 188 186 186 LEU LEU C . n 
C 1 189 ASP 189 187 187 ASP ASP C . n 
C 1 190 LEU 190 188 188 LEU LEU C . n 
C 1 191 LEU 191 189 189 LEU LEU C . n 
C 1 192 PRO 192 190 190 PRO PRO C . n 
C 1 193 LYS 193 191 191 LYS LYS C . n 
C 1 194 GLU 194 192 192 GLU GLU C . n 
C 1 195 GLU 195 193 193 GLU GLU C . n 
C 1 196 LYS 196 194 194 LYS LYS C . n 
C 1 197 LEU 197 195 195 LEU LEU C . n 
C 1 198 ARG 198 196 196 ARG ARG C . n 
C 1 199 HIS 199 197 197 HIS HIS C . n 
C 1 200 TYR 200 198 198 TYR TYR C . n 
C 1 201 PHE 201 199 199 PHE PHE C . n 
C 1 202 ARG 202 200 200 ARG ARG C . n 
C 1 203 TYR 203 201 201 TYR TYR C . n 
C 1 204 LEU 204 202 202 LEU LEU C . n 
C 1 205 GLY 205 203 203 GLY GLY C . n 
C 1 206 SER 206 204 204 SER SER C . n 
C 1 207 LEU 207 205 205 LEU LEU C . n 
C 1 208 THR 208 206 206 THR THR C . n 
C 1 209 THR 209 207 207 THR THR C . n 
C 1 210 PRO 210 208 208 PRO PRO C . n 
C 1 211 THR 211 209 209 THR THR C . n 
C 1 212 CYS 212 210 210 CYS CYS C . n 
C 1 213 ASP 213 211 211 ASP ASP C . n 
C 1 214 GLU 214 212 212 GLU GLU C . n 
C 1 215 LYS 215 213 213 LYS LYS C . n 
C 1 216 VAL 216 214 214 VAL VAL C . n 
C 1 217 VAL 217 215 215 VAL VAL C . n 
C 1 218 TRP 218 216 216 TRP TRP C . n 
C 1 219 THR 219 217 217 THR THR C . n 
C 1 220 VAL 220 218 218 VAL VAL C . n 
C 1 221 PHE 221 219 219 PHE PHE C . n 
C 1 222 ARG 222 220 220 ARG ARG C . n 
C 1 223 GLU 223 221 221 GLU GLU C . n 
C 1 224 PRO 224 222 222 PRO PRO C . n 
C 1 225 ILE 225 223 223 ILE ILE C . n 
C 1 226 GLN 226 224 224 GLN GLN C . n 
C 1 227 LEU 227 225 225 LEU LEU C . n 
C 1 228 HIS 228 226 226 HIS HIS C . n 
C 1 229 ARG 229 227 227 ARG ARG C . n 
C 1 230 GLU 230 228 228 GLU GLU C . n 
C 1 231 GLN 231 229 229 GLN GLN C . n 
C 1 232 ILE 232 230 230 ILE ILE C . n 
C 1 233 LEU 233 231 231 LEU LEU C . n 
C 1 234 ALA 234 232 232 ALA ALA C . n 
C 1 235 PHE 235 233 233 PHE PHE C . n 
C 1 236 SER 236 234 234 SER SER C . n 
C 1 237 GLN 237 235 235 GLN GLN C . n 
C 1 238 LYS 238 236 236 LYS LYS C . n 
C 1 239 LEU 239 237 237 LEU LEU C . n 
C 1 240 TYR 240 238 238 TYR TYR C . n 
C 1 241 TYR 241 239 239 TYR TYR C . n 
C 1 242 ASP 242 240 240 ASP ASP C . n 
C 1 243 LYS 243 241 241 LYS LYS C . n 
C 1 244 GLU 244 242 242 GLU GLU C . n 
C 1 245 GLN 245 243 243 GLN GLN C . n 
C 1 246 THR 246 244 244 THR THR C . n 
C 1 247 VAL 247 245 245 VAL VAL C . n 
C 1 248 SER 248 246 246 SER SER C . n 
C 1 249 MET 249 247 247 MET MET C . n 
C 1 250 LYS 250 248 248 LYS LYS C . n 
C 1 251 ASP 251 249 249 ASP ASP C . n 
C 1 252 ASN 252 250 250 ASN ASN C . n 
C 1 253 VAL 253 251 251 VAL VAL C . n 
C 1 254 ARG 254 252 252 ARG ARG C . n 
C 1 255 PRO 255 253 253 PRO PRO C . n 
C 1 256 LEU 256 254 254 LEU LEU C . n 
C 1 257 GLN 257 255 255 GLN GLN C . n 
C 1 258 GLN 258 256 256 GLN GLN C . n 
C 1 259 LEU 259 257 257 LEU LEU C . n 
C 1 260 GLY 260 258 258 GLY GLY C . n 
C 1 261 GLN 261 259 259 GLN GLN C . n 
C 1 262 ARG 262 260 260 ARG ARG C . n 
C 1 263 THR 263 261 261 THR THR C . n 
C 1 264 VAL 264 262 262 VAL VAL C . n 
C 1 265 ILE 265 263 263 ILE ILE C . n 
C 1 266 LYS 266 264 264 LYS LYS C . n 
C 1 267 SER 267 265 265 SER SER C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   ALA 2   2   ?   ?   ?   D . n 
D 1 3   GLU 3   3   ?   ?   ?   D . n 
D 1 4   SER 4   4   ?   ?   ?   D . n 
D 1 5   HIS 5   5   5   HIS HIS D . n 
D 1 6   TRP 6   6   6   TRP TRP D . n 
D 1 7   CYS 7   7   7   CYS CYS D . n 
D 1 8   TYR 8   8   8   TYR TYR D . n 
D 1 9   GLU 9   9   9   GLU GLU D . n 
D 1 10  VAL 10  10  10  VAL VAL D . n 
D 1 11  GLN 11  11  11  GLN GLN D . n 
D 1 12  ALA 12  12  12  ALA ALA D . n 
D 1 13  GLU 13  13  13  GLU GLU D . n 
D 1 14  SER 14  14  14  SER SER D . n 
D 1 15  SER 15  15  15  SER SER D . n 
D 1 16  ASN 16  16  16  ASN ASN D . n 
D 1 17  TYR 17  17  17  TYR TYR D . n 
D 1 18  PRO 18  18  18  PRO PRO D . n 
D 1 19  CYS 19  19  19  CYS CYS D . n 
D 1 20  LEU 20  20  20  LEU LEU D . n 
D 1 21  VAL 21  21  21  VAL VAL D . n 
D 1 22  PRO 22  22  22  PRO PRO D . n 
D 1 23  VAL 23  23  23  VAL VAL D . n 
D 1 24  LYS 24  24  24  LYS LYS D . n 
D 1 25  TRP 25  25  25  TRP TRP D . n 
D 1 26  GLY 26  26  26  GLY GLY D . n 
D 1 27  GLY 27  27  27  GLY GLY D . n 
D 1 28  ASN 28  28  28  ASN ASN D . n 
D 1 29  CYS 29  29  29  CYS CYS D . n 
D 1 30  GLN 30  30  30  GLN GLN D . n 
D 1 31  LYS 31  31  31  LYS LYS D . n 
D 1 32  ASP 32  32  32  ASP ASP D . n 
D 1 33  ARG 33  33  33  ARG ARG D . n 
D 1 34  GLN 34  34  34  GLN GLN D . n 
D 1 35  SER 35  35  35  SER SER D . n 
D 1 36  PRO 36  36  36  PRO PRO D . n 
D 1 37  ILE 37  37  37  ILE ILE D . n 
D 1 38  ASN 38  38  38  ASN ASN D . n 
D 1 39  ILE 39  39  39  ILE ILE D . n 
D 1 40  VAL 40  40  40  VAL VAL D . n 
D 1 41  THR 41  41  41  THR THR D . n 
D 1 42  THR 42  42  42  THR THR D . n 
D 1 43  LYS 43  43  43  LYS LYS D . n 
D 1 44  ALA 44  44  44  ALA ALA D . n 
D 1 45  LYS 45  45  45  LYS LYS D . n 
D 1 46  VAL 46  46  46  VAL VAL D . n 
D 1 47  ASP 47  47  47  ASP ASP D . n 
D 1 48  LYS 48  48  48  LYS LYS D . n 
D 1 49  LYS 49  49  49  LYS LYS D . n 
D 1 50  LEU 50  50  50  LEU LEU D . n 
D 1 51  GLY 51  51  51  GLY GLY D . n 
D 1 52  ARG 52  52  52  ARG ARG D . n 
D 1 53  PHE 53  53  53  PHE PHE D . n 
D 1 54  PHE 54  54  54  PHE PHE D . n 
D 1 55  PHE 55  55  55  PHE PHE D . n 
D 1 56  SER 56  56  56  SER SER D . n 
D 1 57  GLY 57  57  57  GLY GLY D . n 
D 1 58  TYR 58  58  58  TYR TYR D . n 
D 1 59  ASP 59  59  59  ASP ASP D . n 
D 1 60  LYS 60  60  60  LYS LYS D . n 
D 1 61  LYS 61  61  61  LYS LYS D . n 
D 1 62  GLN 62  62  62  GLN GLN D . n 
D 1 63  THR 63  63  63  THR THR D . n 
D 1 64  TRP 64  64  64  TRP TRP D . n 
D 1 65  THR 65  65  65  THR THR D . n 
D 1 66  VAL 66  66  66  VAL VAL D . n 
D 1 67  GLN 67  67  67  GLN GLN D . n 
D 1 68  ASN 68  68  68  ASN ASN D . n 
D 1 69  ASN 69  69  69  ASN ASN D . n 
D 1 70  GLY 70  70  70  GLY GLY D . n 
D 1 71  HIS 71  71  71  HIS HIS D . n 
D 1 72  SER 72  72  72  SER SER D . n 
D 1 73  VAL 73  73  73  VAL VAL D . n 
D 1 74  MET 74  74  74  MET MET D . n 
D 1 75  MET 75  75  75  MET MET D . n 
D 1 76  LEU 76  76  76  LEU LEU D . n 
D 1 77  LEU 77  77  77  LEU LEU D . n 
D 1 78  GLU 78  78  78  GLU GLU D . n 
D 1 79  ASN 79  79  79  ASN ASN D . n 
D 1 80  LYS 80  80  80  LYS LYS D . n 
D 1 81  ALA 81  81  81  ALA ALA D . n 
D 1 82  SER 82  82  82  SER SER D . n 
D 1 83  ILE 83  83  83  ILE ILE D . n 
D 1 84  SER 84  84  84  SER SER D . n 
D 1 85  GLY 85  85  85  GLY GLY D . n 
D 1 86  GLY 86  86  86  GLY GLY D . n 
D 1 87  GLY 87  87  87  GLY GLY D . n 
D 1 88  LEU 88  88  88  LEU LEU D . n 
D 1 89  PRO 89  89  89  PRO PRO D . n 
D 1 90  ALA 90  90  90  ALA ALA D . n 
D 1 91  PRO 91  91  91  PRO PRO D . n 
D 1 92  TYR 92  92  92  TYR TYR D . n 
D 1 93  GLN 93  93  93  GLN GLN D . n 
D 1 94  ALA 94  94  94  ALA ALA D . n 
D 1 95  LYS 95  95  95  LYS LYS D . n 
D 1 96  GLN 96  96  96  GLN GLN D . n 
D 1 97  LEU 97  97  97  LEU LEU D . n 
D 1 98  HIS 98  98  98  HIS HIS D . n 
D 1 99  LEU 99  99  99  LEU LEU D . n 
D 1 100 HIS 100 100 100 HIS HIS D . n 
D 1 101 TRP 101 101 101 TRP TRP D . n 
D 1 102 SER 102 102 102 SER SER D . n 
D 1 103 ASP 103 103 103 ASP ASP D . n 
D 1 104 LEU 104 104 104 LEU LEU D . n 
D 1 105 PRO 105 105 105 PRO PRO D . n 
D 1 106 TYR 106 106 106 TYR TYR D . n 
D 1 107 LYS 107 107 107 LYS LYS D . n 
D 1 108 GLY 108 108 108 GLY GLY D . n 
D 1 109 SER 109 109 109 SER SER D . n 
D 1 110 GLU 110 110 110 GLU GLU D . n 
D 1 111 HIS 111 111 111 HIS HIS D . n 
D 1 112 SER 112 112 112 SER SER D . n 
D 1 113 LEU 113 113 113 LEU LEU D . n 
D 1 114 ASP 114 114 114 ASP ASP D . n 
D 1 115 GLY 115 115 115 GLY GLY D . n 
D 1 116 GLU 116 116 116 GLU GLU D . n 
D 1 117 HIS 117 117 117 HIS HIS D . n 
D 1 118 PHE 118 118 118 PHE PHE D . n 
D 1 119 ALA 119 119 119 ALA ALA D . n 
D 1 120 MET 120 120 120 MET MET D . n 
D 1 121 GLU 121 121 121 GLU GLU D . n 
D 1 122 MET 122 122 122 MET MET D . n 
D 1 123 HIS 123 123 123 HIS HIS D . n 
D 1 124 ILE 124 124 124 ILE ILE D . n 
D 1 125 VAL 125 125 125 VAL VAL D . n 
D 1 126 HIS 126 126 126 HIS HIS D . n 
D 1 127 GLU 127 127 127 GLU GLU D . n 
D 1 128 LYS 128 128 128 LYS LYS D . n 
D 1 129 GLU 129 129 129 GLU GLU D . n 
D 1 130 LYS 130 130 130 LYS LYS D . n 
D 1 131 GLY 131 131 131 GLY GLY D . n 
D 1 132 THR 132 131 ?   ?   ?   D A n 
D 1 133 SER 133 131 ?   ?   ?   D B n 
D 1 134 ARG 134 131 ?   ?   ?   D C n 
D 1 135 ASN 135 131 ?   ?   ?   D D n 
D 1 136 VAL 136 131 ?   ?   ?   D E n 
D 1 137 LYS 137 131 ?   ?   ?   D F n 
D 1 138 GLU 138 131 ?   ?   ?   D G n 
D 1 139 ALA 139 131 ?   ?   ?   D H n 
D 1 140 GLN 140 131 ?   ?   ?   D I n 
D 1 141 ASP 141 131 ?   ?   ?   D J n 
D 1 142 PRO 142 140 140 PRO PRO D . n 
D 1 143 GLU 143 141 141 GLU GLU D . n 
D 1 144 ASP 144 142 142 ASP ASP D . n 
D 1 145 GLU 145 143 143 GLU GLU D . n 
D 1 146 ILE 146 144 144 ILE ILE D . n 
D 1 147 ALA 147 145 145 ALA ALA D . n 
D 1 148 VAL 148 146 146 VAL VAL D . n 
D 1 149 LEU 149 147 147 LEU LEU D . n 
D 1 150 ALA 150 148 148 ALA ALA D . n 
D 1 151 PHE 151 149 149 PHE PHE D . n 
D 1 152 LEU 152 150 150 LEU LEU D . n 
D 1 153 VAL 153 151 151 VAL VAL D . n 
D 1 154 GLU 154 152 152 GLU GLU D . n 
D 1 155 ALA 155 153 153 ALA ALA D . n 
D 1 156 GLY 156 154 154 GLY GLY D . n 
D 1 157 THR 157 155 155 THR THR D . n 
D 1 158 GLN 158 156 156 GLN GLN D . n 
D 1 159 VAL 159 157 157 VAL VAL D . n 
D 1 160 ASN 160 158 158 ASN ASN D . n 
D 1 161 GLU 161 159 159 GLU GLU D . n 
D 1 162 GLY 162 160 160 GLY GLY D . n 
D 1 163 PHE 163 161 161 PHE PHE D . n 
D 1 164 GLN 164 162 162 GLN GLN D . n 
D 1 165 PRO 165 163 163 PRO PRO D . n 
D 1 166 LEU 166 164 164 LEU LEU D . n 
D 1 167 VAL 167 165 165 VAL VAL D . n 
D 1 168 GLU 168 166 166 GLU GLU D . n 
D 1 169 ALA 169 167 167 ALA ALA D . n 
D 1 170 LEU 170 168 168 LEU LEU D . n 
D 1 171 SER 171 169 169 SER SER D . n 
D 1 172 ASN 172 170 170 ASN ASN D . n 
D 1 173 ILE 173 171 171 ILE ILE D . n 
D 1 174 PRO 174 172 172 PRO PRO D . n 
D 1 175 LYS 175 173 173 LYS LYS D . n 
D 1 176 PRO 176 174 174 PRO PRO D . n 
D 1 177 GLU 177 175 175 GLU GLU D . n 
D 1 178 MET 178 176 176 MET MET D . n 
D 1 179 SER 179 177 177 SER SER D . n 
D 1 180 THR 180 178 178 THR THR D . n 
D 1 181 THR 181 179 179 THR THR D . n 
D 1 182 MET 182 180 180 MET MET D . n 
D 1 183 ALA 183 181 181 ALA ALA D . n 
D 1 184 GLU 184 182 182 GLU GLU D . n 
D 1 185 SER 185 183 183 SER SER D . n 
D 1 186 SER 186 184 184 SER SER D . n 
D 1 187 LEU 187 185 185 LEU LEU D . n 
D 1 188 LEU 188 186 186 LEU LEU D . n 
D 1 189 ASP 189 187 187 ASP ASP D . n 
D 1 190 LEU 190 188 188 LEU LEU D . n 
D 1 191 LEU 191 189 189 LEU LEU D . n 
D 1 192 PRO 192 190 190 PRO PRO D . n 
D 1 193 LYS 193 191 191 LYS LYS D . n 
D 1 194 GLU 194 192 192 GLU GLU D . n 
D 1 195 GLU 195 193 193 GLU GLU D . n 
D 1 196 LYS 196 194 194 LYS LYS D . n 
D 1 197 LEU 197 195 195 LEU LEU D . n 
D 1 198 ARG 198 196 196 ARG ARG D . n 
D 1 199 HIS 199 197 197 HIS HIS D . n 
D 1 200 TYR 200 198 198 TYR TYR D . n 
D 1 201 PHE 201 199 199 PHE PHE D . n 
D 1 202 ARG 202 200 200 ARG ARG D . n 
D 1 203 TYR 203 201 201 TYR TYR D . n 
D 1 204 LEU 204 202 202 LEU LEU D . n 
D 1 205 GLY 205 203 203 GLY GLY D . n 
D 1 206 SER 206 204 204 SER SER D . n 
D 1 207 LEU 207 205 205 LEU LEU D . n 
D 1 208 THR 208 206 206 THR THR D . n 
D 1 209 THR 209 207 207 THR THR D . n 
D 1 210 PRO 210 208 208 PRO PRO D . n 
D 1 211 THR 211 209 209 THR THR D . n 
D 1 212 CYS 212 210 210 CYS CYS D . n 
D 1 213 ASP 213 211 211 ASP ASP D . n 
D 1 214 GLU 214 212 212 GLU GLU D . n 
D 1 215 LYS 215 213 213 LYS LYS D . n 
D 1 216 VAL 216 214 214 VAL VAL D . n 
D 1 217 VAL 217 215 215 VAL VAL D . n 
D 1 218 TRP 218 216 216 TRP TRP D . n 
D 1 219 THR 219 217 217 THR THR D . n 
D 1 220 VAL 220 218 218 VAL VAL D . n 
D 1 221 PHE 221 219 219 PHE PHE D . n 
D 1 222 ARG 222 220 220 ARG ARG D . n 
D 1 223 GLU 223 221 221 GLU GLU D . n 
D 1 224 PRO 224 222 222 PRO PRO D . n 
D 1 225 ILE 225 223 223 ILE ILE D . n 
D 1 226 GLN 226 224 224 GLN GLN D . n 
D 1 227 LEU 227 225 225 LEU LEU D . n 
D 1 228 HIS 228 226 226 HIS HIS D . n 
D 1 229 ARG 229 227 227 ARG ARG D . n 
D 1 230 GLU 230 228 228 GLU GLU D . n 
D 1 231 GLN 231 229 229 GLN GLN D . n 
D 1 232 ILE 232 230 230 ILE ILE D . n 
D 1 233 LEU 233 231 231 LEU LEU D . n 
D 1 234 ALA 234 232 232 ALA ALA D . n 
D 1 235 PHE 235 233 233 PHE PHE D . n 
D 1 236 SER 236 234 234 SER SER D . n 
D 1 237 GLN 237 235 235 GLN GLN D . n 
D 1 238 LYS 238 236 236 LYS LYS D . n 
D 1 239 LEU 239 237 237 LEU LEU D . n 
D 1 240 TYR 240 238 238 TYR TYR D . n 
D 1 241 TYR 241 239 239 TYR TYR D . n 
D 1 242 ASP 242 240 240 ASP ASP D . n 
D 1 243 LYS 243 241 241 LYS LYS D . n 
D 1 244 GLU 244 242 242 GLU GLU D . n 
D 1 245 GLN 245 243 243 GLN GLN D . n 
D 1 246 THR 246 244 244 THR THR D . n 
D 1 247 VAL 247 245 245 VAL VAL D . n 
D 1 248 SER 248 246 246 SER SER D . n 
D 1 249 MET 249 247 247 MET MET D . n 
D 1 250 LYS 250 248 248 LYS LYS D . n 
D 1 251 ASP 251 249 249 ASP ASP D . n 
D 1 252 ASN 252 250 250 ASN ASN D . n 
D 1 253 VAL 253 251 251 VAL VAL D . n 
D 1 254 ARG 254 252 252 ARG ARG D . n 
D 1 255 PRO 255 253 253 PRO PRO D . n 
D 1 256 LEU 256 254 254 LEU LEU D . n 
D 1 257 GLN 257 255 255 GLN GLN D . n 
D 1 258 GLN 258 256 256 GLN GLN D . n 
D 1 259 LEU 259 257 257 LEU LEU D . n 
D 1 260 GLY 260 258 258 GLY GLY D . n 
D 1 261 GLN 261 259 259 GLN GLN D . n 
D 1 262 ARG 262 260 260 ARG ARG D . n 
D 1 263 THR 263 261 261 THR THR D . n 
D 1 264 VAL 264 262 262 VAL VAL D . n 
D 1 265 ILE 265 263 263 ILE ILE D . n 
D 1 266 LYS 266 264 264 LYS LYS D . n 
D 1 267 SER 267 265 265 SER SER D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 ZN  1  301 1   ZN  ZN  A . 
F 3 6CC 1  302 1   6CC E35 A . 
G 2 ZN  1  301 2   ZN  ZN  B . 
H 3 6CC 1  302 2   6CC E35 B . 
I 2 ZN  1  301 3   ZN  ZN  C . 
J 3 6CC 1  302 3   6CC E35 C . 
K 2 ZN  1  301 4   ZN  ZN  D . 
L 4 HOH 1  401 6   HOH HOH A . 
L 4 HOH 2  402 80  HOH HOH A . 
L 4 HOH 3  403 69  HOH HOH A . 
L 4 HOH 4  404 85  HOH HOH A . 
L 4 HOH 5  405 81  HOH HOH A . 
L 4 HOH 6  406 11  HOH HOH A . 
L 4 HOH 7  407 73  HOH HOH A . 
L 4 HOH 8  408 27  HOH HOH A . 
L 4 HOH 9  409 35  HOH HOH A . 
L 4 HOH 10 410 86  HOH HOH A . 
L 4 HOH 11 411 79  HOH HOH A . 
L 4 HOH 12 412 1   HOH HOH A . 
L 4 HOH 13 413 8   HOH HOH A . 
L 4 HOH 14 414 67  HOH HOH A . 
L 4 HOH 15 415 2   HOH HOH A . 
L 4 HOH 16 416 29  HOH HOH A . 
L 4 HOH 17 417 4   HOH HOH A . 
L 4 HOH 18 418 36  HOH HOH A . 
L 4 HOH 19 419 3   HOH HOH A . 
L 4 HOH 20 420 34  HOH HOH A . 
L 4 HOH 21 421 78  HOH HOH A . 
L 4 HOH 22 422 32  HOH HOH A . 
L 4 HOH 23 423 83  HOH HOH A . 
L 4 HOH 24 424 30  HOH HOH A . 
L 4 HOH 25 425 12  HOH HOH A . 
L 4 HOH 26 426 68  HOH HOH A . 
L 4 HOH 27 427 33  HOH HOH A . 
L 4 HOH 28 428 72  HOH HOH A . 
L 4 HOH 29 429 13  HOH HOH A . 
L 4 HOH 30 430 38  HOH HOH A . 
L 4 HOH 31 431 5   HOH HOH A . 
L 4 HOH 32 432 31  HOH HOH A . 
L 4 HOH 33 433 39  HOH HOH A . 
L 4 HOH 34 434 9   HOH HOH A . 
L 4 HOH 35 435 28  HOH HOH A . 
L 4 HOH 36 436 37  HOH HOH A . 
L 4 HOH 37 437 74  HOH HOH A . 
L 4 HOH 38 438 25  HOH HOH A . 
L 4 HOH 39 439 82  HOH HOH A . 
L 4 HOH 40 440 70  HOH HOH A . 
L 4 HOH 41 441 15  HOH HOH A . 
L 4 HOH 42 442 40  HOH HOH A . 
L 4 HOH 43 443 84  HOH HOH A . 
L 4 HOH 44 444 10  HOH HOH A . 
L 4 HOH 45 445 26  HOH HOH A . 
L 4 HOH 46 446 14  HOH HOH A . 
L 4 HOH 47 447 77  HOH HOH A . 
L 4 HOH 48 448 76  HOH HOH A . 
L 4 HOH 49 449 105 HOH HOH A . 
L 4 HOH 50 450 75  HOH HOH A . 
L 4 HOH 51 451 71  HOH HOH A . 
M 4 HOH 1  401 19  HOH HOH B . 
M 4 HOH 2  402 113 HOH HOH B . 
M 4 HOH 3  403 59  HOH HOH B . 
M 4 HOH 4  404 107 HOH HOH B . 
M 4 HOH 5  405 49  HOH HOH B . 
M 4 HOH 6  406 50  HOH HOH B . 
M 4 HOH 7  407 42  HOH HOH B . 
M 4 HOH 8  408 99  HOH HOH B . 
M 4 HOH 9  409 92  HOH HOH B . 
M 4 HOH 10 410 111 HOH HOH B . 
M 4 HOH 11 411 95  HOH HOH B . 
M 4 HOH 12 412 96  HOH HOH B . 
M 4 HOH 13 413 16  HOH HOH B . 
M 4 HOH 14 414 18  HOH HOH B . 
M 4 HOH 15 415 91  HOH HOH B . 
M 4 HOH 16 416 94  HOH HOH B . 
M 4 HOH 17 417 45  HOH HOH B . 
M 4 HOH 18 418 60  HOH HOH B . 
M 4 HOH 19 419 48  HOH HOH B . 
M 4 HOH 20 420 112 HOH HOH B . 
M 4 HOH 21 421 89  HOH HOH B . 
M 4 HOH 22 422 93  HOH HOH B . 
M 4 HOH 23 423 51  HOH HOH B . 
M 4 HOH 24 424 44  HOH HOH B . 
M 4 HOH 25 425 57  HOH HOH B . 
M 4 HOH 26 426 54  HOH HOH B . 
M 4 HOH 27 427 41  HOH HOH B . 
M 4 HOH 28 428 98  HOH HOH B . 
M 4 HOH 29 429 87  HOH HOH B . 
M 4 HOH 30 430 100 HOH HOH B . 
M 4 HOH 31 431 46  HOH HOH B . 
M 4 HOH 32 432 55  HOH HOH B . 
M 4 HOH 33 433 88  HOH HOH B . 
M 4 HOH 34 434 110 HOH HOH B . 
M 4 HOH 35 435 7   HOH HOH B . 
M 4 HOH 36 436 97  HOH HOH B . 
M 4 HOH 37 437 52  HOH HOH B . 
M 4 HOH 38 438 108 HOH HOH B . 
M 4 HOH 39 439 109 HOH HOH B . 
M 4 HOH 40 440 43  HOH HOH B . 
M 4 HOH 41 441 56  HOH HOH B . 
M 4 HOH 42 442 53  HOH HOH B . 
M 4 HOH 43 443 47  HOH HOH B . 
M 4 HOH 44 444 58  HOH HOH B . 
M 4 HOH 45 445 106 HOH HOH B . 
N 4 HOH 1  401 116 HOH HOH C . 
N 4 HOH 2  402 22  HOH HOH C . 
N 4 HOH 3  403 114 HOH HOH C . 
N 4 HOH 4  404 117 HOH HOH C . 
N 4 HOH 5  405 62  HOH HOH C . 
N 4 HOH 6  406 20  HOH HOH C . 
N 4 HOH 7  407 90  HOH HOH C . 
N 4 HOH 8  408 101 HOH HOH C . 
N 4 HOH 9  409 17  HOH HOH C . 
N 4 HOH 10 410 21  HOH HOH C . 
N 4 HOH 11 411 61  HOH HOH C . 
N 4 HOH 12 412 23  HOH HOH C . 
N 4 HOH 13 413 115 HOH HOH C . 
O 4 HOH 1  401 65  HOH HOH D . 
O 4 HOH 2  402 103 HOH HOH D . 
O 4 HOH 3  403 64  HOH HOH D . 
O 4 HOH 4  404 102 HOH HOH D . 
O 4 HOH 5  405 119 HOH HOH D . 
O 4 HOH 6  406 104 HOH HOH D . 
O 4 HOH 7  407 66  HOH HOH D . 
O 4 HOH 8  408 24  HOH HOH D . 
O 4 HOH 9  409 118 HOH HOH D . 
O 4 HOH 10 410 63  HOH HOH D . 
O 4 HOH 11 411 120 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 B ARG 198 ? CD  ? B ARG 198 CD  
2  1 Y 1 B ARG 198 ? NE  ? B ARG 198 NE  
3  1 Y 1 B ARG 198 ? CZ  ? B ARG 198 CZ  
4  1 Y 1 B ARG 198 ? NH1 ? B ARG 198 NH1 
5  1 Y 1 B ARG 198 ? NH2 ? B ARG 198 NH2 
6  1 Y 1 C TYR 17  ? CG  ? C TYR 17  CG  
7  1 Y 1 C TYR 17  ? CD1 ? C TYR 17  CD1 
8  1 Y 1 C TYR 17  ? CD2 ? C TYR 17  CD2 
9  1 Y 1 C TYR 17  ? CE1 ? C TYR 17  CE1 
10 1 Y 1 C TYR 17  ? CE2 ? C TYR 17  CE2 
11 1 Y 1 C TYR 17  ? CZ  ? C TYR 17  CZ  
12 1 Y 1 C TYR 17  ? OH  ? C TYR 17  OH  
13 1 Y 1 D GLU 193 ? CD  ? D GLU 195 CD  
14 1 Y 1 D GLU 193 ? OE1 ? D GLU 195 OE1 
15 1 Y 1 D GLU 193 ? OE2 ? D GLU 195 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.6.0117 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.006    2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? MOSFLM      ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   117.340 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5IPZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.694 
_cell.length_a_esd                 ? 
_cell.length_b                     256.408 
_cell.length_b_esd                 ? 
_cell.length_c                     48.551 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         5IPZ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   5IPZ 
_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            2.21 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         43.9 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'Crystallization buffer was 0.2 M ammonium sulfate, 0.1 M sodium MES (pH 6.5) and 20% PEG MME 2,000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2015-06-26 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.826606 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5IPZ 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.100 
_reflns.d_resolution_low                 43.129 
_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                       51979 
_reflns.number_obs                       51979 
_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             85.000 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  2.800 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.049 
_reflns.pdbx_netI_over_av_sigmaI         7.455 
_reflns.pdbx_netI_over_sigmaI            10.500 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.074 
_reflns.pdbx_Rpim_I_all                  0.041 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         147290 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
2.10 2.21  ? 1.7  ? ? ? ? ? 77.00 ? ? ? ? 0.417 ? ? ? ? ? ? ? ? 2.80 ? ? ? ? ? ? ? 1  1 ? ? 
2.21 2.35  ? 2.3  ? ? ? ? ? 82.00 ? ? ? ? 0.316 ? ? ? ? ? ? ? ? 2.70 ? ? ? ? ? ? ? 2  1 ? ? 
2.35 2.51  ? 3.2  ? ? ? ? ? 85.60 ? ? ? ? 0.224 ? ? ? ? ? ? ? ? 2.70 ? ? ? ? ? ? ? 3  1 ? ? 
2.51 2.71  ? 4.5  ? ? ? ? ? 87.20 ? ? ? ? 0.158 ? ? ? ? ? ? ? ? 2.70 ? ? ? ? ? ? ? 4  1 ? ? 
2.71 2.97  ? 6.4  ? ? ? ? ? 88.90 ? ? ? ? 0.105 ? ? ? ? ? ? ? ? 2.80 ? ? ? ? ? ? ? 5  1 ? ? 
2.97 3.32  ? 9.6  ? ? ? ? ? 85.80 ? ? ? ? 0.064 ? ? ? ? ? ? ? ? 2.80 ? ? ? ? ? ? ? 6  1 ? ? 
3.32 3.83  ? 12.4 ? ? ? ? ? 89.00 ? ? ? ? 0.044 ? ? ? ? ? ? ? ? 3.00 ? ? ? ? ? ? ? 7  1 ? ? 
3.83 4.70  ? 14.8 ? ? ? ? ? 89.00 ? ? ? ? 0.034 ? ? ? ? ? ? ? ? 3.10 ? ? ? ? ? ? ? 8  1 ? ? 
4.70 6.64  ? 16.0 ? ? ? ? ? 88.90 ? ? ? ? 0.029 ? ? ? ? ? ? ? ? 3.00 ? ? ? ? ? ? ? 9  1 ? ? 
6.64 43.13 ? 9.7  ? ? ? ? ? 81.20 ? ? ? ? 0.028 ? ? ? ? ? ? ? ? 3.00 ? ? ? ? ? ? ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            -0.480 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.980 
_refine.aniso_B[2][2]                            -0.250 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            -0.180 
_refine.B_iso_max                                125.97 
_refine.B_iso_mean                               50.333 
_refine.B_iso_min                                17.19 
_refine.correlation_coeff_Fo_to_Fc               0.949 
_refine.correlation_coeff_Fo_to_Fc_free          0.903 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 5IPZ 
_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                            2.100 
_refine.ls_d_res_low                             43.129 
_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                     51926 
_refine.ls_number_reflns_R_free                  5105 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    84.780 
_refine.ls_percent_reflns_R_free                 9.800 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.233 
_refine.ls_R_factor_R_free                       0.306 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.225 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      3F7B 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.414 
_refine.pdbx_overall_ESU_R_Free                  0.298 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.414 
_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.pdbx_number_atoms_protein        8225 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         55 
_refine_hist.number_atoms_solvent             120 
_refine_hist.number_atoms_total               8400 
_refine_hist.d_res_high                       2.100 
_refine_hist.d_res_low                        43.129 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.012  0.020  8508  ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.743  1.965  11548 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.513  5.000  1023  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 38.550 25.063 395   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 20.482 15.000 1524  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 14.214 15.000 32    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.118  0.200  1239  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.021  6438  ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.100 
_refine_ls_shell.d_res_low                        2.154 
_refine_ls_shell.number_reflns_all                3430 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             336 
_refine_ls_shell.number_reflns_R_work             3094 
_refine_ls_shell.percent_reflns_obs               77.040 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.360 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.274 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     5IPZ 
_struct.title                        
'Crystal structure of human carbonic anhydrase isozyme IV with 5-(2-amino-1,3-thiazol-4-yl)-2-chlorobenzenesulfonamide' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5IPZ 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 3 ? 
I N N 2 ? 
J N N 3 ? 
K N N 2 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH4_HUMAN 
_struct_ref.pdbx_db_accession          P22748 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AESHWCYEVQAESSNYPCLVPVKWGGNCQKDRQSPINIVTTKAKVDKKLGRFFFSGYDKKQTWTVQNNGHSVMMLLENKA
SISGGGLPAPYQAKQLHLHWSDLPYKGSEHSLDGEHFAMEMHIVHEKEKGTSRNVKEAQDPEDEIAVLAFLVEAGTQVNE
GFQPLVEALSNIPKPEMSTTMAESSLLDLLPKEEKLRHYFRYLGSLTTPTCDEKVVWTVFREPIQLHREQILAFSQKLYY
DKEQTVSMKDNVRPLQQLGQRTVIKS
;
_struct_ref.pdbx_align_begin           19 
# 
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 5IPZ A 2 ? 267 ? P22748 19 ? 284 ? 2 267 
2 1 5IPZ B 2 ? 267 ? P22748 19 ? 284 ? 2 267 
3 1 5IPZ C 2 ? 267 ? P22748 19 ? 284 ? 2 265 
4 1 5IPZ D 2 ? 267 ? P22748 19 ? 284 ? 2 265 
# 
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 5IPZ MET A 1 ? UNP P22748 ? ? 'initiating methionine' 1 1 
2 5IPZ MET B 1 ? UNP P22748 ? ? 'initiating methionine' 1 2 
3 5IPZ MET C 1 ? UNP P22748 ? ? 'initiating methionine' 1 3 
4 5IPZ MET D 1 ? UNP P22748 ? ? 'initiating methionine' 1 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
4 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,F,L 
2 1 B,G,H,M 
3 1 C,I,J,N 
4 1 D,K,O   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_struct_biol.details                      'biological unit is the same as asym.' 
_struct_biol.id                           1 
_struct_biol.pdbx_parent_biol_id          ? 
_struct_biol.pdbx_formula_weight          ? 
_struct_biol.pdbx_formula_weight_method   ? 
_struct_biol.pdbx_aggregation_state       ? 
_struct_biol.pdbx_assembly_method         ? 
# 
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 TYR A 8   ? ALA A 12  ? TYR A 8   ALA A 12  5 ? 5  
HELX_P HELX_P2  AA2 VAL A 21  ? TRP A 25  ? VAL A 21  TRP A 25  5 ? 5  
HELX_P HELX_P3  AA3 VAL A 40  ? ALA A 44  ? VAL A 40  ALA A 44  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 160 ? GLY A 162 ? ASN A 160 GLY A 162 5 ? 3  
HELX_P HELX_P5  AA5 PHE A 163 ? LEU A 170 ? PHE A 163 LEU A 170 1 ? 8  
HELX_P HELX_P6  AA6 SER A 171 ? ILE A 173 ? SER A 171 ILE A 173 5 ? 3  
HELX_P HELX_P7  AA7 SER A 186 ? LEU A 190 ? SER A 186 LEU A 190 5 ? 5  
HELX_P HELX_P8  AA8 LYS A 193 ? ARG A 198 ? LYS A 193 ARG A 198 5 ? 6  
HELX_P HELX_P9  AA9 ARG A 229 ? LEU A 239 ? ARG A 229 LEU A 239 1 ? 11 
HELX_P HELX_P10 AB1 GLU B 9   ? SER B 14  ? GLU B 9   SER B 14  5 ? 6  
HELX_P HELX_P11 AB2 VAL B 21  ? TRP B 25  ? VAL B 21  TRP B 25  5 ? 5  
HELX_P HELX_P12 AB3 GLY B 26  ? LYS B 31  ? GLY B 26  LYS B 31  5 ? 6  
HELX_P HELX_P13 AB4 VAL B 40  ? ALA B 44  ? VAL B 40  ALA B 44  5 ? 5  
HELX_P HELX_P14 AB5 ASN B 160 ? GLY B 162 ? ASN B 160 GLY B 162 5 ? 3  
HELX_P HELX_P15 AB6 PHE B 163 ? LEU B 170 ? PHE B 163 LEU B 170 1 ? 8  
HELX_P HELX_P16 AB7 SER B 171 ? ILE B 173 ? SER B 171 ILE B 173 5 ? 3  
HELX_P HELX_P17 AB8 LYS B 193 ? LEU B 197 ? LYS B 193 LEU B 197 5 ? 5  
HELX_P HELX_P18 AB9 ARG B 229 ? LYS B 238 ? ARG B 229 LYS B 238 1 ? 10 
HELX_P HELX_P19 AC1 TYR C 8   ? GLU C 13  ? TYR C 8   GLU C 13  1 ? 6  
HELX_P HELX_P20 AC2 VAL C 21  ? TRP C 25  ? VAL C 21  TRP C 25  5 ? 5  
HELX_P HELX_P21 AC3 GLY C 27  ? LYS C 31  ? GLY C 27  LYS C 31  5 ? 5  
HELX_P HELX_P22 AC4 VAL C 40  ? ALA C 44  ? VAL C 40  ALA C 44  5 ? 5  
HELX_P HELX_P23 AC5 ASN C 160 ? GLY C 162 ? ASN C 158 GLY C 160 5 ? 3  
HELX_P HELX_P24 AC6 PHE C 163 ? ALA C 169 ? PHE C 161 ALA C 167 1 ? 7  
HELX_P HELX_P25 AC7 ARG C 229 ? LYS C 238 ? ARG C 227 LYS C 236 1 ? 10 
HELX_P HELX_P26 AC8 VAL D 10  ? SER D 15  ? VAL D 10  SER D 15  1 ? 6  
HELX_P HELX_P27 AC9 VAL D 40  ? ALA D 44  ? VAL D 40  ALA D 44  5 ? 5  
HELX_P HELX_P28 AD1 PHE D 163 ? ALA D 169 ? PHE D 161 ALA D 167 1 ? 7  
HELX_P HELX_P29 AD2 LEU D 170 ? ILE D 173 ? LEU D 168 ILE D 171 5 ? 4  
HELX_P HELX_P30 AD3 ARG D 229 ? LYS D 238 ? ARG D 227 LYS D 236 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 7   SG  ? ? ? 1_555 A CYS 19  SG ? ? A CYS 7   A CYS 19  1_555 ? ? ? ? ? ? ? 2.347 ? ? 
disulf2  disulf ? ? A CYS 29  SG  ? ? ? 1_555 A CYS 212 SG ? ? A CYS 29  A CYS 212 1_555 ? ? ? ? ? ? ? 2.302 ? ? 
disulf3  disulf ? ? B CYS 7   SG  ? ? ? 1_555 B CYS 19  SG ? ? B CYS 7   B CYS 19  1_555 ? ? ? ? ? ? ? 2.586 ? ? 
disulf4  disulf ? ? B CYS 29  SG  ? ? ? 1_555 B CYS 212 SG ? ? B CYS 29  B CYS 212 1_555 ? ? ? ? ? ? ? 2.299 ? ? 
disulf5  disulf ? ? C CYS 7   SG  ? ? ? 1_555 C CYS 19  SG ? ? C CYS 7   C CYS 19  1_555 ? ? ? ? ? ? ? 2.669 ? ? 
disulf6  disulf ? ? C CYS 29  SG  ? ? ? 1_555 C CYS 212 SG ? ? C CYS 29  C CYS 210 1_555 ? ? ? ? ? ? ? 2.669 ? ? 
disulf7  disulf ? ? D CYS 29  SG  ? ? ? 1_555 D CYS 212 SG ? ? D CYS 29  D CYS 210 1_555 ? ? ? ? ? ? ? 2.183 ? ? 
metalc1  metalc ? ? A HIS 98  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 98  A ZN  301 1_555 ? ? ? ? ? ? ? 1.883 ? ? 
metalc2  metalc ? ? A HIS 100 NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 100 A ZN  301 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
metalc3  metalc ? ? A HIS 123 ND1 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 123 A ZN  301 1_555 ? ? ? ? ? ? ? 1.923 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F 6CC .   N8 ? ? A ZN  301 A 6CC 302 1_555 ? ? ? ? ? ? ? 1.922 ? ? 
metalc5  metalc ? ? B HIS 98  NE2 ? ? ? 1_555 G ZN  .   ZN ? ? B HIS 98  B ZN  301 1_555 ? ? ? ? ? ? ? 1.865 ? ? 
metalc6  metalc ? ? B HIS 100 NE2 ? ? ? 1_555 G ZN  .   ZN ? ? B HIS 100 B ZN  301 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc7  metalc ? ? B HIS 123 ND1 ? ? ? 1_555 G ZN  .   ZN ? ? B HIS 123 B ZN  301 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc8  metalc ? ? C HIS 98  NE2 ? ? ? 1_555 I ZN  .   ZN ? ? C HIS 98  C ZN  301 1_555 ? ? ? ? ? ? ? 1.852 ? ? 
metalc9  metalc ? ? C HIS 100 NE2 ? ? ? 1_555 I ZN  .   ZN ? ? C HIS 100 C ZN  301 1_555 ? ? ? ? ? ? ? 2.358 ? ? 
metalc10 metalc ? ? C HIS 123 ND1 ? ? ? 1_555 I ZN  .   ZN ? ? C HIS 123 C ZN  301 1_555 ? ? ? ? ? ? ? 1.845 ? ? 
metalc11 metalc ? ? I ZN  .   ZN  ? ? ? 1_555 J 6CC .   N8 ? ? C ZN  301 C 6CC 302 1_555 ? ? ? ? ? ? ? 1.875 ? ? 
metalc12 metalc ? ? D HIS 98  NE2 ? ? ? 1_555 K ZN  .   ZN ? ? D HIS 98  D ZN  301 1_555 ? ? ? ? ? ? ? 2.100 ? ? 
metalc13 metalc ? ? D HIS 100 NE2 ? ? ? 1_555 K ZN  .   ZN ? ? D HIS 100 D ZN  301 1_555 ? ? ? ? ? ? ? 2.286 ? ? 
metalc14 metalc ? ? D HIS 123 ND1 ? ? ? 1_555 K ZN  .   ZN ? ? D HIS 123 D ZN  301 1_555 ? ? ? ? ? ? ? 1.953 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 98  ? A HIS 98  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 100 ? A HIS 100 ? 1_555 109.5 ? 
2  NE2 ? A HIS 98  ? A HIS 98  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 123 ? A HIS 123 ? 1_555 112.6 ? 
3  NE2 ? A HIS 100 ? A HIS 100 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 123 ? A HIS 123 ? 1_555 100.5 ? 
4  NE2 ? A HIS 98  ? A HIS 98  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N8  ? F 6CC .   ? A 6CC 302 ? 1_555 106.3 ? 
5  NE2 ? A HIS 100 ? A HIS 100 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N8  ? F 6CC .   ? A 6CC 302 ? 1_555 116.6 ? 
6  ND1 ? A HIS 123 ? A HIS 123 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N8  ? F 6CC .   ? A 6CC 302 ? 1_555 111.5 ? 
7  NE2 ? B HIS 98  ? B HIS 98  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 100 ? B HIS 100 ? 1_555 103.1 ? 
8  NE2 ? B HIS 98  ? B HIS 98  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 123 ? B HIS 123 ? 1_555 112.6 ? 
9  NE2 ? B HIS 100 ? B HIS 100 ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 123 ? B HIS 123 ? 1_555 105.8 ? 
10 NE2 ? C HIS 98  ? C HIS 98  ? 1_555 ZN ? I ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 100 ? C HIS 100 ? 1_555 106.1 ? 
11 NE2 ? C HIS 98  ? C HIS 98  ? 1_555 ZN ? I ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 123 ? C HIS 123 ? 1_555 113.7 ? 
12 NE2 ? C HIS 100 ? C HIS 100 ? 1_555 ZN ? I ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 123 ? C HIS 123 ? 1_555 105.2 ? 
13 NE2 ? C HIS 98  ? C HIS 98  ? 1_555 ZN ? I ZN . ? C ZN 301 ? 1_555 N8  ? J 6CC .   ? C 6CC 302 ? 1_555 109.2 ? 
14 NE2 ? C HIS 100 ? C HIS 100 ? 1_555 ZN ? I ZN . ? C ZN 301 ? 1_555 N8  ? J 6CC .   ? C 6CC 302 ? 1_555 104.9 ? 
15 ND1 ? C HIS 123 ? C HIS 123 ? 1_555 ZN ? I ZN . ? C ZN 301 ? 1_555 N8  ? J 6CC .   ? C 6CC 302 ? 1_555 116.6 ? 
16 NE2 ? D HIS 98  ? D HIS 98  ? 1_555 ZN ? K ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 100 ? D HIS 100 ? 1_555 93.9  ? 
17 NE2 ? D HIS 98  ? D HIS 98  ? 1_555 ZN ? K ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 123 ? D HIS 123 ? 1_555 118.3 ? 
18 NE2 ? D HIS 100 ? D HIS 100 ? 1_555 ZN ? K ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 123 ? D HIS 123 ? 1_555 97.1  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 7  ? CYS A 19  ? CYS A 7  ? 1_555 CYS A 19  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 29 ? CYS A 212 ? CYS A 29 ? 1_555 CYS A 212 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS B 7  ? CYS B 19  ? CYS B 7  ? 1_555 CYS B 19  ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS B 29 ? CYS B 212 ? CYS B 29 ? 1_555 CYS B 212 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5 CYS C 7  ? CYS C 19  ? CYS C 7  ? 1_555 CYS C 19  ? 1_555 SG SG . . . None 'Disulfide bridge' 
6 CYS C 29 ? CYS C 212 ? CYS C 29 ? 1_555 CYS C 210 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7 CYS D 29 ? CYS D 212 ? CYS D 29 ? 1_555 CYS D 210 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 35  A . ? SER 35  A PRO 36  A ? PRO 36  A 1 -5.41  
2 PRO 210 A . ? PRO 210 A THR 211 A ? THR 211 A 1 23.14  
3 SER 35  B . ? SER 35  B PRO 36  B ? PRO 36  B 1 4.19   
4 PRO 210 B . ? PRO 210 B THR 211 B ? THR 211 B 1 14.57  
5 SER 35  C . ? SER 35  C PRO 36  C ? PRO 36  C 1 2.23   
6 GLU 78  C . ? GLU 78  C ASN 79  C ? ASN 79  C 1 -14.62 
7 PRO 210 C . ? PRO 208 C THR 211 C ? THR 209 C 1 5.59   
8 SER 35  D . ? SER 35  D PRO 36  D ? PRO 36  D 1 2.36   
9 PRO 210 D . ? PRO 208 D THR 211 D ? THR 209 D 1 13.46  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 6  ? 
AA3 ? 9  ? 
AA4 ? 2  ? 
AA5 ? 9  ? 
AA6 ? 10 ? 
AA7 ? 2  ? 
AA8 ? 10 ? 
AA9 ? 6  ? 
AB1 ? 2  ? 
AB2 ? 9  ? 
AB3 ? 9  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? anti-parallel 
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? anti-parallel 
AA2 5 6  ? parallel      
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? anti-parallel 
AA3 6 7  ? parallel      
AA3 7 8  ? anti-parallel 
AA3 8 9  ? anti-parallel 
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA6 1 2  ? parallel      
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? parallel      
AA6 5 6  ? anti-parallel 
AA6 6 7  ? anti-parallel 
AA6 7 8  ? anti-parallel 
AA6 8 9  ? anti-parallel 
AA6 9 10 ? anti-parallel 
AA7 1 2  ? parallel      
AA8 1 2  ? parallel      
AA8 2 3  ? anti-parallel 
AA8 3 4  ? anti-parallel 
AA8 4 5  ? parallel      
AA8 5 6  ? anti-parallel 
AA8 6 7  ? anti-parallel 
AA8 7 8  ? anti-parallel 
AA8 8 9  ? anti-parallel 
AA8 9 10 ? anti-parallel 
AA9 1 2  ? anti-parallel 
AA9 2 3  ? anti-parallel 
AA9 3 4  ? anti-parallel 
AA9 4 5  ? anti-parallel 
AA9 5 6  ? parallel      
AB1 1 2  ? parallel      
AB2 1 2  ? parallel      
AB2 2 3  ? anti-parallel 
AB2 3 4  ? anti-parallel 
AB2 4 5  ? parallel      
AB2 5 6  ? anti-parallel 
AB2 6 7  ? anti-parallel 
AB2 7 8  ? anti-parallel 
AB2 8 9  ? anti-parallel 
AB3 1 2  ? parallel      
AB3 2 3  ? anti-parallel 
AB3 3 4  ? anti-parallel 
AB3 4 5  ? parallel      
AB3 5 6  ? anti-parallel 
AB3 6 7  ? anti-parallel 
AB3 7 8  ? anti-parallel 
AB3 8 9  ? 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  ASN A 38  ? ILE A 39  ? ASN A 38  ILE A 39  
AA1 2  SER A 112 ? LEU A 113 ? SER A 112 LEU A 113 
AA2 1  PHE A 53  ? SER A 56  ? PHE A 53  SER A 56  
AA2 2  SER A 82  ? GLY A 85  ? SER A 82  GLY A 85  
AA2 3  TYR A 92  ? TRP A 101 ? TYR A 92  TRP A 101 
AA2 4  MET A 120 ? LYS A 128 ? MET A 120 LYS A 128 
AA2 5  ILE A 146 ? GLY A 156 ? ILE A 146 GLY A 156 
AA2 6  ILE A 225 ? HIS A 228 ? ILE A 225 HIS A 228 
AA3 1  MET A 178 ? THR A 181 ? MET A 178 THR A 181 
AA3 2  THR A 65  ? ASN A 68  ? THR A 65  ASN A 68  
AA3 3  VAL A 73  ? LEU A 76  ? VAL A 73  LEU A 76  
AA3 4  TYR A 92  ? TRP A 101 ? TYR A 92  TRP A 101 
AA3 5  MET A 120 ? LYS A 128 ? MET A 120 LYS A 128 
AA3 6  ILE A 146 ? GLY A 156 ? ILE A 146 GLY A 156 
AA3 7  VAL A 216 ? PHE A 221 ? VAL A 216 PHE A 221 
AA3 8  TYR A 200 ? GLY A 205 ? TYR A 200 GLY A 205 
AA3 9  ILE A 265 ? LYS A 266 ? ILE A 265 LYS A 266 
AA4 1  ASN B 38  ? ILE B 39  ? ASN B 38  ILE B 39  
AA4 2  SER B 112 ? LEU B 113 ? SER B 112 LEU B 113 
AA5 1  LYS B 45  ? VAL B 46  ? LYS B 45  VAL B 46  
AA5 2  ILE B 265 ? LYS B 266 ? ILE B 265 LYS B 266 
AA5 3  TYR B 200 ? GLY B 205 ? TYR B 200 GLY B 205 
AA5 4  VAL B 216 ? HIS B 228 ? VAL B 216 HIS B 228 
AA5 5  ILE B 146 ? GLY B 156 ? ILE B 146 GLY B 156 
AA5 6  MET B 120 ? LYS B 128 ? MET B 120 LYS B 128 
AA5 7  TYR B 92  ? TRP B 101 ? TYR B 92  TRP B 101 
AA5 8  SER B 82  ? GLY B 85  ? SER B 82  GLY B 85  
AA5 9  PHE B 53  ? SER B 56  ? PHE B 53  SER B 56  
AA6 1  LYS B 45  ? VAL B 46  ? LYS B 45  VAL B 46  
AA6 2  ILE B 265 ? LYS B 266 ? ILE B 265 LYS B 266 
AA6 3  TYR B 200 ? GLY B 205 ? TYR B 200 GLY B 205 
AA6 4  VAL B 216 ? HIS B 228 ? VAL B 216 HIS B 228 
AA6 5  ILE B 146 ? GLY B 156 ? ILE B 146 GLY B 156 
AA6 6  MET B 120 ? LYS B 128 ? MET B 120 LYS B 128 
AA6 7  TYR B 92  ? TRP B 101 ? TYR B 92  TRP B 101 
AA6 8  VAL B 73  ? LEU B 76  ? VAL B 73  LEU B 76  
AA6 9  THR B 65  ? ASN B 68  ? THR B 65  ASN B 68  
AA6 10 SER B 179 ? THR B 181 ? SER B 179 THR B 181 
AA7 1  ASN C 38  ? ILE C 39  ? ASN C 38  ILE C 39  
AA7 2  SER C 112 ? LEU C 113 ? SER C 112 LEU C 113 
AA8 1  LYS C 45  ? VAL C 46  ? LYS C 45  VAL C 46  
AA8 2  ILE C 265 ? LYS C 266 ? ILE C 263 LYS C 264 
AA8 3  TYR C 200 ? GLY C 205 ? TYR C 198 GLY C 203 
AA8 4  VAL C 216 ? PHE C 221 ? VAL C 214 PHE C 219 
AA8 5  ILE C 146 ? GLY C 156 ? ILE C 144 GLY C 154 
AA8 6  MET C 120 ? LYS C 128 ? MET C 120 LYS C 128 
AA8 7  TYR C 92  ? TRP C 101 ? TYR C 92  TRP C 101 
AA8 8  VAL C 73  ? LEU C 76  ? VAL C 73  LEU C 76  
AA8 9  TRP C 64  ? ASN C 68  ? TRP C 64  ASN C 68  
AA8 10 THR C 181 ? MET C 182 ? THR C 179 MET C 180 
AA9 1  PHE C 53  ? SER C 56  ? PHE C 53  SER C 56  
AA9 2  SER C 82  ? GLY C 85  ? SER C 82  GLY C 85  
AA9 3  TYR C 92  ? TRP C 101 ? TYR C 92  TRP C 101 
AA9 4  MET C 120 ? LYS C 128 ? MET C 120 LYS C 128 
AA9 5  ILE C 146 ? GLY C 156 ? ILE C 144 GLY C 154 
AA9 6  ILE C 225 ? HIS C 228 ? ILE C 223 HIS C 226 
AB1 1  ASN D 38  ? ILE D 39  ? ASN D 38  ILE D 39  
AB1 2  SER D 112 ? LEU D 113 ? SER D 112 LEU D 113 
AB2 1  LYS D 45  ? VAL D 46  ? LYS D 45  VAL D 46  
AB2 2  ILE D 265 ? LYS D 266 ? ILE D 263 LYS D 264 
AB2 3  TYR D 200 ? GLY D 205 ? TYR D 198 GLY D 203 
AB2 4  VAL D 216 ? HIS D 228 ? VAL D 214 HIS D 226 
AB2 5  ILE D 146 ? GLY D 156 ? ILE D 144 GLY D 154 
AB2 6  MET D 120 ? LYS D 128 ? MET D 120 LYS D 128 
AB2 7  TYR D 92  ? TRP D 101 ? TYR D 92  TRP D 101 
AB2 8  SER D 82  ? GLY D 85  ? SER D 82  GLY D 85  
AB2 9  PHE D 53  ? SER D 56  ? PHE D 53  SER D 56  
AB3 1  LYS D 45  ? VAL D 46  ? LYS D 45  VAL D 46  
AB3 2  ILE D 265 ? LYS D 266 ? ILE D 263 LYS D 264 
AB3 3  TYR D 200 ? GLY D 205 ? TYR D 198 GLY D 203 
AB3 4  VAL D 216 ? HIS D 228 ? VAL D 214 HIS D 226 
AB3 5  ILE D 146 ? GLY D 156 ? ILE D 144 GLY D 154 
AB3 6  MET D 120 ? LYS D 128 ? MET D 120 LYS D 128 
AB3 7  TYR D 92  ? TRP D 101 ? TYR D 92  TRP D 101 
AB3 8  VAL D 73  ? LEU D 76  ? VAL D 73  LEU D 76  
AB3 9  VAL D 66  ? ASN D 68  ? VAL D 66  ASN D 68  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 39  ? N ILE A 39  O SER A 112 ? O SER A 112 
AA2 1 2  N PHE A 54  ? N PHE A 54  O SER A 84  ? O SER A 84  
AA2 2 3  N ILE A 83  ? N ILE A 83  O TYR A 92  ? O TYR A 92  
AA2 3 4  N HIS A 100 ? N HIS A 100 O GLU A 121 ? O GLU A 121 
AA2 4 5  N HIS A 126 ? N HIS A 126 O ALA A 147 ? O ALA A 147 
AA2 5 6  N GLY A 156 ? N GLY A 156 O LEU A 227 ? O LEU A 227 
AA3 1 2  O THR A 180 ? O THR A 180 N VAL A 66  ? N VAL A 66  
AA3 2 3  N GLN A 67  ? N GLN A 67  O MET A 74  ? O MET A 74  
AA3 3 4  N MET A 75  ? N MET A 75  O LEU A 97  ? O LEU A 97  
AA3 4 5  N HIS A 100 ? N HIS A 100 O GLU A 121 ? O GLU A 121 
AA3 5 6  N HIS A 126 ? N HIS A 126 O ALA A 147 ? O ALA A 147 
AA3 6 7  N ILE A 146 ? N ILE A 146 O VAL A 217 ? O VAL A 217 
AA3 7 8  O TRP A 218 ? O TRP A 218 N TYR A 203 ? N TYR A 203 
AA3 8 9  N ARG A 202 ? N ARG A 202 O ILE A 265 ? O ILE A 265 
AA4 1 2  N ILE B 39  ? N ILE B 39  O SER B 112 ? O SER B 112 
AA5 1 2  N LYS B 45  ? N LYS B 45  O LYS B 266 ? O LYS B 266 
AA5 2 3  O ILE B 265 ? O ILE B 265 N ARG B 202 ? N ARG B 202 
AA5 3 4  N PHE B 201 ? N PHE B 201 O VAL B 220 ? O VAL B 220 
AA5 4 5  O VAL B 217 ? O VAL B 217 N ILE B 146 ? N ILE B 146 
AA5 5 6  O VAL B 153 ? O VAL B 153 N MET B 120 ? N MET B 120 
AA5 6 7  O VAL B 125 ? O VAL B 125 N LYS B 95  ? N LYS B 95  
AA5 7 8  O TYR B 92  ? O TYR B 92  N ILE B 83  ? N ILE B 83  
AA5 8 9  O SER B 84  ? O SER B 84  N PHE B 54  ? N PHE B 54  
AA6 1 2  N LYS B 45  ? N LYS B 45  O LYS B 266 ? O LYS B 266 
AA6 2 3  O ILE B 265 ? O ILE B 265 N ARG B 202 ? N ARG B 202 
AA6 3 4  N PHE B 201 ? N PHE B 201 O VAL B 220 ? O VAL B 220 
AA6 4 5  O VAL B 217 ? O VAL B 217 N ILE B 146 ? N ILE B 146 
AA6 5 6  O VAL B 153 ? O VAL B 153 N MET B 120 ? N MET B 120 
AA6 6 7  O VAL B 125 ? O VAL B 125 N LYS B 95  ? N LYS B 95  
AA6 7 8  O LEU B 97  ? O LEU B 97  N MET B 75  ? N MET B 75  
AA6 8 9  O MET B 74  ? O MET B 74  N GLN B 67  ? N GLN B 67  
AA6 9 10 N VAL B 66  ? N VAL B 66  O THR B 180 ? O THR B 180 
AA7 1 2  N ILE C 39  ? N ILE C 39  O SER C 112 ? O SER C 112 
AA8 1 2  N LYS C 45  ? N LYS C 45  O LYS C 266 ? O LYS C 264 
AA8 2 3  O ILE C 265 ? O ILE C 263 N ARG C 202 ? N ARG C 200 
AA8 3 4  N PHE C 201 ? N PHE C 199 O VAL C 220 ? O VAL C 218 
AA8 4 5  O THR C 219 ? O THR C 217 N ALA C 150 ? N ALA C 148 
AA8 5 6  O PHE C 151 ? O PHE C 149 N MET C 122 ? N MET C 122 
AA8 6 7  O VAL C 125 ? O VAL C 125 N GLN C 96  ? N GLN C 96  
AA8 7 8  O LEU C 97  ? O LEU C 97  N MET C 75  ? N MET C 75  
AA8 8 9  O MET C 74  ? O MET C 74  N GLN C 67  ? N GLN C 67  
AA8 9 10 N TRP C 64  ? N TRP C 64  O MET C 182 ? O MET C 180 
AA9 1 2  N PHE C 54  ? N PHE C 54  O SER C 84  ? O SER C 84  
AA9 2 3  N ILE C 83  ? N ILE C 83  O TYR C 92  ? O TYR C 92  
AA9 3 4  N GLN C 96  ? N GLN C 96  O VAL C 125 ? O VAL C 125 
AA9 4 5  N MET C 122 ? N MET C 122 O PHE C 151 ? O PHE C 149 
AA9 5 6  N LEU C 152 ? N LEU C 150 O ILE C 225 ? O ILE C 223 
AB1 1 2  N ILE D 39  ? N ILE D 39  O SER D 112 ? O SER D 112 
AB2 1 2  N LYS D 45  ? N LYS D 45  O LYS D 266 ? O LYS D 264 
AB2 2 3  O ILE D 265 ? O ILE D 263 N ARG D 202 ? N ARG D 200 
AB2 3 4  N PHE D 201 ? N PHE D 199 O VAL D 220 ? O VAL D 218 
AB2 4 5  O THR D 219 ? O THR D 217 N ALA D 150 ? N ALA D 148 
AB2 5 6  O VAL D 153 ? O VAL D 151 N MET D 120 ? N MET D 120 
AB2 6 7  O HIS D 123 ? O HIS D 123 N HIS D 98  ? N HIS D 98  
AB2 7 8  O TYR D 92  ? O TYR D 92  N ILE D 83  ? N ILE D 83  
AB2 8 9  O SER D 84  ? O SER D 84  N PHE D 54  ? N PHE D 54  
AB3 1 2  N LYS D 45  ? N LYS D 45  O LYS D 266 ? O LYS D 264 
AB3 2 3  O ILE D 265 ? O ILE D 263 N ARG D 202 ? N ARG D 200 
AB3 3 4  N PHE D 201 ? N PHE D 199 O VAL D 220 ? O VAL D 218 
AB3 4 5  O THR D 219 ? O THR D 217 N ALA D 150 ? N ALA D 148 
AB3 5 6  O VAL D 153 ? O VAL D 151 N MET D 120 ? N MET D 120 
AB3 6 7  O HIS D 123 ? O HIS D 123 N HIS D 98  ? N HIS D 98  
AB3 7 8  O LEU D 97  ? O LEU D 97  N MET D 75  ? N MET D 75  
AB3 8 9  O MET D 74  ? O MET D 74  N GLN D 67  ? N GLN D 67  
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A 6CC 302 ? 12 'binding site for residue 6CC A 302' 
AC3 Software B ZN  301 ? 4  'binding site for residue ZN B 301'  
AC4 Software B 6CC 302 ? 12 'binding site for residue 6CC B 302' 
AC5 Software C ZN  301 ? 4  'binding site for residue ZN C 301'  
AC6 Software C 6CC 302 ? 11 'binding site for residue 6CC C 302' 
AC7 Software D ZN  301 ? 4  'binding site for residue ZN D 301'  
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 98  ? HIS A 98  . ? 1_555 ? 
2  AC1 4  HIS A 100 ? HIS A 100 . ? 1_555 ? 
3  AC1 4  HIS A 123 ? HIS A 123 . ? 1_555 ? 
4  AC1 4  6CC F .   ? 6CC A 302 . ? 1_555 ? 
5  AC2 12 ASN A 69  ? ASN A 69  . ? 1_555 ? 
6  AC2 12 GLN A 96  ? GLN A 96  . ? 1_555 ? 
7  AC2 12 HIS A 98  ? HIS A 98  . ? 1_555 ? 
8  AC2 12 HIS A 100 ? HIS A 100 . ? 1_555 ? 
9  AC2 12 HIS A 123 ? HIS A 123 . ? 1_555 ? 
10 AC2 12 VAL A 125 ? VAL A 125 . ? 1_555 ? 
11 AC2 12 VAL A 148 ? VAL A 148 . ? 1_555 ? 
12 AC2 12 LEU A 207 ? LEU A 207 . ? 1_555 ? 
13 AC2 12 THR A 208 ? THR A 208 . ? 1_555 ? 
14 AC2 12 THR A 209 ? THR A 209 . ? 1_555 ? 
15 AC2 12 TRP A 218 ? TRP A 218 . ? 1_555 ? 
16 AC2 12 ZN  E .   ? ZN  A 301 . ? 1_555 ? 
17 AC3 4  HIS B 98  ? HIS B 98  . ? 1_555 ? 
18 AC3 4  HIS B 100 ? HIS B 100 . ? 1_555 ? 
19 AC3 4  HIS B 123 ? HIS B 123 . ? 1_555 ? 
20 AC3 4  6CC H .   ? 6CC B 302 . ? 1_555 ? 
21 AC4 12 ASN B 69  ? ASN B 69  . ? 1_555 ? 
22 AC4 12 GLN B 96  ? GLN B 96  . ? 1_555 ? 
23 AC4 12 HIS B 98  ? HIS B 98  . ? 1_555 ? 
24 AC4 12 HIS B 100 ? HIS B 100 . ? 1_555 ? 
25 AC4 12 HIS B 123 ? HIS B 123 . ? 1_555 ? 
26 AC4 12 VAL B 125 ? VAL B 125 . ? 1_555 ? 
27 AC4 12 VAL B 148 ? VAL B 148 . ? 1_555 ? 
28 AC4 12 LEU B 207 ? LEU B 207 . ? 1_555 ? 
29 AC4 12 THR B 208 ? THR B 208 . ? 1_555 ? 
30 AC4 12 THR B 209 ? THR B 209 . ? 1_555 ? 
31 AC4 12 TRP B 218 ? TRP B 218 . ? 1_555 ? 
32 AC4 12 ZN  G .   ? ZN  B 301 . ? 1_555 ? 
33 AC5 4  HIS C 98  ? HIS C 98  . ? 1_555 ? 
34 AC5 4  HIS C 100 ? HIS C 100 . ? 1_555 ? 
35 AC5 4  HIS C 123 ? HIS C 123 . ? 1_555 ? 
36 AC5 4  6CC J .   ? 6CC C 302 . ? 1_555 ? 
37 AC6 11 ASN C 69  ? ASN C 69  . ? 1_555 ? 
38 AC6 11 GLN C 96  ? GLN C 96  . ? 1_555 ? 
39 AC6 11 HIS C 98  ? HIS C 98  . ? 1_555 ? 
40 AC6 11 HIS C 100 ? HIS C 100 . ? 1_555 ? 
41 AC6 11 GLU C 110 ? GLU C 110 . ? 1_555 ? 
42 AC6 11 HIS C 123 ? HIS C 123 . ? 1_555 ? 
43 AC6 11 LEU C 207 ? LEU C 205 . ? 1_555 ? 
44 AC6 11 THR C 208 ? THR C 206 . ? 1_555 ? 
45 AC6 11 THR C 209 ? THR C 207 . ? 1_555 ? 
46 AC6 11 TRP C 218 ? TRP C 216 . ? 1_555 ? 
47 AC6 11 ZN  I .   ? ZN  C 301 . ? 1_555 ? 
48 AC7 4  HIS D 98  ? HIS D 98  . ? 1_555 ? 
49 AC7 4  HIS D 100 ? HIS D 100 . ? 1_555 ? 
50 AC7 4  HIS D 123 ? HIS D 123 . ? 1_555 ? 
51 AC7 4  THR D 208 ? THR D 206 . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   5IPZ 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   ZN 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   ZN 
_pdbx_validate_close_contact.auth_seq_id_1    301 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   N8 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   6CC 
_pdbx_validate_close_contact.auth_seq_id_2    302 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.56 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG B HIS 98  ? ? CD2 B HIS 98  ? ? 1.413 1.354 0.059 0.009 N 
2 1 CG C HIS 123 ? ? CD2 C HIS 123 ? ? 1.412 1.354 0.058 0.009 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 N C LEU 77  ? ? CA C LEU 77  ? ? C  C LEU 77  ? ? 89.63  111.00 -21.37 2.70 N 
2 1 N C GLU 78  ? ? CA C GLU 78  ? ? CB C GLU 78  ? ? 86.46  110.60 -24.14 1.80 N 
3 1 C D LEU 189 ? ? N  D PRO 190 ? ? CA D PRO 190 ? ? 128.49 119.30 9.19   1.50 Y 
# 
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 SER A 4   ? ? -152.12 -156.52 
2  1 ARG A 134 ? ? -172.57 128.94  
3  1 GLU A 143 ? ? -57.97  -5.27   
4  1 ASP A 144 ? ? -143.61 33.89   
5  1 LYS A 215 ? ? -141.58 26.75   
6  1 GLN A 245 ? ? 71.14   39.04   
7  1 SER B 4   ? ? 74.88   -55.12  
8  1 ALA B 12  ? ? -97.33  39.73   
9  1 GLU B 13  ? ? -146.59 -8.30   
10 1 SER B 14  ? ? -87.47  -72.38  
11 1 TYR B 17  ? ? 77.13   39.62   
12 1 PRO B 18  ? ? -89.41  31.71   
13 1 ASN B 79  ? ? 51.18   14.10   
14 1 SER B 102 ? ? -129.46 -161.63 
15 1 LYS B 107 ? ? -141.75 12.63   
16 1 ASP B 114 ? ? 32.63   51.92   
17 1 ILE B 173 ? ? -147.05 54.37   
18 1 ALA B 183 ? ? -49.41  153.63  
19 1 THR B 211 ? ? -98.97  30.79   
20 1 GLU B 244 ? ? -64.86  1.40    
21 1 SER C 4   ? ? -102.80 -168.62 
22 1 SER C 14  ? ? -115.99 61.85   
23 1 SER C 15  ? ? -169.25 -163.50 
24 1 ASN C 16  ? ? -121.50 -61.24  
25 1 CYS C 19  ? ? -119.49 -154.06 
26 1 GLN C 30  ? ? -98.02  34.35   
27 1 ARG C 33  ? ? -101.21 60.71   
28 1 ARG C 52  ? ? -44.43  158.20  
29 1 GLN C 62  ? ? 179.01  169.90  
30 1 HIS C 71  ? ? -143.90 -11.02  
31 1 GLU C 78  ? ? -139.24 -30.76  
32 1 ASN C 79  ? ? 163.15  -145.85 
33 1 LYS C 107 ? ? -143.74 13.66   
34 1 GLN C 156 ? ? -177.98 140.90  
35 1 GLU C 175 ? ? 86.15   12.82   
36 1 THR C 178 ? ? -72.22  -169.85 
37 1 SER C 184 ? ? -105.72 -166.11 
38 1 ARG C 227 ? ? -38.72  -36.09  
39 1 LYS C 236 ? ? -67.67  9.60    
40 1 GLN C 243 ? ? 64.68   60.91   
41 1 GLU D 13  ? ? -82.75  -70.05  
42 1 LEU D 20  ? ? -164.09 93.27   
43 1 TRP D 25  ? ? -38.34  139.33  
44 1 LYS D 48  ? ? 75.84   -55.86  
45 1 TYR D 58  ? ? -138.64 -45.48  
46 1 LYS D 61  ? ? -34.00  133.59  
47 1 LEU D 77  ? ? -143.67 -9.36   
48 1 ASN D 79  ? ? 53.28   13.64   
49 1 ILE D 171 ? ? -154.17 51.63   
50 1 GLU D 175 ? ? 65.78   -5.65   
51 1 GLU D 182 ? ? -53.06  104.25  
52 1 LYS D 191 ? ? -32.92  119.02  
53 1 GLU D 193 ? ? 85.70   -8.65   
54 1 ALA D 232 ? ? -39.73  -31.25  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   SER 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    14 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   SER 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    15 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            142.95 
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A LYS 137 ? A LYS 137 
4  1 Y 1 A GLU 138 ? A GLU 138 
5  1 Y 1 A ALA 139 ? A ALA 139 
6  1 Y 1 A GLN 140 ? A GLN 140 
7  1 Y 1 B MET 1   ? B MET 1   
8  1 Y 1 B ALA 2   ? B ALA 2   
9  1 Y 1 B THR 132 ? B THR 132 
10 1 Y 1 B SER 133 ? B SER 133 
11 1 Y 1 B ARG 134 ? B ARG 134 
12 1 Y 1 B ASN 135 ? B ASN 135 
13 1 Y 1 B VAL 136 ? B VAL 136 
14 1 Y 1 B LYS 137 ? B LYS 137 
15 1 Y 1 B GLU 138 ? B GLU 138 
16 1 Y 1 B ALA 139 ? B ALA 139 
17 1 Y 1 B GLN 140 ? B GLN 140 
18 1 Y 1 C MET 1   ? C MET 1   
19 1 Y 1 C ALA 2   ? C ALA 2   
20 1 Y 1 C THR 131 A C THR 132 
21 1 Y 1 C SER 131 B C SER 133 
22 1 Y 1 C ARG 131 C C ARG 134 
23 1 Y 1 C ASN 131 D C ASN 135 
24 1 Y 1 C VAL 131 E C VAL 136 
25 1 Y 1 C LYS 131 F C LYS 137 
26 1 Y 1 C GLU 131 G C GLU 138 
27 1 Y 1 C ALA 131 H C ALA 139 
28 1 Y 1 C GLN 131 I C GLN 140 
29 1 Y 1 C ASP 131 J C ASP 141 
30 1 Y 1 D MET 1   ? D MET 1   
31 1 Y 1 D ALA 2   ? D ALA 2   
32 1 Y 1 D GLU 3   ? D GLU 3   
33 1 Y 1 D SER 4   ? D SER 4   
34 1 Y 1 D THR 131 A D THR 132 
35 1 Y 1 D SER 131 B D SER 133 
36 1 Y 1 D ARG 131 C D ARG 134 
37 1 Y 1 D ASN 131 D D ASN 135 
38 1 Y 1 D VAL 131 E D VAL 136 
39 1 Y 1 D LYS 131 F D LYS 137 
40 1 Y 1 D GLU 131 G D GLU 138 
41 1 Y 1 D ALA 131 H D ALA 139 
42 1 Y 1 D GLN 131 I D GLN 140 
43 1 Y 1 D ASP 131 J D ASP 141 
# 
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 
6CC C13  C  Y N 1   
6CC CL1  CL N N 2   
6CC C5   C  Y N 3   
6CC C6   C  Y N 4   
6CC S7   S  N N 5   
6CC O9   O  N N 6   
6CC O10  O  N N 7   
6CC N8   N  N N 8   
6CC C2   C  Y N 9   
6CC C4   C  Y N 10  
6CC C3   C  Y N 11  
6CC C1   C  Y N 12  
6CC C12  C  Y N 13  
6CC N16  N  Y N 14  
6CC C15  C  Y N 15  
6CC N17  N  N N 16  
6CC S14  S  Y N 17  
6CC H1   H  N N 18  
6CC H2   H  N N 19  
6CC H3   H  N N 20  
6CC H4   H  N N 21  
6CC H5   H  N N 22  
6CC H6   H  N N 23  
6CC H7   H  N N 24  
6CC H8   H  N N 25  
ALA N    N  N N 26  
ALA CA   C  N S 27  
ALA C    C  N N 28  
ALA O    O  N N 29  
ALA CB   C  N N 30  
ALA OXT  O  N N 31  
ALA H    H  N N 32  
ALA H2   H  N N 33  
ALA HA   H  N N 34  
ALA HB1  H  N N 35  
ALA HB2  H  N N 36  
ALA HB3  H  N N 37  
ALA HXT  H  N N 38  
ARG N    N  N N 39  
ARG CA   C  N S 40  
ARG C    C  N N 41  
ARG O    O  N N 42  
ARG CB   C  N N 43  
ARG CG   C  N N 44  
ARG CD   C  N N 45  
ARG NE   N  N N 46  
ARG CZ   C  N N 47  
ARG NH1  N  N N 48  
ARG NH2  N  N N 49  
ARG OXT  O  N N 50  
ARG H    H  N N 51  
ARG H2   H  N N 52  
ARG HA   H  N N 53  
ARG HB2  H  N N 54  
ARG HB3  H  N N 55  
ARG HG2  H  N N 56  
ARG HG3  H  N N 57  
ARG HD2  H  N N 58  
ARG HD3  H  N N 59  
ARG HE   H  N N 60  
ARG HH11 H  N N 61  
ARG HH12 H  N N 62  
ARG HH21 H  N N 63  
ARG HH22 H  N N 64  
ARG HXT  H  N N 65  
ASN N    N  N N 66  
ASN CA   C  N S 67  
ASN C    C  N N 68  
ASN O    O  N N 69  
ASN CB   C  N N 70  
ASN CG   C  N N 71  
ASN OD1  O  N N 72  
ASN ND2  N  N N 73  
ASN OXT  O  N N 74  
ASN H    H  N N 75  
ASN H2   H  N N 76  
ASN HA   H  N N 77  
ASN HB2  H  N N 78  
ASN HB3  H  N N 79  
ASN HD21 H  N N 80  
ASN HD22 H  N N 81  
ASN HXT  H  N N 82  
ASP N    N  N N 83  
ASP CA   C  N S 84  
ASP C    C  N N 85  
ASP O    O  N N 86  
ASP CB   C  N N 87  
ASP CG   C  N N 88  
ASP OD1  O  N N 89  
ASP OD2  O  N N 90  
ASP OXT  O  N N 91  
ASP H    H  N N 92  
ASP H2   H  N N 93  
ASP HA   H  N N 94  
ASP HB2  H  N N 95  
ASP HB3  H  N N 96  
ASP HD2  H  N N 97  
ASP HXT  H  N N 98  
CYS N    N  N N 99  
CYS CA   C  N R 100 
CYS C    C  N N 101 
CYS O    O  N N 102 
CYS CB   C  N N 103 
CYS SG   S  N N 104 
CYS OXT  O  N N 105 
CYS H    H  N N 106 
CYS H2   H  N N 107 
CYS HA   H  N N 108 
CYS HB2  H  N N 109 
CYS HB3  H  N N 110 
CYS HG   H  N N 111 
CYS HXT  H  N N 112 
GLN N    N  N N 113 
GLN CA   C  N S 114 
GLN C    C  N N 115 
GLN O    O  N N 116 
GLN CB   C  N N 117 
GLN CG   C  N N 118 
GLN CD   C  N N 119 
GLN OE1  O  N N 120 
GLN NE2  N  N N 121 
GLN OXT  O  N N 122 
GLN H    H  N N 123 
GLN H2   H  N N 124 
GLN HA   H  N N 125 
GLN HB2  H  N N 126 
GLN HB3  H  N N 127 
GLN HG2  H  N N 128 
GLN HG3  H  N N 129 
GLN HE21 H  N N 130 
GLN HE22 H  N N 131 
GLN HXT  H  N N 132 
GLU N    N  N N 133 
GLU CA   C  N S 134 
GLU C    C  N N 135 
GLU O    O  N N 136 
GLU CB   C  N N 137 
GLU CG   C  N N 138 
GLU CD   C  N N 139 
GLU OE1  O  N N 140 
GLU OE2  O  N N 141 
GLU OXT  O  N N 142 
GLU H    H  N N 143 
GLU H2   H  N N 144 
GLU HA   H  N N 145 
GLU HB2  H  N N 146 
GLU HB3  H  N N 147 
GLU HG2  H  N N 148 
GLU HG3  H  N N 149 
GLU HE2  H  N N 150 
GLU HXT  H  N N 151 
GLY N    N  N N 152 
GLY CA   C  N N 153 
GLY C    C  N N 154 
GLY O    O  N N 155 
GLY OXT  O  N N 156 
GLY H    H  N N 157 
GLY H2   H  N N 158 
GLY HA2  H  N N 159 
GLY HA3  H  N N 160 
GLY HXT  H  N N 161 
HIS N    N  N N 162 
HIS CA   C  N S 163 
HIS C    C  N N 164 
HIS O    O  N N 165 
HIS CB   C  N N 166 
HIS CG   C  Y N 167 
HIS ND1  N  Y N 168 
HIS CD2  C  Y N 169 
HIS CE1  C  Y N 170 
HIS NE2  N  Y N 171 
HIS OXT  O  N N 172 
HIS H    H  N N 173 
HIS H2   H  N N 174 
HIS HA   H  N N 175 
HIS HB2  H  N N 176 
HIS HB3  H  N N 177 
HIS HD1  H  N N 178 
HIS HD2  H  N N 179 
HIS HE1  H  N N 180 
HIS HE2  H  N N 181 
HIS HXT  H  N N 182 
HOH O    O  N N 183 
HOH H1   H  N N 184 
HOH H2   H  N N 185 
ILE N    N  N N 186 
ILE CA   C  N S 187 
ILE C    C  N N 188 
ILE O    O  N N 189 
ILE CB   C  N S 190 
ILE CG1  C  N N 191 
ILE CG2  C  N N 192 
ILE CD1  C  N N 193 
ILE OXT  O  N N 194 
ILE H    H  N N 195 
ILE H2   H  N N 196 
ILE HA   H  N N 197 
ILE HB   H  N N 198 
ILE HG12 H  N N 199 
ILE HG13 H  N N 200 
ILE HG21 H  N N 201 
ILE HG22 H  N N 202 
ILE HG23 H  N N 203 
ILE HD11 H  N N 204 
ILE HD12 H  N N 205 
ILE HD13 H  N N 206 
ILE HXT  H  N N 207 
LEU N    N  N N 208 
LEU CA   C  N S 209 
LEU C    C  N N 210 
LEU O    O  N N 211 
LEU CB   C  N N 212 
LEU CG   C  N N 213 
LEU CD1  C  N N 214 
LEU CD2  C  N N 215 
LEU OXT  O  N N 216 
LEU H    H  N N 217 
LEU H2   H  N N 218 
LEU HA   H  N N 219 
LEU HB2  H  N N 220 
LEU HB3  H  N N 221 
LEU HG   H  N N 222 
LEU HD11 H  N N 223 
LEU HD12 H  N N 224 
LEU HD13 H  N N 225 
LEU HD21 H  N N 226 
LEU HD22 H  N N 227 
LEU HD23 H  N N 228 
LEU HXT  H  N N 229 
LYS N    N  N N 230 
LYS CA   C  N S 231 
LYS C    C  N N 232 
LYS O    O  N N 233 
LYS CB   C  N N 234 
LYS CG   C  N N 235 
LYS CD   C  N N 236 
LYS CE   C  N N 237 
LYS NZ   N  N N 238 
LYS OXT  O  N N 239 
LYS H    H  N N 240 
LYS H2   H  N N 241 
LYS HA   H  N N 242 
LYS HB2  H  N N 243 
LYS HB3  H  N N 244 
LYS HG2  H  N N 245 
LYS HG3  H  N N 246 
LYS HD2  H  N N 247 
LYS HD3  H  N N 248 
LYS HE2  H  N N 249 
LYS HE3  H  N N 250 
LYS HZ1  H  N N 251 
LYS HZ2  H  N N 252 
LYS HZ3  H  N N 253 
LYS HXT  H  N N 254 
MET N    N  N N 255 
MET CA   C  N S 256 
MET C    C  N N 257 
MET O    O  N N 258 
MET CB   C  N N 259 
MET CG   C  N N 260 
MET SD   S  N N 261 
MET CE   C  N N 262 
MET OXT  O  N N 263 
MET H    H  N N 264 
MET H2   H  N N 265 
MET HA   H  N N 266 
MET HB2  H  N N 267 
MET HB3  H  N N 268 
MET HG2  H  N N 269 
MET HG3  H  N N 270 
MET HE1  H  N N 271 
MET HE2  H  N N 272 
MET HE3  H  N N 273 
MET HXT  H  N N 274 
PHE N    N  N N 275 
PHE CA   C  N S 276 
PHE C    C  N N 277 
PHE O    O  N N 278 
PHE CB   C  N N 279 
PHE CG   C  Y N 280 
PHE CD1  C  Y N 281 
PHE CD2  C  Y N 282 
PHE CE1  C  Y N 283 
PHE CE2  C  Y N 284 
PHE CZ   C  Y N 285 
PHE OXT  O  N N 286 
PHE H    H  N N 287 
PHE H2   H  N N 288 
PHE HA   H  N N 289 
PHE HB2  H  N N 290 
PHE HB3  H  N N 291 
PHE HD1  H  N N 292 
PHE HD2  H  N N 293 
PHE HE1  H  N N 294 
PHE HE2  H  N N 295 
PHE HZ   H  N N 296 
PHE HXT  H  N N 297 
PRO N    N  N N 298 
PRO CA   C  N S 299 
PRO C    C  N N 300 
PRO O    O  N N 301 
PRO CB   C  N N 302 
PRO CG   C  N N 303 
PRO CD   C  N N 304 
PRO OXT  O  N N 305 
PRO H    H  N N 306 
PRO HA   H  N N 307 
PRO HB2  H  N N 308 
PRO HB3  H  N N 309 
PRO HG2  H  N N 310 
PRO HG3  H  N N 311 
PRO HD2  H  N N 312 
PRO HD3  H  N N 313 
PRO HXT  H  N N 314 
SER N    N  N N 315 
SER CA   C  N S 316 
SER C    C  N N 317 
SER O    O  N N 318 
SER CB   C  N N 319 
SER OG   O  N N 320 
SER OXT  O  N N 321 
SER H    H  N N 322 
SER H2   H  N N 323 
SER HA   H  N N 324 
SER HB2  H  N N 325 
SER HB3  H  N N 326 
SER HG   H  N N 327 
SER HXT  H  N N 328 
THR N    N  N N 329 
THR CA   C  N S 330 
THR C    C  N N 331 
THR O    O  N N 332 
THR CB   C  N R 333 
THR OG1  O  N N 334 
THR CG2  C  N N 335 
THR OXT  O  N N 336 
THR H    H  N N 337 
THR H2   H  N N 338 
THR HA   H  N N 339 
THR HB   H  N N 340 
THR HG1  H  N N 341 
THR HG21 H  N N 342 
THR HG22 H  N N 343 
THR HG23 H  N N 344 
THR HXT  H  N N 345 
TRP N    N  N N 346 
TRP CA   C  N S 347 
TRP C    C  N N 348 
TRP O    O  N N 349 
TRP CB   C  N N 350 
TRP CG   C  Y N 351 
TRP CD1  C  Y N 352 
TRP CD2  C  Y N 353 
TRP NE1  N  Y N 354 
TRP CE2  C  Y N 355 
TRP CE3  C  Y N 356 
TRP CZ2  C  Y N 357 
TRP CZ3  C  Y N 358 
TRP CH2  C  Y N 359 
TRP OXT  O  N N 360 
TRP H    H  N N 361 
TRP H2   H  N N 362 
TRP HA   H  N N 363 
TRP HB2  H  N N 364 
TRP HB3  H  N N 365 
TRP HD1  H  N N 366 
TRP HE1  H  N N 367 
TRP HE3  H  N N 368 
TRP HZ2  H  N N 369 
TRP HZ3  H  N N 370 
TRP HH2  H  N N 371 
TRP HXT  H  N N 372 
TYR N    N  N N 373 
TYR CA   C  N S 374 
TYR C    C  N N 375 
TYR O    O  N N 376 
TYR CB   C  N N 377 
TYR CG   C  Y N 378 
TYR CD1  C  Y N 379 
TYR CD2  C  Y N 380 
TYR CE1  C  Y N 381 
TYR CE2  C  Y N 382 
TYR CZ   C  Y N 383 
TYR OH   O  N N 384 
TYR OXT  O  N N 385 
TYR H    H  N N 386 
TYR H2   H  N N 387 
TYR HA   H  N N 388 
TYR HB2  H  N N 389 
TYR HB3  H  N N 390 
TYR HD1  H  N N 391 
TYR HD2  H  N N 392 
TYR HE1  H  N N 393 
TYR HE2  H  N N 394 
TYR HH   H  N N 395 
TYR HXT  H  N N 396 
VAL N    N  N N 397 
VAL CA   C  N S 398 
VAL C    C  N N 399 
VAL O    O  N N 400 
VAL CB   C  N N 401 
VAL CG1  C  N N 402 
VAL CG2  C  N N 403 
VAL OXT  O  N N 404 
VAL H    H  N N 405 
VAL H2   H  N N 406 
VAL HA   H  N N 407 
VAL HB   H  N N 408 
VAL HG11 H  N N 409 
VAL HG12 H  N N 410 
VAL HG13 H  N N 411 
VAL HG21 H  N N 412 
VAL HG22 H  N N 413 
VAL HG23 H  N N 414 
VAL HXT  H  N N 415 
ZN  ZN   ZN N N 416 
# 
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 
6CC S14 C15  sing Y N 1   
6CC S14 C13  sing Y N 2   
6CC N17 C15  sing N N 3   
6CC C15 N16  doub Y N 4   
6CC C13 C12  doub Y N 5   
6CC N16 C12  sing Y N 6   
6CC C12 C1   sing N N 7   
6CC C1  C2   doub Y N 8   
6CC C1  C3   sing Y N 9   
6CC C2  C6   sing Y N 10  
6CC C3  C4   doub Y N 11  
6CC O10 S7   doub N N 12  
6CC N8  S7   sing N N 13  
6CC C6  S7   sing N N 14  
6CC C6  C5   doub Y N 15  
6CC C4  C5   sing Y N 16  
6CC S7  O9   doub N N 17  
6CC C5  CL1  sing N N 18  
6CC C13 H1   sing N N 19  
6CC N8  H2   sing N N 20  
6CC N8  H3   sing N N 21  
6CC C2  H4   sing N N 22  
6CC C4  H5   sing N N 23  
6CC C3  H6   sing N N 24  
6CC N17 H7   sing N N 25  
6CC N17 H8   sing N N 26  
ALA N   CA   sing N N 27  
ALA N   H    sing N N 28  
ALA N   H2   sing N N 29  
ALA CA  C    sing N N 30  
ALA CA  CB   sing N N 31  
ALA CA  HA   sing N N 32  
ALA C   O    doub N N 33  
ALA C   OXT  sing N N 34  
ALA CB  HB1  sing N N 35  
ALA CB  HB2  sing N N 36  
ALA CB  HB3  sing N N 37  
ALA OXT HXT  sing N N 38  
ARG N   CA   sing N N 39  
ARG N   H    sing N N 40  
ARG N   H2   sing N N 41  
ARG CA  C    sing N N 42  
ARG CA  CB   sing N N 43  
ARG CA  HA   sing N N 44  
ARG C   O    doub N N 45  
ARG C   OXT  sing N N 46  
ARG CB  CG   sing N N 47  
ARG CB  HB2  sing N N 48  
ARG CB  HB3  sing N N 49  
ARG CG  CD   sing N N 50  
ARG CG  HG2  sing N N 51  
ARG CG  HG3  sing N N 52  
ARG CD  NE   sing N N 53  
ARG CD  HD2  sing N N 54  
ARG CD  HD3  sing N N 55  
ARG NE  CZ   sing N N 56  
ARG NE  HE   sing N N 57  
ARG CZ  NH1  sing N N 58  
ARG CZ  NH2  doub N N 59  
ARG NH1 HH11 sing N N 60  
ARG NH1 HH12 sing N N 61  
ARG NH2 HH21 sing N N 62  
ARG NH2 HH22 sing N N 63  
ARG OXT HXT  sing N N 64  
ASN N   CA   sing N N 65  
ASN N   H    sing N N 66  
ASN N   H2   sing N N 67  
ASN CA  C    sing N N 68  
ASN CA  CB   sing N N 69  
ASN CA  HA   sing N N 70  
ASN C   O    doub N N 71  
ASN C   OXT  sing N N 72  
ASN CB  CG   sing N N 73  
ASN CB  HB2  sing N N 74  
ASN CB  HB3  sing N N 75  
ASN CG  OD1  doub N N 76  
ASN CG  ND2  sing N N 77  
ASN ND2 HD21 sing N N 78  
ASN ND2 HD22 sing N N 79  
ASN OXT HXT  sing N N 80  
ASP N   CA   sing N N 81  
ASP N   H    sing N N 82  
ASP N   H2   sing N N 83  
ASP CA  C    sing N N 84  
ASP CA  CB   sing N N 85  
ASP CA  HA   sing N N 86  
ASP C   O    doub N N 87  
ASP C   OXT  sing N N 88  
ASP CB  CG   sing N N 89  
ASP CB  HB2  sing N N 90  
ASP CB  HB3  sing N N 91  
ASP CG  OD1  doub N N 92  
ASP CG  OD2  sing N N 93  
ASP OD2 HD2  sing N N 94  
ASP OXT HXT  sing N N 95  
CYS N   CA   sing N N 96  
CYS N   H    sing N N 97  
CYS N   H2   sing N N 98  
CYS CA  C    sing N N 99  
CYS CA  CB   sing N N 100 
CYS CA  HA   sing N N 101 
CYS C   O    doub N N 102 
CYS C   OXT  sing N N 103 
CYS CB  SG   sing N N 104 
CYS CB  HB2  sing N N 105 
CYS CB  HB3  sing N N 106 
CYS SG  HG   sing N N 107 
CYS OXT HXT  sing N N 108 
GLN N   CA   sing N N 109 
GLN N   H    sing N N 110 
GLN N   H2   sing N N 111 
GLN CA  C    sing N N 112 
GLN CA  CB   sing N N 113 
GLN CA  HA   sing N N 114 
GLN C   O    doub N N 115 
GLN C   OXT  sing N N 116 
GLN CB  CG   sing N N 117 
GLN CB  HB2  sing N N 118 
GLN CB  HB3  sing N N 119 
GLN CG  CD   sing N N 120 
GLN CG  HG2  sing N N 121 
GLN CG  HG3  sing N N 122 
GLN CD  OE1  doub N N 123 
GLN CD  NE2  sing N N 124 
GLN NE2 HE21 sing N N 125 
GLN NE2 HE22 sing N N 126 
GLN OXT HXT  sing N N 127 
GLU N   CA   sing N N 128 
GLU N   H    sing N N 129 
GLU N   H2   sing N N 130 
GLU CA  C    sing N N 131 
GLU CA  CB   sing N N 132 
GLU CA  HA   sing N N 133 
GLU C   O    doub N N 134 
GLU C   OXT  sing N N 135 
GLU CB  CG   sing N N 136 
GLU CB  HB2  sing N N 137 
GLU CB  HB3  sing N N 138 
GLU CG  CD   sing N N 139 
GLU CG  HG2  sing N N 140 
GLU CG  HG3  sing N N 141 
GLU CD  OE1  doub N N 142 
GLU CD  OE2  sing N N 143 
GLU OE2 HE2  sing N N 144 
GLU OXT HXT  sing N N 145 
GLY N   CA   sing N N 146 
GLY N   H    sing N N 147 
GLY N   H2   sing N N 148 
GLY CA  C    sing N N 149 
GLY CA  HA2  sing N N 150 
GLY CA  HA3  sing N N 151 
GLY C   O    doub N N 152 
GLY C   OXT  sing N N 153 
GLY OXT HXT  sing N N 154 
HIS N   CA   sing N N 155 
HIS N   H    sing N N 156 
HIS N   H2   sing N N 157 
HIS CA  C    sing N N 158 
HIS CA  CB   sing N N 159 
HIS CA  HA   sing N N 160 
HIS C   O    doub N N 161 
HIS C   OXT  sing N N 162 
HIS CB  CG   sing N N 163 
HIS CB  HB2  sing N N 164 
HIS CB  HB3  sing N N 165 
HIS CG  ND1  sing Y N 166 
HIS CG  CD2  doub Y N 167 
HIS ND1 CE1  doub Y N 168 
HIS ND1 HD1  sing N N 169 
HIS CD2 NE2  sing Y N 170 
HIS CD2 HD2  sing N N 171 
HIS CE1 NE2  sing Y N 172 
HIS CE1 HE1  sing N N 173 
HIS NE2 HE2  sing N N 174 
HIS OXT HXT  sing N N 175 
HOH O   H1   sing N N 176 
HOH O   H2   sing N N 177 
ILE N   CA   sing N N 178 
ILE N   H    sing N N 179 
ILE N   H2   sing N N 180 
ILE CA  C    sing N N 181 
ILE CA  CB   sing N N 182 
ILE CA  HA   sing N N 183 
ILE C   O    doub N N 184 
ILE C   OXT  sing N N 185 
ILE CB  CG1  sing N N 186 
ILE CB  CG2  sing N N 187 
ILE CB  HB   sing N N 188 
ILE CG1 CD1  sing N N 189 
ILE CG1 HG12 sing N N 190 
ILE CG1 HG13 sing N N 191 
ILE CG2 HG21 sing N N 192 
ILE CG2 HG22 sing N N 193 
ILE CG2 HG23 sing N N 194 
ILE CD1 HD11 sing N N 195 
ILE CD1 HD12 sing N N 196 
ILE CD1 HD13 sing N N 197 
ILE OXT HXT  sing N N 198 
LEU N   CA   sing N N 199 
LEU N   H    sing N N 200 
LEU N   H2   sing N N 201 
LEU CA  C    sing N N 202 
LEU CA  CB   sing N N 203 
LEU CA  HA   sing N N 204 
LEU C   O    doub N N 205 
LEU C   OXT  sing N N 206 
LEU CB  CG   sing N N 207 
LEU CB  HB2  sing N N 208 
LEU CB  HB3  sing N N 209 
LEU CG  CD1  sing N N 210 
LEU CG  CD2  sing N N 211 
LEU CG  HG   sing N N 212 
LEU CD1 HD11 sing N N 213 
LEU CD1 HD12 sing N N 214 
LEU CD1 HD13 sing N N 215 
LEU CD2 HD21 sing N N 216 
LEU CD2 HD22 sing N N 217 
LEU CD2 HD23 sing N N 218 
LEU OXT HXT  sing N N 219 
LYS N   CA   sing N N 220 
LYS N   H    sing N N 221 
LYS N   H2   sing N N 222 
LYS CA  C    sing N N 223 
LYS CA  CB   sing N N 224 
LYS CA  HA   sing N N 225 
LYS C   O    doub N N 226 
LYS C   OXT  sing N N 227 
LYS CB  CG   sing N N 228 
LYS CB  HB2  sing N N 229 
LYS CB  HB3  sing N N 230 
LYS CG  CD   sing N N 231 
LYS CG  HG2  sing N N 232 
LYS CG  HG3  sing N N 233 
LYS CD  CE   sing N N 234 
LYS CD  HD2  sing N N 235 
LYS CD  HD3  sing N N 236 
LYS CE  NZ   sing N N 237 
LYS CE  HE2  sing N N 238 
LYS CE  HE3  sing N N 239 
LYS NZ  HZ1  sing N N 240 
LYS NZ  HZ2  sing N N 241 
LYS NZ  HZ3  sing N N 242 
LYS OXT HXT  sing N N 243 
MET N   CA   sing N N 244 
MET N   H    sing N N 245 
MET N   H2   sing N N 246 
MET CA  C    sing N N 247 
MET CA  CB   sing N N 248 
MET CA  HA   sing N N 249 
MET C   O    doub N N 250 
MET C   OXT  sing N N 251 
MET CB  CG   sing N N 252 
MET CB  HB2  sing N N 253 
MET CB  HB3  sing N N 254 
MET CG  SD   sing N N 255 
MET CG  HG2  sing N N 256 
MET CG  HG3  sing N N 257 
MET SD  CE   sing N N 258 
MET CE  HE1  sing N N 259 
MET CE  HE2  sing N N 260 
MET CE  HE3  sing N N 261 
MET OXT HXT  sing N N 262 
PHE N   CA   sing N N 263 
PHE N   H    sing N N 264 
PHE N   H2   sing N N 265 
PHE CA  C    sing N N 266 
PHE CA  CB   sing N N 267 
PHE CA  HA   sing N N 268 
PHE C   O    doub N N 269 
PHE C   OXT  sing N N 270 
PHE CB  CG   sing N N 271 
PHE CB  HB2  sing N N 272 
PHE CB  HB3  sing N N 273 
PHE CG  CD1  doub Y N 274 
PHE CG  CD2  sing Y N 275 
PHE CD1 CE1  sing Y N 276 
PHE CD1 HD1  sing N N 277 
PHE CD2 CE2  doub Y N 278 
PHE CD2 HD2  sing N N 279 
PHE CE1 CZ   doub Y N 280 
PHE CE1 HE1  sing N N 281 
PHE CE2 CZ   sing Y N 282 
PHE CE2 HE2  sing N N 283 
PHE CZ  HZ   sing N N 284 
PHE OXT HXT  sing N N 285 
PRO N   CA   sing N N 286 
PRO N   CD   sing N N 287 
PRO N   H    sing N N 288 
PRO CA  C    sing N N 289 
PRO CA  CB   sing N N 290 
PRO CA  HA   sing N N 291 
PRO C   O    doub N N 292 
PRO C   OXT  sing N N 293 
PRO CB  CG   sing N N 294 
PRO CB  HB2  sing N N 295 
PRO CB  HB3  sing N N 296 
PRO CG  CD   sing N N 297 
PRO CG  HG2  sing N N 298 
PRO CG  HG3  sing N N 299 
PRO CD  HD2  sing N N 300 
PRO CD  HD3  sing N N 301 
PRO OXT HXT  sing N N 302 
SER N   CA   sing N N 303 
SER N   H    sing N N 304 
SER N   H2   sing N N 305 
SER CA  C    sing N N 306 
SER CA  CB   sing N N 307 
SER CA  HA   sing N N 308 
SER C   O    doub N N 309 
SER C   OXT  sing N N 310 
SER CB  OG   sing N N 311 
SER CB  HB2  sing N N 312 
SER CB  HB3  sing N N 313 
SER OG  HG   sing N N 314 
SER OXT HXT  sing N N 315 
THR N   CA   sing N N 316 
THR N   H    sing N N 317 
THR N   H2   sing N N 318 
THR CA  C    sing N N 319 
THR CA  CB   sing N N 320 
THR CA  HA   sing N N 321 
THR C   O    doub N N 322 
THR C   OXT  sing N N 323 
THR CB  OG1  sing N N 324 
THR CB  CG2  sing N N 325 
THR CB  HB   sing N N 326 
THR OG1 HG1  sing N N 327 
THR CG2 HG21 sing N N 328 
THR CG2 HG22 sing N N 329 
THR CG2 HG23 sing N N 330 
THR OXT HXT  sing N N 331 
TRP N   CA   sing N N 332 
TRP N   H    sing N N 333 
TRP N   H2   sing N N 334 
TRP CA  C    sing N N 335 
TRP CA  CB   sing N N 336 
TRP CA  HA   sing N N 337 
TRP C   O    doub N N 338 
TRP C   OXT  sing N N 339 
TRP CB  CG   sing N N 340 
TRP CB  HB2  sing N N 341 
TRP CB  HB3  sing N N 342 
TRP CG  CD1  doub Y N 343 
TRP CG  CD2  sing Y N 344 
TRP CD1 NE1  sing Y N 345 
TRP CD1 HD1  sing N N 346 
TRP CD2 CE2  doub Y N 347 
TRP CD2 CE3  sing Y N 348 
TRP NE1 CE2  sing Y N 349 
TRP NE1 HE1  sing N N 350 
TRP CE2 CZ2  sing Y N 351 
TRP CE3 CZ3  doub Y N 352 
TRP CE3 HE3  sing N N 353 
TRP CZ2 CH2  doub Y N 354 
TRP CZ2 HZ2  sing N N 355 
TRP CZ3 CH2  sing Y N 356 
TRP CZ3 HZ3  sing N N 357 
TRP CH2 HH2  sing N N 358 
TRP OXT HXT  sing N N 359 
TYR N   CA   sing N N 360 
TYR N   H    sing N N 361 
TYR N   H2   sing N N 362 
TYR CA  C    sing N N 363 
TYR CA  CB   sing N N 364 
TYR CA  HA   sing N N 365 
TYR C   O    doub N N 366 
TYR C   OXT  sing N N 367 
TYR CB  CG   sing N N 368 
TYR CB  HB2  sing N N 369 
TYR CB  HB3  sing N N 370 
TYR CG  CD1  doub Y N 371 
TYR CG  CD2  sing Y N 372 
TYR CD1 CE1  sing Y N 373 
TYR CD1 HD1  sing N N 374 
TYR CD2 CE2  doub Y N 375 
TYR CD2 HD2  sing N N 376 
TYR CE1 CZ   doub Y N 377 
TYR CE1 HE1  sing N N 378 
TYR CE2 CZ   sing Y N 379 
TYR CE2 HE2  sing N N 380 
TYR CZ  OH   sing N N 381 
TYR OH  HH   sing N N 382 
TYR OXT HXT  sing N N 383 
VAL N   CA   sing N N 384 
VAL N   H    sing N N 385 
VAL N   H2   sing N N 386 
VAL CA  C    sing N N 387 
VAL CA  CB   sing N N 388 
VAL CA  HA   sing N N 389 
VAL C   O    doub N N 390 
VAL C   OXT  sing N N 391 
VAL CB  CG1  sing N N 392 
VAL CB  CG2  sing N N 393 
VAL CB  HB   sing N N 394 
VAL CG1 HG11 sing N N 395 
VAL CG1 HG12 sing N N 396 
VAL CG1 HG13 sing N N 397 
VAL CG2 HG21 sing N N 398 
VAL CG2 HG22 sing N N 399 
VAL CG2 HG23 sing N N 400 
VAL OXT HXT  sing N N 401 
# 
_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   3F7B 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    5IPZ 
_atom_sites.fract_transf_matrix[1][1]   0.020537 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.010617 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.003900 
_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]   0.023186 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLU A 1 3   ? -4.968  10.316  -11.580 1.00 88.41  ? 3   GLU A N   1 
ATOM   2    C  CA  . GLU A 1 3   ? -4.540  11.326  -10.573 1.00 90.37  ? 3   GLU A CA  1 
ATOM   3    C  C   . GLU A 1 3   ? -5.593  11.514  -9.489  1.00 92.95  ? 3   GLU A C   1 
ATOM   4    O  O   . GLU A 1 3   ? -6.196  12.590  -9.363  1.00 99.41  ? 3   GLU A O   1 
ATOM   5    C  CB  . GLU A 1 3   ? -4.214  12.653  -11.256 1.00 95.62  ? 3   GLU A CB  1 
ATOM   6    C  CG  . GLU A 1 3   ? -2.780  12.729  -11.752 1.00 99.44  ? 3   GLU A CG  1 
ATOM   7    C  CD  . GLU A 1 3   ? -2.630  13.606  -12.974 1.00 100.37 ? 3   GLU A CD  1 
ATOM   8    O  OE1 . GLU A 1 3   ? -2.012  13.143  -13.955 1.00 97.57  ? 3   GLU A OE1 1 
ATOM   9    O  OE2 . GLU A 1 3   ? -3.137  14.748  -12.958 1.00 107.59 ? 3   GLU A OE2 1 
ATOM   10   N  N   . SER A 1 4   ? -5.804  10.450  -8.709  1.00 89.75  ? 4   SER A N   1 
ATOM   11   C  CA  . SER A 1 4   ? -6.803  10.436  -7.632  1.00 79.50  ? 4   SER A CA  1 
ATOM   12   C  C   . SER A 1 4   ? -6.417  9.462   -6.497  1.00 68.75  ? 4   SER A C   1 
ATOM   13   O  O   . SER A 1 4   ? -5.240  9.163   -6.272  1.00 59.60  ? 4   SER A O   1 
ATOM   14   C  CB  . SER A 1 4   ? -8.182  10.034  -8.186  1.00 78.81  ? 4   SER A CB  1 
ATOM   15   O  OG  . SER A 1 4   ? -8.163  8.729   -8.748  1.00 76.12  ? 4   SER A OG  1 
ATOM   16   N  N   . HIS A 1 5   ? -7.434  9.019   -5.755  1.00 63.95  ? 5   HIS A N   1 
ATOM   17   C  CA  . HIS A 1 5   ? -7.242  8.251   -4.542  1.00 59.79  ? 5   HIS A CA  1 
ATOM   18   C  C   . HIS A 1 5   ? -6.440  6.984   -4.711  1.00 54.58  ? 5   HIS A C   1 
ATOM   19   O  O   . HIS A 1 5   ? -6.261  6.492   -5.834  1.00 63.72  ? 5   HIS A O   1 
ATOM   20   C  CB  . HIS A 1 5   ? -8.619  7.955   -3.955  1.00 65.43  ? 5   HIS A CB  1 
ATOM   21   C  CG  . HIS A 1 5   ? -8.688  8.072   -2.449  1.00 71.37  ? 5   HIS A CG  1 
ATOM   22   N  ND1 . HIS A 1 5   ? -7.731  8.694   -1.718  1.00 69.62  ? 5   HIS A ND1 1 
ATOM   23   C  CD2 . HIS A 1 5   ? -9.666  7.654   -1.547  1.00 67.63  ? 5   HIS A CD2 1 
ATOM   24   C  CE1 . HIS A 1 5   ? -8.076  8.665   -0.418  1.00 72.95  ? 5   HIS A CE1 1 
ATOM   25   N  NE2 . HIS A 1 5   ? -9.263  8.026   -0.315  1.00 75.25  ? 5   HIS A NE2 1 
ATOM   26   N  N   . TRP A 1 6   ? -5.928  6.460   -3.604  1.00 40.49  ? 6   TRP A N   1 
ATOM   27   C  CA  . TRP A 1 6   ? -5.382  5.112   -3.549  1.00 35.37  ? 6   TRP A CA  1 
ATOM   28   C  C   . TRP A 1 6   ? -6.360  4.233   -2.806  1.00 30.90  ? 6   TRP A C   1 
ATOM   29   O  O   . TRP A 1 6   ? -7.206  4.723   -2.083  1.00 29.39  ? 6   TRP A O   1 
ATOM   30   C  CB  . TRP A 1 6   ? -4.035  5.066   -2.886  1.00 33.36  ? 6   TRP A CB  1 
ATOM   31   C  CG  . TRP A 1 6   ? -4.032  5.599   -1.460  1.00 40.46  ? 6   TRP A CG  1 
ATOM   32   C  CD1 . TRP A 1 6   ? -3.803  6.908   -1.031  1.00 40.25  ? 6   TRP A CD1 1 
ATOM   33   C  CD2 . TRP A 1 6   ? -4.272  4.831   -0.219  1.00 34.70  ? 6   TRP A CD2 1 
ATOM   34   N  NE1 . TRP A 1 6   ? -3.884  6.996   0.344   1.00 34.79  ? 6   TRP A NE1 1 
ATOM   35   C  CE2 . TRP A 1 6   ? -4.159  5.784   0.888   1.00 38.27  ? 6   TRP A CE2 1 
ATOM   36   C  CE3 . TRP A 1 6   ? -4.551  3.490   0.068   1.00 35.86  ? 6   TRP A CE3 1 
ATOM   37   C  CZ2 . TRP A 1 6   ? -4.323  5.393   2.213   1.00 38.28  ? 6   TRP A CZ2 1 
ATOM   38   C  CZ3 . TRP A 1 6   ? -4.715  3.115   1.405   1.00 37.70  ? 6   TRP A CZ3 1 
ATOM   39   C  CH2 . TRP A 1 6   ? -4.602  4.042   2.450   1.00 38.36  ? 6   TRP A CH2 1 
ATOM   40   N  N   . CYS A 1 7   ? -6.236  2.925   -2.940  1.00 29.15  ? 7   CYS A N   1 
ATOM   41   C  CA  . CYS A 1 7   ? -7.156  2.041   -2.247  1.00 33.47  ? 7   CYS A CA  1 
ATOM   42   C  C   . CYS A 1 7   ? -6.470  0.713   -1.943  1.00 30.25  ? 7   CYS A C   1 
ATOM   43   O  O   . CYS A 1 7   ? -5.281  0.548   -2.290  1.00 23.20  ? 7   CYS A O   1 
ATOM   44   C  CB  . CYS A 1 7   ? -8.484  1.890   -3.021  1.00 34.96  ? 7   CYS A CB  1 
ATOM   45   S  SG  . CYS A 1 7   ? -8.244  1.051   -4.589  1.00 52.50  ? 7   CYS A SG  1 
ATOM   46   N  N   . TYR A 1 8   ? -7.176  -0.163  -1.207  1.00 31.15  ? 8   TYR A N   1 
ATOM   47   C  CA  . TYR A 1 8   ? -6.667  -1.490  -0.798  1.00 32.79  ? 8   TYR A CA  1 
ATOM   48   C  C   . TYR A 1 8   ? -7.192  -2.474  -1.829  1.00 35.77  ? 8   TYR A C   1 
ATOM   49   O  O   . TYR A 1 8   ? -8.169  -2.173  -2.520  1.00 36.89  ? 8   TYR A O   1 
ATOM   50   C  CB  . TYR A 1 8   ? -7.153  -1.881  0.632   1.00 30.85  ? 8   TYR A CB  1 
ATOM   51   C  CG  . TYR A 1 8   ? -6.335  -1.198  1.734   1.00 30.58  ? 8   TYR A CG  1 
ATOM   52   C  CD1 . TYR A 1 8   ? -4.991  -1.511  1.909   1.00 29.80  ? 8   TYR A CD1 1 
ATOM   53   C  CD2 . TYR A 1 8   ? -6.887  -0.196  2.537   1.00 27.19  ? 8   TYR A CD2 1 
ATOM   54   C  CE1 . TYR A 1 8   ? -4.223  -0.876  2.877   1.00 28.14  ? 8   TYR A CE1 1 
ATOM   55   C  CE2 . TYR A 1 8   ? -6.121  0.449   3.519   1.00 28.77  ? 8   TYR A CE2 1 
ATOM   56   C  CZ  . TYR A 1 8   ? -4.783  0.104   3.672   1.00 29.51  ? 8   TYR A CZ  1 
ATOM   57   O  OH  . TYR A 1 8   ? -3.988  0.712   4.626   1.00 25.64  ? 8   TYR A OH  1 
ATOM   58   N  N   . GLU A 1 9   ? -6.595  -3.655  -1.929  1.00 39.58  ? 9   GLU A N   1 
ATOM   59   C  CA  . GLU A 1 9   ? -6.991  -4.570  -3.005  1.00 45.33  ? 9   GLU A CA  1 
ATOM   60   C  C   . GLU A 1 9   ? -8.496  -4.799  -3.025  1.00 46.28  ? 9   GLU A C   1 
ATOM   61   O  O   . GLU A 1 9   ? -9.132  -4.641  -4.048  1.00 50.48  ? 9   GLU A O   1 
ATOM   62   C  CB  . GLU A 1 9   ? -6.215  -5.901  -2.945  1.00 48.28  ? 9   GLU A CB  1 
ATOM   63   C  CG  . GLU A 1 9   ? -6.618  -6.912  -4.013  1.00 57.80  ? 9   GLU A CG  1 
ATOM   64   C  CD  . GLU A 1 9   ? -6.463  -6.379  -5.438  1.00 67.70  ? 9   GLU A CD  1 
ATOM   65   O  OE1 . GLU A 1 9   ? -5.461  -5.681  -5.733  1.00 74.25  ? 9   GLU A OE1 1 
ATOM   66   O  OE2 . GLU A 1 9   ? -7.348  -6.657  -6.276  1.00 68.11  ? 9   GLU A OE2 1 
ATOM   67   N  N   . VAL A 1 10  ? -9.057  -5.161  -1.877  1.00 52.05  ? 10  VAL A N   1 
ATOM   68   C  CA  . VAL A 1 10  ? -10.472 -5.507  -1.751  1.00 51.26  ? 10  VAL A CA  1 
ATOM   69   C  C   . VAL A 1 10  ? -11.392 -4.397  -2.239  1.00 54.30  ? 10  VAL A C   1 
ATOM   70   O  O   . VAL A 1 10  ? -12.487 -4.641  -2.736  1.00 61.29  ? 10  VAL A O   1 
ATOM   71   C  CB  . VAL A 1 10  ? -10.811 -5.862  -0.267  1.00 54.56  ? 10  VAL A CB  1 
ATOM   72   C  CG1 . VAL A 1 10  ? -10.922 -4.605  0.623   1.00 43.80  ? 10  VAL A CG1 1 
ATOM   73   C  CG2 . VAL A 1 10  ? -12.069 -6.716  -0.184  1.00 53.64  ? 10  VAL A CG2 1 
ATOM   74   N  N   . GLN A 1 11  ? -10.936 -3.163  -2.091  1.00 59.63  ? 11  GLN A N   1 
ATOM   75   C  CA  . GLN A 1 11  ? -11.826 -2.016  -2.129  1.00 60.03  ? 11  GLN A CA  1 
ATOM   76   C  C   . GLN A 1 11  ? -11.855 -1.377  -3.514  1.00 65.61  ? 11  GLN A C   1 
ATOM   77   O  O   . GLN A 1 11  ? -12.523 -0.369  -3.715  1.00 67.82  ? 11  GLN A O   1 
ATOM   78   C  CB  . GLN A 1 11  ? -11.382 -1.031  -1.039  1.00 59.29  ? 11  GLN A CB  1 
ATOM   79   C  CG  . GLN A 1 11  ? -12.196 0.246   -0.893  1.00 54.78  ? 11  GLN A CG  1 
ATOM   80   C  CD  . GLN A 1 11  ? -11.354 1.389   -0.379  1.00 50.66  ? 11  GLN A CD  1 
ATOM   81   O  OE1 . GLN A 1 11  ? -10.135 1.267   -0.228  1.00 49.69  ? 11  GLN A OE1 1 
ATOM   82   N  NE2 . GLN A 1 11  ? -11.995 2.521   -0.117  1.00 59.97  ? 11  GLN A NE2 1 
ATOM   83   N  N   . ALA A 1 12  ? -11.152 -1.992  -4.471  1.00 72.73  ? 12  ALA A N   1 
ATOM   84   C  CA  . ALA A 1 12  ? -11.064 -1.490  -5.851  1.00 76.35  ? 12  ALA A CA  1 
ATOM   85   C  C   . ALA A 1 12  ? -12.280 -1.849  -6.709  1.00 79.99  ? 12  ALA A C   1 
ATOM   86   O  O   . ALA A 1 12  ? -12.743 -1.042  -7.521  1.00 82.21  ? 12  ALA A O   1 
ATOM   87   C  CB  . ALA A 1 12  ? -9.794  -1.992  -6.520  1.00 76.40  ? 12  ALA A CB  1 
ATOM   88   N  N   . GLU A 1 13  ? -12.783 -3.064  -6.537  1.00 75.33  ? 13  GLU A N   1 
ATOM   89   C  CA  . GLU A 1 13  ? -13.943 -3.519  -7.291  1.00 78.35  ? 13  GLU A CA  1 
ATOM   90   C  C   . GLU A 1 13  ? -15.302 -3.035  -6.742  1.00 80.14  ? 13  GLU A C   1 
ATOM   91   O  O   . GLU A 1 13  ? -16.346 -3.462  -7.245  1.00 82.99  ? 13  GLU A O   1 
ATOM   92   C  CB  . GLU A 1 13  ? -13.924 -5.043  -7.410  1.00 81.33  ? 13  GLU A CB  1 
ATOM   93   C  CG  . GLU A 1 13  ? -13.609 -5.761  -6.113  1.00 79.12  ? 13  GLU A CG  1 
ATOM   94   C  CD  . GLU A 1 13  ? -14.410 -7.031  -5.970  1.00 84.71  ? 13  GLU A CD  1 
ATOM   95   O  OE1 . GLU A 1 13  ? -15.650 -6.932  -5.843  1.00 83.32  ? 13  GLU A OE1 1 
ATOM   96   O  OE2 . GLU A 1 13  ? -13.803 -8.122  -5.982  1.00 85.87  ? 13  GLU A OE2 1 
ATOM   97   N  N   . SER A 1 14  ? -15.292 -2.144  -5.745  1.00 70.99  ? 14  SER A N   1 
ATOM   98   C  CA  . SER A 1 14  ? -16.524 -1.733  -5.052  1.00 66.57  ? 14  SER A CA  1 
ATOM   99   C  C   . SER A 1 14  ? -16.731 -0.221  -5.043  1.00 65.97  ? 14  SER A C   1 
ATOM   100  O  O   . SER A 1 14  ? -17.828 0.262   -4.735  1.00 67.12  ? 14  SER A O   1 
ATOM   101  C  CB  . SER A 1 14  ? -16.511 -2.224  -3.606  1.00 61.48  ? 14  SER A CB  1 
ATOM   102  O  OG  . SER A 1 14  ? -15.922 -3.498  -3.513  1.00 63.68  ? 14  SER A OG  1 
ATOM   103  N  N   . SER A 1 15  ? -15.675 0.515   -5.371  1.00 59.38  ? 15  SER A N   1 
ATOM   104  C  CA  . SER A 1 15  ? -15.681 1.962   -5.289  1.00 62.61  ? 15  SER A CA  1 
ATOM   105  C  C   . SER A 1 15  ? -16.028 2.585   -6.635  1.00 66.41  ? 15  SER A C   1 
ATOM   106  O  O   . SER A 1 15  ? -16.003 1.901   -7.660  1.00 63.41  ? 15  SER A O   1 
ATOM   107  C  CB  . SER A 1 15  ? -14.311 2.448   -4.860  1.00 61.54  ? 15  SER A CB  1 
ATOM   108  O  OG  . SER A 1 15  ? -13.437 2.469   -5.964  1.00 61.92  ? 15  SER A OG  1 
ATOM   109  N  N   . ASN A 1 16  ? -16.317 3.888   -6.637  1.00 69.05  ? 16  ASN A N   1 
ATOM   110  C  CA  . ASN A 1 16  ? -16.726 4.580   -7.869  1.00 69.31  ? 16  ASN A CA  1 
ATOM   111  C  C   . ASN A 1 16  ? -15.739 5.596   -8.431  1.00 71.53  ? 16  ASN A C   1 
ATOM   112  O  O   . ASN A 1 16  ? -15.801 5.924   -9.611  1.00 80.16  ? 16  ASN A O   1 
ATOM   113  C  CB  . ASN A 1 16  ? -18.107 5.208   -7.704  1.00 67.19  ? 16  ASN A CB  1 
ATOM   114  C  CG  . ASN A 1 16  ? -19.023 4.368   -6.837  1.00 66.57  ? 16  ASN A CG  1 
ATOM   115  O  OD1 . ASN A 1 16  ? -19.037 3.134   -6.933  1.00 59.88  ? 16  ASN A OD1 1 
ATOM   116  N  ND2 . ASN A 1 16  ? -19.785 5.031   -5.976  1.00 57.64  ? 16  ASN A ND2 1 
ATOM   117  N  N   . TYR A 1 17  ? -14.854 6.128   -7.598  1.00 72.00  ? 17  TYR A N   1 
ATOM   118  C  CA  . TYR A 1 17  ? -13.730 6.905   -8.110  1.00 67.66  ? 17  TYR A CA  1 
ATOM   119  C  C   . TYR A 1 17  ? -12.788 5.807   -8.598  1.00 59.97  ? 17  TYR A C   1 
ATOM   120  O  O   . TYR A 1 17  ? -12.806 4.709   -8.032  1.00 58.12  ? 17  TYR A O   1 
ATOM   121  C  CB  . TYR A 1 17  ? -13.058 7.702   -6.977  1.00 77.63  ? 17  TYR A CB  1 
ATOM   122  C  CG  . TYR A 1 17  ? -12.865 9.221   -7.176  1.00 89.42  ? 17  TYR A CG  1 
ATOM   123  C  CD1 . TYR A 1 17  ? -12.542 9.780   -8.428  1.00 88.49  ? 17  TYR A CD1 1 
ATOM   124  C  CD2 . TYR A 1 17  ? -12.969 10.092  -6.082  1.00 93.27  ? 17  TYR A CD2 1 
ATOM   125  C  CE1 . TYR A 1 17  ? -12.366 11.157  -8.577  1.00 88.71  ? 17  TYR A CE1 1 
ATOM   126  C  CE2 . TYR A 1 17  ? -12.793 11.464  -6.225  1.00 92.69  ? 17  TYR A CE2 1 
ATOM   127  C  CZ  . TYR A 1 17  ? -12.489 11.997  -7.465  1.00 89.57  ? 17  TYR A CZ  1 
ATOM   128  O  OH  . TYR A 1 17  ? -12.307 13.364  -7.573  1.00 80.19  ? 17  TYR A OH  1 
ATOM   129  N  N   . PRO A 1 18  ? -12.011 6.064   -9.670  1.00 49.29  ? 18  PRO A N   1 
ATOM   130  C  CA  . PRO A 1 18  ? -10.851 5.225   -10.006 1.00 46.59  ? 18  PRO A CA  1 
ATOM   131  C  C   . PRO A 1 18  ? -9.786  5.243   -8.895  1.00 46.07  ? 18  PRO A C   1 
ATOM   132  O  O   . PRO A 1 18  ? -9.567  6.281   -8.265  1.00 42.39  ? 18  PRO A O   1 
ATOM   133  C  CB  . PRO A 1 18  ? -10.289 5.882   -11.279 1.00 42.55  ? 18  PRO A CB  1 
ATOM   134  C  CG  . PRO A 1 18  ? -11.456 6.579   -11.869 1.00 46.65  ? 18  PRO A CG  1 
ATOM   135  C  CD  . PRO A 1 18  ? -12.313 7.042   -10.726 1.00 45.46  ? 18  PRO A CD  1 
ATOM   136  N  N   . CYS A 1 19  ? -9.130  4.107   -8.649  1.00 46.33  ? 19  CYS A N   1 
ATOM   137  C  CA  . CYS A 1 19  ? -8.053  4.061   -7.634  1.00 45.46  ? 19  CYS A CA  1 
ATOM   138  C  C   . CYS A 1 19  ? -6.897  3.085   -7.891  1.00 41.88  ? 19  CYS A C   1 
ATOM   139  O  O   . CYS A 1 19  ? -7.042  2.051   -8.536  1.00 44.19  ? 19  CYS A O   1 
ATOM   140  C  CB  . CYS A 1 19  ? -8.611  3.903   -6.209  1.00 44.41  ? 19  CYS A CB  1 
ATOM   141  S  SG  . CYS A 1 19  ? -9.576  2.396   -5.977  1.00 54.01  ? 19  CYS A SG  1 
ATOM   142  N  N   . LEU A 1 20  ? -5.741  3.459   -7.370  1.00 43.10  ? 20  LEU A N   1 
ATOM   143  C  CA  . LEU A 1 20  ? -4.537  2.641   -7.422  1.00 38.72  ? 20  LEU A CA  1 
ATOM   144  C  C   . LEU A 1 20  ? -4.597  1.546   -6.374  1.00 37.60  ? 20  LEU A C   1 
ATOM   145  O  O   . LEU A 1 20  ? -4.868  1.815   -5.176  1.00 37.06  ? 20  LEU A O   1 
ATOM   146  C  CB  . LEU A 1 20  ? -3.317  3.532   -7.168  1.00 37.09  ? 20  LEU A CB  1 
ATOM   147  C  CG  . LEU A 1 20  ? -3.146  4.718   -8.148  1.00 39.88  ? 20  LEU A CG  1 
ATOM   148  C  CD1 . LEU A 1 20  ? -2.001  5.621   -7.706  1.00 34.62  ? 20  LEU A CD1 1 
ATOM   149  C  CD2 . LEU A 1 20  ? -2.936  4.226   -9.585  1.00 35.99  ? 20  LEU A CD2 1 
ATOM   150  N  N   . VAL A 1 21  ? -4.319  0.325   -6.821  1.00 36.33  ? 21  VAL A N   1 
ATOM   151  C  CA  . VAL A 1 21  ? -4.306  -0.853  -5.962  1.00 36.10  ? 21  VAL A CA  1 
ATOM   152  C  C   . VAL A 1 21  ? -2.897  -0.947  -5.422  1.00 33.91  ? 21  VAL A C   1 
ATOM   153  O  O   . VAL A 1 21  ? -1.989  -0.296  -5.955  1.00 35.55  ? 21  VAL A O   1 
ATOM   154  C  CB  . VAL A 1 21  ? -4.716  -2.197  -6.682  1.00 34.40  ? 21  VAL A CB  1 
ATOM   155  C  CG1 . VAL A 1 21  ? -6.192  -2.256  -6.968  1.00 32.28  ? 21  VAL A CG1 1 
ATOM   156  C  CG2 . VAL A 1 21  ? -3.896  -2.472  -7.937  1.00 32.32  ? 21  VAL A CG2 1 
ATOM   157  N  N   . PRO A 1 22  ? -2.710  -1.737  -4.361  1.00 29.33  ? 22  PRO A N   1 
ATOM   158  C  CA  . PRO A 1 22  ? -1.426  -1.764  -3.695  1.00 30.67  ? 22  PRO A CA  1 
ATOM   159  C  C   . PRO A 1 22  ? -0.272  -1.950  -4.649  1.00 33.07  ? 22  PRO A C   1 
ATOM   160  O  O   . PRO A 1 22  ? 0.655   -1.175  -4.582  1.00 30.06  ? 22  PRO A O   1 
ATOM   161  C  CB  . PRO A 1 22  ? -1.572  -2.944  -2.721  1.00 27.88  ? 22  PRO A CB  1 
ATOM   162  C  CG  . PRO A 1 22  ? -3.000  -2.785  -2.281  1.00 28.98  ? 22  PRO A CG  1 
ATOM   163  C  CD  . PRO A 1 22  ? -3.689  -2.570  -3.633  1.00 30.19  ? 22  PRO A CD  1 
ATOM   164  N  N   . VAL A 1 23  ? -0.326  -2.954  -5.530  1.00 37.92  ? 23  VAL A N   1 
ATOM   165  C  CA  . VAL A 1 23  ? 0.813   -3.205  -6.431  1.00 39.49  ? 23  VAL A CA  1 
ATOM   166  C  C   . VAL A 1 23  ? 1.029   -2.037  -7.423  1.00 41.06  ? 23  VAL A C   1 
ATOM   167  O  O   . VAL A 1 23  ? 2.081   -1.942  -8.072  1.00 49.24  ? 23  VAL A O   1 
ATOM   168  C  CB  . VAL A 1 23  ? 0.715   -4.592  -7.139  1.00 40.30  ? 23  VAL A CB  1 
ATOM   169  C  CG1 . VAL A 1 23  ? 0.812   -5.720  -6.134  1.00 39.60  ? 23  VAL A CG1 1 
ATOM   170  C  CG2 . VAL A 1 23  ? -0.567  -4.744  -7.945  1.00 42.52  ? 23  VAL A CG2 1 
ATOM   171  N  N   . LYS A 1 24  ? 0.051   -1.128  -7.491  1.00 39.56  ? 24  LYS A N   1 
ATOM   172  C  CA  . LYS A 1 24  ? 0.119   0.083   -8.328  1.00 38.85  ? 24  LYS A CA  1 
ATOM   173  C  C   . LYS A 1 24  ? 0.261   1.448   -7.615  1.00 42.73  ? 24  LYS A C   1 
ATOM   174  O  O   . LYS A 1 24  ? 0.382   2.498   -8.294  1.00 39.86  ? 24  LYS A O   1 
ATOM   175  C  CB  . LYS A 1 24  ? -1.080  0.100   -9.275  1.00 45.04  ? 24  LYS A CB  1 
ATOM   176  C  CG  . LYS A 1 24  ? -0.792  -0.615  -10.589 1.00 46.41  ? 24  LYS A CG  1 
ATOM   177  C  CD  . LYS A 1 24  ? -2.008  -1.365  -11.128 1.00 53.77  ? 24  LYS A CD  1 
ATOM   178  C  CE  . LYS A 1 24  ? -1.864  -2.892  -11.005 1.00 52.69  ? 24  LYS A CE  1 
ATOM   179  N  NZ  . LYS A 1 24  ? -3.091  -3.663  -11.394 1.00 49.80  ? 24  LYS A NZ  1 
ATOM   180  N  N   . TRP A 1 25  ? 0.265   1.464   -6.269  1.00 38.79  ? 25  TRP A N   1 
ATOM   181  C  CA  . TRP A 1 25  ? 0.519   2.725   -5.551  1.00 36.93  ? 25  TRP A CA  1 
ATOM   182  C  C   . TRP A 1 25  ? 1.796   3.347   -6.058  1.00 39.01  ? 25  TRP A C   1 
ATOM   183  O  O   . TRP A 1 25  ? 2.759   2.644   -6.358  1.00 40.97  ? 25  TRP A O   1 
ATOM   184  C  CB  . TRP A 1 25  ? 0.651   2.528   -4.036  1.00 32.97  ? 25  TRP A CB  1 
ATOM   185  C  CG  . TRP A 1 25  ? -0.512  1.963   -3.265  1.00 26.88  ? 25  TRP A CG  1 
ATOM   186  C  CD1 . TRP A 1 25  ? -1.847  1.862   -3.645  1.00 27.49  ? 25  TRP A CD1 1 
ATOM   187  C  CD2 . TRP A 1 25  ? -0.462  1.444   -1.898  1.00 27.52  ? 25  TRP A CD2 1 
ATOM   188  N  NE1 . TRP A 1 25  ? -2.600  1.312   -2.643  1.00 26.82  ? 25  TRP A NE1 1 
ATOM   189  C  CE2 . TRP A 1 25  ? -1.827  1.050   -1.556  1.00 28.34  ? 25  TRP A CE2 1 
ATOM   190  C  CE3 . TRP A 1 25  ? 0.561   1.266   -0.945  1.00 27.32  ? 25  TRP A CE3 1 
ATOM   191  C  CZ2 . TRP A 1 25  ? -2.147  0.493   -0.305  1.00 27.77  ? 25  TRP A CZ2 1 
ATOM   192  C  CZ3 . TRP A 1 25  ? 0.220   0.746   0.310   1.00 26.34  ? 25  TRP A CZ3 1 
ATOM   193  C  CH2 . TRP A 1 25  ? -1.093  0.343   0.610   1.00 26.27  ? 25  TRP A CH2 1 
ATOM   194  N  N   . GLY A 1 26  ? 1.841   4.669   -6.109  1.00 45.45  ? 26  GLY A N   1 
ATOM   195  C  CA  . GLY A 1 26  ? 3.038   5.378   -6.595  1.00 52.09  ? 26  GLY A CA  1 
ATOM   196  C  C   . GLY A 1 26  ? 4.051   5.754   -5.522  1.00 55.03  ? 26  GLY A C   1 
ATOM   197  O  O   . GLY A 1 26  ? 4.542   4.892   -4.780  1.00 60.21  ? 26  GLY A O   1 
ATOM   198  N  N   . GLY A 1 27  ? 4.379   7.041   -5.440  1.00 52.33  ? 27  GLY A N   1 
ATOM   199  C  CA  . GLY A 1 27  ? 5.340   7.540   -4.443  1.00 50.03  ? 27  GLY A CA  1 
ATOM   200  C  C   . GLY A 1 27  ? 6.573   6.659   -4.285  1.00 51.28  ? 27  GLY A C   1 
ATOM   201  O  O   . GLY A 1 27  ? 7.191   6.251   -5.281  1.00 47.99  ? 27  GLY A O   1 
ATOM   202  N  N   . ASN A 1 28  ? 6.920   6.353   -3.031  1.00 41.62  ? 28  ASN A N   1 
ATOM   203  C  CA  . ASN A 1 28  ? 8.018   5.452   -2.746  1.00 36.66  ? 28  ASN A CA  1 
ATOM   204  C  C   . ASN A 1 28  ? 7.592   4.006   -2.502  1.00 32.76  ? 28  ASN A C   1 
ATOM   205  O  O   . ASN A 1 28  ? 8.375   3.194   -2.074  1.00 31.52  ? 28  ASN A O   1 
ATOM   206  C  CB  . ASN A 1 28  ? 8.852   5.999   -1.608  1.00 37.63  ? 28  ASN A CB  1 
ATOM   207  C  CG  . ASN A 1 28  ? 9.256   7.445   -1.849  1.00 38.19  ? 28  ASN A CG  1 
ATOM   208  O  OD1 . ASN A 1 28  ? 10.404  7.738   -2.136  1.00 40.81  ? 28  ASN A OD1 1 
ATOM   209  N  ND2 . ASN A 1 28  ? 8.299   8.338   -1.775  1.00 35.75  ? 28  ASN A ND2 1 
ATOM   210  N  N   . CYS A 1 29  ? 6.362   3.685   -2.867  1.00 32.59  ? 29  CYS A N   1 
ATOM   211  C  CA  . CYS A 1 29  ? 5.766   2.426   -2.478  1.00 33.55  ? 29  CYS A CA  1 
ATOM   212  C  C   . CYS A 1 29  ? 6.450   1.217   -3.101  1.00 37.60  ? 29  CYS A C   1 
ATOM   213  O  O   . CYS A 1 29  ? 6.367   0.101   -2.562  1.00 32.88  ? 29  CYS A O   1 
ATOM   214  C  CB  . CYS A 1 29  ? 4.255   2.449   -2.767  1.00 30.82  ? 29  CYS A CB  1 
ATOM   215  S  SG  . CYS A 1 29  ? 3.467   3.795   -1.858  1.00 33.96  ? 29  CYS A SG  1 
ATOM   216  N  N   . GLN A 1 30  ? 7.172   1.462   -4.197  1.00 39.62  ? 30  GLN A N   1 
ATOM   217  C  CA  . GLN A 1 30  ? 7.761   0.402   -5.013  1.00 38.83  ? 30  GLN A CA  1 
ATOM   218  C  C   . GLN A 1 30  ? 9.276   0.287   -4.833  1.00 44.13  ? 30  GLN A C   1 
ATOM   219  O  O   . GLN A 1 30  ? 9.992   -0.205  -5.717  1.00 50.18  ? 30  GLN A O   1 
ATOM   220  C  CB  . GLN A 1 30  ? 7.396   0.628   -6.507  1.00 42.63  ? 30  GLN A CB  1 
ATOM   221  C  CG  . GLN A 1 30  ? 5.921   0.933   -6.812  1.00 39.44  ? 30  GLN A CG  1 
ATOM   222  C  CD  . GLN A 1 30  ? 4.955   -0.208  -6.485  1.00 42.47  ? 30  GLN A CD  1 
ATOM   223  O  OE1 . GLN A 1 30  ? 5.356   -1.366  -6.318  1.00 40.89  ? 30  GLN A OE1 1 
ATOM   224  N  NE2 . GLN A 1 30  ? 3.665   0.122   -6.384  1.00 39.12  ? 30  GLN A NE2 1 
ATOM   225  N  N   . LYS A 1 31  ? 9.769   0.701   -3.674  1.00 42.61  ? 31  LYS A N   1 
ATOM   226  C  CA  . LYS A 1 31  ? 11.177  0.569   -3.371  1.00 38.71  ? 31  LYS A CA  1 
ATOM   227  C  C   . LYS A 1 31  ? 11.495  -0.631  -2.503  1.00 41.33  ? 31  LYS A C   1 
ATOM   228  O  O   . LYS A 1 31  ? 10.685  -1.565  -2.411  1.00 34.74  ? 31  LYS A O   1 
ATOM   229  C  CB  . LYS A 1 31  ? 11.732  1.849   -2.776  1.00 40.12  ? 31  LYS A CB  1 
ATOM   230  C  CG  . LYS A 1 31  ? 11.544  3.065   -3.679  1.00 41.81  ? 31  LYS A CG  1 
ATOM   231  C  CD  . LYS A 1 31  ? 12.636  4.090   -3.424  1.00 41.88  ? 31  LYS A CD  1 
ATOM   232  C  CE  . LYS A 1 31  ? 12.551  5.270   -4.372  1.00 45.49  ? 31  LYS A CE  1 
ATOM   233  N  NZ  . LYS A 1 31  ? 11.884  6.465   -3.758  1.00 50.54  ? 31  LYS A NZ  1 
ATOM   234  N  N   . ASP A 1 32  ? 12.689  -0.600  -1.899  1.00 40.81  ? 32  ASP A N   1 
ATOM   235  C  CA  . ASP A 1 32  ? 13.353  -1.781  -1.345  1.00 44.16  ? 32  ASP A CA  1 
ATOM   236  C  C   . ASP A 1 32  ? 13.469  -1.909  0.185   1.00 39.49  ? 32  ASP A C   1 
ATOM   237  O  O   . ASP A 1 32  ? 13.868  -2.965  0.700   1.00 38.72  ? 32  ASP A O   1 
ATOM   238  C  CB  . ASP A 1 32  ? 14.753  -1.926  -1.971  1.00 50.80  ? 32  ASP A CB  1 
ATOM   239  C  CG  . ASP A 1 32  ? 14.703  -2.132  -3.482  1.00 55.82  ? 32  ASP A CG  1 
ATOM   240  O  OD1 . ASP A 1 32  ? 13.683  -2.617  -4.007  1.00 53.61  ? 32  ASP A OD1 1 
ATOM   241  O  OD2 . ASP A 1 32  ? 15.693  -1.798  -4.154  1.00 62.21  ? 32  ASP A OD2 1 
ATOM   242  N  N   . ARG A 1 33  ? 13.156  -0.856  0.917   1.00 40.42  ? 33  ARG A N   1 
ATOM   243  C  CA  . ARG A 1 33  ? 13.142  -0.970  2.381   1.00 39.63  ? 33  ARG A CA  1 
ATOM   244  C  C   . ARG A 1 33  ? 11.703  -0.774  2.903   1.00 38.61  ? 33  ARG A C   1 
ATOM   245  O  O   . ARG A 1 33  ? 11.449  -0.005  3.850   1.00 44.85  ? 33  ARG A O   1 
ATOM   246  C  CB  . ARG A 1 33  ? 14.187  -0.023  3.004   1.00 38.32  ? 33  ARG A CB  1 
ATOM   247  C  CG  . ARG A 1 33  ? 15.626  -0.504  2.776   1.00 43.48  ? 33  ARG A CG  1 
ATOM   248  C  CD  . ARG A 1 33  ? 16.722  0.443   3.267   1.00 44.51  ? 33  ARG A CD  1 
ATOM   249  N  NE  . ARG A 1 33  ? 16.934  0.441   4.734   1.00 53.73  ? 33  ARG A NE  1 
ATOM   250  C  CZ  . ARG A 1 33  ? 17.773  -0.353  5.414   1.00 52.77  ? 33  ARG A CZ  1 
ATOM   251  N  NH1 . ARG A 1 33  ? 18.518  -1.277  4.799   1.00 55.65  ? 33  ARG A NH1 1 
ATOM   252  N  NH2 . ARG A 1 33  ? 17.871  -0.228  6.734   1.00 51.86  ? 33  ARG A NH2 1 
ATOM   253  N  N   . GLN A 1 34  ? 10.755  -1.470  2.283   1.00 32.37  ? 34  GLN A N   1 
ATOM   254  C  CA  . GLN A 1 34  ? 9.352   -1.273  2.620   1.00 31.24  ? 34  GLN A CA  1 
ATOM   255  C  C   . GLN A 1 34  ? 8.791   -2.093  3.814   1.00 33.61  ? 34  GLN A C   1 
ATOM   256  O  O   . GLN A 1 34  ? 9.461   -2.986  4.336   1.00 33.65  ? 34  GLN A O   1 
ATOM   257  C  CB  . GLN A 1 34  ? 8.494   -1.479  1.390   1.00 31.97  ? 34  GLN A CB  1 
ATOM   258  C  CG  . GLN A 1 34  ? 8.745   -0.487  0.270   1.00 30.89  ? 34  GLN A CG  1 
ATOM   259  C  CD  . GLN A 1 34  ? 8.110   0.844   0.568   1.00 26.70  ? 34  GLN A CD  1 
ATOM   260  O  OE1 . GLN A 1 34  ? 6.896   1.013   0.492   1.00 27.39  ? 34  GLN A OE1 1 
ATOM   261  N  NE2 . GLN A 1 34  ? 8.913   1.779   0.911   1.00 25.68  ? 34  GLN A NE2 1 
ATOM   262  N  N   . SER A 1 35  ? 7.538   -1.769  4.174   1.00 30.84  ? 35  SER A N   1 
ATOM   263  C  CA  . SER A 1 35  ? 6.774   -2.334  5.271   1.00 30.26  ? 35  SER A CA  1 
ATOM   264  C  C   . SER A 1 35  ? 5.345   -2.603  4.818   1.00 28.35  ? 35  SER A C   1 
ATOM   265  O  O   . SER A 1 35  ? 4.816   -1.951  3.904   1.00 25.57  ? 35  SER A O   1 
ATOM   266  C  CB  . SER A 1 35  ? 6.711   -1.325  6.458   1.00 28.33  ? 35  SER A CB  1 
ATOM   267  O  OG  . SER A 1 35  ? 7.971   -1.215  7.108   1.00 28.87  ? 35  SER A OG  1 
ATOM   268  N  N   . PRO A 1 36  ? 4.677   -3.547  5.477   1.00 26.41  ? 36  PRO A N   1 
ATOM   269  C  CA  . PRO A 1 36  ? 5.131   -4.460  6.520   1.00 28.14  ? 36  PRO A CA  1 
ATOM   270  C  C   . PRO A 1 36  ? 5.930   -5.664  6.013   1.00 32.52  ? 36  PRO A C   1 
ATOM   271  O  O   . PRO A 1 36  ? 6.025   -5.869  4.767   1.00 28.54  ? 36  PRO A O   1 
ATOM   272  C  CB  . PRO A 1 36  ? 3.829   -5.011  7.060   1.00 25.42  ? 36  PRO A CB  1 
ATOM   273  C  CG  . PRO A 1 36  ? 2.948   -5.074  5.867   1.00 27.18  ? 36  PRO A CG  1 
ATOM   274  C  CD  . PRO A 1 36  ? 3.289   -3.824  5.075   1.00 24.21  ? 36  PRO A CD  1 
ATOM   275  N  N   . ILE A 1 37  ? 6.446   -6.458  6.976   1.00 29.11  ? 37  ILE A N   1 
ATOM   276  C  CA  . ILE A 1 37  ? 7.128   -7.711  6.642   1.00 30.53  ? 37  ILE A CA  1 
ATOM   277  C  C   . ILE A 1 37  ? 6.649   -8.904  7.423   1.00 31.99  ? 37  ILE A C   1 
ATOM   278  O  O   . ILE A 1 37  ? 5.914   -8.788  8.431   1.00 32.37  ? 37  ILE A O   1 
ATOM   279  C  CB  . ILE A 1 37  ? 8.654   -7.663  6.915   1.00 30.05  ? 37  ILE A CB  1 
ATOM   280  C  CG1 . ILE A 1 37  ? 8.915   -7.398  8.396   1.00 26.44  ? 37  ILE A CG1 1 
ATOM   281  C  CG2 . ILE A 1 37  ? 9.373   -6.660  5.992   1.00 27.47  ? 37  ILE A CG2 1 
ATOM   282  C  CD1 . ILE A 1 37  ? 10.374  -7.225  8.705   1.00 25.29  ? 37  ILE A CD1 1 
ATOM   283  N  N   . ASN A 1 38  ? 7.131   -10.057 6.989   1.00 29.78  ? 38  ASN A N   1 
ATOM   284  C  CA  . ASN A 1 38  ? 7.132   -11.245 7.849   1.00 30.16  ? 38  ASN A CA  1 
ATOM   285  C  C   . ASN A 1 38  ? 8.344   -11.217 8.784   1.00 26.14  ? 38  ASN A C   1 
ATOM   286  O  O   . ASN A 1 38  ? 9.469   -10.966 8.352   1.00 25.80  ? 38  ASN A O   1 
ATOM   287  C  CB  . ASN A 1 38  ? 7.103   -12.530 7.011   1.00 30.58  ? 38  ASN A CB  1 
ATOM   288  C  CG  . ASN A 1 38  ? 7.085   -13.790 7.864   1.00 33.62  ? 38  ASN A CG  1 
ATOM   289  O  OD1 . ASN A 1 38  ? 6.190   -14.001 8.698   1.00 32.89  ? 38  ASN A OD1 1 
ATOM   290  N  ND2 . ASN A 1 38  ? 8.048   -14.661 7.621   1.00 32.90  ? 38  ASN A ND2 1 
ATOM   291  N  N   . ILE A 1 39  ? 8.132   -11.495 10.068  1.00 27.24  ? 39  ILE A N   1 
ATOM   292  C  CA  . ILE A 1 39  ? 9.261   -11.590 11.006  1.00 29.09  ? 39  ILE A CA  1 
ATOM   293  C  C   . ILE A 1 39  ? 9.530   -13.088 11.326  1.00 33.41  ? 39  ILE A C   1 
ATOM   294  O  O   . ILE A 1 39  ? 8.671   -13.791 11.873  1.00 30.26  ? 39  ILE A O   1 
ATOM   295  C  CB  . ILE A 1 39  ? 9.015   -10.795 12.308  1.00 32.58  ? 39  ILE A CB  1 
ATOM   296  C  CG1 . ILE A 1 39  ? 8.819   -9.284  11.999  1.00 32.68  ? 39  ILE A CG1 1 
ATOM   297  C  CG2 . ILE A 1 39  ? 10.113  -11.061 13.346  1.00 31.56  ? 39  ILE A CG2 1 
ATOM   298  C  CD1 . ILE A 1 39  ? 8.447   -8.451  13.191  1.00 31.67  ? 39  ILE A CD1 1 
ATOM   299  N  N   . VAL A 1 40  ? 10.702  -13.586 10.929  1.00 35.85  ? 40  VAL A N   1 
ATOM   300  C  CA  . VAL A 1 40  ? 11.099  -14.917 11.347  1.00 38.34  ? 40  VAL A CA  1 
ATOM   301  C  C   . VAL A 1 40  ? 11.641  -14.766 12.771  1.00 36.56  ? 40  VAL A C   1 
ATOM   302  O  O   . VAL A 1 40  ? 12.791  -14.375 12.978  1.00 38.52  ? 40  VAL A O   1 
ATOM   303  C  CB  . VAL A 1 40  ? 12.171  -15.569 10.425  1.00 41.29  ? 40  VAL A CB  1 
ATOM   304  C  CG1 . VAL A 1 40  ? 12.507  -16.969 10.943  1.00 38.65  ? 40  VAL A CG1 1 
ATOM   305  C  CG2 . VAL A 1 40  ? 11.698  -15.627 8.980   1.00 41.19  ? 40  VAL A CG2 1 
ATOM   306  N  N   . THR A 1 41  ? 10.820  -15.060 13.760  1.00 34.84  ? 41  THR A N   1 
ATOM   307  C  CA  . THR A 1 41  ? 11.256  -14.798 15.140  1.00 37.63  ? 41  THR A CA  1 
ATOM   308  C  C   . THR A 1 41  ? 12.647  -15.390 15.479  1.00 38.68  ? 41  THR A C   1 
ATOM   309  O  O   . THR A 1 41  ? 13.460  -14.711 16.092  1.00 43.03  ? 41  THR A O   1 
ATOM   310  C  CB  . THR A 1 41  ? 10.180  -15.232 16.149  1.00 35.64  ? 41  THR A CB  1 
ATOM   311  O  OG1 . THR A 1 41  ? 10.090  -16.660 16.154  1.00 38.43  ? 41  THR A OG1 1 
ATOM   312  C  CG2 . THR A 1 41  ? 8.814   -14.706 15.714  1.00 33.44  ? 41  THR A CG2 1 
ATOM   313  N  N   . THR A 1 42  ? 12.951  -16.616 15.038  1.00 41.66  ? 42  THR A N   1 
ATOM   314  C  CA  . THR A 1 42  ? 14.256  -17.233 15.384  1.00 45.29  ? 42  THR A CA  1 
ATOM   315  C  C   . THR A 1 42  ? 15.498  -16.521 14.824  1.00 48.88  ? 42  THR A C   1 
ATOM   316  O  O   . THR A 1 42  ? 16.566  -16.525 15.478  1.00 48.85  ? 42  THR A O   1 
ATOM   317  C  CB  . THR A 1 42  ? 14.337  -18.770 15.122  1.00 40.01  ? 42  THR A CB  1 
ATOM   318  O  OG1 . THR A 1 42  ? 13.997  -19.063 13.767  1.00 35.16  ? 42  THR A OG1 1 
ATOM   319  C  CG2 . THR A 1 42  ? 13.395  -19.529 16.052  1.00 36.62  ? 42  THR A CG2 1 
ATOM   320  N  N   . LYS A 1 43  ? 15.327  -15.882 13.660  1.00 48.80  ? 43  LYS A N   1 
ATOM   321  C  CA  . LYS A 1 43  ? 16.399  -15.224 12.896  1.00 47.29  ? 43  LYS A CA  1 
ATOM   322  C  C   . LYS A 1 43  ? 16.795  -13.823 13.333  1.00 46.07  ? 43  LYS A C   1 
ATOM   323  O  O   . LYS A 1 43  ? 17.754  -13.264 12.791  1.00 47.46  ? 43  LYS A O   1 
ATOM   324  C  CB  . LYS A 1 43  ? 16.016  -15.161 11.415  1.00 53.26  ? 43  LYS A CB  1 
ATOM   325  C  CG  . LYS A 1 43  ? 16.540  -16.315 10.573  1.00 54.24  ? 43  LYS A CG  1 
ATOM   326  C  CD  . LYS A 1 43  ? 16.214  -16.140 9.093   1.00 51.11  ? 43  LYS A CD  1 
ATOM   327  C  CE  . LYS A 1 43  ? 16.616  -17.400 8.310   1.00 52.74  ? 43  LYS A CE  1 
ATOM   328  N  NZ  . LYS A 1 43  ? 16.052  -17.410 6.931   1.00 45.65  ? 43  LYS A NZ  1 
ATOM   329  N  N   . ALA A 1 44  ? 16.060  -13.251 14.287  1.00 47.79  ? 44  ALA A N   1 
ATOM   330  C  CA  . ALA A 1 44  ? 16.339  -11.903 14.792  1.00 45.00  ? 44  ALA A CA  1 
ATOM   331  C  C   . ALA A 1 44  ? 17.278  -11.919 16.005  1.00 45.37  ? 44  ALA A C   1 
ATOM   332  O  O   . ALA A 1 44  ? 16.885  -12.310 17.093  1.00 45.65  ? 44  ALA A O   1 
ATOM   333  C  CB  . ALA A 1 44  ? 15.033  -11.177 15.118  1.00 43.14  ? 44  ALA A CB  1 
ATOM   334  N  N   . LYS A 1 45  ? 18.516  -11.480 15.818  1.00 46.69  ? 45  LYS A N   1 
ATOM   335  C  CA  . LYS A 1 45  ? 19.519  -11.526 16.891  1.00 49.19  ? 45  LYS A CA  1 
ATOM   336  C  C   . LYS A 1 45  ? 19.174  -10.564 18.008  1.00 50.18  ? 45  LYS A C   1 
ATOM   337  O  O   . LYS A 1 45  ? 18.777  -9.437  17.751  1.00 51.53  ? 45  LYS A O   1 
ATOM   338  C  CB  . LYS A 1 45  ? 20.938  -11.262 16.352  1.00 49.10  ? 45  LYS A CB  1 
ATOM   339  C  CG  . LYS A 1 45  ? 21.286  -12.185 15.192  1.00 47.85  ? 45  LYS A CG  1 
ATOM   340  C  CD  . LYS A 1 45  ? 22.704  -12.031 14.671  1.00 56.14  ? 45  LYS A CD  1 
ATOM   341  C  CE  . LYS A 1 45  ? 22.956  -13.022 13.532  1.00 59.15  ? 45  LYS A CE  1 
ATOM   342  N  NZ  . LYS A 1 45  ? 24.396  -13.376 13.352  1.00 60.44  ? 45  LYS A NZ  1 
ATOM   343  N  N   . VAL A 1 46  ? 19.320  -11.034 19.247  1.00 50.60  ? 46  VAL A N   1 
ATOM   344  C  CA  . VAL A 1 46  ? 19.055  -10.233 20.437  1.00 49.24  ? 46  VAL A CA  1 
ATOM   345  C  C   . VAL A 1 46  ? 20.045  -9.090  20.460  1.00 50.89  ? 46  VAL A C   1 
ATOM   346  O  O   . VAL A 1 46  ? 21.232  -9.306  20.236  1.00 57.45  ? 46  VAL A O   1 
ATOM   347  C  CB  . VAL A 1 46  ? 19.161  -11.088 21.726  1.00 48.78  ? 46  VAL A CB  1 
ATOM   348  C  CG1 . VAL A 1 46  ? 18.901  -10.255 22.969  1.00 50.23  ? 46  VAL A CG1 1 
ATOM   349  C  CG2 . VAL A 1 46  ? 18.176  -12.248 21.666  1.00 49.26  ? 46  VAL A CG2 1 
ATOM   350  N  N   . ASP A 1 47  ? 19.542  -7.870  20.645  1.00 52.34  ? 47  ASP A N   1 
ATOM   351  C  CA  . ASP A 1 47  ? 20.380  -6.695  20.873  1.00 53.16  ? 47  ASP A CA  1 
ATOM   352  C  C   . ASP A 1 47  ? 20.064  -6.146  22.260  1.00 57.91  ? 47  ASP A C   1 
ATOM   353  O  O   . ASP A 1 47  ? 18.884  -5.901  22.597  1.00 48.87  ? 47  ASP A O   1 
ATOM   354  C  CB  . ASP A 1 47  ? 20.165  -5.617  19.804  1.00 57.72  ? 47  ASP A CB  1 
ATOM   355  C  CG  . ASP A 1 47  ? 21.245  -4.514  19.841  1.00 66.79  ? 47  ASP A CG  1 
ATOM   356  O  OD1 . ASP A 1 47  ? 22.192  -4.602  20.663  1.00 75.46  ? 47  ASP A OD1 1 
ATOM   357  O  OD2 . ASP A 1 47  ? 21.148  -3.549  19.046  1.00 65.74  ? 47  ASP A OD2 1 
ATOM   358  N  N   . LYS A 1 48  ? 21.119  -5.960  23.054  1.00 55.84  ? 48  LYS A N   1 
ATOM   359  C  CA  . LYS A 1 48  ? 20.967  -5.611  24.479  1.00 59.01  ? 48  LYS A CA  1 
ATOM   360  C  C   . LYS A 1 48  ? 20.514  -4.187  24.778  1.00 57.07  ? 48  LYS A C   1 
ATOM   361  O  O   . LYS A 1 48  ? 19.853  -3.948  25.803  1.00 53.78  ? 48  LYS A O   1 
ATOM   362  C  CB  . LYS A 1 48  ? 22.242  -5.947  25.258  1.00 63.36  ? 48  LYS A CB  1 
ATOM   363  C  CG  . LYS A 1 48  ? 22.283  -7.400  25.719  1.00 66.04  ? 48  LYS A CG  1 
ATOM   364  C  CD  . LYS A 1 48  ? 23.648  -7.776  26.261  1.00 67.75  ? 48  LYS A CD  1 
ATOM   365  C  CE  . LYS A 1 48  ? 23.515  -8.714  27.453  1.00 67.92  ? 48  LYS A CE  1 
ATOM   366  N  NZ  . LYS A 1 48  ? 24.847  -9.217  27.881  1.00 65.61  ? 48  LYS A NZ  1 
ATOM   367  N  N   . LYS A 1 49  ? 20.859  -3.249  23.891  1.00 58.01  ? 49  LYS A N   1 
ATOM   368  C  CA  . LYS A 1 49  ? 20.386  -1.850  23.992  1.00 60.84  ? 49  LYS A CA  1 
ATOM   369  C  C   . LYS A 1 49  ? 18.851  -1.661  23.803  1.00 59.51  ? 49  LYS A C   1 
ATOM   370  O  O   . LYS A 1 49  ? 18.300  -0.595  24.108  1.00 53.11  ? 49  LYS A O   1 
ATOM   371  C  CB  . LYS A 1 49  ? 21.191  -0.898  23.073  1.00 61.82  ? 49  LYS A CB  1 
ATOM   372  C  CG  . LYS A 1 49  ? 21.800  -1.532  21.825  1.00 69.53  ? 49  LYS A CG  1 
ATOM   373  C  CD  . LYS A 1 49  ? 22.105  -0.513  20.726  1.00 66.95  ? 49  LYS A CD  1 
ATOM   374  C  CE  . LYS A 1 49  ? 23.187  -1.044  19.786  1.00 70.61  ? 49  LYS A CE  1 
ATOM   375  N  NZ  . LYS A 1 49  ? 23.107  -0.573  18.369  1.00 64.55  ? 49  LYS A NZ  1 
ATOM   376  N  N   . LEU A 1 50  ? 18.178  -2.696  23.302  1.00 53.43  ? 50  LEU A N   1 
ATOM   377  C  CA  . LEU A 1 50  ? 16.728  -2.713  23.249  1.00 50.98  ? 50  LEU A CA  1 
ATOM   378  C  C   . LEU A 1 50  ? 16.118  -2.911  24.644  1.00 46.55  ? 50  LEU A C   1 
ATOM   379  O  O   . LEU A 1 50  ? 15.598  -3.982  24.967  1.00 42.23  ? 50  LEU A O   1 
ATOM   380  C  CB  . LEU A 1 50  ? 16.221  -3.786  22.260  1.00 48.10  ? 50  LEU A CB  1 
ATOM   381  C  CG  . LEU A 1 50  ? 16.569  -3.650  20.757  1.00 51.36  ? 50  LEU A CG  1 
ATOM   382  C  CD1 . LEU A 1 50  ? 15.633  -4.529  19.930  1.00 48.47  ? 50  LEU A CD1 1 
ATOM   383  C  CD2 . LEU A 1 50  ? 16.531  -2.203  20.266  1.00 45.73  ? 50  LEU A CD2 1 
ATOM   384  N  N   . GLY A 1 51  ? 16.160  -1.862  25.458  1.00 46.91  ? 51  GLY A N   1 
ATOM   385  C  CA  . GLY A 1 51  ? 15.604  -1.932  26.802  1.00 41.89  ? 51  GLY A CA  1 
ATOM   386  C  C   . GLY A 1 51  ? 14.167  -1.469  26.854  1.00 43.60  ? 51  GLY A C   1 
ATOM   387  O  O   . GLY A 1 51  ? 13.605  -1.053  25.835  1.00 38.23  ? 51  GLY A O   1 
ATOM   388  N  N   . ARG A 1 52  ? 13.576  -1.540  28.055  1.00 47.08  ? 52  ARG A N   1 
ATOM   389  C  CA  . ARG A 1 52  ? 12.199  -1.061  28.311  1.00 43.56  ? 52  ARG A CA  1 
ATOM   390  C  C   . ARG A 1 52  ? 11.872  0.352   27.763  1.00 40.87  ? 52  ARG A C   1 
ATOM   391  O  O   . ARG A 1 52  ? 12.758  1.206   27.669  1.00 36.67  ? 52  ARG A O   1 
ATOM   392  C  CB  . ARG A 1 52  ? 11.839  -1.189  29.809  1.00 46.57  ? 52  ARG A CB  1 
ATOM   393  C  CG  . ARG A 1 52  ? 13.022  -1.113  30.769  1.00 51.39  ? 52  ARG A CG  1 
ATOM   394  C  CD  . ARG A 1 52  ? 12.636  -1.347  32.228  1.00 52.08  ? 52  ARG A CD  1 
ATOM   395  N  NE  . ARG A 1 52  ? 11.529  -0.478  32.639  1.00 54.13  ? 52  ARG A NE  1 
ATOM   396  C  CZ  . ARG A 1 52  ? 10.301  -0.916  32.904  1.00 53.45  ? 52  ARG A CZ  1 
ATOM   397  N  NH1 . ARG A 1 52  ? 10.026  -2.222  32.835  1.00 52.94  ? 52  ARG A NH1 1 
ATOM   398  N  NH2 . ARG A 1 52  ? 9.347   -0.062  33.264  1.00 50.95  ? 52  ARG A NH2 1 
ATOM   399  N  N   . PHE A 1 53  ? 10.606  0.552   27.359  1.00 38.30  ? 53  PHE A N   1 
ATOM   400  C  CA  . PHE A 1 53  ? 10.112  1.822   26.802  1.00 35.10  ? 53  PHE A CA  1 
ATOM   401  C  C   . PHE A 1 53  ? 9.574   2.577   27.972  1.00 38.64  ? 53  PHE A C   1 
ATOM   402  O  O   . PHE A 1 53  ? 8.997   1.961   28.885  1.00 36.14  ? 53  PHE A O   1 
ATOM   403  C  CB  . PHE A 1 53  ? 8.918   1.621   25.839  1.00 32.54  ? 53  PHE A CB  1 
ATOM   404  C  CG  . PHE A 1 53  ? 9.280   1.391   24.364  1.00 32.02  ? 53  PHE A CG  1 
ATOM   405  C  CD1 . PHE A 1 53  ? 9.300   0.107   23.842  1.00 30.77  ? 53  PHE A CD1 1 
ATOM   406  C  CD2 . PHE A 1 53  ? 9.480   2.473   23.484  1.00 28.37  ? 53  PHE A CD2 1 
ATOM   407  C  CE1 . PHE A 1 53  ? 9.575   -0.117  22.477  1.00 29.60  ? 53  PHE A CE1 1 
ATOM   408  C  CE2 . PHE A 1 53  ? 9.764   2.259   22.141  1.00 26.91  ? 53  PHE A CE2 1 
ATOM   409  C  CZ  . PHE A 1 53  ? 9.810   0.950   21.636  1.00 25.91  ? 53  PHE A CZ  1 
ATOM   410  N  N   . PHE A 1 54  ? 9.715   3.903   27.939  1.00 38.66  ? 54  PHE A N   1 
ATOM   411  C  CA  . PHE A 1 54  ? 9.126   4.737   28.957  1.00 36.18  ? 54  PHE A CA  1 
ATOM   412  C  C   . PHE A 1 54  ? 8.087   5.625   28.312  1.00 40.42  ? 54  PHE A C   1 
ATOM   413  O  O   . PHE A 1 54  ? 8.257   6.119   27.191  1.00 44.35  ? 54  PHE A O   1 
ATOM   414  C  CB  . PHE A 1 54  ? 10.197  5.518   29.740  1.00 34.97  ? 54  PHE A CB  1 
ATOM   415  C  CG  . PHE A 1 54  ? 11.187  4.617   30.431  1.00 37.60  ? 54  PHE A CG  1 
ATOM   416  C  CD1 . PHE A 1 54  ? 10.870  4.012   31.655  1.00 41.03  ? 54  PHE A CD1 1 
ATOM   417  C  CD2 . PHE A 1 54  ? 12.412  4.323   29.845  1.00 34.92  ? 54  PHE A CD2 1 
ATOM   418  C  CE1 . PHE A 1 54  ? 11.778  3.160   32.284  1.00 38.95  ? 54  PHE A CE1 1 
ATOM   419  C  CE2 . PHE A 1 54  ? 13.313  3.480   30.450  1.00 36.00  ? 54  PHE A CE2 1 
ATOM   420  C  CZ  . PHE A 1 54  ? 13.006  2.899   31.674  1.00 39.45  ? 54  PHE A CZ  1 
ATOM   421  N  N   . PHE A 1 55  ? 7.003   5.804   29.045  1.00 37.07  ? 55  PHE A N   1 
ATOM   422  C  CA  . PHE A 1 55  ? 5.821   6.421   28.555  1.00 35.99  ? 55  PHE A CA  1 
ATOM   423  C  C   . PHE A 1 55  ? 5.524   7.648   29.425  1.00 38.19  ? 55  PHE A C   1 
ATOM   424  O  O   . PHE A 1 55  ? 5.542   7.517   30.659  1.00 36.96  ? 55  PHE A O   1 
ATOM   425  C  CB  . PHE A 1 55  ? 4.680   5.406   28.688  1.00 32.55  ? 55  PHE A CB  1 
ATOM   426  C  CG  . PHE A 1 55  ? 4.864   4.138   27.876  1.00 30.79  ? 55  PHE A CG  1 
ATOM   427  C  CD1 . PHE A 1 55  ? 4.387   4.069   26.561  1.00 29.48  ? 55  PHE A CD1 1 
ATOM   428  C  CD2 . PHE A 1 55  ? 5.431   2.992   28.452  1.00 29.79  ? 55  PHE A CD2 1 
ATOM   429  C  CE1 . PHE A 1 55  ? 4.533   2.911   25.813  1.00 32.63  ? 55  PHE A CE1 1 
ATOM   430  C  CE2 . PHE A 1 55  ? 5.585   1.845   27.718  1.00 32.18  ? 55  PHE A CE2 1 
ATOM   431  C  CZ  . PHE A 1 55  ? 5.135   1.798   26.390  1.00 35.54  ? 55  PHE A CZ  1 
ATOM   432  N  N   . SER A 1 56  ? 5.277   8.812   28.795  1.00 36.60  ? 56  SER A N   1 
ATOM   433  C  CA  . SER A 1 56  ? 4.670   10.008  29.445  1.00 35.57  ? 56  SER A CA  1 
ATOM   434  C  C   . SER A 1 56  ? 3.301   10.279  28.847  1.00 34.95  ? 56  SER A C   1 
ATOM   435  O  O   . SER A 1 56  ? 3.152   10.287  27.632  1.00 33.32  ? 56  SER A O   1 
ATOM   436  C  CB  . SER A 1 56  ? 5.446   11.306  29.207  1.00 34.25  ? 56  SER A CB  1 
ATOM   437  O  OG  . SER A 1 56  ? 6.850   11.137  29.197  1.00 42.52  ? 56  SER A OG  1 
ATOM   438  N  N   . GLY A 1 57  ? 2.306   10.545  29.682  1.00 35.63  ? 57  GLY A N   1 
ATOM   439  C  CA  . GLY A 1 57  ? 0.994   10.985  29.173  1.00 35.44  ? 57  GLY A CA  1 
ATOM   440  C  C   . GLY A 1 57  ? 0.050   9.845   28.821  1.00 35.05  ? 57  GLY A C   1 
ATOM   441  O  O   . GLY A 1 57  ? -1.150  10.044  28.597  1.00 32.67  ? 57  GLY A O   1 
ATOM   442  N  N   . TYR A 1 58  ? 0.591   8.635   28.771  1.00 37.93  ? 58  TYR A N   1 
ATOM   443  C  CA  . TYR A 1 58  ? -0.215  7.442   28.506  1.00 34.46  ? 58  TYR A CA  1 
ATOM   444  C  C   . TYR A 1 58  ? -1.301  7.150   29.560  1.00 37.79  ? 58  TYR A C   1 
ATOM   445  O  O   . TYR A 1 58  ? -2.369  6.609   29.220  1.00 41.96  ? 58  TYR A O   1 
ATOM   446  C  CB  . TYR A 1 58  ? 0.696   6.245   28.283  1.00 31.49  ? 58  TYR A CB  1 
ATOM   447  C  CG  . TYR A 1 58  ? 1.159   6.098   26.819  1.00 31.02  ? 58  TYR A CG  1 
ATOM   448  C  CD1 . TYR A 1 58  ? 1.893   7.101   26.164  1.00 31.81  ? 58  TYR A CD1 1 
ATOM   449  C  CD2 . TYR A 1 58  ? 0.835   4.950   26.084  1.00 32.04  ? 58  TYR A CD2 1 
ATOM   450  C  CE1 . TYR A 1 58  ? 2.285   6.954   24.814  1.00 30.11  ? 58  TYR A CE1 1 
ATOM   451  C  CE2 . TYR A 1 58  ? 1.203   4.806   24.740  1.00 30.77  ? 58  TYR A CE2 1 
ATOM   452  C  CZ  . TYR A 1 58  ? 1.925   5.801   24.116  1.00 28.02  ? 58  TYR A CZ  1 
ATOM   453  O  OH  . TYR A 1 58  ? 2.302   5.600   22.809  1.00 30.67  ? 58  TYR A OH  1 
ATOM   454  N  N   . ASP A 1 59  ? -1.059  7.530   30.813  1.00 38.61  ? 59  ASP A N   1 
ATOM   455  C  CA  . ASP A 1 59  ? -1.980  7.205   31.922  1.00 44.84  ? 59  ASP A CA  1 
ATOM   456  C  C   . ASP A 1 59  ? -3.080  8.251   32.042  1.00 43.93  ? 59  ASP A C   1 
ATOM   457  O  O   . ASP A 1 59  ? -4.103  8.019   32.690  1.00 45.45  ? 59  ASP A O   1 
ATOM   458  C  CB  . ASP A 1 59  ? -1.230  7.176   33.261  1.00 44.20  ? 59  ASP A CB  1 
ATOM   459  C  CG  . ASP A 1 59  ? -0.785  8.578   33.701  1.00 52.14  ? 59  ASP A CG  1 
ATOM   460  O  OD1 . ASP A 1 59  ? -0.156  9.319   32.907  1.00 51.86  ? 59  ASP A OD1 1 
ATOM   461  O  OD2 . ASP A 1 59  ? -1.087  8.960   34.845  1.00 60.21  ? 59  ASP A OD2 1 
ATOM   462  N  N   . LYS A 1 60  ? -2.846  9.411   31.445  1.00 41.00  ? 60  LYS A N   1 
ATOM   463  C  CA  . LYS A 1 60  ? -3.741  10.556  31.578  1.00 43.10  ? 60  LYS A CA  1 
ATOM   464  C  C   . LYS A 1 60  ? -5.085  10.305  30.871  1.00 48.00  ? 60  LYS A C   1 
ATOM   465  O  O   . LYS A 1 60  ? -5.126  9.943   29.689  1.00 45.26  ? 60  LYS A O   1 
ATOM   466  C  CB  . LYS A 1 60  ? -3.064  11.793  30.963  1.00 45.65  ? 60  LYS A CB  1 
ATOM   467  C  CG  . LYS A 1 60  ? -2.965  12.999  31.868  1.00 51.67  ? 60  LYS A CG  1 
ATOM   468  C  CD  . LYS A 1 60  ? -1.671  12.984  32.699  1.00 60.42  ? 60  LYS A CD  1 
ATOM   469  C  CE  . LYS A 1 60  ? -1.795  13.822  33.975  1.00 57.48  ? 60  LYS A CE  1 
ATOM   470  N  NZ  . LYS A 1 60  ? -2.297  15.210  33.727  1.00 57.50  ? 60  LYS A NZ  1 
ATOM   471  N  N   . LYS A 1 61  ? -6.191  10.507  31.578  1.00 46.43  ? 61  LYS A N   1 
ATOM   472  C  CA  . LYS A 1 61  ? -7.512  10.307  30.976  1.00 44.42  ? 61  LYS A CA  1 
ATOM   473  C  C   . LYS A 1 61  ? -7.697  11.465  29.996  1.00 46.00  ? 61  LYS A C   1 
ATOM   474  O  O   . LYS A 1 61  ? -7.123  12.528  30.224  1.00 47.18  ? 61  LYS A O   1 
ATOM   475  C  CB  . LYS A 1 61  ? -8.595  10.237  32.075  1.00 47.87  ? 61  LYS A CB  1 
ATOM   476  C  CG  . LYS A 1 61  ? -8.579  8.951   32.933  1.00 44.98  ? 61  LYS A CG  1 
ATOM   477  C  CD  . LYS A 1 61  ? -9.686  7.984   32.502  1.00 47.75  ? 61  LYS A CD  1 
ATOM   478  C  CE  . LYS A 1 61  ? -9.487  6.575   33.041  1.00 46.55  ? 61  LYS A CE  1 
ATOM   479  N  NZ  . LYS A 1 61  ? -9.885  5.598   31.966  1.00 45.56  ? 61  LYS A NZ  1 
ATOM   480  N  N   . GLN A 1 62  ? -8.413  11.246  28.879  1.00 47.90  ? 62  GLN A N   1 
ATOM   481  C  CA  . GLN A 1 62  ? -8.668  12.299  27.863  1.00 44.90  ? 62  GLN A CA  1 
ATOM   482  C  C   . GLN A 1 62  ? -9.893  12.023  26.974  1.00 40.50  ? 62  GLN A C   1 
ATOM   483  O  O   . GLN A 1 62  ? -10.530 11.006  27.141  1.00 40.42  ? 62  GLN A O   1 
ATOM   484  C  CB  . GLN A 1 62  ? -7.411  12.631  27.040  1.00 45.61  ? 62  GLN A CB  1 
ATOM   485  C  CG  . GLN A 1 62  ? -7.124  14.153  27.029  1.00 46.23  ? 62  GLN A CG  1 
ATOM   486  C  CD  . GLN A 1 62  ? -5.636  14.470  27.038  1.00 45.46  ? 62  GLN A CD  1 
ATOM   487  O  OE1 . GLN A 1 62  ? -5.121  15.104  26.127  1.00 58.81  ? 62  GLN A OE1 1 
ATOM   488  N  NE2 . GLN A 1 62  ? -4.941  14.019  28.057  1.00 42.31  ? 62  GLN A NE2 1 
ATOM   489  N  N   . THR A 1 63  ? -10.257 12.937  26.075  1.00 35.79  ? 63  THR A N   1 
ATOM   490  C  CA  . THR A 1 63  ? -11.454 12.727  25.234  1.00 34.55  ? 63  THR A CA  1 
ATOM   491  C  C   . THR A 1 63  ? -11.070 12.838  23.775  1.00 36.26  ? 63  THR A C   1 
ATOM   492  O  O   . THR A 1 63  ? -11.179 13.913  23.148  1.00 31.25  ? 63  THR A O   1 
ATOM   493  C  CB  . THR A 1 63  ? -12.614 13.733  25.503  1.00 38.51  ? 63  THR A CB  1 
ATOM   494  O  OG1 . THR A 1 63  ? -12.131 15.087  25.416  1.00 39.44  ? 63  THR A OG1 1 
ATOM   495  C  CG2 . THR A 1 63  ? -13.260 13.506  26.868  1.00 33.69  ? 63  THR A CG2 1 
ATOM   496  N  N   . TRP A 1 64  ? -10.686 11.698  23.211  1.00 32.23  ? 64  TRP A N   1 
ATOM   497  C  CA  . TRP A 1 64  ? -9.979  11.738  21.955  1.00 32.80  ? 64  TRP A CA  1 
ATOM   498  C  C   . TRP A 1 64  ? -10.927 11.976  20.819  1.00 29.02  ? 64  TRP A C   1 
ATOM   499  O  O   . TRP A 1 64  ? -12.018 11.470  20.814  1.00 32.81  ? 64  TRP A O   1 
ATOM   500  C  CB  . TRP A 1 64  ? -9.246  10.441  21.732  1.00 26.28  ? 64  TRP A CB  1 
ATOM   501  C  CG  . TRP A 1 64  ? -8.204  10.068  22.748  1.00 26.44  ? 64  TRP A CG  1 
ATOM   502  C  CD1 . TRP A 1 64  ? -8.229  8.977   23.613  1.00 24.41  ? 64  TRP A CD1 1 
ATOM   503  C  CD2 . TRP A 1 64  ? -6.922  10.729  23.017  1.00 24.75  ? 64  TRP A CD2 1 
ATOM   504  N  NE1 . TRP A 1 64  ? -7.089  8.924   24.365  1.00 25.70  ? 64  TRP A NE1 1 
ATOM   505  C  CE2 . TRP A 1 64  ? -6.251  9.916   24.035  1.00 25.32  ? 64  TRP A CE2 1 
ATOM   506  C  CE3 . TRP A 1 64  ? -6.274  11.845  22.515  1.00 24.94  ? 64  TRP A CE3 1 
ATOM   507  C  CZ2 . TRP A 1 64  ? -4.989  10.239  24.531  1.00 26.03  ? 64  TRP A CZ2 1 
ATOM   508  C  CZ3 . TRP A 1 64  ? -5.010  12.162  23.041  1.00 26.93  ? 64  TRP A CZ3 1 
ATOM   509  C  CH2 . TRP A 1 64  ? -4.409  11.402  24.054  1.00 23.24  ? 64  TRP A CH2 1 
ATOM   510  N  N   . THR A 1 65  ? -10.500 12.775  19.866  1.00 29.79  ? 65  THR A N   1 
ATOM   511  C  CA  . THR A 1 65  ? -11.196 12.922  18.588  1.00 32.96  ? 65  THR A CA  1 
ATOM   512  C  C   . THR A 1 65  ? -10.876 11.656  17.789  1.00 34.55  ? 65  THR A C   1 
ATOM   513  O  O   . THR A 1 65  ? -9.706  11.292  17.643  1.00 36.58  ? 65  THR A O   1 
ATOM   514  C  CB  . THR A 1 65  ? -10.692 14.211  17.864  1.00 32.61  ? 65  THR A CB  1 
ATOM   515  O  OG1 . THR A 1 65  ? -11.178 15.364  18.568  1.00 33.86  ? 65  THR A OG1 1 
ATOM   516  C  CG2 . THR A 1 65  ? -11.140 14.296  16.379  1.00 31.56  ? 65  THR A CG2 1 
ATOM   517  N  N   . VAL A 1 66  ? -11.898 10.968  17.307  1.00 34.36  ? 66  VAL A N   1 
ATOM   518  C  CA  . VAL A 1 66  ? -11.669 9.801   16.446  1.00 35.54  ? 66  VAL A CA  1 
ATOM   519  C  C   . VAL A 1 66  ? -12.460 9.902   15.146  1.00 37.53  ? 66  VAL A C   1 
ATOM   520  O  O   . VAL A 1 66  ? -13.654 10.222  15.189  1.00 35.09  ? 66  VAL A O   1 
ATOM   521  C  CB  . VAL A 1 66  ? -11.928 8.471   17.186  1.00 33.79  ? 66  VAL A CB  1 
ATOM   522  C  CG1 . VAL A 1 66  ? -13.402 8.284   17.561  1.00 30.12  ? 66  VAL A CG1 1 
ATOM   523  C  CG2 . VAL A 1 66  ? -11.405 7.291   16.374  1.00 30.76  ? 66  VAL A CG2 1 
ATOM   524  N  N   . GLN A 1 67  ? -11.788 9.629   14.013  1.00 35.20  ? 67  GLN A N   1 
ATOM   525  C  CA  . GLN A 1 67  ? -12.394 9.739   12.666  1.00 37.73  ? 67  GLN A CA  1 
ATOM   526  C  C   . GLN A 1 67  ? -12.162 8.588   11.689  1.00 37.43  ? 67  GLN A C   1 
ATOM   527  O  O   . GLN A 1 67  ? -11.073 7.982   11.663  1.00 36.85  ? 67  GLN A O   1 
ATOM   528  C  CB  . GLN A 1 67  ? -11.951 11.038  11.977  1.00 40.30  ? 67  GLN A CB  1 
ATOM   529  C  CG  . GLN A 1 67  ? -10.484 11.077  11.556  1.00 42.82  ? 67  GLN A CG  1 
ATOM   530  C  CD  . GLN A 1 67  ? -9.893  12.470  11.604  1.00 43.09  ? 67  GLN A CD  1 
ATOM   531  O  OE1 . GLN A 1 67  ? -10.525 13.407  12.066  1.00 44.02  ? 67  GLN A OE1 1 
ATOM   532  N  NE2 . GLN A 1 67  ? -8.668  12.604  11.134  1.00 48.36  ? 67  GLN A NE2 1 
ATOM   533  N  N   . ASN A 1 68  ? -13.204 8.325   10.897  1.00 34.15  ? 68  ASN A N   1 
ATOM   534  C  CA  . ASN A 1 68  ? -13.174 7.469   9.730   1.00 35.46  ? 68  ASN A CA  1 
ATOM   535  C  C   . ASN A 1 68  ? -12.631 8.267   8.550   1.00 35.25  ? 68  ASN A C   1 
ATOM   536  O  O   . ASN A 1 68  ? -13.334 9.096   7.988   1.00 36.06  ? 68  ASN A O   1 
ATOM   537  C  CB  . ASN A 1 68  ? -14.598 6.983   9.406   1.00 33.19  ? 68  ASN A CB  1 
ATOM   538  C  CG  . ASN A 1 68  ? -14.658 6.127   8.161   1.00 31.68  ? 68  ASN A CG  1 
ATOM   539  O  OD1 . ASN A 1 68  ? -13.752 6.161   7.306   1.00 31.33  ? 68  ASN A OD1 1 
ATOM   540  N  ND2 . ASN A 1 68  ? -15.744 5.367   8.026   1.00 27.21  ? 68  ASN A ND2 1 
ATOM   541  N  N   . ASN A 1 69  ? -11.379 8.019   8.185   1.00 33.47  ? 69  ASN A N   1 
ATOM   542  C  CA  . ASN A 1 69  ? -10.745 8.762   7.096   1.00 34.81  ? 69  ASN A CA  1 
ATOM   543  C  C   . ASN A 1 69  ? -10.927 8.022   5.769   1.00 35.43  ? 69  ASN A C   1 
ATOM   544  O  O   . ASN A 1 69  ? -10.226 8.306   4.805   1.00 33.20  ? 69  ASN A O   1 
ATOM   545  C  CB  . ASN A 1 69  ? -9.256  8.915   7.391   1.00 32.82  ? 69  ASN A CB  1 
ATOM   546  C  CG  . ASN A 1 69  ? -8.564  7.572   7.489   1.00 35.41  ? 69  ASN A CG  1 
ATOM   547  O  OD1 . ASN A 1 69  ? -9.204  6.552   7.252   1.00 33.14  ? 69  ASN A OD1 1 
ATOM   548  N  ND2 . ASN A 1 69  ? -7.237  7.553   7.803   1.00 32.91  ? 69  ASN A ND2 1 
ATOM   549  N  N   . GLY A 1 70  ? -11.809 7.016   5.744   1.00 33.54  ? 70  GLY A N   1 
ATOM   550  C  CA  . GLY A 1 70  ? -11.973 6.208   4.534   1.00 31.40  ? 70  GLY A CA  1 
ATOM   551  C  C   . GLY A 1 70  ? -10.918 5.136   4.315   1.00 32.56  ? 70  GLY A C   1 
ATOM   552  O  O   . GLY A 1 70  ? -11.034 4.358   3.367   1.00 29.69  ? 70  GLY A O   1 
ATOM   553  N  N   . HIS A 1 71  ? -9.905  5.062   5.180   1.00 30.75  ? 71  HIS A N   1 
ATOM   554  C  CA  . HIS A 1 71  ? -8.920  3.967   5.079   1.00 33.64  ? 71  HIS A CA  1 
ATOM   555  C  C   . HIS A 1 71  ? -8.763  3.164   6.338   1.00 31.37  ? 71  HIS A C   1 
ATOM   556  O  O   . HIS A 1 71  ? -8.399  1.965   6.298   1.00 27.62  ? 71  HIS A O   1 
ATOM   557  C  CB  . HIS A 1 71  ? -7.566  4.489   4.676   1.00 36.53  ? 71  HIS A CB  1 
ATOM   558  C  CG  . HIS A 1 71  ? -7.560  5.216   3.370   1.00 44.80  ? 71  HIS A CG  1 
ATOM   559  N  ND1 . HIS A 1 71  ? -7.920  4.632   2.217   1.00 48.04  ? 71  HIS A ND1 1 
ATOM   560  C  CD2 . HIS A 1 71  ? -7.188  6.519   3.057   1.00 44.84  ? 71  HIS A CD2 1 
ATOM   561  C  CE1 . HIS A 1 71  ? -7.781  5.515   1.213   1.00 47.39  ? 71  HIS A CE1 1 
ATOM   562  N  NE2 . HIS A 1 71  ? -7.323  6.666   1.731   1.00 49.08  ? 71  HIS A NE2 1 
ATOM   563  N  N   . SER A 1 72  ? -8.983  3.842   7.471   1.00 26.98  ? 72  SER A N   1 
ATOM   564  C  CA  . SER A 1 72  ? -8.892  3.228   8.752   1.00 27.26  ? 72  SER A CA  1 
ATOM   565  C  C   . SER A 1 72  ? -9.812  4.028   9.686   1.00 28.42  ? 72  SER A C   1 
ATOM   566  O  O   . SER A 1 72  ? -10.472 4.972   9.249   1.00 25.71  ? 72  SER A O   1 
ATOM   567  C  CB  . SER A 1 72  ? -7.471  3.357   9.243   1.00 26.38  ? 72  SER A CB  1 
ATOM   568  O  OG  . SER A 1 72  ? -7.367  2.600   10.417  1.00 26.66  ? 72  SER A OG  1 
ATOM   569  N  N   . VAL A 1 73  ? -9.829  3.674   10.965  1.00 26.44  ? 73  VAL A N   1 
ATOM   570  C  CA  . VAL A 1 73  ? -10.365 4.613   12.007  1.00 28.08  ? 73  VAL A CA  1 
ATOM   571  C  C   . VAL A 1 73  ? -9.158  5.152   12.794  1.00 30.91  ? 73  VAL A C   1 
ATOM   572  O  O   . VAL A 1 73  ? -8.317  4.367   13.249  1.00 31.32  ? 73  VAL A O   1 
ATOM   573  C  CB  . VAL A 1 73  ? -11.416 3.938   12.928  1.00 28.87  ? 73  VAL A CB  1 
ATOM   574  C  CG1 . VAL A 1 73  ? -10.953 2.538   13.368  1.00 29.79  ? 73  VAL A CG1 1 
ATOM   575  C  CG2 . VAL A 1 73  ? -11.712 4.743   14.192  1.00 27.06  ? 73  VAL A CG2 1 
ATOM   576  N  N   . MET A 1 74  ? -9.049  6.476   12.935  1.00 28.90  ? 74  MET A N   1 
ATOM   577  C  CA  . MET A 1 74  ? -7.864  7.115   13.503  1.00 28.77  ? 74  MET A CA  1 
ATOM   578  C  C   . MET A 1 74  ? -8.207  8.017   14.684  1.00 31.63  ? 74  MET A C   1 
ATOM   579  O  O   . MET A 1 74  ? -9.126  8.845   14.580  1.00 30.94  ? 74  MET A O   1 
ATOM   580  C  CB  . MET A 1 74  ? -7.236  8.004   12.441  1.00 31.94  ? 74  MET A CB  1 
ATOM   581  C  CG  . MET A 1 74  ? -5.867  8.540   12.748  1.00 32.41  ? 74  MET A CG  1 
ATOM   582  S  SD  . MET A 1 74  ? -5.312  9.599   11.389  1.00 42.07  ? 74  MET A SD  1 
ATOM   583  C  CE  . MET A 1 74  ? -4.006  8.601   10.724  1.00 37.43  ? 74  MET A CE  1 
ATOM   584  N  N   . MET A 1 75  ? -7.443  7.923   15.776  1.00 28.28  ? 75  MET A N   1 
ATOM   585  C  CA  . MET A 1 75  ? -7.605  8.870   16.856  1.00 32.28  ? 75  MET A CA  1 
ATOM   586  C  C   . MET A 1 75  ? -6.464  9.863   16.819  1.00 34.19  ? 75  MET A C   1 
ATOM   587  O  O   . MET A 1 75  ? -5.338  9.526   16.478  1.00 39.07  ? 75  MET A O   1 
ATOM   588  C  CB  . MET A 1 75  ? -7.862  8.227   18.253  1.00 30.02  ? 75  MET A CB  1 
ATOM   589  C  CG  . MET A 1 75  ? -7.146  6.965   18.602  1.00 31.40  ? 75  MET A CG  1 
ATOM   590  S  SD  . MET A 1 75  ? -7.960  5.960   19.879  1.00 28.92  ? 75  MET A SD  1 
ATOM   591  C  CE  . MET A 1 75  ? -7.422  6.867   21.324  1.00 25.53  ? 75  MET A CE  1 
ATOM   592  N  N   . LEU A 1 76  ? -6.768  11.112  17.083  1.00 31.45  ? 76  LEU A N   1 
ATOM   593  C  CA  . LEU A 1 76  ? -5.763  12.123  16.931  1.00 31.66  ? 76  LEU A CA  1 
ATOM   594  C  C   . LEU A 1 76  ? -5.221  12.377  18.321  1.00 32.07  ? 76  LEU A C   1 
ATOM   595  O  O   . LEU A 1 76  ? -5.988  12.690  19.234  1.00 32.04  ? 76  LEU A O   1 
ATOM   596  C  CB  . LEU A 1 76  ? -6.393  13.391  16.338  1.00 34.46  ? 76  LEU A CB  1 
ATOM   597  C  CG  . LEU A 1 76  ? -7.153  13.476  15.013  1.00 36.78  ? 76  LEU A CG  1 
ATOM   598  C  CD1 . LEU A 1 76  ? -7.300  14.947  14.615  1.00 36.84  ? 76  LEU A CD1 1 
ATOM   599  C  CD2 . LEU A 1 76  ? -6.467  12.730  13.878  1.00 40.12  ? 76  LEU A CD2 1 
ATOM   600  N  N   . LEU A 1 77  ? -3.904  12.219  18.487  1.00 31.44  ? 77  LEU A N   1 
ATOM   601  C  CA  . LEU A 1 77  ? -3.271  12.283  19.808  1.00 32.92  ? 77  LEU A CA  1 
ATOM   602  C  C   . LEU A 1 77  ? -2.585  13.638  20.116  1.00 35.66  ? 77  LEU A C   1 
ATOM   603  O  O   . LEU A 1 77  ? -2.129  13.884  21.262  1.00 36.10  ? 77  LEU A O   1 
ATOM   604  C  CB  . LEU A 1 77  ? -2.287  11.101  20.006  1.00 29.39  ? 77  LEU A CB  1 
ATOM   605  C  CG  . LEU A 1 77  ? -2.799  9.702   19.606  1.00 29.70  ? 77  LEU A CG  1 
ATOM   606  C  CD1 . LEU A 1 77  ? -1.819  8.613   20.045  1.00 25.67  ? 77  LEU A CD1 1 
ATOM   607  C  CD2 . LEU A 1 77  ? -4.218  9.413   20.094  1.00 26.59  ? 77  LEU A CD2 1 
ATOM   608  N  N   . GLU A 1 78  ? -2.504  14.484  19.084  1.00 37.99  ? 78  GLU A N   1 
ATOM   609  C  CA  . GLU A 1 78  ? -2.053  15.878  19.176  1.00 44.49  ? 78  GLU A CA  1 
ATOM   610  C  C   . GLU A 1 78  ? -0.883  16.099  20.094  1.00 43.82  ? 78  GLU A C   1 
ATOM   611  O  O   . GLU A 1 78  ? -0.941  16.962  20.973  1.00 51.23  ? 78  GLU A O   1 
ATOM   612  C  CB  . GLU A 1 78  ? -3.189  16.831  19.602  1.00 43.06  ? 78  GLU A CB  1 
ATOM   613  C  CG  . GLU A 1 78  ? -4.558  16.577  18.999  1.00 46.70  ? 78  GLU A CG  1 
ATOM   614  C  CD  . GLU A 1 78  ? -5.686  17.210  19.814  1.00 52.61  ? 78  GLU A CD  1 
ATOM   615  O  OE1 . GLU A 1 78  ? -5.412  18.147  20.619  1.00 50.19  ? 78  GLU A OE1 1 
ATOM   616  O  OE2 . GLU A 1 78  ? -6.853  16.761  19.653  1.00 51.22  ? 78  GLU A OE2 1 
ATOM   617  N  N   . ASN A 1 79  ? 0.153   15.289  19.923  1.00 38.05  ? 79  ASN A N   1 
ATOM   618  C  CA  . ASN A 1 79  ? 1.406   15.420  20.669  1.00 38.17  ? 79  ASN A CA  1 
ATOM   619  C  C   . ASN A 1 79  ? 1.226   15.392  22.212  1.00 38.28  ? 79  ASN A C   1 
ATOM   620  O  O   . ASN A 1 79  ? 2.118   15.778  22.958  1.00 38.84  ? 79  ASN A O   1 
ATOM   621  C  CB  . ASN A 1 79  ? 2.304   16.555  20.144  1.00 41.65  ? 79  ASN A CB  1 
ATOM   622  C  CG  . ASN A 1 79  ? 2.526   16.464  18.628  1.00 45.38  ? 79  ASN A CG  1 
ATOM   623  O  OD1 . ASN A 1 79  ? 3.634   16.193  18.155  1.00 44.18  ? 79  ASN A OD1 1 
ATOM   624  N  ND2 . ASN A 1 79  ? 1.464   16.663  17.866  1.00 44.37  ? 79  ASN A ND2 1 
ATOM   625  N  N   . LYS A 1 80  ? 0.102   14.853  22.682  1.00 41.84  ? 80  LYS A N   1 
ATOM   626  C  CA  . LYS A 1 80  ? -0.210  14.865  24.124  1.00 40.90  ? 80  LYS A CA  1 
ATOM   627  C  C   . LYS A 1 80  ? 0.259   13.665  24.908  1.00 41.82  ? 80  LYS A C   1 
ATOM   628  O  O   . LYS A 1 80  ? -0.130  13.473  26.075  1.00 45.07  ? 80  LYS A O   1 
ATOM   629  C  CB  . LYS A 1 80  ? -1.711  15.054  24.319  1.00 40.68  ? 80  LYS A CB  1 
ATOM   630  C  CG  . LYS A 1 80  ? -2.151  16.486  24.094  1.00 39.30  ? 80  LYS A CG  1 
ATOM   631  C  CD  . LYS A 1 80  ? -3.567  16.482  23.579  1.00 42.59  ? 80  LYS A CD  1 
ATOM   632  C  CE  . LYS A 1 80  ? -4.323  17.760  23.871  1.00 43.09  ? 80  LYS A CE  1 
ATOM   633  N  NZ  . LYS A 1 80  ? -5.771  17.382  23.946  1.00 39.16  ? 80  LYS A NZ  1 
ATOM   634  N  N   . ALA A 1 81  ? 1.086   12.846  24.262  1.00 39.36  ? 81  ALA A N   1 
ATOM   635  C  CA  . ALA A 1 81  ? 1.704   11.697  24.908  1.00 34.51  ? 81  ALA A CA  1 
ATOM   636  C  C   . ALA A 1 81  ? 3.081   11.502  24.301  1.00 32.01  ? 81  ALA A C   1 
ATOM   637  O  O   . ALA A 1 81  ? 3.353   11.992  23.184  1.00 31.40  ? 81  ALA A O   1 
ATOM   638  C  CB  . ALA A 1 81  ? 0.845   10.469  24.708  1.00 32.38  ? 81  ALA A CB  1 
ATOM   639  N  N   . SER A 1 82  ? 3.958   10.794  24.990  1.00 31.33  ? 82  SER A N   1 
ATOM   640  C  CA  . SER A 1 82  ? 5.313   10.641  24.435  1.00 33.04  ? 82  SER A CA  1 
ATOM   641  C  C   . SER A 1 82  ? 6.038   9.367   24.851  1.00 29.89  ? 82  SER A C   1 
ATOM   642  O  O   . SER A 1 82  ? 5.644   8.737   25.821  1.00 32.31  ? 82  SER A O   1 
ATOM   643  C  CB  . SER A 1 82  ? 6.152   11.889  24.740  1.00 36.01  ? 82  SER A CB  1 
ATOM   644  O  OG  . SER A 1 82  ? 6.603   11.837  26.092  1.00 43.44  ? 82  SER A OG  1 
ATOM   645  N  N   . ILE A 1 83  ? 7.103   8.985   24.123  1.00 27.88  ? 83  ILE A N   1 
ATOM   646  C  CA  . ILE A 1 83  ? 7.844   7.743   24.405  1.00 29.38  ? 83  ILE A CA  1 
ATOM   647  C  C   . ILE A 1 83  ? 9.355   7.945   24.315  1.00 31.64  ? 83  ILE A C   1 
ATOM   648  O  O   . ILE A 1 83  ? 9.825   8.826   23.594  1.00 29.98  ? 83  ILE A O   1 
ATOM   649  C  CB  . ILE A 1 83  ? 7.427   6.521   23.531  1.00 31.08  ? 83  ILE A CB  1 
ATOM   650  C  CG1 . ILE A 1 83  ? 7.872   6.678   22.052  1.00 29.05  ? 83  ILE A CG1 1 
ATOM   651  C  CG2 . ILE A 1 83  ? 5.927   6.236   23.633  1.00 30.72  ? 83  ILE A CG2 1 
ATOM   652  C  CD1 . ILE A 1 83  ? 7.436   5.530   21.145  1.00 29.02  ? 83  ILE A CD1 1 
ATOM   653  N  N   . SER A 1 84  ? 10.086  7.128   25.073  1.00 31.91  ? 84  SER A N   1 
ATOM   654  C  CA  . SER A 1 84  ? 11.510  7.216   25.197  1.00 34.38  ? 84  SER A CA  1 
ATOM   655  C  C   . SER A 1 84  ? 11.880  5.803   25.532  1.00 36.38  ? 84  SER A C   1 
ATOM   656  O  O   . SER A 1 84  ? 10.996  4.977   25.821  1.00 35.80  ? 84  SER A O   1 
ATOM   657  C  CB  . SER A 1 84  ? 11.884  8.140   26.372  1.00 40.99  ? 84  SER A CB  1 
ATOM   658  O  OG  . SER A 1 84  ? 11.830  7.430   27.618  1.00 45.52  ? 84  SER A OG  1 
ATOM   659  N  N   . GLY A 1 85  ? 13.176  5.498   25.544  1.00 34.66  ? 85  GLY A N   1 
ATOM   660  C  CA  . GLY A 1 85  ? 13.577  4.138   25.797  1.00 32.68  ? 85  GLY A CA  1 
ATOM   661  C  C   . GLY A 1 85  ? 13.485  3.289   24.538  1.00 39.57  ? 85  GLY A C   1 
ATOM   662  O  O   . GLY A 1 85  ? 13.648  3.794   23.437  1.00 40.95  ? 85  GLY A O   1 
ATOM   663  N  N   . GLY A 1 86  ? 13.254  1.991   24.700  1.00 40.14  ? 86  GLY A N   1 
ATOM   664  C  CA  . GLY A 1 86  ? 13.129  1.087   23.543  1.00 47.33  ? 86  GLY A CA  1 
ATOM   665  C  C   . GLY A 1 86  ? 14.211  1.160   22.465  1.00 44.29  ? 86  GLY A C   1 
ATOM   666  O  O   . GLY A 1 86  ? 13.983  0.747   21.308  1.00 41.45  ? 86  GLY A O   1 
ATOM   667  N  N   . GLY A 1 87  ? 15.377  1.679   22.835  1.00 38.40  ? 87  GLY A N   1 
ATOM   668  C  CA  . GLY A 1 87  ? 16.521  1.728   21.930  1.00 39.99  ? 87  GLY A CA  1 
ATOM   669  C  C   . GLY A 1 87  ? 16.484  2.927   21.015  1.00 39.99  ? 87  GLY A C   1 
ATOM   670  O  O   . GLY A 1 87  ? 17.252  3.016   20.050  1.00 44.11  ? 87  GLY A O   1 
ATOM   671  N  N   . LEU A 1 88  ? 15.612  3.873   21.326  1.00 38.49  ? 88  LEU A N   1 
ATOM   672  C  CA  . LEU A 1 88  ? 15.386  5.019   20.474  1.00 39.33  ? 88  LEU A CA  1 
ATOM   673  C  C   . LEU A 1 88  ? 16.391  6.095   20.790  1.00 42.21  ? 88  LEU A C   1 
ATOM   674  O  O   . LEU A 1 88  ? 16.852  6.189   21.919  1.00 48.28  ? 88  LEU A O   1 
ATOM   675  C  CB  . LEU A 1 88  ? 13.947  5.551   20.608  1.00 38.85  ? 88  LEU A CB  1 
ATOM   676  C  CG  . LEU A 1 88  ? 12.794  4.648   20.136  1.00 38.96  ? 88  LEU A CG  1 
ATOM   677  C  CD1 . LEU A 1 88  ? 11.428  5.224   20.550  1.00 41.04  ? 88  LEU A CD1 1 
ATOM   678  C  CD2 . LEU A 1 88  ? 12.864  4.447   18.617  1.00 38.99  ? 88  LEU A CD2 1 
ATOM   679  N  N   . PRO A 1 89  ? 16.739  6.907   19.780  1.00 44.60  ? 89  PRO A N   1 
ATOM   680  C  CA  . PRO A 1 89  ? 17.716  7.976   19.869  1.00 44.09  ? 89  PRO A CA  1 
ATOM   681  C  C   . PRO A 1 89  ? 17.233  9.218   20.605  1.00 48.39  ? 89  PRO A C   1 
ATOM   682  O  O   . PRO A 1 89  ? 18.034  10.123  20.872  1.00 50.19  ? 89  PRO A O   1 
ATOM   683  C  CB  . PRO A 1 89  ? 17.961  8.334   18.391  1.00 44.38  ? 89  PRO A CB  1 
ATOM   684  C  CG  . PRO A 1 89  ? 16.681  7.979   17.701  1.00 44.09  ? 89  PRO A CG  1 
ATOM   685  C  CD  . PRO A 1 89  ? 16.298  6.689   18.387  1.00 42.21  ? 89  PRO A CD  1 
ATOM   686  N  N   . ALA A 1 90  ? 15.941  9.283   20.900  1.00 44.44  ? 90  ALA A N   1 
ATOM   687  C  CA  . ALA A 1 90  ? 15.342  10.530  21.339  1.00 45.96  ? 90  ALA A CA  1 
ATOM   688  C  C   . ALA A 1 90  ? 13.891  10.302  21.708  1.00 46.83  ? 90  ALA A C   1 
ATOM   689  O  O   . ALA A 1 90  ? 13.361  9.199   21.516  1.00 43.93  ? 90  ALA A O   1 
ATOM   690  C  CB  . ALA A 1 90  ? 15.457  11.605  20.251  1.00 45.41  ? 90  ALA A CB  1 
ATOM   691  N  N   . PRO A 1 91  ? 13.241  11.334  22.273  1.00 48.11  ? 91  PRO A N   1 
ATOM   692  C  CA  . PRO A 1 91  ? 11.822  11.186  22.584  1.00 44.61  ? 91  PRO A CA  1 
ATOM   693  C  C   . PRO A 1 91  ? 10.952  11.377  21.364  1.00 40.68  ? 91  PRO A C   1 
ATOM   694  O  O   . PRO A 1 91  ? 11.290  12.170  20.481  1.00 41.57  ? 91  PRO A O   1 
ATOM   695  C  CB  . PRO A 1 91  ? 11.561  12.311  23.593  1.00 42.12  ? 91  PRO A CB  1 
ATOM   696  C  CG  . PRO A 1 91  ? 12.914  12.597  24.167  1.00 49.51  ? 91  PRO A CG  1 
ATOM   697  C  CD  . PRO A 1 91  ? 13.808  12.500  22.963  1.00 48.39  ? 91  PRO A CD  1 
ATOM   698  N  N   . TYR A 1 92  ? 9.817   10.683  21.346  1.00 35.73  ? 92  TYR A N   1 
ATOM   699  C  CA  . TYR A 1 92  ? 8.894   10.768  20.223  1.00 36.16  ? 92  TYR A CA  1 
ATOM   700  C  C   . TYR A 1 92  ? 7.477   11.142  20.676  1.00 35.08  ? 92  TYR A C   1 
ATOM   701  O  O   . TYR A 1 92  ? 6.909   10.510  21.596  1.00 29.35  ? 92  TYR A O   1 
ATOM   702  C  CB  . TYR A 1 92  ? 8.870   9.424   19.473  1.00 33.13  ? 92  TYR A CB  1 
ATOM   703  C  CG  . TYR A 1 92  ? 10.075  9.120   18.604  1.00 30.90  ? 92  TYR A CG  1 
ATOM   704  C  CD1 . TYR A 1 92  ? 11.298  8.865   19.168  1.00 34.34  ? 92  TYR A CD1 1 
ATOM   705  C  CD2 . TYR A 1 92  ? 9.972   9.019   17.208  1.00 30.96  ? 92  TYR A CD2 1 
ATOM   706  C  CE1 . TYR A 1 92  ? 12.426  8.566   18.394  1.00 31.71  ? 92  TYR A CE1 1 
ATOM   707  C  CE2 . TYR A 1 92  ? 11.096  8.709   16.416  1.00 28.13  ? 92  TYR A CE2 1 
ATOM   708  C  CZ  . TYR A 1 92  ? 12.318  8.488   17.040  1.00 32.46  ? 92  TYR A CZ  1 
ATOM   709  O  OH  . TYR A 1 92  ? 13.471  8.174   16.362  1.00 36.29  ? 92  TYR A OH  1 
ATOM   710  N  N   A GLN A 1 93  ? 6.911   12.145  20.010  0.50 35.70  ? 93  GLN A N   1 
ATOM   711  N  N   B GLN A 1 93  ? 6.908   12.150  20.015  0.50 35.10  ? 93  GLN A N   1 
ATOM   712  C  CA  A GLN A 1 93  ? 5.579   12.628  20.330  0.50 37.69  ? 93  GLN A CA  1 
ATOM   713  C  CA  B GLN A 1 93  ? 5.593   12.679  20.365  0.50 36.64  ? 93  GLN A CA  1 
ATOM   714  C  C   A GLN A 1 93  ? 4.492   11.859  19.594  0.50 37.59  ? 93  GLN A C   1 
ATOM   715  C  C   B GLN A 1 93  ? 4.449   11.968  19.610  0.50 36.81  ? 93  GLN A C   1 
ATOM   716  O  O   A GLN A 1 93  ? 4.493   11.768  18.354  0.50 35.47  ? 93  GLN A O   1 
ATOM   717  O  O   B GLN A 1 93  ? 4.392   11.994  18.367  0.50 34.24  ? 93  GLN A O   1 
ATOM   718  C  CB  A GLN A 1 93  ? 5.455   14.100  19.971  0.50 40.18  ? 93  GLN A CB  1 
ATOM   719  C  CB  B GLN A 1 93  ? 5.555   14.196  20.111  0.50 38.63  ? 93  GLN A CB  1 
ATOM   720  C  CG  A GLN A 1 93  ? 6.504   14.998  20.596  0.50 41.38  ? 93  GLN A CG  1 
ATOM   721  C  CG  B GLN A 1 93  ? 6.744   14.987  20.674  0.50 38.17  ? 93  GLN A CG  1 
ATOM   722  C  CD  A GLN A 1 93  ? 6.978   16.025  19.604  0.50 41.43  ? 93  GLN A CD  1 
ATOM   723  C  CD  B GLN A 1 93  ? 6.460   15.659  22.009  0.50 37.75  ? 93  GLN A CD  1 
ATOM   724  O  OE1 A GLN A 1 93  ? 6.627   17.194  19.697  0.50 39.96  ? 93  GLN A OE1 1 
ATOM   725  O  OE1 B GLN A 1 93  ? 5.356   15.567  22.540  0.50 34.92  ? 93  GLN A OE1 1 
ATOM   726  N  NE2 A GLN A 1 93  ? 7.740   15.574  18.604  0.50 40.91  ? 93  GLN A NE2 1 
ATOM   727  N  NE2 B GLN A 1 93  ? 7.470   16.341  22.563  0.50 37.68  ? 93  GLN A NE2 1 
ATOM   728  N  N   . ALA A 1 94  ? 3.554   11.340  20.370  1.00 33.05  ? 94  ALA A N   1 
ATOM   729  C  CA  . ALA A 1 94  ? 2.391   10.655  19.833  1.00 34.70  ? 94  ALA A CA  1 
ATOM   730  C  C   . ALA A 1 94  ? 1.498   11.566  18.958  1.00 37.97  ? 94  ALA A C   1 
ATOM   731  O  O   . ALA A 1 94  ? 1.001   12.595  19.453  1.00 41.82  ? 94  ALA A O   1 
ATOM   732  C  CB  . ALA A 1 94  ? 1.593   10.044  20.973  1.00 34.10  ? 94  ALA A CB  1 
ATOM   733  N  N   . LYS A 1 95  ? 1.311   11.185  17.680  1.00 31.44  ? 95  LYS A N   1 
ATOM   734  C  CA  . LYS A 1 95  ? 0.466   11.911  16.709  1.00 30.35  ? 95  LYS A CA  1 
ATOM   735  C  C   . LYS A 1 95  ? -0.900  11.307  16.478  1.00 28.90  ? 95  LYS A C   1 
ATOM   736  O  O   . LYS A 1 95  ? -1.924  12.015  16.477  1.00 27.28  ? 95  LYS A O   1 
ATOM   737  C  CB  . LYS A 1 95  ? 1.162   12.006  15.331  1.00 33.97  ? 95  LYS A CB  1 
ATOM   738  C  CG  . LYS A 1 95  ? 2.583   12.546  15.347  1.00 34.58  ? 95  LYS A CG  1 
ATOM   739  C  CD  . LYS A 1 95  ? 2.617   14.053  15.557  1.00 37.73  ? 95  LYS A CD  1 
ATOM   740  C  CE  . LYS A 1 95  ? 3.922   14.602  15.009  1.00 42.05  ? 95  LYS A CE  1 
ATOM   741  N  NZ  . LYS A 1 95  ? 4.351   15.889  15.642  1.00 46.93  ? 95  LYS A NZ  1 
ATOM   742  N  N   . GLN A 1 96  ? -0.944  9.989   16.253  1.00 23.95  ? 96  GLN A N   1 
ATOM   743  C  CA  . GLN A 1 96  ? -2.209  9.355   15.952  1.00 22.97  ? 96  GLN A CA  1 
ATOM   744  C  C   . GLN A 1 96  ? -2.125  7.824   16.214  1.00 21.20  ? 96  GLN A C   1 
ATOM   745  O  O   . GLN A 1 96  ? -1.044  7.304   16.423  1.00 22.36  ? 96  GLN A O   1 
ATOM   746  C  CB  . GLN A 1 96  ? -2.663  9.729   14.523  1.00 25.22  ? 96  GLN A CB  1 
ATOM   747  C  CG  . GLN A 1 96  ? -1.578  9.549   13.460  1.00 23.82  ? 96  GLN A CG  1 
ATOM   748  C  CD  . GLN A 1 96  ? -1.774  8.249   12.676  1.00 29.57  ? 96  GLN A CD  1 
ATOM   749  O  OE1 . GLN A 1 96  ? -2.463  7.331   13.136  1.00 29.58  ? 96  GLN A OE1 1 
ATOM   750  N  NE2 . GLN A 1 96  ? -1.151  8.164   11.487  1.00 31.18  ? 96  GLN A NE2 1 
ATOM   751  N  N   . LEU A 1 97  ? -3.268  7.179   16.377  1.00 20.49  ? 97  LEU A N   1 
ATOM   752  C  CA  . LEU A 1 97  ? -3.347  5.731   16.561  1.00 23.98  ? 97  LEU A CA  1 
ATOM   753  C  C   . LEU A 1 97  ? -4.445  5.288   15.616  1.00 21.63  ? 97  LEU A C   1 
ATOM   754  O  O   . LEU A 1 97  ? -5.496  5.926   15.540  1.00 21.94  ? 97  LEU A O   1 
ATOM   755  C  CB  . LEU A 1 97  ? -3.761  5.412   18.010  1.00 25.32  ? 97  LEU A CB  1 
ATOM   756  C  CG  . LEU A 1 97  ? -3.945  3.993   18.521  1.00 25.23  ? 97  LEU A CG  1 
ATOM   757  C  CD1 . LEU A 1 97  ? -3.973  4.078   20.052  1.00 25.99  ? 97  LEU A CD1 1 
ATOM   758  C  CD2 . LEU A 1 97  ? -5.211  3.303   18.032  1.00 26.01  ? 97  LEU A CD2 1 
ATOM   759  N  N   . HIS A 1 98  ? -4.200  4.230   14.873  1.00 20.06  ? 98  HIS A N   1 
ATOM   760  C  CA  . HIS A 1 98  ? -5.173  3.671   13.957  1.00 19.08  ? 98  HIS A CA  1 
ATOM   761  C  C   . HIS A 1 98  ? -4.992  2.180   13.897  1.00 20.34  ? 98  HIS A C   1 
ATOM   762  O  O   . HIS A 1 98  ? -4.036  1.652   14.455  1.00 19.78  ? 98  HIS A O   1 
ATOM   763  C  CB  . HIS A 1 98  ? -4.962  4.284   12.552  1.00 19.44  ? 98  HIS A CB  1 
ATOM   764  C  CG  . HIS A 1 98  ? -3.638  3.911   11.894  1.00 18.89  ? 98  HIS A CG  1 
ATOM   765  N  ND1 . HIS A 1 98  ? -2.583  4.711   11.928  1.00 17.19  ? 98  HIS A ND1 1 
ATOM   766  C  CD2 . HIS A 1 98  ? -3.259  2.790   11.136  1.00 22.34  ? 98  HIS A CD2 1 
ATOM   767  C  CE1 . HIS A 1 98  ? -1.536  4.146   11.277  1.00 21.99  ? 98  HIS A CE1 1 
ATOM   768  N  NE2 . HIS A 1 98  ? -1.958  2.993   10.730  1.00 20.80  ? 98  HIS A NE2 1 
ATOM   769  N  N   . LEU A 1 99  ? -5.889  1.483   13.194  1.00 23.30  ? 99  LEU A N   1 
ATOM   770  C  CA  . LEU A 1 99  ? -5.888  0.043   13.210  1.00 23.28  ? 99  LEU A CA  1 
ATOM   771  C  C   . LEU A 1 99  ? -5.991  -0.498  11.791  1.00 24.59  ? 99  LEU A C   1 
ATOM   772  O  O   . LEU A 1 99  ? -6.368  0.227   10.905  1.00 23.91  ? 99  LEU A O   1 
ATOM   773  C  CB  . LEU A 1 99  ? -7.025  -0.500  14.074  1.00 22.87  ? 99  LEU A CB  1 
ATOM   774  C  CG  . LEU A 1 99  ? -6.988  -0.099  15.557  1.00 25.68  ? 99  LEU A CG  1 
ATOM   775  C  CD1 . LEU A 1 99  ? -7.936  1.077   15.737  1.00 24.49  ? 99  LEU A CD1 1 
ATOM   776  C  CD2 . LEU A 1 99  ? -7.359  -1.255  16.471  1.00 23.67  ? 99  LEU A CD2 1 
ATOM   777  N  N   . HIS A 1 100 ? -5.643  -1.776  11.595  1.00 23.09  ? 100 HIS A N   1 
ATOM   778  C  CA  . HIS A 1 100 ? -5.970  -2.491  10.339  1.00 23.97  ? 100 HIS A CA  1 
ATOM   779  C  C   . HIS A 1 100 ? -6.636  -3.727  10.754  1.00 25.87  ? 100 HIS A C   1 
ATOM   780  O  O   . HIS A 1 100 ? -6.257  -4.278  11.789  1.00 27.61  ? 100 HIS A O   1 
ATOM   781  C  CB  . HIS A 1 100 ? -4.668  -2.798  9.574   1.00 23.62  ? 100 HIS A CB  1 
ATOM   782  C  CG  . HIS A 1 100 ? -3.819  -1.562  9.333   1.00 22.26  ? 100 HIS A CG  1 
ATOM   783  N  ND1 . HIS A 1 100 ? -3.902  -0.837  8.204   1.00 21.53  ? 100 HIS A ND1 1 
ATOM   784  C  CD2 . HIS A 1 100 ? -2.863  -0.947  10.113  1.00 23.74  ? 100 HIS A CD2 1 
ATOM   785  C  CE1 . HIS A 1 100 ? -3.060  0.166   8.237   1.00 20.96  ? 100 HIS A CE1 1 
ATOM   786  N  NE2 . HIS A 1 100 ? -2.414  0.123   9.420   1.00 23.82  ? 100 HIS A NE2 1 
ATOM   787  N  N   . TRP A 1 101 ? -7.645  -4.177  10.004  1.00 29.14  ? 101 TRP A N   1 
ATOM   788  C  CA  . TRP A 1 101 ? -8.371  -5.397  10.370  1.00 29.92  ? 101 TRP A CA  1 
ATOM   789  C  C   . TRP A 1 101 ? -8.955  -6.153  9.216   1.00 31.47  ? 101 TRP A C   1 
ATOM   790  O  O   . TRP A 1 101 ? -9.096  -5.628  8.135   1.00 28.53  ? 101 TRP A O   1 
ATOM   791  C  CB  . TRP A 1 101 ? -9.497  -5.120  11.361  1.00 26.79  ? 101 TRP A CB  1 
ATOM   792  C  CG  . TRP A 1 101 ? -10.585 -4.247  10.807  1.00 28.56  ? 101 TRP A CG  1 
ATOM   793  C  CD1 . TRP A 1 101 ? -11.792 -4.641  10.222  1.00 28.50  ? 101 TRP A CD1 1 
ATOM   794  C  CD2 . TRP A 1 101 ? -10.616 -2.785  10.806  1.00 25.49  ? 101 TRP A CD2 1 
ATOM   795  N  NE1 . TRP A 1 101 ? -12.545 -3.541  9.863   1.00 27.87  ? 101 TRP A NE1 1 
ATOM   796  C  CE2 . TRP A 1 101 ? -11.888 -2.398  10.183  1.00 28.84  ? 101 TRP A CE2 1 
ATOM   797  C  CE3 . TRP A 1 101 ? -9.744  -1.792  11.237  1.00 30.38  ? 101 TRP A CE3 1 
ATOM   798  C  CZ2 . TRP A 1 101 ? -12.255 -1.067  10.022  1.00 25.37  ? 101 TRP A CZ2 1 
ATOM   799  C  CZ3 . TRP A 1 101 ? -10.121 -0.434  11.056  1.00 25.87  ? 101 TRP A CZ3 1 
ATOM   800  C  CH2 . TRP A 1 101 ? -11.350 -0.100  10.470  1.00 25.03  ? 101 TRP A CH2 1 
ATOM   801  N  N   . SER A 1 102 ? -9.319  -7.408  9.486   1.00 33.74  ? 102 SER A N   1 
ATOM   802  C  CA  . SER A 1 102 ? -10.206 -8.176  8.619   1.00 36.68  ? 102 SER A CA  1 
ATOM   803  C  C   . SER A 1 102 ? -11.446 -8.663  9.395   1.00 42.95  ? 102 SER A C   1 
ATOM   804  O  O   . SER A 1 102 ? -11.667 -8.270  10.571  1.00 45.96  ? 102 SER A O   1 
ATOM   805  C  CB  . SER A 1 102 ? -9.456  -9.390  8.057   1.00 37.72  ? 102 SER A CB  1 
ATOM   806  O  OG  . SER A 1 102 ? -10.224 -10.085 7.076   1.00 35.60  ? 102 SER A OG  1 
ATOM   807  N  N   . ASP A 1 103 ? -12.241 -9.533  8.758   1.00 40.24  ? 103 ASP A N   1 
ATOM   808  C  CA  . ASP A 1 103 ? -13.328 -10.218 9.460   1.00 43.48  ? 103 ASP A CA  1 
ATOM   809  C  C   . ASP A 1 103 ? -13.005 -11.697 9.716   1.00 42.49  ? 103 ASP A C   1 
ATOM   810  O  O   . ASP A 1 103 ? -13.834 -12.461 10.176  1.00 41.49  ? 103 ASP A O   1 
ATOM   811  C  CB  . ASP A 1 103 ? -14.663 -10.039 8.710   1.00 44.58  ? 103 ASP A CB  1 
ATOM   812  C  CG  . ASP A 1 103 ? -14.661 -10.666 7.294   1.00 43.98  ? 103 ASP A CG  1 
ATOM   813  O  OD1 . ASP A 1 103 ? -13.690 -11.347 6.896   1.00 44.54  ? 103 ASP A OD1 1 
ATOM   814  O  OD2 . ASP A 1 103 ? -15.652 -10.461 6.572   1.00 42.49  ? 103 ASP A OD2 1 
ATOM   815  N  N   . LEU A 1 104 ? -11.790 -12.099 9.389   1.00 45.49  ? 104 LEU A N   1 
ATOM   816  C  CA  . LEU A 1 104 ? -11.377 -13.471 9.573   1.00 47.22  ? 104 LEU A CA  1 
ATOM   817  C  C   . LEU A 1 104 ? -10.110 -13.424 10.421  1.00 44.91  ? 104 LEU A C   1 
ATOM   818  O  O   . LEU A 1 104 ? -9.228  -12.616 10.154  1.00 43.51  ? 104 LEU A O   1 
ATOM   819  C  CB  . LEU A 1 104 ? -11.177 -14.169 8.215   1.00 44.61  ? 104 LEU A CB  1 
ATOM   820  C  CG  . LEU A 1 104 ? -12.435 -14.587 7.428   1.00 52.50  ? 104 LEU A CG  1 
ATOM   821  C  CD1 . LEU A 1 104 ? -12.186 -14.826 5.933   1.00 47.84  ? 104 LEU A CD1 1 
ATOM   822  C  CD2 . LEU A 1 104 ? -13.119 -15.815 8.029   1.00 46.21  ? 104 LEU A CD2 1 
ATOM   823  N  N   . PRO A 1 105 ? -10.041 -14.257 11.484  1.00 48.27  ? 105 PRO A N   1 
ATOM   824  C  CA  . PRO A 1 105 ? -8.934  -14.255 12.460  1.00 47.68  ? 105 PRO A CA  1 
ATOM   825  C  C   . PRO A 1 105 ? -7.539  -14.368 11.840  1.00 45.33  ? 105 PRO A C   1 
ATOM   826  O  O   . PRO A 1 105 ? -6.542  -13.980 12.459  1.00 40.14  ? 105 PRO A O   1 
ATOM   827  C  CB  . PRO A 1 105 ? -9.214  -15.504 13.325  1.00 48.79  ? 105 PRO A CB  1 
ATOM   828  C  CG  . PRO A 1 105 ? -10.277 -16.281 12.602  1.00 49.14  ? 105 PRO A CG  1 
ATOM   829  C  CD  . PRO A 1 105 ? -11.065 -15.263 11.832  1.00 48.77  ? 105 PRO A CD  1 
ATOM   830  N  N   . TYR A 1 106 ? -7.452  -14.903 10.631  1.00 49.36  ? 106 TYR A N   1 
ATOM   831  C  CA  . TYR A 1 106 ? -6.126  -15.153 10.077  1.00 51.41  ? 106 TYR A CA  1 
ATOM   832  C  C   . TYR A 1 106 ? -5.596  -14.074 9.121   1.00 47.40  ? 106 TYR A C   1 
ATOM   833  O  O   . TYR A 1 106 ? -4.487  -14.213 8.604   1.00 49.56  ? 106 TYR A O   1 
ATOM   834  C  CB  . TYR A 1 106 ? -6.011  -16.580 9.484   1.00 54.70  ? 106 TYR A CB  1 
ATOM   835  C  CG  . TYR A 1 106 ? -6.920  -16.865 8.292   1.00 59.34  ? 106 TYR A CG  1 
ATOM   836  C  CD1 . TYR A 1 106 ? -6.511  -16.552 6.986   1.00 58.92  ? 106 TYR A CD1 1 
ATOM   837  C  CD2 . TYR A 1 106 ? -8.190  -17.444 8.468   1.00 56.43  ? 106 TYR A CD2 1 
ATOM   838  C  CE1 . TYR A 1 106 ? -7.333  -16.799 5.897   1.00 58.05  ? 106 TYR A CE1 1 
ATOM   839  C  CE2 . TYR A 1 106 ? -9.017  -17.694 7.386   1.00 52.97  ? 106 TYR A CE2 1 
ATOM   840  C  CZ  . TYR A 1 106 ? -8.582  -17.368 6.102   1.00 58.56  ? 106 TYR A CZ  1 
ATOM   841  O  OH  . TYR A 1 106 ? -9.378  -17.599 5.007   1.00 59.33  ? 106 TYR A OH  1 
ATOM   842  N  N   . LYS A 1 107 ? -6.333  -12.993 8.877   1.00 44.97  ? 107 LYS A N   1 
ATOM   843  C  CA  . LYS A 1 107 ? -5.848  -12.111 7.811   1.00 46.80  ? 107 LYS A CA  1 
ATOM   844  C  C   . LYS A 1 107 ? -5.829  -10.565 7.976   1.00 44.68  ? 107 LYS A C   1 
ATOM   845  O  O   . LYS A 1 107 ? -5.462  -9.833  7.032   1.00 44.32  ? 107 LYS A O   1 
ATOM   846  C  CB  . LYS A 1 107 ? -6.430  -12.545 6.451   1.00 47.92  ? 107 LYS A CB  1 
ATOM   847  C  CG  . LYS A 1 107 ? -7.936  -12.456 6.303   1.00 48.54  ? 107 LYS A CG  1 
ATOM   848  C  CD  . LYS A 1 107 ? -8.308  -12.847 4.873   1.00 54.54  ? 107 LYS A CD  1 
ATOM   849  C  CE  . LYS A 1 107 ? -9.565  -12.138 4.356   1.00 54.42  ? 107 LYS A CE  1 
ATOM   850  N  NZ  . LYS A 1 107 ? -9.618  -12.060 2.857   1.00 50.11  ? 107 LYS A NZ  1 
ATOM   851  N  N   . GLY A 1 108 ? -6.158  -10.087 9.173   1.00 39.93  ? 108 GLY A N   1 
ATOM   852  C  CA  . GLY A 1 108 ? -6.331  -8.647  9.446   1.00 31.31  ? 108 GLY A CA  1 
ATOM   853  C  C   . GLY A 1 108 ? -5.067  -7.921  9.857   1.00 29.59  ? 108 GLY A C   1 
ATOM   854  O  O   . GLY A 1 108 ? -5.020  -6.682  9.917   1.00 29.89  ? 108 GLY A O   1 
ATOM   855  N  N   . SER A 1 109 ? -4.025  -8.670  10.153  1.00 26.68  ? 109 SER A N   1 
ATOM   856  C  CA  . SER A 1 109 ? -2.802  -8.001  10.562  1.00 27.80  ? 109 SER A CA  1 
ATOM   857  C  C   . SER A 1 109 ? -1.902  -7.659  9.361   1.00 26.97  ? 109 SER A C   1 
ATOM   858  O  O   . SER A 1 109 ? -1.978  -8.319  8.336   1.00 24.91  ? 109 SER A O   1 
ATOM   859  C  CB  . SER A 1 109 ? -2.055  -8.821  11.604  1.00 27.86  ? 109 SER A CB  1 
ATOM   860  O  OG  . SER A 1 109 ? -1.152  -9.713  11.003  1.00 26.27  ? 109 SER A OG  1 
ATOM   861  N  N   . GLU A 1 110 ? -1.049  -6.636  9.505   1.00 25.21  ? 110 GLU A N   1 
ATOM   862  C  CA  . GLU A 1 110 ? -0.133  -6.263  8.432   1.00 24.11  ? 110 GLU A CA  1 
ATOM   863  C  C   . GLU A 1 110 ? 1.189   -6.934  8.638   1.00 25.92  ? 110 GLU A C   1 
ATOM   864  O  O   . GLU A 1 110 ? 1.804   -7.484  7.678   1.00 26.04  ? 110 GLU A O   1 
ATOM   865  C  CB  . GLU A 1 110 ? 0.096   -4.748  8.374   1.00 22.80  ? 110 GLU A CB  1 
ATOM   866  C  CG  . GLU A 1 110 ? -1.154  -3.955  8.027   1.00 22.49  ? 110 GLU A CG  1 
ATOM   867  C  CD  . GLU A 1 110 ? -0.834  -2.624  7.320   1.00 22.62  ? 110 GLU A CD  1 
ATOM   868  O  OE1 . GLU A 1 110 ? -0.115  -1.770  7.870   1.00 24.31  ? 110 GLU A OE1 1 
ATOM   869  O  OE2 . GLU A 1 110 ? -1.334  -2.440  6.202   1.00 21.84  ? 110 GLU A OE2 1 
ATOM   870  N  N   . HIS A 1 111 ? 1.649   -6.961  9.880   1.00 21.19  ? 111 HIS A N   1 
ATOM   871  C  CA  . HIS A 1 111 ? 2.794   -7.805  10.038  1.00 23.53  ? 111 HIS A CA  1 
ATOM   872  C  C   . HIS A 1 111 ? 2.355   -9.230  10.304  1.00 22.52  ? 111 HIS A C   1 
ATOM   873  O  O   . HIS A 1 111 ? 1.194   -9.485  10.652  1.00 20.67  ? 111 HIS A O   1 
ATOM   874  C  CB  . HIS A 1 111 ? 3.770   -7.295  11.069  1.00 22.20  ? 111 HIS A CB  1 
ATOM   875  C  CG  . HIS A 1 111 ? 4.484   -6.039  10.676  1.00 22.78  ? 111 HIS A CG  1 
ATOM   876  N  ND1 . HIS A 1 111 ? 3.931   -4.802  10.840  1.00 22.85  ? 111 HIS A ND1 1 
ATOM   877  C  CD2 . HIS A 1 111 ? 5.764   -5.837  10.182  1.00 21.96  ? 111 HIS A CD2 1 
ATOM   878  C  CE1 . HIS A 1 111 ? 4.819   -3.865  10.482  1.00 23.30  ? 111 HIS A CE1 1 
ATOM   879  N  NE2 . HIS A 1 111 ? 5.954   -4.491  10.091  1.00 25.36  ? 111 HIS A NE2 1 
ATOM   880  N  N   . SER A 1 112 ? 3.265   -10.173 10.059  1.00 27.37  ? 112 SER A N   1 
ATOM   881  C  CA  . SER A 1 112 ? 3.054   -11.579 10.480  1.00 28.69  ? 112 SER A CA  1 
ATOM   882  C  C   . SER A 1 112 ? 4.286   -12.032 11.260  1.00 28.54  ? 112 SER A C   1 
ATOM   883  O  O   . SER A 1 112 ? 5.371   -11.436 11.111  1.00 32.06  ? 112 SER A O   1 
ATOM   884  C  CB  . SER A 1 112 ? 2.769   -12.495 9.266   1.00 28.75  ? 112 SER A CB  1 
ATOM   885  O  OG  . SER A 1 112 ? 3.893   -12.545 8.419   1.00 26.77  ? 112 SER A OG  1 
ATOM   886  N  N   . LEU A 1 113 ? 4.125   -13.060 12.100  1.00 29.24  ? 113 LEU A N   1 
ATOM   887  C  CA  . LEU A 1 113 ? 5.216   -13.580 12.919  1.00 30.96  ? 113 LEU A CA  1 
ATOM   888  C  C   . LEU A 1 113 ? 5.420   -15.072 12.546  1.00 37.07  ? 113 LEU A C   1 
ATOM   889  O  O   . LEU A 1 113 ? 4.589   -15.912 12.878  1.00 34.26  ? 113 LEU A O   1 
ATOM   890  C  CB  . LEU A 1 113 ? 4.900   -13.455 14.432  1.00 31.19  ? 113 LEU A CB  1 
ATOM   891  C  CG  . LEU A 1 113 ? 4.607   -12.101 15.117  1.00 28.77  ? 113 LEU A CG  1 
ATOM   892  C  CD1 . LEU A 1 113 ? 4.511   -12.190 16.657  1.00 27.30  ? 113 LEU A CD1 1 
ATOM   893  C  CD2 . LEU A 1 113 ? 5.681   -11.098 14.735  1.00 24.55  ? 113 LEU A CD2 1 
ATOM   894  N  N   . ASP A 1 114 ? 6.517   -15.391 11.853  1.00 39.63  ? 114 ASP A N   1 
ATOM   895  C  CA  . ASP A 1 114 ? 6.804   -16.797 11.469  1.00 39.83  ? 114 ASP A CA  1 
ATOM   896  C  C   . ASP A 1 114 ? 5.646   -17.297 10.625  1.00 36.61  ? 114 ASP A C   1 
ATOM   897  O  O   . ASP A 1 114 ? 5.139   -18.397 10.849  1.00 35.28  ? 114 ASP A O   1 
ATOM   898  C  CB  . ASP A 1 114 ? 6.962   -17.739 12.702  1.00 38.01  ? 114 ASP A CB  1 
ATOM   899  C  CG  . ASP A 1 114 ? 8.198   -17.451 13.552  1.00 37.53  ? 114 ASP A CG  1 
ATOM   900  O  OD1 . ASP A 1 114 ? 9.224   -16.958 13.043  1.00 33.93  ? 114 ASP A OD1 1 
ATOM   901  O  OD2 . ASP A 1 114 ? 8.153   -17.734 14.788  1.00 43.66  ? 114 ASP A OD2 1 
ATOM   902  N  N   . GLY A 1 115 ? 5.187   -16.451 9.699   1.00 35.37  ? 115 GLY A N   1 
ATOM   903  C  CA  . GLY A 1 115 ? 4.020   -16.753 8.860   1.00 32.90  ? 115 GLY A CA  1 
ATOM   904  C  C   . GLY A 1 115 ? 2.616   -16.590 9.439   1.00 33.07  ? 115 GLY A C   1 
ATOM   905  O  O   . GLY A 1 115 ? 1.651   -16.850 8.746   1.00 29.13  ? 115 GLY A O   1 
ATOM   906  N  N   . GLU A 1 116 ? 2.475   -16.223 10.714  1.00 34.01  ? 116 GLU A N   1 
ATOM   907  C  CA  . GLU A 1 116 ? 1.113   -16.050 11.269  1.00 35.01  ? 116 GLU A CA  1 
ATOM   908  C  C   . GLU A 1 116 ? 0.667   -14.613 11.316  1.00 34.11  ? 116 GLU A C   1 
ATOM   909  O  O   . GLU A 1 116 ? 1.400   -13.748 11.800  1.00 31.83  ? 116 GLU A O   1 
ATOM   910  C  CB  . GLU A 1 116 ? 0.996   -16.641 12.675  1.00 38.95  ? 116 GLU A CB  1 
ATOM   911  C  CG  . GLU A 1 116 ? 1.396   -18.114 12.755  1.00 43.44  ? 116 GLU A CG  1 
ATOM   912  C  CD  . GLU A 1 116 ? 0.902   -18.764 14.030  1.00 45.31  ? 116 GLU A CD  1 
ATOM   913  O  OE1 . GLU A 1 116 ? 1.606   -18.688 15.061  1.00 41.05  ? 116 GLU A OE1 1 
ATOM   914  O  OE2 . GLU A 1 116 ? -0.205  -19.341 13.989  1.00 49.22  ? 116 GLU A OE2 1 
ATOM   915  N  N   . HIS A 1 117 ? -0.560  -14.408 10.830  1.00 39.82  ? 117 HIS A N   1 
ATOM   916  C  CA  . HIS A 1 117 ? -1.266  -13.127 10.769  1.00 36.99  ? 117 HIS A CA  1 
ATOM   917  C  C   . HIS A 1 117 ? -2.312  -13.150 11.830  1.00 36.28  ? 117 HIS A C   1 
ATOM   918  O  O   . HIS A 1 117 ? -2.822  -14.212 12.130  1.00 35.69  ? 117 HIS A O   1 
ATOM   919  C  CB  . HIS A 1 117 ? -1.999  -12.992 9.441   1.00 41.38  ? 117 HIS A CB  1 
ATOM   920  C  CG  . HIS A 1 117 ? -1.111  -12.587 8.279   1.00 45.54  ? 117 HIS A CG  1 
ATOM   921  N  ND1 . HIS A 1 117 ? -0.562  -11.360 8.173   1.00 41.50  ? 117 HIS A ND1 1 
ATOM   922  C  CD2 . HIS A 1 117 ? -0.714  -13.295 7.146   1.00 44.24  ? 117 HIS A CD2 1 
ATOM   923  C  CE1 . HIS A 1 117 ? 0.156   -11.293 7.042   1.00 44.17  ? 117 HIS A CE1 1 
ATOM   924  N  NE2 . HIS A 1 117 ? 0.067   -12.481 6.421   1.00 45.11  ? 117 HIS A NE2 1 
ATOM   925  N  N   . PHE A 1 118 ? -2.660  -11.975 12.374  1.00 32.56  ? 118 PHE A N   1 
ATOM   926  C  CA  . PHE A 1 118 ? -3.558  -11.870 13.506  1.00 31.68  ? 118 PHE A CA  1 
ATOM   927  C  C   . PHE A 1 118 ? -4.794  -11.193 13.042  1.00 28.47  ? 118 PHE A C   1 
ATOM   928  O  O   . PHE A 1 118 ? -4.897  -10.890 11.866  1.00 28.16  ? 118 PHE A O   1 
ATOM   929  C  CB  . PHE A 1 118 ? -2.870  -11.173 14.673  1.00 32.92  ? 118 PHE A CB  1 
ATOM   930  C  CG  . PHE A 1 118 ? -1.748  -11.987 15.256  1.00 37.80  ? 118 PHE A CG  1 
ATOM   931  C  CD1 . PHE A 1 118 ? -0.516  -12.061 14.611  1.00 37.04  ? 118 PHE A CD1 1 
ATOM   932  C  CD2 . PHE A 1 118 ? -1.929  -12.716 16.424  1.00 39.80  ? 118 PHE A CD2 1 
ATOM   933  C  CE1 . PHE A 1 118 ? 0.504   -12.827 15.127  1.00 35.51  ? 118 PHE A CE1 1 
ATOM   934  C  CE2 . PHE A 1 118 ? -0.905  -13.487 16.941  1.00 34.98  ? 118 PHE A CE2 1 
ATOM   935  C  CZ  . PHE A 1 118 ? 0.310   -13.537 16.291  1.00 38.34  ? 118 PHE A CZ  1 
ATOM   936  N  N   . ALA A 1 119 ? -5.770  -11.015 13.930  1.00 27.16  ? 119 ALA A N   1 
ATOM   937  C  CA  . ALA A 1 119 ? -7.097  -10.555 13.507  1.00 23.91  ? 119 ALA A CA  1 
ATOM   938  C  C   . ALA A 1 119 ? -7.090  -9.033  13.265  1.00 25.02  ? 119 ALA A C   1 
ATOM   939  O  O   . ALA A 1 119 ? -7.903  -8.513  12.503  1.00 23.42  ? 119 ALA A O   1 
ATOM   940  C  CB  . ALA A 1 119 ? -8.159  -10.907 14.531  1.00 27.48  ? 119 ALA A CB  1 
ATOM   941  N  N   . MET A 1 120 ? -6.164  -8.311  13.891  1.00 23.56  ? 120 MET A N   1 
ATOM   942  C  CA  . MET A 1 120 ? -6.127  -6.860  13.610  1.00 25.36  ? 120 MET A CA  1 
ATOM   943  C  C   . MET A 1 120 ? -4.753  -6.419  13.903  1.00 24.17  ? 120 MET A C   1 
ATOM   944  O  O   . MET A 1 120 ? -4.023  -7.141  14.569  1.00 27.18  ? 120 MET A O   1 
ATOM   945  C  CB  . MET A 1 120 ? -7.084  -6.029  14.511  1.00 23.16  ? 120 MET A CB  1 
ATOM   946  C  CG  . MET A 1 120 ? -8.554  -6.449  14.663  1.00 26.59  ? 120 MET A CG  1 
ATOM   947  S  SD  . MET A 1 120 ? -9.344  -5.346  15.903  1.00 29.90  ? 120 MET A SD  1 
ATOM   948  C  CE  . MET A 1 120 ? -9.573  -3.879  14.937  1.00 27.48  ? 120 MET A CE  1 
ATOM   949  N  N   . GLU A 1 121 ? -4.402  -5.206  13.478  1.00 24.22  ? 121 GLU A N   1 
ATOM   950  C  CA  . GLU A 1 121 ? -3.187  -4.636  14.007  1.00 20.90  ? 121 GLU A CA  1 
ATOM   951  C  C   . GLU A 1 121 ? -3.282  -3.127  14.263  1.00 19.44  ? 121 GLU A C   1 
ATOM   952  O  O   . GLU A 1 121 ? -3.607  -2.374  13.392  1.00 20.05  ? 121 GLU A O   1 
ATOM   953  C  CB  . GLU A 1 121 ? -2.019  -5.045  13.145  1.00 22.10  ? 121 GLU A CB  1 
ATOM   954  C  CG  . GLU A 1 121 ? -0.698  -4.385  13.477  1.00 24.17  ? 121 GLU A CG  1 
ATOM   955  C  CD  . GLU A 1 121 ? 0.382   -4.742  12.466  1.00 24.67  ? 121 GLU A CD  1 
ATOM   956  O  OE1 . GLU A 1 121 ? 0.241   -5.782  11.816  1.00 26.57  ? 121 GLU A OE1 1 
ATOM   957  O  OE2 . GLU A 1 121 ? 1.376   -3.979  12.309  1.00 29.97  ? 121 GLU A OE2 1 
ATOM   958  N  N   . MET A 1 122 ? -2.925  -2.733  15.488  1.00 22.18  ? 122 MET A N   1 
ATOM   959  C  CA  . MET A 1 122 ? -2.974  -1.362  16.025  1.00 20.14  ? 122 MET A CA  1 
ATOM   960  C  C   . MET A 1 122 ? -1.619  -0.699  15.900  1.00 18.57  ? 122 MET A C   1 
ATOM   961  O  O   . MET A 1 122 ? -0.641  -1.241  16.375  1.00 17.78  ? 122 MET A O   1 
ATOM   962  C  CB  . MET A 1 122 ? -3.315  -1.435  17.523  1.00 22.21  ? 122 MET A CB  1 
ATOM   963  C  CG  . MET A 1 122 ? -3.623  -0.068  18.130  1.00 22.23  ? 122 MET A CG  1 
ATOM   964  S  SD  . MET A 1 122 ? -4.276  -0.115  19.809  1.00 27.91  ? 122 MET A SD  1 
ATOM   965  C  CE  . MET A 1 122 ? -2.743  -0.376  20.661  1.00 24.00  ? 122 MET A CE  1 
ATOM   966  N  N   . HIS A 1 123 ? -1.618  0.498   15.309  1.00 18.45  ? 123 HIS A N   1 
ATOM   967  C  CA  . HIS A 1 123 ? -0.489  1.380   15.118  1.00 20.20  ? 123 HIS A CA  1 
ATOM   968  C  C   . HIS A 1 123 ? -0.565  2.679   15.870  1.00 20.48  ? 123 HIS A C   1 
ATOM   969  O  O   . HIS A 1 123 ? -1.457  3.514   15.647  1.00 24.68  ? 123 HIS A O   1 
ATOM   970  C  CB  . HIS A 1 123 ? -0.324  1.713   13.606  1.00 22.82  ? 123 HIS A CB  1 
ATOM   971  C  CG  . HIS A 1 123 ? 0.004   0.508   12.765  1.00 23.29  ? 123 HIS A CG  1 
ATOM   972  N  ND1 . HIS A 1 123 ? -0.172  0.474   11.431  1.00 27.23  ? 123 HIS A ND1 1 
ATOM   973  C  CD2 . HIS A 1 123 ? 0.562   -0.722  13.122  1.00 23.82  ? 123 HIS A CD2 1 
ATOM   974  C  CE1 . HIS A 1 123 ? 0.225   -0.746  10.962  1.00 28.48  ? 123 HIS A CE1 1 
ATOM   975  N  NE2 . HIS A 1 123 ? 0.674   -1.465  11.995  1.00 24.09  ? 123 HIS A NE2 1 
ATOM   976  N  N   . ILE A 1 124 ? 0.404   2.910   16.729  1.00 20.69  ? 124 ILE A N   1 
ATOM   977  C  CA  . ILE A 1 124 ? 0.501   4.207   17.390  1.00 21.62  ? 124 ILE A CA  1 
ATOM   978  C  C   . ILE A 1 124 ? 1.726   4.867   16.837  1.00 21.50  ? 124 ILE A C   1 
ATOM   979  O  O   . ILE A 1 124 ? 2.824   4.359   17.063  1.00 22.34  ? 124 ILE A O   1 
ATOM   980  C  CB  . ILE A 1 124 ? 0.562   4.089   18.942  1.00 20.77  ? 124 ILE A CB  1 
ATOM   981  C  CG1 . ILE A 1 124 ? -0.416  2.994   19.423  1.00 21.03  ? 124 ILE A CG1 1 
ATOM   982  C  CG2 . ILE A 1 124 ? 0.281   5.473   19.579  1.00 20.22  ? 124 ILE A CG2 1 
ATOM   983  C  CD1 . ILE A 1 124 ? -0.396  2.695   20.937  1.00 21.98  ? 124 ILE A CD1 1 
ATOM   984  N  N   . VAL A 1 125 ? 1.496   5.969   16.090  1.00 23.96  ? 125 VAL A N   1 
ATOM   985  C  CA  . VAL A 1 125 ? 2.455   6.693   15.219  1.00 23.51  ? 125 VAL A CA  1 
ATOM   986  C  C   . VAL A 1 125 ? 3.007   7.885   16.055  1.00 27.11  ? 125 VAL A C   1 
ATOM   987  O  O   . VAL A 1 125 ? 2.233   8.703   16.556  1.00 27.04  ? 125 VAL A O   1 
ATOM   988  C  CB  . VAL A 1 125 ? 1.732   7.167   13.872  1.00 22.62  ? 125 VAL A CB  1 
ATOM   989  C  CG1 . VAL A 1 125 ? 2.616   8.030   12.988  1.00 19.70  ? 125 VAL A CG1 1 
ATOM   990  C  CG2 . VAL A 1 125 ? 1.228   5.985   13.016  1.00 18.70  ? 125 VAL A CG2 1 
ATOM   991  N  N   . HIS A 1 126 ? 4.329   7.903   16.258  1.00 26.82  ? 126 HIS A N   1 
ATOM   992  C  CA  . HIS A 1 126 ? 5.068   8.979   16.862  1.00 28.82  ? 126 HIS A CA  1 
ATOM   993  C  C   . HIS A 1 126 ? 6.042   9.591   15.866  1.00 29.10  ? 126 HIS A C   1 
ATOM   994  O  O   . HIS A 1 126 ? 6.515   8.924   14.913  1.00 30.10  ? 126 HIS A O   1 
ATOM   995  C  CB  . HIS A 1 126 ? 5.858   8.491   18.082  1.00 28.99  ? 126 HIS A CB  1 
ATOM   996  C  CG  . HIS A 1 126 ? 5.023   7.766   19.121  1.00 28.37  ? 126 HIS A CG  1 
ATOM   997  N  ND1 . HIS A 1 126 ? 4.499   6.551   18.902  1.00 27.33  ? 126 HIS A ND1 1 
ATOM   998  C  CD2 . HIS A 1 126 ? 4.670   8.114   20.413  1.00 30.34  ? 126 HIS A CD2 1 
ATOM   999  C  CE1 . HIS A 1 126 ? 3.832   6.146   19.999  1.00 29.32  ? 126 HIS A CE1 1 
ATOM   1000 N  NE2 . HIS A 1 126 ? 3.928   7.106   20.918  1.00 29.42  ? 126 HIS A NE2 1 
ATOM   1001 N  N   . GLU A 1 127 ? 6.371   10.854  16.094  1.00 31.96  ? 127 GLU A N   1 
ATOM   1002 C  CA  . GLU A 1 127 ? 7.379   11.568  15.307  1.00 34.86  ? 127 GLU A CA  1 
ATOM   1003 C  C   . GLU A 1 127 ? 8.500   12.029  16.242  1.00 35.50  ? 127 GLU A C   1 
ATOM   1004 O  O   . GLU A 1 127 ? 8.235   12.465  17.370  1.00 35.34  ? 127 GLU A O   1 
ATOM   1005 C  CB  . GLU A 1 127 ? 6.719   12.760  14.591  1.00 39.65  ? 127 GLU A CB  1 
ATOM   1006 C  CG  . GLU A 1 127 ? 7.661   13.590  13.699  1.00 49.77  ? 127 GLU A CG  1 
ATOM   1007 C  CD  . GLU A 1 127 ? 6.970   14.738  12.944  1.00 55.25  ? 127 GLU A CD  1 
ATOM   1008 O  OE1 . GLU A 1 127 ? 6.164   15.478  13.550  1.00 53.43  ? 127 GLU A OE1 1 
ATOM   1009 O  OE2 . GLU A 1 127 ? 7.248   14.919  11.736  1.00 55.81  ? 127 GLU A OE2 1 
ATOM   1010 N  N   . LYS A 1 128 ? 9.745   11.926  15.775  1.00 34.12  ? 128 LYS A N   1 
ATOM   1011 C  CA  . LYS A 1 128 ? 10.944  12.257  16.561  1.00 36.42  ? 128 LYS A CA  1 
ATOM   1012 C  C   . LYS A 1 128 ? 10.909  13.685  17.121  1.00 36.53  ? 128 LYS A C   1 
ATOM   1013 O  O   . LYS A 1 128 ? 10.476  14.595  16.445  1.00 31.48  ? 128 LYS A O   1 
ATOM   1014 C  CB  . LYS A 1 128 ? 12.207  12.091  15.692  1.00 36.53  ? 128 LYS A CB  1 
ATOM   1015 C  CG  . LYS A 1 128 ? 13.517  12.133  16.457  1.00 36.48  ? 128 LYS A CG  1 
ATOM   1016 C  CD  . LYS A 1 128 ? 14.713  12.221  15.517  1.00 39.29  ? 128 LYS A CD  1 
ATOM   1017 C  CE  . LYS A 1 128 ? 15.186  10.851  15.041  1.00 39.82  ? 128 LYS A CE  1 
ATOM   1018 N  NZ  . LYS A 1 128 ? 16.384  11.007  14.175  1.00 44.05  ? 128 LYS A NZ  1 
ATOM   1019 N  N   . GLU A 1 129 ? 11.405  13.868  18.337  1.00 40.03  ? 129 GLU A N   1 
ATOM   1020 C  CA  . GLU A 1 129 ? 11.434  15.212  18.940  1.00 47.48  ? 129 GLU A CA  1 
ATOM   1021 C  C   . GLU A 1 129 ? 12.367  16.196  18.278  1.00 44.45  ? 129 GLU A C   1 
ATOM   1022 O  O   . GLU A 1 129 ? 13.568  15.963  18.214  1.00 52.01  ? 129 GLU A O   1 
ATOM   1023 C  CB  . GLU A 1 129 ? 11.767  15.163  20.425  1.00 46.47  ? 129 GLU A CB  1 
ATOM   1024 C  CG  . GLU A 1 129 ? 10.554  15.424  21.282  1.00 53.87  ? 129 GLU A CG  1 
ATOM   1025 C  CD  . GLU A 1 129 ? 10.918  15.971  22.650  1.00 58.79  ? 129 GLU A CD  1 
ATOM   1026 O  OE1 . GLU A 1 129 ? 10.014  16.017  23.517  1.00 58.31  ? 129 GLU A OE1 1 
ATOM   1027 O  OE2 . GLU A 1 129 ? 12.100  16.345  22.852  1.00 55.53  ? 129 GLU A OE2 1 
ATOM   1028 N  N   . LYS A 1 130 ? 11.802  17.295  17.788  1.00 43.69  ? 130 LYS A N   1 
ATOM   1029 C  CA  . LYS A 1 130 ? 12.596  18.449  17.416  1.00 48.25  ? 130 LYS A CA  1 
ATOM   1030 C  C   . LYS A 1 130 ? 13.237  19.043  18.681  1.00 49.98  ? 130 LYS A C   1 
ATOM   1031 O  O   . LYS A 1 130 ? 12.528  19.561  19.549  1.00 52.77  ? 130 LYS A O   1 
ATOM   1032 C  CB  . LYS A 1 130 ? 11.724  19.495  16.733  1.00 49.87  ? 130 LYS A CB  1 
ATOM   1033 C  CG  . LYS A 1 130 ? 11.996  19.703  15.248  1.00 51.78  ? 130 LYS A CG  1 
ATOM   1034 C  CD  . LYS A 1 130 ? 11.628  18.488  14.407  1.00 53.51  ? 130 LYS A CD  1 
ATOM   1035 C  CE  . LYS A 1 130 ? 11.695  18.806  12.920  1.00 53.54  ? 130 LYS A CE  1 
ATOM   1036 N  NZ  . LYS A 1 130 ? 10.414  18.456  12.234  1.00 55.54  ? 130 LYS A NZ  1 
ATOM   1037 N  N   . GLY A 1 131 ? 14.561  18.917  18.794  1.00 48.05  ? 131 GLY A N   1 
ATOM   1038 C  CA  . GLY A 1 131 ? 15.336  19.629  19.819  1.00 47.98  ? 131 GLY A CA  1 
ATOM   1039 C  C   . GLY A 1 131 ? 15.469  21.122  19.490  1.00 48.70  ? 131 GLY A C   1 
ATOM   1040 O  O   . GLY A 1 131 ? 14.653  21.694  18.769  1.00 45.21  ? 131 GLY A O   1 
ATOM   1041 N  N   . THR A 1 132 ? 16.503  21.743  20.045  1.00 47.06  ? 132 THR A N   1 
ATOM   1042 C  CA  . THR A 1 132 ? 16.868  23.125  19.785  1.00 47.21  ? 132 THR A CA  1 
ATOM   1043 C  C   . THR A 1 132 ? 18.081  23.132  18.838  1.00 54.27  ? 132 THR A C   1 
ATOM   1044 O  O   . THR A 1 132 ? 18.606  24.195  18.494  1.00 55.63  ? 132 THR A O   1 
ATOM   1045 C  CB  . THR A 1 132 ? 17.232  23.847  21.102  1.00 44.51  ? 132 THR A CB  1 
ATOM   1046 O  OG1 . THR A 1 132 ? 18.224  23.082  21.797  1.00 40.33  ? 132 THR A OG1 1 
ATOM   1047 C  CG2 . THR A 1 132 ? 15.993  24.008  22.004  1.00 41.62  ? 132 THR A CG2 1 
ATOM   1048 N  N   . SER A 1 133 ? 18.524  21.922  18.469  1.00 59.77  ? 133 SER A N   1 
ATOM   1049 C  CA  . SER A 1 133 ? 19.551  21.659  17.449  1.00 61.63  ? 133 SER A CA  1 
ATOM   1050 C  C   . SER A 1 133 ? 18.920  20.773  16.379  1.00 65.96  ? 133 SER A C   1 
ATOM   1051 O  O   . SER A 1 133 ? 17.857  20.193  16.615  1.00 64.39  ? 133 SER A O   1 
ATOM   1052 C  CB  . SER A 1 133 ? 20.745  20.911  18.051  1.00 59.36  ? 133 SER A CB  1 
ATOM   1053 O  OG  . SER A 1 133 ? 21.185  21.526  19.250  1.00 59.04  ? 133 SER A OG  1 
ATOM   1054 N  N   . ARG A 1 134 ? 19.584  20.697  15.259  1.00 65.66  ? 134 ARG A N   1 
ATOM   1055 C  CA  . ARG A 1 134 ? 19.204  19.901  14.109  1.00 64.73  ? 134 ARG A CA  1 
ATOM   1056 C  C   . ARG A 1 134 ? 20.402  20.041  13.205  1.00 67.17  ? 134 ARG A C   1 
ATOM   1057 O  O   . ARG A 1 134 ? 20.862  21.157  12.948  1.00 70.68  ? 134 ARG A O   1 
ATOM   1058 C  CB  . ARG A 1 134 ? 18.002  20.491  13.392  1.00 62.49  ? 134 ARG A CB  1 
ATOM   1059 C  CG  . ARG A 1 134 ? 18.163  20.420  11.882  1.00 63.57  ? 134 ARG A CG  1 
ATOM   1060 C  CD  . ARG A 1 134 ? 16.880  20.759  11.152  1.00 61.18  ? 134 ARG A CD  1 
ATOM   1061 N  NE  . ARG A 1 134 ? 16.991  22.041  10.464  1.00 57.19  ? 134 ARG A NE  1 
ATOM   1062 C  CZ  . ARG A 1 134 ? 17.390  22.180  9.208   1.00 52.96  ? 134 ARG A CZ  1 
ATOM   1063 N  NH1 . ARG A 1 134 ? 17.712  21.117  8.489   1.00 46.12  ? 134 ARG A NH1 1 
ATOM   1064 N  NH2 . ARG A 1 134 ? 17.458  23.386  8.665   1.00 52.44  ? 134 ARG A NH2 1 
ATOM   1065 N  N   . ASN A 1 135 ? 20.934  18.927  12.724  1.00 67.91  ? 135 ASN A N   1 
ATOM   1066 C  CA  . ASN A 1 135 ? 22.193  18.990  11.999  1.00 62.43  ? 135 ASN A CA  1 
ATOM   1067 C  C   . ASN A 1 135 ? 21.813  19.080  10.536  1.00 64.21  ? 135 ASN A C   1 
ATOM   1068 O  O   . ASN A 1 135 ? 20.710  18.735  10.200  1.00 65.97  ? 135 ASN A O   1 
ATOM   1069 C  CB  . ASN A 1 135 ? 22.998  17.741  12.305  1.00 59.64  ? 135 ASN A CB  1 
ATOM   1070 C  CG  . ASN A 1 135 ? 24.444  17.831  11.883  1.00 59.74  ? 135 ASN A CG  1 
ATOM   1071 O  OD1 . ASN A 1 135 ? 24.755  18.111  10.748  1.00 55.86  ? 135 ASN A OD1 1 
ATOM   1072 N  ND2 . ASN A 1 135 ? 25.329  17.523  12.794  1.00 53.73  ? 135 ASN A ND2 1 
ATOM   1073 N  N   . VAL A 1 136 ? 22.698  19.540  9.659   1.00 62.56  ? 136 VAL A N   1 
ATOM   1074 C  CA  . VAL A 1 136 ? 22.328  19.652  8.239   1.00 64.43  ? 136 VAL A CA  1 
ATOM   1075 C  C   . VAL A 1 136 ? 23.004  18.449  7.541   1.00 63.74  ? 136 VAL A C   1 
ATOM   1076 O  O   . VAL A 1 136 ? 24.161  18.123  7.802   1.00 62.76  ? 136 VAL A O   1 
ATOM   1077 C  CB  . VAL A 1 136 ? 22.581  21.003  7.482   1.00 64.91  ? 136 VAL A CB  1 
ATOM   1078 C  CG1 . VAL A 1 136 ? 21.921  22.181  8.197   1.00 67.97  ? 136 VAL A CG1 1 
ATOM   1079 C  CG2 . VAL A 1 136 ? 24.062  21.275  7.251   1.00 68.68  ? 136 VAL A CG2 1 
ATOM   1080 N  N   . ASP A 1 141 ? 16.731  12.205  4.326   1.00 77.01  ? 141 ASP A N   1 
ATOM   1081 C  CA  . ASP A 1 141 ? 15.812  11.065  4.241   1.00 76.15  ? 141 ASP A CA  1 
ATOM   1082 C  C   . ASP A 1 141 ? 15.838  10.255  5.540   1.00 67.74  ? 141 ASP A C   1 
ATOM   1083 O  O   . ASP A 1 141 ? 16.292  9.114   5.565   1.00 74.26  ? 141 ASP A O   1 
ATOM   1084 C  CB  . ASP A 1 141 ? 16.096  10.195  2.993   1.00 81.76  ? 141 ASP A CB  1 
ATOM   1085 C  CG  . ASP A 1 141 ? 17.480  9.505   3.018   1.00 85.95  ? 141 ASP A CG  1 
ATOM   1086 O  OD1 . ASP A 1 141 ? 17.608  8.395   3.593   1.00 82.01  ? 141 ASP A OD1 1 
ATOM   1087 O  OD2 . ASP A 1 141 ? 18.431  10.050  2.414   1.00 89.57  ? 141 ASP A OD2 1 
ATOM   1088 N  N   . PRO A 1 142 ? 15.332  10.844  6.631   1.00 61.80  ? 142 PRO A N   1 
ATOM   1089 C  CA  . PRO A 1 142 ? 15.648  10.300  7.952   1.00 54.93  ? 142 PRO A CA  1 
ATOM   1090 C  C   . PRO A 1 142 ? 15.046  8.914   8.169   1.00 53.37  ? 142 PRO A C   1 
ATOM   1091 O  O   . PRO A 1 142 ? 13.822  8.792   8.289   1.00 54.83  ? 142 PRO A O   1 
ATOM   1092 C  CB  . PRO A 1 142 ? 15.030  11.324  8.917   1.00 55.60  ? 142 PRO A CB  1 
ATOM   1093 C  CG  . PRO A 1 142 ? 14.407  12.396  8.070   1.00 60.37  ? 142 PRO A CG  1 
ATOM   1094 C  CD  . PRO A 1 142 ? 14.259  11.850  6.689   1.00 62.95  ? 142 PRO A CD  1 
ATOM   1095 N  N   . GLU A 1 143 ? 15.887  7.880   8.227   1.00 46.26  ? 143 GLU A N   1 
ATOM   1096 C  CA  . GLU A 1 143 ? 15.403  6.496   8.443   1.00 43.22  ? 143 GLU A CA  1 
ATOM   1097 C  C   . GLU A 1 143 ? 14.585  6.273   9.747   1.00 43.33  ? 143 GLU A C   1 
ATOM   1098 O  O   . GLU A 1 143 ? 14.020  5.196   9.964   1.00 39.81  ? 143 GLU A O   1 
ATOM   1099 C  CB  . GLU A 1 143 ? 16.544  5.469   8.310   1.00 45.65  ? 143 GLU A CB  1 
ATOM   1100 C  CG  . GLU A 1 143 ? 17.567  5.471   9.438   1.00 52.36  ? 143 GLU A CG  1 
ATOM   1101 C  CD  . GLU A 1 143 ? 18.911  4.849   9.048   1.00 57.47  ? 143 GLU A CD  1 
ATOM   1102 O  OE1 . GLU A 1 143 ? 18.913  3.752   8.450   1.00 60.60  ? 143 GLU A OE1 1 
ATOM   1103 O  OE2 . GLU A 1 143 ? 19.970  5.458   9.339   1.00 52.57  ? 143 GLU A OE2 1 
ATOM   1104 N  N   . ASP A 1 144 ? 14.485  7.293   10.591  1.00 42.68  ? 144 ASP A N   1 
ATOM   1105 C  CA  . ASP A 1 144 ? 13.776  7.127   11.866  1.00 41.24  ? 144 ASP A CA  1 
ATOM   1106 C  C   . ASP A 1 144 ? 12.989  8.384   12.279  1.00 41.36  ? 144 ASP A C   1 
ATOM   1107 O  O   . ASP A 1 144 ? 12.861  8.669   13.472  1.00 43.28  ? 144 ASP A O   1 
ATOM   1108 C  CB  . ASP A 1 144 ? 14.779  6.720   12.958  1.00 43.23  ? 144 ASP A CB  1 
ATOM   1109 C  CG  . ASP A 1 144 ? 15.896  7.753   13.150  1.00 46.17  ? 144 ASP A CG  1 
ATOM   1110 O  OD1 . ASP A 1 144 ? 15.814  8.837   12.526  1.00 45.87  ? 144 ASP A OD1 1 
ATOM   1111 O  OD2 . ASP A 1 144 ? 16.851  7.491   13.935  1.00 43.77  ? 144 ASP A OD2 1 
ATOM   1112 N  N   . GLU A 1 145 ? 12.450  9.116   11.295  1.00 42.05  ? 145 GLU A N   1 
ATOM   1113 C  CA  . GLU A 1 145 ? 11.699  10.350  11.563  1.00 40.47  ? 145 GLU A CA  1 
ATOM   1114 C  C   . GLU A 1 145 ? 10.499  9.991   12.417  1.00 37.49  ? 145 GLU A C   1 
ATOM   1115 O  O   . GLU A 1 145 ? 10.111  10.753  13.328  1.00 31.28  ? 145 GLU A O   1 
ATOM   1116 C  CB  . GLU A 1 145 ? 11.239  11.053  10.283  1.00 39.42  ? 145 GLU A CB  1 
ATOM   1117 C  CG  . GLU A 1 145 ? 10.481  12.352  10.565  1.00 50.97  ? 145 GLU A CG  1 
ATOM   1118 C  CD  . GLU A 1 145 ? 9.764   12.956  9.357   1.00 62.07  ? 145 GLU A CD  1 
ATOM   1119 O  OE1 . GLU A 1 145 ? 10.398  13.138  8.277   1.00 62.72  ? 145 GLU A OE1 1 
ATOM   1120 O  OE2 . GLU A 1 145 ? 8.552   13.272  9.493   1.00 62.62  ? 145 GLU A OE2 1 
ATOM   1121 N  N   . ILE A 1 146 ? 9.949   8.809   12.116  1.00 31.15  ? 146 ILE A N   1 
ATOM   1122 C  CA  . ILE A 1 146 ? 8.700   8.338   12.697  1.00 30.55  ? 146 ILE A CA  1 
ATOM   1123 C  C   . ILE A 1 146 ? 8.900   7.050   13.463  1.00 28.68  ? 146 ILE A C   1 
ATOM   1124 O  O   . ILE A 1 146 ? 9.675   6.219   13.034  1.00 30.17  ? 146 ILE A O   1 
ATOM   1125 C  CB  . ILE A 1 146 ? 7.580   8.225   11.643  1.00 29.40  ? 146 ILE A CB  1 
ATOM   1126 C  CG1 . ILE A 1 146 ? 6.939   9.598   11.432  1.00 32.24  ? 146 ILE A CG1 1 
ATOM   1127 C  CG2 . ILE A 1 146 ? 6.513   7.226   12.068  1.00 26.22  ? 146 ILE A CG2 1 
ATOM   1128 C  CD1 . ILE A 1 146 ? 5.818   9.593   10.399  1.00 34.29  ? 146 ILE A CD1 1 
ATOM   1129 N  N   . ALA A 1 147 ? 8.255   6.914   14.627  1.00 23.88  ? 147 ALA A N   1 
ATOM   1130 C  CA  . ALA A 1 147 ? 8.347   5.664   15.401  1.00 23.93  ? 147 ALA A CA  1 
ATOM   1131 C  C   . ALA A 1 147 ? 6.960   5.110   15.516  1.00 25.71  ? 147 ALA A C   1 
ATOM   1132 O  O   . ALA A 1 147 ? 6.058   5.797   16.058  1.00 27.66  ? 147 ALA A O   1 
ATOM   1133 C  CB  . ALA A 1 147 ? 8.952   5.882   16.798  1.00 25.47  ? 147 ALA A CB  1 
ATOM   1134 N  N   . VAL A 1 148 ? 6.761   3.909   14.964  1.00 23.84  ? 148 VAL A N   1 
ATOM   1135 C  CA  . VAL A 1 148 ? 5.473   3.238   15.112  1.00 26.29  ? 148 VAL A CA  1 
ATOM   1136 C  C   . VAL A 1 148 ? 5.523   2.116   16.159  1.00 24.34  ? 148 VAL A C   1 
ATOM   1137 O  O   . VAL A 1 148 ? 6.380   1.275   16.125  1.00 21.92  ? 148 VAL A O   1 
ATOM   1138 C  CB  . VAL A 1 148 ? 4.881   2.702   13.779  1.00 25.80  ? 148 VAL A CB  1 
ATOM   1139 C  CG1 . VAL A 1 148 ? 3.546   2.045   14.072  1.00 23.54  ? 148 VAL A CG1 1 
ATOM   1140 C  CG2 . VAL A 1 148 ? 4.607   3.854   12.794  1.00 21.68  ? 148 VAL A CG2 1 
ATOM   1141 N  N   . LEU A 1 149 ? 4.589   2.145   17.101  1.00 26.41  ? 149 LEU A N   1 
ATOM   1142 C  CA  . LEU A 1 149 ? 4.425   1.029   18.001  1.00 24.54  ? 149 LEU A CA  1 
ATOM   1143 C  C   . LEU A 1 149 ? 3.287   0.175   17.481  1.00 24.12  ? 149 LEU A C   1 
ATOM   1144 O  O   . LEU A 1 149 ? 2.181   0.651   17.294  1.00 22.47  ? 149 LEU A O   1 
ATOM   1145 C  CB  . LEU A 1 149 ? 4.112   1.507   19.428  1.00 24.85  ? 149 LEU A CB  1 
ATOM   1146 C  CG  . LEU A 1 149 ? 5.068   2.372   20.243  1.00 25.98  ? 149 LEU A CG  1 
ATOM   1147 C  CD1 . LEU A 1 149 ? 4.564   2.558   21.700  1.00 21.70  ? 149 LEU A CD1 1 
ATOM   1148 C  CD2 . LEU A 1 149 ? 6.456   1.743   20.264  1.00 25.78  ? 149 LEU A CD2 1 
ATOM   1149 N  N   . ALA A 1 150 ? 3.530   -1.115  17.332  1.00 24.62  ? 150 ALA A N   1 
ATOM   1150 C  CA  . ALA A 1 150 ? 2.550   -1.943  16.701  1.00 23.86  ? 150 ALA A CA  1 
ATOM   1151 C  C   . ALA A 1 150 ? 2.124   -3.096  17.589  1.00 23.93  ? 150 ALA A C   1 
ATOM   1152 O  O   . ALA A 1 150 ? 2.959   -3.803  18.136  1.00 23.77  ? 150 ALA A O   1 
ATOM   1153 C  CB  . ALA A 1 150 ? 3.087   -2.462  15.370  1.00 24.72  ? 150 ALA A CB  1 
ATOM   1154 N  N   . PHE A 1 151 ? 0.809   -3.282  17.703  1.00 23.40  ? 151 PHE A N   1 
ATOM   1155 C  CA  . PHE A 1 151 ? 0.272   -4.383  18.481  1.00 26.14  ? 151 PHE A CA  1 
ATOM   1156 C  C   . PHE A 1 151 ? -0.603  -5.251  17.621  1.00 25.42  ? 151 PHE A C   1 
ATOM   1157 O  O   . PHE A 1 151 ? -1.475  -4.766  16.870  1.00 23.87  ? 151 PHE A O   1 
ATOM   1158 C  CB  . PHE A 1 151 ? -0.475  -3.877  19.741  1.00 25.00  ? 151 PHE A CB  1 
ATOM   1159 C  CG  . PHE A 1 151 ? 0.371   -2.970  20.626  1.00 25.68  ? 151 PHE A CG  1 
ATOM   1160 C  CD1 . PHE A 1 151 ? 0.520   -1.616  20.323  1.00 28.32  ? 151 PHE A CD1 1 
ATOM   1161 C  CD2 . PHE A 1 151 ? 1.017   -3.472  21.746  1.00 26.61  ? 151 PHE A CD2 1 
ATOM   1162 C  CE1 . PHE A 1 151 ? 1.304   -0.780  21.117  1.00 25.69  ? 151 PHE A CE1 1 
ATOM   1163 C  CE2 . PHE A 1 151 ? 1.795   -2.657  22.544  1.00 25.90  ? 151 PHE A CE2 1 
ATOM   1164 C  CZ  . PHE A 1 151 ? 1.938   -1.309  22.217  1.00 27.17  ? 151 PHE A CZ  1 
ATOM   1165 N  N   . LEU A 1 152 ? -0.364  -6.554  17.721  1.00 27.52  ? 152 LEU A N   1 
ATOM   1166 C  CA  . LEU A 1 152 ? -1.203  -7.537  17.068  1.00 24.30  ? 152 LEU A CA  1 
ATOM   1167 C  C   . LEU A 1 152 ? -2.344  -7.784  18.006  1.00 26.35  ? 152 LEU A C   1 
ATOM   1168 O  O   . LEU A 1 152 ? -2.170  -7.657  19.202  1.00 26.04  ? 152 LEU A O   1 
ATOM   1169 C  CB  . LEU A 1 152 ? -0.398  -8.787  16.828  1.00 25.57  ? 152 LEU A CB  1 
ATOM   1170 C  CG  . LEU A 1 152 ? 0.894   -8.489  16.052  1.00 28.66  ? 152 LEU A CG  1 
ATOM   1171 C  CD1 . LEU A 1 152 ? 2.007   -9.383  16.574  1.00 26.33  ? 152 LEU A CD1 1 
ATOM   1172 C  CD2 . LEU A 1 152 ? 0.680   -8.699  14.540  1.00 25.96  ? 152 LEU A CD2 1 
ATOM   1173 N  N   . VAL A 1 153 ? -3.532  -8.025  17.452  1.00 26.41  ? 153 VAL A N   1 
ATOM   1174 C  CA  . VAL A 1 153 ? -4.725  -8.241  18.210  1.00 25.71  ? 153 VAL A CA  1 
ATOM   1175 C  C   . VAL A 1 153 ? -5.228  -9.634  17.787  1.00 28.12  ? 153 VAL A C   1 
ATOM   1176 O  O   . VAL A 1 153 ? -5.264  -9.976  16.573  1.00 30.12  ? 153 VAL A O   1 
ATOM   1177 C  CB  . VAL A 1 153 ? -5.792  -7.210  17.831  1.00 23.96  ? 153 VAL A CB  1 
ATOM   1178 C  CG1 . VAL A 1 153 ? -7.113  -7.476  18.532  1.00 23.13  ? 153 VAL A CG1 1 
ATOM   1179 C  CG2 . VAL A 1 153 ? -5.321  -5.768  18.081  1.00 25.99  ? 153 VAL A CG2 1 
ATOM   1180 N  N   . GLU A 1 154 ? -5.611  -10.440 18.768  1.00 27.68  ? 154 GLU A N   1 
ATOM   1181 C  CA  . GLU A 1 154 ? -6.320  -11.700 18.521  1.00 30.09  ? 154 GLU A CA  1 
ATOM   1182 C  C   . GLU A 1 154 ? -7.608  -11.732 19.352  1.00 32.92  ? 154 GLU A C   1 
ATOM   1183 O  O   . GLU A 1 154 ? -7.735  -10.979 20.325  1.00 32.09  ? 154 GLU A O   1 
ATOM   1184 C  CB  . GLU A 1 154 ? -5.415  -12.901 18.854  1.00 32.97  ? 154 GLU A CB  1 
ATOM   1185 C  CG  . GLU A 1 154 ? -5.015  -13.009 20.329  1.00 36.27  ? 154 GLU A CG  1 
ATOM   1186 C  CD  . GLU A 1 154 ? -3.976  -14.091 20.630  1.00 45.65  ? 154 GLU A CD  1 
ATOM   1187 O  OE1 . GLU A 1 154 ? -3.524  -14.796 19.697  1.00 48.06  ? 154 GLU A OE1 1 
ATOM   1188 O  OE2 . GLU A 1 154 ? -3.598  -14.237 21.818  1.00 49.48  ? 154 GLU A OE2 1 
ATOM   1189 N  N   . ALA A 1 155 ? -8.576  -12.566 18.954  1.00 31.82  ? 155 ALA A N   1 
ATOM   1190 C  CA  . ALA A 1 155 ? -9.795  -12.779 19.745  1.00 33.96  ? 155 ALA A CA  1 
ATOM   1191 C  C   . ALA A 1 155 ? -9.544  -13.484 21.087  1.00 36.79  ? 155 ALA A C   1 
ATOM   1192 O  O   . ALA A 1 155 ? -9.156  -14.641 21.107  1.00 38.33  ? 155 ALA A O   1 
ATOM   1193 C  CB  . ALA A 1 155 ? -10.801 -13.579 18.949  1.00 35.69  ? 155 ALA A CB  1 
ATOM   1194 N  N   . GLY A 1 156 ? -9.765  -12.780 22.198  1.00 39.05  ? 156 GLY A N   1 
ATOM   1195 C  CA  . GLY A 1 156 ? -9.785  -13.399 23.542  1.00 43.16  ? 156 GLY A CA  1 
ATOM   1196 C  C   . GLY A 1 156 ? -11.203 -13.718 23.982  1.00 42.52  ? 156 GLY A C   1 
ATOM   1197 O  O   . GLY A 1 156 ? -12.156 -13.429 23.254  1.00 44.55  ? 156 GLY A O   1 
ATOM   1198 N  N   . THR A 1 157 ? -11.353 -14.300 25.171  1.00 41.62  ? 157 THR A N   1 
ATOM   1199 C  CA  . THR A 1 157 ? -12.676 -14.695 25.653  1.00 44.08  ? 157 THR A CA  1 
ATOM   1200 C  C   . THR A 1 157 ? -13.425 -13.570 26.430  1.00 45.54  ? 157 THR A C   1 
ATOM   1201 O  O   . THR A 1 157 ? -14.655 -13.622 26.579  1.00 43.74  ? 157 THR A O   1 
ATOM   1202 C  CB  . THR A 1 157 ? -12.641 -16.042 26.443  1.00 44.73  ? 157 THR A CB  1 
ATOM   1203 O  OG1 . THR A 1 157 ? -11.920 -15.882 27.669  1.00 47.08  ? 157 THR A OG1 1 
ATOM   1204 C  CG2 . THR A 1 157 ? -11.937 -17.121 25.620  1.00 47.54  ? 157 THR A CG2 1 
ATOM   1205 N  N   . GLN A 1 158 ? -12.709 -12.543 26.882  1.00 42.34  ? 158 GLN A N   1 
ATOM   1206 C  CA  . GLN A 1 158 ? -13.386 -11.458 27.590  1.00 45.78  ? 158 GLN A CA  1 
ATOM   1207 C  C   . GLN A 1 158 ? -13.387 -10.112 26.870  1.00 45.27  ? 158 GLN A C   1 
ATOM   1208 O  O   . GLN A 1 158 ? -12.494 -9.824  26.064  1.00 41.21  ? 158 GLN A O   1 
ATOM   1209 C  CB  . GLN A 1 158 ? -12.865 -11.295 29.031  1.00 49.01  ? 158 GLN A CB  1 
ATOM   1210 C  CG  . GLN A 1 158 ? -11.368 -11.051 29.199  1.00 51.35  ? 158 GLN A CG  1 
ATOM   1211 C  CD  . GLN A 1 158 ? -10.924 -11.128 30.664  1.00 56.36  ? 158 GLN A CD  1 
ATOM   1212 O  OE1 . GLN A 1 158 ? -10.308 -12.116 31.093  1.00 61.72  ? 158 GLN A OE1 1 
ATOM   1213 N  NE2 . GLN A 1 158 ? -11.250 -10.099 31.441  1.00 47.55  ? 158 GLN A NE2 1 
ATOM   1214 N  N   . VAL A 1 159 ? -14.388 -9.286  27.186  1.00 40.05  ? 159 VAL A N   1 
ATOM   1215 C  CA  . VAL A 1 159 ? -14.350 -7.888  26.817  1.00 37.76  ? 159 VAL A CA  1 
ATOM   1216 C  C   . VAL A 1 159 ? -13.043 -7.253  27.303  1.00 40.66  ? 159 VAL A C   1 
ATOM   1217 O  O   . VAL A 1 159 ? -12.604 -7.501  28.439  1.00 42.56  ? 159 VAL A O   1 
ATOM   1218 C  CB  . VAL A 1 159 ? -15.573 -7.109  27.352  1.00 40.58  ? 159 VAL A CB  1 
ATOM   1219 C  CG1 . VAL A 1 159 ? -15.525 -5.643  26.918  1.00 37.91  ? 159 VAL A CG1 1 
ATOM   1220 C  CG2 . VAL A 1 159 ? -16.862 -7.744  26.851  1.00 37.00  ? 159 VAL A CG2 1 
ATOM   1221 N  N   . ASN A 1 160 ? -12.405 -6.472  26.428  1.00 36.29  ? 160 ASN A N   1 
ATOM   1222 C  CA  . ASN A 1 160 ? -11.322 -5.599  26.825  1.00 35.93  ? 160 ASN A CA  1 
ATOM   1223 C  C   . ASN A 1 160 ? -12.042 -4.301  27.112  1.00 38.99  ? 160 ASN A C   1 
ATOM   1224 O  O   . ASN A 1 160 ? -12.509 -3.613  26.195  1.00 38.16  ? 160 ASN A O   1 
ATOM   1225 C  CB  . ASN A 1 160 ? -10.287 -5.468  25.690  1.00 34.90  ? 160 ASN A CB  1 
ATOM   1226 C  CG  . ASN A 1 160 ? -9.006  -4.764  26.119  1.00 37.42  ? 160 ASN A CG  1 
ATOM   1227 O  OD1 . ASN A 1 160 ? -9.020  -3.800  26.899  1.00 44.27  ? 160 ASN A OD1 1 
ATOM   1228 N  ND2 . ASN A 1 160 ? -7.900  -5.211  25.588  1.00 31.81  ? 160 ASN A ND2 1 
ATOM   1229 N  N   . GLU A 1 161 ? -12.238 -4.003  28.387  1.00 41.05  ? 161 GLU A N   1 
ATOM   1230 C  CA  . GLU A 1 161 ? -12.997 -2.798  28.738  1.00 41.36  ? 161 GLU A CA  1 
ATOM   1231 C  C   . GLU A 1 161 ? -12.218 -1.547  28.344  1.00 37.62  ? 161 GLU A C   1 
ATOM   1232 O  O   . GLU A 1 161 ? -12.809 -0.515  28.068  1.00 36.02  ? 161 GLU A O   1 
ATOM   1233 C  CB  . GLU A 1 161 ? -13.410 -2.745  30.222  1.00 45.67  ? 161 GLU A CB  1 
ATOM   1234 C  CG  . GLU A 1 161 ? -14.733 -3.426  30.585  1.00 44.58  ? 161 GLU A CG  1 
ATOM   1235 C  CD  . GLU A 1 161 ? -15.955 -2.961  29.780  1.00 47.83  ? 161 GLU A CD  1 
ATOM   1236 O  OE1 . GLU A 1 161 ? -16.219 -1.755  29.651  1.00 47.54  ? 161 GLU A OE1 1 
ATOM   1237 O  OE2 . GLU A 1 161 ? -16.701 -3.828  29.285  1.00 52.06  ? 161 GLU A OE2 1 
ATOM   1238 N  N   . GLY A 1 162 ? -10.892 -1.662  28.293  1.00 37.04  ? 162 GLY A N   1 
ATOM   1239 C  CA  . GLY A 1 162 ? -10.030 -0.572  27.842  1.00 36.43  ? 162 GLY A CA  1 
ATOM   1240 C  C   . GLY A 1 162 ? -10.417 -0.055  26.473  1.00 35.40  ? 162 GLY A C   1 
ATOM   1241 O  O   . GLY A 1 162 ? -10.405 1.154   26.230  1.00 37.15  ? 162 GLY A O   1 
ATOM   1242 N  N   . PHE A 1 163 ? -10.804 -0.982  25.602  1.00 34.44  ? 163 PHE A N   1 
ATOM   1243 C  CA  . PHE A 1 163 ? -11.178 -0.689  24.225  1.00 32.30  ? 163 PHE A CA  1 
ATOM   1244 C  C   . PHE A 1 163 ? -12.604 -0.174  24.011  1.00 34.28  ? 163 PHE A C   1 
ATOM   1245 O  O   . PHE A 1 163 ? -12.936 0.350   22.927  1.00 29.36  ? 163 PHE A O   1 
ATOM   1246 C  CB  . PHE A 1 163 ? -10.917 -1.923  23.362  1.00 32.16  ? 163 PHE A CB  1 
ATOM   1247 C  CG  . PHE A 1 163 ? -9.551  -1.943  22.787  1.00 31.76  ? 163 PHE A CG  1 
ATOM   1248 C  CD1 . PHE A 1 163 ? -8.477  -2.359  23.542  1.00 29.51  ? 163 PHE A CD1 1 
ATOM   1249 C  CD2 . PHE A 1 163 ? -9.331  -1.497  21.479  1.00 30.86  ? 163 PHE A CD2 1 
ATOM   1250 C  CE1 . PHE A 1 163 ? -7.187  -2.368  22.998  1.00 32.08  ? 163 PHE A CE1 1 
ATOM   1251 C  CE2 . PHE A 1 163 ? -8.056  -1.517  20.927  1.00 28.18  ? 163 PHE A CE2 1 
ATOM   1252 C  CZ  . PHE A 1 163 ? -6.989  -1.939  21.684  1.00 28.69  ? 163 PHE A CZ  1 
ATOM   1253 N  N   . GLN A 1 164 ? -13.445 -0.288  25.045  1.00 34.72  ? 164 GLN A N   1 
ATOM   1254 C  CA  . GLN A 1 164 ? -14.850 0.082   24.907  1.00 34.46  ? 164 GLN A CA  1 
ATOM   1255 C  C   . GLN A 1 164 ? -15.202 1.538   24.498  1.00 34.53  ? 164 GLN A C   1 
ATOM   1256 O  O   . GLN A 1 164 ? -16.148 1.732   23.749  1.00 44.45  ? 164 GLN A O   1 
ATOM   1257 C  CB  . GLN A 1 164 ? -15.663 -0.364  26.136  1.00 39.36  ? 164 GLN A CB  1 
ATOM   1258 C  CG  . GLN A 1 164 ? -16.103 -1.820  26.126  1.00 46.52  ? 164 GLN A CG  1 
ATOM   1259 C  CD  . GLN A 1 164 ? -16.681 -2.255  24.786  1.00 47.05  ? 164 GLN A CD  1 
ATOM   1260 O  OE1 . GLN A 1 164 ? -15.958 -2.652  23.885  1.00 42.24  ? 164 GLN A OE1 1 
ATOM   1261 N  NE2 . GLN A 1 164 ? -17.997 -2.193  24.662  1.00 56.51  ? 164 GLN A NE2 1 
ATOM   1262 N  N   . PRO A 1 165 ? -14.514 2.574   25.008  1.00 32.27  ? 165 PRO A N   1 
ATOM   1263 C  CA  . PRO A 1 165 ? -14.916 3.833   24.389  1.00 30.71  ? 165 PRO A CA  1 
ATOM   1264 C  C   . PRO A 1 165 ? -14.573 3.926   22.894  1.00 30.95  ? 165 PRO A C   1 
ATOM   1265 O  O   . PRO A 1 165 ? -15.235 4.653   22.170  1.00 31.76  ? 165 PRO A O   1 
ATOM   1266 C  CB  . PRO A 1 165 ? -14.143 4.879   25.193  1.00 34.63  ? 165 PRO A CB  1 
ATOM   1267 C  CG  . PRO A 1 165 ? -13.903 4.201   26.546  1.00 34.49  ? 165 PRO A CG  1 
ATOM   1268 C  CD  . PRO A 1 165 ? -13.557 2.798   26.107  1.00 34.21  ? 165 PRO A CD  1 
ATOM   1269 N  N   . LEU A 1 166 ? -13.538 3.228   22.424  1.00 32.87  ? 166 LEU A N   1 
ATOM   1270 C  CA  . LEU A 1 166 ? -13.204 3.293   20.967  1.00 30.33  ? 166 LEU A CA  1 
ATOM   1271 C  C   . LEU A 1 166 ? -14.254 2.529   20.205  1.00 29.03  ? 166 LEU A C   1 
ATOM   1272 O  O   . LEU A 1 166 ? -14.790 3.032   19.235  1.00 29.78  ? 166 LEU A O   1 
ATOM   1273 C  CB  . LEU A 1 166 ? -11.795 2.744   20.666  1.00 30.18  ? 166 LEU A CB  1 
ATOM   1274 C  CG  . LEU A 1 166 ? -11.340 2.547   19.213  1.00 29.98  ? 166 LEU A CG  1 
ATOM   1275 C  CD1 . LEU A 1 166 ? -11.450 3.806   18.354  1.00 26.75  ? 166 LEU A CD1 1 
ATOM   1276 C  CD2 . LEU A 1 166 ? -9.895  2.031   19.209  1.00 32.61  ? 166 LEU A CD2 1 
ATOM   1277 N  N   . VAL A 1 167 ? -14.591 1.330   20.683  1.00 33.32  ? 167 VAL A N   1 
ATOM   1278 C  CA  . VAL A 1 167 ? -15.555 0.451   20.004  1.00 34.84  ? 167 VAL A CA  1 
ATOM   1279 C  C   . VAL A 1 167 ? -16.979 1.040   19.921  1.00 38.93  ? 167 VAL A C   1 
ATOM   1280 O  O   . VAL A 1 167 ? -17.684 0.861   18.904  1.00 41.36  ? 167 VAL A O   1 
ATOM   1281 C  CB  . VAL A 1 167 ? -15.537 -0.970  20.656  1.00 35.94  ? 167 VAL A CB  1 
ATOM   1282 C  CG1 . VAL A 1 167 ? -16.621 -1.877  20.116  1.00 30.71  ? 167 VAL A CG1 1 
ATOM   1283 C  CG2 . VAL A 1 167 ? -14.160 -1.609  20.496  1.00 37.59  ? 167 VAL A CG2 1 
ATOM   1284 N  N   . GLU A 1 168 ? -17.387 1.756   20.967  1.00 35.41  ? 168 GLU A N   1 
ATOM   1285 C  CA  . GLU A 1 168 ? -18.690 2.415   20.977  1.00 39.27  ? 168 GLU A CA  1 
ATOM   1286 C  C   . GLU A 1 168 ? -18.736 3.593   20.020  1.00 38.15  ? 168 GLU A C   1 
ATOM   1287 O  O   . GLU A 1 168 ? -19.760 3.834   19.393  1.00 42.60  ? 168 GLU A O   1 
ATOM   1288 C  CB  . GLU A 1 168 ? -19.052 2.881   22.392  1.00 44.24  ? 168 GLU A CB  1 
ATOM   1289 C  CG  . GLU A 1 168 ? -19.116 1.755   23.417  1.00 47.16  ? 168 GLU A CG  1 
ATOM   1290 C  CD  . GLU A 1 168 ? -19.522 2.233   24.793  1.00 55.20  ? 168 GLU A CD  1 
ATOM   1291 O  OE1 . GLU A 1 168 ? -19.250 1.500   25.769  1.00 60.96  ? 168 GLU A OE1 1 
ATOM   1292 O  OE2 . GLU A 1 168 ? -20.107 3.346   24.903  1.00 60.00  ? 168 GLU A OE2 1 
ATOM   1293 N  N   . ALA A 1 169 ? -17.637 4.337   19.912  1.00 34.97  ? 169 ALA A N   1 
ATOM   1294 C  CA  . ALA A 1 169 ? -17.587 5.523   19.070  1.00 33.88  ? 169 ALA A CA  1 
ATOM   1295 C  C   . ALA A 1 169 ? -17.642 5.131   17.596  1.00 36.52  ? 169 ALA A C   1 
ATOM   1296 O  O   . ALA A 1 169 ? -17.944 5.961   16.769  1.00 33.59  ? 169 ALA A O   1 
ATOM   1297 C  CB  . ALA A 1 169 ? -16.341 6.347   19.362  1.00 32.74  ? 169 ALA A CB  1 
ATOM   1298 N  N   . LEU A 1 170 ? -17.388 3.852   17.285  1.00 39.22  ? 170 LEU A N   1 
ATOM   1299 C  CA  . LEU A 1 170 ? -17.490 3.357   15.918  1.00 37.58  ? 170 LEU A CA  1 
ATOM   1300 C  C   . LEU A 1 170 ? -18.876 3.656   15.347  1.00 39.96  ? 170 LEU A C   1 
ATOM   1301 O  O   . LEU A 1 170 ? -18.999 4.064   14.189  1.00 39.88  ? 170 LEU A O   1 
ATOM   1302 C  CB  . LEU A 1 170 ? -17.171 1.852   15.833  1.00 36.93  ? 170 LEU A CB  1 
ATOM   1303 C  CG  . LEU A 1 170 ? -15.725 1.458   16.198  1.00 37.68  ? 170 LEU A CG  1 
ATOM   1304 C  CD1 . LEU A 1 170 ? -15.440 0.042   15.778  1.00 35.94  ? 170 LEU A CD1 1 
ATOM   1305 C  CD2 . LEU A 1 170 ? -14.703 2.417   15.596  1.00 34.55  ? 170 LEU A CD2 1 
ATOM   1306 N  N   . SER A 1 171 ? -19.909 3.487   16.168  1.00 39.17  ? 171 SER A N   1 
ATOM   1307 C  CA  . SER A 1 171 ? -21.288 3.784   15.748  1.00 41.72  ? 171 SER A CA  1 
ATOM   1308 C  C   . SER A 1 171 ? -21.488 5.206   15.201  1.00 44.71  ? 171 SER A C   1 
ATOM   1309 O  O   . SER A 1 171 ? -22.382 5.417   14.392  1.00 54.07  ? 171 SER A O   1 
ATOM   1310 C  CB  . SER A 1 171 ? -22.271 3.550   16.912  1.00 42.47  ? 171 SER A CB  1 
ATOM   1311 O  OG  . SER A 1 171 ? -22.271 2.199   17.322  1.00 41.22  ? 171 SER A OG  1 
ATOM   1312 N  N   . ASN A 1 172 ? -20.675 6.173   15.629  1.00 38.84  ? 172 ASN A N   1 
ATOM   1313 C  CA  . ASN A 1 172 ? -20.868 7.555   15.198  1.00 38.21  ? 172 ASN A CA  1 
ATOM   1314 C  C   . ASN A 1 172 ? -20.045 7.998   14.013  1.00 41.69  ? 172 ASN A C   1 
ATOM   1315 O  O   . ASN A 1 172 ? -20.086 9.186   13.663  1.00 40.37  ? 172 ASN A O   1 
ATOM   1316 C  CB  . ASN A 1 172 ? -20.538 8.529   16.326  1.00 39.03  ? 172 ASN A CB  1 
ATOM   1317 C  CG  . ASN A 1 172 ? -21.345 8.283   17.559  1.00 40.35  ? 172 ASN A CG  1 
ATOM   1318 O  OD1 . ASN A 1 172 ? -22.539 7.996   17.483  1.00 46.18  ? 172 ASN A OD1 1 
ATOM   1319 N  ND2 . ASN A 1 172 ? -20.700 8.365   18.706  1.00 37.83  ? 172 ASN A ND2 1 
ATOM   1320 N  N   . ILE A 1 173 ? -19.251 7.098   13.419  1.00 42.37  ? 173 ILE A N   1 
ATOM   1321 C  CA  . ILE A 1 173 ? -18.420 7.508   12.262  1.00 36.78  ? 173 ILE A CA  1 
ATOM   1322 C  C   . ILE A 1 173 ? -18.432 6.466   11.104  1.00 39.64  ? 173 ILE A C   1 
ATOM   1323 O  O   . ILE A 1 173 ? -17.357 6.068   10.599  1.00 37.17  ? 173 ILE A O   1 
ATOM   1324 C  CB  . ILE A 1 173 ? -16.971 7.808   12.717  1.00 33.09  ? 173 ILE A CB  1 
ATOM   1325 C  CG1 . ILE A 1 173 ? -16.408 6.622   13.498  1.00 31.99  ? 173 ILE A CG1 1 
ATOM   1326 C  CG2 . ILE A 1 173 ? -16.904 9.046   13.600  1.00 36.82  ? 173 ILE A CG2 1 
ATOM   1327 C  CD1 . ILE A 1 173 ? -14.919 6.610   13.643  1.00 31.10  ? 173 ILE A CD1 1 
ATOM   1328 N  N   . PRO A 1 174 ? -19.633 6.011   10.681  1.00 39.66  ? 174 PRO A N   1 
ATOM   1329 C  CA  . PRO A 1 174 ? -19.728 4.941   9.672   1.00 40.80  ? 174 PRO A CA  1 
ATOM   1330 C  C   . PRO A 1 174 ? -19.168 5.332   8.303   1.00 38.90  ? 174 PRO A C   1 
ATOM   1331 O  O   . PRO A 1 174 ? -18.550 4.487   7.622   1.00 38.94  ? 174 PRO A O   1 
ATOM   1332 C  CB  . PRO A 1 174 ? -21.242 4.670   9.557   1.00 39.94  ? 174 PRO A CB  1 
ATOM   1333 C  CG  . PRO A 1 174 ? -21.907 5.463   10.631  1.00 40.97  ? 174 PRO A CG  1 
ATOM   1334 C  CD  . PRO A 1 174 ? -20.962 6.569   10.998  1.00 44.83  ? 174 PRO A CD  1 
ATOM   1335 N  N   . LYS A 1 175 ? -19.385 6.589   7.928   1.00 38.99  ? 175 LYS A N   1 
ATOM   1336 C  CA  . LYS A 1 175 ? -18.971 7.135   6.641   1.00 42.28  ? 175 LYS A CA  1 
ATOM   1337 C  C   . LYS A 1 175 ? -17.605 7.797   6.724   1.00 40.30  ? 175 LYS A C   1 
ATOM   1338 O  O   . LYS A 1 175 ? -17.315 8.451   7.724   1.00 41.11  ? 175 LYS A O   1 
ATOM   1339 C  CB  . LYS A 1 175 ? -19.954 8.227   6.172   1.00 44.34  ? 175 LYS A CB  1 
ATOM   1340 C  CG  . LYS A 1 175 ? -21.396 7.802   5.934   1.00 45.42  ? 175 LYS A CG  1 
ATOM   1341 C  CD  . LYS A 1 175 ? -22.313 9.030   5.958   1.00 45.02  ? 175 LYS A CD  1 
ATOM   1342 C  CE  . LYS A 1 175 ? -23.736 8.707   5.520   1.00 47.06  ? 175 LYS A CE  1 
ATOM   1343 N  NZ  . LYS A 1 175 ? -24.131 7.270   5.661   1.00 40.48  ? 175 LYS A NZ  1 
ATOM   1344 N  N   . PRO A 1 176 ? -16.799 7.685   5.643   1.00 35.99  ? 176 PRO A N   1 
ATOM   1345 C  CA  . PRO A 1 176 ? -15.568 8.423   5.461   1.00 38.62  ? 176 PRO A CA  1 
ATOM   1346 C  C   . PRO A 1 176 ? -15.845 9.897   5.702   1.00 39.73  ? 176 PRO A C   1 
ATOM   1347 O  O   . PRO A 1 176 ? -16.943 10.360  5.404   1.00 35.17  ? 176 PRO A O   1 
ATOM   1348 C  CB  . PRO A 1 176 ? -15.225 8.201   3.978   1.00 36.23  ? 176 PRO A CB  1 
ATOM   1349 C  CG  . PRO A 1 176 ? -15.863 6.902   3.636   1.00 38.65  ? 176 PRO A CG  1 
ATOM   1350 C  CD  . PRO A 1 176 ? -17.133 6.880   4.453   1.00 38.98  ? 176 PRO A CD  1 
ATOM   1351 N  N   . GLU A 1 177 ? -14.852 10.590  6.261   1.00 46.06  ? 177 GLU A N   1 
ATOM   1352 C  CA  . GLU A 1 177 ? -14.923 12.017  6.655   1.00 46.54  ? 177 GLU A CA  1 
ATOM   1353 C  C   . GLU A 1 177 ? -15.817 12.345  7.872   1.00 47.06  ? 177 GLU A C   1 
ATOM   1354 O  O   . GLU A 1 177 ? -16.033 13.516  8.184   1.00 54.23  ? 177 GLU A O   1 
ATOM   1355 C  CB  . GLU A 1 177 ? -15.286 12.914  5.449   1.00 44.44  ? 177 GLU A CB  1 
ATOM   1356 C  CG  . GLU A 1 177 ? -14.207 13.007  4.379   1.00 45.72  ? 177 GLU A CG  1 
ATOM   1357 C  CD  . GLU A 1 177 ? -12.849 13.435  4.928   1.00 56.62  ? 177 GLU A CD  1 
ATOM   1358 O  OE1 . GLU A 1 177 ? -12.716 14.602  5.392   1.00 54.41  ? 177 GLU A OE1 1 
ATOM   1359 O  OE2 . GLU A 1 177 ? -11.903 12.596  4.899   1.00 57.12  ? 177 GLU A OE2 1 
ATOM   1360 N  N   . MET A 1 178 ? -16.349 11.344  8.558   1.00 46.25  ? 178 MET A N   1 
ATOM   1361 C  CA  . MET A 1 178 ? -17.037 11.637  9.822   1.00 45.33  ? 178 MET A CA  1 
ATOM   1362 C  C   . MET A 1 178 ? -16.075 11.634  10.988  1.00 43.95  ? 178 MET A C   1 
ATOM   1363 O  O   . MET A 1 178 ? -15.111 10.878  11.006  1.00 39.07  ? 178 MET A O   1 
ATOM   1364 C  CB  . MET A 1 178 ? -18.167 10.649  10.094  1.00 46.74  ? 178 MET A CB  1 
ATOM   1365 C  CG  . MET A 1 178 ? -19.444 10.990  9.343   1.00 48.66  ? 178 MET A CG  1 
ATOM   1366 S  SD  . MET A 1 178 ? -20.527 9.574   9.164   1.00 49.94  ? 178 MET A SD  1 
ATOM   1367 C  CE  . MET A 1 178 ? -21.643 9.848   10.545  1.00 50.21  ? 178 MET A CE  1 
ATOM   1368 N  N   . SER A 1 179 ? -16.329 12.487  11.965  1.00 44.81  ? 179 SER A N   1 
ATOM   1369 C  CA  . SER A 1 179 ? -15.603 12.388  13.210  1.00 45.12  ? 179 SER A CA  1 
ATOM   1370 C  C   . SER A 1 179 ? -16.516 12.326  14.434  1.00 43.17  ? 179 SER A C   1 
ATOM   1371 O  O   . SER A 1 179 ? -17.753 12.471  14.341  1.00 41.84  ? 179 SER A O   1 
ATOM   1372 C  CB  . SER A 1 179 ? -14.550 13.497  13.325  1.00 48.49  ? 179 SER A CB  1 
ATOM   1373 O  OG  . SER A 1 179 ? -15.117 14.774  13.124  1.00 60.20  ? 179 SER A OG  1 
ATOM   1374 N  N   . THR A 1 180 ? -15.905 12.065  15.587  1.00 39.58  ? 180 THR A N   1 
ATOM   1375 C  CA  . THR A 1 180 ? -16.613 12.141  16.863  1.00 38.20  ? 180 THR A CA  1 
ATOM   1376 C  C   . THR A 1 180 ? -15.624 12.322  17.997  1.00 38.11  ? 180 THR A C   1 
ATOM   1377 O  O   . THR A 1 180 ? -14.438 12.515  17.764  1.00 32.32  ? 180 THR A O   1 
ATOM   1378 C  CB  . THR A 1 180 ? -17.599 10.960  17.114  1.00 40.04  ? 180 THR A CB  1 
ATOM   1379 O  OG1 . THR A 1 180 ? -18.384 11.233  18.287  1.00 41.65  ? 180 THR A OG1 1 
ATOM   1380 C  CG2 . THR A 1 180 ? -16.902 9.603   17.299  1.00 40.31  ? 180 THR A CG2 1 
ATOM   1381 N  N   . THR A 1 181 ? -16.126 12.267  19.223  1.00 36.91  ? 181 THR A N   1 
ATOM   1382 C  CA  . THR A 1 181 ? -15.304 12.375  20.416  1.00 35.97  ? 181 THR A CA  1 
ATOM   1383 C  C   . THR A 1 181 ? -15.597 11.113  21.233  1.00 36.61  ? 181 THR A C   1 
ATOM   1384 O  O   . THR A 1 181 ? -16.777 10.756  21.441  1.00 36.35  ? 181 THR A O   1 
ATOM   1385 C  CB  . THR A 1 181 ? -15.601 13.707  21.162  1.00 40.69  ? 181 THR A CB  1 
ATOM   1386 O  OG1 . THR A 1 181 ? -15.206 14.803  20.322  1.00 43.53  ? 181 THR A OG1 1 
ATOM   1387 C  CG2 . THR A 1 181 ? -14.833 13.834  22.496  1.00 40.01  ? 181 THR A CG2 1 
ATOM   1388 N  N   . MET A 1 182 ? -14.541 10.387  21.607  1.00 29.50  ? 182 MET A N   1 
ATOM   1389 C  CA  . MET A 1 182 ? -14.703 9.227   22.467  1.00 33.18  ? 182 MET A CA  1 
ATOM   1390 C  C   . MET A 1 182 ? -15.009 9.700   23.890  1.00 34.73  ? 182 MET A C   1 
ATOM   1391 O  O   . MET A 1 182 ? -14.576 10.777  24.291  1.00 36.20  ? 182 MET A O   1 
ATOM   1392 C  CB  . MET A 1 182 ? -13.418 8.365   22.490  1.00 32.50  ? 182 MET A CB  1 
ATOM   1393 C  CG  . MET A 1 182 ? -13.098 7.567   21.188  1.00 30.55  ? 182 MET A CG  1 
ATOM   1394 S  SD  . MET A 1 182 ? -11.312 7.220   21.004  1.00 32.57  ? 182 MET A SD  1 
ATOM   1395 C  CE  . MET A 1 182 ? -10.997 6.257   22.489  1.00 33.55  ? 182 MET A CE  1 
ATOM   1396 N  N   . ALA A 1 183 ? -15.740 8.882   24.641  1.00 38.68  ? 183 ALA A N   1 
ATOM   1397 C  CA  . ALA A 1 183 ? -15.801 8.997   26.099  1.00 40.87  ? 183 ALA A CA  1 
ATOM   1398 C  C   . ALA A 1 183 ? -14.378 8.926   26.653  1.00 45.56  ? 183 ALA A C   1 
ATOM   1399 O  O   . ALA A 1 183 ? -13.469 8.369   26.025  1.00 38.48  ? 183 ALA A O   1 
ATOM   1400 C  CB  . ALA A 1 183 ? -16.638 7.876   26.688  1.00 42.05  ? 183 ALA A CB  1 
ATOM   1401 N  N   . GLU A 1 184 ? -14.212 9.488   27.845  1.00 43.12  ? 184 GLU A N   1 
ATOM   1402 C  CA  . GLU A 1 184 ? -12.940 9.598   28.536  1.00 39.93  ? 184 GLU A CA  1 
ATOM   1403 C  C   . GLU A 1 184 ? -12.161 8.292   28.650  1.00 39.08  ? 184 GLU A C   1 
ATOM   1404 O  O   . GLU A 1 184 ? -12.700 7.277   29.094  1.00 35.27  ? 184 GLU A O   1 
ATOM   1405 C  CB  . GLU A 1 184 ? -13.255 10.028  29.947  1.00 45.76  ? 184 GLU A CB  1 
ATOM   1406 C  CG  . GLU A 1 184 ? -12.222 10.884  30.601  1.00 47.13  ? 184 GLU A CG  1 
ATOM   1407 C  CD  . GLU A 1 184 ? -12.742 11.399  31.922  1.00 50.44  ? 184 GLU A CD  1 
ATOM   1408 O  OE1 . GLU A 1 184 ? -12.668 12.623  32.134  1.00 49.93  ? 184 GLU A OE1 1 
ATOM   1409 O  OE2 . GLU A 1 184 ? -13.252 10.573  32.718  1.00 50.12  ? 184 GLU A OE2 1 
ATOM   1410 N  N   . SER A 1 185 ? -10.865 8.357   28.354  1.00 33.41  ? 185 SER A N   1 
ATOM   1411 C  CA  . SER A 1 185 ? -10.046 7.165   28.324  1.00 33.81  ? 185 SER A CA  1 
ATOM   1412 C  C   . SER A 1 185 ? -8.591  7.567   28.157  1.00 35.37  ? 185 SER A C   1 
ATOM   1413 O  O   . SER A 1 185 ? -8.279  8.722   27.866  1.00 37.84  ? 185 SER A O   1 
ATOM   1414 C  CB  . SER A 1 185 ? -10.466 6.272   27.145  1.00 38.04  ? 185 SER A CB  1 
ATOM   1415 O  OG  . SER A 1 185 ? -9.984  6.815   25.923  1.00 40.68  ? 185 SER A OG  1 
ATOM   1416 N  N   . SER A 1 186 ? -7.705  6.601   28.346  1.00 32.40  ? 186 SER A N   1 
ATOM   1417 C  CA  . SER A 1 186 ? -6.277  6.821   28.214  1.00 32.22  ? 186 SER A CA  1 
ATOM   1418 C  C   . SER A 1 186 ? -5.689  5.843   27.168  1.00 27.97  ? 186 SER A C   1 
ATOM   1419 O  O   . SER A 1 186 ? -6.219  4.787   26.944  1.00 30.68  ? 186 SER A O   1 
ATOM   1420 C  CB  . SER A 1 186 ? -5.598  6.594   29.576  1.00 26.81  ? 186 SER A CB  1 
ATOM   1421 O  OG  . SER A 1 186 ? -5.768  5.239   30.031  1.00 28.47  ? 186 SER A OG  1 
ATOM   1422 N  N   . LEU A 1 187 ? -4.567  6.203   26.582  1.00 30.50  ? 187 LEU A N   1 
ATOM   1423 C  CA  . LEU A 1 187 ? -3.762  5.264   25.782  1.00 30.99  ? 187 LEU A CA  1 
ATOM   1424 C  C   . LEU A 1 187 ? -3.384  3.998   26.568  1.00 32.46  ? 187 LEU A C   1 
ATOM   1425 O  O   . LEU A 1 187 ? -3.316  2.908   26.011  1.00 25.96  ? 187 LEU A O   1 
ATOM   1426 C  CB  . LEU A 1 187 ? -2.502  5.994   25.350  1.00 28.24  ? 187 LEU A CB  1 
ATOM   1427 C  CG  . LEU A 1 187 ? -2.953  7.136   24.423  1.00 30.42  ? 187 LEU A CG  1 
ATOM   1428 C  CD1 . LEU A 1 187 ? -1.793  8.036   24.019  1.00 33.86  ? 187 LEU A CD1 1 
ATOM   1429 C  CD2 . LEU A 1 187 ? -3.647  6.557   23.200  1.00 28.45  ? 187 LEU A CD2 1 
ATOM   1430 N  N   . LEU A 1 188 ? -3.186  4.166   27.879  1.00 34.63  ? 188 LEU A N   1 
ATOM   1431 C  CA  . LEU A 1 188 ? -2.806  3.076   28.761  1.00 39.81  ? 188 LEU A CA  1 
ATOM   1432 C  C   . LEU A 1 188 ? -3.860  1.988   28.797  1.00 37.02  ? 188 LEU A C   1 
ATOM   1433 O  O   . LEU A 1 188 ? -3.499  0.817   28.879  1.00 36.48  ? 188 LEU A O   1 
ATOM   1434 C  CB  . LEU A 1 188 ? -2.510  3.583   30.172  1.00 43.78  ? 188 LEU A CB  1 
ATOM   1435 C  CG  . LEU A 1 188 ? -1.550  2.728   31.011  1.00 50.57  ? 188 LEU A CG  1 
ATOM   1436 C  CD1 . LEU A 1 188 ? -0.268  2.352   30.254  1.00 52.98  ? 188 LEU A CD1 1 
ATOM   1437 C  CD2 . LEU A 1 188 ? -1.201  3.460   32.299  1.00 51.25  ? 188 LEU A CD2 1 
ATOM   1438 N  N   . ASP A 1 189 ? -5.138  2.392   28.691  1.00 33.40  ? 189 ASP A N   1 
ATOM   1439 C  CA  . ASP A 1 189 ? -6.296  1.498   28.699  1.00 33.19  ? 189 ASP A CA  1 
ATOM   1440 C  C   . ASP A 1 189 ? -6.266  0.521   27.533  1.00 37.41  ? 189 ASP A C   1 
ATOM   1441 O  O   . ASP A 1 189 ? -6.894  -0.538  27.607  1.00 39.23  ? 189 ASP A O   1 
ATOM   1442 C  CB  . ASP A 1 189 ? -7.603  2.282   28.502  1.00 38.21  ? 189 ASP A CB  1 
ATOM   1443 C  CG  . ASP A 1 189 ? -8.141  2.945   29.776  1.00 43.94  ? 189 ASP A CG  1 
ATOM   1444 O  OD1 . ASP A 1 189 ? -7.415  3.007   30.783  1.00 45.65  ? 189 ASP A OD1 1 
ATOM   1445 O  OD2 . ASP A 1 189 ? -9.308  3.432   29.739  1.00 41.00  ? 189 ASP A OD2 1 
ATOM   1446 N  N   . LEU A 1 190 ? -5.634  0.919   26.424  1.00 35.14  ? 190 LEU A N   1 
ATOM   1447 C  CA  . LEU A 1 190 ? -5.594  0.072   25.228  1.00 36.19  ? 190 LEU A CA  1 
ATOM   1448 C  C   . LEU A 1 190 ? -4.333  -0.839  25.225  1.00 35.93  ? 190 LEU A C   1 
ATOM   1449 O  O   . LEU A 1 190 ? -4.274  -1.863  24.544  1.00 37.57  ? 190 LEU A O   1 
ATOM   1450 C  CB  . LEU A 1 190 ? -5.710  0.935   23.943  1.00 35.83  ? 190 LEU A CB  1 
ATOM   1451 C  CG  . LEU A 1 190 ? -6.818  1.991   23.880  1.00 29.31  ? 190 LEU A CG  1 
ATOM   1452 C  CD1 . LEU A 1 190 ? -6.492  3.108   22.931  1.00 30.29  ? 190 LEU A CD1 1 
ATOM   1453 C  CD2 . LEU A 1 190 ? -8.160  1.388   23.499  1.00 34.12  ? 190 LEU A CD2 1 
ATOM   1454 N  N   . LEU A 1 191 ? -3.338  -0.458  26.007  1.00 40.80  ? 191 LEU A N   1 
ATOM   1455 C  CA  . LEU A 1 191 ? -2.109  -1.222  26.123  1.00 40.93  ? 191 LEU A CA  1 
ATOM   1456 C  C   . LEU A 1 191 ? -2.245  -2.493  26.995  1.00 46.46  ? 191 LEU A C   1 
ATOM   1457 O  O   . LEU A 1 191 ? -3.218  -2.631  27.773  1.00 45.17  ? 191 LEU A O   1 
ATOM   1458 C  CB  . LEU A 1 191 ? -0.987  -0.318  26.628  1.00 38.00  ? 191 LEU A CB  1 
ATOM   1459 C  CG  . LEU A 1 191 ? -0.495  0.806   25.731  1.00 38.76  ? 191 LEU A CG  1 
ATOM   1460 C  CD1 . LEU A 1 191 ? 1.019   0.748   25.590  1.00 38.48  ? 191 LEU A CD1 1 
ATOM   1461 C  CD2 . LEU A 1 191 ? -1.109  0.732   24.352  1.00 44.67  ? 191 LEU A CD2 1 
ATOM   1462 N  N   . PRO A 1 192 ? -1.311  -3.453  26.826  1.00 48.44  ? 192 PRO A N   1 
ATOM   1463 C  CA  . PRO A 1 192 ? -1.304  -4.605  27.740  1.00 47.25  ? 192 PRO A CA  1 
ATOM   1464 C  C   . PRO A 1 192 ? -0.397  -4.267  28.918  1.00 47.32  ? 192 PRO A C   1 
ATOM   1465 O  O   . PRO A 1 192 ? 0.316   -3.263  28.871  1.00 44.92  ? 192 PRO A O   1 
ATOM   1466 C  CB  . PRO A 1 192 ? -0.721  -5.740  26.882  1.00 47.39  ? 192 PRO A CB  1 
ATOM   1467 C  CG  . PRO A 1 192 ? 0.083   -5.069  25.802  1.00 43.49  ? 192 PRO A CG  1 
ATOM   1468 C  CD  . PRO A 1 192 ? -0.320  -3.606  25.735  1.00 47.86  ? 192 PRO A CD  1 
ATOM   1469 N  N   . LYS A 1 193 ? -0.430  -5.069  29.973  1.00 53.08  ? 193 LYS A N   1 
ATOM   1470 C  CA  . LYS A 1 193 ? 0.393   -4.783  31.164  1.00 55.81  ? 193 LYS A CA  1 
ATOM   1471 C  C   . LYS A 1 193 ? 1.883   -4.778  30.777  1.00 55.21  ? 193 LYS A C   1 
ATOM   1472 O  O   . LYS A 1 193 ? 2.239   -5.330  29.724  1.00 51.30  ? 193 LYS A O   1 
ATOM   1473 C  CB  . LYS A 1 193 ? 0.061   -5.759  32.306  1.00 59.73  ? 193 LYS A CB  1 
ATOM   1474 C  CG  . LYS A 1 193 ? -1.435  -6.055  32.430  1.00 56.42  ? 193 LYS A CG  1 
ATOM   1475 C  CD  . LYS A 1 193 ? -1.971  -5.881  33.841  1.00 63.79  ? 193 LYS A CD  1 
ATOM   1476 C  CE  . LYS A 1 193 ? -3.455  -5.514  33.822  1.00 63.61  ? 193 LYS A CE  1 
ATOM   1477 N  NZ  . LYS A 1 193 ? -4.046  -5.474  35.185  1.00 60.68  ? 193 LYS A NZ  1 
ATOM   1478 N  N   . GLU A 1 194 ? 2.732   -4.146  31.596  1.00 52.08  ? 194 GLU A N   1 
ATOM   1479 C  CA  . GLU A 1 194 ? 4.142   -3.876  31.230  1.00 55.69  ? 194 GLU A CA  1 
ATOM   1480 C  C   . GLU A 1 194 ? 5.034   -5.103  30.932  1.00 55.07  ? 194 GLU A C   1 
ATOM   1481 O  O   . GLU A 1 194 ? 5.999   -4.980  30.183  1.00 57.07  ? 194 GLU A O   1 
ATOM   1482 C  CB  . GLU A 1 194 ? 4.843   -2.922  32.237  1.00 58.19  ? 194 GLU A CB  1 
ATOM   1483 C  CG  . GLU A 1 194 ? 4.090   -1.621  32.602  1.00 60.58  ? 194 GLU A CG  1 
ATOM   1484 C  CD  . GLU A 1 194 ? 4.555   -0.345  31.863  1.00 64.25  ? 194 GLU A CD  1 
ATOM   1485 O  OE1 . GLU A 1 194 ? 5.779   -0.162  31.637  1.00 67.33  ? 194 GLU A OE1 1 
ATOM   1486 O  OE2 . GLU A 1 194 ? 3.693   0.512   31.530  1.00 58.08  ? 194 GLU A OE2 1 
ATOM   1487 N  N   A GLU A 1 195 ? 4.721   -6.247  31.538  0.50 54.51  ? 195 GLU A N   1 
ATOM   1488 N  N   B GLU A 1 195 ? 4.717   -6.264  31.506  0.50 53.28  ? 195 GLU A N   1 
ATOM   1489 C  CA  A GLU A 1 195 ? 5.455   -7.484  31.274  0.50 54.50  ? 195 GLU A CA  1 
ATOM   1490 C  CA  B GLU A 1 195 ? 5.506   -7.478  31.251  0.50 52.65  ? 195 GLU A CA  1 
ATOM   1491 C  C   A GLU A 1 195 ? 5.259   -7.924  29.828  0.50 53.61  ? 195 GLU A C   1 
ATOM   1492 C  C   B GLU A 1 195 ? 5.235   -8.036  29.852  0.50 52.51  ? 195 GLU A C   1 
ATOM   1493 O  O   A GLU A 1 195 ? 6.217   -8.329  29.158  0.50 51.79  ? 195 GLU A O   1 
ATOM   1494 O  O   B GLU A 1 195 ? 6.123   -8.633  29.234  0.50 50.86  ? 195 GLU A O   1 
ATOM   1495 C  CB  A GLU A 1 195 ? 5.060   -8.612  32.249  0.50 55.78  ? 195 GLU A CB  1 
ATOM   1496 C  CB  B GLU A 1 195 ? 5.315   -8.552  32.350  0.50 52.45  ? 195 GLU A CB  1 
ATOM   1497 C  CG  A GLU A 1 195 ? 3.617   -8.578  32.729  0.50 52.88  ? 195 GLU A CG  1 
ATOM   1498 C  CG  B GLU A 1 195 ? 4.298   -9.648  32.060  0.50 47.64  ? 195 GLU A CG  1 
ATOM   1499 C  CD  A GLU A 1 195 ? 3.333   -7.378  33.604  0.50 53.18  ? 195 GLU A CD  1 
ATOM   1500 C  CD  B GLU A 1 195 ? 4.876   -10.803 31.255  0.50 45.81  ? 195 GLU A CD  1 
ATOM   1501 O  OE1 A GLU A 1 195 ? 2.241   -7.314  34.206  0.50 53.57  ? 195 GLU A OE1 1 
ATOM   1502 O  OE1 B GLU A 1 195 ? 6.120   -10.917 31.171  0.50 43.14  ? 195 GLU A OE1 1 
ATOM   1503 O  OE2 A GLU A 1 195 ? 4.208   -6.493  33.688  0.50 55.04  ? 195 GLU A OE2 1 
ATOM   1504 O  OE2 B GLU A 1 195 ? 4.080   -11.602 30.709  0.50 43.48  ? 195 GLU A OE2 1 
ATOM   1505 N  N   . LYS A 1 196 ? 4.019   -7.815  29.353  1.00 49.29  ? 196 LYS A N   1 
ATOM   1506 C  CA  . LYS A 1 196 ? 3.683   -8.113  27.958  1.00 48.16  ? 196 LYS A CA  1 
ATOM   1507 C  C   . LYS A 1 196 ? 4.377   -7.179  26.956  1.00 40.66  ? 196 LYS A C   1 
ATOM   1508 O  O   . LYS A 1 196 ? 4.344   -7.421  25.756  1.00 41.91  ? 196 LYS A O   1 
ATOM   1509 C  CB  . LYS A 1 196 ? 2.167   -8.094  27.749  1.00 50.31  ? 196 LYS A CB  1 
ATOM   1510 C  CG  . LYS A 1 196 ? 1.357   -8.971  28.702  1.00 51.77  ? 196 LYS A CG  1 
ATOM   1511 C  CD  . LYS A 1 196 ? 1.765   -10.439 28.693  1.00 55.20  ? 196 LYS A CD  1 
ATOM   1512 C  CE  . LYS A 1 196 ? 1.737   -11.058 27.297  1.00 55.38  ? 196 LYS A CE  1 
ATOM   1513 N  NZ  . LYS A 1 196 ? 0.457   -10.865 26.550  1.00 54.24  ? 196 LYS A NZ  1 
ATOM   1514 N  N   . LEU A 1 197 ? 4.998   -6.129  27.488  1.00 37.69  ? 197 LEU A N   1 
ATOM   1515 C  CA  . LEU A 1 197 ? 5.697   -5.059  26.806  1.00 36.02  ? 197 LEU A CA  1 
ATOM   1516 C  C   . LEU A 1 197 ? 7.206   -5.267  26.775  1.00 39.47  ? 197 LEU A C   1 
ATOM   1517 O  O   . LEU A 1 197 ? 7.909   -4.502  26.106  1.00 44.68  ? 197 LEU A O   1 
ATOM   1518 C  CB  . LEU A 1 197 ? 5.431   -3.725  27.531  1.00 36.43  ? 197 LEU A CB  1 
ATOM   1519 C  CG  . LEU A 1 197 ? 4.568   -2.653  26.850  1.00 35.76  ? 197 LEU A CG  1 
ATOM   1520 C  CD1 . LEU A 1 197 ? 3.453   -3.325  26.063  1.00 32.10  ? 197 LEU A CD1 1 
ATOM   1521 C  CD2 . LEU A 1 197 ? 4.015   -1.678  27.890  1.00 35.66  ? 197 LEU A CD2 1 
ATOM   1522 N  N   . ARG A 1 198 ? 7.730   -6.266  27.489  1.00 40.07  ? 198 ARG A N   1 
ATOM   1523 C  CA  . ARG A 1 198 ? 9.199   -6.415  27.521  1.00 41.42  ? 198 ARG A CA  1 
ATOM   1524 C  C   . ARG A 1 198 ? 9.805   -6.974  26.213  1.00 38.17  ? 198 ARG A C   1 
ATOM   1525 O  O   . ARG A 1 198 ? 10.924  -6.573  25.825  1.00 36.23  ? 198 ARG A O   1 
ATOM   1526 C  CB  . ARG A 1 198 ? 9.673   -7.210  28.744  1.00 45.13  ? 198 ARG A CB  1 
ATOM   1527 C  CG  . ARG A 1 198 ? 11.178  -7.114  29.023  1.00 50.77  ? 198 ARG A CG  1 
ATOM   1528 C  CD  . ARG A 1 198 ? 11.549  -6.001  30.005  1.00 58.56  ? 198 ARG A CD  1 
ATOM   1529 N  NE  . ARG A 1 198 ? 12.848  -5.354  29.727  1.00 59.41  ? 198 ARG A NE  1 
ATOM   1530 C  CZ  . ARG A 1 198 ? 13.620  -4.755  30.649  1.00 62.60  ? 198 ARG A CZ  1 
ATOM   1531 N  NH1 . ARG A 1 198 ? 13.253  -4.732  31.933  1.00 58.93  ? 198 ARG A NH1 1 
ATOM   1532 N  NH2 . ARG A 1 198 ? 14.786  -4.203  30.296  1.00 57.40  ? 198 ARG A NH2 1 
ATOM   1533 N  N   . HIS A 1 199 ? 9.068   -7.884  25.554  1.00 35.05  ? 199 HIS A N   1 
ATOM   1534 C  CA  . HIS A 1 199 ? 9.480   -8.513  24.279  1.00 37.31  ? 199 HIS A CA  1 
ATOM   1535 C  C   . HIS A 1 199 ? 8.964   -7.861  22.994  1.00 35.38  ? 199 HIS A C   1 
ATOM   1536 O  O   . HIS A 1 199 ? 7.753   -7.803  22.755  1.00 32.72  ? 199 HIS A O   1 
ATOM   1537 C  CB  . HIS A 1 199 ? 9.086   -9.982  24.290  1.00 42.79  ? 199 HIS A CB  1 
ATOM   1538 C  CG  . HIS A 1 199 ? 9.666   -10.731 25.448  1.00 53.61  ? 199 HIS A CG  1 
ATOM   1539 N  ND1 . HIS A 1 199 ? 10.996  -10.945 25.576  1.00 53.58  ? 199 HIS A ND1 1 
ATOM   1540 C  CD2 . HIS A 1 199 ? 9.061   -11.288 26.572  1.00 50.16  ? 199 HIS A CD2 1 
ATOM   1541 C  CE1 . HIS A 1 199 ? 11.222  -11.608 26.722  1.00 58.91  ? 199 HIS A CE1 1 
ATOM   1542 N  NE2 . HIS A 1 199 ? 10.036  -11.819 27.328  1.00 59.97  ? 199 HIS A NE2 1 
ATOM   1543 N  N   . TYR A 1 200 ? 9.881   -7.406  22.139  1.00 32.48  ? 200 TYR A N   1 
ATOM   1544 C  CA  . TYR A 1 200 ? 9.478   -6.866  20.840  1.00 32.63  ? 200 TYR A CA  1 
ATOM   1545 C  C   . TYR A 1 200 ? 10.564  -6.886  19.771  1.00 32.88  ? 200 TYR A C   1 
ATOM   1546 O  O   . TYR A 1 200 ? 11.775  -6.830  20.061  1.00 29.29  ? 200 TYR A O   1 
ATOM   1547 C  CB  . TYR A 1 200 ? 9.057   -5.412  21.024  1.00 31.43  ? 200 TYR A CB  1 
ATOM   1548 C  CG  . TYR A 1 200 ? 10.167  -4.586  21.584  1.00 28.55  ? 200 TYR A CG  1 
ATOM   1549 C  CD1 . TYR A 1 200 ? 11.121  -4.012  20.732  1.00 27.64  ? 200 TYR A CD1 1 
ATOM   1550 C  CD2 . TYR A 1 200 ? 10.272  -4.368  22.967  1.00 29.78  ? 200 TYR A CD2 1 
ATOM   1551 C  CE1 . TYR A 1 200 ? 12.158  -3.250  21.226  1.00 28.14  ? 200 TYR A CE1 1 
ATOM   1552 C  CE2 . TYR A 1 200 ? 11.314  -3.590  23.479  1.00 32.24  ? 200 TYR A CE2 1 
ATOM   1553 C  CZ  . TYR A 1 200 ? 12.264  -3.070  22.601  1.00 29.33  ? 200 TYR A CZ  1 
ATOM   1554 O  OH  . TYR A 1 200 ? 13.276  -2.314  23.076  1.00 28.60  ? 200 TYR A OH  1 
ATOM   1555 N  N   . PHE A 1 201 ? 10.110  -6.840  18.523  1.00 33.44  ? 201 PHE A N   1 
ATOM   1556 C  CA  . PHE A 1 201 ? 11.013  -6.816  17.374  1.00 30.13  ? 201 PHE A CA  1 
ATOM   1557 C  C   . PHE A 1 201 ? 11.225  -5.381  16.829  1.00 32.57  ? 201 PHE A C   1 
ATOM   1558 O  O   . PHE A 1 201 ? 10.380  -4.499  17.038  1.00 28.08  ? 201 PHE A O   1 
ATOM   1559 C  CB  . PHE A 1 201 ? 10.482  -7.782  16.331  1.00 31.46  ? 201 PHE A CB  1 
ATOM   1560 C  CG  . PHE A 1 201 ? 10.223  -9.186  16.862  1.00 32.86  ? 201 PHE A CG  1 
ATOM   1561 C  CD1 . PHE A 1 201 ? 11.214  -10.163 16.810  1.00 34.73  ? 201 PHE A CD1 1 
ATOM   1562 C  CD2 . PHE A 1 201 ? 8.998   -9.530  17.398  1.00 34.37  ? 201 PHE A CD2 1 
ATOM   1563 C  CE1 . PHE A 1 201 ? 10.967  -11.442 17.295  1.00 37.67  ? 201 PHE A CE1 1 
ATOM   1564 C  CE2 . PHE A 1 201 ? 8.743   -10.790 17.891  1.00 37.42  ? 201 PHE A CE2 1 
ATOM   1565 C  CZ  . PHE A 1 201 ? 9.728   -11.767 17.830  1.00 37.20  ? 201 PHE A CZ  1 
ATOM   1566 N  N   . ARG A 1 202 ? 12.380  -5.139  16.190  1.00 29.19  ? 202 ARG A N   1 
ATOM   1567 C  CA  . ARG A 1 202 ? 12.743  -3.826  15.699  1.00 32.71  ? 202 ARG A CA  1 
ATOM   1568 C  C   . ARG A 1 202 ? 13.367  -3.917  14.299  1.00 33.22  ? 202 ARG A C   1 
ATOM   1569 O  O   . ARG A 1 202 ? 14.132  -4.816  14.033  1.00 35.49  ? 202 ARG A O   1 
ATOM   1570 C  CB  . ARG A 1 202 ? 13.725  -3.120  16.678  1.00 31.94  ? 202 ARG A CB  1 
ATOM   1571 C  CG  . ARG A 1 202 ? 14.495  -1.934  16.112  1.00 28.62  ? 202 ARG A CG  1 
ATOM   1572 C  CD  . ARG A 1 202 ? 13.644  -0.697  15.943  1.00 29.37  ? 202 ARG A CD  1 
ATOM   1573 N  NE  . ARG A 1 202 ? 12.760  -0.519  17.093  1.00 33.58  ? 202 ARG A NE  1 
ATOM   1574 C  CZ  . ARG A 1 202 ? 13.133  0.011   18.242  1.00 31.92  ? 202 ARG A CZ  1 
ATOM   1575 N  NH1 . ARG A 1 202 ? 14.377  0.446   18.386  1.00 32.48  ? 202 ARG A NH1 1 
ATOM   1576 N  NH2 . ARG A 1 202 ? 12.260  0.098   19.245  1.00 36.79  ? 202 ARG A NH2 1 
ATOM   1577 N  N   . TYR A 1 203 ? 13.008  -2.983  13.424  1.00 33.81  ? 203 TYR A N   1 
ATOM   1578 C  CA  . TYR A 1 203 ? 13.597  -2.877  12.109  1.00 34.32  ? 203 TYR A CA  1 
ATOM   1579 C  C   . TYR A 1 203 ? 13.130  -1.551  11.509  1.00 37.53  ? 203 TYR A C   1 
ATOM   1580 O  O   . TYR A 1 203 ? 12.114  -0.974  11.929  1.00 34.68  ? 203 TYR A O   1 
ATOM   1581 C  CB  . TYR A 1 203 ? 13.207  -4.078  11.206  1.00 33.67  ? 203 TYR A CB  1 
ATOM   1582 C  CG  . TYR A 1 203 ? 11.830  -3.950  10.620  1.00 32.67  ? 203 TYR A CG  1 
ATOM   1583 C  CD1 . TYR A 1 203 ? 10.706  -4.424  11.296  1.00 30.31  ? 203 TYR A CD1 1 
ATOM   1584 C  CD2 . TYR A 1 203 ? 11.648  -3.322  9.384   1.00 33.11  ? 203 TYR A CD2 1 
ATOM   1585 C  CE1 . TYR A 1 203 ? 9.434   -4.267  10.755  1.00 28.81  ? 203 TYR A CE1 1 
ATOM   1586 C  CE2 . TYR A 1 203 ? 10.394  -3.151  8.843   1.00 29.46  ? 203 TYR A CE2 1 
ATOM   1587 C  CZ  . TYR A 1 203 ? 9.292   -3.612  9.527   1.00 28.35  ? 203 TYR A CZ  1 
ATOM   1588 O  OH  . TYR A 1 203 ? 8.063   -3.390  8.959   1.00 25.89  ? 203 TYR A OH  1 
ATOM   1589 N  N   . LEU A 1 204 ? 13.905  -1.111  10.524  1.00 34.16  ? 204 LEU A N   1 
ATOM   1590 C  CA  . LEU A 1 204 ? 13.735  0.094   9.773   1.00 37.47  ? 204 LEU A CA  1 
ATOM   1591 C  C   . LEU A 1 204 ? 12.947  -0.127  8.479   1.00 37.26  ? 204 LEU A C   1 
ATOM   1592 O  O   . LEU A 1 204 ? 13.248  -1.023  7.696   1.00 41.54  ? 204 LEU A O   1 
ATOM   1593 C  CB  . LEU A 1 204 ? 15.130  0.635   9.461   1.00 39.85  ? 204 LEU A CB  1 
ATOM   1594 C  CG  . LEU A 1 204 ? 15.869  1.205   10.666  1.00 37.16  ? 204 LEU A CG  1 
ATOM   1595 C  CD1 . LEU A 1 204 ? 17.185  1.821   10.210  1.00 37.81  ? 204 LEU A CD1 1 
ATOM   1596 C  CD2 . LEU A 1 204 ? 15.018  2.265   11.379  1.00 36.71  ? 204 LEU A CD2 1 
ATOM   1597 N  N   . GLY A 1 205 ? 11.928  0.692   8.267   1.00 37.10  ? 205 GLY A N   1 
ATOM   1598 C  CA  . GLY A 1 205 ? 10.999  0.459   7.183   1.00 36.36  ? 205 GLY A CA  1 
ATOM   1599 C  C   . GLY A 1 205 ? 10.293  1.704   6.724   1.00 32.63  ? 205 GLY A C   1 
ATOM   1600 O  O   . GLY A 1 205 ? 10.876  2.790   6.743   1.00 35.64  ? 205 GLY A O   1 
ATOM   1601 N  N   . SER A 1 206 ? 9.025   1.537   6.336   1.00 33.85  ? 206 SER A N   1 
ATOM   1602 C  CA  . SER A 1 206 ? 8.226   2.613   5.709   1.00 31.93  ? 206 SER A CA  1 
ATOM   1603 C  C   . SER A 1 206 ? 6.850   2.701   6.342   1.00 30.19  ? 206 SER A C   1 
ATOM   1604 O  O   . SER A 1 206 ? 6.506   1.846   7.162   1.00 27.65  ? 206 SER A O   1 
ATOM   1605 C  CB  . SER A 1 206 ? 8.078   2.409   4.181   1.00 34.31  ? 206 SER A CB  1 
ATOM   1606 O  OG  . SER A 1 206 ? 7.121   1.407   3.867   1.00 34.08  ? 206 SER A OG  1 
ATOM   1607 N  N   . LEU A 1 207 ? 6.091   3.669   5.885   1.00 30.14  ? 207 LEU A N   1 
ATOM   1608 C  CA  . LEU A 1 207 ? 4.685   3.840   6.243   1.00 35.66  ? 207 LEU A CA  1 
ATOM   1609 C  C   . LEU A 1 207 ? 4.066   2.769   5.405   1.00 34.17  ? 207 LEU A C   1 
ATOM   1610 O  O   . LEU A 1 207 ? 4.671   2.410   4.410   1.00 36.50  ? 207 LEU A O   1 
ATOM   1611 C  CB  . LEU A 1 207 ? 4.150   5.183   5.746   1.00 35.52  ? 207 LEU A CB  1 
ATOM   1612 C  CG  . LEU A 1 207 ? 4.549   6.527   6.357   1.00 35.76  ? 207 LEU A CG  1 
ATOM   1613 C  CD1 . LEU A 1 207 ? 3.491   7.567   6.019   1.00 35.57  ? 207 LEU A CD1 1 
ATOM   1614 C  CD2 . LEU A 1 207 ? 4.737   6.424   7.862   1.00 39.98  ? 207 LEU A CD2 1 
ATOM   1615 N  N   . THR A 1 208 ? 2.900   2.240   5.782   1.00 30.82  ? 208 THR A N   1 
ATOM   1616 C  CA  . THR A 1 208 ? 2.399   1.093   5.022   1.00 27.58  ? 208 THR A CA  1 
ATOM   1617 C  C   . THR A 1 208 ? 1.291   1.570   4.134   1.00 25.05  ? 208 THR A C   1 
ATOM   1618 O  O   . THR A 1 208 ? 0.565   0.775   3.585   1.00 24.35  ? 208 THR A O   1 
ATOM   1619 C  CB  . THR A 1 208 ? 1.873   -0.062  5.903   1.00 27.51  ? 208 THR A CB  1 
ATOM   1620 O  OG1 . THR A 1 208 ? 0.763   0.394   6.689   1.00 25.49  ? 208 THR A OG1 1 
ATOM   1621 C  CG2 . THR A 1 208 ? 2.964   -0.630  6.788   1.00 27.93  ? 208 THR A CG2 1 
ATOM   1622 N  N   . THR A 1 209 ? 1.143   2.887   4.042   1.00 21.67  ? 209 THR A N   1 
ATOM   1623 C  CA  . THR A 1 209 ? 0.176   3.517   3.139   1.00 24.90  ? 209 THR A CA  1 
ATOM   1624 C  C   . THR A 1 209 ? 0.895   4.627   2.390   1.00 24.83  ? 209 THR A C   1 
ATOM   1625 O  O   . THR A 1 209 ? 1.985   5.075   2.854   1.00 27.61  ? 209 THR A O   1 
ATOM   1626 C  CB  . THR A 1 209 ? -0.987  4.165   3.899   1.00 21.29  ? 209 THR A CB  1 
ATOM   1627 O  OG1 . THR A 1 209 ? -0.455  5.238   4.655   1.00 21.79  ? 209 THR A OG1 1 
ATOM   1628 C  CG2 . THR A 1 209 ? -1.668  3.115   4.810   1.00 18.20  ? 209 THR A CG2 1 
ATOM   1629 N  N   . PRO A 1 210 ? 0.367   5.020   1.208   1.00 26.55  ? 210 PRO A N   1 
ATOM   1630 C  CA  . PRO A 1 210 ? 1.100   6.004   0.363   1.00 28.49  ? 210 PRO A CA  1 
ATOM   1631 C  C   . PRO A 1 210 ? 1.267   7.297   1.151   1.00 30.21  ? 210 PRO A C   1 
ATOM   1632 O  O   . PRO A 1 210 ? 0.306   7.742   1.758   1.00 31.75  ? 210 PRO A O   1 
ATOM   1633 C  CB  . PRO A 1 210 ? 0.180   6.186   -0.858  1.00 26.28  ? 210 PRO A CB  1 
ATOM   1634 C  CG  . PRO A 1 210 ? -0.622  4.931   -0.904  1.00 28.40  ? 210 PRO A CG  1 
ATOM   1635 C  CD  . PRO A 1 210 ? -0.875  4.576   0.545   1.00 26.64  ? 210 PRO A CD  1 
ATOM   1636 N  N   . THR A 1 211 ? 2.454   7.899   1.146   1.00 31.03  ? 211 THR A N   1 
ATOM   1637 C  CA  . THR A 1 211 ? 3.470   7.711   0.082   1.00 33.60  ? 211 THR A CA  1 
ATOM   1638 C  C   . THR A 1 211 ? 4.568   6.723   0.383   1.00 30.43  ? 211 THR A C   1 
ATOM   1639 O  O   . THR A 1 211 ? 5.576   6.672   -0.327  1.00 34.55  ? 211 THR A O   1 
ATOM   1640 C  CB  . THR A 1 211 ? 4.087   9.061   -0.316  1.00 34.56  ? 211 THR A CB  1 
ATOM   1641 O  OG1 . THR A 1 211 ? 4.430   9.802   0.872   1.00 41.14  ? 211 THR A OG1 1 
ATOM   1642 C  CG2 . THR A 1 211 ? 3.073   9.880   -1.162  1.00 36.34  ? 211 THR A CG2 1 
ATOM   1643 N  N   . CYS A 1 212 ? 4.345   5.915   1.414   1.00 29.54  ? 212 CYS A N   1 
ATOM   1644 C  CA  . CYS A 1 212 ? 5.189   4.775   1.757   1.00 29.74  ? 212 CYS A CA  1 
ATOM   1645 C  C   . CYS A 1 212 ? 6.590   5.164   2.053   1.00 28.84  ? 212 CYS A C   1 
ATOM   1646 O  O   . CYS A 1 212 ? 7.504   4.396   1.791   1.00 27.47  ? 212 CYS A O   1 
ATOM   1647 C  CB  . CYS A 1 212 ? 5.235   3.727   0.657   1.00 28.92  ? 212 CYS A CB  1 
ATOM   1648 S  SG  . CYS A 1 212 ? 3.638   3.036   0.309   1.00 31.03  ? 212 CYS A SG  1 
ATOM   1649 N  N   . ASP A 1 213 ? 6.741   6.332   2.641   1.00 31.68  ? 213 ASP A N   1 
ATOM   1650 C  CA  . ASP A 1 213 ? 8.048   6.877   2.922   1.00 35.67  ? 213 ASP A CA  1 
ATOM   1651 C  C   . ASP A 1 213 ? 8.864   6.029   3.870   1.00 36.92  ? 213 ASP A C   1 
ATOM   1652 O  O   . ASP A 1 213 ? 8.363   5.543   4.896   1.00 32.79  ? 213 ASP A O   1 
ATOM   1653 C  CB  . ASP A 1 213 ? 7.895   8.296   3.449   1.00 38.50  ? 213 ASP A CB  1 
ATOM   1654 C  CG  . ASP A 1 213 ? 7.204   9.200   2.450   1.00 45.46  ? 213 ASP A CG  1 
ATOM   1655 O  OD1 . ASP A 1 213 ? 7.489   9.086   1.228   1.00 44.50  ? 213 ASP A OD1 1 
ATOM   1656 O  OD2 . ASP A 1 213 ? 6.367   10.025  2.893   1.00 52.18  ? 213 ASP A OD2 1 
ATOM   1657 N  N   . GLU A 1 214 ? 10.140  5.886   3.517   1.00 35.87  ? 214 GLU A N   1 
ATOM   1658 C  CA  . GLU A 1 214 ? 11.052  4.984   4.184   1.00 37.80  ? 214 GLU A CA  1 
ATOM   1659 C  C   . GLU A 1 214 ? 11.751  5.690   5.327   1.00 37.73  ? 214 GLU A C   1 
ATOM   1660 O  O   . GLU A 1 214 ? 12.950  5.923   5.323   1.00 35.99  ? 214 GLU A O   1 
ATOM   1661 C  CB  . GLU A 1 214 ? 12.031  4.324   3.185   1.00 38.65  ? 214 GLU A CB  1 
ATOM   1662 C  CG  . GLU A 1 214 ? 11.295  3.528   2.099   1.00 38.11  ? 214 GLU A CG  1 
ATOM   1663 C  CD  . GLU A 1 214 ? 12.200  2.717   1.184   1.00 42.13  ? 214 GLU A CD  1 
ATOM   1664 O  OE1 . GLU A 1 214 ? 13.362  3.118   0.958   1.00 39.82  ? 214 GLU A OE1 1 
ATOM   1665 O  OE2 . GLU A 1 214 ? 11.747  1.655   0.701   1.00 46.41  ? 214 GLU A OE2 1 
ATOM   1666 N  N   . LYS A 1 215 ? 10.967  6.010   6.340   1.00 37.48  ? 215 LYS A N   1 
ATOM   1667 C  CA  . LYS A 1 215 ? 11.479  6.796   7.435   1.00 38.23  ? 215 LYS A CA  1 
ATOM   1668 C  C   . LYS A 1 215 ? 10.936  6.336   8.763   1.00 35.25  ? 215 LYS A C   1 
ATOM   1669 O  O   . LYS A 1 215 ? 10.844  7.153   9.697   1.00 36.94  ? 215 LYS A O   1 
ATOM   1670 C  CB  . LYS A 1 215 ? 11.109  8.279   7.234   1.00 38.29  ? 215 LYS A CB  1 
ATOM   1671 C  CG  . LYS A 1 215 ? 9.624   8.550   7.096   1.00 36.66  ? 215 LYS A CG  1 
ATOM   1672 C  CD  . LYS A 1 215 ? 9.409   10.046  7.018   1.00 39.37  ? 215 LYS A CD  1 
ATOM   1673 C  CE  . LYS A 1 215 ? 7.988   10.376  6.618   1.00 42.90  ? 215 LYS A CE  1 
ATOM   1674 N  NZ  . LYS A 1 215 ? 7.549   11.620  7.305   1.00 44.76  ? 215 LYS A NZ  1 
ATOM   1675 N  N   . VAL A 1 216 ? 10.572  5.058   8.843   1.00 29.50  ? 216 VAL A N   1 
ATOM   1676 C  CA  . VAL A 1 216 ? 9.963   4.493   10.061  1.00 31.78  ? 216 VAL A CA  1 
ATOM   1677 C  C   . VAL A 1 216 ? 10.875  3.531   10.784  1.00 30.74  ? 216 VAL A C   1 
ATOM   1678 O  O   . VAL A 1 216 ? 11.368  2.554   10.190  1.00 32.83  ? 216 VAL A O   1 
ATOM   1679 C  CB  . VAL A 1 216 ? 8.635   3.777   9.761   1.00 29.87  ? 216 VAL A CB  1 
ATOM   1680 C  CG1 . VAL A 1 216 ? 7.955   3.343   11.043  1.00 32.92  ? 216 VAL A CG1 1 
ATOM   1681 C  CG2 . VAL A 1 216 ? 7.702   4.697   8.996   1.00 30.95  ? 216 VAL A CG2 1 
ATOM   1682 N  N   . VAL A 1 217 ? 11.122  3.801   12.060  1.00 28.12  ? 217 VAL A N   1 
ATOM   1683 C  CA  . VAL A 1 217 ? 11.745  2.808   12.893  1.00 29.64  ? 217 VAL A CA  1 
ATOM   1684 C  C   . VAL A 1 217 ? 10.602  2.014   13.503  1.00 30.82  ? 217 VAL A C   1 
ATOM   1685 O  O   . VAL A 1 217 ? 9.750   2.595   14.177  1.00 32.63  ? 217 VAL A O   1 
ATOM   1686 C  CB  . VAL A 1 217 ? 12.750  3.416   13.932  1.00 28.49  ? 217 VAL A CB  1 
ATOM   1687 C  CG1 . VAL A 1 217 ? 12.107  4.460   14.832  1.00 28.61  ? 217 VAL A CG1 1 
ATOM   1688 C  CG2 . VAL A 1 217 ? 13.374  2.325   14.794  1.00 31.07  ? 217 VAL A CG2 1 
ATOM   1689 N  N   . TRP A 1 218 ? 10.567  0.710   13.226  1.00 28.75  ? 218 TRP A N   1 
ATOM   1690 C  CA  . TRP A 1 218 ? 9.431   -0.132  13.589  1.00 28.76  ? 218 TRP A CA  1 
ATOM   1691 C  C   . TRP A 1 218 ? 9.589   -0.855  14.886  1.00 27.30  ? 218 TRP A C   1 
ATOM   1692 O  O   . TRP A 1 218 ? 10.702  -1.269  15.211  1.00 25.74  ? 218 TRP A O   1 
ATOM   1693 C  CB  . TRP A 1 218 ? 9.125   -1.135  12.479  1.00 27.14  ? 218 TRP A CB  1 
ATOM   1694 C  CG  . TRP A 1 218 ? 8.294   -0.535  11.384  1.00 27.39  ? 218 TRP A CG  1 
ATOM   1695 C  CD1 . TRP A 1 218 ? 8.733   0.011   10.183  1.00 26.82  ? 218 TRP A CD1 1 
ATOM   1696 C  CD2 . TRP A 1 218 ? 6.841   -0.366  11.373  1.00 24.40  ? 218 TRP A CD2 1 
ATOM   1697 N  NE1 . TRP A 1 218 ? 7.675   0.481   9.448   1.00 24.82  ? 218 TRP A NE1 1 
ATOM   1698 C  CE2 . TRP A 1 218 ? 6.513   0.285   10.102  1.00 25.49  ? 218 TRP A CE2 1 
ATOM   1699 C  CE3 . TRP A 1 218 ? 5.814   -0.686  12.254  1.00 27.92  ? 218 TRP A CE3 1 
ATOM   1700 C  CZ2 . TRP A 1 218 ? 5.212   0.594   9.756   1.00 23.83  ? 218 TRP A CZ2 1 
ATOM   1701 C  CZ3 . TRP A 1 218 ? 4.505   -0.369  11.887  1.00 25.57  ? 218 TRP A CZ3 1 
ATOM   1702 C  CH2 . TRP A 1 218 ? 4.216   0.258   10.671  1.00 25.20  ? 218 TRP A CH2 1 
ATOM   1703 N  N   . THR A 1 219 ? 8.486   -1.020  15.636  1.00 26.60  ? 219 THR A N   1 
ATOM   1704 C  CA  . THR A 1 219 ? 8.491   -1.854  16.844  1.00 24.48  ? 219 THR A CA  1 
ATOM   1705 C  C   . THR A 1 219 ? 7.245   -2.673  16.769  1.00 24.82  ? 219 THR A C   1 
ATOM   1706 O  O   . THR A 1 219 ? 6.151   -2.117  16.702  1.00 24.86  ? 219 THR A O   1 
ATOM   1707 C  CB  . THR A 1 219 ? 8.428   -1.051  18.191  1.00 25.80  ? 219 THR A CB  1 
ATOM   1708 O  OG1 . THR A 1 219 ? 9.464   -0.065  18.261  1.00 30.22  ? 219 THR A OG1 1 
ATOM   1709 C  CG2 . THR A 1 219 ? 8.551   -1.985  19.395  1.00 24.56  ? 219 THR A CG2 1 
ATOM   1710 N  N   . VAL A 1 220 ? 7.408   -3.992  16.817  1.00 25.56  ? 220 VAL A N   1 
ATOM   1711 C  CA  . VAL A 1 220 ? 6.305   -4.955  16.818  1.00 24.29  ? 220 VAL A CA  1 
ATOM   1712 C  C   . VAL A 1 220 ? 6.432   -5.821  18.086  1.00 28.78  ? 220 VAL A C   1 
ATOM   1713 O  O   . VAL A 1 220 ? 7.448   -6.513  18.303  1.00 34.21  ? 220 VAL A O   1 
ATOM   1714 C  CB  . VAL A 1 220 ? 6.336   -5.782  15.509  1.00 23.27  ? 220 VAL A CB  1 
ATOM   1715 C  CG1 . VAL A 1 220 ? 5.197   -6.815  15.446  1.00 23.25  ? 220 VAL A CG1 1 
ATOM   1716 C  CG2 . VAL A 1 220 ? 6.278   -4.854  14.312  1.00 22.16  ? 220 VAL A CG2 1 
ATOM   1717 N  N   . PHE A 1 221 ? 5.433   -5.741  18.962  1.00 33.14  ? 221 PHE A N   1 
ATOM   1718 C  CA  . PHE A 1 221 ? 5.512   -6.409  20.251  1.00 32.08  ? 221 PHE A CA  1 
ATOM   1719 C  C   . PHE A 1 221 ? 5.187   -7.870  20.067  1.00 29.22  ? 221 PHE A C   1 
ATOM   1720 O  O   . PHE A 1 221 ? 4.239   -8.208  19.363  1.00 30.39  ? 221 PHE A O   1 
ATOM   1721 C  CB  . PHE A 1 221 ? 4.615   -5.737  21.300  1.00 29.35  ? 221 PHE A CB  1 
ATOM   1722 C  CG  . PHE A 1 221 ? 5.108   -4.387  21.696  1.00 30.33  ? 221 PHE A CG  1 
ATOM   1723 C  CD1 . PHE A 1 221 ? 4.745   -3.260  20.957  1.00 28.55  ? 221 PHE A CD1 1 
ATOM   1724 C  CD2 . PHE A 1 221 ? 5.985   -4.242  22.778  1.00 27.24  ? 221 PHE A CD2 1 
ATOM   1725 C  CE1 . PHE A 1 221 ? 5.228   -1.997  21.315  1.00 26.66  ? 221 PHE A CE1 1 
ATOM   1726 C  CE2 . PHE A 1 221 ? 6.479   -2.999  23.115  1.00 28.54  ? 221 PHE A CE2 1 
ATOM   1727 C  CZ  . PHE A 1 221 ? 6.103   -1.883  22.395  1.00 26.21  ? 221 PHE A CZ  1 
ATOM   1728 N  N   . ARG A 1 222 ? 5.997   -8.720  20.679  1.00 30.82  ? 222 ARG A N   1 
ATOM   1729 C  CA  . ARG A 1 222 ? 5.888   -10.162 20.463  1.00 36.56  ? 222 ARG A CA  1 
ATOM   1730 C  C   . ARG A 1 222 ? 4.524   -10.710 20.881  1.00 36.43  ? 222 ARG A C   1 
ATOM   1731 O  O   . ARG A 1 222 ? 3.986   -11.594 20.237  1.00 36.71  ? 222 ARG A O   1 
ATOM   1732 C  CB  . ARG A 1 222 ? 7.033   -10.936 21.158  1.00 41.04  ? 222 ARG A CB  1 
ATOM   1733 C  CG  . ARG A 1 222 ? 7.217   -12.399 20.670  1.00 43.74  ? 222 ARG A CG  1 
ATOM   1734 C  CD  . ARG A 1 222 ? 8.127   -13.230 21.592  1.00 46.97  ? 222 ARG A CD  1 
ATOM   1735 N  NE  . ARG A 1 222 ? 7.515   -13.494 22.904  1.00 45.26  ? 222 ARG A NE  1 
ATOM   1736 C  CZ  . ARG A 1 222 ? 8.197   -13.607 24.045  1.00 50.28  ? 222 ARG A CZ  1 
ATOM   1737 N  NH1 . ARG A 1 222 ? 9.522   -13.483 24.051  1.00 45.64  ? 222 ARG A NH1 1 
ATOM   1738 N  NH2 . ARG A 1 222 ? 7.558   -13.842 25.185  1.00 47.24  ? 222 ARG A NH2 1 
ATOM   1739 N  N   . GLU A 1 223 ? 3.949   -10.148 21.927  1.00 39.51  ? 223 GLU A N   1 
ATOM   1740 C  CA  . GLU A 1 223 ? 2.667   -10.635 22.462  1.00 39.31  ? 223 GLU A CA  1 
ATOM   1741 C  C   . GLU A 1 223 ? 1.425   -9.852  21.975  1.00 32.07  ? 223 GLU A C   1 
ATOM   1742 O  O   . GLU A 1 223 ? 1.392   -8.651  22.126  1.00 30.59  ? 223 GLU A O   1 
ATOM   1743 C  CB  . GLU A 1 223 ? 2.734   -10.580 23.998  1.00 40.15  ? 223 GLU A CB  1 
ATOM   1744 C  CG  . GLU A 1 223 ? 3.888   -11.370 24.611  1.00 39.74  ? 223 GLU A CG  1 
ATOM   1745 C  CD  . GLU A 1 223 ? 3.869   -12.857 24.288  1.00 43.51  ? 223 GLU A CD  1 
ATOM   1746 O  OE1 . GLU A 1 223 ? 2.795   -13.410 23.972  1.00 38.66  ? 223 GLU A OE1 1 
ATOM   1747 O  OE2 . GLU A 1 223 ? 4.964   -13.483 24.338  1.00 48.15  ? 223 GLU A OE2 1 
ATOM   1748 N  N   . PRO A 1 224 ? 0.391   -10.552 21.436  1.00 34.53  ? 224 PRO A N   1 
ATOM   1749 C  CA  . PRO A 1 224 ? -0.887  -9.921  21.060  1.00 33.99  ? 224 PRO A CA  1 
ATOM   1750 C  C   . PRO A 1 224 ? -1.702  -9.330  22.199  1.00 39.14  ? 224 PRO A C   1 
ATOM   1751 O  O   . PRO A 1 224 ? -1.611  -9.793  23.340  1.00 38.54  ? 224 PRO A O   1 
ATOM   1752 C  CB  . PRO A 1 224 ? -1.707  -11.064 20.467  1.00 33.37  ? 224 PRO A CB  1 
ATOM   1753 C  CG  . PRO A 1 224 ? -1.020  -12.321 20.856  1.00 33.19  ? 224 PRO A CG  1 
ATOM   1754 C  CD  . PRO A 1 224 ? 0.418   -11.993 21.086  1.00 32.09  ? 224 PRO A CD  1 
ATOM   1755 N  N   . ILE A 1 225 ? -2.508  -8.318  21.860  1.00 36.54  ? 225 ILE A N   1 
ATOM   1756 C  CA  . ILE A 1 225 ? -3.581  -7.809  22.693  1.00 36.50  ? 225 ILE A CA  1 
ATOM   1757 C  C   . ILE A 1 225 ? -4.789  -8.683  22.433  1.00 36.89  ? 225 ILE A C   1 
ATOM   1758 O  O   . ILE A 1 225 ? -4.907  -9.277  21.355  1.00 35.56  ? 225 ILE A O   1 
ATOM   1759 C  CB  . ILE A 1 225 ? -3.931  -6.356  22.304  1.00 38.74  ? 225 ILE A CB  1 
ATOM   1760 C  CG1 . ILE A 1 225 ? -3.016  -5.388  23.035  1.00 41.43  ? 225 ILE A CG1 1 
ATOM   1761 C  CG2 . ILE A 1 225 ? -5.372  -6.016  22.644  1.00 39.26  ? 225 ILE A CG2 1 
ATOM   1762 C  CD1 . ILE A 1 225 ? -2.859  -4.063  22.296  1.00 38.14  ? 225 ILE A CD1 1 
ATOM   1763 N  N   . GLN A 1 226 ? -5.682  -8.765  23.415  1.00 30.57  ? 226 GLN A N   1 
ATOM   1764 C  CA  . GLN A 1 226 ? -6.901  -9.506  23.257  1.00 32.50  ? 226 GLN A CA  1 
ATOM   1765 C  C   . GLN A 1 226 ? -8.094  -8.593  23.317  1.00 30.14  ? 226 GLN A C   1 
ATOM   1766 O  O   . GLN A 1 226 ? -8.178  -7.744  24.188  1.00 28.68  ? 226 GLN A O   1 
ATOM   1767 C  CB  . GLN A 1 226 ? -7.029  -10.591 24.336  1.00 37.06  ? 226 GLN A CB  1 
ATOM   1768 C  CG  . GLN A 1 226 ? -6.633  -11.971 23.845  1.00 45.39  ? 226 GLN A CG  1 
ATOM   1769 C  CD  . GLN A 1 226 ? -5.364  -12.511 24.473  1.00 53.18  ? 226 GLN A CD  1 
ATOM   1770 O  OE1 . GLN A 1 226 ? -4.305  -11.863 24.461  1.00 55.84  ? 226 GLN A OE1 1 
ATOM   1771 N  NE2 . GLN A 1 226 ? -5.456  -13.728 25.010  1.00 50.92  ? 226 GLN A NE2 1 
ATOM   1772 N  N   . LEU A 1 227 ? -8.976  -8.758  22.343  1.00 33.35  ? 227 LEU A N   1 
ATOM   1773 C  CA  . LEU A 1 227 ? -10.297 -8.172  22.311  1.00 35.21  ? 227 LEU A CA  1 
ATOM   1774 C  C   . LEU A 1 227 ? -11.280 -9.312  22.271  1.00 38.04  ? 227 LEU A C   1 
ATOM   1775 O  O   . LEU A 1 227 ? -10.906 -10.419 21.891  1.00 36.18  ? 227 LEU A O   1 
ATOM   1776 C  CB  . LEU A 1 227 ? -10.503 -7.381  21.017  1.00 35.41  ? 227 LEU A CB  1 
ATOM   1777 C  CG  . LEU A 1 227 ? -9.789  -6.052  20.861  1.00 35.97  ? 227 LEU A CG  1 
ATOM   1778 C  CD1 . LEU A 1 227 ? -10.725 -5.030  20.225  1.00 36.48  ? 227 LEU A CD1 1 
ATOM   1779 C  CD2 . LEU A 1 227 ? -9.236  -5.552  22.173  1.00 35.05  ? 227 LEU A CD2 1 
ATOM   1780 N  N   . HIS A 1 228 ? -12.545 -9.051  22.623  1.00 42.16  ? 228 HIS A N   1 
ATOM   1781 C  CA  . HIS A 1 228 ? -13.567 -10.054 22.394  1.00 43.46  ? 228 HIS A CA  1 
ATOM   1782 C  C   . HIS A 1 228 ? -13.794 -10.131 20.927  1.00 46.84  ? 228 HIS A C   1 
ATOM   1783 O  O   . HIS A 1 228 ? -13.628 -9.133  20.228  1.00 46.85  ? 228 HIS A O   1 
ATOM   1784 C  CB  . HIS A 1 228 ? -14.823 -9.788  23.190  1.00 43.69  ? 228 HIS A CB  1 
ATOM   1785 C  CG  . HIS A 1 228 ? -15.879 -10.864 23.021  1.00 48.26  ? 228 HIS A CG  1 
ATOM   1786 N  ND1 . HIS A 1 228 ? -16.076 -11.856 23.934  1.00 48.61  ? 228 HIS A ND1 1 
ATOM   1787 C  CD2 . HIS A 1 228 ? -16.797 -11.092 21.987  1.00 46.82  ? 228 HIS A CD2 1 
ATOM   1788 C  CE1 . HIS A 1 228 ? -17.072 -12.663 23.494  1.00 52.66  ? 228 HIS A CE1 1 
ATOM   1789 N  NE2 . HIS A 1 228 ? -17.503 -12.192 22.298  1.00 46.37  ? 228 HIS A NE2 1 
ATOM   1790 N  N   . ARG A 1 229 ? -14.210 -11.308 20.450  1.00 46.02  ? 229 ARG A N   1 
ATOM   1791 C  CA  . ARG A 1 229 ? -14.624 -11.490 19.057  1.00 45.36  ? 229 ARG A CA  1 
ATOM   1792 C  C   . ARG A 1 229 ? -15.568 -10.410 18.524  1.00 43.21  ? 229 ARG A C   1 
ATOM   1793 O  O   . ARG A 1 229 ? -15.519 -10.086 17.347  1.00 35.54  ? 229 ARG A O   1 
ATOM   1794 C  CB  . ARG A 1 229 ? -15.431 -12.796 18.933  1.00 46.44  ? 229 ARG A CB  1 
ATOM   1795 C  CG  . ARG A 1 229 ? -14.613 -14.032 18.571  1.00 54.40  ? 229 ARG A CG  1 
ATOM   1796 C  CD  . ARG A 1 229 ? -15.434 -15.338 18.567  1.00 54.35  ? 229 ARG A CD  1 
ATOM   1797 N  NE  . ARG A 1 229 ? -16.865 -15.133 18.288  1.00 60.68  ? 229 ARG A NE  1 
ATOM   1798 C  CZ  . ARG A 1 229 ? -17.414 -15.070 17.072  1.00 60.81  ? 229 ARG A CZ  1 
ATOM   1799 N  NH1 . ARG A 1 229 ? -16.661 -15.216 15.983  1.00 53.70  ? 229 ARG A NH1 1 
ATOM   1800 N  NH2 . ARG A 1 229 ? -18.722 -14.847 16.947  1.00 58.07  ? 229 ARG A NH2 1 
ATOM   1801 N  N   . GLU A 1 230 ? -16.405 -9.849  19.407  1.00 40.80  ? 230 GLU A N   1 
ATOM   1802 C  CA  . GLU A 1 230 ? -17.508 -8.987  19.005  1.00 40.09  ? 230 GLU A CA  1 
ATOM   1803 C  C   . GLU A 1 230 ? -16.988 -7.578  18.942  1.00 37.38  ? 230 GLU A C   1 
ATOM   1804 O  O   . GLU A 1 230 ? -17.568 -6.743  18.277  1.00 36.41  ? 230 GLU A O   1 
ATOM   1805 C  CB  . GLU A 1 230 ? -18.731 -9.041  19.924  1.00 50.47  ? 230 GLU A CB  1 
ATOM   1806 C  CG  . GLU A 1 230 ? -19.420 -10.413 20.012  1.00 59.65  ? 230 GLU A CG  1 
ATOM   1807 C  CD  . GLU A 1 230 ? -20.330 -10.717 18.827  1.00 67.78  ? 230 GLU A CD  1 
ATOM   1808 O  OE1 . GLU A 1 230 ? -21.050 -9.793  18.369  1.00 74.20  ? 230 GLU A OE1 1 
ATOM   1809 O  OE2 . GLU A 1 230 ? -20.332 -11.883 18.357  1.00 68.99  ? 230 GLU A OE2 1 
ATOM   1810 N  N   . GLN A 1 231 ? -15.909 -7.300  19.661  1.00 35.08  ? 231 GLN A N   1 
ATOM   1811 C  CA  . GLN A 1 231 ? -15.287 -6.007  19.530  1.00 37.46  ? 231 GLN A CA  1 
ATOM   1812 C  C   . GLN A 1 231 ? -14.561 -5.962  18.188  1.00 36.50  ? 231 GLN A C   1 
ATOM   1813 O  O   . GLN A 1 231 ? -14.695 -5.005  17.458  1.00 34.53  ? 231 GLN A O   1 
ATOM   1814 C  CB  . GLN A 1 231 ? -14.343 -5.742  20.693  1.00 35.65  ? 231 GLN A CB  1 
ATOM   1815 C  CG  . GLN A 1 231 ? -15.089 -5.352  21.961  1.00 34.89  ? 231 GLN A CG  1 
ATOM   1816 C  CD  . GLN A 1 231 ? -14.143 -5.300  23.111  1.00 31.37  ? 231 GLN A CD  1 
ATOM   1817 O  OE1 . GLN A 1 231 ? -13.502 -6.281  23.426  1.00 36.00  ? 231 GLN A OE1 1 
ATOM   1818 N  NE2 . GLN A 1 231 ? -13.995 -4.138  23.697  1.00 32.34  ? 231 GLN A NE2 1 
ATOM   1819 N  N   . ILE A 1 232 ? -13.835 -7.033  17.858  1.00 37.06  ? 232 ILE A N   1 
ATOM   1820 C  CA  . ILE A 1 232 ? -13.127 -7.100  16.598  1.00 37.43  ? 232 ILE A CA  1 
ATOM   1821 C  C   . ILE A 1 232 ? -14.136 -6.878  15.500  1.00 39.51  ? 232 ILE A C   1 
ATOM   1822 O  O   . ILE A 1 232 ? -13.916 -6.061  14.599  1.00 38.47  ? 232 ILE A O   1 
ATOM   1823 C  CB  . ILE A 1 232 ? -12.391 -8.430  16.422  1.00 35.47  ? 232 ILE A CB  1 
ATOM   1824 C  CG1 . ILE A 1 232 ? -11.216 -8.452  17.383  1.00 34.64  ? 232 ILE A CG1 1 
ATOM   1825 C  CG2 . ILE A 1 232 ? -11.941 -8.600  14.963  1.00 34.15  ? 232 ILE A CG2 1 
ATOM   1826 C  CD1 . ILE A 1 232 ? -10.873 -9.836  17.904  1.00 37.42  ? 232 ILE A CD1 1 
ATOM   1827 N  N   . LEU A 1 233 ? -15.272 -7.556  15.638  1.00 39.54  ? 233 LEU A N   1 
ATOM   1828 C  CA  . LEU A 1 233 ? -16.283 -7.587  14.593  1.00 38.31  ? 233 LEU A CA  1 
ATOM   1829 C  C   . LEU A 1 233 ? -16.966 -6.257  14.357  1.00 35.90  ? 233 LEU A C   1 
ATOM   1830 O  O   . LEU A 1 233 ? -17.420 -5.990  13.236  1.00 37.39  ? 233 LEU A O   1 
ATOM   1831 C  CB  . LEU A 1 233 ? -17.290 -8.733  14.794  1.00 37.76  ? 233 LEU A CB  1 
ATOM   1832 C  CG  . LEU A 1 233 ? -16.853 -10.178 14.399  1.00 46.77  ? 233 LEU A CG  1 
ATOM   1833 C  CD1 . LEU A 1 233 ? -18.033 -11.180 14.432  1.00 39.68  ? 233 LEU A CD1 1 
ATOM   1834 C  CD2 . LEU A 1 233 ? -16.146 -10.252 13.030  1.00 43.04  ? 233 LEU A CD2 1 
ATOM   1835 N  N   . ALA A 1 234 ? -17.019 -5.421  15.394  1.00 34.34  ? 234 ALA A N   1 
ATOM   1836 C  CA  . ALA A 1 234 ? -17.609 -4.072  15.285  1.00 35.43  ? 234 ALA A CA  1 
ATOM   1837 C  C   . ALA A 1 234 ? -16.858 -3.184  14.294  1.00 34.44  ? 234 ALA A C   1 
ATOM   1838 O  O   . ALA A 1 234 ? -17.460 -2.301  13.678  1.00 38.57  ? 234 ALA A O   1 
ATOM   1839 C  CB  . ALA A 1 234 ? -17.650 -3.400  16.639  1.00 36.32  ? 234 ALA A CB  1 
ATOM   1840 N  N   . PHE A 1 235 ? -15.540 -3.374  14.154  1.00 28.69  ? 235 PHE A N   1 
ATOM   1841 C  CA  . PHE A 1 235 ? -14.821 -2.629  13.113  1.00 30.06  ? 235 PHE A CA  1 
ATOM   1842 C  C   . PHE A 1 235 ? -15.341 -2.892  11.672  1.00 30.64  ? 235 PHE A C   1 
ATOM   1843 O  O   . PHE A 1 235 ? -15.636 -1.961  10.956  1.00 32.17  ? 235 PHE A O   1 
ATOM   1844 C  CB  . PHE A 1 235 ? -13.299 -2.773  13.264  1.00 30.99  ? 235 PHE A CB  1 
ATOM   1845 C  CG  . PHE A 1 235 ? -12.762 -2.162  14.538  1.00 28.23  ? 235 PHE A CG  1 
ATOM   1846 C  CD1 . PHE A 1 235 ? -12.777 -2.881  15.741  1.00 27.51  ? 235 PHE A CD1 1 
ATOM   1847 C  CD2 . PHE A 1 235 ? -12.262 -0.866  14.534  1.00 27.84  ? 235 PHE A CD2 1 
ATOM   1848 C  CE1 . PHE A 1 235 ? -12.301 -2.323  16.919  1.00 28.86  ? 235 PHE A CE1 1 
ATOM   1849 C  CE2 . PHE A 1 235 ? -11.769 -0.300  15.698  1.00 27.68  ? 235 PHE A CE2 1 
ATOM   1850 C  CZ  . PHE A 1 235 ? -11.798 -1.025  16.898  1.00 28.94  ? 235 PHE A CZ  1 
ATOM   1851 N  N   . SER A 1 236 ? -15.495 -4.149  11.257  1.00 35.80  ? 236 SER A N   1 
ATOM   1852 C  CA  . SER A 1 236 ? -16.118 -4.441  9.947   1.00 37.70  ? 236 SER A CA  1 
ATOM   1853 C  C   . SER A 1 236 ? -17.650 -4.256  9.937   1.00 39.48  ? 236 SER A C   1 
ATOM   1854 O  O   . SER A 1 236 ? -18.249 -3.977  8.886   1.00 43.05  ? 236 SER A O   1 
ATOM   1855 C  CB  . SER A 1 236 ? -15.723 -5.834  9.409   1.00 38.56  ? 236 SER A CB  1 
ATOM   1856 O  OG  . SER A 1 236 ? -15.842 -6.847  10.383  1.00 37.41  ? 236 SER A OG  1 
ATOM   1857 N  N   . GLN A 1 237 ? -18.291 -4.357  11.097  1.00 37.76  ? 237 GLN A N   1 
ATOM   1858 C  CA  . GLN A 1 237 ? -19.753 -4.144  11.131  1.00 44.95  ? 237 GLN A CA  1 
ATOM   1859 C  C   . GLN A 1 237 ? -20.244 -2.666  11.166  1.00 48.17  ? 237 GLN A C   1 
ATOM   1860 O  O   . GLN A 1 237 ? -21.393 -2.390  10.807  1.00 47.58  ? 237 GLN A O   1 
ATOM   1861 C  CB  . GLN A 1 237 ? -20.407 -4.952  12.276  1.00 46.39  ? 237 GLN A CB  1 
ATOM   1862 C  CG  . GLN A 1 237 ? -20.503 -6.462  12.047  1.00 50.54  ? 237 GLN A CG  1 
ATOM   1863 C  CD  . GLN A 1 237 ? -20.551 -7.258  13.359  1.00 57.76  ? 237 GLN A CD  1 
ATOM   1864 O  OE1 . GLN A 1 237 ? -20.476 -6.690  14.454  1.00 58.23  ? 237 GLN A OE1 1 
ATOM   1865 N  NE2 . GLN A 1 237 ? -20.663 -8.580  13.252  1.00 54.35  ? 237 GLN A NE2 1 
ATOM   1866 N  N   . LYS A 1 238 ? -19.405 -1.724  11.604  1.00 47.27  ? 238 LYS A N   1 
ATOM   1867 C  CA  . LYS A 1 238 ? -19.872 -0.328  11.807  1.00 45.50  ? 238 LYS A CA  1 
ATOM   1868 C  C   . LYS A 1 238 ? -19.236 0.669   10.851  1.00 41.13  ? 238 LYS A C   1 
ATOM   1869 O  O   . LYS A 1 238 ? -19.807 1.729   10.595  1.00 42.79  ? 238 LYS A O   1 
ATOM   1870 C  CB  . LYS A 1 238 ? -19.635 0.173   13.255  1.00 44.26  ? 238 LYS A CB  1 
ATOM   1871 C  CG  . LYS A 1 238 ? -19.996 -0.788  14.384  1.00 44.00  ? 238 LYS A CG  1 
ATOM   1872 C  CD  . LYS A 1 238 ? -21.493 -0.889  14.629  1.00 47.49  ? 238 LYS A CD  1 
ATOM   1873 C  CE  . LYS A 1 238 ? -21.732 -0.825  16.132  1.00 48.17  ? 238 LYS A CE  1 
ATOM   1874 N  NZ  . LYS A 1 238 ? -23.134 -1.137  16.498  1.00 51.98  ? 238 LYS A NZ  1 
ATOM   1875 N  N   . LEU A 1 239 ? -18.034 0.360   10.362  1.00 39.28  ? 239 LEU A N   1 
ATOM   1876 C  CA  . LEU A 1 239 ? -17.308 1.274   9.459   1.00 37.05  ? 239 LEU A CA  1 
ATOM   1877 C  C   . LEU A 1 239 ? -17.606 0.914   8.013   1.00 36.66  ? 239 LEU A C   1 
ATOM   1878 O  O   . LEU A 1 239 ? -17.837 -0.259  7.691   1.00 40.63  ? 239 LEU A O   1 
ATOM   1879 C  CB  . LEU A 1 239 ? -15.795 1.213   9.732   1.00 29.42  ? 239 LEU A CB  1 
ATOM   1880 C  CG  . LEU A 1 239 ? -15.465 1.646   11.171  1.00 37.11  ? 239 LEU A CG  1 
ATOM   1881 C  CD1 . LEU A 1 239 ? -14.097 1.181   11.668  1.00 28.88  ? 239 LEU A CD1 1 
ATOM   1882 C  CD2 . LEU A 1 239 ? -15.628 3.165   11.371  1.00 33.35  ? 239 LEU A CD2 1 
ATOM   1883 N  N   . TYR A 1 240 ? -17.614 1.919   7.148   1.00 36.96  ? 240 TYR A N   1 
ATOM   1884 C  CA  . TYR A 1 240 ? -17.704 1.699   5.707   1.00 37.96  ? 240 TYR A CA  1 
ATOM   1885 C  C   . TYR A 1 240 ? -16.594 2.386   4.952   1.00 36.92  ? 240 TYR A C   1 
ATOM   1886 O  O   . TYR A 1 240 ? -16.063 3.410   5.388   1.00 33.12  ? 240 TYR A O   1 
ATOM   1887 C  CB  . TYR A 1 240 ? -19.056 2.144   5.148   1.00 42.05  ? 240 TYR A CB  1 
ATOM   1888 C  CG  . TYR A 1 240 ? -20.174 1.295   5.671   1.00 44.57  ? 240 TYR A CG  1 
ATOM   1889 C  CD1 . TYR A 1 240 ? -20.868 1.674   6.810   1.00 42.16  ? 240 TYR A CD1 1 
ATOM   1890 C  CD2 . TYR A 1 240 ? -20.507 0.089   5.056   1.00 46.24  ? 240 TYR A CD2 1 
ATOM   1891 C  CE1 . TYR A 1 240 ? -21.894 0.905   7.311   1.00 45.92  ? 240 TYR A CE1 1 
ATOM   1892 C  CE2 . TYR A 1 240 ? -21.529 -0.703  5.558   1.00 48.78  ? 240 TYR A CE2 1 
ATOM   1893 C  CZ  . TYR A 1 240 ? -22.214 -0.279  6.689   1.00 48.13  ? 240 TYR A CZ  1 
ATOM   1894 O  OH  . TYR A 1 240 ? -23.212 -1.037  7.210   1.00 46.41  ? 240 TYR A OH  1 
ATOM   1895 N  N   . TYR A 1 241 ? -16.238 1.785   3.823   1.00 39.03  ? 241 TYR A N   1 
ATOM   1896 C  CA  . TYR A 1 241 ? -15.323 2.403   2.874   1.00 41.19  ? 241 TYR A CA  1 
ATOM   1897 C  C   . TYR A 1 241 ? -16.077 3.465   2.073   1.00 40.60  ? 241 TYR A C   1 
ATOM   1898 O  O   . TYR A 1 241 ? -15.452 4.358   1.484   1.00 39.19  ? 241 TYR A O   1 
ATOM   1899 C  CB  . TYR A 1 241 ? -14.823 1.361   1.867   1.00 41.37  ? 241 TYR A CB  1 
ATOM   1900 C  CG  . TYR A 1 241 ? -13.585 0.569   2.237   1.00 38.66  ? 241 TYR A CG  1 
ATOM   1901 C  CD1 . TYR A 1 241 ? -12.415 1.204   2.606   1.00 33.29  ? 241 TYR A CD1 1 
ATOM   1902 C  CD2 . TYR A 1 241 ? -13.584 -0.821  2.148   1.00 38.68  ? 241 TYR A CD2 1 
ATOM   1903 C  CE1 . TYR A 1 241 ? -11.283 0.484   2.923   1.00 36.07  ? 241 TYR A CE1 1 
ATOM   1904 C  CE2 . TYR A 1 241 ? -12.448 -1.566  2.450   1.00 37.19  ? 241 TYR A CE2 1 
ATOM   1905 C  CZ  . TYR A 1 241 ? -11.299 -0.906  2.837   1.00 35.26  ? 241 TYR A CZ  1 
ATOM   1906 O  OH  . TYR A 1 241 ? -10.168 -1.623  3.129   1.00 33.05  ? 241 TYR A OH  1 
ATOM   1907 N  N   . ASP A 1 242 ? -17.409 3.345   2.018   1.00 38.83  ? 242 ASP A N   1 
ATOM   1908 C  CA  . ASP A 1 242 ? -18.228 4.255   1.211   1.00 43.75  ? 242 ASP A CA  1 
ATOM   1909 C  C   . ASP A 1 242 ? -19.307 5.028   1.989   1.00 47.21  ? 242 ASP A C   1 
ATOM   1910 O  O   . ASP A 1 242 ? -19.912 4.508   2.944   1.00 48.06  ? 242 ASP A O   1 
ATOM   1911 C  CB  . ASP A 1 242 ? -18.810 3.553   -0.053  1.00 44.99  ? 242 ASP A CB  1 
ATOM   1912 C  CG  . ASP A 1 242 ? -19.860 2.457   0.265   1.00 50.70  ? 242 ASP A CG  1 
ATOM   1913 O  OD1 . ASP A 1 242 ? -19.806 1.788   1.315   1.00 51.90  ? 242 ASP A OD1 1 
ATOM   1914 O  OD2 . ASP A 1 242 ? -20.747 2.230   -0.574  1.00 51.33  ? 242 ASP A OD2 1 
ATOM   1915 N  N   . LYS A 1 243 ? -19.519 6.278   1.576   1.00 49.11  ? 243 LYS A N   1 
ATOM   1916 C  CA  . LYS A 1 243 ? -20.565 7.151   2.143   1.00 54.28  ? 243 LYS A CA  1 
ATOM   1917 C  C   . LYS A 1 243 ? -21.952 6.527   2.099   1.00 56.30  ? 243 LYS A C   1 
ATOM   1918 O  O   . LYS A 1 243 ? -22.736 6.674   3.045   1.00 57.54  ? 243 LYS A O   1 
ATOM   1919 C  CB  . LYS A 1 243 ? -20.589 8.517   1.441   1.00 50.10  ? 243 LYS A CB  1 
ATOM   1920 C  CG  . LYS A 1 243 ? -19.302 9.307   1.627   1.00 53.35  ? 243 LYS A CG  1 
ATOM   1921 C  CD  . LYS A 1 243 ? -19.550 10.800  1.790   1.00 57.37  ? 243 LYS A CD  1 
ATOM   1922 C  CE  . LYS A 1 243 ? -18.269 11.570  2.090   1.00 59.55  ? 243 LYS A CE  1 
ATOM   1923 N  NZ  . LYS A 1 243 ? -17.429 11.816  0.877   1.00 65.48  ? 243 LYS A NZ  1 
ATOM   1924 N  N   . GLU A 1 244 ? -22.236 5.818   1.006   1.00 52.16  ? 244 GLU A N   1 
ATOM   1925 C  CA  . GLU A 1 244 ? -23.501 5.127   0.818   1.00 53.46  ? 244 GLU A CA  1 
ATOM   1926 C  C   . GLU A 1 244 ? -23.702 3.968   1.793   1.00 53.80  ? 244 GLU A C   1 
ATOM   1927 O  O   . GLU A 1 244 ? -24.834 3.533   2.006   1.00 58.12  ? 244 GLU A O   1 
ATOM   1928 C  CB  . GLU A 1 244 ? -23.643 4.643   -0.626  1.00 57.61  ? 244 GLU A CB  1 
ATOM   1929 C  CG  . GLU A 1 244 ? -23.314 5.690   -1.682  1.00 55.38  ? 244 GLU A CG  1 
ATOM   1930 C  CD  . GLU A 1 244 ? -21.849 5.699   -2.077  1.00 59.70  ? 244 GLU A CD  1 
ATOM   1931 O  OE1 . GLU A 1 244 ? -20.981 5.811   -1.186  1.00 66.56  ? 244 GLU A OE1 1 
ATOM   1932 O  OE2 . GLU A 1 244 ? -21.556 5.621   -3.289  1.00 62.70  ? 244 GLU A OE2 1 
ATOM   1933 N  N   . GLN A 1 245 ? -22.607 3.485   2.382   1.00 49.77  ? 245 GLN A N   1 
ATOM   1934 C  CA  . GLN A 1 245 ? -22.642 2.514   3.469   1.00 46.50  ? 245 GLN A CA  1 
ATOM   1935 C  C   . GLN A 1 245 ? -23.073 1.145   2.976   1.00 52.51  ? 245 GLN A C   1 
ATOM   1936 O  O   . GLN A 1 245 ? -23.828 0.426   3.664   1.00 50.73  ? 245 GLN A O   1 
ATOM   1937 C  CB  . GLN A 1 245 ? -23.576 2.959   4.589   1.00 43.99  ? 245 GLN A CB  1 
ATOM   1938 C  CG  . GLN A 1 245 ? -23.081 4.084   5.465   1.00 44.04  ? 245 GLN A CG  1 
ATOM   1939 C  CD  . GLN A 1 245 ? -23.744 4.076   6.838   1.00 43.92  ? 245 GLN A CD  1 
ATOM   1940 O  OE1 . GLN A 1 245 ? -23.543 4.976   7.640   1.00 43.86  ? 245 GLN A OE1 1 
ATOM   1941 N  NE2 . GLN A 1 245 ? -24.528 3.047   7.115   1.00 50.04  ? 245 GLN A NE2 1 
ATOM   1942 N  N   . THR A 1 246 ? -22.596 0.782   1.788   1.00 51.77  ? 246 THR A N   1 
ATOM   1943 C  CA  . THR A 1 246 ? -22.807 -0.572  1.263   1.00 51.63  ? 246 THR A CA  1 
ATOM   1944 C  C   . THR A 1 246 ? -21.567 -1.434  1.446   1.00 49.92  ? 246 THR A C   1 
ATOM   1945 O  O   . THR A 1 246 ? -21.683 -2.600  1.807   1.00 51.32  ? 246 THR A O   1 
ATOM   1946 C  CB  . THR A 1 246 ? -23.161 -0.570  -0.227  1.00 50.95  ? 246 THR A CB  1 
ATOM   1947 O  OG1 . THR A 1 246 ? -22.159 0.150   -0.959  1.00 48.15  ? 246 THR A OG1 1 
ATOM   1948 C  CG2 . THR A 1 246 ? -24.512 0.055   -0.439  1.00 53.72  ? 246 THR A CG2 1 
ATOM   1949 N  N   . VAL A 1 247 ? -20.389 -0.835  1.215   1.00 50.63  ? 247 VAL A N   1 
ATOM   1950 C  CA  . VAL A 1 247 ? -19.087 -1.516  1.306   1.00 42.55  ? 247 VAL A CA  1 
ATOM   1951 C  C   . VAL A 1 247 ? -18.510 -1.397  2.716   1.00 44.22  ? 247 VAL A C   1 
ATOM   1952 O  O   . VAL A 1 247 ? -18.176 -0.299  3.169   1.00 43.91  ? 247 VAL A O   1 
ATOM   1953 C  CB  . VAL A 1 247 ? -18.083 -0.973  0.266   1.00 41.84  ? 247 VAL A CB  1 
ATOM   1954 C  CG1 . VAL A 1 247 ? -16.878 -1.904  0.149   1.00 38.38  ? 247 VAL A CG1 1 
ATOM   1955 C  CG2 . VAL A 1 247 ? -18.761 -0.779  -1.094  1.00 40.10  ? 247 VAL A CG2 1 
ATOM   1956 N  N   . SER A 1 248 ? -18.422 -2.538  3.408   1.00 49.21  ? 248 SER A N   1 
ATOM   1957 C  CA  . SER A 1 248 ? -17.898 -2.623  4.777   1.00 45.44  ? 248 SER A CA  1 
ATOM   1958 C  C   . SER A 1 248 ? -16.393 -2.464  4.781   1.00 38.33  ? 248 SER A C   1 
ATOM   1959 O  O   . SER A 1 248 ? -15.711 -3.084  3.981   1.00 36.94  ? 248 SER A O   1 
ATOM   1960 C  CB  . SER A 1 248 ? -18.238 -3.966  5.414   1.00 48.17  ? 248 SER A CB  1 
ATOM   1961 O  OG  . SER A 1 248 ? -19.525 -3.938  6.005   1.00 59.15  ? 248 SER A OG  1 
ATOM   1962 N  N   . MET A 1 249 ? -15.891 -1.637  5.701   1.00 38.76  ? 249 MET A N   1 
ATOM   1963 C  CA  . MET A 1 249 ? -14.458 -1.435  5.897   1.00 33.88  ? 249 MET A CA  1 
ATOM   1964 C  C   . MET A 1 249 ? -13.837 -2.670  6.522   1.00 34.47  ? 249 MET A C   1 
ATOM   1965 O  O   . MET A 1 249 ? -14.008 -2.946  7.709   1.00 35.25  ? 249 MET A O   1 
ATOM   1966 C  CB  . MET A 1 249 ? -14.187 -0.163  6.736   1.00 33.29  ? 249 MET A CB  1 
ATOM   1967 C  CG  . MET A 1 249 ? -12.715 0.224   6.832   1.00 31.97  ? 249 MET A CG  1 
ATOM   1968 S  SD  . MET A 1 249 ? -12.347 1.758   7.706   1.00 32.32  ? 249 MET A SD  1 
ATOM   1969 C  CE  . MET A 1 249 ? -12.534 3.088   6.501   1.00 27.87  ? 249 MET A CE  1 
ATOM   1970 N  N   . LYS A 1 250 ? -13.106 -3.422  5.701   1.00 35.98  ? 250 LYS A N   1 
ATOM   1971 C  CA  . LYS A 1 250 ? -12.285 -4.531  6.175   1.00 32.25  ? 250 LYS A CA  1 
ATOM   1972 C  C   . LYS A 1 250 ? -11.138 -4.815  5.219   1.00 32.59  ? 250 LYS A C   1 
ATOM   1973 O  O   . LYS A 1 250 ? -11.125 -4.312  4.087   1.00 30.16  ? 250 LYS A O   1 
ATOM   1974 C  CB  . LYS A 1 250 ? -13.126 -5.792  6.354   1.00 32.57  ? 250 LYS A CB  1 
ATOM   1975 C  CG  . LYS A 1 250 ? -14.206 -5.980  5.307   1.00 33.33  ? 250 LYS A CG  1 
ATOM   1976 C  CD  . LYS A 1 250 ? -14.666 -7.432  5.310   1.00 38.45  ? 250 LYS A CD  1 
ATOM   1977 C  CE  . LYS A 1 250 ? -15.136 -7.866  3.923   1.00 40.78  ? 250 LYS A CE  1 
ATOM   1978 N  NZ  . LYS A 1 250 ? -15.294 -9.344  3.873   1.00 46.16  ? 250 LYS A NZ  1 
ATOM   1979 N  N   . ASP A 1 251 ? -10.169 -5.610  5.673   1.00 31.59  ? 251 ASP A N   1 
ATOM   1980 C  CA  . ASP A 1 251 ? -8.987  -5.928  4.835   1.00 35.90  ? 251 ASP A CA  1 
ATOM   1981 C  C   . ASP A 1 251 ? -8.234  -4.686  4.343   1.00 32.78  ? 251 ASP A C   1 
ATOM   1982 O  O   . ASP A 1 251 ? -7.642  -4.668  3.254   1.00 34.88  ? 251 ASP A O   1 
ATOM   1983 C  CB  . ASP A 1 251 ? -9.356  -6.917  3.700   1.00 32.64  ? 251 ASP A CB  1 
ATOM   1984 C  CG  . ASP A 1 251 ? -9.995  -8.172  4.258   1.00 35.94  ? 251 ASP A CG  1 
ATOM   1985 O  OD1 . ASP A 1 251 ? -9.321  -8.912  4.994   1.00 36.09  ? 251 ASP A OD1 1 
ATOM   1986 O  OD2 . ASP A 1 251 ? -11.188 -8.386  4.020   1.00 40.06  ? 251 ASP A OD2 1 
ATOM   1987 N  N   . ASN A 1 252 ? -8.249  -3.663  5.189   1.00 30.61  ? 252 ASN A N   1 
ATOM   1988 C  CA  . ASN A 1 252 ? -7.456  -2.451  5.012   1.00 27.58  ? 252 ASN A CA  1 
ATOM   1989 C  C   . ASN A 1 252 ? -5.986  -2.725  5.362   1.00 28.41  ? 252 ASN A C   1 
ATOM   1990 O  O   . ASN A 1 252 ? -5.363  -2.047  6.195   1.00 27.27  ? 252 ASN A O   1 
ATOM   1991 C  CB  . ASN A 1 252 ? -8.078  -1.270  5.817   1.00 27.97  ? 252 ASN A CB  1 
ATOM   1992 C  CG  . ASN A 1 252 ? -8.253  -1.575  7.310   1.00 28.49  ? 252 ASN A CG  1 
ATOM   1993 O  OD1 . ASN A 1 252 ? -8.205  -2.721  7.742   1.00 28.92  ? 252 ASN A OD1 1 
ATOM   1994 N  ND2 . ASN A 1 252 ? -8.447  -0.526  8.108   1.00 29.18  ? 252 ASN A ND2 1 
ATOM   1995 N  N   . VAL A 1 253 ? -5.435  -3.753  4.707   1.00 28.69  ? 253 VAL A N   1 
ATOM   1996 C  CA  . VAL A 1 253 ? -4.079  -4.210  4.971   1.00 27.15  ? 253 VAL A CA  1 
ATOM   1997 C  C   . VAL A 1 253 ? -3.248  -4.298  3.680   1.00 29.28  ? 253 VAL A C   1 
ATOM   1998 O  O   . VAL A 1 253 ? -3.724  -4.819  2.676   1.00 31.85  ? 253 VAL A O   1 
ATOM   1999 C  CB  . VAL A 1 253 ? -4.067  -5.542  5.826   1.00 29.07  ? 253 VAL A CB  1 
ATOM   2000 C  CG1 . VAL A 1 253 ? -5.455  -5.872  6.376   1.00 24.55  ? 253 VAL A CG1 1 
ATOM   2001 C  CG2 . VAL A 1 253 ? -3.491  -6.731  5.101   1.00 23.61  ? 253 VAL A CG2 1 
ATOM   2002 N  N   . ARG A 1 254 ? -2.026  -3.774  3.739   1.00 27.27  ? 254 ARG A N   1 
ATOM   2003 C  CA  . ARG A 1 254 ? -1.046  -3.811  2.668   1.00 29.04  ? 254 ARG A CA  1 
ATOM   2004 C  C   . ARG A 1 254 ? -0.349  -5.209  2.538   1.00 28.66  ? 254 ARG A C   1 
ATOM   2005 O  O   . ARG A 1 254 ? -0.002  -5.822  3.533   1.00 29.95  ? 254 ARG A O   1 
ATOM   2006 C  CB  . ARG A 1 254 ? -0.013  -2.713  2.900   1.00 25.59  ? 254 ARG A CB  1 
ATOM   2007 C  CG  . ARG A 1 254 ? 0.951   -2.515  1.741   1.00 29.68  ? 254 ARG A CG  1 
ATOM   2008 C  CD  . ARG A 1 254 ? 2.231   -1.747  2.065   1.00 29.12  ? 254 ARG A CD  1 
ATOM   2009 N  NE  . ARG A 1 254 ? 2.945   -1.418  0.819   1.00 29.51  ? 254 ARG A NE  1 
ATOM   2010 C  CZ  . ARG A 1 254 ? 4.125   -0.803  0.716   1.00 28.58  ? 254 ARG A CZ  1 
ATOM   2011 N  NH1 . ARG A 1 254 ? 4.796   -0.370  1.773   1.00 23.75  ? 254 ARG A NH1 1 
ATOM   2012 N  NH2 . ARG A 1 254 ? 4.626   -0.584  -0.491  1.00 33.93  ? 254 ARG A NH2 1 
ATOM   2013 N  N   . PRO A 1 255 ? -0.178  -5.717  1.302   1.00 25.52  ? 255 PRO A N   1 
ATOM   2014 C  CA  . PRO A 1 255 ? 0.472   -7.019  1.147   1.00 27.08  ? 255 PRO A CA  1 
ATOM   2015 C  C   . PRO A 1 255 ? 1.863   -6.911  1.731   1.00 27.09  ? 255 PRO A C   1 
ATOM   2016 O  O   . PRO A 1 255 ? 2.430   -5.804  1.851   1.00 29.27  ? 255 PRO A O   1 
ATOM   2017 C  CB  . PRO A 1 255 ? 0.462   -7.278  -0.417  1.00 25.54  ? 255 PRO A CB  1 
ATOM   2018 C  CG  . PRO A 1 255 ? 0.058   -5.969  -1.052  1.00 25.50  ? 255 PRO A CG  1 
ATOM   2019 C  CD  . PRO A 1 255 ? -0.717  -5.196  0.030   1.00 26.84  ? 255 PRO A CD  1 
ATOM   2020 N  N   . LEU A 1 256 ? 2.398   -8.038  2.156   1.00 27.99  ? 256 LEU A N   1 
ATOM   2021 C  CA  . LEU A 1 256 ? 3.739   -8.106  2.701   1.00 25.07  ? 256 LEU A CA  1 
ATOM   2022 C  C   . LEU A 1 256 ? 4.764   -7.663  1.685   1.00 29.81  ? 256 LEU A C   1 
ATOM   2023 O  O   . LEU A 1 256 ? 4.549   -7.783  0.496   1.00 30.18  ? 256 LEU A O   1 
ATOM   2024 C  CB  . LEU A 1 256 ? 4.053   -9.554  3.123   1.00 25.22  ? 256 LEU A CB  1 
ATOM   2025 C  CG  . LEU A 1 256 ? 3.313   -10.096 4.339   1.00 22.49  ? 256 LEU A CG  1 
ATOM   2026 C  CD1 . LEU A 1 256 ? 3.540   -11.584 4.666   1.00 22.26  ? 256 LEU A CD1 1 
ATOM   2027 C  CD2 . LEU A 1 256 ? 3.699   -9.253  5.559   1.00 21.98  ? 256 LEU A CD2 1 
ATOM   2028 N  N   . GLN A 1 257 ? 5.904   -7.193  2.185   1.00 32.20  ? 257 GLN A N   1 
ATOM   2029 C  CA  . GLN A 1 257 ? 6.970   -6.615  1.402   1.00 32.16  ? 257 GLN A CA  1 
ATOM   2030 C  C   . GLN A 1 257 ? 8.202   -7.432  1.736   1.00 36.97  ? 257 GLN A C   1 
ATOM   2031 O  O   . GLN A 1 257 ? 8.267   -8.051  2.812   1.00 37.09  ? 257 GLN A O   1 
ATOM   2032 C  CB  . GLN A 1 257 ? 7.173   -5.162  1.878   1.00 32.03  ? 257 GLN A CB  1 
ATOM   2033 C  CG  . GLN A 1 257 ? 5.930   -4.270  1.698   1.00 26.50  ? 257 GLN A CG  1 
ATOM   2034 C  CD  . GLN A 1 257 ? 5.570   -4.161  0.227   1.00 27.13  ? 257 GLN A CD  1 
ATOM   2035 O  OE1 . GLN A 1 257 ? 6.450   -3.909  -0.575  1.00 24.95  ? 257 GLN A OE1 1 
ATOM   2036 N  NE2 . GLN A 1 257 ? 4.286   -4.378  -0.136  1.00 21.94  ? 257 GLN A NE2 1 
ATOM   2037 N  N   . GLN A 1 258 ? 9.192   -7.450  0.848   1.00 38.34  ? 258 GLN A N   1 
ATOM   2038 C  CA  . GLN A 1 258 ? 10.397  -8.248  1.137   1.00 37.89  ? 258 GLN A CA  1 
ATOM   2039 C  C   . GLN A 1 258 ? 11.428  -7.542  2.005   1.00 34.34  ? 258 GLN A C   1 
ATOM   2040 O  O   . GLN A 1 258 ? 11.656  -6.315  1.900   1.00 31.86  ? 258 GLN A O   1 
ATOM   2041 C  CB  . GLN A 1 258 ? 11.044  -8.822  -0.139  1.00 39.09  ? 258 GLN A CB  1 
ATOM   2042 C  CG  . GLN A 1 258 ? 10.076  -9.571  -1.043  1.00 41.25  ? 258 GLN A CG  1 
ATOM   2043 C  CD  . GLN A 1 258 ? 9.751   -10.967 -0.551  1.00 43.52  ? 258 GLN A CD  1 
ATOM   2044 O  OE1 . GLN A 1 258 ? 10.598  -11.656 0.032   1.00 45.76  ? 258 GLN A OE1 1 
ATOM   2045 N  NE2 . GLN A 1 258 ? 8.519   -11.402 -0.791  1.00 43.16  ? 258 GLN A NE2 1 
ATOM   2046 N  N   . LEU A 1 259 ? 12.052  -8.350  2.852   1.00 36.05  ? 259 LEU A N   1 
ATOM   2047 C  CA  . LEU A 1 259 ? 13.003  -7.889  3.833   1.00 41.67  ? 259 LEU A CA  1 
ATOM   2048 C  C   . LEU A 1 259 ? 14.207  -7.296  3.103   1.00 43.95  ? 259 LEU A C   1 
ATOM   2049 O  O   . LEU A 1 259 ? 14.734  -6.255  3.490   1.00 40.06  ? 259 LEU A O   1 
ATOM   2050 C  CB  . LEU A 1 259 ? 13.422  -9.046  4.746   1.00 42.01  ? 259 LEU A CB  1 
ATOM   2051 C  CG  . LEU A 1 259 ? 14.426  -8.674  5.851   1.00 49.35  ? 259 LEU A CG  1 
ATOM   2052 C  CD1 . LEU A 1 259 ? 13.921  -7.543  6.756   1.00 52.72  ? 259 LEU A CD1 1 
ATOM   2053 C  CD2 . LEU A 1 259 ? 14.842  -9.863  6.699   1.00 48.00  ? 259 LEU A CD2 1 
ATOM   2054 N  N   . GLY A 1 260 ? 14.623  -7.963  2.023   1.00 44.88  ? 260 GLY A N   1 
ATOM   2055 C  CA  . GLY A 1 260 ? 15.790  -7.541  1.272   1.00 40.99  ? 260 GLY A CA  1 
ATOM   2056 C  C   . GLY A 1 260 ? 17.027  -7.625  2.137   1.00 44.58  ? 260 GLY A C   1 
ATOM   2057 O  O   . GLY A 1 260 ? 17.271  -8.634  2.844   1.00 45.10  ? 260 GLY A O   1 
ATOM   2058 N  N   . GLN A 1 261 ? 17.772  -6.531  2.098   1.00 41.16  ? 261 GLN A N   1 
ATOM   2059 C  CA  . GLN A 1 261 ? 19.040  -6.350  2.798   1.00 44.73  ? 261 GLN A CA  1 
ATOM   2060 C  C   . GLN A 1 261 ? 18.868  -5.976  4.280   1.00 47.88  ? 261 GLN A C   1 
ATOM   2061 O  O   . GLN A 1 261 ? 19.834  -5.636  4.975   1.00 48.83  ? 261 GLN A O   1 
ATOM   2062 C  CB  . GLN A 1 261 ? 19.844  -5.257  2.069   1.00 45.60  ? 261 GLN A CB  1 
ATOM   2063 C  CG  . GLN A 1 261 ? 20.265  -5.591  0.631   1.00 47.41  ? 261 GLN A CG  1 
ATOM   2064 C  CD  . GLN A 1 261 ? 19.747  -6.943  0.114   1.00 51.48  ? 261 GLN A CD  1 
ATOM   2065 O  OE1 . GLN A 1 261 ? 20.117  -8.019  0.622   1.00 46.75  ? 261 GLN A OE1 1 
ATOM   2066 N  NE2 . GLN A 1 261 ? 18.878  -6.892  -0.903  1.00 54.98  ? 261 GLN A NE2 1 
ATOM   2067 N  N   . ARG A 1 262 ? 17.647  -6.045  4.784   1.00 44.22  ? 262 ARG A N   1 
ATOM   2068 C  CA  . ARG A 1 262 ? 17.473  -5.685  6.170   1.00 43.99  ? 262 ARG A CA  1 
ATOM   2069 C  C   . ARG A 1 262 ? 17.633  -6.906  7.080   1.00 41.59  ? 262 ARG A C   1 
ATOM   2070 O  O   . ARG A 1 262 ? 17.475  -8.056  6.657   1.00 45.95  ? 262 ARG A O   1 
ATOM   2071 C  CB  . ARG A 1 262 ? 16.144  -4.969  6.383   1.00 40.45  ? 262 ARG A CB  1 
ATOM   2072 C  CG  . ARG A 1 262 ? 16.102  -3.565  5.831   1.00 41.78  ? 262 ARG A CG  1 
ATOM   2073 C  CD  . ARG A 1 262 ? 14.677  -3.003  5.884   1.00 39.59  ? 262 ARG A CD  1 
ATOM   2074 N  NE  . ARG A 1 262 ? 13.767  -3.829  5.101   1.00 34.42  ? 262 ARG A NE  1 
ATOM   2075 C  CZ  . ARG A 1 262 ? 12.470  -3.603  4.921   1.00 36.61  ? 262 ARG A CZ  1 
ATOM   2076 N  NH1 . ARG A 1 262 ? 11.852  -2.553  5.470   1.00 38.22  ? 262 ARG A NH1 1 
ATOM   2077 N  NH2 . ARG A 1 262 ? 11.768  -4.455  4.198   1.00 40.22  ? 262 ARG A NH2 1 
ATOM   2078 N  N   . THR A 1 263 ? 18.006  -6.644  8.319   1.00 43.50  ? 263 THR A N   1 
ATOM   2079 C  CA  . THR A 1 263 ? 17.826  -7.613  9.388   1.00 38.92  ? 263 THR A CA  1 
ATOM   2080 C  C   . THR A 1 263 ? 16.733  -7.057  10.292  1.00 40.43  ? 263 THR A C   1 
ATOM   2081 O  O   . THR A 1 263 ? 16.402  -5.857  10.217  1.00 39.29  ? 263 THR A O   1 
ATOM   2082 C  CB  . THR A 1 263 ? 19.115  -7.812  10.189  1.00 36.54  ? 263 THR A CB  1 
ATOM   2083 O  OG1 . THR A 1 263 ? 19.619  -6.538  10.549  1.00 39.19  ? 263 THR A OG1 1 
ATOM   2084 C  CG2 . THR A 1 263 ? 20.207  -8.529  9.348   1.00 37.13  ? 263 THR A CG2 1 
ATOM   2085 N  N   . VAL A 1 264 ? 16.161  -7.941  11.115  1.00 43.89  ? 264 VAL A N   1 
ATOM   2086 C  CA  . VAL A 1 264 ? 15.306  -7.592  12.250  1.00 40.57  ? 264 VAL A CA  1 
ATOM   2087 C  C   . VAL A 1 264 ? 16.087  -7.989  13.507  1.00 42.82  ? 264 VAL A C   1 
ATOM   2088 O  O   . VAL A 1 264 ? 16.584  -9.120  13.577  1.00 45.45  ? 264 VAL A O   1 
ATOM   2089 C  CB  . VAL A 1 264 ? 13.980  -8.421  12.271  1.00 41.54  ? 264 VAL A CB  1 
ATOM   2090 C  CG1 . VAL A 1 264 ? 13.041  -7.966  13.407  1.00 40.00  ? 264 VAL A CG1 1 
ATOM   2091 C  CG2 . VAL A 1 264 ? 13.242  -8.366  10.948  1.00 39.66  ? 264 VAL A CG2 1 
ATOM   2092 N  N   . ILE A 1 265 ? 16.180  -7.082  14.488  1.00 42.97  ? 265 ILE A N   1 
ATOM   2093 C  CA  . ILE A 1 265 ? 16.699  -7.390  15.844  1.00 40.39  ? 265 ILE A CA  1 
ATOM   2094 C  C   . ILE A 1 265 ? 15.548  -7.504  16.839  1.00 41.59  ? 265 ILE A C   1 
ATOM   2095 O  O   . ILE A 1 265 ? 14.414  -7.253  16.462  1.00 42.73  ? 265 ILE A O   1 
ATOM   2096 C  CB  . ILE A 1 265 ? 17.761  -6.372  16.328  1.00 44.80  ? 265 ILE A CB  1 
ATOM   2097 C  CG1 . ILE A 1 265 ? 17.302  -4.934  16.069  1.00 46.88  ? 265 ILE A CG1 1 
ATOM   2098 C  CG2 . ILE A 1 265 ? 19.114  -6.669  15.666  1.00 46.03  ? 265 ILE A CG2 1 
ATOM   2099 C  CD1 . ILE A 1 265 ? 18.247  -3.849  16.535  1.00 41.69  ? 265 ILE A CD1 1 
ATOM   2100 N  N   . LYS A 1 266 ? 15.829  -7.922  18.084  1.00 41.87  ? 266 LYS A N   1 
ATOM   2101 C  CA  . LYS A 1 266 ? 14.816  -8.026  19.155  1.00 37.92  ? 266 LYS A CA  1 
ATOM   2102 C  C   . LYS A 1 266 ? 15.388  -7.821  20.567  1.00 41.52  ? 266 LYS A C   1 
ATOM   2103 O  O   . LYS A 1 266 ? 16.562  -8.133  20.817  1.00 38.70  ? 266 LYS A O   1 
ATOM   2104 C  CB  . LYS A 1 266 ? 14.093  -9.361  19.096  1.00 39.01  ? 266 LYS A CB  1 
ATOM   2105 C  CG  . LYS A 1 266 ? 14.795  -10.511 19.808  1.00 40.54  ? 266 LYS A CG  1 
ATOM   2106 C  CD  . LYS A 1 266 ? 14.100  -11.841 19.529  1.00 40.82  ? 266 LYS A CD  1 
ATOM   2107 C  CE  . LYS A 1 266 ? 15.094  -12.997 19.485  1.00 45.11  ? 266 LYS A CE  1 
ATOM   2108 N  NZ  . LYS A 1 266 ? 14.535  -14.266 18.910  1.00 45.04  ? 266 LYS A NZ  1 
ATOM   2109 N  N   . SER A 1 267 ? 14.537  -7.324  21.479  1.00 38.23  ? 267 SER A N   1 
ATOM   2110 C  CA  . SER A 1 267 ? 14.925  -6.922  22.834  1.00 39.98  ? 267 SER A CA  1 
ATOM   2111 C  C   . SER A 1 267 ? 15.489  -8.063  23.666  1.00 46.20  ? 267 SER A C   1 
ATOM   2112 O  O   . SER A 1 267 ? 15.038  -9.210  23.501  1.00 41.19  ? 267 SER A O   1 
ATOM   2113 C  CB  . SER A 1 267 ? 13.741  -6.302  23.592  1.00 36.39  ? 267 SER A CB  1 
ATOM   2114 O  OG  . SER A 1 267 ? 12.621  -7.171  23.622  1.00 32.92  ? 267 SER A OG  1 
ATOM   2115 O  OXT . SER A 1 267 ? 16.364  -7.809  24.522  1.00 47.44  ? 267 SER A OXT 1 
ATOM   2116 N  N   . GLU B 1 3   ? -46.959 26.468  5.373   1.00 95.60  ? 3   GLU B N   1 
ATOM   2117 C  CA  . GLU B 1 3   ? -46.816 25.064  5.858   1.00 88.64  ? 3   GLU B CA  1 
ATOM   2118 C  C   . GLU B 1 3   ? -45.377 24.746  6.320   1.00 87.46  ? 3   GLU B C   1 
ATOM   2119 O  O   . GLU B 1 3   ? -44.531 24.293  5.538   1.00 87.15  ? 3   GLU B O   1 
ATOM   2120 C  CB  . GLU B 1 3   ? -47.298 24.080  4.789   1.00 91.07  ? 3   GLU B CB  1 
ATOM   2121 C  CG  . GLU B 1 3   ? -47.978 22.841  5.349   1.00 94.58  ? 3   GLU B CG  1 
ATOM   2122 C  CD  . GLU B 1 3   ? -48.814 22.110  4.312   1.00 94.09  ? 3   GLU B CD  1 
ATOM   2123 O  OE1 . GLU B 1 3   ? -48.226 21.516  3.383   1.00 89.32  ? 3   GLU B OE1 1 
ATOM   2124 O  OE2 . GLU B 1 3   ? -50.059 22.121  4.435   1.00 94.71  ? 3   GLU B OE2 1 
ATOM   2125 N  N   . SER B 1 4   ? -45.132 25.019  7.603   1.00 79.86  ? 4   SER B N   1 
ATOM   2126 C  CA  . SER B 1 4   ? -43.879 24.735  8.332   1.00 73.31  ? 4   SER B CA  1 
ATOM   2127 C  C   . SER B 1 4   ? -42.668 25.639  8.049   1.00 68.63  ? 4   SER B C   1 
ATOM   2128 O  O   . SER B 1 4   ? -42.115 26.213  8.993   1.00 69.91  ? 4   SER B O   1 
ATOM   2129 C  CB  . SER B 1 4   ? -43.491 23.244  8.313   1.00 72.48  ? 4   SER B CB  1 
ATOM   2130 O  OG  . SER B 1 4   ? -42.659 22.932  7.213   1.00 77.63  ? 4   SER B OG  1 
ATOM   2131 N  N   . HIS B 1 5   ? -42.248 25.780  6.791   1.00 56.62  ? 5   HIS B N   1 
ATOM   2132 C  CA  . HIS B 1 5   ? -41.078 26.614  6.522   1.00 52.01  ? 5   HIS B CA  1 
ATOM   2133 C  C   . HIS B 1 5   ? -41.325 28.027  6.970   1.00 46.76  ? 5   HIS B C   1 
ATOM   2134 O  O   . HIS B 1 5   ? -42.382 28.590  6.691   1.00 44.54  ? 5   HIS B O   1 
ATOM   2135 C  CB  . HIS B 1 5   ? -40.668 26.568  5.073   1.00 56.01  ? 5   HIS B CB  1 
ATOM   2136 C  CG  . HIS B 1 5   ? -40.252 25.202  4.617   1.00 66.96  ? 5   HIS B CG  1 
ATOM   2137 N  ND1 . HIS B 1 5   ? -39.100 24.630  5.008   1.00 73.38  ? 5   HIS B ND1 1 
ATOM   2138 C  CD2 . HIS B 1 5   ? -40.890 24.282  3.790   1.00 71.34  ? 5   HIS B CD2 1 
ATOM   2139 C  CE1 . HIS B 1 5   ? -38.998 23.409  4.455   1.00 76.64  ? 5   HIS B CE1 1 
ATOM   2140 N  NE2 . HIS B 1 5   ? -40.095 23.198  3.707   1.00 77.72  ? 5   HIS B NE2 1 
ATOM   2141 N  N   . TRP B 1 6   ? -40.364 28.578  7.711   1.00 37.55  ? 6   TRP B N   1 
ATOM   2142 C  CA  . TRP B 1 6   ? -40.462 29.907  8.270   1.00 33.35  ? 6   TRP B CA  1 
ATOM   2143 C  C   . TRP B 1 6   ? -39.332 30.761  7.818   1.00 32.59  ? 6   TRP B C   1 
ATOM   2144 O  O   . TRP B 1 6   ? -38.260 30.273  7.453   1.00 32.98  ? 6   TRP B O   1 
ATOM   2145 C  CB  . TRP B 1 6   ? -40.521 29.835  9.798   1.00 34.59  ? 6   TRP B CB  1 
ATOM   2146 C  CG  . TRP B 1 6   ? -39.244 29.279  10.433  1.00 37.67  ? 6   TRP B CG  1 
ATOM   2147 C  CD1 . TRP B 1 6   ? -38.940 27.942  10.688  1.00 38.71  ? 6   TRP B CD1 1 
ATOM   2148 C  CD2 . TRP B 1 6   ? -38.049 30.028  10.883  1.00 35.63  ? 6   TRP B CD2 1 
ATOM   2149 N  NE1 . TRP B 1 6   ? -37.695 27.819  11.256  1.00 37.61  ? 6   TRP B NE1 1 
ATOM   2150 C  CE2 . TRP B 1 6   ? -37.109 29.026  11.401  1.00 36.94  ? 6   TRP B CE2 1 
ATOM   2151 C  CE3 . TRP B 1 6   ? -37.687 31.368  10.916  1.00 34.61  ? 6   TRP B CE3 1 
ATOM   2152 C  CZ2 . TRP B 1 6   ? -35.872 29.379  11.919  1.00 36.00  ? 6   TRP B CZ2 1 
ATOM   2153 C  CZ3 . TRP B 1 6   ? -36.436 31.707  11.442  1.00 36.31  ? 6   TRP B CZ3 1 
ATOM   2154 C  CH2 . TRP B 1 6   ? -35.555 30.737  11.930  1.00 32.99  ? 6   TRP B CH2 1 
ATOM   2155 N  N   . CYS B 1 7   ? -39.544 32.074  7.830   1.00 36.61  ? 7   CYS B N   1 
ATOM   2156 C  CA  . CYS B 1 7   ? -38.514 32.978  7.347   1.00 36.69  ? 7   CYS B CA  1 
ATOM   2157 C  C   . CYS B 1 7   ? -38.502 34.310  8.090   1.00 34.84  ? 7   CYS B C   1 
ATOM   2158 O  O   . CYS B 1 7   ? -39.315 34.556  8.966   1.00 33.70  ? 7   CYS B O   1 
ATOM   2159 C  CB  . CYS B 1 7   ? -38.679 33.171  5.841   1.00 40.35  ? 7   CYS B CB  1 
ATOM   2160 S  SG  . CYS B 1 7   ? -40.394 33.551  5.486   1.00 54.08  ? 7   CYS B SG  1 
ATOM   2161 N  N   . TYR B 1 8   ? -37.552 35.161  7.755   1.00 34.67  ? 8   TYR B N   1 
ATOM   2162 C  CA  . TYR B 1 8   ? -37.572 36.497  8.290   1.00 35.81  ? 8   TYR B CA  1 
ATOM   2163 C  C   . TYR B 1 8   ? -38.324 37.431  7.331   1.00 37.92  ? 8   TYR B C   1 
ATOM   2164 O  O   . TYR B 1 8   ? -38.552 37.076  6.166   1.00 38.47  ? 8   TYR B O   1 
ATOM   2165 C  CB  . TYR B 1 8   ? -36.153 36.967  8.560   1.00 28.92  ? 8   TYR B CB  1 
ATOM   2166 C  CG  . TYR B 1 8   ? -35.535 36.197  9.728   1.00 30.32  ? 8   TYR B CG  1 
ATOM   2167 C  CD1 . TYR B 1 8   ? -35.910 36.476  11.035  1.00 24.74  ? 8   TYR B CD1 1 
ATOM   2168 C  CD2 . TYR B 1 8   ? -34.603 35.165  9.513   1.00 25.55  ? 8   TYR B CD2 1 
ATOM   2169 C  CE1 . TYR B 1 8   ? -35.379 35.763  12.088  1.00 25.57  ? 8   TYR B CE1 1 
ATOM   2170 C  CE2 . TYR B 1 8   ? -34.028 34.476  10.566  1.00 25.66  ? 8   TYR B CE2 1 
ATOM   2171 C  CZ  . TYR B 1 8   ? -34.427 34.764  11.866  1.00 28.73  ? 8   TYR B CZ  1 
ATOM   2172 O  OH  . TYR B 1 8   ? -33.867 34.062  12.955  1.00 27.19  ? 8   TYR B OH  1 
ATOM   2173 N  N   . GLU B 1 9   ? -38.702 38.609  7.820   1.00 35.69  ? 9   GLU B N   1 
ATOM   2174 C  CA  . GLU B 1 9   ? -39.543 39.500  7.049   1.00 42.31  ? 9   GLU B CA  1 
ATOM   2175 C  C   . GLU B 1 9   ? -38.928 39.711  5.673   1.00 43.02  ? 9   GLU B C   1 
ATOM   2176 O  O   . GLU B 1 9   ? -39.636 39.578  4.685   1.00 45.26  ? 9   GLU B O   1 
ATOM   2177 C  CB  . GLU B 1 9   ? -39.841 40.817  7.798   1.00 44.74  ? 9   GLU B CB  1 
ATOM   2178 C  CG  . GLU B 1 9   ? -40.145 42.032  6.907   1.00 56.03  ? 9   GLU B CG  1 
ATOM   2179 C  CD  . GLU B 1 9   ? -41.590 42.123  6.396   1.00 66.83  ? 9   GLU B CD  1 
ATOM   2180 O  OE1 . GLU B 1 9   ? -41.943 41.445  5.386   1.00 70.52  ? 9   GLU B OE1 1 
ATOM   2181 O  OE2 . GLU B 1 9   ? -42.375 42.917  6.981   1.00 66.64  ? 9   GLU B OE2 1 
ATOM   2182 N  N   . VAL B 1 10  ? -37.619 39.986  5.594   1.00 43.95  ? 10  VAL B N   1 
ATOM   2183 C  CA  . VAL B 1 10  ? -36.969 40.302  4.303   1.00 43.01  ? 10  VAL B CA  1 
ATOM   2184 C  C   . VAL B 1 10  ? -36.849 39.099  3.404   1.00 47.91  ? 10  VAL B C   1 
ATOM   2185 O  O   . VAL B 1 10  ? -36.855 39.209  2.180   1.00 50.40  ? 10  VAL B O   1 
ATOM   2186 C  CB  . VAL B 1 10  ? -35.576 40.954  4.474   1.00 47.82  ? 10  VAL B CB  1 
ATOM   2187 C  CG1 . VAL B 1 10  ? -34.524 39.943  4.935   1.00 49.69  ? 10  VAL B CG1 1 
ATOM   2188 C  CG2 . VAL B 1 10  ? -35.132 41.607  3.171   1.00 47.81  ? 10  VAL B CG2 1 
ATOM   2189 N  N   . GLN B 1 11  ? -36.754 37.940  4.033   1.00 50.16  ? 11  GLN B N   1 
ATOM   2190 C  CA  . GLN B 1 11  ? -36.388 36.705  3.362   1.00 52.94  ? 11  GLN B CA  1 
ATOM   2191 C  C   . GLN B 1 11  ? -37.546 36.180  2.520   1.00 62.03  ? 11  GLN B C   1 
ATOM   2192 O  O   . GLN B 1 11  ? -37.341 35.336  1.646   1.00 60.97  ? 11  GLN B O   1 
ATOM   2193 C  CB  . GLN B 1 11  ? -35.991 35.681  4.422   1.00 48.00  ? 11  GLN B CB  1 
ATOM   2194 C  CG  . GLN B 1 11  ? -35.279 34.442  3.928   1.00 42.30  ? 11  GLN B CG  1 
ATOM   2195 C  CD  . GLN B 1 11  ? -35.139 33.406  5.020   1.00 42.93  ? 11  GLN B CD  1 
ATOM   2196 O  OE1 . GLN B 1 11  ? -35.503 33.644  6.201   1.00 37.94  ? 11  GLN B OE1 1 
ATOM   2197 N  NE2 . GLN B 1 11  ? -34.616 32.235  4.645   1.00 39.43  ? 11  GLN B NE2 1 
ATOM   2198 N  N   . ALA B 1 12  ? -38.752 36.699  2.781   1.00 74.58  ? 12  ALA B N   1 
ATOM   2199 C  CA  . ALA B 1 12  ? -39.972 36.305  2.062   1.00 75.29  ? 12  ALA B CA  1 
ATOM   2200 C  C   . ALA B 1 12  ? -40.312 37.288  0.929   1.00 83.81  ? 12  ALA B C   1 
ATOM   2201 O  O   . ALA B 1 12  ? -41.477 37.628  0.707   1.00 93.62  ? 12  ALA B O   1 
ATOM   2202 C  CB  . ALA B 1 12  ? -41.134 36.157  3.037   1.00 65.62  ? 12  ALA B CB  1 
ATOM   2203 N  N   . GLU B 1 13  ? -39.274 37.745  0.229   1.00 85.14  ? 13  GLU B N   1 
ATOM   2204 C  CA  . GLU B 1 13  ? -39.388 38.631  -0.927  1.00 83.40  ? 13  GLU B CA  1 
ATOM   2205 C  C   . GLU B 1 13  ? -38.252 38.256  -1.875  1.00 91.02  ? 13  GLU B C   1 
ATOM   2206 O  O   . GLU B 1 13  ? -38.170 38.748  -3.006  1.00 95.96  ? 13  GLU B O   1 
ATOM   2207 C  CB  . GLU B 1 13  ? -39.267 40.103  -0.515  1.00 80.46  ? 13  GLU B CB  1 
ATOM   2208 C  CG  . GLU B 1 13  ? -40.218 40.533  0.594   1.00 80.59  ? 13  GLU B CG  1 
ATOM   2209 C  CD  . GLU B 1 13  ? -40.111 42.005  0.951   1.00 87.24  ? 13  GLU B CD  1 
ATOM   2210 O  OE1 . GLU B 1 13  ? -41.173 42.648  1.112   1.00 88.46  ? 13  GLU B OE1 1 
ATOM   2211 O  OE2 . GLU B 1 13  ? -38.977 42.523  1.078   1.00 86.52  ? 13  GLU B OE2 1 
ATOM   2212 N  N   . SER B 1 14  ? -37.369 37.389  -1.375  1.00 88.26  ? 14  SER B N   1 
ATOM   2213 C  CA  . SER B 1 14  ? -36.327 36.736  -2.159  1.00 89.68  ? 14  SER B CA  1 
ATOM   2214 C  C   . SER B 1 14  ? -36.663 35.430  -2.870  1.00 89.35  ? 14  SER B C   1 
ATOM   2215 O  O   . SER B 1 14  ? -36.783 35.411  -4.098  1.00 96.97  ? 14  SER B O   1 
ATOM   2216 C  CB  . SER B 1 14  ? -35.172 36.345  -1.250  1.00 90.97  ? 14  SER B CB  1 
ATOM   2217 O  OG  . SER B 1 14  ? -34.864 37.401  -0.361  1.00 97.77  ? 14  SER B OG  1 
ATOM   2218 N  N   . SER B 1 15  ? -36.808 34.343  -2.107  1.00 79.49  ? 15  SER B N   1 
ATOM   2219 C  CA  . SER B 1 15  ? -37.761 33.263  -2.292  1.00 83.85  ? 15  SER B CA  1 
ATOM   2220 C  C   . SER B 1 15  ? -39.029 33.936  -1.826  1.00 90.78  ? 15  SER B C   1 
ATOM   2221 O  O   . SER B 1 15  ? -39.092 34.423  -0.694  1.00 95.31  ? 15  SER B O   1 
ATOM   2222 C  CB  . SER B 1 15  ? -37.466 32.079  -1.389  1.00 76.07  ? 15  SER B CB  1 
ATOM   2223 O  OG  . SER B 1 15  ? -38.057 32.275  -0.115  1.00 63.11  ? 15  SER B OG  1 
ATOM   2224 N  N   . ASN B 1 16  ? -39.983 34.066  -2.730  1.00 96.70  ? 16  ASN B N   1 
ATOM   2225 C  CA  . ASN B 1 16  ? -41.220 34.856  -2.603  1.00 95.14  ? 16  ASN B CA  1 
ATOM   2226 C  C   . ASN B 1 16  ? -42.310 34.298  -1.687  1.00 93.53  ? 16  ASN B C   1 
ATOM   2227 O  O   . ASN B 1 16  ? -43.358 33.908  -2.206  1.00 94.59  ? 16  ASN B O   1 
ATOM   2228 C  CB  . ASN B 1 16  ? -41.923 34.838  -3.954  1.00 92.71  ? 16  ASN B CB  1 
ATOM   2229 C  CG  . ASN B 1 16  ? -41.923 36.187  -4.641  1.00 96.43  ? 16  ASN B CG  1 
ATOM   2230 O  OD1 . ASN B 1 16  ? -42.102 37.227  -4.004  1.00 98.18  ? 16  ASN B OD1 1 
ATOM   2231 N  ND2 . ASN B 1 16  ? -41.735 36.162  -5.948  1.00 98.55  ? 16  ASN B ND2 1 
ATOM   2232 N  N   . TYR B 1 17  ? -42.025 34.037  -0.405  1.00 90.58  ? 17  TYR B N   1 
ATOM   2233 C  CA  . TYR B 1 17  ? -43.058 33.596  0.575   1.00 87.48  ? 17  TYR B CA  1 
ATOM   2234 C  C   . TYR B 1 17  ? -43.625 32.119  0.628   1.00 87.79  ? 17  TYR B C   1 
ATOM   2235 O  O   . TYR B 1 17  ? -44.861 31.994  0.743   1.00 90.97  ? 17  TYR B O   1 
ATOM   2236 C  CB  . TYR B 1 17  ? -44.260 34.547  0.430   1.00 94.42  ? 17  TYR B CB  1 
ATOM   2237 C  CG  . TYR B 1 17  ? -44.704 35.305  1.672   1.00 100.60 ? 17  TYR B CG  1 
ATOM   2238 C  CD1 . TYR B 1 17  ? -44.672 36.697  1.711   1.00 98.43  ? 17  TYR B CD1 1 
ATOM   2239 C  CD2 . TYR B 1 17  ? -45.200 34.638  2.782   1.00 95.90  ? 17  TYR B CD2 1 
ATOM   2240 C  CE1 . TYR B 1 17  ? -45.093 37.396  2.825   1.00 94.11  ? 17  TYR B CE1 1 
ATOM   2241 C  CE2 . TYR B 1 17  ? -45.626 35.331  3.907   1.00 95.32  ? 17  TYR B CE2 1 
ATOM   2242 C  CZ  . TYR B 1 17  ? -45.570 36.709  3.921   1.00 96.97  ? 17  TYR B CZ  1 
ATOM   2243 O  OH  . TYR B 1 17  ? -45.990 37.409  5.031   1.00 97.77  ? 17  TYR B OH  1 
ATOM   2244 N  N   . PRO B 1 18  ? -42.815 31.093  0.449   1.00 77.36  ? 18  PRO B N   1 
ATOM   2245 C  CA  . PRO B 1 18  ? -43.359 29.747  0.604   1.00 65.60  ? 18  PRO B CA  1 
ATOM   2246 C  C   . PRO B 1 18  ? -43.182 29.402  2.059   1.00 62.45  ? 18  PRO B C   1 
ATOM   2247 O  O   . PRO B 1 18  ? -42.972 28.233  2.376   1.00 58.22  ? 18  PRO B O   1 
ATOM   2248 C  CB  . PRO B 1 18  ? -42.461 28.883  -0.283  1.00 66.85  ? 18  PRO B CB  1 
ATOM   2249 C  CG  . PRO B 1 18  ? -41.232 29.685  -0.543  1.00 71.54  ? 18  PRO B CG  1 
ATOM   2250 C  CD  . PRO B 1 18  ? -41.446 31.098  -0.092  1.00 75.85  ? 18  PRO B CD  1 
ATOM   2251 N  N   . CYS B 1 19  ? -43.252 30.424  2.917   1.00 57.68  ? 19  CYS B N   1 
ATOM   2252 C  CA  . CYS B 1 19  ? -42.743 30.365  4.277   1.00 50.34  ? 19  CYS B CA  1 
ATOM   2253 C  C   . CYS B 1 19  ? -43.394 31.429  5.126   1.00 45.38  ? 19  CYS B C   1 
ATOM   2254 O  O   . CYS B 1 19  ? -43.809 32.487  4.642   1.00 44.76  ? 19  CYS B O   1 
ATOM   2255 C  CB  . CYS B 1 19  ? -41.225 30.530  4.298   1.00 50.65  ? 19  CYS B CB  1 
ATOM   2256 S  SG  . CYS B 1 19  ? -40.711 32.009  3.435   1.00 58.05  ? 19  CYS B SG  1 
ATOM   2257 N  N   . LEU B 1 20  ? -43.506 31.130  6.409   1.00 42.19  ? 20  LEU B N   1 
ATOM   2258 C  CA  . LEU B 1 20  ? -44.184 32.023  7.331   1.00 39.26  ? 20  LEU B CA  1 
ATOM   2259 C  C   . LEU B 1 20  ? -43.270 33.194  7.696   1.00 40.32  ? 20  LEU B C   1 
ATOM   2260 O  O   . LEU B 1 20  ? -42.084 32.980  8.052   1.00 37.69  ? 20  LEU B O   1 
ATOM   2261 C  CB  . LEU B 1 20  ? -44.605 31.218  8.575   1.00 41.83  ? 20  LEU B CB  1 
ATOM   2262 C  CG  . LEU B 1 20  ? -45.584 30.072  8.268   1.00 39.87  ? 20  LEU B CG  1 
ATOM   2263 C  CD1 . LEU B 1 20  ? -46.033 29.387  9.539   1.00 36.35  ? 20  LEU B CD1 1 
ATOM   2264 C  CD2 . LEU B 1 20  ? -46.786 30.569  7.446   1.00 40.05  ? 20  LEU B CD2 1 
ATOM   2265 N  N   . VAL B 1 21  ? -43.793 34.422  7.564   1.00 38.29  ? 21  VAL B N   1 
ATOM   2266 C  CA  . VAL B 1 21  ? -43.095 35.601  8.066   1.00 36.89  ? 21  VAL B CA  1 
ATOM   2267 C  C   . VAL B 1 21  ? -43.305 35.664  9.570   1.00 34.99  ? 21  VAL B C   1 
ATOM   2268 O  O   . VAL B 1 21  ? -44.161 34.967  10.108  1.00 37.06  ? 21  VAL B O   1 
ATOM   2269 C  CB  . VAL B 1 21  ? -43.524 36.929  7.388   1.00 39.28  ? 21  VAL B CB  1 
ATOM   2270 C  CG1 . VAL B 1 21  ? -43.203 36.901  5.901   1.00 40.96  ? 21  VAL B CG1 1 
ATOM   2271 C  CG2 . VAL B 1 21  ? -44.989 37.234  7.633   1.00 36.11  ? 21  VAL B CG2 1 
ATOM   2272 N  N   . PRO B 1 22  ? -42.499 36.464  10.266  1.00 34.02  ? 22  PRO B N   1 
ATOM   2273 C  CA  . PRO B 1 22  ? -42.568 36.392  11.737  1.00 31.61  ? 22  PRO B CA  1 
ATOM   2274 C  C   . PRO B 1 22  ? -43.972 36.551  12.373  1.00 32.83  ? 22  PRO B C   1 
ATOM   2275 O  O   . PRO B 1 22  ? -44.362 35.735  13.221  1.00 27.85  ? 22  PRO B O   1 
ATOM   2276 C  CB  . PRO B 1 22  ? -41.594 37.491  12.147  1.00 30.01  ? 22  PRO B CB  1 
ATOM   2277 C  CG  . PRO B 1 22  ? -40.502 37.350  11.114  1.00 29.97  ? 22  PRO B CG  1 
ATOM   2278 C  CD  . PRO B 1 22  ? -41.250 37.125  9.825   1.00 32.25  ? 22  PRO B CD  1 
ATOM   2279 N  N   . VAL B 1 23  ? -44.732 37.564  11.965  1.00 36.49  ? 23  VAL B N   1 
ATOM   2280 C  CA  . VAL B 1 23  ? -46.061 37.787  12.577  1.00 40.25  ? 23  VAL B CA  1 
ATOM   2281 C  C   . VAL B 1 23  ? -47.009 36.610  12.282  1.00 39.47  ? 23  VAL B C   1 
ATOM   2282 O  O   . VAL B 1 23  ? -48.050 36.449  12.925  1.00 41.59  ? 23  VAL B O   1 
ATOM   2283 C  CB  . VAL B 1 23  ? -46.667 39.184  12.248  1.00 41.90  ? 23  VAL B CB  1 
ATOM   2284 C  CG1 . VAL B 1 23  ? -47.419 39.731  13.452  1.00 44.34  ? 23  VAL B CG1 1 
ATOM   2285 C  CG2 . VAL B 1 23  ? -45.586 40.213  11.911  1.00 44.10  ? 23  VAL B CG2 1 
ATOM   2286 N  N   . LYS B 1 24  ? -46.617 35.753  11.343  1.00 39.46  ? 24  LYS B N   1 
ATOM   2287 C  CA  . LYS B 1 24  ? -47.371 34.547  11.063  1.00 41.36  ? 24  LYS B CA  1 
ATOM   2288 C  C   . LYS B 1 24  ? -46.709 33.225  11.433  1.00 45.87  ? 24  LYS B C   1 
ATOM   2289 O  O   . LYS B 1 24  ? -47.252 32.160  11.089  1.00 41.70  ? 24  LYS B O   1 
ATOM   2290 C  CB  . LYS B 1 24  ? -47.782 34.532  9.596   1.00 48.88  ? 24  LYS B CB  1 
ATOM   2291 C  CG  . LYS B 1 24  ? -49.037 35.347  9.331   1.00 50.51  ? 24  LYS B CG  1 
ATOM   2292 C  CD  . LYS B 1 24  ? -48.911 36.029  7.987   1.00 53.07  ? 24  LYS B CD  1 
ATOM   2293 C  CE  . LYS B 1 24  ? -50.182 36.773  7.604   1.00 54.51  ? 24  LYS B CE  1 
ATOM   2294 N  NZ  . LYS B 1 24  ? -50.162 37.138  6.156   1.00 51.49  ? 24  LYS B NZ  1 
ATOM   2295 N  N   . TRP B 1 25  ? -45.563 33.255  12.137  1.00 44.77  ? 25  TRP B N   1 
ATOM   2296 C  CA  . TRP B 1 25  ? -44.958 31.996  12.617  1.00 42.20  ? 25  TRP B CA  1 
ATOM   2297 C  C   . TRP B 1 25  ? -45.964 31.294  13.559  1.00 44.55  ? 25  TRP B C   1 
ATOM   2298 O  O   . TRP B 1 25  ? -46.774 31.947  14.217  1.00 43.58  ? 25  TRP B O   1 
ATOM   2299 C  CB  . TRP B 1 25  ? -43.630 32.215  13.357  1.00 40.09  ? 25  TRP B CB  1 
ATOM   2300 C  CG  . TRP B 1 25  ? -42.430 32.728  12.571  1.00 34.45  ? 25  TRP B CG  1 
ATOM   2301 C  CD1 . TRP B 1 25  ? -42.240 32.778  11.186  1.00 35.02  ? 25  TRP B CD1 1 
ATOM   2302 C  CD2 . TRP B 1 25  ? -41.181 33.260  13.144  1.00 35.65  ? 25  TRP B CD2 1 
ATOM   2303 N  NE1 . TRP B 1 25  ? -40.998 33.298  10.883  1.00 34.85  ? 25  TRP B NE1 1 
ATOM   2304 C  CE2 . TRP B 1 25  ? -40.315 33.606  12.014  1.00 35.44  ? 25  TRP B CE2 1 
ATOM   2305 C  CE3 . TRP B 1 25  ? -40.719 33.478  14.436  1.00 34.91  ? 25  TRP B CE3 1 
ATOM   2306 C  CZ2 . TRP B 1 25  ? -39.049 34.145  12.199  1.00 31.41  ? 25  TRP B CZ2 1 
ATOM   2307 C  CZ3 . TRP B 1 25  ? -39.445 34.020  14.608  1.00 30.48  ? 25  TRP B CZ3 1 
ATOM   2308 C  CH2 . TRP B 1 25  ? -38.631 34.344  13.517  1.00 29.48  ? 25  TRP B CH2 1 
ATOM   2309 N  N   . GLY B 1 26  ? -45.917 29.962  13.609  1.00 43.78  ? 26  GLY B N   1 
ATOM   2310 C  CA  . GLY B 1 26  ? -46.919 29.194  14.323  1.00 47.60  ? 26  GLY B CA  1 
ATOM   2311 C  C   . GLY B 1 26  ? -46.476 28.819  15.711  1.00 52.50  ? 26  GLY B C   1 
ATOM   2312 O  O   . GLY B 1 26  ? -45.879 29.629  16.421  1.00 54.00  ? 26  GLY B O   1 
ATOM   2313 N  N   . GLY B 1 27  ? -46.779 27.584  16.099  1.00 51.73  ? 27  GLY B N   1 
ATOM   2314 C  CA  . GLY B 1 27  ? -46.588 27.135  17.472  1.00 47.53  ? 27  GLY B CA  1 
ATOM   2315 C  C   . GLY B 1 27  ? -46.799 28.238  18.481  1.00 48.48  ? 27  GLY B C   1 
ATOM   2316 O  O   . GLY B 1 27  ? -47.770 29.008  18.411  1.00 49.87  ? 27  GLY B O   1 
ATOM   2317 N  N   . ASN B 1 28  ? -45.833 28.338  19.386  1.00 47.86  ? 28  ASN B N   1 
ATOM   2318 C  CA  . ASN B 1 28  ? -45.867 29.242  20.529  1.00 39.78  ? 28  ASN B CA  1 
ATOM   2319 C  C   . ASN B 1 28  ? -45.477 30.696  20.286  1.00 36.79  ? 28  ASN B C   1 
ATOM   2320 O  O   . ASN B 1 28  ? -45.405 31.475  21.230  1.00 32.83  ? 28  ASN B O   1 
ATOM   2321 C  CB  . ASN B 1 28  ? -44.960 28.664  21.609  1.00 41.17  ? 28  ASN B CB  1 
ATOM   2322 C  CG  . ASN B 1 28  ? -45.369 27.251  22.019  1.00 42.44  ? 28  ASN B CG  1 
ATOM   2323 O  OD1 . ASN B 1 28  ? -46.336 27.060  22.743  1.00 42.44  ? 28  ASN B OD1 1 
ATOM   2324 N  ND2 . ASN B 1 28  ? -44.628 26.272  21.560  1.00 38.90  ? 28  ASN B ND2 1 
ATOM   2325 N  N   . CYS B 1 29  ? -45.247 31.072  19.033  1.00 37.74  ? 29  CYS B N   1 
ATOM   2326 C  CA  . CYS B 1 29  ? -44.737 32.418  18.733  1.00 38.23  ? 29  CYS B CA  1 
ATOM   2327 C  C   . CYS B 1 29  ? -45.708 33.567  19.041  1.00 40.21  ? 29  CYS B C   1 
ATOM   2328 O  O   . CYS B 1 29  ? -45.301 34.725  19.123  1.00 34.54  ? 29  CYS B O   1 
ATOM   2329 C  CB  . CYS B 1 29  ? -44.237 32.487  17.285  1.00 37.76  ? 29  CYS B CB  1 
ATOM   2330 S  SG  . CYS B 1 29  ? -43.136 31.110  16.885  1.00 39.14  ? 29  CYS B SG  1 
ATOM   2331 N  N   . GLN B 1 30  ? -46.987 33.247  19.216  1.00 43.01  ? 30  GLN B N   1 
ATOM   2332 C  CA  . GLN B 1 30  ? -48.004 34.266  19.406  1.00 43.30  ? 30  GLN B CA  1 
ATOM   2333 C  C   . GLN B 1 30  ? -48.415 34.439  20.845  1.00 46.53  ? 30  GLN B C   1 
ATOM   2334 O  O   . GLN B 1 30  ? -49.362 35.180  21.129  1.00 46.55  ? 30  GLN B O   1 
ATOM   2335 C  CB  . GLN B 1 30  ? -49.238 33.948  18.564  1.00 46.60  ? 30  GLN B CB  1 
ATOM   2336 C  CG  . GLN B 1 30  ? -48.912 33.636  17.112  1.00 50.89  ? 30  GLN B CG  1 
ATOM   2337 C  CD  . GLN B 1 30  ? -48.005 34.681  16.474  1.00 55.48  ? 30  GLN B CD  1 
ATOM   2338 O  OE1 . GLN B 1 30  ? -48.070 35.875  16.809  1.00 49.95  ? 30  GLN B OE1 1 
ATOM   2339 N  NE2 . GLN B 1 30  ? -47.141 34.235  15.557  1.00 54.60  ? 30  GLN B NE2 1 
ATOM   2340 N  N   . LYS B 1 31  ? -47.707 33.762  21.748  1.00 47.71  ? 31  LYS B N   1 
ATOM   2341 C  CA  . LYS B 1 31  ? -48.007 33.832  23.181  1.00 46.59  ? 31  LYS B CA  1 
ATOM   2342 C  C   . LYS B 1 31  ? -47.363 35.020  23.890  1.00 45.82  ? 31  LYS B C   1 
ATOM   2343 O  O   . LYS B 1 31  ? -46.888 35.944  23.230  1.00 48.55  ? 31  LYS B O   1 
ATOM   2344 C  CB  . LYS B 1 31  ? -47.693 32.505  23.854  1.00 49.10  ? 31  LYS B CB  1 
ATOM   2345 C  CG  . LYS B 1 31  ? -48.602 31.399  23.359  1.00 48.82  ? 31  LYS B CG  1 
ATOM   2346 C  CD  . LYS B 1 31  ? -47.972 30.037  23.556  1.00 53.60  ? 31  LYS B CD  1 
ATOM   2347 C  CE  . LYS B 1 31  ? -49.037 29.002  23.861  1.00 57.96  ? 31  LYS B CE  1 
ATOM   2348 N  NZ  . LYS B 1 31  ? -49.749 29.363  25.125  1.00 57.32  ? 31  LYS B NZ  1 
ATOM   2349 N  N   . ASP B 1 32  ? -47.338 34.999  25.220  1.00 48.74  ? 32  ASP B N   1 
ATOM   2350 C  CA  . ASP B 1 32  ? -47.219 36.239  25.992  1.00 49.09  ? 32  ASP B CA  1 
ATOM   2351 C  C   . ASP B 1 32  ? -45.900 36.490  26.735  1.00 50.06  ? 32  ASP B C   1 
ATOM   2352 O  O   . ASP B 1 32  ? -45.718 37.564  27.309  1.00 49.21  ? 32  ASP B O   1 
ATOM   2353 C  CB  . ASP B 1 32  ? -48.392 36.372  26.974  1.00 55.09  ? 32  ASP B CB  1 
ATOM   2354 C  CG  . ASP B 1 32  ? -49.714 36.775  26.289  1.00 64.07  ? 32  ASP B CG  1 
ATOM   2355 O  OD1 . ASP B 1 32  ? -49.803 36.745  25.037  1.00 65.11  ? 32  ASP B OD1 1 
ATOM   2356 O  OD2 . ASP B 1 32  ? -50.674 37.122  27.017  1.00 60.55  ? 32  ASP B OD2 1 
ATOM   2357 N  N   . ARG B 1 33  ? -45.007 35.502  26.759  1.00 49.83  ? 33  ARG B N   1 
ATOM   2358 C  CA  . ARG B 1 33  ? -43.714 35.661  27.440  1.00 43.85  ? 33  ARG B CA  1 
ATOM   2359 C  C   . ARG B 1 33  ? -42.603 35.457  26.420  1.00 42.07  ? 33  ARG B C   1 
ATOM   2360 O  O   . ARG B 1 33  ? -41.697 34.641  26.613  1.00 45.59  ? 33  ARG B O   1 
ATOM   2361 C  CB  . ARG B 1 33  ? -43.616 34.705  28.631  1.00 40.69  ? 33  ARG B CB  1 
ATOM   2362 C  CG  . ARG B 1 33  ? -44.571 35.096  29.759  1.00 45.76  ? 33  ARG B CG  1 
ATOM   2363 C  CD  . ARG B 1 33  ? -44.665 34.098  30.917  1.00 45.02  ? 33  ARG B CD  1 
ATOM   2364 N  NE  . ARG B 1 33  ? -43.446 34.058  31.715  1.00 51.03  ? 33  ARG B NE  1 
ATOM   2365 C  CZ  . ARG B 1 33  ? -43.098 34.947  32.658  1.00 54.88  ? 33  ARG B CZ  1 
ATOM   2366 N  NH1 . ARG B 1 33  ? -43.883 35.986  32.969  1.00 51.86  ? 33  ARG B NH1 1 
ATOM   2367 N  NH2 . ARG B 1 33  ? -41.948 34.792  33.310  1.00 49.61  ? 33  ARG B NH2 1 
ATOM   2368 N  N   . GLN B 1 34  ? -42.696 36.211  25.320  1.00 39.21  ? 34  GLN B N   1 
ATOM   2369 C  CA  . GLN B 1 34  ? -41.850 36.023  24.135  1.00 35.74  ? 34  GLN B CA  1 
ATOM   2370 C  C   . GLN B 1 34  ? -40.553 36.852  24.117  1.00 34.22  ? 34  GLN B C   1 
ATOM   2371 O  O   . GLN B 1 34  ? -40.403 37.859  24.844  1.00 30.69  ? 34  GLN B O   1 
ATOM   2372 C  CB  . GLN B 1 34  ? -42.647 36.299  22.856  1.00 35.19  ? 34  GLN B CB  1 
ATOM   2373 C  CG  . GLN B 1 34  ? -43.723 35.284  22.496  1.00 36.70  ? 34  GLN B CG  1 
ATOM   2374 C  CD  . GLN B 1 34  ? -43.142 33.950  22.127  1.00 38.19  ? 34  GLN B CD  1 
ATOM   2375 O  OE1 . GLN B 1 34  ? -42.597 33.772  21.013  1.00 34.05  ? 34  GLN B OE1 1 
ATOM   2376 N  NE2 . GLN B 1 34  ? -43.264 32.990  23.036  1.00 32.87  ? 34  GLN B NE2 1 
ATOM   2377 N  N   . SER B 1 35  ? -39.637 36.445  23.239  1.00 31.60  ? 35  SER B N   1 
ATOM   2378 C  CA  . SER B 1 35  ? -38.353 37.112  23.096  1.00 27.79  ? 35  SER B CA  1 
ATOM   2379 C  C   . SER B 1 35  ? -38.119 37.386  21.635  1.00 29.72  ? 35  SER B C   1 
ATOM   2380 O  O   . SER B 1 35  ? -38.603 36.640  20.803  1.00 31.95  ? 35  SER B O   1 
ATOM   2381 C  CB  . SER B 1 35  ? -37.235 36.191  23.581  1.00 28.08  ? 35  SER B CB  1 
ATOM   2382 O  OG  . SER B 1 35  ? -37.112 36.240  24.968  1.00 27.52  ? 35  SER B OG  1 
ATOM   2383 N  N   . PRO B 1 36  ? -37.340 38.433  21.298  1.00 28.53  ? 36  PRO B N   1 
ATOM   2384 C  CA  . PRO B 1 36  ? -36.560 39.383  22.084  1.00 27.77  ? 36  PRO B CA  1 
ATOM   2385 C  C   . PRO B 1 36  ? -37.350 40.583  22.653  1.00 30.55  ? 36  PRO B C   1 
ATOM   2386 O  O   . PRO B 1 36  ? -38.473 40.854  22.230  1.00 28.36  ? 36  PRO B O   1 
ATOM   2387 C  CB  . PRO B 1 36  ? -35.569 39.913  21.064  1.00 27.22  ? 36  PRO B CB  1 
ATOM   2388 C  CG  . PRO B 1 36  ? -36.267 39.873  19.758  1.00 25.00  ? 36  PRO B CG  1 
ATOM   2389 C  CD  . PRO B 1 36  ? -37.155 38.641  19.854  1.00 26.26  ? 36  PRO B CD  1 
ATOM   2390 N  N   . ILE B 1 37  ? -36.737 41.287  23.606  1.00 26.85  ? 37  ILE B N   1 
ATOM   2391 C  CA  . ILE B 1 37  ? -37.312 42.479  24.209  1.00 28.16  ? 37  ILE B CA  1 
ATOM   2392 C  C   . ILE B 1 37  ? -36.368 43.665  24.216  1.00 28.76  ? 37  ILE B C   1 
ATOM   2393 O  O   . ILE B 1 37  ? -35.120 43.560  24.028  1.00 29.25  ? 37  ILE B O   1 
ATOM   2394 C  CB  . ILE B 1 37  ? -37.748 42.247  25.676  1.00 27.86  ? 37  ILE B CB  1 
ATOM   2395 C  CG1 . ILE B 1 37  ? -36.519 41.950  26.549  1.00 27.01  ? 37  ILE B CG1 1 
ATOM   2396 C  CG2 . ILE B 1 37  ? -38.770 41.107  25.728  1.00 27.14  ? 37  ILE B CG2 1 
ATOM   2397 C  CD1 . ILE B 1 37  ? -36.823 41.791  28.017  1.00 27.04  ? 37  ILE B CD1 1 
ATOM   2398 N  N   . ASN B 1 38  ? -36.980 44.806  24.438  1.00 27.90  ? 38  ASN B N   1 
ATOM   2399 C  CA  . ASN B 1 38  ? -36.224 45.983  24.753  1.00 31.51  ? 38  ASN B CA  1 
ATOM   2400 C  C   . ASN B 1 38  ? -36.026 46.070  26.274  1.00 31.65  ? 38  ASN B C   1 
ATOM   2401 O  O   . ASN B 1 38  ? -36.942 45.816  27.072  1.00 30.21  ? 38  ASN B O   1 
ATOM   2402 C  CB  . ASN B 1 38  ? -36.915 47.203  24.169  1.00 31.71  ? 38  ASN B CB  1 
ATOM   2403 C  CG  . ASN B 1 38  ? -36.163 48.479  24.441  1.00 32.60  ? 38  ASN B CG  1 
ATOM   2404 O  OD1 . ASN B 1 38  ? -34.980 48.623  24.091  1.00 36.46  ? 38  ASN B OD1 1 
ATOM   2405 N  ND2 . ASN B 1 38  ? -36.839 49.419  25.064  1.00 32.05  ? 38  ASN B ND2 1 
ATOM   2406 N  N   . ILE B 1 39  ? -34.804 46.361  26.670  1.00 36.53  ? 39  ILE B N   1 
ATOM   2407 C  CA  . ILE B 1 39  ? -34.466 46.447  28.074  1.00 39.59  ? 39  ILE B CA  1 
ATOM   2408 C  C   . ILE B 1 39  ? -34.331 47.918  28.430  1.00 38.10  ? 39  ILE B C   1 
ATOM   2409 O  O   . ILE B 1 39  ? -33.551 48.661  27.804  1.00 34.27  ? 39  ILE B O   1 
ATOM   2410 C  CB  . ILE B 1 39  ? -33.189 45.653  28.392  1.00 40.61  ? 39  ILE B CB  1 
ATOM   2411 C  CG1 . ILE B 1 39  ? -33.487 44.145  28.303  1.00 40.36  ? 39  ILE B CG1 1 
ATOM   2412 C  CG2 . ILE B 1 39  ? -32.665 46.010  29.779  1.00 43.30  ? 39  ILE B CG2 1 
ATOM   2413 C  CD1 . ILE B 1 39  ? -32.262 43.240  28.362  1.00 34.26  ? 39  ILE B CD1 1 
ATOM   2414 N  N   . VAL B 1 40  ? -35.144 48.348  29.393  1.00 39.19  ? 40  VAL B N   1 
ATOM   2415 C  CA  . VAL B 1 40  ? -35.004 49.705  29.912  1.00 35.30  ? 40  VAL B CA  1 
ATOM   2416 C  C   . VAL B 1 40  ? -34.033 49.584  31.063  1.00 34.76  ? 40  VAL B C   1 
ATOM   2417 O  O   . VAL B 1 40  ? -34.424 49.088  32.132  1.00 33.92  ? 40  VAL B O   1 
ATOM   2418 C  CB  . VAL B 1 40  ? -36.327 50.289  30.437  1.00 37.10  ? 40  VAL B CB  1 
ATOM   2419 C  CG1 . VAL B 1 40  ? -36.139 51.785  30.712  1.00 38.80  ? 40  VAL B CG1 1 
ATOM   2420 C  CG2 . VAL B 1 40  ? -37.456 50.073  29.449  1.00 32.75  ? 40  VAL B CG2 1 
ATOM   2421 N  N   . THR B 1 41  ? -32.781 50.012  30.838  1.00 36.32  ? 41  THR B N   1 
ATOM   2422 C  CA  . THR B 1 41  ? -31.681 49.794  31.782  1.00 40.07  ? 41  THR B CA  1 
ATOM   2423 C  C   . THR B 1 41  ? -31.922 50.416  33.154  1.00 45.49  ? 41  THR B C   1 
ATOM   2424 O  O   . THR B 1 41  ? -31.530 49.859  34.181  1.00 49.21  ? 41  THR B O   1 
ATOM   2425 C  CB  . THR B 1 41  ? -30.301 50.221  31.219  1.00 43.11  ? 41  THR B CB  1 
ATOM   2426 O  OG1 . THR B 1 41  ? -30.227 51.647  31.083  1.00 53.86  ? 41  THR B OG1 1 
ATOM   2427 C  CG2 . THR B 1 41  ? -30.047 49.598  29.851  1.00 40.89  ? 41  THR B CG2 1 
ATOM   2428 N  N   . THR B 1 42  ? -32.582 51.566  33.182  1.00 51.85  ? 42  THR B N   1 
ATOM   2429 C  CA  . THR B 1 42  ? -32.803 52.243  34.450  1.00 52.96  ? 42  THR B CA  1 
ATOM   2430 C  C   . THR B 1 42  ? -33.985 51.618  35.170  1.00 51.35  ? 42  THR B C   1 
ATOM   2431 O  O   . THR B 1 42  ? -34.206 51.875  36.342  1.00 53.80  ? 42  THR B O   1 
ATOM   2432 C  CB  . THR B 1 42  ? -33.039 53.750  34.260  1.00 50.81  ? 42  THR B CB  1 
ATOM   2433 O  OG1 . THR B 1 42  ? -34.193 53.948  33.427  1.00 55.44  ? 42  THR B OG1 1 
ATOM   2434 C  CG2 . THR B 1 42  ? -31.808 54.411  33.632  1.00 46.80  ? 42  THR B CG2 1 
ATOM   2435 N  N   . LYS B 1 43  ? -34.737 50.779  34.472  1.00 51.15  ? 43  LYS B N   1 
ATOM   2436 C  CA  . LYS B 1 43  ? -35.876 50.136  35.110  1.00 50.22  ? 43  LYS B CA  1 
ATOM   2437 C  C   . LYS B 1 43  ? -35.630 48.698  35.540  1.00 50.34  ? 43  LYS B C   1 
ATOM   2438 O  O   . LYS B 1 43  ? -36.528 48.055  36.098  1.00 53.70  ? 43  LYS B O   1 
ATOM   2439 C  CB  . LYS B 1 43  ? -37.106 50.244  34.229  1.00 53.39  ? 43  LYS B CB  1 
ATOM   2440 C  CG  . LYS B 1 43  ? -37.571 51.681  34.025  1.00 50.74  ? 43  LYS B CG  1 
ATOM   2441 C  CD  . LYS B 1 43  ? -38.940 51.638  33.388  1.00 50.49  ? 43  LYS B CD  1 
ATOM   2442 C  CE  . LYS B 1 43  ? -39.581 53.004  33.323  1.00 48.50  ? 43  LYS B CE  1 
ATOM   2443 N  NZ  . LYS B 1 43  ? -40.827 52.806  32.542  1.00 43.13  ? 43  LYS B NZ  1 
ATOM   2444 N  N   . ALA B 1 44  ? -34.429 48.190  35.281  1.00 45.05  ? 44  ALA B N   1 
ATOM   2445 C  CA  . ALA B 1 44  ? -34.043 46.871  35.777  1.00 47.47  ? 44  ALA B CA  1 
ATOM   2446 C  C   . ALA B 1 44  ? -33.304 47.050  37.105  1.00 50.44  ? 44  ALA B C   1 
ATOM   2447 O  O   . ALA B 1 44  ? -32.473 47.942  37.235  1.00 53.58  ? 44  ALA B O   1 
ATOM   2448 C  CB  . ALA B 1 44  ? -33.178 46.135  34.757  1.00 41.19  ? 44  ALA B CB  1 
ATOM   2449 N  N   . LYS B 1 45  ? -33.611 46.183  38.074  1.00 56.52  ? 45  LYS B N   1 
ATOM   2450 C  CA  . LYS B 1 45  ? -33.202 46.356  39.473  1.00 56.57  ? 45  LYS B CA  1 
ATOM   2451 C  C   . LYS B 1 45  ? -32.108 45.395  39.926  1.00 56.60  ? 45  LYS B C   1 
ATOM   2452 O  O   . LYS B 1 45  ? -32.189 44.185  39.678  1.00 53.32  ? 45  LYS B O   1 
ATOM   2453 C  CB  . LYS B 1 45  ? -34.429 46.215  40.396  1.00 62.64  ? 45  LYS B CB  1 
ATOM   2454 C  CG  . LYS B 1 45  ? -35.173 47.534  40.637  1.00 68.12  ? 45  LYS B CG  1 
ATOM   2455 C  CD  . LYS B 1 45  ? -36.693 47.390  40.579  1.00 67.28  ? 45  LYS B CD  1 
ATOM   2456 C  CE  . LYS B 1 45  ? -37.218 46.463  41.668  1.00 70.39  ? 45  LYS B CE  1 
ATOM   2457 N  NZ  . LYS B 1 45  ? -38.661 46.149  41.496  1.00 71.55  ? 45  LYS B NZ  1 
ATOM   2458 N  N   . VAL B 1 46  ? -31.094 45.930  40.608  1.00 53.35  ? 46  VAL B N   1 
ATOM   2459 C  CA  . VAL B 1 46  ? -30.022 45.087  41.127  1.00 50.44  ? 46  VAL B CA  1 
ATOM   2460 C  C   . VAL B 1 46  ? -30.649 43.954  41.931  1.00 53.08  ? 46  VAL B C   1 
ATOM   2461 O  O   . VAL B 1 46  ? -31.537 44.170  42.754  1.00 57.37  ? 46  VAL B O   1 
ATOM   2462 C  CB  . VAL B 1 46  ? -28.990 45.881  41.960  1.00 50.35  ? 46  VAL B CB  1 
ATOM   2463 C  CG1 . VAL B 1 46  ? -27.845 44.985  42.427  1.00 49.61  ? 46  VAL B CG1 1 
ATOM   2464 C  CG2 . VAL B 1 46  ? -28.430 47.026  41.145  1.00 53.48  ? 46  VAL B CG2 1 
ATOM   2465 N  N   . ASP B 1 47  ? -30.221 42.734  41.640  1.00 57.98  ? 47  ASP B N   1 
ATOM   2466 C  CA  . ASP B 1 47  ? -30.578 41.568  42.423  1.00 56.94  ? 47  ASP B CA  1 
ATOM   2467 C  C   . ASP B 1 47  ? -29.230 40.978  42.804  1.00 64.20  ? 47  ASP B C   1 
ATOM   2468 O  O   . ASP B 1 47  ? -28.420 40.663  41.927  1.00 62.25  ? 47  ASP B O   1 
ATOM   2469 C  CB  . ASP B 1 47  ? -31.394 40.597  41.577  1.00 58.71  ? 47  ASP B CB  1 
ATOM   2470 C  CG  . ASP B 1 47  ? -32.026 39.466  42.394  1.00 61.94  ? 47  ASP B CG  1 
ATOM   2471 O  OD1 . ASP B 1 47  ? -31.371 38.884  43.286  1.00 64.92  ? 47  ASP B OD1 1 
ATOM   2472 O  OD2 . ASP B 1 47  ? -33.189 39.124  42.113  1.00 63.21  ? 47  ASP B OD2 1 
ATOM   2473 N  N   . LYS B 1 48  ? -28.963 40.867  44.103  1.00 60.40  ? 48  LYS B N   1 
ATOM   2474 C  CA  . LYS B 1 48  ? -27.646 40.394  44.556  1.00 61.25  ? 48  LYS B CA  1 
ATOM   2475 C  C   . LYS B 1 48  ? -27.420 38.871  44.436  1.00 55.25  ? 48  LYS B C   1 
ATOM   2476 O  O   . LYS B 1 48  ? -26.288 38.403  44.518  1.00 54.65  ? 48  LYS B O   1 
ATOM   2477 C  CB  . LYS B 1 48  ? -27.327 40.921  45.971  1.00 65.13  ? 48  LYS B CB  1 
ATOM   2478 C  CG  . LYS B 1 48  ? -26.612 42.270  45.970  1.00 64.68  ? 48  LYS B CG  1 
ATOM   2479 C  CD  . LYS B 1 48  ? -26.916 43.102  47.212  1.00 66.67  ? 48  LYS B CD  1 
ATOM   2480 C  CE  . LYS B 1 48  ? -26.201 44.454  47.149  1.00 65.08  ? 48  LYS B CE  1 
ATOM   2481 N  NZ  . LYS B 1 48  ? -26.992 45.577  47.736  1.00 63.75  ? 48  LYS B NZ  1 
ATOM   2482 N  N   . LYS B 1 49  ? -28.489 38.106  44.237  1.00 53.13  ? 49  LYS B N   1 
ATOM   2483 C  CA  . LYS B 1 49  ? -28.367 36.685  43.935  1.00 54.18  ? 49  LYS B CA  1 
ATOM   2484 C  C   . LYS B 1 49  ? -27.700 36.463  42.562  1.00 55.06  ? 49  LYS B C   1 
ATOM   2485 O  O   . LYS B 1 49  ? -27.434 35.330  42.174  1.00 52.92  ? 49  LYS B O   1 
ATOM   2486 C  CB  . LYS B 1 49  ? -29.742 36.014  43.947  1.00 55.95  ? 49  LYS B CB  1 
ATOM   2487 C  CG  . LYS B 1 49  ? -30.095 35.279  45.236  1.00 57.13  ? 49  LYS B CG  1 
ATOM   2488 C  CD  . LYS B 1 49  ? -31.579 34.960  45.266  1.00 57.85  ? 49  LYS B CD  1 
ATOM   2489 C  CE  . LYS B 1 49  ? -31.866 33.630  45.949  1.00 63.72  ? 49  LYS B CE  1 
ATOM   2490 N  NZ  . LYS B 1 49  ? -32.492 33.726  47.301  1.00 68.44  ? 49  LYS B NZ  1 
ATOM   2491 N  N   . LEU B 1 50  ? -27.445 37.552  41.834  1.00 51.92  ? 50  LEU B N   1 
ATOM   2492 C  CA  . LEU B 1 50  ? -26.863 37.480  40.491  1.00 47.09  ? 50  LEU B CA  1 
ATOM   2493 C  C   . LEU B 1 50  ? -25.335 37.598  40.517  1.00 48.54  ? 50  LEU B C   1 
ATOM   2494 O  O   . LEU B 1 50  ? -24.752 38.634  40.194  1.00 49.72  ? 50  LEU B O   1 
ATOM   2495 C  CB  . LEU B 1 50  ? -27.571 38.466  39.526  1.00 46.89  ? 50  LEU B CB  1 
ATOM   2496 C  CG  . LEU B 1 50  ? -29.061 38.133  39.194  1.00 41.75  ? 50  LEU B CG  1 
ATOM   2497 C  CD1 . LEU B 1 50  ? -29.632 39.019  38.102  1.00 40.57  ? 50  LEU B CD1 1 
ATOM   2498 C  CD2 . LEU B 1 50  ? -29.246 36.669  38.786  1.00 42.29  ? 50  LEU B CD2 1 
ATOM   2499 N  N   . GLY B 1 51  ? -24.692 36.507  40.926  1.00 52.62  ? 51  GLY B N   1 
ATOM   2500 C  CA  . GLY B 1 51  ? -23.244 36.469  41.067  1.00 48.69  ? 51  GLY B CA  1 
ATOM   2501 C  C   . GLY B 1 51  ? -22.539 36.309  39.728  1.00 52.30  ? 51  GLY B C   1 
ATOM   2502 O  O   . GLY B 1 51  ? -23.118 36.496  38.660  1.00 49.56  ? 51  GLY B O   1 
ATOM   2503 N  N   . ARG B 1 52  ? -21.270 35.960  39.777  1.00 47.05  ? 52  ARG B N   1 
ATOM   2504 C  CA  . ARG B 1 52  ? -20.490 35.885  38.561  1.00 46.87  ? 52  ARG B CA  1 
ATOM   2505 C  C   . ARG B 1 52  ? -20.681 34.532  37.835  1.00 42.09  ? 52  ARG B C   1 
ATOM   2506 O  O   . ARG B 1 52  ? -20.979 33.550  38.466  1.00 39.37  ? 52  ARG B O   1 
ATOM   2507 C  CB  . ARG B 1 52  ? -19.037 36.186  38.911  1.00 47.97  ? 52  ARG B CB  1 
ATOM   2508 C  CG  . ARG B 1 52  ? -18.765 37.678  39.103  1.00 59.37  ? 52  ARG B CG  1 
ATOM   2509 C  CD  . ARG B 1 52  ? -19.893 38.480  39.789  1.00 69.27  ? 52  ARG B CD  1 
ATOM   2510 N  NE  . ARG B 1 52  ? -19.777 39.943  39.620  1.00 70.42  ? 52  ARG B NE  1 
ATOM   2511 C  CZ  . ARG B 1 52  ? -20.652 40.843  40.080  1.00 77.57  ? 52  ARG B CZ  1 
ATOM   2512 N  NH1 . ARG B 1 52  ? -21.732 40.453  40.747  1.00 78.53  ? 52  ARG B NH1 1 
ATOM   2513 N  NH2 . ARG B 1 52  ? -20.450 42.148  39.870  1.00 79.28  ? 52  ARG B NH2 1 
ATOM   2514 N  N   . PHE B 1 53  ? -20.559 34.484  36.511  1.00 37.67  ? 53  PHE B N   1 
ATOM   2515 C  CA  . PHE B 1 53  ? -20.671 33.177  35.807  1.00 35.55  ? 53  PHE B CA  1 
ATOM   2516 C  C   . PHE B 1 53  ? -19.373 32.437  35.950  1.00 34.94  ? 53  PHE B C   1 
ATOM   2517 O  O   . PHE B 1 53  ? -18.317 33.039  36.058  1.00 34.35  ? 53  PHE B O   1 
ATOM   2518 C  CB  . PHE B 1 53  ? -20.972 33.328  34.295  1.00 32.88  ? 53  PHE B CB  1 
ATOM   2519 C  CG  . PHE B 1 53  ? -22.413 33.709  33.984  1.00 30.28  ? 53  PHE B CG  1 
ATOM   2520 C  CD1 . PHE B 1 53  ? -22.751 35.051  33.702  1.00 29.04  ? 53  PHE B CD1 1 
ATOM   2521 C  CD2 . PHE B 1 53  ? -23.422 32.736  33.977  1.00 28.05  ? 53  PHE B CD2 1 
ATOM   2522 C  CE1 . PHE B 1 53  ? -24.079 35.408  33.388  1.00 26.45  ? 53  PHE B CE1 1 
ATOM   2523 C  CE2 . PHE B 1 53  ? -24.736 33.084  33.696  1.00 25.64  ? 53  PHE B CE2 1 
ATOM   2524 C  CZ  . PHE B 1 53  ? -25.057 34.433  33.379  1.00 25.52  ? 53  PHE B CZ  1 
ATOM   2525 N  N   . PHE B 1 54  ? -19.456 31.121  35.937  1.00 39.03  ? 54  PHE B N   1 
ATOM   2526 C  CA  . PHE B 1 54  ? -18.262 30.327  35.945  1.00 41.94  ? 54  PHE B CA  1 
ATOM   2527 C  C   . PHE B 1 54  ? -18.218 29.533  34.666  1.00 42.36  ? 54  PHE B C   1 
ATOM   2528 O  O   . PHE B 1 54  ? -19.230 28.996  34.211  1.00 47.14  ? 54  PHE B O   1 
ATOM   2529 C  CB  . PHE B 1 54  ? -18.214 29.438  37.190  1.00 41.34  ? 54  PHE B CB  1 
ATOM   2530 C  CG  . PHE B 1 54  ? -17.827 30.196  38.420  1.00 46.18  ? 54  PHE B CG  1 
ATOM   2531 C  CD1 . PHE B 1 54  ? -16.484 30.356  38.757  1.00 47.18  ? 54  PHE B CD1 1 
ATOM   2532 C  CD2 . PHE B 1 54  ? -18.794 30.815  39.196  1.00 48.24  ? 54  PHE B CD2 1 
ATOM   2533 C  CE1 . PHE B 1 54  ? -16.122 31.093  39.861  1.00 48.10  ? 54  PHE B CE1 1 
ATOM   2534 C  CE2 . PHE B 1 54  ? -18.445 31.548  40.306  1.00 51.35  ? 54  PHE B CE2 1 
ATOM   2535 C  CZ  . PHE B 1 54  ? -17.106 31.696  40.629  1.00 50.61  ? 54  PHE B CZ  1 
ATOM   2536 N  N   . PHE B 1 55  ? -17.035 29.456  34.089  1.00 42.22  ? 55  PHE B N   1 
ATOM   2537 C  CA  . PHE B 1 55  ? -16.867 28.714  32.858  1.00 39.15  ? 55  PHE B CA  1 
ATOM   2538 C  C   . PHE B 1 55  ? -16.056 27.452  33.044  1.00 37.38  ? 55  PHE B C   1 
ATOM   2539 O  O   . PHE B 1 55  ? -15.049 27.449  33.744  1.00 37.10  ? 55  PHE B O   1 
ATOM   2540 C  CB  . PHE B 1 55  ? -16.251 29.605  31.788  1.00 34.57  ? 55  PHE B CB  1 
ATOM   2541 C  CG  . PHE B 1 55  ? -17.065 30.821  31.491  1.00 34.88  ? 55  PHE B CG  1 
ATOM   2542 C  CD1 . PHE B 1 55  ? -18.152 30.752  30.617  1.00 32.53  ? 55  PHE B CD1 1 
ATOM   2543 C  CD2 . PHE B 1 55  ? -16.762 32.048  32.105  1.00 34.85  ? 55  PHE B CD2 1 
ATOM   2544 C  CE1 . PHE B 1 55  ? -18.911 31.876  30.353  1.00 32.56  ? 55  PHE B CE1 1 
ATOM   2545 C  CE2 . PHE B 1 55  ? -17.513 33.173  31.835  1.00 33.59  ? 55  PHE B CE2 1 
ATOM   2546 C  CZ  . PHE B 1 55  ? -18.590 33.085  30.956  1.00 37.09  ? 55  PHE B CZ  1 
ATOM   2547 N  N   . SER B 1 56  ? -16.521 26.382  32.406  1.00 38.42  ? 56  SER B N   1 
ATOM   2548 C  CA  . SER B 1 56  ? -15.761 25.139  32.264  1.00 38.83  ? 56  SER B CA  1 
ATOM   2549 C  C   . SER B 1 56  ? -15.690 24.775  30.775  1.00 39.35  ? 56  SER B C   1 
ATOM   2550 O  O   . SER B 1 56  ? -16.711 24.730  30.067  1.00 40.32  ? 56  SER B O   1 
ATOM   2551 C  CB  . SER B 1 56  ? -16.402 24.031  33.097  1.00 38.67  ? 56  SER B CB  1 
ATOM   2552 O  OG  . SER B 1 56  ? -15.967 22.728  32.734  1.00 40.30  ? 56  SER B OG  1 
ATOM   2553 N  N   . GLY B 1 57  ? -14.473 24.549  30.295  1.00 36.56  ? 57  GLY B N   1 
ATOM   2554 C  CA  . GLY B 1 57  ? -14.271 24.103  28.917  1.00 37.59  ? 57  GLY B CA  1 
ATOM   2555 C  C   . GLY B 1 57  ? -14.118 25.253  27.948  1.00 37.80  ? 57  GLY B C   1 
ATOM   2556 O  O   . GLY B 1 57  ? -13.713 25.047  26.800  1.00 40.95  ? 57  GLY B O   1 
ATOM   2557 N  N   . TYR B 1 58  ? -14.433 26.462  28.404  1.00 31.75  ? 58  TYR B N   1 
ATOM   2558 C  CA  . TYR B 1 58  ? -14.422 27.637  27.548  1.00 33.45  ? 58  TYR B CA  1 
ATOM   2559 C  C   . TYR B 1 58  ? -13.024 28.005  27.104  1.00 33.49  ? 58  TYR B C   1 
ATOM   2560 O  O   . TYR B 1 58  ? -12.865 28.713  26.119  1.00 38.07  ? 58  TYR B O   1 
ATOM   2561 C  CB  . TYR B 1 58  ? -15.091 28.826  28.264  1.00 32.78  ? 58  TYR B CB  1 
ATOM   2562 C  CG  . TYR B 1 58  ? -16.577 28.983  27.985  1.00 33.54  ? 58  TYR B CG  1 
ATOM   2563 C  CD1 . TYR B 1 58  ? -17.502 28.031  28.425  1.00 34.71  ? 58  TYR B CD1 1 
ATOM   2564 C  CD2 . TYR B 1 58  ? -17.063 30.118  27.305  1.00 34.27  ? 58  TYR B CD2 1 
ATOM   2565 C  CE1 . TYR B 1 58  ? -18.853 28.183  28.165  1.00 37.17  ? 58  TYR B CE1 1 
ATOM   2566 C  CE2 . TYR B 1 58  ? -18.417 30.272  27.029  1.00 34.59  ? 58  TYR B CE2 1 
ATOM   2567 C  CZ  . TYR B 1 58  ? -19.300 29.303  27.457  1.00 35.48  ? 58  TYR B CZ  1 
ATOM   2568 O  OH  . TYR B 1 58  ? -20.631 29.460  27.202  1.00 35.08  ? 58  TYR B OH  1 
ATOM   2569 N  N   . ASP B 1 59  ? -12.017 27.533  27.847  1.00 40.16  ? 59  ASP B N   1 
ATOM   2570 C  CA  . ASP B 1 59  ? -10.599 27.744  27.526  1.00 40.80  ? 59  ASP B CA  1 
ATOM   2571 C  C   . ASP B 1 59  ? -9.950  26.732  26.587  1.00 45.90  ? 59  ASP B C   1 
ATOM   2572 O  O   . ASP B 1 59  ? -8.982  27.060  25.902  1.00 47.21  ? 59  ASP B O   1 
ATOM   2573 C  CB  . ASP B 1 59  ? -9.756  27.827  28.795  1.00 44.47  ? 59  ASP B CB  1 
ATOM   2574 C  CG  . ASP B 1 59  ? -10.017 26.677  29.767  1.00 50.11  ? 59  ASP B CG  1 
ATOM   2575 O  OD1 . ASP B 1 59  ? -10.634 25.630  29.408  1.00 43.50  ? 59  ASP B OD1 1 
ATOM   2576 O  OD2 . ASP B 1 59  ? -9.603  26.858  30.935  1.00 52.60  ? 59  ASP B OD2 1 
ATOM   2577 N  N   . LYS B 1 60  ? -10.452 25.503  26.580  1.00 49.08  ? 60  LYS B N   1 
ATOM   2578 C  CA  . LYS B 1 60  ? -9.889  24.437  25.761  1.00 46.29  ? 60  LYS B CA  1 
ATOM   2579 C  C   . LYS B 1 60  ? -10.023 24.740  24.262  1.00 46.64  ? 60  LYS B C   1 
ATOM   2580 O  O   . LYS B 1 60  ? -11.123 25.046  23.771  1.00 42.80  ? 60  LYS B O   1 
ATOM   2581 C  CB  . LYS B 1 60  ? -10.588 23.129  26.104  1.00 48.68  ? 60  LYS B CB  1 
ATOM   2582 C  CG  . LYS B 1 60  ? -10.462 22.726  27.569  1.00 53.47  ? 60  LYS B CG  1 
ATOM   2583 C  CD  . LYS B 1 60  ? -11.211 21.431  27.903  1.00 51.82  ? 60  LYS B CD  1 
ATOM   2584 C  CE  . LYS B 1 60  ? -11.223 20.452  26.733  1.00 55.38  ? 60  LYS B CE  1 
ATOM   2585 N  NZ  . LYS B 1 60  ? -10.885 19.039  27.095  1.00 59.60  ? 60  LYS B NZ  1 
ATOM   2586 N  N   . LYS B 1 61  ? -8.901  24.674  23.539  1.00 50.26  ? 61  LYS B N   1 
ATOM   2587 C  CA  . LYS B 1 61  ? -8.871  24.850  22.074  1.00 45.63  ? 61  LYS B CA  1 
ATOM   2588 C  C   . LYS B 1 61  ? -9.572  23.683  21.334  1.00 43.50  ? 61  LYS B C   1 
ATOM   2589 O  O   . LYS B 1 61  ? -9.574  22.575  21.806  1.00 40.39  ? 61  LYS B O   1 
ATOM   2590 C  CB  . LYS B 1 61  ? -7.416  24.979  21.607  1.00 49.07  ? 61  LYS B CB  1 
ATOM   2591 C  CG  . LYS B 1 61  ? -6.722  26.284  21.965  1.00 50.92  ? 61  LYS B CG  1 
ATOM   2592 C  CD  . LYS B 1 61  ? -7.078  27.380  20.973  1.00 47.39  ? 61  LYS B CD  1 
ATOM   2593 C  CE  . LYS B 1 61  ? -6.447  28.713  21.336  1.00 45.48  ? 61  LYS B CE  1 
ATOM   2594 N  NZ  . LYS B 1 61  ? -6.884  29.706  20.303  1.00 44.27  ? 61  LYS B NZ  1 
ATOM   2595 N  N   . GLN B 1 62  ? -10.201 23.939  20.190  1.00 47.30  ? 62  GLN B N   1 
ATOM   2596 C  CA  . GLN B 1 62  ? -10.878 22.865  19.442  1.00 43.55  ? 62  GLN B CA  1 
ATOM   2597 C  C   . GLN B 1 62  ? -11.010 23.150  17.952  1.00 45.98  ? 62  GLN B C   1 
ATOM   2598 O  O   . GLN B 1 62  ? -10.594 24.198  17.459  1.00 44.85  ? 62  GLN B O   1 
ATOM   2599 C  CB  . GLN B 1 62  ? -12.249 22.548  20.023  1.00 42.15  ? 62  GLN B CB  1 
ATOM   2600 C  CG  . GLN B 1 62  ? -12.305 21.225  20.801  1.00 51.70  ? 62  GLN B CG  1 
ATOM   2601 C  CD  . GLN B 1 62  ? -12.871 21.462  22.184  1.00 53.95  ? 62  GLN B CD  1 
ATOM   2602 O  OE1 . GLN B 1 62  ? -12.950 20.563  23.040  1.00 48.39  ? 62  GLN B OE1 1 
ATOM   2603 N  NE2 . GLN B 1 62  ? -13.256 22.714  22.421  1.00 49.59  ? 62  GLN B NE2 1 
ATOM   2604 N  N   . THR B 1 63  ? -11.592 22.193  17.243  1.00 40.64  ? 63  THR B N   1 
ATOM   2605 C  CA  . THR B 1 63  ? -11.893 22.374  15.866  1.00 35.93  ? 63  THR B CA  1 
ATOM   2606 C  C   . THR B 1 63  ? -13.403 22.210  15.761  1.00 37.35  ? 63  THR B C   1 
ATOM   2607 O  O   . THR B 1 63  ? -13.926 21.115  15.556  1.00 34.38  ? 63  THR B O   1 
ATOM   2608 C  CB  . THR B 1 63  ? -11.133 21.352  14.999  1.00 39.96  ? 63  THR B CB  1 
ATOM   2609 O  OG1 . THR B 1 63  ? -11.309 20.043  15.547  1.00 34.09  ? 63  THR B OG1 1 
ATOM   2610 C  CG2 . THR B 1 63  ? -9.638  21.711  14.955  1.00 36.17  ? 63  THR B CG2 1 
ATOM   2611 N  N   . TRP B 1 64  ? -14.100 23.324  15.932  1.00 34.01  ? 64  TRP B N   1 
ATOM   2612 C  CA  . TRP B 1 64  ? -15.528 23.331  15.898  1.00 31.90  ? 64  TRP B CA  1 
ATOM   2613 C  C   . TRP B 1 64  ? -16.050 23.131  14.522  1.00 33.32  ? 64  TRP B C   1 
ATOM   2614 O  O   . TRP B 1 64  ? -15.508 23.667  13.533  1.00 33.48  ? 64  TRP B O   1 
ATOM   2615 C  CB  . TRP B 1 64  ? -16.037 24.672  16.412  1.00 30.39  ? 64  TRP B CB  1 
ATOM   2616 C  CG  . TRP B 1 64  ? -15.611 25.043  17.819  1.00 28.36  ? 64  TRP B CG  1 
ATOM   2617 C  CD1 . TRP B 1 64  ? -14.779 26.093  18.200  1.00 29.41  ? 64  TRP B CD1 1 
ATOM   2618 C  CD2 . TRP B 1 64  ? -16.004 24.396  19.085  1.00 29.40  ? 64  TRP B CD2 1 
ATOM   2619 N  NE1 . TRP B 1 64  ? -14.626 26.130  19.563  1.00 29.68  ? 64  TRP B NE1 1 
ATOM   2620 C  CE2 . TRP B 1 64  ? -15.332 25.143  20.153  1.00 29.21  ? 64  TRP B CE2 1 
ATOM   2621 C  CE3 . TRP B 1 64  ? -16.804 23.315  19.424  1.00 29.57  ? 64  TRP B CE3 1 
ATOM   2622 C  CZ2 . TRP B 1 64  ? -15.471 24.804  21.487  1.00 27.84  ? 64  TRP B CZ2 1 
ATOM   2623 C  CZ3 . TRP B 1 64  ? -16.936 22.984  20.776  1.00 28.93  ? 64  TRP B CZ3 1 
ATOM   2624 C  CH2 . TRP B 1 64  ? -16.285 23.712  21.779  1.00 30.38  ? 64  TRP B CH2 1 
ATOM   2625 N  N   . THR B 1 65  ? -17.133 22.372  14.448  1.00 33.26  ? 65  THR B N   1 
ATOM   2626 C  CA  . THR B 1 65  ? -17.979 22.314  13.248  1.00 34.83  ? 65  THR B CA  1 
ATOM   2627 C  C   . THR B 1 65  ? -18.968 23.494  13.190  1.00 37.34  ? 65  THR B C   1 
ATOM   2628 O  O   . THR B 1 65  ? -19.831 23.659  14.085  1.00 37.55  ? 65  THR B O   1 
ATOM   2629 C  CB  . THR B 1 65  ? -18.740 20.976  13.187  1.00 35.81  ? 65  THR B CB  1 
ATOM   2630 O  OG1 . THR B 1 65  ? -17.794 19.900  13.155  1.00 34.20  ? 65  THR B OG1 1 
ATOM   2631 C  CG2 . THR B 1 65  ? -19.626 20.900  11.959  1.00 37.55  ? 65  THR B CG2 1 
ATOM   2632 N  N   . VAL B 1 66  ? -18.837 24.288  12.127  1.00 32.68  ? 66  VAL B N   1 
ATOM   2633 C  CA  . VAL B 1 66  ? -19.727 25.424  11.840  1.00 32.08  ? 66  VAL B CA  1 
ATOM   2634 C  C   . VAL B 1 66  ? -20.592 25.227  10.567  1.00 36.32  ? 66  VAL B C   1 
ATOM   2635 O  O   . VAL B 1 66  ? -20.101 24.793  9.499   1.00 33.59  ? 66  VAL B O   1 
ATOM   2636 C  CB  . VAL B 1 66  ? -18.931 26.756  11.829  1.00 31.07  ? 66  VAL B CB  1 
ATOM   2637 C  CG1 . VAL B 1 66  ? -17.761 26.732  10.828  1.00 29.67  ? 66  VAL B CG1 1 
ATOM   2638 C  CG2 . VAL B 1 66  ? -19.841 27.951  11.605  1.00 28.32  ? 66  VAL B CG2 1 
ATOM   2639 N  N   . GLN B 1 67  ? -21.890 25.513  10.691  1.00 35.56  ? 67  GLN B N   1 
ATOM   2640 C  CA  . GLN B 1 67  ? -22.838 25.310  9.578   1.00 35.85  ? 67  GLN B CA  1 
ATOM   2641 C  C   . GLN B 1 67  ? -23.638 26.549  9.209   1.00 37.15  ? 67  GLN B C   1 
ATOM   2642 O  O   . GLN B 1 67  ? -23.963 27.359  10.088  1.00 31.91  ? 67  GLN B O   1 
ATOM   2643 C  CB  . GLN B 1 67  ? -23.830 24.233  9.947   1.00 36.02  ? 67  GLN B CB  1 
ATOM   2644 C  CG  . GLN B 1 67  ? -23.174 22.873  10.156  1.00 41.88  ? 67  GLN B CG  1 
ATOM   2645 C  CD  . GLN B 1 67  ? -24.126 21.828  10.699  1.00 39.06  ? 67  GLN B CD  1 
ATOM   2646 O  OE1 . GLN B 1 67  ? -23.876 20.637  10.565  1.00 46.70  ? 67  GLN B OE1 1 
ATOM   2647 N  NE2 . GLN B 1 67  ? -25.219 22.262  11.290  1.00 37.07  ? 67  GLN B NE2 1 
ATOM   2648 N  N   . ASN B 1 68  ? -23.948 26.666  7.920   1.00 31.62  ? 68  ASN B N   1 
ATOM   2649 C  CA  . ASN B 1 68  ? -24.978 27.547  7.388   1.00 32.73  ? 68  ASN B CA  1 
ATOM   2650 C  C   . ASN B 1 68  ? -26.298 26.778  7.306   1.00 36.01  ? 68  ASN B C   1 
ATOM   2651 O  O   . ASN B 1 68  ? -26.470 25.919  6.451   1.00 38.17  ? 68  ASN B O   1 
ATOM   2652 C  CB  . ASN B 1 68  ? -24.578 28.005  5.994   1.00 31.92  ? 68  ASN B CB  1 
ATOM   2653 C  CG  . ASN B 1 68  ? -25.653 28.810  5.300   1.00 37.02  ? 68  ASN B CG  1 
ATOM   2654 O  OD1 . ASN B 1 68  ? -26.832 28.723  5.657   1.00 30.24  ? 68  ASN B OD1 1 
ATOM   2655 N  ND2 . ASN B 1 68  ? -25.248 29.606  4.275   1.00 33.82  ? 68  ASN B ND2 1 
ATOM   2656 N  N   . ASN B 1 69  ? -27.233 27.086  8.191   1.00 32.66  ? 69  ASN B N   1 
ATOM   2657 C  CA  . ASN B 1 69  ? -28.475 26.332  8.277   1.00 32.92  ? 69  ASN B CA  1 
ATOM   2658 C  C   . ASN B 1 69  ? -29.649 27.009  7.556   1.00 31.89  ? 69  ASN B C   1 
ATOM   2659 O  O   . ASN B 1 69  ? -30.804 26.690  7.816   1.00 35.11  ? 69  ASN B O   1 
ATOM   2660 C  CB  . ASN B 1 69  ? -28.830 26.083  9.741   1.00 30.16  ? 69  ASN B CB  1 
ATOM   2661 C  CG  . ASN B 1 69  ? -29.325 27.337  10.446  1.00 34.86  ? 69  ASN B CG  1 
ATOM   2662 O  OD1 . ASN B 1 69  ? -29.301 28.437  9.883   1.00 38.19  ? 69  ASN B OD1 1 
ATOM   2663 N  ND2 . ASN B 1 69  ? -29.822 27.174  11.667  1.00 32.15  ? 69  ASN B ND2 1 
ATOM   2664 N  N   . GLY B 1 70  ? -29.358 27.979  6.700   1.00 30.00  ? 70  GLY B N   1 
ATOM   2665 C  CA  . GLY B 1 70  ? -30.422 28.742  6.041   1.00 33.40  ? 70  GLY B CA  1 
ATOM   2666 C  C   . GLY B 1 70  ? -31.091 29.881  6.812   1.00 36.67  ? 70  GLY B C   1 
ATOM   2667 O  O   . GLY B 1 70  ? -31.874 30.662  6.225   1.00 32.63  ? 70  GLY B O   1 
ATOM   2668 N  N   . HIS B 1 71  ? -30.794 29.982  8.113   1.00 34.76  ? 71  HIS B N   1 
ATOM   2669 C  CA  . HIS B 1 71  ? -31.346 31.055  8.952   1.00 32.04  ? 71  HIS B CA  1 
ATOM   2670 C  C   . HIS B 1 71  ? -30.287 31.764  9.697   1.00 31.86  ? 71  HIS B C   1 
ATOM   2671 O  O   . HIS B 1 71  ? -30.516 32.879  10.215  1.00 33.95  ? 71  HIS B O   1 
ATOM   2672 C  CB  . HIS B 1 71  ? -32.360 30.512  9.937   1.00 33.96  ? 71  HIS B CB  1 
ATOM   2673 C  CG  . HIS B 1 71  ? -33.507 29.845  9.269   1.00 36.45  ? 71  HIS B CG  1 
ATOM   2674 N  ND1 . HIS B 1 71  ? -34.528 30.525  8.772   1.00 39.78  ? 71  HIS B ND1 1 
ATOM   2675 C  CD2 . HIS B 1 71  ? -33.736 28.515  8.976   1.00 44.18  ? 71  HIS B CD2 1 
ATOM   2676 C  CE1 . HIS B 1 71  ? -35.389 29.687  8.195   1.00 41.73  ? 71  HIS B CE1 1 
ATOM   2677 N  NE2 . HIS B 1 71  ? -34.904 28.446  8.327   1.00 45.75  ? 71  HIS B NE2 1 
ATOM   2678 N  N   . SER B 1 72  ? -29.126 31.107  9.791   1.00 32.13  ? 72  SER B N   1 
ATOM   2679 C  CA  . SER B 1 72  ? -27.986 31.619  10.514  1.00 29.71  ? 72  SER B CA  1 
ATOM   2680 C  C   . SER B 1 72  ? -26.716 30.829  10.197  1.00 32.04  ? 72  SER B C   1 
ATOM   2681 O  O   . SER B 1 72  ? -26.754 29.779  9.557   1.00 32.76  ? 72  SER B O   1 
ATOM   2682 C  CB  . SER B 1 72  ? -28.215 31.506  12.027  1.00 26.82  ? 72  SER B CB  1 
ATOM   2683 O  OG  . SER B 1 72  ? -27.224 32.269  12.692  1.00 24.38  ? 72  SER B OG  1 
ATOM   2684 N  N   . VAL B 1 73  ? -25.594 31.324  10.715  1.00 29.29  ? 73  VAL B N   1 
ATOM   2685 C  CA  . VAL B 1 73  ? -24.394 30.493  10.890  1.00 29.50  ? 73  VAL B CA  1 
ATOM   2686 C  C   . VAL B 1 73  ? -24.321 29.927  12.325  1.00 30.69  ? 73  VAL B C   1 
ATOM   2687 O  O   . VAL B 1 73  ? -24.575 30.656  13.294  1.00 30.07  ? 73  VAL B O   1 
ATOM   2688 C  CB  . VAL B 1 73  ? -23.113 31.244  10.469  1.00 29.56  ? 73  VAL B CB  1 
ATOM   2689 C  CG1 . VAL B 1 73  ? -22.862 32.507  11.299  1.00 28.52  ? 73  VAL B CG1 1 
ATOM   2690 C  CG2 . VAL B 1 73  ? -21.920 30.321  10.554  1.00 31.62  ? 73  VAL B CG2 1 
ATOM   2691 N  N   . MET B 1 74  ? -24.033 28.627  12.446  1.00 28.51  ? 74  MET B N   1 
ATOM   2692 C  CA  . MET B 1 74  ? -24.056 27.933  13.704  1.00 27.62  ? 74  MET B CA  1 
ATOM   2693 C  C   . MET B 1 74  ? -22.863 27.029  13.997  1.00 29.35  ? 74  MET B C   1 
ATOM   2694 O  O   . MET B 1 74  ? -22.586 26.073  13.250  1.00 28.74  ? 74  MET B O   1 
ATOM   2695 C  CB  . MET B 1 74  ? -25.310 27.090  13.792  1.00 31.92  ? 74  MET B CB  1 
ATOM   2696 C  CG  . MET B 1 74  ? -25.465 26.449  15.146  1.00 32.15  ? 74  MET B CG  1 
ATOM   2697 S  SD  . MET B 1 74  ? -26.953 25.455  15.293  1.00 42.39  ? 74  MET B SD  1 
ATOM   2698 C  CE  . MET B 1 74  ? -28.207 26.473  14.510  1.00 44.31  ? 74  MET B CE  1 
ATOM   2699 N  N   . MET B 1 75  ? -22.180 27.303  15.104  1.00 26.74  ? 75  MET B N   1 
ATOM   2700 C  CA  . MET B 1 75  ? -21.187 26.373  15.614  1.00 29.75  ? 75  MET B CA  1 
ATOM   2701 C  C   . MET B 1 75  ? -21.849 25.338  16.503  1.00 30.64  ? 75  MET B C   1 
ATOM   2702 O  O   . MET B 1 75  ? -22.605 25.679  17.418  1.00 33.50  ? 75  MET B O   1 
ATOM   2703 C  CB  . MET B 1 75  ? -20.079 27.060  16.411  1.00 27.21  ? 75  MET B CB  1 
ATOM   2704 C  CG  . MET B 1 75  ? -19.286 28.107  15.653  1.00 29.67  ? 75  MET B CG  1 
ATOM   2705 S  SD  . MET B 1 75  ? -18.352 29.178  16.784  1.00 33.87  ? 75  MET B SD  1 
ATOM   2706 C  CE  . MET B 1 75  ? -17.450 27.992  17.738  1.00 30.00  ? 75  MET B CE  1 
ATOM   2707 N  N   . LEU B 1 76  ? -21.522 24.075  16.268  1.00 29.41  ? 76  LEU B N   1 
ATOM   2708 C  CA  . LEU B 1 76  ? -22.011 22.991  17.086  1.00 28.86  ? 76  LEU B CA  1 
ATOM   2709 C  C   . LEU B 1 76  ? -21.103 22.812  18.281  1.00 30.71  ? 76  LEU B C   1 
ATOM   2710 O  O   . LEU B 1 76  ? -19.894 22.587  18.113  1.00 28.15  ? 76  LEU B O   1 
ATOM   2711 C  CB  . LEU B 1 76  ? -22.042 21.715  16.245  1.00 28.79  ? 76  LEU B CB  1 
ATOM   2712 C  CG  . LEU B 1 76  ? -22.957 21.753  15.025  1.00 29.95  ? 76  LEU B CG  1 
ATOM   2713 C  CD1 . LEU B 1 76  ? -22.803 20.464  14.242  1.00 35.18  ? 76  LEU B CD1 1 
ATOM   2714 C  CD2 . LEU B 1 76  ? -24.426 21.914  15.452  1.00 37.22  ? 76  LEU B CD2 1 
ATOM   2715 N  N   . LEU B 1 77  ? -21.666 22.887  19.501  1.00 29.22  ? 77  LEU B N   1 
ATOM   2716 C  CA  . LEU B 1 77  ? -20.833 22.767  20.715  1.00 27.32  ? 77  LEU B CA  1 
ATOM   2717 C  C   . LEU B 1 77  ? -20.794 21.372  21.383  1.00 26.98  ? 77  LEU B C   1 
ATOM   2718 O  O   . LEU B 1 77  ? -20.002 21.121  22.289  1.00 25.22  ? 77  LEU B O   1 
ATOM   2719 C  CB  . LEU B 1 77  ? -21.201 23.859  21.726  1.00 26.40  ? 77  LEU B CB  1 
ATOM   2720 C  CG  . LEU B 1 77  ? -21.062 25.294  21.185  1.00 24.99  ? 77  LEU B CG  1 
ATOM   2721 C  CD1 . LEU B 1 77  ? -21.317 26.317  22.298  1.00 25.81  ? 77  LEU B CD1 1 
ATOM   2722 C  CD2 . LEU B 1 77  ? -19.735 25.572  20.492  1.00 25.77  ? 77  LEU B CD2 1 
ATOM   2723 N  N   . GLU B 1 78  ? -21.699 20.494  20.986  1.00 31.96  ? 78  GLU B N   1 
ATOM   2724 C  CA  . GLU B 1 78  ? -21.580 19.077  21.328  1.00 32.39  ? 78  GLU B CA  1 
ATOM   2725 C  C   . GLU B 1 78  ? -21.161 18.841  22.758  1.00 35.45  ? 78  GLU B C   1 
ATOM   2726 O  O   . GLU B 1 78  ? -20.189 18.095  23.011  1.00 39.08  ? 78  GLU B O   1 
ATOM   2727 C  CB  . GLU B 1 78  ? -20.563 18.435  20.381  1.00 33.84  ? 78  GLU B CB  1 
ATOM   2728 C  CG  . GLU B 1 78  ? -21.173 18.055  19.041  1.00 36.38  ? 78  GLU B CG  1 
ATOM   2729 C  CD  . GLU B 1 78  ? -20.155 17.982  17.923  1.00 42.08  ? 78  GLU B CD  1 
ATOM   2730 O  OE1 . GLU B 1 78  ? -18.950 18.034  18.206  1.00 39.87  ? 78  GLU B OE1 1 
ATOM   2731 O  OE2 . GLU B 1 78  ? -20.567 17.892  16.741  1.00 48.92  ? 78  GLU B OE2 1 
ATOM   2732 N  N   . ASN B 1 79  ? -21.870 19.486  23.692  1.00 35.93  ? 79  ASN B N   1 
ATOM   2733 C  CA  . ASN B 1 79  ? -21.592 19.387  25.142  1.00 33.09  ? 79  ASN B CA  1 
ATOM   2734 C  C   . ASN B 1 79  ? -20.153 19.635  25.607  1.00 35.21  ? 79  ASN B C   1 
ATOM   2735 O  O   . ASN B 1 79  ? -19.791 19.296  26.757  1.00 33.83  ? 79  ASN B O   1 
ATOM   2736 C  CB  . ASN B 1 79  ? -22.002 18.010  25.677  1.00 37.91  ? 79  ASN B CB  1 
ATOM   2737 C  CG  . ASN B 1 79  ? -23.480 17.782  25.636  1.00 36.65  ? 79  ASN B CG  1 
ATOM   2738 O  OD1 . ASN B 1 79  ? -24.258 18.687  25.363  1.00 35.33  ? 79  ASN B OD1 1 
ATOM   2739 N  ND2 . ASN B 1 79  ? -23.885 16.559  25.918  1.00 43.47  ? 79  ASN B ND2 1 
ATOM   2740 N  N   . LYS B 1 80  ? -19.308 20.194  24.755  1.00 32.75  ? 80  LYS B N   1 
ATOM   2741 C  CA  . LYS B 1 80  ? -17.889 20.282  25.137  1.00 33.53  ? 80  LYS B CA  1 
ATOM   2742 C  C   . LYS B 1 80  ? -17.547 21.410  26.139  1.00 36.73  ? 80  LYS B C   1 
ATOM   2743 O  O   . LYS B 1 80  ? -16.362 21.682  26.406  1.00 36.09  ? 80  LYS B O   1 
ATOM   2744 C  CB  . LYS B 1 80  ? -17.017 20.380  23.893  1.00 33.99  ? 80  LYS B CB  1 
ATOM   2745 C  CG  . LYS B 1 80  ? -16.899 19.070  23.112  1.00 33.17  ? 80  LYS B CG  1 
ATOM   2746 C  CD  . LYS B 1 80  ? -16.167 19.274  21.781  1.00 33.84  ? 80  LYS B CD  1 
ATOM   2747 C  CE  . LYS B 1 80  ? -16.129 17.958  20.996  1.00 40.67  ? 80  LYS B CE  1 
ATOM   2748 N  NZ  . LYS B 1 80  ? -15.490 18.093  19.644  1.00 42.00  ? 80  LYS B NZ  1 
ATOM   2749 N  N   . ALA B 1 81  ? -18.571 22.071  26.690  1.00 35.17  ? 81  ALA B N   1 
ATOM   2750 C  CA  . ALA B 1 81  ? -18.350 23.176  27.631  1.00 28.87  ? 81  ALA B CA  1 
ATOM   2751 C  C   . ALA B 1 81  ? -19.591 23.373  28.459  1.00 31.36  ? 81  ALA B C   1 
ATOM   2752 O  O   . ALA B 1 81  ? -20.664 22.877  28.090  1.00 33.46  ? 81  ALA B O   1 
ATOM   2753 C  CB  . ALA B 1 81  ? -18.035 24.428  26.880  1.00 27.40  ? 81  ALA B CB  1 
ATOM   2754 N  N   . SER B 1 82  ? -19.455 24.078  29.582  1.00 31.53  ? 82  SER B N   1 
ATOM   2755 C  CA  . SER B 1 82  ? -20.615 24.400  30.426  1.00 31.29  ? 82  SER B CA  1 
ATOM   2756 C  C   . SER B 1 82  ? -20.481 25.692  31.213  1.00 29.93  ? 82  SER B C   1 
ATOM   2757 O  O   . SER B 1 82  ? -19.419 26.283  31.270  1.00 28.21  ? 82  SER B O   1 
ATOM   2758 C  CB  . SER B 1 82  ? -20.863 23.271  31.399  1.00 28.59  ? 82  SER B CB  1 
ATOM   2759 O  OG  . SER B 1 82  ? -19.646 23.029  32.057  1.00 34.65  ? 82  SER B OG  1 
ATOM   2760 N  N   . ILE B 1 83  ? -21.560 26.118  31.865  1.00 28.12  ? 83  ILE B N   1 
ATOM   2761 C  CA  . ILE B 1 83  ? -21.478 27.318  32.669  1.00 30.43  ? 83  ILE B CA  1 
ATOM   2762 C  C   . ILE B 1 83  ? -22.192 27.053  33.988  1.00 32.36  ? 83  ILE B C   1 
ATOM   2763 O  O   . ILE B 1 83  ? -22.976 26.121  34.081  1.00 29.94  ? 83  ILE B O   1 
ATOM   2764 C  CB  . ILE B 1 83  ? -22.098 28.562  31.964  1.00 28.13  ? 83  ILE B CB  1 
ATOM   2765 C  CG1 . ILE B 1 83  ? -23.615 28.376  31.780  1.00 29.47  ? 83  ILE B CG1 1 
ATOM   2766 C  CG2 . ILE B 1 83  ? -21.398 28.854  30.628  1.00 28.09  ? 83  ILE B CG2 1 
ATOM   2767 C  CD1 . ILE B 1 83  ? -24.235 29.479  30.959  1.00 31.27  ? 83  ILE B CD1 1 
ATOM   2768 N  N   . SER B 1 84  ? -21.899 27.872  34.996  1.00 33.30  ? 84  SER B N   1 
ATOM   2769 C  CA  . SER B 1 84  ? -22.580 27.765  36.282  1.00 36.84  ? 84  SER B CA  1 
ATOM   2770 C  C   . SER B 1 84  ? -22.507 29.123  36.931  1.00 38.45  ? 84  SER B C   1 
ATOM   2771 O  O   . SER B 1 84  ? -21.810 30.013  36.428  1.00 34.10  ? 84  SER B O   1 
ATOM   2772 C  CB  . SER B 1 84  ? -21.928 26.721  37.181  1.00 37.66  ? 84  SER B CB  1 
ATOM   2773 O  OG  . SER B 1 84  ? -20.614 27.131  37.514  1.00 48.15  ? 84  SER B OG  1 
ATOM   2774 N  N   . GLY B 1 85  ? -23.229 29.280  38.036  1.00 36.06  ? 85  GLY B N   1 
ATOM   2775 C  CA  . GLY B 1 85  ? -23.230 30.543  38.738  1.00 37.62  ? 85  GLY B CA  1 
ATOM   2776 C  C   . GLY B 1 85  ? -24.167 31.509  38.073  1.00 44.77  ? 85  GLY B C   1 
ATOM   2777 O  O   . GLY B 1 85  ? -25.282 31.144  37.686  1.00 45.46  ? 85  GLY B O   1 
ATOM   2778 N  N   . GLY B 1 86  ? -23.724 32.754  37.962  1.00 45.58  ? 86  GLY B N   1 
ATOM   2779 C  CA  . GLY B 1 86  ? -24.554 33.810  37.424  1.00 50.33  ? 86  GLY B CA  1 
ATOM   2780 C  C   . GLY B 1 86  ? -26.013 33.623  37.763  1.00 49.94  ? 86  GLY B C   1 
ATOM   2781 O  O   . GLY B 1 86  ? -26.862 33.662  36.875  1.00 56.45  ? 86  GLY B O   1 
ATOM   2782 N  N   . GLY B 1 87  ? -26.303 33.382  39.038  1.00 45.22  ? 87  GLY B N   1 
ATOM   2783 C  CA  . GLY B 1 87  ? -27.685 33.312  39.504  1.00 48.08  ? 87  GLY B CA  1 
ATOM   2784 C  C   . GLY B 1 87  ? -28.523 32.147  39.015  1.00 47.06  ? 87  GLY B C   1 
ATOM   2785 O  O   . GLY B 1 87  ? -29.704 32.062  39.338  1.00 50.54  ? 87  GLY B O   1 
ATOM   2786 N  N   . LEU B 1 88  ? -27.916 31.249  38.245  1.00 48.01  ? 88  LEU B N   1 
ATOM   2787 C  CA  . LEU B 1 88  ? -28.582 30.055  37.710  1.00 47.99  ? 88  LEU B CA  1 
ATOM   2788 C  C   . LEU B 1 88  ? -28.680 28.904  38.737  1.00 51.03  ? 88  LEU B C   1 
ATOM   2789 O  O   . LEU B 1 88  ? -27.828 28.795  39.644  1.00 51.74  ? 88  LEU B O   1 
ATOM   2790 C  CB  . LEU B 1 88  ? -27.846 29.562  36.445  1.00 49.10  ? 88  LEU B CB  1 
ATOM   2791 C  CG  . LEU B 1 88  ? -27.962 30.402  35.161  1.00 46.75  ? 88  LEU B CG  1 
ATOM   2792 C  CD1 . LEU B 1 88  ? -27.144 29.788  34.038  1.00 42.81  ? 88  LEU B CD1 1 
ATOM   2793 C  CD2 . LEU B 1 88  ? -29.413 30.592  34.733  1.00 47.15  ? 88  LEU B CD2 1 
ATOM   2794 N  N   . PRO B 1 89  ? -29.708 28.040  38.593  1.00 47.96  ? 89  PRO B N   1 
ATOM   2795 C  CA  . PRO B 1 89  ? -30.017 27.024  39.596  1.00 47.08  ? 89  PRO B CA  1 
ATOM   2796 C  C   . PRO B 1 89  ? -29.218 25.738  39.461  1.00 51.78  ? 89  PRO B C   1 
ATOM   2797 O  O   . PRO B 1 89  ? -29.316 24.879  40.342  1.00 53.41  ? 89  PRO B O   1 
ATOM   2798 C  CB  . PRO B 1 89  ? -31.495 26.720  39.322  1.00 47.96  ? 89  PRO B CB  1 
ATOM   2799 C  CG  . PRO B 1 89  ? -31.657 26.968  37.865  1.00 43.26  ? 89  PRO B CG  1 
ATOM   2800 C  CD  . PRO B 1 89  ? -30.773 28.135  37.578  1.00 45.84  ? 89  PRO B CD  1 
ATOM   2801 N  N   . ALA B 1 90  ? -28.458 25.598  38.370  1.00 46.90  ? 90  ALA B N   1 
ATOM   2802 C  CA  . ALA B 1 90  ? -27.760 24.358  38.059  1.00 41.65  ? 90  ALA B CA  1 
ATOM   2803 C  C   . ALA B 1 90  ? -26.686 24.593  36.991  1.00 40.51  ? 90  ALA B C   1 
ATOM   2804 O  O   . ALA B 1 90  ? -26.621 25.665  36.404  1.00 39.48  ? 90  ALA B O   1 
ATOM   2805 C  CB  . ALA B 1 90  ? -28.758 23.304  37.593  1.00 42.23  ? 90  ALA B CB  1 
ATOM   2806 N  N   . PRO B 1 91  ? -25.817 23.603  36.746  1.00 41.57  ? 91  PRO B N   1 
ATOM   2807 C  CA  . PRO B 1 91  ? -24.882 23.743  35.626  1.00 39.78  ? 91  PRO B CA  1 
ATOM   2808 C  C   . PRO B 1 91  ? -25.645 23.743  34.305  1.00 42.37  ? 91  PRO B C   1 
ATOM   2809 O  O   . PRO B 1 91  ? -26.826 23.418  34.312  1.00 43.45  ? 91  PRO B O   1 
ATOM   2810 C  CB  . PRO B 1 91  ? -24.048 22.469  35.732  1.00 41.24  ? 91  PRO B CB  1 
ATOM   2811 C  CG  . PRO B 1 91  ? -24.066 22.146  37.177  1.00 39.16  ? 91  PRO B CG  1 
ATOM   2812 C  CD  . PRO B 1 91  ? -25.476 22.447  37.590  1.00 41.23  ? 91  PRO B CD  1 
ATOM   2813 N  N   . TYR B 1 92  ? -24.989 24.100  33.191  1.00 38.86  ? 92  TYR B N   1 
ATOM   2814 C  CA  . TYR B 1 92  ? -25.640 24.100  31.883  1.00 33.30  ? 92  TYR B CA  1 
ATOM   2815 C  C   . TYR B 1 92  ? -24.652 23.763  30.770  1.00 33.10  ? 92  TYR B C   1 
ATOM   2816 O  O   . TYR B 1 92  ? -23.600 24.389  30.653  1.00 32.64  ? 92  TYR B O   1 
ATOM   2817 C  CB  . TYR B 1 92  ? -26.247 25.493  31.588  1.00 37.73  ? 92  TYR B CB  1 
ATOM   2818 C  CG  . TYR B 1 92  ? -27.603 25.771  32.179  1.00 36.51  ? 92  TYR B CG  1 
ATOM   2819 C  CD1 . TYR B 1 92  ? -27.734 26.214  33.489  1.00 37.64  ? 92  TYR B CD1 1 
ATOM   2820 C  CD2 . TYR B 1 92  ? -28.754 25.641  31.414  1.00 39.53  ? 92  TYR B CD2 1 
ATOM   2821 C  CE1 . TYR B 1 92  ? -28.976 26.485  34.035  1.00 37.96  ? 92  TYR B CE1 1 
ATOM   2822 C  CE2 . TYR B 1 92  ? -30.013 25.923  31.938  1.00 38.44  ? 92  TYR B CE2 1 
ATOM   2823 C  CZ  . TYR B 1 92  ? -30.112 26.319  33.258  1.00 40.69  ? 92  TYR B CZ  1 
ATOM   2824 O  OH  . TYR B 1 92  ? -31.336 26.598  33.785  1.00 34.70  ? 92  TYR B OH  1 
ATOM   2825 N  N   A GLN B 1 93  ? -24.985 22.770  29.949  0.50 34.44  ? 93  GLN B N   1 
ATOM   2826 N  N   B GLN B 1 93  ? -25.039 22.815  29.917  0.50 34.03  ? 93  GLN B N   1 
ATOM   2827 C  CA  A GLN B 1 93  ? -24.052 22.287  28.937  0.50 34.09  ? 93  GLN B CA  1 
ATOM   2828 C  CA  B GLN B 1 93  ? -24.164 22.253  28.894  0.50 33.78  ? 93  GLN B CA  1 
ATOM   2829 C  C   A GLN B 1 93  ? -24.212 23.099  27.655  0.50 32.70  ? 93  GLN B C   1 
ATOM   2830 C  C   B GLN B 1 93  ? -24.235 23.065  27.594  0.50 32.31  ? 93  GLN B C   1 
ATOM   2831 O  O   A GLN B 1 93  ? -25.323 23.352  27.189  0.50 31.17  ? 93  GLN B O   1 
ATOM   2832 O  O   B GLN B 1 93  ? -25.318 23.284  27.047  0.50 30.50  ? 93  GLN B O   1 
ATOM   2833 C  CB  A GLN B 1 93  ? -24.238 20.781  28.679  0.50 37.26  ? 93  GLN B CB  1 
ATOM   2834 C  CB  B GLN B 1 93  ? -24.541 20.778  28.652  0.50 36.27  ? 93  GLN B CB  1 
ATOM   2835 C  CG  A GLN B 1 93  ? -23.887 19.870  29.861  0.50 39.30  ? 93  GLN B CG  1 
ATOM   2836 C  CG  B GLN B 1 93  ? -23.825 19.778  29.568  0.50 38.81  ? 93  GLN B CG  1 
ATOM   2837 C  CD  A GLN B 1 93  ? -22.614 19.049  29.675  0.50 39.48  ? 93  GLN B CD  1 
ATOM   2838 C  CD  B GLN B 1 93  ? -24.671 18.568  29.934  0.50 39.39  ? 93  GLN B CD  1 
ATOM   2839 O  OE1 A GLN B 1 93  ? -22.595 17.864  29.990  0.50 40.86  ? 93  GLN B OE1 1 
ATOM   2840 O  OE1 B GLN B 1 93  ? -25.853 18.495  29.601  0.50 40.49  ? 93  GLN B OE1 1 
ATOM   2841 N  NE2 A GLN B 1 93  ? -21.547 19.674  29.178  0.50 39.59  ? 93  GLN B NE2 1 
ATOM   2842 N  NE2 B GLN B 1 93  ? -24.068 17.616  30.643  0.50 41.04  ? 93  GLN B NE2 1 
ATOM   2843 N  N   . ALA B 1 94  ? -23.086 23.519  27.105  1.00 30.39  ? 94  ALA B N   1 
ATOM   2844 C  CA  . ALA B 1 94  ? -23.063 24.307  25.886  1.00 28.20  ? 94  ALA B CA  1 
ATOM   2845 C  C   . ALA B 1 94  ? -23.510 23.432  24.706  1.00 28.96  ? 94  ALA B C   1 
ATOM   2846 O  O   . ALA B 1 94  ? -22.945 22.350  24.503  1.00 29.95  ? 94  ALA B O   1 
ATOM   2847 C  CB  . ALA B 1 94  ? -21.661 24.882  25.681  1.00 29.72  ? 94  ALA B CB  1 
ATOM   2848 N  N   . LYS B 1 95  ? -24.527 23.891  23.957  1.00 28.00  ? 95  LYS B N   1 
ATOM   2849 C  CA  . LYS B 1 95  ? -25.083 23.163  22.831  1.00 26.74  ? 95  LYS B CA  1 
ATOM   2850 C  C   . LYS B 1 95  ? -24.716 23.704  21.454  1.00 28.52  ? 95  LYS B C   1 
ATOM   2851 O  O   . LYS B 1 95  ? -24.319 22.922  20.562  1.00 26.59  ? 95  LYS B O   1 
ATOM   2852 C  CB  . LYS B 1 95  ? -26.616 23.090  22.907  1.00 30.98  ? 95  LYS B CB  1 
ATOM   2853 C  CG  . LYS B 1 95  ? -27.171 22.353  24.120  1.00 34.36  ? 95  LYS B CG  1 
ATOM   2854 C  CD  . LYS B 1 95  ? -26.658 20.938  24.185  1.00 37.27  ? 95  LYS B CD  1 
ATOM   2855 C  CE  . LYS B 1 95  ? -26.881 20.374  25.577  1.00 41.00  ? 95  LYS B CE  1 
ATOM   2856 N  NZ  . LYS B 1 95  ? -26.764 18.890  25.469  1.00 39.30  ? 95  LYS B NZ  1 
ATOM   2857 N  N   . GLN B 1 96  ? -24.922 25.013  21.241  1.00 24.49  ? 96  GLN B N   1 
ATOM   2858 C  CA  . GLN B 1 96  ? -24.494 25.637  19.983  1.00 23.83  ? 96  GLN B CA  1 
ATOM   2859 C  C   . GLN B 1 96  ? -24.244 27.129  20.228  1.00 23.28  ? 96  GLN B C   1 
ATOM   2860 O  O   . GLN B 1 96  ? -24.567 27.657  21.278  1.00 21.18  ? 96  GLN B O   1 
ATOM   2861 C  CB  . GLN B 1 96  ? -25.513 25.382  18.839  1.00 23.12  ? 96  GLN B CB  1 
ATOM   2862 C  CG  . GLN B 1 96  ? -26.997 25.461  19.245  1.00 25.56  ? 96  GLN B CG  1 
ATOM   2863 C  CD  . GLN B 1 96  ? -27.686 26.757  18.885  1.00 26.25  ? 96  GLN B CD  1 
ATOM   2864 O  OE1 . GLN B 1 96  ? -27.041 27.726  18.604  1.00 29.71  ? 96  GLN B OE1 1 
ATOM   2865 N  NE2 . GLN B 1 96  ? -29.026 26.752  18.852  1.00 30.60  ? 96  GLN B NE2 1 
ATOM   2866 N  N   . LEU B 1 97  ? -23.681 27.775  19.240  1.00 23.10  ? 97  LEU B N   1 
ATOM   2867 C  CA  . LEU B 1 97  ? -23.396 29.172  19.268  1.00 26.10  ? 97  LEU B CA  1 
ATOM   2868 C  C   . LEU B 1 97  ? -23.852 29.628  17.824  1.00 26.85  ? 97  LEU B C   1 
ATOM   2869 O  O   . LEU B 1 97  ? -23.496 28.939  16.844  1.00 22.07  ? 97  LEU B O   1 
ATOM   2870 C  CB  . LEU B 1 97  ? -21.906 29.419  19.461  1.00 23.81  ? 97  LEU B CB  1 
ATOM   2871 C  CG  . LEU B 1 97  ? -21.346 30.842  19.508  1.00 26.18  ? 97  LEU B CG  1 
ATOM   2872 C  CD1 . LEU B 1 97  ? -19.959 30.747  20.120  1.00 23.92  ? 97  LEU B CD1 1 
ATOM   2873 C  CD2 . LEU B 1 97  ? -21.265 31.457  18.117  1.00 24.80  ? 97  LEU B CD2 1 
ATOM   2874 N  N   . HIS B 1 98  ? -24.608 30.733  17.707  1.00 23.02  ? 98  HIS B N   1 
ATOM   2875 C  CA  . HIS B 1 98  ? -25.079 31.207  16.403  1.00 22.87  ? 98  HIS B CA  1 
ATOM   2876 C  C   . HIS B 1 98  ? -25.168 32.679  16.480  1.00 25.78  ? 98  HIS B C   1 
ATOM   2877 O  O   . HIS B 1 98  ? -25.121 33.237  17.607  1.00 24.88  ? 98  HIS B O   1 
ATOM   2878 C  CB  . HIS B 1 98  ? -26.444 30.600  16.005  1.00 22.93  ? 98  HIS B CB  1 
ATOM   2879 C  CG  . HIS B 1 98  ? -27.594 31.021  16.887  1.00 23.55  ? 98  HIS B CG  1 
ATOM   2880 N  ND1 . HIS B 1 98  ? -28.050 30.251  17.912  1.00 21.61  ? 98  HIS B ND1 1 
ATOM   2881 C  CD2 . HIS B 1 98  ? -28.392 32.187  16.879  1.00 23.36  ? 98  HIS B CD2 1 
ATOM   2882 C  CE1 . HIS B 1 98  ? -29.087 30.878  18.516  1.00 22.76  ? 98  HIS B CE1 1 
ATOM   2883 N  NE2 . HIS B 1 98  ? -29.281 32.069  17.903  1.00 26.63  ? 98  HIS B NE2 1 
ATOM   2884 N  N   . LEU B 1 99  ? -25.282 33.339  15.318  1.00 24.49  ? 99  LEU B N   1 
ATOM   2885 C  CA  . LEU B 1 99  ? -25.377 34.831  15.309  1.00 27.68  ? 99  LEU B CA  1 
ATOM   2886 C  C   . LEU B 1 99  ? -26.602 35.430  14.532  1.00 28.92  ? 99  LEU B C   1 
ATOM   2887 O  O   . LEU B 1 99  ? -27.273 34.715  13.777  1.00 31.99  ? 99  LEU B O   1 
ATOM   2888 C  CB  . LEU B 1 99  ? -24.040 35.477  14.894  1.00 26.64  ? 99  LEU B CB  1 
ATOM   2889 C  CG  . LEU B 1 99  ? -22.718 35.225  15.703  1.00 27.92  ? 99  LEU B CG  1 
ATOM   2890 C  CD1 . LEU B 1 99  ? -21.997 33.979  15.207  1.00 25.25  ? 99  LEU B CD1 1 
ATOM   2891 C  CD2 . LEU B 1 99  ? -21.723 36.378  15.685  1.00 26.23  ? 99  LEU B CD2 1 
ATOM   2892 N  N   . HIS B 1 100 ? -26.878 36.727  14.731  1.00 26.83  ? 100 HIS B N   1 
ATOM   2893 C  CA  . HIS B 1 100 ? -27.972 37.444  14.073  1.00 27.51  ? 100 HIS B CA  1 
ATOM   2894 C  C   . HIS B 1 100 ? -27.338 38.743  13.651  1.00 28.73  ? 100 HIS B C   1 
ATOM   2895 O  O   . HIS B 1 100 ? -26.533 39.247  14.367  1.00 30.25  ? 100 HIS B O   1 
ATOM   2896 C  CB  . HIS B 1 100 ? -29.141 37.752  15.059  1.00 25.45  ? 100 HIS B CB  1 
ATOM   2897 C  CG  . HIS B 1 100 ? -29.825 36.518  15.617  1.00 24.44  ? 100 HIS B CG  1 
ATOM   2898 N  ND1 . HIS B 1 100 ? -30.943 35.985  15.073  1.00 27.13  ? 100 HIS B ND1 1 
ATOM   2899 C  CD2 . HIS B 1 100 ? -29.467 35.679  16.653  1.00 25.32  ? 100 HIS B CD2 1 
ATOM   2900 C  CE1 . HIS B 1 100 ? -31.274 34.873  15.734  1.00 22.74  ? 100 HIS B CE1 1 
ATOM   2901 N  NE2 . HIS B 1 100 ? -30.361 34.684  16.695  1.00 24.39  ? 100 HIS B NE2 1 
ATOM   2902 N  N   . TRP B 1 101 ? -27.670 39.301  12.494  1.00 29.42  ? 101 TRP B N   1 
ATOM   2903 C  CA  . TRP B 1 101 ? -26.972 40.516  12.053  1.00 30.74  ? 101 TRP B CA  1 
ATOM   2904 C  C   . TRP B 1 101 ? -27.624 41.258  10.922  1.00 28.46  ? 101 TRP B C   1 
ATOM   2905 O  O   . TRP B 1 101 ? -28.553 40.776  10.301  1.00 32.57  ? 101 TRP B O   1 
ATOM   2906 C  CB  . TRP B 1 101 ? -25.517 40.220  11.691  1.00 27.17  ? 101 TRP B CB  1 
ATOM   2907 C  CG  . TRP B 1 101 ? -25.437 39.311  10.505  1.00 32.88  ? 101 TRP B CG  1 
ATOM   2908 C  CD1 . TRP B 1 101 ? -25.442 39.658  9.158   1.00 31.87  ? 101 TRP B CD1 1 
ATOM   2909 C  CD2 . TRP B 1 101 ? -25.412 37.850  10.532  1.00 28.09  ? 101 TRP B CD2 1 
ATOM   2910 N  NE1 . TRP B 1 101 ? -25.419 38.535  8.380   1.00 32.33  ? 101 TRP B NE1 1 
ATOM   2911 C  CE2 . TRP B 1 101 ? -25.395 37.417  9.153   1.00 31.31  ? 101 TRP B CE2 1 
ATOM   2912 C  CE3 . TRP B 1 101 ? -25.410 36.900  11.540  1.00 29.13  ? 101 TRP B CE3 1 
ATOM   2913 C  CZ2 . TRP B 1 101 ? -25.347 36.072  8.805   1.00 27.72  ? 101 TRP B CZ2 1 
ATOM   2914 C  CZ3 . TRP B 1 101 ? -25.395 35.553  11.185  1.00 28.99  ? 101 TRP B CZ3 1 
ATOM   2915 C  CH2 . TRP B 1 101 ? -25.354 35.154  9.849   1.00 27.05  ? 101 TRP B CH2 1 
ATOM   2916 N  N   . SER B 1 102 ? -27.138 42.459  10.651  1.00 31.00  ? 102 SER B N   1 
ATOM   2917 C  CA  . SER B 1 102 ? -27.561 43.199  9.465   1.00 34.30  ? 102 SER B CA  1 
ATOM   2918 C  C   . SER B 1 102 ? -26.319 43.677  8.708   1.00 35.79  ? 102 SER B C   1 
ATOM   2919 O  O   . SER B 1 102 ? -25.242 43.159  8.929   1.00 35.47  ? 102 SER B O   1 
ATOM   2920 C  CB  . SER B 1 102 ? -28.426 44.381  9.882   1.00 37.74  ? 102 SER B CB  1 
ATOM   2921 O  OG  . SER B 1 102 ? -28.915 45.047  8.741   1.00 41.23  ? 102 SER B OG  1 
ATOM   2922 N  N   . ASP B 1 103 ? -26.469 44.664  7.828   1.00 37.75  ? 103 ASP B N   1 
ATOM   2923 C  CA  . ASP B 1 103 ? -25.308 45.280  7.160   1.00 39.51  ? 103 ASP B CA  1 
ATOM   2924 C  C   . ASP B 1 103 ? -25.244 46.792  7.499   1.00 40.54  ? 103 ASP B C   1 
ATOM   2925 O  O   . ASP B 1 103 ? -24.386 47.525  7.013   1.00 45.98  ? 103 ASP B O   1 
ATOM   2926 C  CB  . ASP B 1 103 ? -25.318 44.979  5.635   1.00 37.36  ? 103 ASP B CB  1 
ATOM   2927 C  CG  . ASP B 1 103 ? -26.611 45.433  4.944   1.00 41.14  ? 103 ASP B CG  1 
ATOM   2928 O  OD1 . ASP B 1 103 ? -27.552 45.865  5.651   1.00 40.80  ? 103 ASP B OD1 1 
ATOM   2929 O  OD2 . ASP B 1 103 ? -26.704 45.349  3.696   1.00 41.11  ? 103 ASP B OD2 1 
ATOM   2930 N  N   . LEU B 1 104 ? -26.167 47.232  8.351   1.00 40.07  ? 104 LEU B N   1 
ATOM   2931 C  CA  . LEU B 1 104 ? -26.155 48.574  8.934   1.00 43.47  ? 104 LEU B CA  1 
ATOM   2932 C  C   . LEU B 1 104 ? -26.030 48.478  10.471  1.00 43.99  ? 104 LEU B C   1 
ATOM   2933 O  O   . LEU B 1 104 ? -26.558 47.532  11.082  1.00 42.98  ? 104 LEU B O   1 
ATOM   2934 C  CB  . LEU B 1 104 ? -27.413 49.350  8.508   1.00 43.83  ? 104 LEU B CB  1 
ATOM   2935 C  CG  . LEU B 1 104 ? -27.535 49.653  7.004   1.00 46.63  ? 104 LEU B CG  1 
ATOM   2936 C  CD1 . LEU B 1 104 ? -28.817 50.412  6.690   1.00 41.11  ? 104 LEU B CD1 1 
ATOM   2937 C  CD2 . LEU B 1 104 ? -26.307 50.397  6.476   1.00 42.65  ? 104 LEU B CD2 1 
ATOM   2938 N  N   . PRO B 1 105 ? -25.301 49.424  11.094  1.00 47.86  ? 105 PRO B N   1 
ATOM   2939 C  CA  . PRO B 1 105 ? -24.958 49.249  12.522  1.00 49.58  ? 105 PRO B CA  1 
ATOM   2940 C  C   . PRO B 1 105 ? -26.119 49.422  13.498  1.00 52.99  ? 105 PRO B C   1 
ATOM   2941 O  O   . PRO B 1 105 ? -26.002 49.027  14.658  1.00 55.04  ? 105 PRO B O   1 
ATOM   2942 C  CB  . PRO B 1 105 ? -23.888 50.331  12.781  1.00 50.56  ? 105 PRO B CB  1 
ATOM   2943 C  CG  . PRO B 1 105 ? -23.435 50.807  11.419  1.00 48.59  ? 105 PRO B CG  1 
ATOM   2944 C  CD  . PRO B 1 105 ? -24.596 50.577  10.487  1.00 49.56  ? 105 PRO B CD  1 
ATOM   2945 N  N   . TYR B 1 106 ? -27.213 50.027  13.044  1.00 54.70  ? 106 TYR B N   1 
ATOM   2946 C  CA  . TYR B 1 106 ? -28.302 50.421  13.946  1.00 53.62  ? 106 TYR B CA  1 
ATOM   2947 C  C   . TYR B 1 106 ? -29.439 49.376  14.000  1.00 53.89  ? 106 TYR B C   1 
ATOM   2948 O  O   . TYR B 1 106 ? -30.446 49.608  14.674  1.00 51.57  ? 106 TYR B O   1 
ATOM   2949 C  CB  . TYR B 1 106 ? -28.826 51.841  13.594  1.00 56.10  ? 106 TYR B CB  1 
ATOM   2950 C  CG  . TYR B 1 106 ? -29.662 51.912  12.312  1.00 56.06  ? 106 TYR B CG  1 
ATOM   2951 C  CD1 . TYR B 1 106 ? -31.031 51.592  12.329  1.00 56.61  ? 106 TYR B CD1 1 
ATOM   2952 C  CD2 . TYR B 1 106 ? -29.089 52.287  11.091  1.00 54.80  ? 106 TYR B CD2 1 
ATOM   2953 C  CE1 . TYR B 1 106 ? -31.796 51.630  11.181  1.00 56.02  ? 106 TYR B CE1 1 
ATOM   2954 C  CE2 . TYR B 1 106 ? -29.850 52.332  9.928   1.00 54.21  ? 106 TYR B CE2 1 
ATOM   2955 C  CZ  . TYR B 1 106 ? -31.203 52.006  9.981   1.00 61.88  ? 106 TYR B CZ  1 
ATOM   2956 O  OH  . TYR B 1 106 ? -31.984 52.034  8.840   1.00 68.57  ? 106 TYR B OH  1 
ATOM   2957 N  N   . LYS B 1 107 ? -29.275 48.220  13.333  1.00 50.95  ? 107 LYS B N   1 
ATOM   2958 C  CA  . LYS B 1 107 ? -30.381 47.237  13.268  1.00 49.22  ? 107 LYS B CA  1 
ATOM   2959 C  C   . LYS B 1 107 ? -30.118 45.714  13.347  1.00 47.28  ? 107 LYS B C   1 
ATOM   2960 O  O   . LYS B 1 107 ? -31.032 44.924  13.092  1.00 49.09  ? 107 LYS B O   1 
ATOM   2961 C  CB  . LYS B 1 107 ? -31.263 47.529  12.051  1.00 55.13  ? 107 LYS B CB  1 
ATOM   2962 C  CG  . LYS B 1 107 ? -30.577 47.395  10.707  1.00 53.36  ? 107 LYS B CG  1 
ATOM   2963 C  CD  . LYS B 1 107 ? -31.549 47.761  9.594   1.00 60.38  ? 107 LYS B CD  1 
ATOM   2964 C  CE  . LYS B 1 107 ? -32.806 46.890  9.632   1.00 65.81  ? 107 LYS B CE  1 
ATOM   2965 N  NZ  . LYS B 1 107 ? -33.239 46.388  8.291   1.00 63.11  ? 107 LYS B NZ  1 
ATOM   2966 N  N   . GLY B 1 108 ? -28.915 45.292  13.728  1.00 41.62  ? 108 GLY B N   1 
ATOM   2967 C  CA  . GLY B 1 108 ? -28.548 43.852  13.639  1.00 35.44  ? 108 GLY B CA  1 
ATOM   2968 C  C   . GLY B 1 108 ? -28.777 42.969  14.870  1.00 32.37  ? 108 GLY B C   1 
ATOM   2969 O  O   . GLY B 1 108 ? -28.747 41.767  14.769  1.00 29.80  ? 108 GLY B O   1 
ATOM   2970 N  N   . SER B 1 109 ? -28.984 43.543  16.047  1.00 28.43  ? 109 SER B N   1 
ATOM   2971 C  CA  . SER B 1 109 ? -29.191 42.713  17.197  1.00 26.53  ? 109 SER B CA  1 
ATOM   2972 C  C   . SER B 1 109 ? -30.694 42.413  17.322  1.00 28.79  ? 109 SER B C   1 
ATOM   2973 O  O   . SER B 1 109 ? -31.528 43.018  16.657  1.00 28.43  ? 109 SER B O   1 
ATOM   2974 C  CB  . SER B 1 109 ? -28.672 43.443  18.427  1.00 27.90  ? 109 SER B CB  1 
ATOM   2975 O  OG  . SER B 1 109 ? -29.406 44.676  18.604  1.00 26.00  ? 109 SER B OG  1 
ATOM   2976 N  N   . GLU B 1 110 ? -31.043 41.481  18.196  1.00 28.90  ? 110 GLU B N   1 
ATOM   2977 C  CA  . GLU B 1 110 ? -32.420 41.127  18.399  1.00 27.13  ? 110 GLU B CA  1 
ATOM   2978 C  C   . GLU B 1 110 ? -32.932 41.854  19.626  1.00 27.09  ? 110 GLU B C   1 
ATOM   2979 O  O   . GLU B 1 110 ? -34.048 42.376  19.615  1.00 27.76  ? 110 GLU B O   1 
ATOM   2980 C  CB  . GLU B 1 110 ? -32.592 39.603  18.573  1.00 26.35  ? 110 GLU B CB  1 
ATOM   2981 C  CG  . GLU B 1 110 ? -32.009 38.745  17.437  1.00 26.01  ? 110 GLU B CG  1 
ATOM   2982 C  CD  . GLU B 1 110 ? -32.837 37.478  17.207  1.00 27.77  ? 110 GLU B CD  1 
ATOM   2983 O  OE1 . GLU B 1 110 ? -32.847 36.536  18.043  1.00 27.43  ? 110 GLU B OE1 1 
ATOM   2984 O  OE2 . GLU B 1 110 ? -33.516 37.440  16.185  1.00 29.85  ? 110 GLU B OE2 1 
ATOM   2985 N  N   . HIS B 1 111 ? -32.151 41.832  20.697  1.00 25.76  ? 111 HIS B N   1 
ATOM   2986 C  CA  . HIS B 1 111 ? -32.490 42.644  21.853  1.00 28.89  ? 111 HIS B CA  1 
ATOM   2987 C  C   . HIS B 1 111 ? -32.028 44.032  21.547  1.00 29.43  ? 111 HIS B C   1 
ATOM   2988 O  O   . HIS B 1 111 ? -31.098 44.240  20.765  1.00 26.74  ? 111 HIS B O   1 
ATOM   2989 C  CB  . HIS B 1 111 ? -31.887 42.110  23.144  1.00 26.53  ? 111 HIS B CB  1 
ATOM   2990 C  CG  . HIS B 1 111 ? -32.479 40.782  23.591  1.00 27.11  ? 111 HIS B CG  1 
ATOM   2991 N  ND1 . HIS B 1 111 ? -32.035 39.581  23.123  1.00 26.75  ? 111 HIS B ND1 1 
ATOM   2992 C  CD2 . HIS B 1 111 ? -33.510 40.491  24.494  1.00 28.18  ? 111 HIS B CD2 1 
ATOM   2993 C  CE1 . HIS B 1 111 ? -32.736 38.586  23.682  1.00 25.58  ? 111 HIS B CE1 1 
ATOM   2994 N  NE2 . HIS B 1 111 ? -33.653 39.133  24.520  1.00 28.96  ? 111 HIS B NE2 1 
ATOM   2995 N  N   . SER B 1 112 ? -32.723 45.009  22.109  1.00 31.44  ? 112 SER B N   1 
ATOM   2996 C  CA  . SER B 1 112 ? -32.216 46.389  22.082  1.00 28.08  ? 112 SER B CA  1 
ATOM   2997 C  C   . SER B 1 112 ? -31.955 46.847  23.527  1.00 28.26  ? 112 SER B C   1 
ATOM   2998 O  O   . SER B 1 112 ? -32.559 46.313  24.447  1.00 28.80  ? 112 SER B O   1 
ATOM   2999 C  CB  . SER B 1 112 ? -33.233 47.309  21.411  1.00 27.00  ? 112 SER B CB  1 
ATOM   3000 O  OG  . SER B 1 112 ? -34.429 47.393  22.183  1.00 25.73  ? 112 SER B OG  1 
ATOM   3001 N  N   . LEU B 1 113 ? -31.084 47.844  23.712  1.00 27.59  ? 113 LEU B N   1 
ATOM   3002 C  CA  . LEU B 1 113 ? -30.812 48.411  25.040  1.00 31.41  ? 113 LEU B CA  1 
ATOM   3003 C  C   . LEU B 1 113 ? -31.211 49.903  25.042  1.00 31.59  ? 113 LEU B C   1 
ATOM   3004 O  O   . LEU B 1 113 ? -30.760 50.694  24.193  1.00 30.61  ? 113 LEU B O   1 
ATOM   3005 C  CB  . LEU B 1 113 ? -29.317 48.222  25.437  1.00 30.38  ? 113 LEU B CB  1 
ATOM   3006 C  CG  . LEU B 1 113 ? -28.693 46.873  25.860  1.00 28.97  ? 113 LEU B CG  1 
ATOM   3007 C  CD1 . LEU B 1 113 ? -27.289 47.077  26.427  1.00 28.44  ? 113 LEU B CD1 1 
ATOM   3008 C  CD2 . LEU B 1 113 ? -29.519 46.071  26.883  1.00 27.19  ? 113 LEU B CD2 1 
ATOM   3009 N  N   . ASP B 1 114 ? -32.079 50.280  25.967  1.00 33.63  ? 114 ASP B N   1 
ATOM   3010 C  CA  . ASP B 1 114 ? -32.700 51.619  25.914  1.00 36.91  ? 114 ASP B CA  1 
ATOM   3011 C  C   . ASP B 1 114 ? -32.912 52.128  24.467  1.00 37.04  ? 114 ASP B C   1 
ATOM   3012 O  O   . ASP B 1 114 ? -32.488 53.241  24.092  1.00 38.53  ? 114 ASP B O   1 
ATOM   3013 C  CB  . ASP B 1 114 ? -31.877 52.614  26.727  1.00 34.61  ? 114 ASP B CB  1 
ATOM   3014 C  CG  . ASP B 1 114 ? -31.695 52.177  28.173  1.00 40.31  ? 114 ASP B CG  1 
ATOM   3015 O  OD1 . ASP B 1 114 ? -32.665 51.658  28.814  1.00 39.10  ? 114 ASP B OD1 1 
ATOM   3016 O  OD2 . ASP B 1 114 ? -30.561 52.351  28.675  1.00 41.66  ? 114 ASP B OD2 1 
ATOM   3017 N  N   . GLY B 1 115 ? -33.552 51.292  23.655  1.00 39.18  ? 115 GLY B N   1 
ATOM   3018 C  CA  . GLY B 1 115 ? -33.917 51.643  22.257  1.00 35.54  ? 115 GLY B CA  1 
ATOM   3019 C  C   . GLY B 1 115 ? -32.841 51.484  21.197  1.00 33.94  ? 115 GLY B C   1 
ATOM   3020 O  O   . GLY B 1 115 ? -33.121 51.641  19.996  1.00 31.84  ? 115 GLY B O   1 
ATOM   3021 N  N   . GLU B 1 116 ? -31.619 51.162  21.627  1.00 34.88  ? 116 GLU B N   1 
ATOM   3022 C  CA  . GLU B 1 116 ? -30.473 50.972  20.711  1.00 34.77  ? 116 GLU B CA  1 
ATOM   3023 C  C   . GLU B 1 116 ? -30.228 49.497  20.312  1.00 32.31  ? 116 GLU B C   1 
ATOM   3024 O  O   . GLU B 1 116 ? -30.131 48.611  21.181  1.00 31.35  ? 116 GLU B O   1 
ATOM   3025 C  CB  . GLU B 1 116 ? -29.190 51.492  21.363  1.00 37.68  ? 116 GLU B CB  1 
ATOM   3026 C  CG  . GLU B 1 116 ? -28.999 53.003  21.349  1.00 48.25  ? 116 GLU B CG  1 
ATOM   3027 C  CD  . GLU B 1 116 ? -27.549 53.385  21.610  1.00 50.08  ? 116 GLU B CD  1 
ATOM   3028 O  OE1 . GLU B 1 116 ? -27.244 53.801  22.749  1.00 48.20  ? 116 GLU B OE1 1 
ATOM   3029 O  OE2 . GLU B 1 116 ? -26.713 53.237  20.686  1.00 54.32  ? 116 GLU B OE2 1 
ATOM   3030 N  N   . HIS B 1 117 ? -30.077 49.267  19.015  1.00 31.74  ? 117 HIS B N   1 
ATOM   3031 C  CA  . HIS B 1 117 ? -29.752 47.951  18.437  1.00 32.49  ? 117 HIS B CA  1 
ATOM   3032 C  C   . HIS B 1 117 ? -28.339 48.033  18.045  1.00 31.01  ? 117 HIS B C   1 
ATOM   3033 O  O   . HIS B 1 117 ? -27.834 49.132  17.866  1.00 30.03  ? 117 HIS B O   1 
ATOM   3034 C  CB  . HIS B 1 117 ? -30.604 47.651  17.192  1.00 33.51  ? 117 HIS B CB  1 
ATOM   3035 C  CG  . HIS B 1 117 ? -32.066 47.415  17.494  1.00 37.41  ? 117 HIS B CG  1 
ATOM   3036 N  ND1 . HIS B 1 117 ? -32.533 46.230  17.944  1.00 42.82  ? 117 HIS B ND1 1 
ATOM   3037 C  CD2 . HIS B 1 117 ? -33.169 48.264  17.403  1.00 37.14  ? 117 HIS B CD2 1 
ATOM   3038 C  CE1 . HIS B 1 117 ? -33.873 46.312  18.116  1.00 45.78  ? 117 HIS B CE1 1 
ATOM   3039 N  NE2 . HIS B 1 117 ? -34.254 47.570  17.812  1.00 40.82  ? 117 HIS B NE2 1 
ATOM   3040 N  N   . PHE B 1 118 ? -27.674 46.884  17.941  1.00 30.91  ? 118 PHE B N   1 
ATOM   3041 C  CA  . PHE B 1 118 ? -26.249 46.837  17.609  1.00 29.78  ? 118 PHE B CA  1 
ATOM   3042 C  C   . PHE B 1 118 ? -25.979 46.224  16.255  1.00 28.81  ? 118 PHE B C   1 
ATOM   3043 O  O   . PHE B 1 118 ? -26.902 45.949  15.517  1.00 32.71  ? 118 PHE B O   1 
ATOM   3044 C  CB  . PHE B 1 118 ? -25.479 46.163  18.717  1.00 30.62  ? 118 PHE B CB  1 
ATOM   3045 C  CG  . PHE B 1 118 ? -25.285 47.044  19.891  1.00 36.76  ? 118 PHE B CG  1 
ATOM   3046 C  CD1 . PHE B 1 118 ? -26.265 47.148  20.874  1.00 37.55  ? 118 PHE B CD1 1 
ATOM   3047 C  CD2 . PHE B 1 118 ? -24.158 47.865  19.977  1.00 40.81  ? 118 PHE B CD2 1 
ATOM   3048 C  CE1 . PHE B 1 118 ? -26.101 48.018  21.954  1.00 37.28  ? 118 PHE B CE1 1 
ATOM   3049 C  CE2 . PHE B 1 118 ? -23.998 48.727  21.055  1.00 42.38  ? 118 PHE B CE2 1 
ATOM   3050 C  CZ  . PHE B 1 118 ? -24.973 48.793  22.046  1.00 38.16  ? 118 PHE B CZ  1 
ATOM   3051 N  N   . ALA B 1 119 ? -24.725 46.069  15.875  1.00 27.65  ? 119 ALA B N   1 
ATOM   3052 C  CA  . ALA B 1 119 ? -24.480 45.522  14.548  1.00 28.00  ? 119 ALA B CA  1 
ATOM   3053 C  C   . ALA B 1 119 ? -24.786 44.012  14.474  1.00 26.17  ? 119 ALA B C   1 
ATOM   3054 O  O   . ALA B 1 119 ? -25.216 43.539  13.432  1.00 29.90  ? 119 ALA B O   1 
ATOM   3055 C  CB  . ALA B 1 119 ? -23.050 45.828  14.094  1.00 26.35  ? 119 ALA B CB  1 
ATOM   3056 N  N   . MET B 1 120 ? -24.559 43.257  15.563  1.00 26.96  ? 120 MET B N   1 
ATOM   3057 C  CA  . MET B 1 120 ? -24.884 41.819  15.609  1.00 24.30  ? 120 MET B CA  1 
ATOM   3058 C  C   . MET B 1 120 ? -25.258 41.386  17.008  1.00 26.59  ? 120 MET B C   1 
ATOM   3059 O  O   . MET B 1 120 ? -24.977 42.096  17.962  1.00 25.41  ? 120 MET B O   1 
ATOM   3060 C  CB  . MET B 1 120 ? -23.695 40.942  15.192  1.00 28.45  ? 120 MET B CB  1 
ATOM   3061 C  CG  . MET B 1 120 ? -22.958 41.351  13.919  1.00 28.68  ? 120 MET B CG  1 
ATOM   3062 S  SD  . MET B 1 120 ? -21.499 40.346  13.727  1.00 32.51  ? 120 MET B SD  1 
ATOM   3063 C  CE  . MET B 1 120 ? -22.293 38.934  12.932  1.00 26.56  ? 120 MET B CE  1 
ATOM   3064 N  N   . GLU B 1 121 ? -25.861 40.200  17.150  1.00 20.94  ? 121 GLU B N   1 
ATOM   3065 C  CA  . GLU B 1 121 ? -25.965 39.649  18.453  1.00 23.75  ? 121 GLU B CA  1 
ATOM   3066 C  C   . GLU B 1 121 ? -25.582 38.148  18.430  1.00 23.40  ? 121 GLU B C   1 
ATOM   3067 O  O   . GLU B 1 121 ? -26.053 37.446  17.585  1.00 24.78  ? 121 GLU B O   1 
ATOM   3068 C  CB  . GLU B 1 121 ? -27.382 39.836  18.934  1.00 20.70  ? 121 GLU B CB  1 
ATOM   3069 C  CG  . GLU B 1 121 ? -27.648 39.350  20.345  1.00 26.17  ? 121 GLU B CG  1 
ATOM   3070 C  CD  . GLU B 1 121 ? -29.056 39.674  20.819  1.00 25.34  ? 121 GLU B CD  1 
ATOM   3071 O  OE1 . GLU B 1 121 ? -29.584 40.708  20.404  1.00 24.27  ? 121 GLU B OE1 1 
ATOM   3072 O  OE2 . GLU B 1 121 ? -29.636 38.884  21.584  1.00 27.81  ? 121 GLU B OE2 1 
ATOM   3073 N  N   . MET B 1 122 ? -24.753 37.704  19.369  1.00 21.97  ? 122 MET B N   1 
ATOM   3074 C  CA  . MET B 1 122 ? -24.230 36.352  19.422  1.00 24.32  ? 122 MET B CA  1 
ATOM   3075 C  C   . MET B 1 122 ? -24.953 35.646  20.568  1.00 24.82  ? 122 MET B C   1 
ATOM   3076 O  O   . MET B 1 122 ? -25.029 36.209  21.688  1.00 27.29  ? 122 MET B O   1 
ATOM   3077 C  CB  . MET B 1 122 ? -22.716 36.390  19.710  1.00 24.28  ? 122 MET B CB  1 
ATOM   3078 C  CG  . MET B 1 122 ? -21.987 35.047  19.542  1.00 27.73  ? 122 MET B CG  1 
ATOM   3079 S  SD  . MET B 1 122 ? -20.173 35.064  19.814  1.00 31.02  ? 122 MET B SD  1 
ATOM   3080 C  CE  . MET B 1 122 ? -20.147 35.480  21.560  1.00 29.04  ? 122 MET B CE  1 
ATOM   3081 N  N   . HIS B 1 123 ? -25.488 34.449  20.298  1.00 22.88  ? 123 HIS B N   1 
ATOM   3082 C  CA  . HIS B 1 123 ? -26.226 33.670  21.285  1.00 22.73  ? 123 HIS B CA  1 
ATOM   3083 C  C   . HIS B 1 123 ? -25.485 32.387  21.562  1.00 25.17  ? 123 HIS B C   1 
ATOM   3084 O  O   . HIS B 1 123 ? -25.265 31.579  20.618  1.00 24.36  ? 123 HIS B O   1 
ATOM   3085 C  CB  . HIS B 1 123 ? -27.679 33.359  20.814  1.00 21.99  ? 123 HIS B CB  1 
ATOM   3086 C  CG  . HIS B 1 123 ? -28.573 34.574  20.717  1.00 21.79  ? 123 HIS B CG  1 
ATOM   3087 N  ND1 . HIS B 1 123 ? -29.650 34.628  19.904  1.00 23.89  ? 123 HIS B ND1 1 
ATOM   3088 C  CD2 . HIS B 1 123 ? -28.508 35.789  21.355  1.00 23.23  ? 123 HIS B CD2 1 
ATOM   3089 C  CE1 . HIS B 1 123 ? -30.230 35.811  20.003  1.00 22.36  ? 123 HIS B CE1 1 
ATOM   3090 N  NE2 . HIS B 1 123 ? -29.530 36.534  20.903  1.00 25.65  ? 123 HIS B NE2 1 
ATOM   3091 N  N   . ILE B 1 124 ? -25.086 32.166  22.822  1.00 23.61  ? 124 ILE B N   1 
ATOM   3092 C  CA  . ILE B 1 124 ? -24.460 30.908  23.187  1.00 25.07  ? 124 ILE B CA  1 
ATOM   3093 C  C   . ILE B 1 124 ? -25.480 30.079  23.918  1.00 27.42  ? 124 ILE B C   1 
ATOM   3094 O  O   . ILE B 1 124 ? -25.802 30.373  25.068  1.00 28.32  ? 124 ILE B O   1 
ATOM   3095 C  CB  . ILE B 1 124 ? -23.132 31.035  23.980  1.00 24.08  ? 124 ILE B CB  1 
ATOM   3096 C  CG1 . ILE B 1 124 ? -22.224 32.069  23.333  1.00 22.53  ? 124 ILE B CG1 1 
ATOM   3097 C  CG2 . ILE B 1 124 ? -22.427 29.672  24.001  1.00 23.54  ? 124 ILE B CG2 1 
ATOM   3098 C  CD1 . ILE B 1 124 ? -20.897 32.370  24.007  1.00 19.34  ? 124 ILE B CD1 1 
ATOM   3099 N  N   . VAL B 1 125 ? -25.983 29.046  23.232  1.00 28.08  ? 125 VAL B N   1 
ATOM   3100 C  CA  . VAL B 1 125 ? -27.114 28.240  23.714  1.00 28.77  ? 125 VAL B CA  1 
ATOM   3101 C  C   . VAL B 1 125 ? -26.737 27.028  24.616  1.00 30.78  ? 125 VAL B C   1 
ATOM   3102 O  O   . VAL B 1 125 ? -25.863 26.233  24.273  1.00 30.39  ? 125 VAL B O   1 
ATOM   3103 C  CB  . VAL B 1 125 ? -28.020 27.862  22.529  1.00 27.37  ? 125 VAL B CB  1 
ATOM   3104 C  CG1 . VAL B 1 125 ? -29.287 27.167  22.992  1.00 26.72  ? 125 VAL B CG1 1 
ATOM   3105 C  CG2 . VAL B 1 125 ? -28.399 29.122  21.744  1.00 28.02  ? 125 VAL B CG2 1 
ATOM   3106 N  N   . HIS B 1 126 ? -27.358 26.940  25.800  1.00 30.97  ? 126 HIS B N   1 
ATOM   3107 C  CA  . HIS B 1 126 ? -27.056 25.885  26.791  1.00 29.99  ? 126 HIS B CA  1 
ATOM   3108 C  C   . HIS B 1 126 ? -28.302 25.208  27.245  1.00 34.57  ? 126 HIS B C   1 
ATOM   3109 O  O   . HIS B 1 126 ? -29.355 25.857  27.308  1.00 36.36  ? 126 HIS B O   1 
ATOM   3110 C  CB  . HIS B 1 126 ? -26.442 26.456  28.068  1.00 29.08  ? 126 HIS B CB  1 
ATOM   3111 C  CG  . HIS B 1 126 ? -25.164 27.210  27.850  1.00 26.83  ? 126 HIS B CG  1 
ATOM   3112 N  ND1 . HIS B 1 126 ? -25.127 28.404  27.244  1.00 27.68  ? 126 HIS B ND1 1 
ATOM   3113 C  CD2 . HIS B 1 126 ? -23.868 26.920  28.215  1.00 26.77  ? 126 HIS B CD2 1 
ATOM   3114 C  CE1 . HIS B 1 126 ? -23.863 28.835  27.183  1.00 25.60  ? 126 HIS B CE1 1 
ATOM   3115 N  NE2 . HIS B 1 126 ? -23.089 27.930  27.769  1.00 24.21  ? 126 HIS B NE2 1 
ATOM   3116 N  N   . GLU B 1 127 ? -28.196 23.925  27.626  1.00 36.46  ? 127 GLU B N   1 
ATOM   3117 C  CA  . GLU B 1 127 ? -29.325 23.200  28.214  1.00 39.74  ? 127 GLU B CA  1 
ATOM   3118 C  C   . GLU B 1 127 ? -29.050 22.686  29.634  1.00 40.22  ? 127 GLU B C   1 
ATOM   3119 O  O   . GLU B 1 127 ? -27.928 22.345  29.963  1.00 37.74  ? 127 GLU B O   1 
ATOM   3120 C  CB  . GLU B 1 127 ? -29.773 22.054  27.293  1.00 39.38  ? 127 GLU B CB  1 
ATOM   3121 C  CG  . GLU B 1 127 ? -30.309 22.552  25.973  1.00 41.38  ? 127 GLU B CG  1 
ATOM   3122 C  CD  . GLU B 1 127 ? -30.752 21.435  25.050  1.00 47.76  ? 127 GLU B CD  1 
ATOM   3123 O  OE1 . GLU B 1 127 ? -31.379 20.459  25.547  1.00 44.77  ? 127 GLU B OE1 1 
ATOM   3124 O  OE2 . GLU B 1 127 ? -30.459 21.533  23.829  1.00 50.10  ? 127 GLU B OE2 1 
ATOM   3125 N  N   . LYS B 1 128 ? -30.092 22.645  30.465  1.00 43.42  ? 128 LYS B N   1 
ATOM   3126 C  CA  . LYS B 1 128 ? -29.966 22.312  31.893  1.00 44.22  ? 128 LYS B CA  1 
ATOM   3127 C  C   . LYS B 1 128 ? -29.569 20.862  32.083  1.00 43.21  ? 128 LYS B C   1 
ATOM   3128 O  O   . LYS B 1 128 ? -30.033 20.006  31.347  1.00 40.40  ? 128 LYS B O   1 
ATOM   3129 C  CB  . LYS B 1 128 ? -31.292 22.581  32.622  1.00 41.28  ? 128 LYS B CB  1 
ATOM   3130 C  CG  . LYS B 1 128 ? -31.134 22.910  34.103  1.00 46.34  ? 128 LYS B CG  1 
ATOM   3131 C  CD  . LYS B 1 128 ? -32.412 22.716  34.919  1.00 47.52  ? 128 LYS B CD  1 
ATOM   3132 C  CE  . LYS B 1 128 ? -33.603 23.494  34.381  1.00 47.58  ? 128 LYS B CE  1 
ATOM   3133 N  NZ  . LYS B 1 128 ? -34.572 23.865  35.459  1.00 54.11  ? 128 LYS B NZ  1 
ATOM   3134 N  N   . GLU B 1 129 ? -28.707 20.612  33.069  1.00 55.61  ? 129 GLU B N   1 
ATOM   3135 C  CA  . GLU B 1 129 ? -28.303 19.255  33.503  1.00 60.01  ? 129 GLU B CA  1 
ATOM   3136 C  C   . GLU B 1 129 ? -29.522 18.398  33.842  1.00 62.91  ? 129 GLU B C   1 
ATOM   3137 O  O   . GLU B 1 129 ? -30.575 18.927  34.207  1.00 72.96  ? 129 GLU B O   1 
ATOM   3138 C  CB  . GLU B 1 129 ? -27.384 19.334  34.743  1.00 58.67  ? 129 GLU B CB  1 
ATOM   3139 C  CG  . GLU B 1 129 ? -25.884 19.124  34.489  1.00 57.63  ? 129 GLU B CG  1 
ATOM   3140 C  CD  . GLU B 1 129 ? -25.016 19.085  35.774  1.00 60.53  ? 129 GLU B CD  1 
ATOM   3141 O  OE1 . GLU B 1 129 ? -23.766 19.091  35.629  1.00 53.37  ? 129 GLU B OE1 1 
ATOM   3142 O  OE2 . GLU B 1 129 ? -25.548 19.062  36.927  1.00 53.56  ? 129 GLU B OE2 1 
ATOM   3143 N  N   . LYS B 1 130 ? -29.380 17.081  33.720  1.00 66.83  ? 130 LYS B N   1 
ATOM   3144 C  CA  . LYS B 1 130 ? -30.415 16.145  34.174  1.00 69.37  ? 130 LYS B CA  1 
ATOM   3145 C  C   . LYS B 1 130 ? -29.964 15.474  35.472  1.00 71.63  ? 130 LYS B C   1 
ATOM   3146 O  O   . LYS B 1 130 ? -30.260 14.288  35.706  1.00 73.84  ? 130 LYS B O   1 
ATOM   3147 C  CB  . LYS B 1 130 ? -30.722 15.085  33.102  1.00 66.07  ? 130 LYS B CB  1 
ATOM   3148 C  CG  . LYS B 1 130 ? -31.598 15.576  31.965  1.00 60.96  ? 130 LYS B CG  1 
ATOM   3149 C  CD  . LYS B 1 130 ? -31.162 14.944  30.655  1.00 61.12  ? 130 LYS B CD  1 
ATOM   3150 C  CE  . LYS B 1 130 ? -31.250 15.945  29.512  1.00 65.22  ? 130 LYS B CE  1 
ATOM   3151 N  NZ  . LYS B 1 130 ? -30.425 17.169  29.739  1.00 55.39  ? 130 LYS B NZ  1 
ATOM   3152 N  N   . GLY B 1 131 ? -29.247 16.243  36.300  1.00 68.17  ? 131 GLY B N   1 
ATOM   3153 C  CA  . GLY B 1 131 ? -28.654 15.745  37.541  1.00 62.59  ? 131 GLY B CA  1 
ATOM   3154 C  C   . GLY B 1 131 ? -29.681 15.383  38.594  1.00 58.08  ? 131 GLY B C   1 
ATOM   3155 O  O   . GLY B 1 131 ? -30.207 16.257  39.272  1.00 61.48  ? 131 GLY B O   1 
ATOM   3156 N  N   . ASP B 1 141 ? -43.700 22.199  33.255  1.00 63.72  ? 141 ASP B N   1 
ATOM   3157 C  CA  . ASP B 1 141 ? -43.299 22.942  32.058  1.00 64.04  ? 141 ASP B CA  1 
ATOM   3158 C  C   . ASP B 1 141 ? -42.411 24.141  32.416  1.00 56.55  ? 141 ASP B C   1 
ATOM   3159 O  O   . ASP B 1 141 ? -42.907 25.215  32.741  1.00 52.23  ? 141 ASP B O   1 
ATOM   3160 C  CB  . ASP B 1 141 ? -44.527 23.324  31.233  1.00 70.84  ? 141 ASP B CB  1 
ATOM   3161 C  CG  . ASP B 1 141 ? -45.303 22.098  30.766  1.00 76.61  ? 141 ASP B CG  1 
ATOM   3162 O  OD1 . ASP B 1 141 ? -44.789 20.969  30.975  1.00 81.60  ? 141 ASP B OD1 1 
ATOM   3163 O  OD2 . ASP B 1 141 ? -46.411 22.252  30.202  1.00 73.69  ? 141 ASP B OD2 1 
ATOM   3164 N  N   . PRO B 1 142 ? -41.080 23.934  32.356  1.00 48.56  ? 142 PRO B N   1 
ATOM   3165 C  CA  . PRO B 1 142 ? -40.061 24.737  33.019  1.00 46.72  ? 142 PRO B CA  1 
ATOM   3166 C  C   . PRO B 1 142 ? -39.753 26.026  32.251  1.00 47.97  ? 142 PRO B C   1 
ATOM   3167 O  O   . PRO B 1 142 ? -39.885 26.068  31.025  1.00 48.07  ? 142 PRO B O   1 
ATOM   3168 C  CB  . PRO B 1 142 ? -38.853 23.813  32.988  1.00 44.55  ? 142 PRO B CB  1 
ATOM   3169 C  CG  . PRO B 1 142 ? -39.007 23.078  31.707  1.00 46.29  ? 142 PRO B CG  1 
ATOM   3170 C  CD  . PRO B 1 142 ? -40.475 22.930  31.456  1.00 49.18  ? 142 PRO B CD  1 
ATOM   3171 N  N   . GLU B 1 143 ? -39.347 27.065  32.962  1.00 41.42  ? 143 GLU B N   1 
ATOM   3172 C  CA  . GLU B 1 143 ? -39.091 28.348  32.319  1.00 48.25  ? 143 GLU B CA  1 
ATOM   3173 C  C   . GLU B 1 143 ? -37.599 28.641  32.024  1.00 44.41  ? 143 GLU B C   1 
ATOM   3174 O  O   . GLU B 1 143 ? -37.287 29.646  31.381  1.00 48.02  ? 143 GLU B O   1 
ATOM   3175 C  CB  . GLU B 1 143 ? -39.744 29.501  33.107  1.00 53.77  ? 143 GLU B CB  1 
ATOM   3176 C  CG  . GLU B 1 143 ? -40.033 29.255  34.588  1.00 60.15  ? 143 GLU B CG  1 
ATOM   3177 C  CD  . GLU B 1 143 ? -41.093 30.215  35.139  1.00 65.79  ? 143 GLU B CD  1 
ATOM   3178 O  OE1 . GLU B 1 143 ? -42.109 30.442  34.434  1.00 65.09  ? 143 GLU B OE1 1 
ATOM   3179 O  OE2 . GLU B 1 143 ? -40.918 30.742  36.270  1.00 61.53  ? 143 GLU B OE2 1 
ATOM   3180 N  N   . ASP B 1 144 ? -36.717 27.737  32.453  1.00 40.00  ? 144 ASP B N   1 
ATOM   3181 C  CA  . ASP B 1 144 ? -35.261 27.913  32.431  1.00 37.99  ? 144 ASP B CA  1 
ATOM   3182 C  C   . ASP B 1 144 ? -34.566 26.642  31.966  1.00 38.98  ? 144 ASP B C   1 
ATOM   3183 O  O   . ASP B 1 144 ? -33.442 26.347  32.372  1.00 40.71  ? 144 ASP B O   1 
ATOM   3184 C  CB  . ASP B 1 144 ? -34.754 28.281  33.831  1.00 41.69  ? 144 ASP B CB  1 
ATOM   3185 C  CG  . ASP B 1 144 ? -35.200 27.287  34.896  1.00 42.30  ? 144 ASP B CG  1 
ATOM   3186 O  OD1 . ASP B 1 144 ? -35.943 26.349  34.561  1.00 50.15  ? 144 ASP B OD1 1 
ATOM   3187 O  OD2 . ASP B 1 144 ? -34.813 27.428  36.065  1.00 45.66  ? 144 ASP B OD2 1 
ATOM   3188 N  N   . GLU B 1 145 ? -35.245 25.898  31.104  1.00 38.20  ? 145 GLU B N   1 
ATOM   3189 C  CA  . GLU B 1 145 ? -34.700 24.714  30.509  1.00 39.60  ? 145 GLU B CA  1 
ATOM   3190 C  C   . GLU B 1 145 ? -33.577 25.094  29.578  1.00 35.95  ? 145 GLU B C   1 
ATOM   3191 O  O   . GLU B 1 145 ? -32.732 24.269  29.275  1.00 32.54  ? 145 GLU B O   1 
ATOM   3192 C  CB  . GLU B 1 145 ? -35.776 23.983  29.720  1.00 42.88  ? 145 GLU B CB  1 
ATOM   3193 C  CG  . GLU B 1 145 ? -35.905 22.534  30.110  1.00 53.26  ? 145 GLU B CG  1 
ATOM   3194 C  CD  . GLU B 1 145 ? -35.946 21.617  28.902  1.00 61.26  ? 145 GLU B CD  1 
ATOM   3195 O  OE1 . GLU B 1 145 ? -36.855 20.754  28.843  1.00 63.15  ? 145 GLU B OE1 1 
ATOM   3196 O  OE2 . GLU B 1 145 ? -35.063 21.755  28.024  1.00 61.37  ? 145 GLU B OE2 1 
ATOM   3197 N  N   . ILE B 1 146 ? -33.573 26.337  29.086  1.00 33.96  ? 146 ILE B N   1 
ATOM   3198 C  CA  . ILE B 1 146 ? -32.466 26.759  28.239  1.00 28.53  ? 146 ILE B CA  1 
ATOM   3199 C  C   . ILE B 1 146 ? -31.881 28.054  28.743  1.00 27.59  ? 146 ILE B C   1 
ATOM   3200 O  O   . ILE B 1 146 ? -32.599 29.012  29.024  1.00 31.82  ? 146 ILE B O   1 
ATOM   3201 C  CB  . ILE B 1 146 ? -32.870 26.842  26.760  1.00 28.31  ? 146 ILE B CB  1 
ATOM   3202 C  CG1 . ILE B 1 146 ? -33.136 25.441  26.180  1.00 29.22  ? 146 ILE B CG1 1 
ATOM   3203 C  CG2 . ILE B 1 146 ? -31.772 27.509  25.940  1.00 29.43  ? 146 ILE B CG2 1 
ATOM   3204 C  CD1 . ILE B 1 146 ? -34.019 25.463  24.932  1.00 32.57  ? 146 ILE B CD1 1 
ATOM   3205 N  N   . ALA B 1 147 ? -30.572 28.119  28.826  1.00 26.42  ? 147 ALA B N   1 
ATOM   3206 C  CA  . ALA B 1 147 ? -29.953 29.410  29.130  1.00 26.65  ? 147 ALA B CA  1 
ATOM   3207 C  C   . ALA B 1 147 ? -29.237 29.927  27.889  1.00 26.14  ? 147 ALA B C   1 
ATOM   3208 O  O   . ALA B 1 147 ? -28.349 29.241  27.365  1.00 27.77  ? 147 ALA B O   1 
ATOM   3209 C  CB  . ALA B 1 147 ? -28.964 29.261  30.280  1.00 24.71  ? 147 ALA B CB  1 
ATOM   3210 N  N   . VAL B 1 148 ? -29.621 31.097  27.405  1.00 24.49  ? 148 VAL B N   1 
ATOM   3211 C  CA  . VAL B 1 148 ? -28.776 31.771  26.420  1.00 25.85  ? 148 VAL B CA  1 
ATOM   3212 C  C   . VAL B 1 148 ? -27.920 32.884  27.041  1.00 25.41  ? 148 VAL B C   1 
ATOM   3213 O  O   . VAL B 1 148 ? -28.448 33.798  27.690  1.00 30.83  ? 148 VAL B O   1 
ATOM   3214 C  CB  . VAL B 1 148 ? -29.541 32.429  25.254  1.00 23.00  ? 148 VAL B CB  1 
ATOM   3215 C  CG1 . VAL B 1 148 ? -28.570 32.775  24.134  1.00 23.98  ? 148 VAL B CG1 1 
ATOM   3216 C  CG2 . VAL B 1 148 ? -30.643 31.540  24.705  1.00 28.56  ? 148 VAL B CG2 1 
ATOM   3217 N  N   . LEU B 1 149 ? -26.609 32.818  26.794  1.00 24.73  ? 149 LEU B N   1 
ATOM   3218 C  CA  . LEU B 1 149 ? -25.740 33.989  26.875  1.00 22.92  ? 149 LEU B CA  1 
ATOM   3219 C  C   . LEU B 1 149 ? -25.812 34.823  25.588  1.00 26.09  ? 149 LEU B C   1 
ATOM   3220 O  O   . LEU B 1 149 ? -25.486 34.357  24.494  1.00 21.64  ? 149 LEU B O   1 
ATOM   3221 C  CB  . LEU B 1 149 ? -24.297 33.574  27.105  1.00 22.91  ? 149 LEU B CB  1 
ATOM   3222 C  CG  . LEU B 1 149 ? -24.079 32.642  28.299  1.00 23.71  ? 149 LEU B CG  1 
ATOM   3223 C  CD1 . LEU B 1 149 ? -22.614 32.603  28.601  1.00 23.73  ? 149 LEU B CD1 1 
ATOM   3224 C  CD2 . LEU B 1 149 ? -24.839 33.054  29.578  1.00 23.40  ? 149 LEU B CD2 1 
ATOM   3225 N  N   . ALA B 1 150 ? -26.201 36.078  25.726  1.00 24.51  ? 150 ALA B N   1 
ATOM   3226 C  CA  . ALA B 1 150 ? -26.250 36.940  24.576  1.00 27.48  ? 150 ALA B CA  1 
ATOM   3227 C  C   . ALA B 1 150 ? -25.266 38.089  24.694  1.00 27.17  ? 150 ALA B C   1 
ATOM   3228 O  O   . ALA B 1 150 ? -25.224 38.807  25.700  1.00 30.49  ? 150 ALA B O   1 
ATOM   3229 C  CB  . ALA B 1 150 ? -27.671 37.439  24.314  1.00 20.29  ? 150 ALA B CB  1 
ATOM   3230 N  N   . PHE B 1 151 ? -24.484 38.264  23.636  1.00 31.73  ? 151 PHE B N   1 
ATOM   3231 C  CA  . PHE B 1 151 ? -23.576 39.385  23.536  1.00 31.56  ? 151 PHE B CA  1 
ATOM   3232 C  C   . PHE B 1 151 ? -23.975 40.212  22.335  1.00 31.95  ? 151 PHE B C   1 
ATOM   3233 O  O   . PHE B 1 151 ? -24.014 39.725  21.185  1.00 34.01  ? 151 PHE B O   1 
ATOM   3234 C  CB  . PHE B 1 151 ? -22.136 38.903  23.362  1.00 31.22  ? 151 PHE B CB  1 
ATOM   3235 C  CG  . PHE B 1 151 ? -21.636 38.065  24.496  1.00 35.75  ? 151 PHE B CG  1 
ATOM   3236 C  CD1 . PHE B 1 151 ? -21.854 36.682  24.513  1.00 33.47  ? 151 PHE B CD1 1 
ATOM   3237 C  CD2 . PHE B 1 151 ? -20.942 38.649  25.561  1.00 37.42  ? 151 PHE B CD2 1 
ATOM   3238 C  CE1 . PHE B 1 151 ? -21.427 35.906  25.575  1.00 33.49  ? 151 PHE B CE1 1 
ATOM   3239 C  CE2 . PHE B 1 151 ? -20.468 37.858  26.609  1.00 37.18  ? 151 PHE B CE2 1 
ATOM   3240 C  CZ  . PHE B 1 151 ? -20.719 36.490  26.620  1.00 34.40  ? 151 PHE B CZ  1 
ATOM   3241 N  N   . LEU B 1 152 ? -24.274 41.468  22.604  1.00 31.86  ? 152 LEU B N   1 
ATOM   3242 C  CA  . LEU B 1 152 ? -24.414 42.469  21.589  1.00 32.24  ? 152 LEU B CA  1 
ATOM   3243 C  C   . LEU B 1 152 ? -23.048 42.731  20.991  1.00 33.18  ? 152 LEU B C   1 
ATOM   3244 O  O   . LEU B 1 152 ? -22.047 42.733  21.705  1.00 32.77  ? 152 LEU B O   1 
ATOM   3245 C  CB  . LEU B 1 152 ? -24.996 43.735  22.221  1.00 35.03  ? 152 LEU B CB  1 
ATOM   3246 C  CG  . LEU B 1 152 ? -26.364 43.398  22.841  1.00 34.42  ? 152 LEU B CG  1 
ATOM   3247 C  CD1 . LEU B 1 152 ? -26.770 44.402  23.904  1.00 31.81  ? 152 LEU B CD1 1 
ATOM   3248 C  CD2 . LEU B 1 152 ? -27.436 43.272  21.758  1.00 30.51  ? 152 LEU B CD2 1 
ATOM   3249 N  N   . VAL B 1 153 ? -23.013 42.880  19.670  1.00 35.99  ? 153 VAL B N   1 
ATOM   3250 C  CA  . VAL B 1 153 ? -21.788 43.161  18.930  1.00 35.09  ? 153 VAL B CA  1 
ATOM   3251 C  C   . VAL B 1 153 ? -21.820 44.561  18.300  1.00 39.17  ? 153 VAL B C   1 
ATOM   3252 O  O   . VAL B 1 153 ? -22.871 44.971  17.825  1.00 41.60  ? 153 VAL B O   1 
ATOM   3253 C  CB  . VAL B 1 153 ? -21.582 42.130  17.819  1.00 33.20  ? 153 VAL B CB  1 
ATOM   3254 C  CG1 . VAL B 1 153 ? -20.406 42.528  16.917  1.00 29.86  ? 153 VAL B CG1 1 
ATOM   3255 C  CG2 . VAL B 1 153 ? -21.326 40.762  18.436  1.00 34.64  ? 153 VAL B CG2 1 
ATOM   3256 N  N   . GLU B 1 154 ? -20.679 45.272  18.297  1.00 42.09  ? 154 GLU B N   1 
ATOM   3257 C  CA  . GLU B 1 154 ? -20.516 46.572  17.582  1.00 40.42  ? 154 GLU B CA  1 
ATOM   3258 C  C   . GLU B 1 154 ? -19.195 46.681  16.811  1.00 42.87  ? 154 GLU B C   1 
ATOM   3259 O  O   . GLU B 1 154 ? -18.252 45.923  17.070  1.00 41.46  ? 154 GLU B O   1 
ATOM   3260 C  CB  . GLU B 1 154 ? -20.691 47.784  18.521  1.00 44.84  ? 154 GLU B CB  1 
ATOM   3261 C  CG  . GLU B 1 154 ? -19.609 47.967  19.592  1.00 51.25  ? 154 GLU B CG  1 
ATOM   3262 C  CD  . GLU B 1 154 ? -19.978 48.978  20.683  1.00 53.51  ? 154 GLU B CD  1 
ATOM   3263 O  OE1 . GLU B 1 154 ? -20.867 49.825  20.429  1.00 56.85  ? 154 GLU B OE1 1 
ATOM   3264 O  OE2 . GLU B 1 154 ? -19.383 48.924  21.799  1.00 48.15  ? 154 GLU B OE2 1 
ATOM   3265 N  N   . ALA B 1 155 ? -19.130 47.626  15.867  1.00 39.44  ? 155 ALA B N   1 
ATOM   3266 C  CA  . ALA B 1 155 ? -17.909 47.871  15.112  1.00 39.19  ? 155 ALA B CA  1 
ATOM   3267 C  C   . ALA B 1 155 ? -16.823 48.524  15.956  1.00 39.73  ? 155 ALA B C   1 
ATOM   3268 O  O   . ALA B 1 155 ? -17.090 49.412  16.756  1.00 39.67  ? 155 ALA B O   1 
ATOM   3269 C  CB  . ALA B 1 155 ? -18.191 48.683  13.856  1.00 40.79  ? 155 ALA B CB  1 
ATOM   3270 N  N   . GLY B 1 156 ? -15.590 48.047  15.776  1.00 50.09  ? 156 GLY B N   1 
ATOM   3271 C  CA  . GLY B 1 156 ? -14.377 48.638  16.396  1.00 50.28  ? 156 GLY B CA  1 
ATOM   3272 C  C   . GLY B 1 156 ? -13.277 48.909  15.366  1.00 53.05  ? 156 GLY B C   1 
ATOM   3273 O  O   . GLY B 1 156 ? -13.439 48.605  14.162  1.00 51.63  ? 156 GLY B O   1 
ATOM   3274 N  N   . THR B 1 157 ? -12.155 49.467  15.837  1.00 49.33  ? 157 THR B N   1 
ATOM   3275 C  CA  . THR B 1 157 ? -11.035 49.831  14.964  1.00 48.22  ? 157 THR B CA  1 
ATOM   3276 C  C   . THR B 1 157 ? -10.083 48.706  14.580  1.00 51.86  ? 157 THR B C   1 
ATOM   3277 O  O   . THR B 1 157 ? -9.407  48.804  13.540  1.00 52.59  ? 157 THR B O   1 
ATOM   3278 C  CB  . THR B 1 157 ? -10.223 51.024  15.502  1.00 48.62  ? 157 THR B CB  1 
ATOM   3279 O  OG1 . THR B 1 157 ? -10.022 50.888  16.922  1.00 51.44  ? 157 THR B OG1 1 
ATOM   3280 C  CG2 . THR B 1 157 ? -10.967 52.301  15.216  1.00 48.87  ? 157 THR B CG2 1 
ATOM   3281 N  N   . GLN B 1 158 ? -10.025 47.632  15.369  1.00 50.08  ? 158 GLN B N   1 
ATOM   3282 C  CA  . GLN B 1 158 ? -9.199  46.517  14.930  1.00 49.06  ? 158 GLN B CA  1 
ATOM   3283 C  C   . GLN B 1 158 ? -9.811  45.126  14.866  1.00 51.84  ? 158 GLN B C   1 
ATOM   3284 O  O   . GLN B 1 158 ? -10.954 44.906  15.279  1.00 49.36  ? 158 GLN B O   1 
ATOM   3285 C  CB  . GLN B 1 158 ? -7.860  46.491  15.648  1.00 53.65  ? 158 GLN B CB  1 
ATOM   3286 C  CG  . GLN B 1 158 ? -7.899  46.455  17.158  1.00 54.07  ? 158 GLN B CG  1 
ATOM   3287 C  CD  . GLN B 1 158 ? -6.491  46.439  17.704  1.00 61.47  ? 158 GLN B CD  1 
ATOM   3288 O  OE1 . GLN B 1 158 ? -6.287  46.304  18.911  1.00 63.52  ? 158 GLN B OE1 1 
ATOM   3289 N  NE2 . GLN B 1 158 ? -5.496  46.571  16.803  1.00 58.38  ? 158 GLN B NE2 1 
ATOM   3290 N  N   . VAL B 1 159 ? -9.025  44.204  14.297  1.00 48.41  ? 159 VAL B N   1 
ATOM   3291 C  CA  . VAL B 1 159 ? -9.418  42.804  14.150  1.00 45.89  ? 159 VAL B CA  1 
ATOM   3292 C  C   . VAL B 1 159 ? -9.540  42.216  15.558  1.00 47.34  ? 159 VAL B C   1 
ATOM   3293 O  O   . VAL B 1 159 ? -8.592  42.274  16.353  1.00 45.56  ? 159 VAL B O   1 
ATOM   3294 C  CB  . VAL B 1 159 ? -8.414  42.021  13.238  1.00 44.33  ? 159 VAL B CB  1 
ATOM   3295 C  CG1 . VAL B 1 159 ? -9.027  40.735  12.697  1.00 41.32  ? 159 VAL B CG1 1 
ATOM   3296 C  CG2 . VAL B 1 159 ? -8.012  42.872  12.037  1.00 41.60  ? 159 VAL B CG2 1 
ATOM   3297 N  N   . ASN B 1 160 ? -10.748 41.774  15.911  1.00 44.26  ? 160 ASN B N   1 
ATOM   3298 C  CA  . ASN B 1 160 ? -10.902 40.853  17.026  1.00 41.75  ? 160 ASN B CA  1 
ATOM   3299 C  C   . ASN B 1 160 ? -10.365 39.502  16.505  1.00 45.55  ? 160 ASN B C   1 
ATOM   3300 O  O   . ASN B 1 160 ? -11.076 38.791  15.798  1.00 42.56  ? 160 ASN B O   1 
ATOM   3301 C  CB  . ASN B 1 160 ? -12.377 40.736  17.401  1.00 41.47  ? 160 ASN B CB  1 
ATOM   3302 C  CG  . ASN B 1 160 ? -12.592 39.983  18.690  1.00 38.27  ? 160 ASN B CG  1 
ATOM   3303 O  OD1 . ASN B 1 160 ? -12.092 38.873  18.864  1.00 43.98  ? 160 ASN B OD1 1 
ATOM   3304 N  ND2 . ASN B 1 160 ? -13.323 40.582  19.609  1.00 42.51  ? 160 ASN B ND2 1 
ATOM   3305 N  N   . GLU B 1 161 ? -9.097  39.193  16.798  1.00 47.13  ? 161 GLU B N   1 
ATOM   3306 C  CA  . GLU B 1 161 ? -8.403  38.051  16.178  1.00 46.65  ? 161 GLU B CA  1 
ATOM   3307 C  C   . GLU B 1 161 ? -9.010  36.724  16.610  1.00 44.70  ? 161 GLU B C   1 
ATOM   3308 O  O   . GLU B 1 161 ? -8.996  35.763  15.854  1.00 40.02  ? 161 GLU B O   1 
ATOM   3309 C  CB  . GLU B 1 161 ? -6.889  38.056  16.481  1.00 48.45  ? 161 GLU B CB  1 
ATOM   3310 C  CG  . GLU B 1 161 ? -6.008  38.708  15.422  1.00 52.59  ? 161 GLU B CG  1 
ATOM   3311 C  CD  . GLU B 1 161 ? -5.929  37.930  14.098  1.00 60.49  ? 161 GLU B CD  1 
ATOM   3312 O  OE1 . GLU B 1 161 ? -5.833  36.674  14.096  1.00 58.64  ? 161 GLU B OE1 1 
ATOM   3313 O  OE2 . GLU B 1 161 ? -5.939  38.587  13.033  1.00 63.96  ? 161 GLU B OE2 1 
ATOM   3314 N  N   . GLY B 1 162 ? -9.542  36.688  17.827  1.00 41.33  ? 162 GLY B N   1 
ATOM   3315 C  CA  . GLY B 1 162 ? -10.256 35.512  18.328  1.00 45.38  ? 162 GLY B CA  1 
ATOM   3316 C  C   . GLY B 1 162 ? -11.418 35.070  17.450  1.00 43.55  ? 162 GLY B C   1 
ATOM   3317 O  O   . GLY B 1 162 ? -11.806 33.889  17.448  1.00 44.11  ? 162 GLY B O   1 
ATOM   3318 N  N   . PHE B 1 163 ? -11.966 36.010  16.691  1.00 42.37  ? 163 PHE B N   1 
ATOM   3319 C  CA  . PHE B 1 163 ? -13.101 35.726  15.807  1.00 41.92  ? 163 PHE B CA  1 
ATOM   3320 C  C   . PHE B 1 163 ? -12.629 35.289  14.437  1.00 44.63  ? 163 PHE B C   1 
ATOM   3321 O  O   . PHE B 1 163 ? -13.443 34.869  13.600  1.00 45.61  ? 163 PHE B O   1 
ATOM   3322 C  CB  . PHE B 1 163 ? -13.970 36.976  15.640  1.00 38.18  ? 163 PHE B CB  1 
ATOM   3323 C  CG  . PHE B 1 163 ? -15.141 37.012  16.551  1.00 36.77  ? 163 PHE B CG  1 
ATOM   3324 C  CD1 . PHE B 1 163 ? -14.993 37.390  17.875  1.00 35.55  ? 163 PHE B CD1 1 
ATOM   3325 C  CD2 . PHE B 1 163 ? -16.410 36.663  16.083  1.00 37.03  ? 163 PHE B CD2 1 
ATOM   3326 C  CE1 . PHE B 1 163 ? -16.082 37.426  18.727  1.00 33.12  ? 163 PHE B CE1 1 
ATOM   3327 C  CE2 . PHE B 1 163 ? -17.502 36.690  16.934  1.00 36.12  ? 163 PHE B CE2 1 
ATOM   3328 C  CZ  . PHE B 1 163 ? -17.342 37.075  18.256  1.00 35.87  ? 163 PHE B CZ  1 
ATOM   3329 N  N   . GLN B 1 164 ? -11.325 35.422  14.195  1.00 40.93  ? 164 GLN B N   1 
ATOM   3330 C  CA  . GLN B 1 164 ? -10.798 35.166  12.860  1.00 44.47  ? 164 GLN B CA  1 
ATOM   3331 C  C   . GLN B 1 164 ? -11.026 33.753  12.331  1.00 40.28  ? 164 GLN B C   1 
ATOM   3332 O  O   . GLN B 1 164 ? -11.364 33.607  11.174  1.00 42.38  ? 164 GLN B O   1 
ATOM   3333 C  CB  . GLN B 1 164 ? -9.344  35.649  12.695  1.00 45.21  ? 164 GLN B CB  1 
ATOM   3334 C  CG  . GLN B 1 164 ? -9.276  37.111  12.259  1.00 49.60  ? 164 GLN B CG  1 
ATOM   3335 C  CD  . GLN B 1 164 ? -10.180 37.426  11.072  1.00 48.47  ? 164 GLN B CD  1 
ATOM   3336 O  OE1 . GLN B 1 164 ? -11.169 38.143  11.212  1.00 47.65  ? 164 GLN B OE1 1 
ATOM   3337 N  NE2 . GLN B 1 164 ? -9.848  36.882  9.895   1.00 52.96  ? 164 GLN B NE2 1 
ATOM   3338 N  N   . PRO B 1 165 ? -10.839 32.712  13.171  1.00 41.58  ? 165 PRO B N   1 
ATOM   3339 C  CA  . PRO B 1 165 ? -11.168 31.367  12.724  1.00 37.79  ? 165 PRO B CA  1 
ATOM   3340 C  C   . PRO B 1 165 ? -12.615 31.228  12.227  1.00 41.61  ? 165 PRO B C   1 
ATOM   3341 O  O   . PRO B 1 165 ? -12.837 30.644  11.152  1.00 39.86  ? 165 PRO B O   1 
ATOM   3342 C  CB  . PRO B 1 165 ? -10.945 30.527  13.993  1.00 41.46  ? 165 PRO B CB  1 
ATOM   3343 C  CG  . PRO B 1 165 ? -9.813  31.239  14.680  1.00 37.59  ? 165 PRO B CG  1 
ATOM   3344 C  CD  . PRO B 1 165 ? -10.166 32.693  14.491  1.00 38.56  ? 165 PRO B CD  1 
ATOM   3345 N  N   . LEU B 1 166 ? -13.578 31.769  12.995  1.00 39.38  ? 166 LEU B N   1 
ATOM   3346 C  CA  . LEU B 1 166 ? -14.998 31.796  12.603  1.00 33.63  ? 166 LEU B CA  1 
ATOM   3347 C  C   . LEU B 1 166 ? -15.194 32.604  11.312  1.00 37.09  ? 166 LEU B C   1 
ATOM   3348 O  O   . LEU B 1 166 ? -15.803 32.105  10.362  1.00 39.21  ? 166 LEU B O   1 
ATOM   3349 C  CB  . LEU B 1 166 ? -15.882 32.373  13.721  1.00 32.24  ? 166 LEU B CB  1 
ATOM   3350 C  CG  . LEU B 1 166 ? -17.348 32.695  13.340  1.00 32.26  ? 166 LEU B CG  1 
ATOM   3351 C  CD1 . LEU B 1 166 ? -18.031 31.523  12.635  1.00 29.75  ? 166 LEU B CD1 1 
ATOM   3352 C  CD2 . LEU B 1 166 ? -18.157 33.111  14.567  1.00 29.00  ? 166 LEU B CD2 1 
ATOM   3353 N  N   . VAL B 1 167 ? -14.687 33.836  11.269  1.00 32.68  ? 167 VAL B N   1 
ATOM   3354 C  CA  . VAL B 1 167 ? -14.806 34.656  10.050  1.00 40.27  ? 167 VAL B CA  1 
ATOM   3355 C  C   . VAL B 1 167 ? -14.228 33.946  8.811   1.00 40.46  ? 167 VAL B C   1 
ATOM   3356 O  O   . VAL B 1 167 ? -14.858 33.921  7.766   1.00 42.34  ? 167 VAL B O   1 
ATOM   3357 C  CB  . VAL B 1 167 ? -14.235 36.086  10.238  1.00 41.46  ? 167 VAL B CB  1 
ATOM   3358 C  CG1 . VAL B 1 167 ? -14.218 36.845  8.924   1.00 42.04  ? 167 VAL B CG1 1 
ATOM   3359 C  CG2 . VAL B 1 167 ? -15.071 36.849  11.258  1.00 41.34  ? 167 VAL B CG2 1 
ATOM   3360 N  N   . GLU B 1 168 ? -13.062 33.326  8.957   1.00 42.82  ? 168 GLU B N   1 
ATOM   3361 C  CA  . GLU B 1 168 ? -12.442 32.570  7.875   1.00 46.18  ? 168 GLU B CA  1 
ATOM   3362 C  C   . GLU B 1 168 ? -13.226 31.355  7.355   1.00 43.51  ? 168 GLU B C   1 
ATOM   3363 O  O   . GLU B 1 168 ? -13.277 31.122  6.161   1.00 41.23  ? 168 GLU B O   1 
ATOM   3364 C  CB  . GLU B 1 168 ? -10.997 32.194  8.254   1.00 50.76  ? 168 GLU B CB  1 
ATOM   3365 C  CG  . GLU B 1 168 ? -9.994  33.280  7.812   1.00 52.11  ? 168 GLU B CG  1 
ATOM   3366 C  CD  . GLU B 1 168 ? -8.812  33.414  8.742   1.00 56.91  ? 168 GLU B CD  1 
ATOM   3367 O  OE1 . GLU B 1 168 ? -7.681  33.103  8.323   1.00 59.62  ? 168 GLU B OE1 1 
ATOM   3368 O  OE2 . GLU B 1 168 ? -9.005  33.837  9.901   1.00 63.36  ? 168 GLU B OE2 1 
ATOM   3369 N  N   . ALA B 1 169 ? -13.822 30.584  8.260   1.00 42.39  ? 169 ALA B N   1 
ATOM   3370 C  CA  . ALA B 1 169 ? -14.638 29.417  7.909   1.00 37.86  ? 169 ALA B CA  1 
ATOM   3371 C  C   . ALA B 1 169 ? -15.883 29.763  7.087   1.00 36.39  ? 169 ALA B C   1 
ATOM   3372 O  O   . ALA B 1 169 ? -16.523 28.885  6.553   1.00 36.55  ? 169 ALA B O   1 
ATOM   3373 C  CB  . ALA B 1 169 ? -15.047 28.667  9.177   1.00 36.28  ? 169 ALA B CB  1 
ATOM   3374 N  N   . LEU B 1 170 ? -16.235 31.041  7.003   1.00 38.15  ? 170 LEU B N   1 
ATOM   3375 C  CA  . LEU B 1 170 ? -17.481 31.424  6.365   1.00 36.17  ? 170 LEU B CA  1 
ATOM   3376 C  C   . LEU B 1 170 ? -17.359 31.309  4.870   1.00 39.92  ? 170 LEU B C   1 
ATOM   3377 O  O   . LEU B 1 170 ? -18.333 30.965  4.213   1.00 39.03  ? 170 LEU B O   1 
ATOM   3378 C  CB  . LEU B 1 170 ? -17.866 32.854  6.709   1.00 39.08  ? 170 LEU B CB  1 
ATOM   3379 C  CG  . LEU B 1 170 ? -18.033 33.245  8.168   1.00 30.97  ? 170 LEU B CG  1 
ATOM   3380 C  CD1 . LEU B 1 170 ? -18.084 34.760  8.134   1.00 31.89  ? 170 LEU B CD1 1 
ATOM   3381 C  CD2 . LEU B 1 170 ? -19.288 32.614  8.771   1.00 33.06  ? 170 LEU B CD2 1 
ATOM   3382 N  N   . SER B 1 171 ? -16.164 31.594  4.337   1.00 41.97  ? 171 SER B N   1 
ATOM   3383 C  CA  . SER B 1 171 ? -15.859 31.382  2.901   1.00 42.46  ? 171 SER B CA  1 
ATOM   3384 C  C   . SER B 1 171 ? -16.282 30.000  2.409   1.00 42.31  ? 171 SER B C   1 
ATOM   3385 O  O   . SER B 1 171 ? -16.707 29.861  1.255   1.00 48.59  ? 171 SER B O   1 
ATOM   3386 C  CB  . SER B 1 171 ? -14.363 31.602  2.604   1.00 38.44  ? 171 SER B CB  1 
ATOM   3387 O  OG  . SER B 1 171 ? -14.045 32.967  2.548   1.00 36.98  ? 171 SER B OG  1 
ATOM   3388 N  N   . ASN B 1 172 ? -16.187 28.997  3.285   1.00 43.51  ? 172 ASN B N   1 
ATOM   3389 C  CA  . ASN B 1 172 ? -16.546 27.586  2.953   1.00 46.27  ? 172 ASN B CA  1 
ATOM   3390 C  C   . ASN B 1 172 ? -17.986 27.114  3.265   1.00 51.09  ? 172 ASN B C   1 
ATOM   3391 O  O   . ASN B 1 172 ? -18.276 25.911  3.217   1.00 51.88  ? 172 ASN B O   1 
ATOM   3392 C  CB  . ASN B 1 172 ? -15.535 26.616  3.585   1.00 48.43  ? 172 ASN B CB  1 
ATOM   3393 C  CG  . ASN B 1 172 ? -14.095 26.940  3.198   1.00 51.04  ? 172 ASN B CG  1 
ATOM   3394 O  OD1 . ASN B 1 172 ? -13.814 27.254  2.044   1.00 54.37  ? 172 ASN B OD1 1 
ATOM   3395 N  ND2 . ASN B 1 172 ? -13.185 26.905  4.172   1.00 50.22  ? 172 ASN B ND2 1 
ATOM   3396 N  N   . ILE B 1 173 ? -18.895 28.039  3.569   1.00 48.49  ? 173 ILE B N   1 
ATOM   3397 C  CA  . ILE B 1 173 ? -20.282 27.647  3.848   1.00 44.66  ? 173 ILE B CA  1 
ATOM   3398 C  C   . ILE B 1 173 ? -21.341 28.708  3.397   1.00 49.86  ? 173 ILE B C   1 
ATOM   3399 O  O   . ILE B 1 173 ? -22.182 29.123  4.203   1.00 44.64  ? 173 ILE B O   1 
ATOM   3400 C  CB  . ILE B 1 173 ? -20.467 27.305  5.358   1.00 44.04  ? 173 ILE B CB  1 
ATOM   3401 C  CG1 . ILE B 1 173 ? -19.836 28.392  6.251   1.00 44.27  ? 173 ILE B CG1 1 
ATOM   3402 C  CG2 . ILE B 1 173 ? -19.883 25.953  5.727   1.00 39.15  ? 173 ILE B CG2 1 
ATOM   3403 C  CD1 . ILE B 1 173 ? -20.546 28.575  7.581   1.00 37.16  ? 173 ILE B CD1 1 
ATOM   3404 N  N   . PRO B 1 174 ? -21.330 29.139  2.105   1.00 47.07  ? 174 PRO B N   1 
ATOM   3405 C  CA  . PRO B 1 174 ? -22.266 30.214  1.748   1.00 45.65  ? 174 PRO B CA  1 
ATOM   3406 C  C   . PRO B 1 174 ? -23.713 29.728  1.565   1.00 42.08  ? 174 PRO B C   1 
ATOM   3407 O  O   . PRO B 1 174 ? -24.643 30.517  1.720   1.00 40.09  ? 174 PRO B O   1 
ATOM   3408 C  CB  . PRO B 1 174 ? -21.716 30.759  0.411   1.00 43.64  ? 174 PRO B CB  1 
ATOM   3409 C  CG  . PRO B 1 174 ? -20.610 29.837  -0.010  1.00 45.50  ? 174 PRO B CG  1 
ATOM   3410 C  CD  . PRO B 1 174 ? -20.569 28.671  0.933   1.00 48.53  ? 174 PRO B CD  1 
ATOM   3411 N  N   . LYS B 1 175 ? -23.888 28.435  1.286   1.00 42.14  ? 175 LYS B N   1 
ATOM   3412 C  CA  . LYS B 1 175 ? -25.193 27.879  0.983   1.00 42.15  ? 175 LYS B CA  1 
ATOM   3413 C  C   . LYS B 1 175 ? -25.854 27.332  2.231   1.00 44.44  ? 175 LYS B C   1 
ATOM   3414 O  O   . LYS B 1 175 ? -25.169 26.758  3.068   1.00 48.31  ? 175 LYS B O   1 
ATOM   3415 C  CB  . LYS B 1 175 ? -25.093 26.731  -0.031  1.00 45.57  ? 175 LYS B CB  1 
ATOM   3416 C  CG  . LYS B 1 175 ? -24.538 27.086  -1.388  1.00 47.06  ? 175 LYS B CG  1 
ATOM   3417 C  CD  . LYS B 1 175 ? -24.401 25.812  -2.214  1.00 49.11  ? 175 LYS B CD  1 
ATOM   3418 C  CE  . LYS B 1 175 ? -23.962 26.087  -3.648  1.00 46.88  ? 175 LYS B CE  1 
ATOM   3419 N  NZ  . LYS B 1 175 ? -24.292 24.908  -4.522  1.00 42.59  ? 175 LYS B NZ  1 
ATOM   3420 N  N   . PRO B 1 176 ? -27.197 27.460  2.336   1.00 36.77  ? 176 PRO B N   1 
ATOM   3421 C  CA  . PRO B 1 176 ? -27.831 26.733  3.409   1.00 42.12  ? 176 PRO B CA  1 
ATOM   3422 C  C   . PRO B 1 176 ? -27.394 25.291  3.263   1.00 43.12  ? 176 PRO B C   1 
ATOM   3423 O  O   . PRO B 1 176 ? -27.254 24.814  2.132   1.00 38.26  ? 176 PRO B O   1 
ATOM   3424 C  CB  . PRO B 1 176 ? -29.348 26.850  3.100   1.00 41.22  ? 176 PRO B CB  1 
ATOM   3425 C  CG  . PRO B 1 176 ? -29.479 28.014  2.157   1.00 40.16  ? 176 PRO B CG  1 
ATOM   3426 C  CD  . PRO B 1 176 ? -28.172 28.032  1.388   1.00 38.35  ? 176 PRO B CD  1 
ATOM   3427 N  N   . GLU B 1 177 ? -27.153 24.637  4.398   1.00 43.70  ? 177 GLU B N   1 
ATOM   3428 C  CA  . GLU B 1 177 ? -26.874 23.204  4.472   1.00 40.81  ? 177 GLU B CA  1 
ATOM   3429 C  C   . GLU B 1 177 ? -25.432 22.783  4.110   1.00 42.37  ? 177 GLU B C   1 
ATOM   3430 O  O   . GLU B 1 177 ? -25.139 21.590  4.026   1.00 42.48  ? 177 GLU B O   1 
ATOM   3431 C  CB  . GLU B 1 177 ? -27.924 22.407  3.670   1.00 42.61  ? 177 GLU B CB  1 
ATOM   3432 C  CG  . GLU B 1 177 ? -29.365 22.738  4.022   1.00 44.59  ? 177 GLU B CG  1 
ATOM   3433 C  CD  . GLU B 1 177 ? -29.621 22.681  5.521   1.00 50.34  ? 177 GLU B CD  1 
ATOM   3434 O  OE1 . GLU B 1 177 ? -29.282 21.641  6.114   1.00 52.84  ? 177 GLU B OE1 1 
ATOM   3435 O  OE2 . GLU B 1 177 ? -30.155 23.671  6.109   1.00 52.31  ? 177 GLU B OE2 1 
ATOM   3436 N  N   . MET B 1 178 ? -24.548 23.753  3.893   1.00 41.12  ? 178 MET B N   1 
ATOM   3437 C  CA  . MET B 1 178 ? -23.093 23.503  3.906   1.00 40.70  ? 178 MET B CA  1 
ATOM   3438 C  C   . MET B 1 178 ? -22.512 23.462  5.330   1.00 47.37  ? 178 MET B C   1 
ATOM   3439 O  O   . MET B 1 178 ? -23.016 24.154  6.245   1.00 43.88  ? 178 MET B O   1 
ATOM   3440 C  CB  . MET B 1 178 ? -22.361 24.542  3.048   1.00 39.35  ? 178 MET B CB  1 
ATOM   3441 C  CG  . MET B 1 178 ? -22.645 24.361  1.537   1.00 38.30  ? 178 MET B CG  1 
ATOM   3442 S  SD  . MET B 1 178 ? -21.605 25.422  0.510   1.00 43.13  ? 178 MET B SD  1 
ATOM   3443 C  CE  . MET B 1 178 ? -20.115 24.423  0.439   1.00 38.47  ? 178 MET B CE  1 
ATOM   3444 N  N   . SER B 1 179 ? -21.455 22.659  5.506   1.00 46.99  ? 179 SER B N   1 
ATOM   3445 C  CA  . SER B 1 179 ? -20.773 22.470  6.794   1.00 43.54  ? 179 SER B CA  1 
ATOM   3446 C  C   . SER B 1 179 ? -19.237 22.531  6.641   1.00 47.46  ? 179 SER B C   1 
ATOM   3447 O  O   . SER B 1 179 ? -18.692 22.140  5.607   1.00 49.88  ? 179 SER B O   1 
ATOM   3448 C  CB  . SER B 1 179 ? -21.186 21.122  7.381   1.00 43.52  ? 179 SER B CB  1 
ATOM   3449 O  OG  . SER B 1 179 ? -20.694 20.951  8.694   1.00 43.92  ? 179 SER B OG  1 
ATOM   3450 N  N   . THR B 1 180 ? -18.521 23.002  7.660   1.00 43.09  ? 180 THR B N   1 
ATOM   3451 C  CA  . THR B 1 180 ? -17.046 22.936  7.625   1.00 41.83  ? 180 THR B CA  1 
ATOM   3452 C  C   . THR B 1 180 ? -16.448 22.812  9.029   1.00 42.79  ? 180 THR B C   1 
ATOM   3453 O  O   . THR B 1 180 ? -17.180 22.691  10.010  1.00 48.43  ? 180 THR B O   1 
ATOM   3454 C  CB  . THR B 1 180 ? -16.431 24.132  6.844   1.00 44.83  ? 180 THR B CB  1 
ATOM   3455 O  OG1 . THR B 1 180 ? -15.041 23.910  6.615   1.00 46.59  ? 180 THR B OG1 1 
ATOM   3456 C  CG2 . THR B 1 180 ? -16.601 25.459  7.610   1.00 43.97  ? 180 THR B CG2 1 
ATOM   3457 N  N   . THR B 1 181 ? -15.121 22.825  9.119   1.00 46.65  ? 181 THR B N   1 
ATOM   3458 C  CA  . THR B 1 181 ? -14.402 22.782  10.392  1.00 45.78  ? 181 THR B CA  1 
ATOM   3459 C  C   . THR B 1 181 ? -13.589 24.082  10.494  1.00 46.75  ? 181 THR B C   1 
ATOM   3460 O  O   . THR B 1 181 ? -13.008 24.544  9.511   1.00 46.71  ? 181 THR B O   1 
ATOM   3461 C  CB  . THR B 1 181 ? -13.502 21.519  10.481  1.00 48.95  ? 181 THR B CB  1 
ATOM   3462 O  OG1 . THR B 1 181 ? -14.262 20.361  10.106  1.00 47.92  ? 181 THR B OG1 1 
ATOM   3463 C  CG2 . THR B 1 181 ? -13.017 21.281  11.878  1.00 49.81  ? 181 THR B CG2 1 
ATOM   3464 N  N   . MET B 1 182 ? -13.587 24.701  11.667  1.00 44.12  ? 182 MET B N   1 
ATOM   3465 C  CA  . MET B 1 182 ? -12.776 25.904  11.876  1.00 39.87  ? 182 MET B CA  1 
ATOM   3466 C  C   . MET B 1 182 ? -11.369 25.486  12.272  1.00 38.58  ? 182 MET B C   1 
ATOM   3467 O  O   . MET B 1 182 ? -11.174 24.422  12.887  1.00 35.09  ? 182 MET B O   1 
ATOM   3468 C  CB  . MET B 1 182 ? -13.363 26.773  12.998  1.00 34.35  ? 182 MET B CB  1 
ATOM   3469 C  CG  . MET B 1 182 ? -14.669 27.473  12.641  1.00 37.69  ? 182 MET B CG  1 
ATOM   3470 S  SD  . MET B 1 182 ? -15.744 27.839  14.044  1.00 42.04  ? 182 MET B SD  1 
ATOM   3471 C  CE  . MET B 1 182 ? -14.667 28.859  15.063  1.00 39.52  ? 182 MET B CE  1 
ATOM   3472 N  N   . ALA B 1 183 ? -10.400 26.331  11.950  1.00 36.04  ? 183 ALA B N   1 
ATOM   3473 C  CA  . ALA B 1 183 ? -9.104  26.280  12.630  1.00 43.08  ? 183 ALA B CA  1 
ATOM   3474 C  C   . ALA B 1 183 ? -9.321  26.253  14.157  1.00 46.48  ? 183 ALA B C   1 
ATOM   3475 O  O   . ALA B 1 183 ? -10.368 26.743  14.647  1.00 46.19  ? 183 ALA B O   1 
ATOM   3476 C  CB  . ALA B 1 183 ? -8.234  27.477  12.223  1.00 38.32  ? 183 ALA B CB  1 
ATOM   3477 N  N   . GLU B 1 184 ? -8.351  25.674  14.890  1.00 45.46  ? 184 GLU B N   1 
ATOM   3478 C  CA  . GLU B 1 184 ? -8.369  25.640  16.363  1.00 42.15  ? 184 GLU B CA  1 
ATOM   3479 C  C   . GLU B 1 184 ? -8.807  26.958  16.987  1.00 43.15  ? 184 GLU B C   1 
ATOM   3480 O  O   . GLU B 1 184 ? -8.444  28.048  16.516  1.00 38.76  ? 184 GLU B O   1 
ATOM   3481 C  CB  . GLU B 1 184 ? -7.035  25.158  16.954  1.00 48.34  ? 184 GLU B CB  1 
ATOM   3482 C  CG  . GLU B 1 184 ? -6.959  23.635  17.071  1.00 52.10  ? 184 GLU B CG  1 
ATOM   3483 C  CD  . GLU B 1 184 ? -5.561  23.090  17.368  1.00 55.94  ? 184 GLU B CD  1 
ATOM   3484 O  OE1 . GLU B 1 184 ? -5.198  22.041  16.768  1.00 54.19  ? 184 GLU B OE1 1 
ATOM   3485 O  OE2 . GLU B 1 184 ? -4.836  23.693  18.200  1.00 48.83  ? 184 GLU B OE2 1 
ATOM   3486 N  N   . SER B 1 185 ? -9.628  26.848  18.024  1.00 40.90  ? 185 SER B N   1 
ATOM   3487 C  CA  . SER B 1 185 ? -10.255 28.008  18.637  1.00 40.86  ? 185 SER B CA  1 
ATOM   3488 C  C   . SER B 1 185 ? -10.802 27.549  19.959  1.00 39.04  ? 185 SER B C   1 
ATOM   3489 O  O   . SER B 1 185 ? -11.074 26.355  20.149  1.00 39.97  ? 185 SER B O   1 
ATOM   3490 C  CB  . SER B 1 185 ? -11.454 28.497  17.790  1.00 43.67  ? 185 SER B CB  1 
ATOM   3491 O  OG  . SER B 1 185 ? -11.042 29.375  16.772  1.00 46.77  ? 185 SER B OG  1 
ATOM   3492 N  N   . SER B 1 186 ? -10.995 28.516  20.850  1.00 36.97  ? 186 SER B N   1 
ATOM   3493 C  CA  . SER B 1 186 ? -11.706 28.322  22.098  1.00 33.82  ? 186 SER B CA  1 
ATOM   3494 C  C   . SER B 1 186 ? -12.894 29.266  22.140  1.00 33.27  ? 186 SER B C   1 
ATOM   3495 O  O   . SER B 1 186 ? -12.962 30.280  21.401  1.00 34.57  ? 186 SER B O   1 
ATOM   3496 C  CB  . SER B 1 186 ? -10.793 28.665  23.265  1.00 31.48  ? 186 SER B CB  1 
ATOM   3497 O  OG  . SER B 1 186 ? -10.453 30.024  23.148  1.00 35.19  ? 186 SER B OG  1 
ATOM   3498 N  N   . LEU B 1 187 ? -13.809 28.970  23.045  1.00 34.13  ? 187 LEU B N   1 
ATOM   3499 C  CA  . LEU B 1 187 ? -14.928 29.854  23.288  1.00 33.95  ? 187 LEU B CA  1 
ATOM   3500 C  C   . LEU B 1 187 ? -14.503 31.193  23.956  1.00 35.83  ? 187 LEU B C   1 
ATOM   3501 O  O   . LEU B 1 187 ? -15.094 32.250  23.664  1.00 30.77  ? 187 LEU B O   1 
ATOM   3502 C  CB  . LEU B 1 187 ? -16.011 29.116  24.081  1.00 33.74  ? 187 LEU B CB  1 
ATOM   3503 C  CG  . LEU B 1 187 ? -16.805 28.082  23.256  1.00 34.41  ? 187 LEU B CG  1 
ATOM   3504 C  CD1 . LEU B 1 187 ? -17.787 27.273  24.113  1.00 31.31  ? 187 LEU B CD1 1 
ATOM   3505 C  CD2 . LEU B 1 187 ? -17.519 28.692  22.057  1.00 30.48  ? 187 LEU B CD2 1 
ATOM   3506 N  N   . LEU B 1 188 ? -13.468 31.149  24.808  1.00 35.61  ? 188 LEU B N   1 
ATOM   3507 C  CA  . LEU B 1 188 ? -12.944 32.368  25.455  1.00 37.85  ? 188 LEU B CA  1 
ATOM   3508 C  C   . LEU B 1 188 ? -12.434 33.368  24.433  1.00 38.09  ? 188 LEU B C   1 
ATOM   3509 O  O   . LEU B 1 188 ? -12.569 34.556  24.642  1.00 40.36  ? 188 LEU B O   1 
ATOM   3510 C  CB  . LEU B 1 188 ? -11.846 32.052  26.496  1.00 39.35  ? 188 LEU B CB  1 
ATOM   3511 C  CG  . LEU B 1 188 ? -11.763 32.996  27.714  1.00 45.10  ? 188 LEU B CG  1 
ATOM   3512 C  CD1 . LEU B 1 188 ? -13.039 32.954  28.578  1.00 45.42  ? 188 LEU B CD1 1 
ATOM   3513 C  CD2 . LEU B 1 188 ? -10.551 32.743  28.601  1.00 44.02  ? 188 LEU B CD2 1 
ATOM   3514 N  N   . ASP B 1 189 ? -11.863 32.873  23.332  1.00 36.43  ? 189 ASP B N   1 
ATOM   3515 C  CA  . ASP B 1 189 ? -11.441 33.684  22.191  1.00 38.77  ? 189 ASP B CA  1 
ATOM   3516 C  C   . ASP B 1 189 ? -12.474 34.645  21.603  1.00 38.05  ? 189 ASP B C   1 
ATOM   3517 O  O   . ASP B 1 189 ? -12.124 35.698  21.091  1.00 37.25  ? 189 ASP B O   1 
ATOM   3518 C  CB  . ASP B 1 189 ? -10.998 32.775  21.050  1.00 42.74  ? 189 ASP B CB  1 
ATOM   3519 C  CG  . ASP B 1 189 ? -9.753  31.993  21.371  1.00 47.51  ? 189 ASP B CG  1 
ATOM   3520 O  OD1 . ASP B 1 189 ? -9.044  32.350  22.341  1.00 47.72  ? 189 ASP B OD1 1 
ATOM   3521 O  OD2 . ASP B 1 189 ? -9.489  31.009  20.637  1.00 51.83  ? 189 ASP B OD2 1 
ATOM   3522 N  N   . LEU B 1 190 ? -13.738 34.249  21.628  1.00 39.08  ? 190 LEU B N   1 
ATOM   3523 C  CA  . LEU B 1 190 ? -14.826 35.091  21.133  1.00 36.97  ? 190 LEU B CA  1 
ATOM   3524 C  C   . LEU B 1 190 ? -15.281 36.122  22.187  1.00 36.67  ? 190 LEU B C   1 
ATOM   3525 O  O   . LEU B 1 190 ? -15.775 37.179  21.842  1.00 45.33  ? 190 LEU B O   1 
ATOM   3526 C  CB  . LEU B 1 190 ? -16.004 34.188  20.692  1.00 35.92  ? 190 LEU B CB  1 
ATOM   3527 C  CG  . LEU B 1 190 ? -15.737 33.022  19.710  1.00 34.43  ? 190 LEU B CG  1 
ATOM   3528 C  CD1 . LEU B 1 190 ? -16.990 32.191  19.462  1.00 33.48  ? 190 LEU B CD1 1 
ATOM   3529 C  CD2 . LEU B 1 190 ? -15.174 33.466  18.363  1.00 31.52  ? 190 LEU B CD2 1 
ATOM   3530 N  N   . LEU B 1 191 ? -15.093 35.807  23.463  1.00 38.77  ? 191 LEU B N   1 
ATOM   3531 C  CA  . LEU B 1 191 ? -15.654 36.593  24.574  1.00 43.35  ? 191 LEU B CA  1 
ATOM   3532 C  C   . LEU B 1 191 ? -14.772 37.768  25.010  1.00 44.85  ? 191 LEU B C   1 
ATOM   3533 O  O   . LEU B 1 191 ? -13.568 37.734  24.811  1.00 44.98  ? 191 LEU B O   1 
ATOM   3534 C  CB  . LEU B 1 191 ? -15.845 35.710  25.798  1.00 41.19  ? 191 LEU B CB  1 
ATOM   3535 C  CG  . LEU B 1 191 ? -16.631 34.409  25.731  1.00 44.90  ? 191 LEU B CG  1 
ATOM   3536 C  CD1 . LEU B 1 191 ? -17.014 34.021  27.151  1.00 43.54  ? 191 LEU B CD1 1 
ATOM   3537 C  CD2 . LEU B 1 191 ? -17.856 34.517  24.834  1.00 40.50  ? 191 LEU B CD2 1 
ATOM   3538 N  N   . PRO B 1 192 ? -15.371 38.804  25.635  1.00 49.17  ? 192 PRO B N   1 
ATOM   3539 C  CA  . PRO B 1 192 ? -14.557 39.880  26.205  1.00 50.31  ? 192 PRO B CA  1 
ATOM   3540 C  C   . PRO B 1 192 ? -13.915 39.406  27.511  1.00 50.54  ? 192 PRO B C   1 
ATOM   3541 O  O   . PRO B 1 192 ? -14.352 38.391  28.066  1.00 46.34  ? 192 PRO B O   1 
ATOM   3542 C  CB  . PRO B 1 192 ? -15.597 40.986  26.484  1.00 48.38  ? 192 PRO B CB  1 
ATOM   3543 C  CG  . PRO B 1 192 ? -16.841 40.568  25.763  1.00 43.71  ? 192 PRO B CG  1 
ATOM   3544 C  CD  . PRO B 1 192 ? -16.802 39.075  25.839  1.00 47.79  ? 192 PRO B CD  1 
ATOM   3545 N  N   . LYS B 1 193 ? -12.910 40.137  28.000  1.00 54.64  ? 193 LYS B N   1 
ATOM   3546 C  CA  . LYS B 1 193 ? -12.278 39.871  29.322  1.00 60.17  ? 193 LYS B CA  1 
ATOM   3547 C  C   . LYS B 1 193 ? -13.335 39.830  30.438  1.00 60.97  ? 193 LYS B C   1 
ATOM   3548 O  O   . LYS B 1 193 ? -14.309 40.576  30.381  1.00 57.40  ? 193 LYS B O   1 
ATOM   3549 C  CB  . LYS B 1 193 ? -11.203 40.928  29.628  1.00 63.66  ? 193 LYS B CB  1 
ATOM   3550 C  CG  . LYS B 1 193 ? -10.194 41.173  28.489  1.00 62.87  ? 193 LYS B CG  1 
ATOM   3551 C  CD  . LYS B 1 193 ? -9.045  42.092  28.909  1.00 64.27  ? 193 LYS B CD  1 
ATOM   3552 C  CE  . LYS B 1 193 ? -7.694  41.661  28.324  1.00 64.20  ? 193 LYS B CE  1 
ATOM   3553 N  NZ  . LYS B 1 193 ? -7.463  41.985  26.880  1.00 56.61  ? 193 LYS B NZ  1 
ATOM   3554 N  N   . GLU B 1 194 ? -13.154 38.979  31.447  1.00 66.73  ? 194 GLU B N   1 
ATOM   3555 C  CA  . GLU B 1 194 ? -14.258 38.708  32.392  1.00 75.02  ? 194 GLU B CA  1 
ATOM   3556 C  C   . GLU B 1 194 ? -14.529 39.738  33.511  1.00 75.16  ? 194 GLU B C   1 
ATOM   3557 O  O   . GLU B 1 194 ? -15.440 39.566  34.331  1.00 74.73  ? 194 GLU B O   1 
ATOM   3558 C  CB  . GLU B 1 194 ? -14.258 37.243  32.903  1.00 80.71  ? 194 GLU B CB  1 
ATOM   3559 C  CG  . GLU B 1 194 ? -13.150 36.812  33.862  1.00 83.72  ? 194 GLU B CG  1 
ATOM   3560 C  CD  . GLU B 1 194 ? -13.150 35.301  34.133  1.00 87.63  ? 194 GLU B CD  1 
ATOM   3561 O  OE1 . GLU B 1 194 ? -12.411 34.856  35.043  1.00 91.62  ? 194 GLU B OE1 1 
ATOM   3562 O  OE2 . GLU B 1 194 ? -13.882 34.550  33.445  1.00 79.21  ? 194 GLU B OE2 1 
ATOM   3563 N  N   . GLU B 1 195 ? -13.753 40.815  33.522  1.00 76.74  ? 195 GLU B N   1 
ATOM   3564 C  CA  . GLU B 1 195 ? -14.096 42.005  34.301  1.00 79.90  ? 195 GLU B CA  1 
ATOM   3565 C  C   . GLU B 1 195 ? -15.275 42.679  33.614  1.00 74.99  ? 195 GLU B C   1 
ATOM   3566 O  O   . GLU B 1 195 ? -16.008 43.464  34.218  1.00 82.35  ? 195 GLU B O   1 
ATOM   3567 C  CB  . GLU B 1 195 ? -12.910 42.987  34.365  1.00 83.75  ? 195 GLU B CB  1 
ATOM   3568 C  CG  . GLU B 1 195 ? -11.955 42.791  35.539  1.00 84.02  ? 195 GLU B CG  1 
ATOM   3569 C  CD  . GLU B 1 195 ? -11.184 41.484  35.475  1.00 85.62  ? 195 GLU B CD  1 
ATOM   3570 O  OE1 . GLU B 1 195 ? -10.828 41.043  34.360  1.00 83.27  ? 195 GLU B OE1 1 
ATOM   3571 O  OE2 . GLU B 1 195 ? -10.927 40.897  36.547  1.00 88.09  ? 195 GLU B OE2 1 
ATOM   3572 N  N   . LYS B 1 196 ? -15.436 42.358  32.334  1.00 65.12  ? 196 LYS B N   1 
ATOM   3573 C  CA  . LYS B 1 196 ? -16.458 42.941  31.488  1.00 52.14  ? 196 LYS B CA  1 
ATOM   3574 C  C   . LYS B 1 196 ? -17.678 42.025  31.369  1.00 43.94  ? 196 LYS B C   1 
ATOM   3575 O  O   . LYS B 1 196 ? -18.586 42.281  30.586  1.00 43.18  ? 196 LYS B O   1 
ATOM   3576 C  CB  . LYS B 1 196 ? -15.860 43.252  30.119  1.00 54.93  ? 196 LYS B CB  1 
ATOM   3577 C  CG  . LYS B 1 196 ? -14.833 44.376  30.148  1.00 52.28  ? 196 LYS B CG  1 
ATOM   3578 C  CD  . LYS B 1 196 ? -15.462 45.688  29.736  1.00 54.44  ? 196 LYS B CD  1 
ATOM   3579 C  CE  . LYS B 1 196 ? -15.144 46.016  28.283  1.00 56.63  ? 196 LYS B CE  1 
ATOM   3580 N  NZ  . LYS B 1 196 ? -16.372 46.388  27.528  1.00 49.86  ? 196 LYS B NZ  1 
ATOM   3581 N  N   . LEU B 1 197 ? -17.704 40.987  32.187  1.00 42.64  ? 197 LEU B N   1 
ATOM   3582 C  CA  . LEU B 1 197 ? -18.823 40.046  32.252  1.00 42.46  ? 197 LEU B CA  1 
ATOM   3583 C  C   . LEU B 1 197 ? -19.546 40.134  33.591  1.00 44.15  ? 197 LEU B C   1 
ATOM   3584 O  O   . LEU B 1 197 ? -20.470 39.366  33.889  1.00 45.40  ? 197 LEU B O   1 
ATOM   3585 C  CB  . LEU B 1 197 ? -18.352 38.625  31.957  1.00 36.30  ? 197 LEU B CB  1 
ATOM   3586 C  CG  . LEU B 1 197 ? -17.674 38.439  30.592  1.00 38.50  ? 197 LEU B CG  1 
ATOM   3587 C  CD1 . LEU B 1 197 ? -17.569 36.964  30.277  1.00 38.66  ? 197 LEU B CD1 1 
ATOM   3588 C  CD2 . LEU B 1 197 ? -18.396 39.160  29.459  1.00 36.41  ? 197 LEU B CD2 1 
ATOM   3589 N  N   . ARG B 1 198 ? -19.118 41.103  34.382  1.00 46.46  ? 198 ARG B N   1 
ATOM   3590 C  CA  . ARG B 1 198 ? -19.749 41.446  35.641  1.00 44.40  ? 198 ARG B CA  1 
ATOM   3591 C  C   . ARG B 1 198 ? -21.196 41.925  35.437  1.00 39.67  ? 198 ARG B C   1 
ATOM   3592 O  O   . ARG B 1 198 ? -22.102 41.520  36.161  1.00 36.19  ? 198 ARG B O   1 
ATOM   3593 C  CB  . ARG B 1 198 ? -18.943 42.563  36.317  1.00 49.50  ? 198 ARG B CB  1 
ATOM   3594 C  CG  . ARG B 1 198 ? -17.467 42.260  36.548  1.00 54.60  ? 198 ARG B CG  1 
ATOM   3595 N  N   . HIS B 1 199 ? -21.399 42.788  34.446  1.00 35.26  ? 199 HIS B N   1 
ATOM   3596 C  CA  . HIS B 1 199 ? -22.680 43.469  34.269  1.00 40.02  ? 199 HIS B CA  1 
ATOM   3597 C  C   . HIS B 1 199 ? -23.612 42.838  33.258  1.00 37.80  ? 199 HIS B C   1 
ATOM   3598 O  O   . HIS B 1 199 ? -23.323 42.802  32.056  1.00 34.46  ? 199 HIS B O   1 
ATOM   3599 C  CB  . HIS B 1 199 ? -22.444 44.958  34.001  1.00 42.52  ? 199 HIS B CB  1 
ATOM   3600 C  CG  . HIS B 1 199 ? -22.039 45.713  35.241  1.00 54.04  ? 199 HIS B CG  1 
ATOM   3601 N  ND1 . HIS B 1 199 ? -22.942 46.249  36.092  1.00 56.39  ? 199 HIS B ND1 1 
ATOM   3602 C  CD2 . HIS B 1 199 ? -20.783 45.934  35.808  1.00 59.36  ? 199 HIS B CD2 1 
ATOM   3603 C  CE1 . HIS B 1 199 ? -22.298 46.818  37.126  1.00 63.72  ? 199 HIS B CE1 1 
ATOM   3604 N  NE2 . HIS B 1 199 ? -20.975 46.621  36.955  1.00 64.02  ? 199 HIS B NE2 1 
ATOM   3605 N  N   . TYR B 1 200 ? -24.740 42.326  33.744  1.00 33.65  ? 200 TYR B N   1 
ATOM   3606 C  CA  . TYR B 1 200 ? -25.670 41.663  32.872  1.00 36.42  ? 200 TYR B CA  1 
ATOM   3607 C  C   . TYR B 1 200 ? -27.123 41.764  33.331  1.00 37.24  ? 200 TYR B C   1 
ATOM   3608 O  O   . TYR B 1 200 ? -27.416 41.811  34.540  1.00 35.85  ? 200 TYR B O   1 
ATOM   3609 C  CB  . TYR B 1 200 ? -25.274 40.185  32.704  1.00 32.51  ? 200 TYR B CB  1 
ATOM   3610 C  CG  . TYR B 1 200 ? -25.366 39.318  33.971  1.00 32.07  ? 200 TYR B CG  1 
ATOM   3611 C  CD1 . TYR B 1 200 ? -26.581 38.773  34.387  1.00 29.42  ? 200 TYR B CD1 1 
ATOM   3612 C  CD2 . TYR B 1 200 ? -24.230 39.016  34.726  1.00 31.07  ? 200 TYR B CD2 1 
ATOM   3613 C  CE1 . TYR B 1 200 ? -26.650 37.978  35.516  1.00 28.26  ? 200 TYR B CE1 1 
ATOM   3614 C  CE2 . TYR B 1 200 ? -24.295 38.190  35.857  1.00 28.39  ? 200 TYR B CE2 1 
ATOM   3615 C  CZ  . TYR B 1 200 ? -25.501 37.710  36.262  1.00 29.61  ? 200 TYR B CZ  1 
ATOM   3616 O  OH  . TYR B 1 200 ? -25.562 36.890  37.381  1.00 34.16  ? 200 TYR B OH  1 
ATOM   3617 N  N   . PHE B 1 201 ? -28.008 41.742  32.334  1.00 33.93  ? 201 PHE B N   1 
ATOM   3618 C  CA  . PHE B 1 201 ? -29.462 41.739  32.488  1.00 30.22  ? 201 PHE B CA  1 
ATOM   3619 C  C   . PHE B 1 201 ? -30.014 40.314  32.386  1.00 29.56  ? 201 PHE B C   1 
ATOM   3620 O  O   . PHE B 1 201 ? -29.487 39.501  31.621  1.00 30.76  ? 201 PHE B O   1 
ATOM   3621 C  CB  . PHE B 1 201 ? -30.102 42.643  31.399  1.00 28.80  ? 201 PHE B CB  1 
ATOM   3622 C  CG  . PHE B 1 201 ? -29.604 44.073  31.411  1.00 29.64  ? 201 PHE B CG  1 
ATOM   3623 C  CD1 . PHE B 1 201 ? -30.051 44.982  32.382  1.00 31.05  ? 201 PHE B CD1 1 
ATOM   3624 C  CD2 . PHE B 1 201 ? -28.705 44.519  30.471  1.00 33.70  ? 201 PHE B CD2 1 
ATOM   3625 C  CE1 . PHE B 1 201 ? -29.572 46.286  32.406  1.00 33.53  ? 201 PHE B CE1 1 
ATOM   3626 C  CE2 . PHE B 1 201 ? -28.218 45.837  30.482  1.00 34.25  ? 201 PHE B CE2 1 
ATOM   3627 C  CZ  . PHE B 1 201 ? -28.654 46.715  31.460  1.00 35.65  ? 201 PHE B CZ  1 
ATOM   3628 N  N   . ARG B 1 202 ? -31.119 40.059  33.093  1.00 31.71  ? 202 ARG B N   1 
ATOM   3629 C  CA  . ARG B 1 202 ? -31.744 38.756  33.278  1.00 33.09  ? 202 ARG B CA  1 
ATOM   3630 C  C   . ARG B 1 202 ? -33.248 38.883  33.125  1.00 35.24  ? 202 ARG B C   1 
ATOM   3631 O  O   . ARG B 1 202 ? -33.842 39.756  33.724  1.00 37.21  ? 202 ARG B O   1 
ATOM   3632 C  CB  . ARG B 1 202 ? -31.447 38.233  34.702  1.00 31.76  ? 202 ARG B CB  1 
ATOM   3633 C  CG  . ARG B 1 202 ? -32.009 36.868  35.091  1.00 29.37  ? 202 ARG B CG  1 
ATOM   3634 C  CD  . ARG B 1 202 ? -31.572 35.715  34.182  1.00 36.14  ? 202 ARG B CD  1 
ATOM   3635 N  NE  . ARG B 1 202 ? -30.114 35.682  33.981  1.00 36.30  ? 202 ARG B NE  1 
ATOM   3636 C  CZ  . ARG B 1 202 ? -29.291 34.915  34.685  1.00 33.35  ? 202 ARG B CZ  1 
ATOM   3637 N  NH1 . ARG B 1 202 ? -29.779 34.111  35.599  1.00 39.26  ? 202 ARG B NH1 1 
ATOM   3638 N  NH2 . ARG B 1 202 ? -27.990 34.941  34.464  1.00 34.38  ? 202 ARG B NH2 1 
ATOM   3639 N  N   . TYR B 1 203 ? -33.853 38.005  32.330  1.00 32.61  ? 203 TYR B N   1 
ATOM   3640 C  CA  . TYR B 1 203 ? -35.321 37.825  32.308  1.00 31.92  ? 203 TYR B CA  1 
ATOM   3641 C  C   . TYR B 1 203 ? -35.679 36.440  31.754  1.00 34.18  ? 203 TYR B C   1 
ATOM   3642 O  O   . TYR B 1 203 ? -34.828 35.719  31.210  1.00 31.92  ? 203 TYR B O   1 
ATOM   3643 C  CB  . TYR B 1 203 ? -36.026 38.934  31.511  1.00 29.43  ? 203 TYR B CB  1 
ATOM   3644 C  CG  . TYR B 1 203 ? -35.848 38.796  30.020  1.00 29.52  ? 203 TYR B CG  1 
ATOM   3645 C  CD1 . TYR B 1 203 ? -34.645 39.092  29.383  1.00 29.73  ? 203 TYR B CD1 1 
ATOM   3646 C  CD2 . TYR B 1 203 ? -36.905 38.357  29.252  1.00 29.98  ? 203 TYR B CD2 1 
ATOM   3647 C  CE1 . TYR B 1 203 ? -34.524 38.946  27.988  1.00 27.98  ? 203 TYR B CE1 1 
ATOM   3648 C  CE2 . TYR B 1 203 ? -36.804 38.222  27.904  1.00 27.59  ? 203 TYR B CE2 1 
ATOM   3649 C  CZ  . TYR B 1 203 ? -35.635 38.491  27.269  1.00 27.93  ? 203 TYR B CZ  1 
ATOM   3650 O  OH  . TYR B 1 203 ? -35.675 38.257  25.913  1.00 25.88  ? 203 TYR B OH  1 
ATOM   3651 N  N   . LEU B 1 204 ? -36.949 36.084  31.893  1.00 39.34  ? 204 LEU B N   1 
ATOM   3652 C  CA  . LEU B 1 204 ? -37.460 34.825  31.400  1.00 38.84  ? 204 LEU B CA  1 
ATOM   3653 C  C   . LEU B 1 204 ? -38.213 35.023  30.093  1.00 38.66  ? 204 LEU B C   1 
ATOM   3654 O  O   . LEU B 1 204 ? -39.110 35.865  30.016  1.00 36.53  ? 204 LEU B O   1 
ATOM   3655 C  CB  . LEU B 1 204 ? -38.380 34.199  32.446  1.00 37.39  ? 204 LEU B CB  1 
ATOM   3656 C  CG  . LEU B 1 204 ? -37.734 33.794  33.778  1.00 39.78  ? 204 LEU B CG  1 
ATOM   3657 C  CD1 . LEU B 1 204 ? -38.842 33.438  34.757  1.00 37.81  ? 204 LEU B CD1 1 
ATOM   3658 C  CD2 . LEU B 1 204 ? -36.778 32.619  33.625  1.00 37.85  ? 204 LEU B CD2 1 
ATOM   3659 N  N   . GLY B 1 205 ? -37.878 34.212  29.088  1.00 35.00  ? 205 GLY B N   1 
ATOM   3660 C  CA  . GLY B 1 205 ? -38.449 34.380  27.768  1.00 33.28  ? 205 GLY B CA  1 
ATOM   3661 C  C   . GLY B 1 205 ? -38.612 33.169  26.886  1.00 30.49  ? 205 GLY B C   1 
ATOM   3662 O  O   . GLY B 1 205 ? -38.756 32.032  27.360  1.00 28.66  ? 205 GLY B O   1 
ATOM   3663 N  N   . SER B 1 206 ? -38.586 33.414  25.576  1.00 31.28  ? 206 SER B N   1 
ATOM   3664 C  CA  . SER B 1 206 ? -38.722 32.331  24.585  1.00 29.59  ? 206 SER B CA  1 
ATOM   3665 C  C   . SER B 1 206 ? -37.482 32.167  23.699  1.00 31.44  ? 206 SER B C   1 
ATOM   3666 O  O   . SER B 1 206 ? -36.615 33.028  23.671  1.00 30.35  ? 206 SER B O   1 
ATOM   3667 C  CB  . SER B 1 206 ? -39.886 32.640  23.668  1.00 29.54  ? 206 SER B CB  1 
ATOM   3668 O  OG  . SER B 1 206 ? -39.533 33.679  22.734  1.00 31.28  ? 206 SER B OG  1 
ATOM   3669 N  N   . LEU B 1 207 ? -37.458 31.117  22.890  1.00 32.79  ? 207 LEU B N   1 
ATOM   3670 C  CA  . LEU B 1 207 ? -36.536 31.087  21.769  1.00 31.85  ? 207 LEU B CA  1 
ATOM   3671 C  C   . LEU B 1 207 ? -37.043 32.155  20.801  1.00 32.31  ? 207 LEU B C   1 
ATOM   3672 O  O   . LEU B 1 207 ? -38.248 32.455  20.811  1.00 28.80  ? 207 LEU B O   1 
ATOM   3673 C  CB  . LEU B 1 207 ? -36.537 29.714  21.101  1.00 34.26  ? 207 LEU B CB  1 
ATOM   3674 C  CG  . LEU B 1 207 ? -36.501 28.503  22.036  1.00 37.02  ? 207 LEU B CG  1 
ATOM   3675 C  CD1 . LEU B 1 207 ? -36.047 27.259  21.288  1.00 39.29  ? 207 LEU B CD1 1 
ATOM   3676 C  CD2 . LEU B 1 207 ? -35.600 28.773  23.231  1.00 39.14  ? 207 LEU B CD2 1 
ATOM   3677 N  N   . THR B 1 208 ? -36.134 32.709  19.988  1.00 27.14  ? 208 THR B N   1 
ATOM   3678 C  CA  . THR B 1 208 ? -36.497 33.774  19.001  1.00 30.08  ? 208 THR B CA  1 
ATOM   3679 C  C   . THR B 1 208 ? -36.666 33.183  17.604  1.00 31.32  ? 208 THR B C   1 
ATOM   3680 O  O   . THR B 1 208 ? -36.776 33.886  16.623  1.00 29.69  ? 208 THR B O   1 
ATOM   3681 C  CB  . THR B 1 208 ? -35.516 34.990  18.952  1.00 27.84  ? 208 THR B CB  1 
ATOM   3682 O  OG1 . THR B 1 208 ? -34.232 34.607  18.426  1.00 24.66  ? 208 THR B OG1 1 
ATOM   3683 C  CG2 . THR B 1 208 ? -35.317 35.592  20.350  1.00 27.57  ? 208 THR B CG2 1 
ATOM   3684 N  N   . THR B 1 209 ? -36.696 31.863  17.539  1.00 36.24  ? 209 THR B N   1 
ATOM   3685 C  CA  . THR B 1 209 ? -37.016 31.161  16.316  1.00 33.81  ? 209 THR B CA  1 
ATOM   3686 C  C   . THR B 1 209 ? -38.145 30.172  16.643  1.00 34.89  ? 209 THR B C   1 
ATOM   3687 O  O   . THR B 1 209 ? -38.274 29.761  17.802  1.00 36.35  ? 209 THR B O   1 
ATOM   3688 C  CB  . THR B 1 209 ? -35.794 30.373  15.797  1.00 33.79  ? 209 THR B CB  1 
ATOM   3689 O  OG1 . THR B 1 209 ? -35.272 29.556  16.846  1.00 30.81  ? 209 THR B OG1 1 
ATOM   3690 C  CG2 . THR B 1 209 ? -34.698 31.317  15.272  1.00 29.72  ? 209 THR B CG2 1 
ATOM   3691 N  N   . PRO B 1 210 ? -38.950 29.778  15.635  1.00 32.93  ? 210 PRO B N   1 
ATOM   3692 C  CA  . PRO B 1 210 ? -39.976 28.777  15.851  1.00 34.91  ? 210 PRO B CA  1 
ATOM   3693 C  C   . PRO B 1 210 ? -39.332 27.487  16.421  1.00 35.12  ? 210 PRO B C   1 
ATOM   3694 O  O   . PRO B 1 210 ? -38.258 27.100  15.984  1.00 34.98  ? 210 PRO B O   1 
ATOM   3695 C  CB  . PRO B 1 210 ? -40.549 28.553  14.446  1.00 37.37  ? 210 PRO B CB  1 
ATOM   3696 C  CG  . PRO B 1 210 ? -40.201 29.800  13.684  1.00 39.44  ? 210 PRO B CG  1 
ATOM   3697 C  CD  . PRO B 1 210 ? -38.843 30.146  14.215  1.00 38.02  ? 210 PRO B CD  1 
ATOM   3698 N  N   . THR B 1 211 ? -39.957 26.854  17.394  1.00 30.80  ? 211 THR B N   1 
ATOM   3699 C  CA  . THR B 1 211 ? -41.344 27.114  17.751  1.00 34.72  ? 211 THR B CA  1 
ATOM   3700 C  C   . THR B 1 211 ? -41.503 28.032  18.941  1.00 36.31  ? 211 THR B C   1 
ATOM   3701 O  O   . THR B 1 211 ? -42.479 27.936  19.658  1.00 41.31  ? 211 THR B O   1 
ATOM   3702 C  CB  . THR B 1 211 ? -42.101 25.768  17.979  1.00 34.56  ? 211 THR B CB  1 
ATOM   3703 O  OG1 . THR B 1 211 ? -41.710 25.220  19.238  1.00 39.25  ? 211 THR B OG1 1 
ATOM   3704 C  CG2 . THR B 1 211 ? -41.730 24.771  16.871  1.00 30.99  ? 211 THR B CG2 1 
ATOM   3705 N  N   . CYS B 1 212 ? -40.564 28.958  19.136  1.00 37.39  ? 212 CYS B N   1 
ATOM   3706 C  CA  . CYS B 1 212 ? -40.696 29.993  20.175  1.00 38.89  ? 212 CYS B CA  1 
ATOM   3707 C  C   . CYS B 1 212 ? -41.072 29.519  21.580  1.00 40.04  ? 212 CYS B C   1 
ATOM   3708 O  O   . CYS B 1 212 ? -41.847 30.186  22.290  1.00 38.13  ? 212 CYS B O   1 
ATOM   3709 C  CB  . CYS B 1 212 ? -41.670 31.073  19.715  1.00 40.06  ? 212 CYS B CB  1 
ATOM   3710 S  SG  . CYS B 1 212 ? -41.249 31.690  18.063  1.00 37.41  ? 212 CYS B SG  1 
ATOM   3711 N  N   . ASP B 1 213 ? -40.544 28.352  21.959  1.00 42.87  ? 213 ASP B N   1 
ATOM   3712 C  CA  . ASP B 1 213 ? -40.742 27.773  23.297  1.00 43.56  ? 213 ASP B CA  1 
ATOM   3713 C  C   . ASP B 1 213 ? -40.530 28.745  24.457  1.00 41.29  ? 213 ASP B C   1 
ATOM   3714 O  O   . ASP B 1 213 ? -39.446 29.311  24.625  1.00 38.78  ? 213 ASP B O   1 
ATOM   3715 C  CB  . ASP B 1 213 ? -39.808 26.576  23.488  1.00 46.20  ? 213 ASP B CB  1 
ATOM   3716 C  CG  . ASP B 1 213 ? -40.293 25.338  22.772  1.00 50.53  ? 213 ASP B CG  1 
ATOM   3717 O  OD1 . ASP B 1 213 ? -41.513 25.262  22.516  1.00 43.77  ? 213 ASP B OD1 1 
ATOM   3718 O  OD2 . ASP B 1 213 ? -39.452 24.443  22.472  1.00 55.73  ? 213 ASP B OD2 1 
ATOM   3719 N  N   . GLU B 1 214 ? -41.546 28.894  25.291  1.00 39.86  ? 214 GLU B N   1 
ATOM   3720 C  CA  . GLU B 1 214 ? -41.422 29.753  26.458  1.00 41.06  ? 214 GLU B CA  1 
ATOM   3721 C  C   . GLU B 1 214 ? -40.652 29.115  27.626  1.00 41.23  ? 214 GLU B C   1 
ATOM   3722 O  O   . GLU B 1 214 ? -41.125 29.039  28.772  1.00 42.14  ? 214 GLU B O   1 
ATOM   3723 C  CB  . GLU B 1 214 ? -42.760 30.420  26.832  1.00 41.01  ? 214 GLU B CB  1 
ATOM   3724 C  CG  . GLU B 1 214 ? -43.171 31.463  25.773  1.00 45.81  ? 214 GLU B CG  1 
ATOM   3725 C  CD  . GLU B 1 214 ? -44.396 32.312  26.120  1.00 44.40  ? 214 GLU B CD  1 
ATOM   3726 O  OE1 . GLU B 1 214 ? -44.939 32.220  27.244  1.00 49.39  ? 214 GLU B OE1 1 
ATOM   3727 O  OE2 . GLU B 1 214 ? -44.807 33.102  25.255  1.00 39.04  ? 214 GLU B OE2 1 
ATOM   3728 N  N   . LYS B 1 215 ? -39.430 28.693  27.309  1.00 41.93  ? 215 LYS B N   1 
ATOM   3729 C  CA  . LYS B 1 215 ? -38.563 28.003  28.269  1.00 40.72  ? 215 LYS B CA  1 
ATOM   3730 C  C   . LYS B 1 215 ? -37.108 28.477  28.364  1.00 35.49  ? 215 LYS B C   1 
ATOM   3731 O  O   . LYS B 1 215 ? -36.253 27.709  28.774  1.00 36.36  ? 215 LYS B O   1 
ATOM   3732 C  CB  . LYS B 1 215 ? -38.583 26.502  27.986  1.00 42.01  ? 215 LYS B CB  1 
ATOM   3733 C  CG  . LYS B 1 215 ? -38.016 26.105  26.631  1.00 46.09  ? 215 LYS B CG  1 
ATOM   3734 C  CD  . LYS B 1 215 ? -38.034 24.583  26.487  1.00 49.12  ? 215 LYS B CD  1 
ATOM   3735 C  CE  . LYS B 1 215 ? -37.629 24.155  25.088  1.00 48.52  ? 215 LYS B CE  1 
ATOM   3736 N  NZ  . LYS B 1 215 ? -37.752 22.679  24.893  1.00 50.54  ? 215 LYS B NZ  1 
ATOM   3737 N  N   . VAL B 1 216 ? -36.832 29.732  28.012  1.00 33.82  ? 216 VAL B N   1 
ATOM   3738 C  CA  . VAL B 1 216 ? -35.469 30.277  28.063  1.00 29.68  ? 216 VAL B CA  1 
ATOM   3739 C  C   . VAL B 1 216 ? -35.235 31.223  29.211  1.00 30.24  ? 216 VAL B C   1 
ATOM   3740 O  O   . VAL B 1 216 ? -36.023 32.153  29.418  1.00 29.67  ? 216 VAL B O   1 
ATOM   3741 C  CB  . VAL B 1 216 ? -35.067 31.023  26.769  1.00 28.85  ? 216 VAL B CB  1 
ATOM   3742 C  CG1 . VAL B 1 216 ? -33.610 31.430  26.848  1.00 27.49  ? 216 VAL B CG1 1 
ATOM   3743 C  CG2 . VAL B 1 216 ? -35.209 30.082  25.577  1.00 27.29  ? 216 VAL B CG2 1 
ATOM   3744 N  N   . VAL B 1 217 ? -34.149 30.982  29.950  1.00 28.50  ? 217 VAL B N   1 
ATOM   3745 C  CA  . VAL B 1 217 ? -33.633 31.981  30.861  1.00 28.70  ? 217 VAL B CA  1 
ATOM   3746 C  C   . VAL B 1 217 ? -32.520 32.751  30.167  1.00 27.98  ? 217 VAL B C   1 
ATOM   3747 O  O   . VAL B 1 217 ? -31.463 32.196  29.881  1.00 25.80  ? 217 VAL B O   1 
ATOM   3748 C  CB  . VAL B 1 217 ? -33.175 31.434  32.224  1.00 26.16  ? 217 VAL B CB  1 
ATOM   3749 C  CG1 . VAL B 1 217 ? -32.091 30.378  32.081  1.00 25.66  ? 217 VAL B CG1 1 
ATOM   3750 C  CG2 . VAL B 1 217 ? -32.671 32.598  33.072  1.00 24.27  ? 217 VAL B CG2 1 
ATOM   3751 N  N   . TRP B 1 218 ? -32.818 34.027  29.930  1.00 28.85  ? 218 TRP B N   1 
ATOM   3752 C  CA  . TRP B 1 218 ? -32.039 34.943  29.116  1.00 29.30  ? 218 TRP B CA  1 
ATOM   3753 C  C   . TRP B 1 218 ? -31.045 35.670  29.963  1.00 33.62  ? 218 TRP B C   1 
ATOM   3754 O  O   . TRP B 1 218 ? -31.297 35.952  31.157  1.00 31.05  ? 218 TRP B O   1 
ATOM   3755 C  CB  . TRP B 1 218 ? -32.953 35.935  28.347  1.00 30.32  ? 218 TRP B CB  1 
ATOM   3756 C  CG  . TRP B 1 218 ? -33.447 35.347  27.042  1.00 31.95  ? 218 TRP B CG  1 
ATOM   3757 C  CD1 . TRP B 1 218 ? -34.674 34.746  26.801  1.00 29.53  ? 218 TRP B CD1 1 
ATOM   3758 C  CD2 . TRP B 1 218 ? -32.702 35.226  25.763  1.00 30.57  ? 218 TRP B CD2 1 
ATOM   3759 N  NE1 . TRP B 1 218 ? -34.753 34.298  25.501  1.00 31.23  ? 218 TRP B NE1 1 
ATOM   3760 C  CE2 . TRP B 1 218 ? -33.609 34.563  24.821  1.00 29.97  ? 218 TRP B CE2 1 
ATOM   3761 C  CE3 . TRP B 1 218 ? -31.435 35.604  25.323  1.00 29.89  ? 218 TRP B CE3 1 
ATOM   3762 C  CZ2 . TRP B 1 218 ? -33.240 34.277  23.513  1.00 28.34  ? 218 TRP B CZ2 1 
ATOM   3763 C  CZ3 . TRP B 1 218 ? -31.085 35.328  23.985  1.00 32.07  ? 218 TRP B CZ3 1 
ATOM   3764 C  CH2 . TRP B 1 218 ? -31.955 34.649  23.114  1.00 29.50  ? 218 TRP B CH2 1 
ATOM   3765 N  N   . THR B 1 219 ? -29.880 35.927  29.360  1.00 29.81  ? 219 THR B N   1 
ATOM   3766 C  CA  . THR B 1 219 ? -28.876 36.774  29.938  1.00 27.85  ? 219 THR B CA  1 
ATOM   3767 C  C   . THR B 1 219 ? -28.313 37.591  28.796  1.00 29.76  ? 219 THR B C   1 
ATOM   3768 O  O   . THR B 1 219 ? -27.795 37.050  27.806  1.00 28.46  ? 219 THR B O   1 
ATOM   3769 C  CB  . THR B 1 219 ? -27.750 35.960  30.593  1.00 31.79  ? 219 THR B CB  1 
ATOM   3770 O  OG1 . THR B 1 219 ? -28.295 35.133  31.658  1.00 27.17  ? 219 THR B OG1 1 
ATOM   3771 C  CG2 . THR B 1 219 ? -26.585 36.918  31.076  1.00 28.44  ? 219 THR B CG2 1 
ATOM   3772 N  N   . VAL B 1 220 ? -28.437 38.906  28.935  1.00 30.03  ? 220 VAL B N   1 
ATOM   3773 C  CA  . VAL B 1 220 ? -27.857 39.864  28.021  1.00 27.30  ? 220 VAL B CA  1 
ATOM   3774 C  C   . VAL B 1 220 ? -26.816 40.727  28.735  1.00 30.76  ? 220 VAL B C   1 
ATOM   3775 O  O   . VAL B 1 220 ? -27.126 41.404  29.763  1.00 26.12  ? 220 VAL B O   1 
ATOM   3776 C  CB  . VAL B 1 220 ? -28.954 40.729  27.385  1.00 28.69  ? 220 VAL B CB  1 
ATOM   3777 C  CG1 . VAL B 1 220 ? -28.397 41.621  26.267  1.00 24.06  ? 220 VAL B CG1 1 
ATOM   3778 C  CG2 . VAL B 1 220 ? -30.125 39.856  26.899  1.00 24.94  ? 220 VAL B CG2 1 
ATOM   3779 N  N   . PHE B 1 221 ? -25.582 40.658  28.214  1.00 32.40  ? 221 PHE B N   1 
ATOM   3780 C  CA  . PHE B 1 221 ? -24.457 41.391  28.772  1.00 36.69  ? 221 PHE B CA  1 
ATOM   3781 C  C   . PHE B 1 221 ? -24.462 42.829  28.295  1.00 35.96  ? 221 PHE B C   1 
ATOM   3782 O  O   . PHE B 1 221 ? -24.776 43.113  27.116  1.00 32.82  ? 221 PHE B O   1 
ATOM   3783 C  CB  . PHE B 1 221 ? -23.114 40.760  28.446  1.00 32.30  ? 221 PHE B CB  1 
ATOM   3784 C  CG  . PHE B 1 221 ? -22.902 39.427  29.099  1.00 35.26  ? 221 PHE B CG  1 
ATOM   3785 C  CD1 . PHE B 1 221 ? -23.347 38.258  28.483  1.00 30.70  ? 221 PHE B CD1 1 
ATOM   3786 C  CD2 . PHE B 1 221 ? -22.265 39.340  30.337  1.00 32.08  ? 221 PHE B CD2 1 
ATOM   3787 C  CE1 . PHE B 1 221 ? -23.141 37.044  29.066  1.00 31.65  ? 221 PHE B CE1 1 
ATOM   3788 C  CE2 . PHE B 1 221 ? -22.062 38.125  30.923  1.00 28.09  ? 221 PHE B CE2 1 
ATOM   3789 C  CZ  . PHE B 1 221 ? -22.490 36.982  30.296  1.00 33.91  ? 221 PHE B CZ  1 
ATOM   3790 N  N   . ARG B 1 222 ? -24.143 43.715  29.240  1.00 38.43  ? 222 ARG B N   1 
ATOM   3791 C  CA  . ARG B 1 222 ? -24.292 45.170  29.047  1.00 45.93  ? 222 ARG B CA  1 
ATOM   3792 C  C   . ARG B 1 222 ? -23.258 45.777  28.104  1.00 45.26  ? 222 ARG B C   1 
ATOM   3793 O  O   . ARG B 1 222 ? -23.581 46.700  27.364  1.00 48.63  ? 222 ARG B O   1 
ATOM   3794 C  CB  . ARG B 1 222 ? -24.288 45.924  30.387  1.00 50.75  ? 222 ARG B CB  1 
ATOM   3795 C  CG  . ARG B 1 222 ? -24.490 47.437  30.243  1.00 53.08  ? 222 ARG B CG  1 
ATOM   3796 C  CD  . ARG B 1 222 ? -24.303 48.172  31.572  1.00 60.59  ? 222 ARG B CD  1 
ATOM   3797 N  NE  . ARG B 1 222 ? -22.940 48.058  32.096  1.00 56.63  ? 222 ARG B NE  1 
ATOM   3798 C  CZ  . ARG B 1 222 ? -22.500 48.647  33.205  1.00 57.71  ? 222 ARG B CZ  1 
ATOM   3799 N  NH1 . ARG B 1 222 ? -23.310 49.410  33.923  1.00 52.58  ? 222 ARG B NH1 1 
ATOM   3800 N  NH2 . ARG B 1 222 ? -21.242 48.468  33.590  1.00 54.39  ? 222 ARG B NH2 1 
ATOM   3801 N  N   . GLU B 1 223 ? -22.018 45.289  28.167  1.00 46.31  ? 223 GLU B N   1 
ATOM   3802 C  CA  . GLU B 1 223 ? -20.957 45.786  27.312  1.00 49.24  ? 223 GLU B CA  1 
ATOM   3803 C  C   . GLU B 1 223 ? -20.822 44.868  26.102  1.00 47.38  ? 223 GLU B C   1 
ATOM   3804 O  O   . GLU B 1 223 ? -20.868 43.650  26.221  1.00 44.14  ? 223 GLU B O   1 
ATOM   3805 C  CB  . GLU B 1 223 ? -19.600 45.906  28.034  1.00 50.52  ? 223 GLU B CB  1 
ATOM   3806 C  CG  . GLU B 1 223 ? -19.545 46.698  29.337  1.00 51.74  ? 223 GLU B CG  1 
ATOM   3807 C  CD  . GLU B 1 223 ? -20.124 48.114  29.273  1.00 51.69  ? 223 GLU B CD  1 
ATOM   3808 O  OE1 . GLU B 1 223 ? -19.921 48.858  28.277  1.00 44.45  ? 223 GLU B OE1 1 
ATOM   3809 O  OE2 . GLU B 1 223 ? -20.772 48.492  30.272  1.00 55.71  ? 223 GLU B OE2 1 
ATOM   3810 N  N   . PRO B 1 224 ? -20.662 45.468  24.930  1.00 48.34  ? 224 PRO B N   1 
ATOM   3811 C  CA  . PRO B 1 224 ? -20.686 44.697  23.712  1.00 49.29  ? 224 PRO B CA  1 
ATOM   3812 C  C   . PRO B 1 224 ? -19.304 44.180  23.317  1.00 47.18  ? 224 PRO B C   1 
ATOM   3813 O  O   . PRO B 1 224 ? -18.295 44.760  23.702  1.00 51.71  ? 224 PRO B O   1 
ATOM   3814 C  CB  . PRO B 1 224 ? -21.206 45.708  22.674  1.00 50.42  ? 224 PRO B CB  1 
ATOM   3815 C  CG  . PRO B 1 224 ? -21.686 46.896  23.446  1.00 52.96  ? 224 PRO B CG  1 
ATOM   3816 C  CD  . PRO B 1 224 ? -20.847 46.908  24.679  1.00 51.81  ? 224 PRO B CD  1 
ATOM   3817 N  N   . ILE B 1 225 ? -19.274 43.081  22.579  1.00 41.83  ? 225 ILE B N   1 
ATOM   3818 C  CA  . ILE B 1 225 ? -18.084 42.642  21.846  1.00 39.52  ? 225 ILE B CA  1 
ATOM   3819 C  C   . ILE B 1 225 ? -17.828 43.702  20.790  1.00 38.02  ? 225 ILE B C   1 
ATOM   3820 O  O   . ILE B 1 225 ? -18.765 44.379  20.350  1.00 35.00  ? 225 ILE B O   1 
ATOM   3821 C  CB  . ILE B 1 225 ? -18.348 41.312  21.112  1.00 35.79  ? 225 ILE B CB  1 
ATOM   3822 C  CG1 . ILE B 1 225 ? -18.678 40.226  22.123  1.00 36.66  ? 225 ILE B CG1 1 
ATOM   3823 C  CG2 . ILE B 1 225 ? -17.180 40.881  20.221  1.00 36.23  ? 225 ILE B CG2 1 
ATOM   3824 C  CD1 . ILE B 1 225 ? -19.111 38.910  21.521  1.00 32.93  ? 225 ILE B CD1 1 
ATOM   3825 N  N   . GLN B 1 226 ? -16.565 43.855  20.391  1.00 35.62  ? 226 GLN B N   1 
ATOM   3826 C  CA  . GLN B 1 226 ? -16.236 44.660  19.227  1.00 36.55  ? 226 GLN B CA  1 
ATOM   3827 C  C   . GLN B 1 226 ? -15.582 43.805  18.144  1.00 34.34  ? 226 GLN B C   1 
ATOM   3828 O  O   . GLN B 1 226 ? -14.769 42.932  18.440  1.00 34.81  ? 226 GLN B O   1 
ATOM   3829 C  CB  . GLN B 1 226 ? -15.350 45.858  19.618  1.00 42.05  ? 226 GLN B CB  1 
ATOM   3830 C  CG  . GLN B 1 226 ? -15.973 46.710  20.728  1.00 45.34  ? 226 GLN B CG  1 
ATOM   3831 C  CD  . GLN B 1 226 ? -15.693 48.196  20.578  1.00 52.10  ? 226 GLN B CD  1 
ATOM   3832 O  OE1 . GLN B 1 226 ? -14.548 48.630  20.687  1.00 54.79  ? 226 GLN B OE1 1 
ATOM   3833 N  NE2 . GLN B 1 226 ? -16.749 48.992  20.347  1.00 52.32  ? 226 GLN B NE2 1 
ATOM   3834 N  N   . LEU B 1 227 ? -15.983 44.027  16.899  1.00 32.41  ? 227 LEU B N   1 
ATOM   3835 C  CA  . LEU B 1 227 ? -15.348 43.432  15.742  1.00 35.63  ? 227 LEU B CA  1 
ATOM   3836 C  C   . LEU B 1 227 ? -14.977 44.561  14.837  1.00 38.22  ? 227 LEU B C   1 
ATOM   3837 O  O   . LEU B 1 227 ? -15.464 45.674  15.031  1.00 39.24  ? 227 LEU B O   1 
ATOM   3838 C  CB  . LEU B 1 227 ? -16.332 42.519  14.968  1.00 36.89  ? 227 LEU B CB  1 
ATOM   3839 C  CG  . LEU B 1 227 ? -17.042 41.330  15.643  1.00 42.94  ? 227 LEU B CG  1 
ATOM   3840 C  CD1 . LEU B 1 227 ? -17.370 40.263  14.589  1.00 40.27  ? 227 LEU B CD1 1 
ATOM   3841 C  CD2 . LEU B 1 227 ? -16.338 40.677  16.841  1.00 33.58  ? 227 LEU B CD2 1 
ATOM   3842 N  N   . HIS B 1 228 ? -14.154 44.278  13.828  1.00 40.96  ? 228 HIS B N   1 
ATOM   3843 C  CA  . HIS B 1 228 ? -13.892 45.240  12.754  1.00 41.24  ? 228 HIS B CA  1 
ATOM   3844 C  C   . HIS B 1 228 ? -15.086 45.263  11.862  1.00 43.69  ? 228 HIS B C   1 
ATOM   3845 O  O   . HIS B 1 228 ? -15.727 44.229  11.659  1.00 41.03  ? 228 HIS B O   1 
ATOM   3846 C  CB  . HIS B 1 228 ? -12.666 44.824  11.948  1.00 41.48  ? 228 HIS B CB  1 
ATOM   3847 C  CG  . HIS B 1 228 ? -12.170 45.890  10.974  1.00 44.59  ? 228 HIS B CG  1 
ATOM   3848 N  ND1 . HIS B 1 228 ? -12.417 45.839  9.635   1.00 45.36  ? 228 HIS B ND1 1 
ATOM   3849 C  CD2 . HIS B 1 228 ? -11.415 47.057  11.187  1.00 44.98  ? 228 HIS B CD2 1 
ATOM   3850 C  CE1 . HIS B 1 228 ? -11.853 46.911  9.033   1.00 42.36  ? 228 HIS B CE1 1 
ATOM   3851 N  NE2 . HIS B 1 228 ? -11.249 47.658  9.981   1.00 40.99  ? 228 HIS B NE2 1 
ATOM   3852 N  N   . ARG B 1 229 ? -15.390 46.429  11.286  1.00 41.94  ? 229 ARG B N   1 
ATOM   3853 C  CA  . ARG B 1 229 ? -16.524 46.535  10.365  1.00 42.41  ? 229 ARG B CA  1 
ATOM   3854 C  C   . ARG B 1 229 ? -16.507 45.412  9.297   1.00 42.89  ? 229 ARG B C   1 
ATOM   3855 O  O   . ARG B 1 229 ? -17.504 44.726  9.099   1.00 44.72  ? 229 ARG B O   1 
ATOM   3856 C  CB  . ARG B 1 229 ? -16.614 47.939  9.754   1.00 43.65  ? 229 ARG B CB  1 
ATOM   3857 C  CG  . ARG B 1 229 ? -15.677 48.206  8.593   1.00 44.62  ? 229 ARG B CG  1 
ATOM   3858 C  CD  . ARG B 1 229 ? -15.972 49.538  7.913   1.00 50.59  ? 229 ARG B CD  1 
ATOM   3859 N  NE  . ARG B 1 229 ? -16.023 49.367  6.457   1.00 49.82  ? 229 ARG B NE  1 
ATOM   3860 C  CZ  . ARG B 1 229 ? -17.148 49.372  5.749   1.00 55.42  ? 229 ARG B CZ  1 
ATOM   3861 N  NH1 . ARG B 1 229 ? -18.314 49.561  6.360   1.00 56.12  ? 229 ARG B NH1 1 
ATOM   3862 N  NH2 . ARG B 1 229 ? -17.115 49.200  4.428   1.00 60.43  ? 229 ARG B NH2 1 
ATOM   3863 N  N   . GLU B 1 230 ? -15.365 45.213  8.642   1.00 44.37  ? 230 GLU B N   1 
ATOM   3864 C  CA  . GLU B 1 230 ? -15.193 44.163  7.626   1.00 42.34  ? 230 GLU B CA  1 
ATOM   3865 C  C   . GLU B 1 230 ? -15.368 42.728  8.141   1.00 35.78  ? 230 GLU B C   1 
ATOM   3866 O  O   . GLU B 1 230 ? -15.672 41.818  7.377   1.00 37.02  ? 230 GLU B O   1 
ATOM   3867 C  CB  . GLU B 1 230 ? -13.839 44.318  6.923   1.00 49.33  ? 230 GLU B CB  1 
ATOM   3868 C  CG  . GLU B 1 230 ? -13.797 45.427  5.863   1.00 57.28  ? 230 GLU B CG  1 
ATOM   3869 C  CD  . GLU B 1 230 ? -12.470 45.475  5.095   1.00 60.92  ? 230 GLU B CD  1 
ATOM   3870 O  OE1 . GLU B 1 230 ? -11.426 45.083  5.677   1.00 56.53  ? 230 GLU B OE1 1 
ATOM   3871 O  OE2 . GLU B 1 230 ? -12.479 45.904  3.908   1.00 59.89  ? 230 GLU B OE2 1 
ATOM   3872 N  N   . GLN B 1 231 ? -15.173 42.522  9.429   1.00 35.43  ? 231 GLN B N   1 
ATOM   3873 C  CA  . GLN B 1 231 ? -15.498 41.232  10.028  1.00 36.87  ? 231 GLN B CA  1 
ATOM   3874 C  C   . GLN B 1 231 ? -17.008 41.056  10.198  1.00 34.16  ? 231 GLN B C   1 
ATOM   3875 O  O   . GLN B 1 231 ? -17.515 39.952  10.078  1.00 36.98  ? 231 GLN B O   1 
ATOM   3876 C  CB  . GLN B 1 231 ? -14.811 41.077  11.374  1.00 38.90  ? 231 GLN B CB  1 
ATOM   3877 C  CG  . GLN B 1 231 ? -13.362 40.635  11.363  1.00 38.97  ? 231 GLN B CG  1 
ATOM   3878 C  CD  . GLN B 1 231 ? -12.802 40.677  12.764  1.00 36.49  ? 231 GLN B CD  1 
ATOM   3879 O  OE1 . GLN B 1 231 ? -12.993 41.654  13.457  1.00 40.34  ? 231 GLN B OE1 1 
ATOM   3880 N  NE2 . GLN B 1 231 ? -12.160 39.608  13.206  1.00 40.64  ? 231 GLN B NE2 1 
ATOM   3881 N  N   . ILE B 1 232 ? -17.712 42.151  10.485  1.00 36.42  ? 232 ILE B N   1 
ATOM   3882 C  CA  . ILE B 1 232 ? -19.172 42.163  10.626  1.00 34.80  ? 232 ILE B CA  1 
ATOM   3883 C  C   . ILE B 1 232 ? -19.799 42.019  9.263   1.00 37.35  ? 232 ILE B C   1 
ATOM   3884 O  O   . ILE B 1 232 ? -20.798 41.298  9.088   1.00 34.81  ? 232 ILE B O   1 
ATOM   3885 C  CB  . ILE B 1 232 ? -19.697 43.476  11.255  1.00 34.32  ? 232 ILE B CB  1 
ATOM   3886 C  CG1 . ILE B 1 232 ? -19.224 43.593  12.696  1.00 35.00  ? 232 ILE B CG1 1 
ATOM   3887 C  CG2 . ILE B 1 232 ? -21.215 43.513  11.185  1.00 36.77  ? 232 ILE B CG2 1 
ATOM   3888 C  CD1 . ILE B 1 232 ? -19.449 44.957  13.357  1.00 37.16  ? 232 ILE B CD1 1 
ATOM   3889 N  N   . LEU B 1 233 ? -19.215 42.727  8.294   1.00 38.36  ? 233 LEU B N   1 
ATOM   3890 C  CA  . LEU B 1 233 ? -19.699 42.701  6.937   1.00 37.87  ? 233 LEU B CA  1 
ATOM   3891 C  C   . LEU B 1 233 ? -19.495 41.354  6.263   1.00 40.85  ? 233 LEU B C   1 
ATOM   3892 O  O   . LEU B 1 233 ? -20.294 40.974  5.405   1.00 38.00  ? 233 LEU B O   1 
ATOM   3893 C  CB  . LEU B 1 233 ? -19.089 43.824  6.114   1.00 46.58  ? 233 LEU B CB  1 
ATOM   3894 C  CG  . LEU B 1 233 ? -19.619 45.218  6.471   1.00 47.79  ? 233 LEU B CG  1 
ATOM   3895 C  CD1 . LEU B 1 233 ? -18.773 46.277  5.781   1.00 48.09  ? 233 LEU B CD1 1 
ATOM   3896 C  CD2 . LEU B 1 233 ? -21.095 45.338  6.106   1.00 42.69  ? 233 LEU B CD2 1 
ATOM   3897 N  N   . ALA B 1 234 ? -18.457 40.617  6.658   1.00 38.65  ? 234 ALA B N   1 
ATOM   3898 C  CA  . ALA B 1 234 ? -18.237 39.309  6.023   1.00 41.84  ? 234 ALA B CA  1 
ATOM   3899 C  C   . ALA B 1 234 ? -19.423 38.379  6.210   1.00 39.95  ? 234 ALA B C   1 
ATOM   3900 O  O   . ALA B 1 234 ? -19.677 37.504  5.361   1.00 39.57  ? 234 ALA B O   1 
ATOM   3901 C  CB  . ALA B 1 234 ? -16.953 38.653  6.509   1.00 46.01  ? 234 ALA B CB  1 
ATOM   3902 N  N   . PHE B 1 235 ? -20.160 38.563  7.304   1.00 35.24  ? 235 PHE B N   1 
ATOM   3903 C  CA  . PHE B 1 235 ? -21.315 37.711  7.561   1.00 38.41  ? 235 PHE B CA  1 
ATOM   3904 C  C   . PHE B 1 235 ? -22.390 37.887  6.467   1.00 40.99  ? 235 PHE B C   1 
ATOM   3905 O  O   . PHE B 1 235 ? -23.078 36.933  6.103   1.00 37.43  ? 235 PHE B O   1 
ATOM   3906 C  CB  . PHE B 1 235 ? -21.875 37.904  8.991   1.00 35.60  ? 235 PHE B CB  1 
ATOM   3907 C  CG  . PHE B 1 235 ? -21.012 37.272  10.084  1.00 32.15  ? 235 PHE B CG  1 
ATOM   3908 C  CD1 . PHE B 1 235 ? -19.927 37.932  10.592  1.00 32.35  ? 235 PHE B CD1 1 
ATOM   3909 C  CD2 . PHE B 1 235 ? -21.306 36.028  10.575  1.00 31.65  ? 235 PHE B CD2 1 
ATOM   3910 C  CE1 . PHE B 1 235 ? -19.143 37.378  11.574  1.00 30.73  ? 235 PHE B CE1 1 
ATOM   3911 C  CE2 . PHE B 1 235 ? -20.534 35.442  11.556  1.00 31.46  ? 235 PHE B CE2 1 
ATOM   3912 C  CZ  . PHE B 1 235 ? -19.446 36.124  12.057  1.00 35.15  ? 235 PHE B CZ  1 
ATOM   3913 N  N   . SER B 1 236 ? -22.506 39.103  5.932   1.00 45.07  ? 236 SER B N   1 
ATOM   3914 C  CA  . SER B 1 236 ? -23.572 39.419  4.985   1.00 45.62  ? 236 SER B CA  1 
ATOM   3915 C  C   . SER B 1 236 ? -23.139 39.396  3.518   1.00 47.45  ? 236 SER B C   1 
ATOM   3916 O  O   . SER B 1 236 ? -23.993 39.485  2.631   1.00 44.01  ? 236 SER B O   1 
ATOM   3917 C  CB  . SER B 1 236 ? -24.210 40.772  5.322   1.00 45.32  ? 236 SER B CB  1 
ATOM   3918 O  OG  . SER B 1 236 ? -23.256 41.810  5.236   1.00 42.59  ? 236 SER B OG  1 
ATOM   3919 N  N   . GLN B 1 237 ? -21.832 39.310  3.248   1.00 47.73  ? 237 GLN B N   1 
ATOM   3920 C  CA  . GLN B 1 237 ? -21.397 39.161  1.848   1.00 48.38  ? 237 GLN B CA  1 
ATOM   3921 C  C   . GLN B 1 237 ? -20.802 37.827  1.548   1.00 44.58  ? 237 GLN B C   1 
ATOM   3922 O  O   . GLN B 1 237 ? -20.563 37.502  0.386   1.00 47.47  ? 237 GLN B O   1 
ATOM   3923 C  CB  . GLN B 1 237 ? -20.504 40.301  1.325   1.00 54.70  ? 237 GLN B CB  1 
ATOM   3924 C  CG  . GLN B 1 237 ? -19.389 40.768  2.230   1.00 54.79  ? 237 GLN B CG  1 
ATOM   3925 C  CD  . GLN B 1 237 ? -19.471 42.267  2.476   1.00 67.31  ? 237 GLN B CD  1 
ATOM   3926 O  OE1 . GLN B 1 237 ? -18.465 42.920  2.785   1.00 67.99  ? 237 GLN B OE1 1 
ATOM   3927 N  NE2 . GLN B 1 237 ? -20.685 42.825  2.355   1.00 61.91  ? 237 GLN B NE2 1 
ATOM   3928 N  N   . LYS B 1 238 ? -20.607 37.020  2.580   1.00 46.52  ? 238 LYS B N   1 
ATOM   3929 C  CA  . LYS B 1 238 ? -20.128 35.659  2.347   1.00 42.97  ? 238 LYS B CA  1 
ATOM   3930 C  C   . LYS B 1 238 ? -21.164 34.579  2.637   1.00 43.65  ? 238 LYS B C   1 
ATOM   3931 O  O   . LYS B 1 238 ? -20.928 33.408  2.326   1.00 40.73  ? 238 LYS B O   1 
ATOM   3932 C  CB  . LYS B 1 238 ? -18.813 35.394  3.108   1.00 44.36  ? 238 LYS B CB  1 
ATOM   3933 C  CG  . LYS B 1 238 ? -17.618 36.227  2.636   1.00 42.19  ? 238 LYS B CG  1 
ATOM   3934 C  CD  . LYS B 1 238 ? -16.761 35.514  1.578   1.00 44.79  ? 238 LYS B CD  1 
ATOM   3935 C  CE  . LYS B 1 238 ? -17.118 35.914  0.147   1.00 45.60  ? 238 LYS B CE  1 
ATOM   3936 N  NZ  . LYS B 1 238 ? -15.909 36.125  -0.701  1.00 45.25  ? 238 LYS B NZ  1 
ATOM   3937 N  N   . LEU B 1 239 ? -22.309 34.953  3.217   1.00 38.17  ? 239 LEU B N   1 
ATOM   3938 C  CA  . LEU B 1 239 ? -23.345 33.962  3.484   1.00 38.30  ? 239 LEU B CA  1 
ATOM   3939 C  C   . LEU B 1 239 ? -24.626 34.281  2.711   1.00 42.31  ? 239 LEU B C   1 
ATOM   3940 O  O   . LEU B 1 239 ? -24.987 35.457  2.547   1.00 43.41  ? 239 LEU B O   1 
ATOM   3941 C  CB  . LEU B 1 239 ? -23.654 33.896  4.986   1.00 38.42  ? 239 LEU B CB  1 
ATOM   3942 C  CG  . LEU B 1 239 ? -22.615 33.430  5.981   1.00 41.59  ? 239 LEU B CG  1 
ATOM   3943 C  CD1 . LEU B 1 239 ? -23.135 33.545  7.408   1.00 40.80  ? 239 LEU B CD1 1 
ATOM   3944 C  CD2 . LEU B 1 239 ? -22.254 31.985  5.685   1.00 41.10  ? 239 LEU B CD2 1 
ATOM   3945 N  N   . TYR B 1 240 ? -25.333 33.244  2.259   1.00 42.90  ? 240 TYR B N   1 
ATOM   3946 C  CA  . TYR B 1 240 ? -26.543 33.434  1.464   1.00 39.50  ? 240 TYR B CA  1 
ATOM   3947 C  C   . TYR B 1 240 ? -27.748 32.690  2.045   1.00 37.53  ? 240 TYR B C   1 
ATOM   3948 O  O   . TYR B 1 240 ? -27.591 31.609  2.605   1.00 35.51  ? 240 TYR B O   1 
ATOM   3949 C  CB  . TYR B 1 240 ? -26.324 32.982  0.020   1.00 44.80  ? 240 TYR B CB  1 
ATOM   3950 C  CG  . TYR B 1 240 ? -25.193 33.676  -0.687  1.00 48.53  ? 240 TYR B CG  1 
ATOM   3951 C  CD1 . TYR B 1 240 ? -23.906 33.165  -0.633  1.00 48.78  ? 240 TYR B CD1 1 
ATOM   3952 C  CD2 . TYR B 1 240 ? -25.409 34.854  -1.407  1.00 55.33  ? 240 TYR B CD2 1 
ATOM   3953 C  CE1 . TYR B 1 240 ? -22.852 33.810  -1.262  1.00 52.54  ? 240 TYR B CE1 1 
ATOM   3954 C  CE2 . TYR B 1 240 ? -24.360 35.502  -2.053  1.00 55.23  ? 240 TYR B CE2 1 
ATOM   3955 C  CZ  . TYR B 1 240 ? -23.085 34.969  -1.978  1.00 55.85  ? 240 TYR B CZ  1 
ATOM   3956 O  OH  . TYR B 1 240 ? -22.027 35.598  -2.611  1.00 57.92  ? 240 TYR B OH  1 
ATOM   3957 N  N   . TYR B 1 241 ? -28.943 33.285  1.902   1.00 39.05  ? 241 TYR B N   1 
ATOM   3958 C  CA  . TYR B 1 241 ? -30.221 32.637  2.261   1.00 41.90  ? 241 TYR B CA  1 
ATOM   3959 C  C   . TYR B 1 241 ? -30.590 31.535  1.248   1.00 43.36  ? 241 TYR B C   1 
ATOM   3960 O  O   . TYR B 1 241 ? -31.394 30.643  1.573   1.00 40.65  ? 241 TYR B O   1 
ATOM   3961 C  CB  . TYR B 1 241 ? -31.406 33.639  2.283   1.00 39.49  ? 241 TYR B CB  1 
ATOM   3962 C  CG  . TYR B 1 241 ? -31.630 34.463  3.553   1.00 36.75  ? 241 TYR B CG  1 
ATOM   3963 C  CD1 . TYR B 1 241 ? -31.875 33.850  4.783   1.00 35.28  ? 241 TYR B CD1 1 
ATOM   3964 C  CD2 . TYR B 1 241 ? -31.646 35.869  3.501   1.00 33.70  ? 241 TYR B CD2 1 
ATOM   3965 C  CE1 . TYR B 1 241 ? -32.110 34.598  5.923   1.00 32.54  ? 241 TYR B CE1 1 
ATOM   3966 C  CE2 . TYR B 1 241 ? -31.869 36.625  4.632   1.00 33.14  ? 241 TYR B CE2 1 
ATOM   3967 C  CZ  . TYR B 1 241 ? -32.111 35.978  5.835   1.00 35.24  ? 241 TYR B CZ  1 
ATOM   3968 O  OH  . TYR B 1 241 ? -32.328 36.729  6.949   1.00 35.20  ? 241 TYR B OH  1 
ATOM   3969 N  N   . ASP B 1 242 ? -30.039 31.631  0.025   1.00 43.17  ? 242 ASP B N   1 
ATOM   3970 C  CA  . ASP B 1 242 ? -30.335 30.675  -1.075  1.00 45.10  ? 242 ASP B CA  1 
ATOM   3971 C  C   . ASP B 1 242 ? -29.075 30.075  -1.726  1.00 46.09  ? 242 ASP B C   1 
ATOM   3972 O  O   . ASP B 1 242 ? -28.027 30.732  -1.763  1.00 46.38  ? 242 ASP B O   1 
ATOM   3973 C  CB  . ASP B 1 242 ? -31.237 31.319  -2.147  1.00 41.40  ? 242 ASP B CB  1 
ATOM   3974 C  CG  . ASP B 1 242 ? -30.493 32.327  -3.050  1.00 47.59  ? 242 ASP B CG  1 
ATOM   3975 O  OD1 . ASP B 1 242 ? -29.771 33.229  -2.561  1.00 45.12  ? 242 ASP B OD1 1 
ATOM   3976 O  OD2 . ASP B 1 242 ? -30.683 32.251  -4.276  1.00 54.44  ? 242 ASP B OD2 1 
ATOM   3977 N  N   . LYS B 1 243 ? -29.196 28.842  -2.231  1.00 46.04  ? 243 LYS B N   1 
ATOM   3978 C  CA  . LYS B 1 243 ? -28.137 28.174  -3.034  1.00 50.34  ? 243 LYS B CA  1 
ATOM   3979 C  C   . LYS B 1 243 ? -27.607 28.988  -4.213  1.00 51.03  ? 243 LYS B C   1 
ATOM   3980 O  O   . LYS B 1 243 ? -26.393 29.129  -4.364  1.00 53.14  ? 243 LYS B O   1 
ATOM   3981 C  CB  . LYS B 1 243 ? -28.594 26.807  -3.566  1.00 48.81  ? 243 LYS B CB  1 
ATOM   3982 C  CG  . LYS B 1 243 ? -28.139 25.596  -2.766  1.00 54.80  ? 243 LYS B CG  1 
ATOM   3983 C  CD  . LYS B 1 243 ? -29.011 25.429  -1.531  1.00 56.27  ? 243 LYS B CD  1 
ATOM   3984 C  CE  . LYS B 1 243 ? -29.205 23.967  -1.171  1.00 49.23  ? 243 LYS B CE  1 
ATOM   3985 N  NZ  . LYS B 1 243 ? -30.621 23.812  -0.755  1.00 50.54  ? 243 LYS B NZ  1 
ATOM   3986 N  N   . GLU B 1 244 ? -28.508 29.514  -5.044  1.00 53.15  ? 244 GLU B N   1 
ATOM   3987 C  CA  . GLU B 1 244 ? -28.113 30.210  -6.288  1.00 53.19  ? 244 GLU B CA  1 
ATOM   3988 C  C   . GLU B 1 244 ? -27.345 31.445  -5.885  1.00 58.60  ? 244 GLU B C   1 
ATOM   3989 O  O   . GLU B 1 244 ? -26.962 32.262  -6.726  1.00 64.02  ? 244 GLU B O   1 
ATOM   3990 C  CB  . GLU B 1 244 ? -29.333 30.623  -7.136  1.00 53.14  ? 244 GLU B CB  1 
ATOM   3991 C  CG  . GLU B 1 244 ? -30.364 29.535  -7.403  1.00 58.10  ? 244 GLU B CG  1 
ATOM   3992 C  CD  . GLU B 1 244 ? -30.946 28.947  -6.125  1.00 57.98  ? 244 GLU B CD  1 
ATOM   3993 O  OE1 . GLU B 1 244 ? -31.783 29.605  -5.473  1.00 61.45  ? 244 GLU B OE1 1 
ATOM   3994 O  OE2 . GLU B 1 244 ? -30.539 27.827  -5.764  1.00 57.20  ? 244 GLU B OE2 1 
ATOM   3995 N  N   . GLN B 1 245 ? -27.182 31.599  -4.572  1.00 56.65  ? 245 GLN B N   1 
ATOM   3996 C  CA  . GLN B 1 245 ? -26.329 32.618  -4.006  1.00 55.26  ? 245 GLN B CA  1 
ATOM   3997 C  C   . GLN B 1 245 ? -26.651 34.018  -4.578  1.00 58.75  ? 245 GLN B C   1 
ATOM   3998 O  O   . GLN B 1 245 ? -25.749 34.792  -4.942  1.00 58.06  ? 245 GLN B O   1 
ATOM   3999 C  CB  . GLN B 1 245 ? -24.853 32.169  -4.130  1.00 52.68  ? 245 GLN B CB  1 
ATOM   4000 C  CG  . GLN B 1 245 ? -24.638 30.892  -3.322  1.00 52.26  ? 245 GLN B CG  1 
ATOM   4001 C  CD  . GLN B 1 245 ? -23.243 30.284  -3.353  1.00 55.38  ? 245 GLN B CD  1 
ATOM   4002 O  OE1 . GLN B 1 245 ? -23.097 29.099  -3.633  1.00 54.80  ? 245 GLN B OE1 1 
ATOM   4003 N  NE2 . GLN B 1 245 ? -22.229 31.067  -3.029  1.00 52.98  ? 245 GLN B NE2 1 
ATOM   4004 N  N   . THR B 1 246 ? -27.956 34.326  -4.636  1.00 55.36  ? 246 THR B N   1 
ATOM   4005 C  CA  . THR B 1 246 ? -28.440 35.651  -5.064  1.00 56.44  ? 246 THR B CA  1 
ATOM   4006 C  C   . THR B 1 246 ? -28.941 36.520  -3.904  1.00 54.85  ? 246 THR B C   1 
ATOM   4007 O  O   . THR B 1 246 ? -28.982 37.745  -4.026  1.00 52.08  ? 246 THR B O   1 
ATOM   4008 C  CB  . THR B 1 246 ? -29.577 35.568  -6.107  1.00 53.38  ? 246 THR B CB  1 
ATOM   4009 O  OG1 . THR B 1 246 ? -30.794 35.155  -5.475  1.00 58.02  ? 246 THR B OG1 1 
ATOM   4010 C  CG2 . THR B 1 246 ? -29.238 34.602  -7.231  1.00 54.61  ? 246 THR B CG2 1 
ATOM   4011 N  N   . VAL B 1 247 ? -29.333 35.877  -2.804  1.00 52.13  ? 247 VAL B N   1 
ATOM   4012 C  CA  . VAL B 1 247 ? -29.863 36.567  -1.619  1.00 49.13  ? 247 VAL B CA  1 
ATOM   4013 C  C   . VAL B 1 247 ? -28.919 36.483  -0.438  1.00 47.63  ? 247 VAL B C   1 
ATOM   4014 O  O   . VAL B 1 247 ? -28.712 35.407  0.146   1.00 44.12  ? 247 VAL B O   1 
ATOM   4015 C  CB  . VAL B 1 247 ? -31.253 36.023  -1.240  1.00 52.06  ? 247 VAL B CB  1 
ATOM   4016 C  CG1 . VAL B 1 247 ? -31.855 36.807  -0.084  1.00 47.60  ? 247 VAL B CG1 1 
ATOM   4017 C  CG2 . VAL B 1 247 ? -32.161 36.076  -2.462  1.00 55.95  ? 247 VAL B CG2 1 
ATOM   4018 N  N   . SER B 1 248 ? -28.341 37.634  -0.100  1.00 47.25  ? 248 SER B N   1 
ATOM   4019 C  CA  . SER B 1 248 ? -27.403 37.748  1.013   1.00 46.49  ? 248 SER B CA  1 
ATOM   4020 C  C   . SER B 1 248 ? -28.104 37.439  2.323   1.00 41.23  ? 248 SER B C   1 
ATOM   4021 O  O   . SER B 1 248 ? -29.214 37.935  2.556   1.00 37.98  ? 248 SER B O   1 
ATOM   4022 C  CB  . SER B 1 248 ? -26.851 39.168  1.083   1.00 49.70  ? 248 SER B CB  1 
ATOM   4023 O  OG  . SER B 1 248 ? -26.407 39.574  -0.195  1.00 60.72  ? 248 SER B OG  1 
ATOM   4024 N  N   . MET B 1 249 ? -27.471 36.634  3.177   1.00 34.06  ? 249 MET B N   1 
ATOM   4025 C  CA  . MET B 1 249 ? -28.032 36.393  4.515   1.00 33.94  ? 249 MET B CA  1 
ATOM   4026 C  C   . MET B 1 249 ? -27.824 37.641  5.396   1.00 34.37  ? 249 MET B C   1 
ATOM   4027 O  O   . MET B 1 249 ? -26.708 38.006  5.705   1.00 34.48  ? 249 MET B O   1 
ATOM   4028 C  CB  . MET B 1 249 ? -27.434 35.129  5.150   1.00 32.17  ? 249 MET B CB  1 
ATOM   4029 C  CG  . MET B 1 249 ? -27.889 34.856  6.585   1.00 29.35  ? 249 MET B CG  1 
ATOM   4030 S  SD  . MET B 1 249 ? -27.302 33.257  7.197   1.00 30.33  ? 249 MET B SD  1 
ATOM   4031 C  CE  . MET B 1 249 ? -27.981 32.205  5.936   1.00 27.76  ? 249 MET B CE  1 
ATOM   4032 N  N   . LYS B 1 250 ? -28.913 38.324  5.749   1.00 36.60  ? 250 LYS B N   1 
ATOM   4033 C  CA  . LYS B 1 250 ? -28.863 39.427  6.694   1.00 35.49  ? 250 LYS B CA  1 
ATOM   4034 C  C   . LYS B 1 250 ? -30.258 39.754  7.167   1.00 33.29  ? 250 LYS B C   1 
ATOM   4035 O  O   . LYS B 1 250 ? -31.227 39.198  6.656   1.00 38.65  ? 250 LYS B O   1 
ATOM   4036 C  CB  . LYS B 1 250 ? -28.132 40.669  6.126   1.00 37.82  ? 250 LYS B CB  1 
ATOM   4037 C  CG  . LYS B 1 250 ? -28.993 41.621  5.332   1.00 45.61  ? 250 LYS B CG  1 
ATOM   4038 C  CD  . LYS B 1 250 ? -28.154 42.323  4.263   1.00 48.92  ? 250 LYS B CD  1 
ATOM   4039 C  CE  . LYS B 1 250 ? -29.015 43.012  3.212   1.00 49.08  ? 250 LYS B CE  1 
ATOM   4040 N  NZ  . LYS B 1 250 ? -28.117 43.567  2.155   1.00 48.92  ? 250 LYS B NZ  1 
ATOM   4041 N  N   . ASP B 1 251 ? -30.352 40.617  8.179   1.00 33.49  ? 251 ASP B N   1 
ATOM   4042 C  CA  . ASP B 1 251 ? -31.607 40.918  8.872   1.00 32.01  ? 251 ASP B CA  1 
ATOM   4043 C  C   . ASP B 1 251 ? -32.363 39.658  9.243   1.00 31.12  ? 251 ASP B C   1 
ATOM   4044 O  O   . ASP B 1 251 ? -33.605 39.589  9.198   1.00 28.65  ? 251 ASP B O   1 
ATOM   4045 C  CB  . ASP B 1 251 ? -32.438 41.958  8.111   1.00 33.26  ? 251 ASP B CB  1 
ATOM   4046 C  CG  . ASP B 1 251 ? -31.617 43.222  7.825   1.00 37.07  ? 251 ASP B CG  1 
ATOM   4047 O  OD1 . ASP B 1 251 ? -31.375 43.995  8.762   1.00 38.44  ? 251 ASP B OD1 1 
ATOM   4048 O  OD2 . ASP B 1 251 ? -31.186 43.421  6.673   1.00 39.28  ? 251 ASP B OD2 1 
ATOM   4049 N  N   . ASN B 1 252 ? -31.575 38.654  9.619   1.00 27.13  ? 252 ASN B N   1 
ATOM   4050 C  CA  . ASN B 1 252 ? -32.102 37.449  10.206  1.00 28.62  ? 252 ASN B CA  1 
ATOM   4051 C  C   . ASN B 1 252 ? -32.419 37.677  11.697  1.00 28.96  ? 252 ASN B C   1 
ATOM   4052 O  O   . ASN B 1 252 ? -31.810 37.037  12.563  1.00 33.64  ? 252 ASN B O   1 
ATOM   4053 C  CB  . ASN B 1 252 ? -31.102 36.310  10.034  1.00 25.20  ? 252 ASN B CB  1 
ATOM   4054 C  CG  . ASN B 1 252 ? -29.693 36.639  10.584  1.00 27.69  ? 252 ASN B CG  1 
ATOM   4055 O  OD1 . ASN B 1 252 ? -29.332 37.812  10.850  1.00 27.05  ? 252 ASN B OD1 1 
ATOM   4056 N  ND2 . ASN B 1 252 ? -28.888 35.583  10.767  1.00 26.22  ? 252 ASN B ND2 1 
ATOM   4057 N  N   . VAL B 1 253 ? -33.366 38.573  11.991  1.00 29.29  ? 253 VAL B N   1 
ATOM   4058 C  CA  . VAL B 1 253 ? -33.697 38.941  13.387  1.00 28.91  ? 253 VAL B CA  1 
ATOM   4059 C  C   . VAL B 1 253 ? -35.212 39.074  13.641  1.00 29.76  ? 253 VAL B C   1 
ATOM   4060 O  O   . VAL B 1 253 ? -35.923 39.813  12.975  1.00 33.63  ? 253 VAL B O   1 
ATOM   4061 C  CB  . VAL B 1 253 ? -32.838 40.164  13.906  1.00 33.06  ? 253 VAL B CB  1 
ATOM   4062 C  CG1 . VAL B 1 253 ? -31.893 40.701  12.836  1.00 32.22  ? 253 VAL B CG1 1 
ATOM   4063 C  CG2 . VAL B 1 253 ? -33.656 41.305  14.522  1.00 28.67  ? 253 VAL B CG2 1 
ATOM   4064 N  N   . ARG B 1 254 ? -35.700 38.321  14.589  1.00 27.53  ? 254 ARG B N   1 
ATOM   4065 C  CA  . ARG B 1 254 ? -37.090 38.409  15.024  1.00 28.97  ? 254 ARG B CA  1 
ATOM   4066 C  C   . ARG B 1 254 ? -37.429 39.865  15.426  1.00 28.81  ? 254 ARG B C   1 
ATOM   4067 O  O   . ARG B 1 254 ? -36.591 40.517  16.008  1.00 32.83  ? 254 ARG B O   1 
ATOM   4068 C  CB  . ARG B 1 254 ? -37.277 37.470  16.224  1.00 27.64  ? 254 ARG B CB  1 
ATOM   4069 C  CG  . ARG B 1 254 ? -38.730 37.443  16.678  1.00 30.00  ? 254 ARG B CG  1 
ATOM   4070 C  CD  . ARG B 1 254 ? -39.025 36.366  17.666  1.00 31.25  ? 254 ARG B CD  1 
ATOM   4071 N  NE  . ARG B 1 254 ? -40.468 36.131  17.673  1.00 30.61  ? 254 ARG B NE  1 
ATOM   4072 C  CZ  . ARG B 1 254 ? -41.090 35.411  18.588  1.00 30.07  ? 254 ARG B CZ  1 
ATOM   4073 N  NH1 . ARG B 1 254 ? -40.417 34.888  19.602  1.00 27.95  ? 254 ARG B NH1 1 
ATOM   4074 N  NH2 . ARG B 1 254 ? -42.392 35.235  18.496  1.00 34.63  ? 254 ARG B NH2 1 
ATOM   4075 N  N   . PRO B 1 255 ? -38.639 40.374  15.105  1.00 30.20  ? 255 PRO B N   1 
ATOM   4076 C  CA  . PRO B 1 255 ? -38.978 41.732  15.565  1.00 32.93  ? 255 PRO B CA  1 
ATOM   4077 C  C   . PRO B 1 255 ? -39.129 41.729  17.076  1.00 30.49  ? 255 PRO B C   1 
ATOM   4078 O  O   . PRO B 1 255 ? -39.367 40.667  17.657  1.00 33.01  ? 255 PRO B O   1 
ATOM   4079 C  CB  . PRO B 1 255 ? -40.329 42.041  14.877  1.00 32.64  ? 255 PRO B CB  1 
ATOM   4080 C  CG  . PRO B 1 255 ? -40.601 40.890  13.942  1.00 31.94  ? 255 PRO B CG  1 
ATOM   4081 C  CD  . PRO B 1 255 ? -39.756 39.737  14.381  1.00 30.39  ? 255 PRO B CD  1 
ATOM   4082 N  N   . LEU B 1 256 ? -38.959 42.889  17.709  1.00 30.80  ? 256 LEU B N   1 
ATOM   4083 C  CA  . LEU B 1 256 ? -39.180 43.021  19.160  1.00 30.91  ? 256 LEU B CA  1 
ATOM   4084 C  C   . LEU B 1 256 ? -40.535 42.536  19.600  1.00 33.79  ? 256 LEU B C   1 
ATOM   4085 O  O   . LEU B 1 256 ? -41.506 42.646  18.863  1.00 34.24  ? 256 LEU B O   1 
ATOM   4086 C  CB  . LEU B 1 256 ? -38.978 44.465  19.639  1.00 29.18  ? 256 LEU B CB  1 
ATOM   4087 C  CG  . LEU B 1 256 ? -37.558 44.946  19.614  1.00 25.71  ? 256 LEU B CG  1 
ATOM   4088 C  CD1 . LEU B 1 256 ? -37.416 46.432  19.848  1.00 25.07  ? 256 LEU B CD1 1 
ATOM   4089 C  CD2 . LEU B 1 256 ? -36.827 44.135  20.687  1.00 28.86  ? 256 LEU B CD2 1 
ATOM   4090 N  N   . GLN B 1 257 ? -40.579 42.015  20.821  1.00 36.22  ? 257 GLN B N   1 
ATOM   4091 C  CA  . GLN B 1 257 ? -41.773 41.470  21.432  1.00 35.80  ? 257 GLN B CA  1 
ATOM   4092 C  C   . GLN B 1 257 ? -42.049 42.231  22.721  1.00 42.20  ? 257 GLN B C   1 
ATOM   4093 O  O   . GLN B 1 257 ? -41.129 42.796  23.341  1.00 51.31  ? 257 GLN B O   1 
ATOM   4094 C  CB  . GLN B 1 257 ? -41.580 39.968  21.723  1.00 35.06  ? 257 GLN B CB  1 
ATOM   4095 C  CG  . GLN B 1 257 ? -41.184 39.145  20.516  1.00 34.28  ? 257 GLN B CG  1 
ATOM   4096 C  CD  . GLN B 1 257 ? -42.274 39.138  19.461  1.00 36.49  ? 257 GLN B CD  1 
ATOM   4097 O  OE1 . GLN B 1 257 ? -43.395 38.727  19.736  1.00 41.62  ? 257 GLN B OE1 1 
ATOM   4098 N  NE2 . GLN B 1 257 ? -41.965 39.630  18.271  1.00 34.87  ? 257 GLN B NE2 1 
ATOM   4099 N  N   . GLN B 1 258 ? -43.297 42.244  23.156  1.00 44.61  ? 258 GLN B N   1 
ATOM   4100 C  CA  . GLN B 1 258 ? -43.666 43.149  24.249  1.00 46.13  ? 258 GLN B CA  1 
ATOM   4101 C  C   . GLN B 1 258 ? -43.480 42.449  25.593  1.00 43.63  ? 258 GLN B C   1 
ATOM   4102 O  O   . GLN B 1 258 ? -43.735 41.247  25.725  1.00 44.75  ? 258 GLN B O   1 
ATOM   4103 C  CB  . GLN B 1 258 ? -45.078 43.711  24.025  1.00 50.39  ? 258 GLN B CB  1 
ATOM   4104 C  CG  . GLN B 1 258 ? -45.281 45.185  24.371  1.00 59.20  ? 258 GLN B CG  1 
ATOM   4105 C  CD  . GLN B 1 258 ? -46.191 45.356  25.594  1.00 61.95  ? 258 GLN B CD  1 
ATOM   4106 O  OE1 . GLN B 1 258 ? -47.398 45.591  25.449  1.00 60.88  ? 258 GLN B OE1 1 
ATOM   4107 N  NE2 . GLN B 1 258 ? -45.624 45.197  26.801  1.00 56.24  ? 258 GLN B NE2 1 
ATOM   4108 N  N   . LEU B 1 259 ? -42.987 43.196  26.575  1.00 41.94  ? 259 LEU B N   1 
ATOM   4109 C  CA  . LEU B 1 259 ? -42.640 42.643  27.876  1.00 39.51  ? 259 LEU B CA  1 
ATOM   4110 C  C   . LEU B 1 259 ? -43.818 41.985  28.625  1.00 39.07  ? 259 LEU B C   1 
ATOM   4111 O  O   . LEU B 1 259 ? -43.672 40.871  29.187  1.00 35.15  ? 259 LEU B O   1 
ATOM   4112 C  CB  . LEU B 1 259 ? -41.957 43.712  28.725  1.00 39.73  ? 259 LEU B CB  1 
ATOM   4113 C  CG  . LEU B 1 259 ? -41.303 43.245  30.039  1.00 46.45  ? 259 LEU B CG  1 
ATOM   4114 C  CD1 . LEU B 1 259 ? -40.283 42.123  29.836  1.00 44.34  ? 259 LEU B CD1 1 
ATOM   4115 C  CD2 . LEU B 1 259 ? -40.700 44.384  30.864  1.00 46.00  ? 259 LEU B CD2 1 
ATOM   4116 N  N   . GLY B 1 260 ? -44.982 42.643  28.622  1.00 38.76  ? 260 GLY B N   1 
ATOM   4117 C  CA  . GLY B 1 260 ? -46.140 42.175  29.438  1.00 38.87  ? 260 GLY B CA  1 
ATOM   4118 C  C   . GLY B 1 260 ? -45.855 42.196  30.940  1.00 38.67  ? 260 GLY B C   1 
ATOM   4119 O  O   . GLY B 1 260 ? -45.320 43.178  31.447  1.00 35.56  ? 260 GLY B O   1 
ATOM   4120 N  N   . GLN B 1 261 ? -46.164 41.085  31.621  1.00 41.23  ? 261 GLN B N   1 
ATOM   4121 C  CA  . GLN B 1 261 ? -46.069 40.953  33.088  1.00 48.73  ? 261 GLN B CA  1 
ATOM   4122 C  C   . GLN B 1 261 ? -44.667 40.848  33.684  1.00 53.48  ? 261 GLN B C   1 
ATOM   4123 O  O   . GLN B 1 261 ? -44.479 41.082  34.881  1.00 55.42  ? 261 GLN B O   1 
ATOM   4124 C  CB  . GLN B 1 261 ? -46.876 39.744  33.597  1.00 53.25  ? 261 GLN B CB  1 
ATOM   4125 C  CG  . GLN B 1 261 ? -48.393 39.927  33.671  1.00 54.65  ? 261 GLN B CG  1 
ATOM   4126 C  CD  . GLN B 1 261 ? -48.814 41.311  34.156  1.00 59.03  ? 261 GLN B CD  1 
ATOM   4127 O  OE1 . GLN B 1 261 ? -48.795 41.607  35.365  1.00 60.59  ? 261 GLN B OE1 1 
ATOM   4128 N  NE2 . GLN B 1 261 ? -49.194 42.174  33.207  1.00 52.04  ? 261 GLN B NE2 1 
ATOM   4129 N  N   . ARG B 1 262 ? -43.692 40.503  32.852  1.00 50.62  ? 262 ARG B N   1 
ATOM   4130 C  CA  . ARG B 1 262 ? -42.332 40.215  33.310  1.00 45.64  ? 262 ARG B CA  1 
ATOM   4131 C  C   . ARG B 1 262 ? -41.535 41.486  33.684  1.00 46.74  ? 262 ARG B C   1 
ATOM   4132 O  O   . ARG B 1 262 ? -41.830 42.579  33.192  1.00 48.56  ? 262 ARG B O   1 
ATOM   4133 C  CB  . ARG B 1 262 ? -41.587 39.447  32.215  1.00 39.77  ? 262 ARG B CB  1 
ATOM   4134 C  CG  . ARG B 1 262 ? -42.363 38.350  31.502  1.00 36.76  ? 262 ARG B CG  1 
ATOM   4135 C  CD  . ARG B 1 262 ? -41.600 37.799  30.283  1.00 35.15  ? 262 ARG B CD  1 
ATOM   4136 N  NE  . ARG B 1 262 ? -41.840 38.607  29.087  1.00 32.08  ? 262 ARG B NE  1 
ATOM   4137 C  CZ  . ARG B 1 262 ? -41.317 38.379  27.884  1.00 33.28  ? 262 ARG B CZ  1 
ATOM   4138 N  NH1 . ARG B 1 262 ? -40.502 37.369  27.692  1.00 29.41  ? 262 ARG B NH1 1 
ATOM   4139 N  NH2 . ARG B 1 262 ? -41.607 39.169  26.860  1.00 32.76  ? 262 ARG B NH2 1 
ATOM   4140 N  N   . THR B 1 263 ? -40.543 41.342  34.566  1.00 44.50  ? 263 THR B N   1 
ATOM   4141 C  CA  . THR B 1 263 ? -39.536 42.381  34.750  1.00 40.97  ? 263 THR B CA  1 
ATOM   4142 C  C   . THR B 1 263 ? -38.210 41.811  34.314  1.00 38.94  ? 263 THR B C   1 
ATOM   4143 O  O   . THR B 1 263 ? -38.012 40.596  34.328  1.00 36.63  ? 263 THR B O   1 
ATOM   4144 C  CB  . THR B 1 263 ? -39.372 42.870  36.223  1.00 43.66  ? 263 THR B CB  1 
ATOM   4145 O  OG1 . THR B 1 263 ? -39.119 41.754  37.079  1.00 46.98  ? 263 THR B OG1 1 
ATOM   4146 C  CG2 . THR B 1 263 ? -40.609 43.619  36.717  1.00 43.63  ? 263 THR B CG2 1 
ATOM   4147 N  N   . VAL B 1 264 ? -37.322 42.708  33.890  1.00 41.16  ? 264 VAL B N   1 
ATOM   4148 C  CA  . VAL B 1 264 ? -35.916 42.453  33.828  1.00 38.96  ? 264 VAL B CA  1 
ATOM   4149 C  C   . VAL B 1 264 ? -35.307 42.744  35.219  1.00 45.35  ? 264 VAL B C   1 
ATOM   4150 O  O   . VAL B 1 264 ? -35.835 43.592  35.957  1.00 44.04  ? 264 VAL B O   1 
ATOM   4151 C  CB  . VAL B 1 264 ? -35.271 43.374  32.789  1.00 40.18  ? 264 VAL B CB  1 
ATOM   4152 C  CG1 . VAL B 1 264 ? -33.874 42.874  32.442  1.00 38.83  ? 264 VAL B CG1 1 
ATOM   4153 C  CG2 . VAL B 1 264 ? -36.128 43.449  31.545  1.00 40.01  ? 264 VAL B CG2 1 
ATOM   4154 N  N   . ILE B 1 265 ? -34.237 42.010  35.576  1.00 43.62  ? 265 ILE B N   1 
ATOM   4155 C  CA  . ILE B 1 265 ? -33.317 42.356  36.684  1.00 43.45  ? 265 ILE B CA  1 
ATOM   4156 C  C   . ILE B 1 265 ? -31.868 42.388  36.229  1.00 44.12  ? 265 ILE B C   1 
ATOM   4157 O  O   . ILE B 1 265 ? -31.529 41.861  35.177  1.00 48.07  ? 265 ILE B O   1 
ATOM   4158 C  CB  . ILE B 1 265 ? -33.409 41.394  37.886  1.00 44.90  ? 265 ILE B CB  1 
ATOM   4159 C  CG1 . ILE B 1 265 ? -33.363 39.931  37.399  1.00 41.17  ? 265 ILE B CG1 1 
ATOM   4160 C  CG2 . ILE B 1 265 ? -34.623 41.777  38.731  1.00 45.23  ? 265 ILE B CG2 1 
ATOM   4161 C  CD1 . ILE B 1 265 ? -33.209 38.862  38.462  1.00 43.05  ? 265 ILE B CD1 1 
ATOM   4162 N  N   . LYS B 1 266 ? -31.004 43.034  37.003  1.00 46.03  ? 266 LYS B N   1 
ATOM   4163 C  CA  . LYS B 1 266 ? -29.601 43.144  36.617  1.00 45.92  ? 266 LYS B CA  1 
ATOM   4164 C  C   . LYS B 1 266 ? -28.610 42.810  37.732  1.00 48.55  ? 266 LYS B C   1 
ATOM   4165 O  O   . LYS B 1 266 ? -28.908 42.994  38.907  1.00 55.07  ? 266 LYS B O   1 
ATOM   4166 C  CB  . LYS B 1 266 ? -29.306 44.510  35.987  1.00 47.30  ? 266 LYS B CB  1 
ATOM   4167 C  CG  . LYS B 1 266 ? -29.640 45.725  36.835  1.00 51.89  ? 266 LYS B CG  1 
ATOM   4168 C  CD  . LYS B 1 266 ? -29.408 47.003  36.032  1.00 50.86  ? 266 LYS B CD  1 
ATOM   4169 C  CE  . LYS B 1 266 ? -29.373 48.223  36.934  1.00 53.82  ? 266 LYS B CE  1 
ATOM   4170 N  NZ  . LYS B 1 266 ? -28.823 49.386  36.176  1.00 52.82  ? 266 LYS B NZ  1 
ATOM   4171 N  N   . SER B 1 267 ? -27.436 42.314  37.347  1.00 45.81  ? 267 SER B N   1 
ATOM   4172 C  CA  . SER B 1 267 ? -26.388 41.956  38.293  1.00 47.72  ? 267 SER B CA  1 
ATOM   4173 C  C   . SER B 1 267 ? -25.797 43.182  39.018  1.00 48.16  ? 267 SER B C   1 
ATOM   4174 O  O   . SER B 1 267 ? -25.911 44.338  38.570  1.00 43.42  ? 267 SER B O   1 
ATOM   4175 C  CB  . SER B 1 267 ? -25.265 41.187  37.593  1.00 46.83  ? 267 SER B CB  1 
ATOM   4176 O  OG  . SER B 1 267 ? -24.573 42.026  36.685  1.00 43.48  ? 267 SER B OG  1 
ATOM   4177 O  OXT . SER B 1 267 ? -25.180 43.005  40.078  1.00 51.36  ? 267 SER B OXT 1 
ATOM   4178 N  N   . GLU C 1 3   ? -48.818 63.029  -10.111 1.00 101.01 ? 3   GLU C N   1 
ATOM   4179 C  CA  . GLU C 1 3   ? -48.466 62.524  -8.753  1.00 106.85 ? 3   GLU C CA  1 
ATOM   4180 C  C   . GLU C 1 3   ? -49.561 62.845  -7.728  1.00 109.56 ? 3   GLU C C   1 
ATOM   4181 O  O   . GLU C 1 3   ? -50.294 63.826  -7.869  1.00 111.07 ? 3   GLU C O   1 
ATOM   4182 C  CB  . GLU C 1 3   ? -47.131 63.121  -8.293  1.00 105.68 ? 3   GLU C CB  1 
ATOM   4183 C  CG  . GLU C 1 3   ? -46.497 62.401  -7.108  1.00 106.28 ? 3   GLU C CG  1 
ATOM   4184 C  CD  . GLU C 1 3   ? -45.708 63.319  -6.188  1.00 104.05 ? 3   GLU C CD  1 
ATOM   4185 O  OE1 . GLU C 1 3   ? -46.031 64.525  -6.098  1.00 100.50 ? 3   GLU C OE1 1 
ATOM   4186 O  OE2 . GLU C 1 3   ? -44.767 62.821  -5.536  1.00 99.03  ? 3   GLU C OE2 1 
ATOM   4187 N  N   . SER C 1 4   ? -49.664 62.003  -6.702  1.00 109.78 ? 4   SER C N   1 
ATOM   4188 C  CA  . SER C 1 4   ? -50.532 62.262  -5.558  1.00 103.01 ? 4   SER C CA  1 
ATOM   4189 C  C   . SER C 1 4   ? -49.709 62.746  -4.349  1.00 104.10 ? 4   SER C C   1 
ATOM   4190 O  O   . SER C 1 4   ? -48.520 63.065  -4.477  1.00 101.70 ? 4   SER C O   1 
ATOM   4191 C  CB  . SER C 1 4   ? -51.341 61.009  -5.214  1.00 99.64  ? 4   SER C CB  1 
ATOM   4192 O  OG  . SER C 1 4   ? -50.491 59.961  -4.794  1.00 94.20  ? 4   SER C OG  1 
ATOM   4193 N  N   . HIS C 1 5   ? -50.343 62.793  -3.180  1.00 101.45 ? 5   HIS C N   1 
ATOM   4194 C  CA  . HIS C 1 5   ? -49.713 63.334  -1.978  1.00 92.74  ? 5   HIS C CA  1 
ATOM   4195 C  C   . HIS C 1 5   ? -48.924 62.293  -1.223  1.00 87.54  ? 5   HIS C C   1 
ATOM   4196 O  O   . HIS C 1 5   ? -48.760 61.154  -1.686  1.00 79.32  ? 5   HIS C O   1 
ATOM   4197 C  CB  . HIS C 1 5   ? -50.761 63.987  -1.072  1.00 100.60 ? 5   HIS C CB  1 
ATOM   4198 C  CG  . HIS C 1 5   ? -51.846 64.739  -1.824  1.00 109.68 ? 5   HIS C CG  1 
ATOM   4199 N  ND1 . HIS C 1 5   ? -51.584 65.534  -2.886  1.00 111.20 ? 5   HIS C ND1 1 
ATOM   4200 C  CD2 . HIS C 1 5   ? -53.225 64.805  -1.617  1.00 112.08 ? 5   HIS C CD2 1 
ATOM   4201 C  CE1 . HIS C 1 5   ? -52.734 66.069  -3.341  1.00 111.71 ? 5   HIS C CE1 1 
ATOM   4202 N  NE2 . HIS C 1 5   ? -53.738 65.626  -2.562  1.00 110.34 ? 5   HIS C NE2 1 
ATOM   4203 N  N   . TRP C 1 6   ? -48.423 62.689  -0.052  1.00 76.86  ? 6   TRP C N   1 
ATOM   4204 C  CA  . TRP C 1 6   ? -47.682 61.800  0.838   1.00 64.13  ? 6   TRP C CA  1 
ATOM   4205 C  C   . TRP C 1 6   ? -48.627 61.200  1.845   1.00 60.79  ? 6   TRP C C   1 
ATOM   4206 O  O   . TRP C 1 6   ? -49.737 61.705  2.025   1.00 58.12  ? 6   TRP C O   1 
ATOM   4207 C  CB  . TRP C 1 6   ? -46.589 62.573  1.552   1.00 63.08  ? 6   TRP C CB  1 
ATOM   4208 C  CG  . TRP C 1 6   ? -47.093 63.755  2.364   1.00 62.52  ? 6   TRP C CG  1 
ATOM   4209 C  CD1 . TRP C 1 6   ? -47.177 65.086  1.967   1.00 61.39  ? 6   TRP C CD1 1 
ATOM   4210 C  CD2 . TRP C 1 6   ? -47.596 63.742  3.754   1.00 58.66  ? 6   TRP C CD2 1 
ATOM   4211 N  NE1 . TRP C 1 6   ? -47.683 65.871  2.975   1.00 60.88  ? 6   TRP C NE1 1 
ATOM   4212 C  CE2 . TRP C 1 6   ? -47.955 65.129  4.073   1.00 61.34  ? 6   TRP C CE2 1 
ATOM   4213 C  CE3 . TRP C 1 6   ? -47.780 62.761  4.724   1.00 53.82  ? 6   TRP C CE3 1 
ATOM   4214 C  CZ2 . TRP C 1 6   ? -48.471 65.487  5.312   1.00 56.55  ? 6   TRP C CZ2 1 
ATOM   4215 C  CZ3 . TRP C 1 6   ? -48.300 63.138  5.965   1.00 52.61  ? 6   TRP C CZ3 1 
ATOM   4216 C  CH2 . TRP C 1 6   ? -48.637 64.469  6.250   1.00 56.43  ? 6   TRP C CH2 1 
ATOM   4217 N  N   . CYS C 1 7   ? -48.192 60.129  2.514   1.00 57.48  ? 7   CYS C N   1 
ATOM   4218 C  CA  . CYS C 1 7   ? -48.960 59.517  3.608   1.00 62.58  ? 7   CYS C CA  1 
ATOM   4219 C  C   . CYS C 1 7   ? -48.115 58.741  4.638   1.00 59.04  ? 7   CYS C C   1 
ATOM   4220 O  O   . CYS C 1 7   ? -46.890 58.605  4.499   1.00 60.58  ? 7   CYS C O   1 
ATOM   4221 C  CB  . CYS C 1 7   ? -50.036 58.591  3.034   1.00 62.72  ? 7   CYS C CB  1 
ATOM   4222 S  SG  . CYS C 1 7   ? -49.339 57.171  2.178   1.00 63.64  ? 7   CYS C SG  1 
ATOM   4223 N  N   . TYR C 1 8   ? -48.796 58.244  5.669   1.00 54.79  ? 8   TYR C N   1 
ATOM   4224 C  CA  . TYR C 1 8   ? -48.233 57.270  6.599   1.00 56.90  ? 8   TYR C CA  1 
ATOM   4225 C  C   . TYR C 1 8   ? -48.399 55.829  6.106   1.00 60.54  ? 8   TYR C C   1 
ATOM   4226 O  O   . TYR C 1 8   ? -49.333 55.523  5.373   1.00 63.63  ? 8   TYR C O   1 
ATOM   4227 C  CB  . TYR C 1 8   ? -48.896 57.421  7.963   1.00 52.11  ? 8   TYR C CB  1 
ATOM   4228 C  CG  . TYR C 1 8   ? -48.705 58.794  8.574   1.00 53.53  ? 8   TYR C CG  1 
ATOM   4229 C  CD1 . TYR C 1 8   ? -47.446 59.235  8.985   1.00 52.15  ? 8   TYR C CD1 1 
ATOM   4230 C  CD2 . TYR C 1 8   ? -49.795 59.656  8.750   1.00 55.80  ? 8   TYR C CD2 1 
ATOM   4231 C  CE1 . TYR C 1 8   ? -47.280 60.495  9.558   1.00 54.73  ? 8   TYR C CE1 1 
ATOM   4232 C  CE2 . TYR C 1 8   ? -49.637 60.915  9.321   1.00 55.38  ? 8   TYR C CE2 1 
ATOM   4233 C  CZ  . TYR C 1 8   ? -48.383 61.324  9.722   1.00 51.72  ? 8   TYR C CZ  1 
ATOM   4234 O  OH  . TYR C 1 8   ? -48.249 62.566  10.284  1.00 58.39  ? 8   TYR C OH  1 
ATOM   4235 N  N   . GLU C 1 9   ? -47.485 54.953  6.506   1.00 63.30  ? 9   GLU C N   1 
ATOM   4236 C  CA  . GLU C 1 9   ? -47.609 53.502  6.321   1.00 68.39  ? 9   GLU C CA  1 
ATOM   4237 C  C   . GLU C 1 9   ? -49.048 52.973  6.346   1.00 67.72  ? 9   GLU C C   1 
ATOM   4238 O  O   . GLU C 1 9   ? -49.463 52.236  5.453   1.00 69.90  ? 9   GLU C O   1 
ATOM   4239 C  CB  . GLU C 1 9   ? -46.893 52.799  7.485   1.00 73.35  ? 9   GLU C CB  1 
ATOM   4240 C  CG  . GLU C 1 9   ? -45.884 51.733  7.107   1.00 77.21  ? 9   GLU C CG  1 
ATOM   4241 C  CD  . GLU C 1 9   ? -44.523 52.331  6.823   1.00 85.73  ? 9   GLU C CD  1 
ATOM   4242 O  OE1 . GLU C 1 9   ? -43.964 53.011  7.724   1.00 86.66  ? 9   GLU C OE1 1 
ATOM   4243 O  OE2 . GLU C 1 9   ? -44.021 52.127  5.695   1.00 86.45  ? 9   GLU C OE2 1 
ATOM   4244 N  N   . VAL C 1 10  ? -49.790 53.387  7.381   1.00 68.19  ? 10  VAL C N   1 
ATOM   4245 C  CA  . VAL C 1 10  ? -51.101 52.829  7.763   1.00 67.33  ? 10  VAL C CA  1 
ATOM   4246 C  C   . VAL C 1 10  ? -52.218 53.278  6.828   1.00 67.19  ? 10  VAL C C   1 
ATOM   4247 O  O   . VAL C 1 10  ? -53.338 52.766  6.898   1.00 67.73  ? 10  VAL C O   1 
ATOM   4248 C  CB  . VAL C 1 10  ? -51.464 53.175  9.231   1.00 66.42  ? 10  VAL C CB  1 
ATOM   4249 C  CG1 . VAL C 1 10  ? -51.774 54.662  9.383   1.00 63.92  ? 10  VAL C CG1 1 
ATOM   4250 C  CG2 . VAL C 1 10  ? -52.617 52.320  9.737   1.00 59.79  ? 10  VAL C CG2 1 
ATOM   4251 N  N   . GLN C 1 11  ? -51.903 54.229  5.956   1.00 63.47  ? 11  GLN C N   1 
ATOM   4252 C  CA  . GLN C 1 11  ? -52.860 54.755  4.994   1.00 60.53  ? 11  GLN C CA  1 
ATOM   4253 C  C   . GLN C 1 11  ? -52.749 54.062  3.647   1.00 62.29  ? 11  GLN C C   1 
ATOM   4254 O  O   . GLN C 1 11  ? -53.764 53.843  2.994   1.00 62.41  ? 11  GLN C O   1 
ATOM   4255 C  CB  . GLN C 1 11  ? -52.646 56.251  4.794   1.00 58.38  ? 11  GLN C CB  1 
ATOM   4256 C  CG  . GLN C 1 11  ? -53.233 57.126  5.881   1.00 58.52  ? 11  GLN C CG  1 
ATOM   4257 C  CD  . GLN C 1 11  ? -53.110 58.603  5.555   1.00 57.38  ? 11  GLN C CD  1 
ATOM   4258 O  OE1 . GLN C 1 11  ? -52.022 59.184  5.611   1.00 51.67  ? 11  GLN C OE1 1 
ATOM   4259 N  NE2 . GLN C 1 11  ? -54.235 59.220  5.224   1.00 55.63  ? 11  GLN C NE2 1 
ATOM   4260 N  N   . ALA C 1 12  ? -51.518 53.731  3.245   1.00 63.64  ? 12  ALA C N   1 
ATOM   4261 C  CA  . ALA C 1 12  ? -51.219 53.208  1.904   1.00 69.59  ? 12  ALA C CA  1 
ATOM   4262 C  C   . ALA C 1 12  ? -51.789 51.817  1.678   1.00 70.94  ? 12  ALA C C   1 
ATOM   4263 O  O   . ALA C 1 12  ? -52.223 51.499  0.578   1.00 70.11  ? 12  ALA C O   1 
ATOM   4264 C  CB  . ALA C 1 12  ? -49.717 53.205  1.653   1.00 65.50  ? 12  ALA C CB  1 
ATOM   4265 N  N   . GLU C 1 13  ? -51.767 51.007  2.735   1.00 78.74  ? 13  GLU C N   1 
ATOM   4266 C  CA  . GLU C 1 13  ? -52.213 49.610  2.727   1.00 83.31  ? 13  GLU C CA  1 
ATOM   4267 C  C   . GLU C 1 13  ? -53.740 49.473  2.834   1.00 91.51  ? 13  GLU C C   1 
ATOM   4268 O  O   . GLU C 1 13  ? -54.316 48.459  2.410   1.00 90.02  ? 13  GLU C O   1 
ATOM   4269 C  CB  . GLU C 1 13  ? -51.514 48.824  3.860   1.00 82.03  ? 13  GLU C CB  1 
ATOM   4270 C  CG  . GLU C 1 13  ? -51.585 49.481  5.241   1.00 78.85  ? 13  GLU C CG  1 
ATOM   4271 C  CD  . GLU C 1 13  ? -50.718 48.810  6.305   1.00 79.05  ? 13  GLU C CD  1 
ATOM   4272 O  OE1 . GLU C 1 13  ? -51.135 48.798  7.488   1.00 77.33  ? 13  GLU C OE1 1 
ATOM   4273 O  OE2 . GLU C 1 13  ? -49.617 48.313  5.978   1.00 73.15  ? 13  GLU C OE2 1 
ATOM   4274 N  N   . SER C 1 14  ? -54.375 50.499  3.406   1.00 94.06  ? 14  SER C N   1 
ATOM   4275 C  CA  . SER C 1 14  ? -55.826 50.547  3.603   1.00 96.12  ? 14  SER C CA  1 
ATOM   4276 C  C   . SER C 1 14  ? -56.432 51.691  2.785   1.00 99.34  ? 14  SER C C   1 
ATOM   4277 O  O   . SER C 1 14  ? -57.004 52.636  3.339   1.00 100.30 ? 14  SER C O   1 
ATOM   4278 C  CB  . SER C 1 14  ? -56.153 50.696  5.099   1.00 98.44  ? 14  SER C CB  1 
ATOM   4279 O  OG  . SER C 1 14  ? -57.517 51.026  5.324   1.00 95.03  ? 14  SER C OG  1 
ATOM   4280 N  N   . SER C 1 15  ? -56.278 51.601  1.464   1.00 101.78 ? 15  SER C N   1 
ATOM   4281 C  CA  . SER C 1 15  ? -56.830 52.580  0.517   1.00 105.09 ? 15  SER C CA  1 
ATOM   4282 C  C   . SER C 1 15  ? -56.687 52.012  -0.893  1.00 107.90 ? 15  SER C C   1 
ATOM   4283 O  O   . SER C 1 15  ? -56.462 50.810  -1.053  1.00 114.72 ? 15  SER C O   1 
ATOM   4284 C  CB  . SER C 1 15  ? -56.056 53.896  0.580   1.00 103.09 ? 15  SER C CB  1 
ATOM   4285 O  OG  . SER C 1 15  ? -54.703 53.685  0.227   1.00 103.40 ? 15  SER C OG  1 
ATOM   4286 N  N   . ASN C 1 16  ? -56.812 52.869  -1.908  1.00 108.06 ? 16  ASN C N   1 
ATOM   4287 C  CA  . ASN C 1 16  ? -56.630 52.437  -3.299  1.00 108.16 ? 16  ASN C CA  1 
ATOM   4288 C  C   . ASN C 1 16  ? -55.548 53.124  -4.146  1.00 107.65 ? 16  ASN C C   1 
ATOM   4289 O  O   . ASN C 1 16  ? -54.615 52.464  -4.603  1.00 109.55 ? 16  ASN C O   1 
ATOM   4290 C  CB  . ASN C 1 16  ? -57.995 52.427  -4.012  1.00 103.32 ? 16  ASN C CB  1 
ATOM   4291 C  CG  . ASN C 1 16  ? -58.662 51.057  -3.987  1.00 101.52 ? 16  ASN C CG  1 
ATOM   4292 O  OD1 . ASN C 1 16  ? -58.042 50.044  -3.644  1.00 96.12  ? 16  ASN C OD1 1 
ATOM   4293 N  ND2 . ASN C 1 16  ? -59.935 51.020  -4.357  1.00 97.80  ? 16  ASN C ND2 1 
ATOM   4294 N  N   . TYR C 1 17  ? -55.672 54.436  -4.350  1.00 103.28 ? 17  TYR C N   1 
ATOM   4295 C  CA  . TYR C 1 17  ? -54.736 55.184  -5.192  1.00 103.30 ? 17  TYR C CA  1 
ATOM   4296 C  C   . TYR C 1 17  ? -53.329 55.234  -4.583  1.00 111.56 ? 17  TYR C C   1 
ATOM   4297 O  O   . TYR C 1 17  ? -53.190 55.496  -3.385  1.00 112.05 ? 17  TYR C O   1 
ATOM   4298 C  CB  . TYR C 1 17  ? -55.260 56.598  -5.432  1.00 102.68 ? 17  TYR C CB  1 
ATOM   4299 N  N   . PRO C 1 18  ? -52.284 54.950  -5.398  1.00 119.56 ? 18  PRO C N   1 
ATOM   4300 C  CA  . PRO C 1 18  ? -50.840 54.865  -4.986  1.00 117.66 ? 18  PRO C CA  1 
ATOM   4301 C  C   . PRO C 1 18  ? -49.923 56.160  -4.725  1.00 115.64 ? 18  PRO C C   1 
ATOM   4302 O  O   . PRO C 1 18  ? -49.606 56.868  -5.686  1.00 117.62 ? 18  PRO C O   1 
ATOM   4303 C  CB  . PRO C 1 18  ? -50.224 54.141  -6.173  1.00 119.38 ? 18  PRO C CB  1 
ATOM   4304 C  CG  . PRO C 1 18  ? -51.032 54.630  -7.334  1.00 125.83 ? 18  PRO C CG  1 
ATOM   4305 C  CD  . PRO C 1 18  ? -52.456 54.769  -6.847  1.00 125.97 ? 18  PRO C CD  1 
ATOM   4306 N  N   . CYS C 1 19  ? -49.555 56.420  -3.474  1.00 108.46 ? 19  CYS C N   1 
ATOM   4307 C  CA  . CYS C 1 19  ? -48.963 57.662  -2.981  1.00 97.59  ? 19  CYS C CA  1 
ATOM   4308 C  C   . CYS C 1 19  ? -47.592 57.303  -2.417  1.00 90.92  ? 19  CYS C C   1 
ATOM   4309 O  O   . CYS C 1 19  ? -46.987 56.315  -2.833  1.00 93.70  ? 19  CYS C O   1 
ATOM   4310 C  CB  . CYS C 1 19  ? -49.844 58.053  -1.790  1.00 90.31  ? 19  CYS C CB  1 
ATOM   4311 S  SG  . CYS C 1 19  ? -49.772 56.861  -0.437  1.00 78.52  ? 19  CYS C SG  1 
ATOM   4312 N  N   . LEU C 1 20  ? -47.107 58.103  -1.473  1.00 85.28  ? 20  LEU C N   1 
ATOM   4313 C  CA  . LEU C 1 20  ? -45.864 57.805  -0.789  1.00 83.47  ? 20  LEU C CA  1 
ATOM   4314 C  C   . LEU C 1 20  ? -45.928 57.452  0.683   1.00 81.12  ? 20  LEU C C   1 
ATOM   4315 O  O   . LEU C 1 20  ? -46.443 58.224  1.490   1.00 76.85  ? 20  LEU C O   1 
ATOM   4316 C  CB  . LEU C 1 20  ? -44.998 59.049  -0.975  1.00 83.06  ? 20  LEU C CB  1 
ATOM   4317 C  CG  . LEU C 1 20  ? -44.363 59.259  -2.344  1.00 79.52  ? 20  LEU C CG  1 
ATOM   4318 C  CD1 . LEU C 1 20  ? -43.535 60.534  -2.322  1.00 75.25  ? 20  LEU C CD1 1 
ATOM   4319 C  CD2 . LEU C 1 20  ? -43.520 58.053  -2.743  1.00 78.06  ? 20  LEU C CD2 1 
ATOM   4320 N  N   . VAL C 1 21  ? -45.403 56.273  1.014   1.00 82.57  ? 21  VAL C N   1 
ATOM   4321 C  CA  . VAL C 1 21  ? -45.092 55.902  2.398   1.00 76.06  ? 21  VAL C CA  1 
ATOM   4322 C  C   . VAL C 1 21  ? -43.959 56.813  2.929   1.00 75.25  ? 21  VAL C C   1 
ATOM   4323 O  O   . VAL C 1 21  ? -43.233 57.441  2.134   1.00 68.46  ? 21  VAL C O   1 
ATOM   4324 C  CB  . VAL C 1 21  ? -44.713 54.398  2.536   1.00 75.65  ? 21  VAL C CB  1 
ATOM   4325 C  CG1 . VAL C 1 21  ? -45.955 53.520  2.601   1.00 75.27  ? 21  VAL C CG1 1 
ATOM   4326 C  CG2 . VAL C 1 21  ? -43.792 53.950  1.410   1.00 74.00  ? 21  VAL C CG2 1 
ATOM   4327 N  N   . PRO C 1 22  ? -43.820 56.911  4.269   1.00 70.38  ? 22  PRO C N   1 
ATOM   4328 C  CA  . PRO C 1 22  ? -42.784 57.756  4.861   1.00 72.17  ? 22  PRO C CA  1 
ATOM   4329 C  C   . PRO C 1 22  ? -41.365 57.534  4.352   1.00 74.41  ? 22  PRO C C   1 
ATOM   4330 O  O   . PRO C 1 22  ? -40.694 58.490  3.960   1.00 78.11  ? 22  PRO C O   1 
ATOM   4331 C  CB  . PRO C 1 22  ? -42.816 57.357  6.335   1.00 67.83  ? 22  PRO C CB  1 
ATOM   4332 C  CG  . PRO C 1 22  ? -44.244 57.013  6.563   1.00 70.79  ? 22  PRO C CG  1 
ATOM   4333 C  CD  . PRO C 1 22  ? -44.693 56.326  5.305   1.00 68.21  ? 22  PRO C CD  1 
ATOM   4334 N  N   . VAL C 1 23  ? -40.934 56.277  4.345   1.00 71.85  ? 23  VAL C N   1 
ATOM   4335 C  CA  . VAL C 1 23  ? -39.573 55.892  3.984   1.00 72.83  ? 23  VAL C CA  1 
ATOM   4336 C  C   . VAL C 1 23  ? -39.202 56.483  2.623   1.00 69.47  ? 23  VAL C C   1 
ATOM   4337 O  O   . VAL C 1 23  ? -38.028 56.515  2.243   1.00 71.18  ? 23  VAL C O   1 
ATOM   4338 C  CB  . VAL C 1 23  ? -39.437 54.347  3.915   1.00 71.86  ? 23  VAL C CB  1 
ATOM   4339 C  CG1 . VAL C 1 23  ? -37.987 53.933  4.131   1.00 68.98  ? 23  VAL C CG1 1 
ATOM   4340 C  CG2 . VAL C 1 23  ? -40.336 53.677  4.943   1.00 67.74  ? 23  VAL C CG2 1 
ATOM   4341 N  N   . LYS C 1 24  ? -40.207 56.956  1.897   1.00 62.46  ? 24  LYS C N   1 
ATOM   4342 C  CA  . LYS C 1 24  ? -39.999 57.448  0.544   1.00 66.10  ? 24  LYS C CA  1 
ATOM   4343 C  C   . LYS C 1 24  ? -40.407 58.916  0.402   1.00 63.78  ? 24  LYS C C   1 
ATOM   4344 O  O   . LYS C 1 24  ? -41.001 59.298  -0.598  1.00 64.33  ? 24  LYS C O   1 
ATOM   4345 C  CB  . LYS C 1 24  ? -40.790 56.580  -0.445  1.00 62.29  ? 24  LYS C CB  1 
ATOM   4346 C  CG  . LYS C 1 24  ? -39.979 56.069  -1.634  1.00 70.35  ? 24  LYS C CG  1 
ATOM   4347 C  CD  . LYS C 1 24  ? -39.161 54.817  -1.319  1.00 66.79  ? 24  LYS C CD  1 
ATOM   4348 C  CE  . LYS C 1 24  ? -38.587 54.203  -2.596  1.00 69.04  ? 24  LYS C CE  1 
ATOM   4349 N  NZ  . LYS C 1 24  ? -37.368 53.378  -2.347  1.00 62.48  ? 24  LYS C NZ  1 
ATOM   4350 N  N   . TRP C 1 25  ? -40.086 59.738  1.400   1.00 65.94  ? 25  TRP C N   1 
ATOM   4351 C  CA  . TRP C 1 25  ? -40.460 61.154  1.368   1.00 63.51  ? 25  TRP C CA  1 
ATOM   4352 C  C   . TRP C 1 25  ? -39.469 62.010  0.617   1.00 65.47  ? 25  TRP C C   1 
ATOM   4353 O  O   . TRP C 1 25  ? -38.246 61.837  0.723   1.00 60.29  ? 25  TRP C O   1 
ATOM   4354 C  CB  . TRP C 1 25  ? -40.727 61.688  2.776   1.00 63.55  ? 25  TRP C CB  1 
ATOM   4355 C  CG  . TRP C 1 25  ? -42.095 61.316  3.319   1.00 62.44  ? 25  TRP C CG  1 
ATOM   4356 C  CD1 . TRP C 1 25  ? -43.159 60.742  2.624   1.00 62.27  ? 25  TRP C CD1 1 
ATOM   4357 C  CD2 . TRP C 1 25  ? -42.606 61.520  4.688   1.00 57.65  ? 25  TRP C CD2 1 
ATOM   4358 N  NE1 . TRP C 1 25  ? -44.247 60.577  3.445   1.00 61.65  ? 25  TRP C NE1 1 
ATOM   4359 C  CE2 . TRP C 1 25  ? -43.984 61.016  4.690   1.00 55.61  ? 25  TRP C CE2 1 
ATOM   4360 C  CE3 . TRP C 1 25  ? -42.085 62.056  5.855   1.00 55.31  ? 25  TRP C CE3 1 
ATOM   4361 C  CZ2 . TRP C 1 25  ? -44.773 61.044  5.818   1.00 54.92  ? 25  TRP C CZ2 1 
ATOM   4362 C  CZ3 . TRP C 1 25  ? -42.895 62.084  6.991   1.00 53.12  ? 25  TRP C CZ3 1 
ATOM   4363 C  CH2 . TRP C 1 25  ? -44.205 61.586  6.974   1.00 54.99  ? 25  TRP C CH2 1 
ATOM   4364 N  N   . GLY C 1 26  ? -39.999 62.939  -0.170  1.00 70.98  ? 26  GLY C N   1 
ATOM   4365 C  CA  . GLY C 1 26  ? -39.182 63.752  -1.067  1.00 74.63  ? 26  GLY C CA  1 
ATOM   4366 C  C   . GLY C 1 26  ? -38.683 65.057  -0.465  1.00 74.62  ? 26  GLY C C   1 
ATOM   4367 O  O   . GLY C 1 26  ? -39.419 65.750  0.244   1.00 75.54  ? 26  GLY C O   1 
ATOM   4368 N  N   . GLY C 1 27  ? -37.428 65.385  -0.769  1.00 75.12  ? 27  GLY C N   1 
ATOM   4369 C  CA  . GLY C 1 27  ? -36.810 66.634  -0.342  1.00 73.48  ? 27  GLY C CA  1 
ATOM   4370 C  C   . GLY C 1 27  ? -35.873 66.434  0.826   1.00 69.38  ? 27  GLY C C   1 
ATOM   4371 O  O   . GLY C 1 27  ? -35.078 65.487  0.842   1.00 70.42  ? 27  GLY C O   1 
ATOM   4372 N  N   . ASN C 1 28  ? -35.972 67.327  1.811   1.00 67.43  ? 28  ASN C N   1 
ATOM   4373 C  CA  . ASN C 1 28  ? -35.079 67.294  2.977   1.00 66.15  ? 28  ASN C CA  1 
ATOM   4374 C  C   . ASN C 1 28  ? -35.181 66.020  3.806   1.00 66.81  ? 28  ASN C C   1 
ATOM   4375 O  O   . ASN C 1 28  ? -34.216 65.625  4.437   1.00 64.87  ? 28  ASN C O   1 
ATOM   4376 C  CB  . ASN C 1 28  ? -35.335 68.478  3.919   1.00 63.14  ? 28  ASN C CB  1 
ATOM   4377 C  CG  . ASN C 1 28  ? -34.791 69.801  3.373   1.00 61.74  ? 28  ASN C CG  1 
ATOM   4378 O  OD1 . ASN C 1 28  ? -33.579 69.965  3.169   1.00 60.54  ? 28  ASN C OD1 1 
ATOM   4379 N  ND2 . ASN C 1 28  ? -35.691 70.754  3.143   1.00 53.13  ? 28  ASN C ND2 1 
ATOM   4380 N  N   . CYS C 1 29  ? -36.348 65.376  3.757   1.00 70.21  ? 29  CYS C N   1 
ATOM   4381 C  CA  . CYS C 1 29  ? -36.665 64.141  4.487   1.00 71.28  ? 29  CYS C CA  1 
ATOM   4382 C  C   . CYS C 1 29  ? -35.556 63.095  4.420   1.00 74.76  ? 29  CYS C C   1 
ATOM   4383 O  O   . CYS C 1 29  ? -35.413 62.268  5.328   1.00 78.24  ? 29  CYS C O   1 
ATOM   4384 C  CB  . CYS C 1 29  ? -37.938 63.533  3.905   1.00 72.14  ? 29  CYS C CB  1 
ATOM   4385 S  SG  . CYS C 1 29  ? -39.197 64.725  3.395   1.00 71.92  ? 29  CYS C SG  1 
ATOM   4386 N  N   . GLN C 1 30  ? -34.791 63.132  3.332   1.00 73.24  ? 30  GLN C N   1 
ATOM   4387 C  CA  . GLN C 1 30  ? -33.695 62.200  3.120   1.00 74.95  ? 30  GLN C CA  1 
ATOM   4388 C  C   . GLN C 1 30  ? -32.341 62.810  3.513   1.00 74.86  ? 30  GLN C C   1 
ATOM   4389 O  O   . GLN C 1 30  ? -31.320 62.517  2.891   1.00 77.49  ? 30  GLN C O   1 
ATOM   4390 C  CB  . GLN C 1 30  ? -33.686 61.710  1.658   1.00 76.77  ? 30  GLN C CB  1 
ATOM   4391 C  CG  . GLN C 1 30  ? -34.995 61.083  1.170   1.00 74.54  ? 30  GLN C CG  1 
ATOM   4392 C  CD  . GLN C 1 30  ? -35.371 59.795  1.904   1.00 76.27  ? 30  GLN C CD  1 
ATOM   4393 O  OE1 . GLN C 1 30  ? -34.545 58.896  2.077   1.00 75.72  ? 30  GLN C OE1 1 
ATOM   4394 N  NE2 . GLN C 1 30  ? -36.629 59.701  2.331   1.00 71.92  ? 30  GLN C NE2 1 
ATOM   4395 N  N   . LYS C 1 31  ? -32.339 63.651  4.547   1.00 75.07  ? 31  LYS C N   1 
ATOM   4396 C  CA  . LYS C 1 31  ? -31.105 64.293  5.037   1.00 80.40  ? 31  LYS C CA  1 
ATOM   4397 C  C   . LYS C 1 31  ? -30.756 63.863  6.460   1.00 79.55  ? 31  LYS C C   1 
ATOM   4398 O  O   . LYS C 1 31  ? -31.554 63.203  7.122   1.00 78.93  ? 31  LYS C O   1 
ATOM   4399 C  CB  . LYS C 1 31  ? -31.178 65.830  4.945   1.00 86.09  ? 31  LYS C CB  1 
ATOM   4400 C  CG  . LYS C 1 31  ? -30.516 66.455  3.714   1.00 86.21  ? 31  LYS C CG  1 
ATOM   4401 C  CD  . LYS C 1 31  ? -31.478 66.594  2.544   1.00 86.28  ? 31  LYS C CD  1 
ATOM   4402 C  CE  . LYS C 1 31  ? -31.135 67.799  1.685   1.00 87.54  ? 31  LYS C CE  1 
ATOM   4403 N  NZ  . LYS C 1 31  ? -32.345 68.282  0.966   1.00 87.46  ? 31  LYS C NZ  1 
ATOM   4404 N  N   . ASP C 1 32  ? -29.573 64.270  6.918   1.00 76.51  ? 32  ASP C N   1 
ATOM   4405 C  CA  . ASP C 1 32  ? -28.921 63.704  8.107   1.00 77.31  ? 32  ASP C CA  1 
ATOM   4406 C  C   . ASP C 1 32  ? -29.636 63.859  9.447   1.00 74.96  ? 32  ASP C C   1 
ATOM   4407 O  O   . ASP C 1 32  ? -29.781 62.885  10.188  1.00 77.66  ? 32  ASP C O   1 
ATOM   4408 C  CB  . ASP C 1 32  ? -27.495 64.257  8.240   1.00 80.62  ? 32  ASP C CB  1 
ATOM   4409 C  CG  . ASP C 1 32  ? -26.551 63.720  7.175   1.00 84.83  ? 32  ASP C CG  1 
ATOM   4410 O  OD1 . ASP C 1 32  ? -27.004 63.402  6.048   1.00 86.47  ? 32  ASP C OD1 1 
ATOM   4411 O  OD2 . ASP C 1 32  ? -25.341 63.630  7.468   1.00 85.43  ? 32  ASP C OD2 1 
ATOM   4412 N  N   . ARG C 1 33  ? -30.062 65.080  9.756   1.00 68.85  ? 33  ARG C N   1 
ATOM   4413 C  CA  . ARG C 1 33  ? -30.511 65.424  11.102  1.00 69.71  ? 33  ARG C CA  1 
ATOM   4414 C  C   . ARG C 1 33  ? -32.034 65.444  11.185  1.00 70.89  ? 33  ARG C C   1 
ATOM   4415 O  O   . ARG C 1 33  ? -32.639 66.478  11.481  1.00 73.97  ? 33  ARG C O   1 
ATOM   4416 C  CB  . ARG C 1 33  ? -29.942 66.790  11.509  1.00 69.96  ? 33  ARG C CB  1 
ATOM   4417 C  CG  . ARG C 1 33  ? -28.485 66.803  11.968  1.00 73.45  ? 33  ARG C CG  1 
ATOM   4418 C  CD  . ARG C 1 33  ? -27.806 68.145  11.688  1.00 69.80  ? 33  ARG C CD  1 
ATOM   4419 N  NE  . ARG C 1 33  ? -28.742 69.272  11.774  1.00 66.83  ? 33  ARG C NE  1 
ATOM   4420 C  CZ  . ARG C 1 33  ? -28.835 70.111  12.799  1.00 63.71  ? 33  ARG C CZ  1 
ATOM   4421 N  NH1 . ARG C 1 33  ? -28.025 69.974  13.848  1.00 64.57  ? 33  ARG C NH1 1 
ATOM   4422 N  NH2 . ARG C 1 33  ? -29.728 71.100  12.765  1.00 58.65  ? 33  ARG C NH2 1 
ATOM   4423 N  N   . GLN C 1 34  ? -32.659 64.304  10.912  1.00 67.90  ? 34  GLN C N   1 
ATOM   4424 C  CA  . GLN C 1 34  ? -34.117 64.228  10.894  1.00 60.97  ? 34  GLN C CA  1 
ATOM   4425 C  C   . GLN C 1 34  ? -34.725 63.886  12.256  1.00 60.77  ? 34  GLN C C   1 
ATOM   4426 O  O   . GLN C 1 34  ? -34.039 63.390  13.161  1.00 55.28  ? 34  GLN C O   1 
ATOM   4427 C  CB  . GLN C 1 34  ? -34.594 63.226  9.837   1.00 63.18  ? 34  GLN C CB  1 
ATOM   4428 C  CG  . GLN C 1 34  ? -34.237 63.587  8.397   1.00 64.97  ? 34  GLN C CG  1 
ATOM   4429 C  CD  . GLN C 1 34  ? -34.978 64.804  7.874   1.00 63.84  ? 34  GLN C CD  1 
ATOM   4430 O  OE1 . GLN C 1 34  ? -36.070 65.140  8.339   1.00 57.14  ? 34  GLN C OE1 1 
ATOM   4431 N  NE2 . GLN C 1 34  ? -34.384 65.473  6.892   1.00 68.33  ? 34  GLN C NE2 1 
ATOM   4432 N  N   . SER C 1 35  ? -36.019 64.180  12.379  1.00 56.28  ? 35  SER C N   1 
ATOM   4433 C  CA  . SER C 1 35  ? -36.842 63.825  13.535  1.00 50.00  ? 35  SER C CA  1 
ATOM   4434 C  C   . SER C 1 35  ? -38.002 62.921  13.066  1.00 41.30  ? 35  SER C C   1 
ATOM   4435 O  O   . SER C 1 35  ? -38.380 62.967  11.893  1.00 41.32  ? 35  SER C O   1 
ATOM   4436 C  CB  . SER C 1 35  ? -37.384 65.094  14.210  1.00 47.35  ? 35  SER C CB  1 
ATOM   4437 O  OG  . SER C 1 35  ? -36.333 65.844  14.815  1.00 50.95  ? 35  SER C OG  1 
ATOM   4438 N  N   . PRO C 1 36  ? -38.575 62.106  13.969  1.00 41.16  ? 36  PRO C N   1 
ATOM   4439 C  CA  . PRO C 1 36  ? -38.345 61.904  15.419  1.00 37.62  ? 36  PRO C CA  1 
ATOM   4440 C  C   . PRO C 1 36  ? -37.160 60.994  15.704  1.00 35.00  ? 36  PRO C C   1 
ATOM   4441 O  O   . PRO C 1 36  ? -36.617 60.406  14.800  1.00 34.04  ? 36  PRO C O   1 
ATOM   4442 C  CB  . PRO C 1 36  ? -39.624 61.209  15.856  1.00 40.34  ? 36  PRO C CB  1 
ATOM   4443 C  CG  . PRO C 1 36  ? -39.998 60.389  14.657  1.00 41.82  ? 36  PRO C CG  1 
ATOM   4444 C  CD  . PRO C 1 36  ? -39.718 61.296  13.497  1.00 41.20  ? 36  PRO C CD  1 
ATOM   4445 N  N   . ILE C 1 37  ? -36.782 60.845  16.963  1.00 33.99  ? 37  ILE C N   1 
ATOM   4446 C  CA  . ILE C 1 37  ? -35.602 60.057  17.281  1.00 33.93  ? 37  ILE C CA  1 
ATOM   4447 C  C   . ILE C 1 37  ? -35.898 59.256  18.490  1.00 34.31  ? 37  ILE C C   1 
ATOM   4448 O  O   . ILE C 1 37  ? -36.901 59.504  19.182  1.00 35.13  ? 37  ILE C O   1 
ATOM   4449 C  CB  . ILE C 1 37  ? -34.373 60.950  17.637  1.00 36.28  ? 37  ILE C CB  1 
ATOM   4450 C  CG1 . ILE C 1 37  ? -34.757 61.995  18.699  1.00 33.95  ? 37  ILE C CG1 1 
ATOM   4451 C  CG2 . ILE C 1 37  ? -33.830 61.653  16.398  1.00 35.14  ? 37  ILE C CG2 1 
ATOM   4452 C  CD1 . ILE C 1 37  ? -33.683 62.252  19.738  1.00 38.97  ? 37  ILE C CD1 1 
ATOM   4453 N  N   . ASN C 1 38  ? -35.015 58.314  18.786  1.00 34.00  ? 38  ASN C N   1 
ATOM   4454 C  CA  . ASN C 1 38  ? -35.045 57.685  20.085  1.00 36.14  ? 38  ASN C CA  1 
ATOM   4455 C  C   . ASN C 1 38  ? -34.132 58.436  21.050  1.00 34.93  ? 38  ASN C C   1 
ATOM   4456 O  O   . ASN C 1 38  ? -33.038 58.768  20.676  1.00 36.79  ? 38  ASN C O   1 
ATOM   4457 C  CB  . ASN C 1 38  ? -34.613 56.217  20.011  1.00 36.04  ? 38  ASN C CB  1 
ATOM   4458 C  CG  . ASN C 1 38  ? -34.468 55.609  21.385  1.00 36.99  ? 38  ASN C CG  1 
ATOM   4459 O  OD1 . ASN C 1 38  ? -35.414 55.662  22.186  1.00 36.59  ? 38  ASN C OD1 1 
ATOM   4460 N  ND2 . ASN C 1 38  ? -33.278 55.064  21.693  1.00 36.35  ? 38  ASN C ND2 1 
ATOM   4461 N  N   . ILE C 1 39  ? -34.564 58.677  22.291  1.00 34.73  ? 39  ILE C N   1 
ATOM   4462 C  CA  . ILE C 1 39  ? -33.723 59.398  23.258  1.00 37.31  ? 39  ILE C CA  1 
ATOM   4463 C  C   . ILE C 1 39  ? -33.178 58.443  24.324  1.00 40.90  ? 39  ILE C C   1 
ATOM   4464 O  O   . ILE C 1 39  ? -33.966 57.857  25.069  1.00 45.64  ? 39  ILE C O   1 
ATOM   4465 C  CB  . ILE C 1 39  ? -34.473 60.547  23.997  1.00 36.93  ? 39  ILE C CB  1 
ATOM   4466 C  CG1 . ILE C 1 39  ? -35.010 61.611  23.033  1.00 34.30  ? 39  ILE C CG1 1 
ATOM   4467 C  CG2 . ILE C 1 39  ? -33.588 61.154  25.088  1.00 35.50  ? 39  ILE C CG2 1 
ATOM   4468 C  CD1 . ILE C 1 39  ? -35.759 62.732  23.743  1.00 32.13  ? 39  ILE C CD1 1 
ATOM   4469 N  N   . VAL C 1 40  ? -31.847 58.297  24.407  1.00 41.55  ? 40  VAL C N   1 
ATOM   4470 C  CA  . VAL C 1 40  ? -31.262 57.477  25.465  1.00 43.24  ? 40  VAL C CA  1 
ATOM   4471 C  C   . VAL C 1 40  ? -31.037 58.408  26.633  1.00 42.69  ? 40  VAL C C   1 
ATOM   4472 O  O   . VAL C 1 40  ? -30.287 59.366  26.533  1.00 48.28  ? 40  VAL C O   1 
ATOM   4473 C  CB  . VAL C 1 40  ? -29.952 56.734  25.042  1.00 48.70  ? 40  VAL C CB  1 
ATOM   4474 C  CG1 . VAL C 1 40  ? -29.662 55.566  25.999  1.00 37.71  ? 40  VAL C CG1 1 
ATOM   4475 C  CG2 . VAL C 1 40  ? -30.038 56.215  23.600  1.00 39.55  ? 40  VAL C CG2 1 
ATOM   4476 N  N   . THR C 1 41  ? -31.734 58.137  27.722  1.00 47.71  ? 41  THR C N   1 
ATOM   4477 C  CA  . THR C 1 41  ? -31.895 59.101  28.794  1.00 49.62  ? 41  THR C CA  1 
ATOM   4478 C  C   . THR C 1 41  ? -30.655 59.304  29.624  1.00 51.54  ? 41  THR C C   1 
ATOM   4479 O  O   . THR C 1 41  ? -30.340 60.454  29.950  1.00 55.17  ? 41  THR C O   1 
ATOM   4480 C  CB  . THR C 1 41  ? -33.071 58.772  29.718  1.00 47.08  ? 41  THR C CB  1 
ATOM   4481 O  OG1 . THR C 1 41  ? -32.897 57.465  30.254  1.00 49.81  ? 41  THR C OG1 1 
ATOM   4482 C  CG2 . THR C 1 41  ? -34.365 58.826  28.952  1.00 50.65  ? 41  THR C CG2 1 
ATOM   4483 N  N   . THR C 1 42  ? -29.967 58.211  29.977  1.00 47.28  ? 42  THR C N   1 
ATOM   4484 C  CA  . THR C 1 42  ? -28.635 58.291  30.628  1.00 46.94  ? 42  THR C CA  1 
ATOM   4485 C  C   . THR C 1 42  ? -27.550 58.913  29.759  1.00 49.64  ? 42  THR C C   1 
ATOM   4486 O  O   . THR C 1 42  ? -26.466 59.221  30.259  1.00 52.46  ? 42  THR C O   1 
ATOM   4487 C  CB  . THR C 1 42  ? -28.103 56.929  31.103  1.00 45.03  ? 42  THR C CB  1 
ATOM   4488 O  OG1 . THR C 1 42  ? -27.932 56.046  29.975  1.00 46.97  ? 42  THR C OG1 1 
ATOM   4489 C  CG2 . THR C 1 42  ? -29.033 56.334  32.111  1.00 44.62  ? 42  THR C CG2 1 
ATOM   4490 N  N   . LYS C 1 43  ? -27.834 59.107  28.474  1.00 50.29  ? 43  LYS C N   1 
ATOM   4491 C  CA  . LYS C 1 43  ? -26.840 59.689  27.550  1.00 54.82  ? 43  LYS C CA  1 
ATOM   4492 C  C   . LYS C 1 43  ? -27.024 61.187  27.248  1.00 56.44  ? 43  LYS C C   1 
ATOM   4493 O  O   . LYS C 1 43  ? -26.181 61.803  26.575  1.00 59.70  ? 43  LYS C O   1 
ATOM   4494 C  CB  . LYS C 1 43  ? -26.769 58.885  26.246  1.00 54.66  ? 43  LYS C CB  1 
ATOM   4495 C  CG  . LYS C 1 43  ? -26.394 57.423  26.457  1.00 54.74  ? 43  LYS C CG  1 
ATOM   4496 C  CD  . LYS C 1 43  ? -25.882 56.787  25.170  1.00 50.68  ? 43  LYS C CD  1 
ATOM   4497 C  CE  . LYS C 1 43  ? -25.468 55.345  25.409  1.00 48.96  ? 43  LYS C CE  1 
ATOM   4498 N  NZ  . LYS C 1 43  ? -24.697 54.838  24.245  1.00 45.63  ? 43  LYS C NZ  1 
ATOM   4499 N  N   . ALA C 1 44  ? -28.120 61.773  27.726  1.00 53.44  ? 44  ALA C N   1 
ATOM   4500 C  CA  . ALA C 1 44  ? -28.256 63.239  27.668  1.00 53.18  ? 44  ALA C CA  1 
ATOM   4501 C  C   . ALA C 1 44  ? -27.793 63.883  28.985  1.00 51.59  ? 44  ALA C C   1 
ATOM   4502 O  O   . ALA C 1 44  ? -28.334 63.622  30.065  1.00 43.93  ? 44  ALA C O   1 
ATOM   4503 C  CB  . ALA C 1 44  ? -29.670 63.663  27.309  1.00 47.10  ? 44  ALA C CB  1 
ATOM   4504 N  N   . LYS C 1 45  ? -26.752 64.701  28.863  1.00 55.38  ? 45  LYS C N   1 
ATOM   4505 C  CA  . LYS C 1 45  ? -26.117 65.408  29.982  1.00 58.69  ? 45  LYS C CA  1 
ATOM   4506 C  C   . LYS C 1 45  ? -26.953 66.599  30.512  1.00 57.28  ? 45  LYS C C   1 
ATOM   4507 O  O   . LYS C 1 45  ? -27.635 67.302  29.725  1.00 53.18  ? 45  LYS C O   1 
ATOM   4508 C  CB  . LYS C 1 45  ? -24.739 65.880  29.517  1.00 62.43  ? 45  LYS C CB  1 
ATOM   4509 C  CG  . LYS C 1 45  ? -24.677 66.100  28.012  1.00 61.76  ? 45  LYS C CG  1 
ATOM   4510 C  CD  . LYS C 1 45  ? -23.294 66.525  27.549  1.00 64.69  ? 45  LYS C CD  1 
ATOM   4511 C  CE  . LYS C 1 45  ? -23.163 66.395  26.037  1.00 63.56  ? 45  LYS C CE  1 
ATOM   4512 N  NZ  . LYS C 1 45  ? -23.942 67.410  25.271  1.00 63.46  ? 45  LYS C NZ  1 
ATOM   4513 N  N   . VAL C 1 46  ? -26.908 66.816  31.836  1.00 55.00  ? 46  VAL C N   1 
ATOM   4514 C  CA  . VAL C 1 46  ? -27.592 67.970  32.455  1.00 53.49  ? 46  VAL C CA  1 
ATOM   4515 C  C   . VAL C 1 46  ? -26.911 69.257  31.980  1.00 53.80  ? 46  VAL C C   1 
ATOM   4516 O  O   . VAL C 1 46  ? -25.728 69.431  32.229  1.00 54.35  ? 46  VAL C O   1 
ATOM   4517 C  CB  . VAL C 1 46  ? -27.602 67.937  34.024  1.00 58.25  ? 46  VAL C CB  1 
ATOM   4518 C  CG1 . VAL C 1 46  ? -28.277 69.185  34.598  1.00 54.87  ? 46  VAL C CG1 1 
ATOM   4519 C  CG2 . VAL C 1 46  ? -28.286 66.688  34.573  1.00 55.67  ? 46  VAL C CG2 1 
ATOM   4520 N  N   . ASP C 1 47  ? -27.643 70.121  31.264  1.00 51.73  ? 47  ASP C N   1 
ATOM   4521 C  CA  . ASP C 1 47  ? -27.172 71.467  30.903  1.00 49.47  ? 47  ASP C CA  1 
ATOM   4522 C  C   . ASP C 1 47  ? -28.013 72.479  31.695  1.00 52.67  ? 47  ASP C C   1 
ATOM   4523 O  O   . ASP C 1 47  ? -29.208 72.647  31.439  1.00 51.59  ? 47  ASP C O   1 
ATOM   4524 C  CB  . ASP C 1 47  ? -27.259 71.702  29.377  1.00 47.14  ? 47  ASP C CB  1 
ATOM   4525 C  CG  . ASP C 1 47  ? -27.128 73.185  28.976  1.00 49.79  ? 47  ASP C CG  1 
ATOM   4526 O  OD1 . ASP C 1 47  ? -27.167 74.063  29.857  1.00 48.69  ? 47  ASP C OD1 1 
ATOM   4527 O  OD2 . ASP C 1 47  ? -26.987 73.486  27.763  1.00 48.44  ? 47  ASP C OD2 1 
ATOM   4528 N  N   . LYS C 1 48  ? -27.373 73.155  32.648  1.00 57.32  ? 48  LYS C N   1 
ATOM   4529 C  CA  . LYS C 1 48  ? -28.075 74.015  33.615  1.00 56.74  ? 48  LYS C CA  1 
ATOM   4530 C  C   . LYS C 1 48  ? -28.660 75.316  33.049  1.00 52.91  ? 48  LYS C C   1 
ATOM   4531 O  O   . LYS C 1 48  ? -29.433 75.990  33.738  1.00 47.85  ? 48  LYS C O   1 
ATOM   4532 C  CB  . LYS C 1 48  ? -27.200 74.281  34.847  1.00 63.21  ? 48  LYS C CB  1 
ATOM   4533 C  CG  . LYS C 1 48  ? -27.369 73.234  35.943  1.00 68.21  ? 48  LYS C CG  1 
ATOM   4534 C  CD  . LYS C 1 48  ? -26.073 72.987  36.700  1.00 70.50  ? 48  LYS C CD  1 
ATOM   4535 C  CE  . LYS C 1 48  ? -26.172 71.736  37.565  1.00 75.89  ? 48  LYS C CE  1 
ATOM   4536 N  NZ  . LYS C 1 48  ? -24.970 71.567  38.434  1.00 81.57  ? 48  LYS C NZ  1 
ATOM   4537 N  N   . LYS C 1 49  ? -28.322 75.641  31.800  1.00 50.51  ? 49  LYS C N   1 
ATOM   4538 C  CA  . LYS C 1 49  ? -28.877 76.814  31.128  1.00 49.30  ? 49  LYS C CA  1 
ATOM   4539 C  C   . LYS C 1 49  ? -30.263 76.515  30.547  1.00 53.78  ? 49  LYS C C   1 
ATOM   4540 O  O   . LYS C 1 49  ? -30.942 77.401  30.022  1.00 50.62  ? 49  LYS C O   1 
ATOM   4541 C  CB  . LYS C 1 49  ? -27.978 77.301  29.990  1.00 51.98  ? 49  LYS C CB  1 
ATOM   4542 C  CG  . LYS C 1 49  ? -26.567 76.749  29.954  1.00 55.20  ? 49  LYS C CG  1 
ATOM   4543 C  CD  . LYS C 1 49  ? -26.108 76.631  28.497  1.00 56.35  ? 49  LYS C CD  1 
ATOM   4544 C  CE  . LYS C 1 49  ? -24.786 75.888  28.377  1.00 57.86  ? 49  LYS C CE  1 
ATOM   4545 N  NZ  . LYS C 1 49  ? -23.879 76.501  27.354  1.00 65.91  ? 49  LYS C NZ  1 
ATOM   4546 N  N   . LEU C 1 50  ? -30.675 75.256  30.584  1.00 53.47  ? 50  LEU C N   1 
ATOM   4547 C  CA  . LEU C 1 50  ? -32.035 74.954  30.218  1.00 48.34  ? 50  LEU C CA  1 
ATOM   4548 C  C   . LEU C 1 50  ? -32.843 75.064  31.511  1.00 49.99  ? 50  LEU C C   1 
ATOM   4549 O  O   . LEU C 1 50  ? -32.950 74.097  32.277  1.00 45.90  ? 50  LEU C O   1 
ATOM   4550 C  CB  . LEU C 1 50  ? -32.145 73.571  29.571  1.00 51.87  ? 50  LEU C CB  1 
ATOM   4551 C  CG  . LEU C 1 50  ? -31.131 73.165  28.493  1.00 50.82  ? 50  LEU C CG  1 
ATOM   4552 C  CD1 . LEU C 1 50  ? -31.482 71.789  27.954  1.00 52.20  ? 50  LEU C CD1 1 
ATOM   4553 C  CD2 . LEU C 1 50  ? -31.022 74.189  27.366  1.00 50.04  ? 50  LEU C CD2 1 
ATOM   4554 N  N   . GLY C 1 51  ? -33.358 76.269  31.769  1.00 48.07  ? 51  GLY C N   1 
ATOM   4555 C  CA  . GLY C 1 51  ? -34.207 76.536  32.935  1.00 50.62  ? 51  GLY C CA  1 
ATOM   4556 C  C   . GLY C 1 51  ? -35.659 76.593  32.509  1.00 58.28  ? 51  GLY C C   1 
ATOM   4557 O  O   . GLY C 1 51  ? -35.950 76.406  31.335  1.00 65.07  ? 51  GLY C O   1 
ATOM   4558 N  N   . ARG C 1 52  ? -36.569 76.859  33.448  1.00 60.15  ? 52  ARG C N   1 
ATOM   4559 C  CA  . ARG C 1 52  ? -38.009 76.845  33.169  1.00 58.85  ? 52  ARG C CA  1 
ATOM   4560 C  C   . ARG C 1 52  ? -38.444 77.532  31.883  1.00 62.83  ? 52  ARG C C   1 
ATOM   4561 O  O   . ARG C 1 52  ? -37.734 78.380  31.326  1.00 65.90  ? 52  ARG C O   1 
ATOM   4562 C  CB  . ARG C 1 52  ? -38.794 77.463  34.319  1.00 64.00  ? 52  ARG C CB  1 
ATOM   4563 C  CG  . ARG C 1 52  ? -39.164 76.507  35.419  1.00 70.35  ? 52  ARG C CG  1 
ATOM   4564 C  CD  . ARG C 1 52  ? -38.019 76.346  36.388  1.00 72.36  ? 52  ARG C CD  1 
ATOM   4565 N  NE  . ARG C 1 52  ? -38.449 75.590  37.552  1.00 75.63  ? 52  ARG C NE  1 
ATOM   4566 C  CZ  . ARG C 1 52  ? -37.651 74.836  38.294  1.00 74.56  ? 52  ARG C CZ  1 
ATOM   4567 N  NH1 . ARG C 1 52  ? -36.355 74.716  37.999  1.00 70.35  ? 52  ARG C NH1 1 
ATOM   4568 N  NH2 . ARG C 1 52  ? -38.165 74.196  39.332  1.00 74.00  ? 52  ARG C NH2 1 
ATOM   4569 N  N   . PHE C 1 53  ? -39.624 77.138  31.415  1.00 57.89  ? 53  PHE C N   1 
ATOM   4570 C  CA  . PHE C 1 53  ? -40.310 77.824  30.334  1.00 58.02  ? 53  PHE C CA  1 
ATOM   4571 C  C   . PHE C 1 53  ? -41.252 78.859  30.951  1.00 59.13  ? 53  PHE C C   1 
ATOM   4572 O  O   . PHE C 1 53  ? -41.772 78.625  32.049  1.00 54.57  ? 53  PHE C O   1 
ATOM   4573 C  CB  . PHE C 1 53  ? -41.101 76.815  29.484  1.00 53.70  ? 53  PHE C CB  1 
ATOM   4574 C  CG  . PHE C 1 53  ? -40.254 76.061  28.499  1.00 52.84  ? 53  PHE C CG  1 
ATOM   4575 C  CD1 . PHE C 1 53  ? -39.713 74.828  28.831  1.00 52.72  ? 53  PHE C CD1 1 
ATOM   4576 C  CD2 . PHE C 1 53  ? -39.978 76.596  27.244  1.00 51.42  ? 53  PHE C CD2 1 
ATOM   4577 C  CE1 . PHE C 1 53  ? -38.904 74.142  27.922  1.00 54.93  ? 53  PHE C CE1 1 
ATOM   4578 C  CE2 . PHE C 1 53  ? -39.181 75.922  26.339  1.00 53.36  ? 53  PHE C CE2 1 
ATOM   4579 C  CZ  . PHE C 1 53  ? -38.643 74.685  26.679  1.00 53.39  ? 53  PHE C CZ  1 
ATOM   4580 N  N   . PHE C 1 54  ? -41.467 79.995  30.276  1.00 56.99  ? 54  PHE C N   1 
ATOM   4581 C  CA  . PHE C 1 54  ? -42.511 80.936  30.733  1.00 58.38  ? 54  PHE C CA  1 
ATOM   4582 C  C   . PHE C 1 54  ? -43.703 80.867  29.798  1.00 55.24  ? 54  PHE C C   1 
ATOM   4583 O  O   . PHE C 1 54  ? -43.535 80.885  28.586  1.00 43.74  ? 54  PHE C O   1 
ATOM   4584 C  CB  . PHE C 1 54  ? -42.051 82.411  30.857  1.00 64.27  ? 54  PHE C CB  1 
ATOM   4585 C  CG  . PHE C 1 54  ? -40.554 82.632  30.793  1.00 69.98  ? 54  PHE C CG  1 
ATOM   4586 C  CD1 . PHE C 1 54  ? -39.685 82.031  31.700  1.00 68.78  ? 54  PHE C CD1 1 
ATOM   4587 C  CD2 . PHE C 1 54  ? -40.021 83.513  29.846  1.00 70.64  ? 54  PHE C CD2 1 
ATOM   4588 C  CE1 . PHE C 1 54  ? -38.316 82.268  31.627  1.00 73.20  ? 54  PHE C CE1 1 
ATOM   4589 C  CE2 . PHE C 1 54  ? -38.653 83.753  29.774  1.00 67.26  ? 54  PHE C CE2 1 
ATOM   4590 C  CZ  . PHE C 1 54  ? -37.799 83.130  30.673  1.00 71.13  ? 54  PHE C CZ  1 
ATOM   4591 N  N   . PHE C 1 55  ? -44.904 80.826  30.376  1.00 69.26  ? 55  PHE C N   1 
ATOM   4592 C  CA  . PHE C 1 55  ? -46.146 80.539  29.630  1.00 76.01  ? 55  PHE C CA  1 
ATOM   4593 C  C   . PHE C 1 55  ? -47.119 81.730  29.535  1.00 78.65  ? 55  PHE C C   1 
ATOM   4594 O  O   . PHE C 1 55  ? -47.986 81.920  30.400  1.00 78.05  ? 55  PHE C O   1 
ATOM   4595 C  CB  . PHE C 1 55  ? -46.874 79.311  30.219  1.00 72.77  ? 55  PHE C CB  1 
ATOM   4596 C  CG  . PHE C 1 55  ? -46.107 78.013  30.104  1.00 70.35  ? 55  PHE C CG  1 
ATOM   4597 C  CD1 . PHE C 1 55  ? -45.946 77.382  28.869  1.00 70.81  ? 55  PHE C CD1 1 
ATOM   4598 C  CD2 . PHE C 1 55  ? -45.585 77.397  31.240  1.00 66.37  ? 55  PHE C CD2 1 
ATOM   4599 C  CE1 . PHE C 1 55  ? -45.251 76.180  28.767  1.00 67.65  ? 55  PHE C CE1 1 
ATOM   4600 C  CE2 . PHE C 1 55  ? -44.898 76.193  31.145  1.00 66.99  ? 55  PHE C CE2 1 
ATOM   4601 C  CZ  . PHE C 1 55  ? -44.728 75.584  29.909  1.00 64.99  ? 55  PHE C CZ  1 
ATOM   4602 N  N   . SER C 1 56  ? -46.976 82.501  28.459  1.00 78.56  ? 56  SER C N   1 
ATOM   4603 C  CA  . SER C 1 56  ? -47.821 83.657  28.202  1.00 81.18  ? 56  SER C CA  1 
ATOM   4604 C  C   . SER C 1 56  ? -49.223 83.221  27.790  1.00 83.07  ? 56  SER C C   1 
ATOM   4605 O  O   . SER C 1 56  ? -49.429 82.765  26.664  1.00 77.64  ? 56  SER C O   1 
ATOM   4606 C  CB  . SER C 1 56  ? -47.199 84.549  27.119  1.00 81.44  ? 56  SER C CB  1 
ATOM   4607 O  OG  . SER C 1 56  ? -47.072 83.842  25.896  1.00 71.51  ? 56  SER C OG  1 
ATOM   4608 N  N   . GLY C 1 57  ? -50.168 83.332  28.725  1.00 87.23  ? 57  GLY C N   1 
ATOM   4609 C  CA  . GLY C 1 57  ? -51.595 83.176  28.429  1.00 91.05  ? 57  GLY C CA  1 
ATOM   4610 C  C   . GLY C 1 57  ? -52.127 81.757  28.381  1.00 93.20  ? 57  GLY C C   1 
ATOM   4611 O  O   . GLY C 1 57  ? -53.346 81.550  28.335  1.00 93.27  ? 57  GLY C O   1 
ATOM   4612 N  N   . TYR C 1 58  ? -51.215 80.785  28.380  1.00 92.30  ? 58  TYR C N   1 
ATOM   4613 C  CA  . TYR C 1 58  ? -51.557 79.358  28.453  1.00 90.08  ? 58  TYR C CA  1 
ATOM   4614 C  C   . TYR C 1 58  ? -52.626 79.100  29.514  1.00 93.87  ? 58  TYR C C   1 
ATOM   4615 O  O   . TYR C 1 58  ? -53.494 78.240  29.346  1.00 88.34  ? 58  TYR C O   1 
ATOM   4616 C  CB  . TYR C 1 58  ? -50.299 78.526  28.774  1.00 83.65  ? 58  TYR C CB  1 
ATOM   4617 C  CG  . TYR C 1 58  ? -49.474 78.112  27.566  1.00 77.81  ? 58  TYR C CG  1 
ATOM   4618 C  CD1 . TYR C 1 58  ? -48.841 79.057  26.765  1.00 71.32  ? 58  TYR C CD1 1 
ATOM   4619 C  CD2 . TYR C 1 58  ? -49.320 76.759  27.234  1.00 78.85  ? 58  TYR C CD2 1 
ATOM   4620 C  CE1 . TYR C 1 58  ? -48.091 78.672  25.661  1.00 69.96  ? 58  TYR C CE1 1 
ATOM   4621 C  CE2 . TYR C 1 58  ? -48.569 76.362  26.134  1.00 71.40  ? 58  TYR C CE2 1 
ATOM   4622 C  CZ  . TYR C 1 58  ? -47.954 77.319  25.347  1.00 73.86  ? 58  TYR C CZ  1 
ATOM   4623 O  OH  . TYR C 1 58  ? -47.208 76.926  24.248  1.00 63.85  ? 58  TYR C OH  1 
ATOM   4624 N  N   . ASP C 1 59  ? -52.547 79.877  30.594  1.00 102.98 ? 59  ASP C N   1 
ATOM   4625 C  CA  . ASP C 1 59  ? -53.420 79.760  31.766  1.00 108.34 ? 59  ASP C CA  1 
ATOM   4626 C  C   . ASP C 1 59  ? -54.869 80.236  31.557  1.00 111.44 ? 59  ASP C C   1 
ATOM   4627 O  O   . ASP C 1 59  ? -55.768 79.836  32.310  1.00 109.80 ? 59  ASP C O   1 
ATOM   4628 C  CB  . ASP C 1 59  ? -52.795 80.520  32.947  1.00 103.64 ? 59  ASP C CB  1 
ATOM   4629 C  CG  . ASP C 1 59  ? -52.546 81.988  32.634  1.00 105.12 ? 59  ASP C CG  1 
ATOM   4630 O  OD1 . ASP C 1 59  ? -51.892 82.283  31.606  1.00 103.99 ? 59  ASP C OD1 1 
ATOM   4631 O  OD2 . ASP C 1 59  ? -53.004 82.844  33.422  1.00 100.01 ? 59  ASP C OD2 1 
ATOM   4632 N  N   . LYS C 1 60  ? -55.092 81.079  30.545  1.00 105.27 ? 60  LYS C N   1 
ATOM   4633 C  CA  . LYS C 1 60  ? -56.386 81.729  30.361  1.00 99.22  ? 60  LYS C CA  1 
ATOM   4634 C  C   . LYS C 1 60  ? -57.362 80.925  29.505  1.00 97.19  ? 60  LYS C C   1 
ATOM   4635 O  O   . LYS C 1 60  ? -57.082 80.597  28.346  1.00 99.04  ? 60  LYS C O   1 
ATOM   4636 C  CB  . LYS C 1 60  ? -56.210 83.149  29.817  1.00 100.21 ? 60  LYS C CB  1 
ATOM   4637 C  CG  . LYS C 1 60  ? -57.353 84.081  30.180  1.00 95.95  ? 60  LYS C CG  1 
ATOM   4638 C  CD  . LYS C 1 60  ? -56.844 85.474  30.505  1.00 95.17  ? 60  LYS C CD  1 
ATOM   4639 C  CE  . LYS C 1 60  ? -57.960 86.341  31.076  1.00 95.16  ? 60  LYS C CE  1 
ATOM   4640 N  NZ  . LYS C 1 60  ? -57.511 87.732  31.360  1.00 86.75  ? 60  LYS C NZ  1 
ATOM   4641 N  N   . LYS C 1 61  ? -58.511 80.627  30.112  1.00 94.12  ? 61  LYS C N   1 
ATOM   4642 C  CA  . LYS C 1 61  ? -59.616 79.873  29.503  1.00 88.15  ? 61  LYS C CA  1 
ATOM   4643 C  C   . LYS C 1 61  ? -60.137 80.573  28.250  1.00 84.49  ? 61  LYS C C   1 
ATOM   4644 O  O   . LYS C 1 61  ? -59.909 81.771  28.075  1.00 84.50  ? 61  LYS C O   1 
ATOM   4645 C  CB  . LYS C 1 61  ? -60.757 79.710  30.521  1.00 87.74  ? 61  LYS C CB  1 
ATOM   4646 C  CG  . LYS C 1 61  ? -60.298 79.528  31.967  1.00 93.42  ? 61  LYS C CG  1 
ATOM   4647 C  CD  . LYS C 1 61  ? -59.716 78.141  32.222  1.00 98.14  ? 61  LYS C CD  1 
ATOM   4648 C  CE  . LYS C 1 61  ? -58.870 78.096  33.487  1.00 92.71  ? 61  LYS C CE  1 
ATOM   4649 N  NZ  . LYS C 1 61  ? -58.433 76.704  33.796  1.00 91.26  ? 61  LYS C NZ  1 
ATOM   4650 N  N   . GLN C 1 62  ? -60.848 79.837  27.391  1.00 80.53  ? 62  GLN C N   1 
ATOM   4651 C  CA  . GLN C 1 62  ? -61.218 80.356  26.073  1.00 76.05  ? 62  GLN C CA  1 
ATOM   4652 C  C   . GLN C 1 62  ? -62.002 79.347  25.253  1.00 70.30  ? 62  GLN C C   1 
ATOM   4653 O  O   . GLN C 1 62  ? -62.093 78.180  25.628  1.00 68.78  ? 62  GLN C O   1 
ATOM   4654 C  CB  . GLN C 1 62  ? -59.939 80.660  25.314  1.00 78.78  ? 62  GLN C CB  1 
ATOM   4655 C  CG  . GLN C 1 62  ? -59.999 81.828  24.363  1.00 77.62  ? 62  GLN C CG  1 
ATOM   4656 C  CD  . GLN C 1 62  ? -58.646 82.058  23.735  1.00 76.29  ? 62  GLN C CD  1 
ATOM   4657 O  OE1 . GLN C 1 62  ? -57.618 81.613  24.264  1.00 70.25  ? 62  GLN C OE1 1 
ATOM   4658 N  NE2 . GLN C 1 62  ? -58.630 82.747  22.604  1.00 74.82  ? 62  GLN C NE2 1 
ATOM   4659 N  N   . THR C 1 63  ? -62.558 79.799  24.130  1.00 63.52  ? 63  THR C N   1 
ATOM   4660 C  CA  . THR C 1 63  ? -62.992 78.878  23.069  1.00 60.90  ? 63  THR C CA  1 
ATOM   4661 C  C   . THR C 1 63  ? -61.836 78.732  22.080  1.00 56.23  ? 63  THR C C   1 
ATOM   4662 O  O   . THR C 1 63  ? -60.852 79.479  22.179  1.00 60.55  ? 63  THR C O   1 
ATOM   4663 C  CB  . THR C 1 63  ? -64.255 79.353  22.313  1.00 60.26  ? 63  THR C CB  1 
ATOM   4664 O  OG1 . THR C 1 63  ? -63.901 80.377  21.370  1.00 59.44  ? 63  THR C OG1 1 
ATOM   4665 C  CG2 . THR C 1 63  ? -65.347 79.834  23.277  1.00 58.47  ? 63  THR C CG2 1 
ATOM   4666 N  N   . TRP C 1 64  ? -61.945 77.789  21.138  1.00 52.35  ? 64  TRP C N   1 
ATOM   4667 C  CA  . TRP C 1 64  ? -60.847 77.492  20.204  1.00 50.42  ? 64  TRP C CA  1 
ATOM   4668 C  C   . TRP C 1 64  ? -61.297 77.008  18.877  1.00 50.77  ? 64  TRP C C   1 
ATOM   4669 O  O   . TRP C 1 64  ? -62.207 76.206  18.799  1.00 51.70  ? 64  TRP C O   1 
ATOM   4670 C  CB  . TRP C 1 64  ? -59.944 76.398  20.766  1.00 52.18  ? 64  TRP C CB  1 
ATOM   4671 C  CG  . TRP C 1 64  ? -59.200 76.773  22.013  1.00 47.87  ? 64  TRP C CG  1 
ATOM   4672 C  CD1 . TRP C 1 64  ? -59.529 76.457  23.332  1.00 45.72  ? 64  TRP C CD1 1 
ATOM   4673 C  CD2 . TRP C 1 64  ? -57.980 77.556  22.098  1.00 42.65  ? 64  TRP C CD2 1 
ATOM   4674 N  NE1 . TRP C 1 64  ? -58.618 76.983  24.195  1.00 44.84  ? 64  TRP C NE1 1 
ATOM   4675 C  CE2 . TRP C 1 64  ? -57.658 77.653  23.524  1.00 43.78  ? 64  TRP C CE2 1 
ATOM   4676 C  CE3 . TRP C 1 64  ? -57.143 78.164  21.170  1.00 44.98  ? 64  TRP C CE3 1 
ATOM   4677 C  CZ2 . TRP C 1 64  ? -56.542 78.337  23.979  1.00 44.07  ? 64  TRP C CZ2 1 
ATOM   4678 C  CZ3 . TRP C 1 64  ? -56.027 78.851  21.637  1.00 38.60  ? 64  TRP C CZ3 1 
ATOM   4679 C  CH2 . TRP C 1 64  ? -55.737 78.937  23.009  1.00 42.53  ? 64  TRP C CH2 1 
ATOM   4680 N  N   . THR C 1 65  ? -60.634 77.436  17.812  1.00 54.71  ? 65  THR C N   1 
ATOM   4681 C  CA  . THR C 1 65  ? -60.818 76.748  16.540  1.00 65.04  ? 65  THR C CA  1 
ATOM   4682 C  C   . THR C 1 65  ? -60.017 75.434  16.626  1.00 72.56  ? 65  THR C C   1 
ATOM   4683 O  O   . THR C 1 65  ? -59.065 75.335  17.404  1.00 74.05  ? 65  THR C O   1 
ATOM   4684 C  CB  . THR C 1 65  ? -60.410 77.617  15.331  1.00 72.06  ? 65  THR C CB  1 
ATOM   4685 O  OG1 . THR C 1 65  ? -60.957 78.934  15.474  1.00 77.48  ? 65  THR C OG1 1 
ATOM   4686 C  CG2 . THR C 1 65  ? -60.927 77.015  14.027  1.00 74.18  ? 65  THR C CG2 1 
ATOM   4687 N  N   . VAL C 1 66  ? -60.430 74.423  15.863  1.00 72.97  ? 66  VAL C N   1 
ATOM   4688 C  CA  . VAL C 1 66  ? -59.889 73.066  15.995  1.00 72.03  ? 66  VAL C CA  1 
ATOM   4689 C  C   . VAL C 1 66  ? -60.302 72.242  14.777  1.00 74.65  ? 66  VAL C C   1 
ATOM   4690 O  O   . VAL C 1 66  ? -61.495 72.112  14.498  1.00 79.69  ? 66  VAL C O   1 
ATOM   4691 C  CB  . VAL C 1 66  ? -60.329 72.410  17.335  1.00 68.55  ? 66  VAL C CB  1 
ATOM   4692 C  CG1 . VAL C 1 66  ? -61.820 72.573  17.578  1.00 67.68  ? 66  VAL C CG1 1 
ATOM   4693 C  CG2 . VAL C 1 66  ? -59.928 70.950  17.403  1.00 72.00  ? 66  VAL C CG2 1 
ATOM   4694 N  N   . GLN C 1 67  ? -59.324 71.711  14.037  1.00 74.89  ? 67  GLN C N   1 
ATOM   4695 C  CA  . GLN C 1 67  ? -59.628 70.994  12.784  1.00 70.98  ? 67  GLN C CA  1 
ATOM   4696 C  C   . GLN C 1 67  ? -58.926 69.664  12.477  1.00 70.00  ? 67  GLN C C   1 
ATOM   4697 O  O   . GLN C 1 67  ? -57.776 69.427  12.870  1.00 70.04  ? 67  GLN C O   1 
ATOM   4698 C  CB  . GLN C 1 67  ? -59.549 71.909  11.554  1.00 64.65  ? 67  GLN C CB  1 
ATOM   4699 C  CG  . GLN C 1 67  ? -58.286 72.735  11.388  1.00 67.95  ? 67  GLN C CG  1 
ATOM   4700 C  CD  . GLN C 1 67  ? -58.518 73.967  10.523  1.00 66.77  ? 67  GLN C CD  1 
ATOM   4701 O  OE1 . GLN C 1 67  ? -59.500 74.694  10.703  1.00 64.53  ? 67  GLN C OE1 1 
ATOM   4702 N  NE2 . GLN C 1 67  ? -57.613 74.204  9.575   1.00 64.88  ? 67  GLN C NE2 1 
ATOM   4703 N  N   . ASN C 1 68  ? -59.670 68.815  11.768  1.00 63.24  ? 68  ASN C N   1 
ATOM   4704 C  CA  . ASN C 1 68  ? -59.147 67.640  11.096  1.00 61.11  ? 68  ASN C CA  1 
ATOM   4705 C  C   . ASN C 1 68  ? -58.477 68.055  9.798   1.00 61.53  ? 68  ASN C C   1 
ATOM   4706 O  O   . ASN C 1 68  ? -59.144 68.221  8.767   1.00 56.22  ? 68  ASN C O   1 
ATOM   4707 C  CB  . ASN C 1 68  ? -60.286 66.651  10.814  1.00 62.07  ? 68  ASN C CB  1 
ATOM   4708 C  CG  . ASN C 1 68  ? -59.803 65.337  10.204  1.00 64.16  ? 68  ASN C CG  1 
ATOM   4709 O  OD1 . ASN C 1 68  ? -58.844 65.298  9.417   1.00 59.07  ? 68  ASN C OD1 1 
ATOM   4710 N  ND2 . ASN C 1 68  ? -60.494 64.249  10.542  1.00 64.12  ? 68  ASN C ND2 1 
ATOM   4711 N  N   . ASN C 1 69  ? -57.154 68.212  9.853   1.00 63.53  ? 69  ASN C N   1 
ATOM   4712 C  CA  . ASN C 1 69  ? -56.362 68.604  8.674   1.00 63.09  ? 69  ASN C CA  1 
ATOM   4713 C  C   . ASN C 1 69  ? -56.020 67.465  7.706   1.00 59.80  ? 69  ASN C C   1 
ATOM   4714 O  O   . ASN C 1 69  ? -55.196 67.624  6.793   1.00 58.15  ? 69  ASN C O   1 
ATOM   4715 C  CB  . ASN C 1 69  ? -55.079 69.339  9.102   1.00 63.04  ? 69  ASN C CB  1 
ATOM   4716 C  CG  . ASN C 1 69  ? -54.045 68.425  9.753   1.00 58.95  ? 69  ASN C CG  1 
ATOM   4717 O  OD1 . ASN C 1 69  ? -54.220 67.206  9.872   1.00 57.93  ? 69  ASN C OD1 1 
ATOM   4718 N  ND2 . ASN C 1 69  ? -52.957 69.028  10.191  1.00 53.97  ? 69  ASN C ND2 1 
ATOM   4719 N  N   . GLY C 1 70  ? -56.640 66.314  7.927   1.00 61.84  ? 70  GLY C N   1 
ATOM   4720 C  CA  . GLY C 1 70  ? -56.440 65.138  7.077   1.00 62.38  ? 70  GLY C CA  1 
ATOM   4721 C  C   . GLY C 1 70  ? -55.451 64.151  7.657   1.00 59.22  ? 70  GLY C C   1 
ATOM   4722 O  O   . GLY C 1 70  ? -55.311 63.037  7.143   1.00 62.86  ? 70  GLY C O   1 
ATOM   4723 N  N   . HIS C 1 71  ? -54.769 64.569  8.725   1.00 56.57  ? 71  HIS C N   1 
ATOM   4724 C  CA  . HIS C 1 71  ? -53.674 63.806  9.335   1.00 53.78  ? 71  HIS C CA  1 
ATOM   4725 C  C   . HIS C 1 71  ? -53.626 63.921  10.834  1.00 47.81  ? 71  HIS C C   1 
ATOM   4726 O  O   . HIS C 1 71  ? -52.874 63.187  11.481  1.00 47.85  ? 71  HIS C O   1 
ATOM   4727 C  CB  . HIS C 1 71  ? -52.331 64.241  8.761   1.00 60.07  ? 71  HIS C CB  1 
ATOM   4728 C  CG  . HIS C 1 71  ? -52.333 64.431  7.263   1.00 65.79  ? 71  HIS C CG  1 
ATOM   4729 N  ND1 . HIS C 1 71  ? -52.563 63.417  6.402   1.00 71.47  ? 71  HIS C ND1 1 
ATOM   4730 C  CD2 . HIS C 1 71  ? -52.117 65.574  6.482   1.00 72.87  ? 71  HIS C CD2 1 
ATOM   4731 C  CE1 . HIS C 1 71  ? -52.495 63.882  5.132   1.00 76.91  ? 71  HIS C CE1 1 
ATOM   4732 N  NE2 . HIS C 1 71  ? -52.224 65.203  5.184   1.00 75.64  ? 71  HIS C NE2 1 
ATOM   4733 N  N   . SER C 1 72  ? -54.401 64.846  11.398  1.00 42.99  ? 72  SER C N   1 
ATOM   4734 C  CA  . SER C 1 72  ? -54.494 65.009  12.858  1.00 40.32  ? 72  SER C CA  1 
ATOM   4735 C  C   . SER C 1 72  ? -55.644 65.900  13.314  1.00 41.16  ? 72  SER C C   1 
ATOM   4736 O  O   . SER C 1 72  ? -56.230 66.638  12.505  1.00 44.80  ? 72  SER C O   1 
ATOM   4737 C  CB  . SER C 1 72  ? -53.192 65.611  13.377  1.00 39.05  ? 72  SER C CB  1 
ATOM   4738 O  OG  . SER C 1 72  ? -53.124 65.573  14.788  1.00 37.42  ? 72  SER C OG  1 
ATOM   4739 N  N   . VAL C 1 73  ? -55.946 65.858  14.616  1.00 41.96  ? 73  VAL C N   1 
ATOM   4740 C  CA  . VAL C 1 73  ? -56.725 66.925  15.240  1.00 46.97  ? 73  VAL C CA  1 
ATOM   4741 C  C   . VAL C 1 73  ? -55.856 68.166  15.599  1.00 51.82  ? 73  VAL C C   1 
ATOM   4742 O  O   . VAL C 1 73  ? -55.166 68.184  16.629  1.00 48.79  ? 73  VAL C O   1 
ATOM   4743 C  CB  . VAL C 1 73  ? -57.547 66.443  16.466  1.00 49.34  ? 73  VAL C CB  1 
ATOM   4744 C  CG1 . VAL C 1 73  ? -56.705 65.628  17.448  1.00 46.80  ? 73  VAL C CG1 1 
ATOM   4745 C  CG2 . VAL C 1 73  ? -58.211 67.624  17.171  1.00 48.61  ? 73  VAL C CG2 1 
ATOM   4746 N  N   . MET C 1 74  ? -55.913 69.199  14.755  1.00 55.29  ? 74  MET C N   1 
ATOM   4747 C  CA  . MET C 1 74  ? -55.097 70.419  14.933  1.00 52.05  ? 74  MET C CA  1 
ATOM   4748 C  C   . MET C 1 74  ? -55.880 71.666  15.393  1.00 56.77  ? 74  MET C C   1 
ATOM   4749 O  O   . MET C 1 74  ? -56.598 72.309  14.607  1.00 53.15  ? 74  MET C O   1 
ATOM   4750 C  CB  . MET C 1 74  ? -54.337 70.700  13.646  1.00 49.65  ? 74  MET C CB  1 
ATOM   4751 C  CG  . MET C 1 74  ? -53.334 71.811  13.762  1.00 50.97  ? 74  MET C CG  1 
ATOM   4752 S  SD  . MET C 1 74  ? -53.517 72.790  12.286  1.00 48.78  ? 74  MET C SD  1 
ATOM   4753 C  CE  . MET C 1 74  ? -52.224 72.214  11.205  1.00 48.52  ? 74  MET C CE  1 
ATOM   4754 N  N   . MET C 1 75  ? -55.728 72.012  16.670  1.00 55.56  ? 75  MET C N   1 
ATOM   4755 C  CA  . MET C 1 75  ? -56.515 73.093  17.255  1.00 53.83  ? 75  MET C CA  1 
ATOM   4756 C  C   . MET C 1 75  ? -55.868 74.480  17.063  1.00 53.84  ? 75  MET C C   1 
ATOM   4757 O  O   . MET C 1 75  ? -54.699 74.699  17.403  1.00 43.35  ? 75  MET C O   1 
ATOM   4758 C  CB  . MET C 1 75  ? -56.929 72.792  18.720  1.00 49.20  ? 75  MET C CB  1 
ATOM   4759 C  CG  . MET C 1 75  ? -55.814 72.689  19.737  1.00 47.00  ? 75  MET C CG  1 
ATOM   4760 S  SD  . MET C 1 75  ? -56.355 72.520  21.451  1.00 53.06  ? 75  MET C SD  1 
ATOM   4761 C  CE  . MET C 1 75  ? -56.665 74.235  21.876  1.00 48.85  ? 75  MET C CE  1 
ATOM   4762 N  N   . LEU C 1 76  ? -56.630 75.404  16.478  1.00 58.06  ? 76  LEU C N   1 
ATOM   4763 C  CA  . LEU C 1 76  ? -56.062 76.703  16.120  1.00 62.72  ? 76  LEU C CA  1 
ATOM   4764 C  C   . LEU C 1 76  ? -55.748 77.562  17.337  1.00 62.61  ? 76  LEU C C   1 
ATOM   4765 O  O   . LEU C 1 76  ? -56.634 77.987  18.085  1.00 63.80  ? 76  LEU C O   1 
ATOM   4766 C  CB  . LEU C 1 76  ? -56.908 77.440  15.081  1.00 62.42  ? 76  LEU C CB  1 
ATOM   4767 C  CG  . LEU C 1 76  ? -56.886 76.785  13.695  1.00 67.30  ? 76  LEU C CG  1 
ATOM   4768 C  CD1 . LEU C 1 76  ? -57.750 77.538  12.688  1.00 71.02  ? 76  LEU C CD1 1 
ATOM   4769 C  CD2 . LEU C 1 76  ? -55.463 76.658  13.170  1.00 69.12  ? 76  LEU C CD2 1 
ATOM   4770 N  N   . LEU C 1 77  ? -54.478 77.922  17.455  1.00 63.72  ? 77  LEU C N   1 
ATOM   4771 C  CA  . LEU C 1 77  ? -54.011 78.761  18.537  1.00 65.05  ? 77  LEU C CA  1 
ATOM   4772 C  C   . LEU C 1 77  ? -53.664 79.865  17.518  1.00 73.66  ? 77  LEU C C   1 
ATOM   4773 O  O   . LEU C 1 77  ? -53.460 79.564  16.357  1.00 77.07  ? 77  LEU C O   1 
ATOM   4774 C  CB  . LEU C 1 77  ? -52.659 78.290  19.040  1.00 57.74  ? 77  LEU C CB  1 
ATOM   4775 C  CG  . LEU C 1 77  ? -52.557 76.838  19.482  1.00 51.77  ? 77  LEU C CG  1 
ATOM   4776 C  CD1 . LEU C 1 77  ? -51.403 76.631  20.407  1.00 50.61  ? 77  LEU C CD1 1 
ATOM   4777 C  CD2 . LEU C 1 77  ? -53.806 76.330  20.130  1.00 58.58  ? 77  LEU C CD2 1 
ATOM   4778 N  N   . GLU C 1 78  ? -53.568 81.123  17.909  1.00 75.59  ? 78  GLU C N   1 
ATOM   4779 C  CA  . GLU C 1 78  ? -52.995 82.135  16.994  1.00 73.15  ? 78  GLU C CA  1 
ATOM   4780 C  C   . GLU C 1 78  ? -52.035 83.243  17.475  1.00 69.88  ? 78  GLU C C   1 
ATOM   4781 O  O   . GLU C 1 78  ? -51.142 83.608  16.714  1.00 63.10  ? 78  GLU C O   1 
ATOM   4782 C  CB  . GLU C 1 78  ? -54.446 82.612  16.767  1.00 66.20  ? 78  GLU C CB  1 
ATOM   4783 C  CG  . GLU C 1 78  ? -55.138 81.895  15.604  1.00 62.23  ? 78  GLU C CG  1 
ATOM   4784 C  CD  . GLU C 1 78  ? -56.651 81.809  15.712  1.00 56.85  ? 78  GLU C CD  1 
ATOM   4785 O  OE1 . GLU C 1 78  ? -57.158 81.889  16.827  1.00 51.01  ? 78  GLU C OE1 1 
ATOM   4786 O  OE2 . GLU C 1 78  ? -57.323 81.647  14.674  1.00 49.73  ? 78  GLU C OE2 1 
ATOM   4787 N  N   . ASN C 1 79  ? -52.124 83.740  18.706  1.00 60.16  ? 79  ASN C N   1 
ATOM   4788 C  CA  . ASN C 1 79  ? -53.206 83.601  19.651  1.00 58.08  ? 79  ASN C CA  1 
ATOM   4789 C  C   . ASN C 1 79  ? -52.856 83.942  21.135  1.00 58.42  ? 79  ASN C C   1 
ATOM   4790 O  O   . ASN C 1 79  ? -52.082 84.829  21.418  1.00 48.68  ? 79  ASN C O   1 
ATOM   4791 C  CB  . ASN C 1 79  ? -54.147 82.475  19.402  1.00 63.62  ? 79  ASN C CB  1 
ATOM   4792 C  CG  . ASN C 1 79  ? -55.466 82.647  20.120  1.00 62.68  ? 79  ASN C CG  1 
ATOM   4793 O  OD1 . ASN C 1 79  ? -55.508 82.952  21.291  1.00 64.19  ? 79  ASN C OD1 1 
ATOM   4794 N  ND2 . ASN C 1 79  ? -56.544 82.452  19.410  1.00 63.08  ? 79  ASN C ND2 1 
ATOM   4795 N  N   . LYS C 1 80  ? -53.483 83.218  22.046  1.00 58.52  ? 80  LYS C N   1 
ATOM   4796 C  CA  . LYS C 1 80  ? -53.439 83.530  23.439  1.00 57.99  ? 80  LYS C CA  1 
ATOM   4797 C  C   . LYS C 1 80  ? -52.104 83.049  24.009  1.00 55.39  ? 80  LYS C C   1 
ATOM   4798 O  O   . LYS C 1 80  ? -51.919 82.996  25.198  1.00 61.41  ? 80  LYS C O   1 
ATOM   4799 C  CB  . LYS C 1 80  ? -54.621 82.882  24.183  1.00 62.31  ? 80  LYS C CB  1 
ATOM   4800 C  CG  . LYS C 1 80  ? -54.618 83.006  25.679  1.00 63.77  ? 80  LYS C CG  1 
ATOM   4801 C  CD  . LYS C 1 80  ? -55.916 83.620  26.150  1.00 67.90  ? 80  LYS C CD  1 
ATOM   4802 C  CE  . LYS C 1 80  ? -55.822 85.144  26.239  1.00 60.19  ? 80  LYS C CE  1 
ATOM   4803 N  NZ  . LYS C 1 80  ? -55.332 85.647  27.544  1.00 56.82  ? 80  LYS C NZ  1 
ATOM   4804 N  N   . ALA C 1 81  ? -51.172 82.708  23.133  1.00 49.57  ? 81  ALA C N   1 
ATOM   4805 C  CA  . ALA C 1 81  ? -49.922 82.114  23.543  1.00 48.92  ? 81  ALA C CA  1 
ATOM   4806 C  C   . ALA C 1 81  ? -48.652 82.344  22.777  1.00 43.64  ? 81  ALA C C   1 
ATOM   4807 O  O   . ALA C 1 81  ? -48.584 82.353  21.570  1.00 39.66  ? 81  ALA C O   1 
ATOM   4808 C  CB  . ALA C 1 81  ? -50.192 80.627  23.407  1.00 51.24  ? 81  ALA C CB  1 
ATOM   4809 N  N   . SER C 1 82  ? -47.611 82.505  23.559  1.00 45.88  ? 82  SER C N   1 
ATOM   4810 C  CA  . SER C 1 82  ? -46.255 82.432  23.046  1.00 45.24  ? 82  SER C CA  1 
ATOM   4811 C  C   . SER C 1 82  ? -45.418 81.825  24.173  1.00 43.86  ? 82  SER C C   1 
ATOM   4812 O  O   . SER C 1 82  ? -45.937 81.536  25.276  1.00 38.46  ? 82  SER C O   1 
ATOM   4813 C  CB  . SER C 1 82  ? -45.810 83.860  22.729  1.00 46.88  ? 82  SER C CB  1 
ATOM   4814 O  OG  . SER C 1 82  ? -45.572 84.575  23.926  1.00 52.78  ? 82  SER C OG  1 
ATOM   4815 N  N   . ILE C 1 83  ? -44.138 81.609  23.936  1.00 37.87  ? 83  ILE C N   1 
ATOM   4816 C  CA  . ILE C 1 83  ? -43.339 81.072  25.035  1.00 43.37  ? 83  ILE C CA  1 
ATOM   4817 C  C   . ILE C 1 83  ? -42.006 81.746  25.053  1.00 43.23  ? 83  ILE C C   1 
ATOM   4818 O  O   . ILE C 1 83  ? -41.571 82.294  24.053  1.00 45.33  ? 83  ILE C O   1 
ATOM   4819 C  CB  . ILE C 1 83  ? -43.053 79.536  24.920  1.00 41.48  ? 83  ILE C CB  1 
ATOM   4820 C  CG1 . ILE C 1 83  ? -42.592 79.175  23.496  1.00 42.09  ? 83  ILE C CG1 1 
ATOM   4821 C  CG2 . ILE C 1 83  ? -44.225 78.701  25.459  1.00 41.68  ? 83  ILE C CG2 1 
ATOM   4822 C  CD1 . ILE C 1 83  ? -42.145 77.727  23.332  1.00 44.66  ? 83  ILE C CD1 1 
ATOM   4823 N  N   . SER C 1 84  ? -41.332 81.649  26.185  1.00 45.52  ? 84  SER C N   1 
ATOM   4824 C  CA  . SER C 1 84  ? -39.904 81.910  26.179  1.00 45.59  ? 84  SER C CA  1 
ATOM   4825 C  C   . SER C 1 84  ? -39.360 81.231  27.393  1.00 47.35  ? 84  SER C C   1 
ATOM   4826 O  O   . SER C 1 84  ? -40.124 80.686  28.220  1.00 46.72  ? 84  SER C O   1 
ATOM   4827 C  CB  . SER C 1 84  ? -39.601 83.420  26.226  1.00 49.50  ? 84  SER C CB  1 
ATOM   4828 O  OG  . SER C 1 84  ? -40.179 83.993  27.375  1.00 43.93  ? 84  SER C OG  1 
ATOM   4829 N  N   . GLY C 1 85  ? -38.042 81.291  27.507  1.00 46.26  ? 85  GLY C N   1 
ATOM   4830 C  CA  . GLY C 1 85  ? -37.332 80.620  28.572  1.00 50.14  ? 85  GLY C CA  1 
ATOM   4831 C  C   . GLY C 1 85  ? -36.863 79.266  28.086  1.00 51.28  ? 85  GLY C C   1 
ATOM   4832 O  O   . GLY C 1 85  ? -36.512 79.106  26.904  1.00 47.07  ? 85  GLY C O   1 
ATOM   4833 N  N   . GLY C 1 86  ? -36.846 78.299  28.999  1.00 48.25  ? 86  GLY C N   1 
ATOM   4834 C  CA  . GLY C 1 86  ? -36.418 76.957  28.668  1.00 49.77  ? 86  GLY C CA  1 
ATOM   4835 C  C   . GLY C 1 86  ? -35.213 76.956  27.760  1.00 48.36  ? 86  GLY C C   1 
ATOM   4836 O  O   . GLY C 1 86  ? -35.133 76.148  26.843  1.00 49.49  ? 86  GLY C O   1 
ATOM   4837 N  N   . GLY C 1 87  ? -34.303 77.898  27.992  1.00 50.47  ? 87  GLY C N   1 
ATOM   4838 C  CA  . GLY C 1 87  ? -33.057 78.023  27.229  1.00 45.31  ? 87  GLY C CA  1 
ATOM   4839 C  C   . GLY C 1 87  ? -33.182 78.379  25.762  1.00 45.60  ? 87  GLY C C   1 
ATOM   4840 O  O   . GLY C 1 87  ? -32.267 78.094  24.981  1.00 43.62  ? 87  GLY C O   1 
ATOM   4841 N  N   . LEU C 1 88  ? -34.317 78.982  25.402  1.00 46.46  ? 88  LEU C N   1 
ATOM   4842 C  CA  . LEU C 1 88  ? -34.633 79.431  24.045  1.00 50.93  ? 88  LEU C CA  1 
ATOM   4843 C  C   . LEU C 1 88  ? -33.996 80.776  23.728  1.00 59.58  ? 88  LEU C C   1 
ATOM   4844 O  O   . LEU C 1 88  ? -33.941 81.648  24.594  1.00 58.30  ? 88  LEU C O   1 
ATOM   4845 C  CB  . LEU C 1 88  ? -36.165 79.538  23.847  1.00 46.09  ? 88  LEU C CB  1 
ATOM   4846 C  CG  . LEU C 1 88  ? -36.863 78.212  23.500  1.00 50.51  ? 88  LEU C CG  1 
ATOM   4847 C  CD1 . LEU C 1 88  ? -38.388 78.264  23.602  1.00 43.74  ? 88  LEU C CD1 1 
ATOM   4848 C  CD2 . LEU C 1 88  ? -36.414 77.716  22.123  1.00 46.59  ? 88  LEU C CD2 1 
ATOM   4849 N  N   . PRO C 1 89  ? -33.520 80.950  22.477  1.00 65.70  ? 89  PRO C N   1 
ATOM   4850 C  CA  . PRO C 1 89  ? -32.873 82.196  22.034  1.00 66.45  ? 89  PRO C CA  1 
ATOM   4851 C  C   . PRO C 1 89  ? -33.690 83.467  22.303  1.00 64.55  ? 89  PRO C C   1 
ATOM   4852 O  O   . PRO C 1 89  ? -33.130 84.458  22.791  1.00 64.85  ? 89  PRO C O   1 
ATOM   4853 C  CB  . PRO C 1 89  ? -32.697 81.973  20.528  1.00 65.98  ? 89  PRO C CB  1 
ATOM   4854 C  CG  . PRO C 1 89  ? -32.507 80.496  20.416  1.00 70.15  ? 89  PRO C CG  1 
ATOM   4855 C  CD  . PRO C 1 89  ? -33.408 79.887  21.457  1.00 65.99  ? 89  PRO C CD  1 
ATOM   4856 N  N   . ALA C 1 90  ? -34.992 83.411  22.004  1.00 61.92  ? 90  ALA C N   1 
ATOM   4857 C  CA  . ALA C 1 90  ? -35.900 84.568  22.016  1.00 60.81  ? 90  ALA C CA  1 
ATOM   4858 C  C   . ALA C 1 90  ? -37.351 84.091  22.194  1.00 58.94  ? 90  ALA C C   1 
ATOM   4859 O  O   . ALA C 1 90  ? -37.580 82.897  22.279  1.00 63.54  ? 90  ALA C O   1 
ATOM   4860 C  CB  . ALA C 1 90  ? -35.743 85.366  20.727  1.00 56.33  ? 90  ALA C CB  1 
ATOM   4861 N  N   . PRO C 1 91  ? -38.335 85.014  22.296  1.00 61.40  ? 91  PRO C N   1 
ATOM   4862 C  CA  . PRO C 1 91  ? -39.741 84.542  22.327  1.00 57.38  ? 91  PRO C CA  1 
ATOM   4863 C  C   . PRO C 1 91  ? -40.172 83.801  21.048  1.00 57.30  ? 91  PRO C C   1 
ATOM   4864 O  O   . PRO C 1 91  ? -39.691 84.104  19.942  1.00 56.88  ? 91  PRO C O   1 
ATOM   4865 C  CB  . PRO C 1 91  ? -40.551 85.839  22.479  1.00 56.21  ? 91  PRO C CB  1 
ATOM   4866 C  CG  . PRO C 1 91  ? -39.615 86.789  23.141  1.00 57.46  ? 91  PRO C CG  1 
ATOM   4867 C  CD  . PRO C 1 91  ? -38.220 86.428  22.713  1.00 58.74  ? 91  PRO C CD  1 
ATOM   4868 N  N   . TYR C 1 92  ? -41.064 82.822  21.209  1.00 55.50  ? 92  TYR C N   1 
ATOM   4869 C  CA  . TYR C 1 92  ? -41.628 82.097  20.069  1.00 48.45  ? 92  TYR C CA  1 
ATOM   4870 C  C   . TYR C 1 92  ? -43.156 82.228  20.154  1.00 46.59  ? 92  TYR C C   1 
ATOM   4871 O  O   . TYR C 1 92  ? -43.727 82.053  21.222  1.00 42.71  ? 92  TYR C O   1 
ATOM   4872 C  CB  . TYR C 1 92  ? -41.191 80.628  20.130  1.00 46.12  ? 92  TYR C CB  1 
ATOM   4873 C  CG  . TYR C 1 92  ? -39.747 80.325  19.683  1.00 45.96  ? 92  TYR C CG  1 
ATOM   4874 C  CD1 . TYR C 1 92  ? -38.639 80.805  20.402  1.00 41.82  ? 92  TYR C CD1 1 
ATOM   4875 C  CD2 . TYR C 1 92  ? -39.494 79.515  18.562  1.00 39.16  ? 92  TYR C CD2 1 
ATOM   4876 C  CE1 . TYR C 1 92  ? -37.336 80.509  20.001  1.00 40.08  ? 92  TYR C CE1 1 
ATOM   4877 C  CE2 . TYR C 1 92  ? -38.187 79.225  18.158  1.00 40.54  ? 92  TYR C CE2 1 
ATOM   4878 C  CZ  . TYR C 1 92  ? -37.121 79.730  18.868  1.00 39.21  ? 92  TYR C CZ  1 
ATOM   4879 O  OH  . TYR C 1 92  ? -35.841 79.425  18.471  1.00 42.36  ? 92  TYR C OH  1 
ATOM   4880 N  N   . GLN C 1 93  ? -43.838 82.579  19.070  1.00 46.59  ? 93  GLN C N   1 
ATOM   4881 C  CA  . GLN C 1 93  ? -45.312 82.648  19.175  1.00 54.24  ? 93  GLN C CA  1 
ATOM   4882 C  C   . GLN C 1 93  ? -46.009 81.333  18.743  1.00 55.84  ? 93  GLN C C   1 
ATOM   4883 O  O   . GLN C 1 93  ? -45.578 80.686  17.791  1.00 62.82  ? 93  GLN C O   1 
ATOM   4884 C  CB  . GLN C 1 93  ? -45.899 83.883  18.452  1.00 57.02  ? 93  GLN C CB  1 
ATOM   4885 C  CG  . GLN C 1 93  ? -46.298 85.053  19.363  1.00 54.78  ? 93  GLN C CG  1 
ATOM   4886 C  CD  . GLN C 1 93  ? -47.669 85.641  19.013  1.00 58.35  ? 93  GLN C CD  1 
ATOM   4887 O  OE1 . GLN C 1 93  ? -48.575 85.751  19.870  1.00 50.53  ? 93  GLN C OE1 1 
ATOM   4888 N  NE2 . GLN C 1 93  ? -47.832 86.023  17.748  1.00 54.59  ? 93  GLN C NE2 1 
ATOM   4889 N  N   . ALA C 1 94  ? -47.063 80.945  19.461  1.00 56.54  ? 94  ALA C N   1 
ATOM   4890 C  CA  . ALA C 1 94  ? -47.870 79.770  19.097  1.00 61.11  ? 94  ALA C CA  1 
ATOM   4891 C  C   . ALA C 1 94  ? -48.352 79.853  17.641  1.00 64.90  ? 94  ALA C C   1 
ATOM   4892 O  O   . ALA C 1 94  ? -48.789 80.922  17.174  1.00 62.40  ? 94  ALA C O   1 
ATOM   4893 C  CB  . ALA C 1 94  ? -49.044 79.595  20.057  1.00 57.57  ? 94  ALA C CB  1 
ATOM   4894 N  N   . LYS C 1 95  ? -48.211 78.738  16.921  1.00 57.56  ? 95  LYS C N   1 
ATOM   4895 C  CA  . LYS C 1 95  ? -48.709 78.605  15.551  1.00 54.03  ? 95  LYS C CA  1 
ATOM   4896 C  C   . LYS C 1 95  ? -49.855 77.591  15.599  1.00 54.84  ? 95  LYS C C   1 
ATOM   4897 O  O   . LYS C 1 95  ? -50.980 77.925  15.227  1.00 52.18  ? 95  LYS C O   1 
ATOM   4898 C  CB  . LYS C 1 95  ? -47.584 78.163  14.583  1.00 59.17  ? 95  LYS C CB  1 
ATOM   4899 C  CG  . LYS C 1 95  ? -47.457 78.970  13.285  1.00 62.60  ? 95  LYS C CG  1 
ATOM   4900 C  CD  . LYS C 1 95  ? -48.085 78.284  12.061  1.00 65.17  ? 95  LYS C CD  1 
ATOM   4901 C  CE  . LYS C 1 95  ? -48.428 79.248  10.909  1.00 67.92  ? 95  LYS C CE  1 
ATOM   4902 N  NZ  . LYS C 1 95  ? -47.525 80.421  10.650  1.00 64.93  ? 95  LYS C NZ  1 
ATOM   4903 N  N   . GLN C 1 96  ? -49.584 76.370  16.094  1.00 53.79  ? 96  GLN C N   1 
ATOM   4904 C  CA  . GLN C 1 96  ? -50.647 75.358  16.304  1.00 52.22  ? 96  GLN C CA  1 
ATOM   4905 C  C   . GLN C 1 96  ? -50.361 74.262  17.354  1.00 50.78  ? 96  GLN C C   1 
ATOM   4906 O  O   . GLN C 1 96  ? -49.219 74.076  17.756  1.00 49.11  ? 96  GLN C O   1 
ATOM   4907 C  CB  . GLN C 1 96  ? -51.108 74.772  14.958  1.00 49.51  ? 96  GLN C CB  1 
ATOM   4908 C  CG  . GLN C 1 96  ? -50.002 74.467  13.959  1.00 49.89  ? 96  GLN C CG  1 
ATOM   4909 C  CD  . GLN C 1 96  ? -49.678 72.995  13.902  1.00 46.15  ? 96  GLN C CD  1 
ATOM   4910 O  OE1 . GLN C 1 96  ? -49.766 72.292  14.900  1.00 47.90  ? 96  GLN C OE1 1 
ATOM   4911 N  NE2 . GLN C 1 96  ? -49.333 72.520  12.732  1.00 45.44  ? 96  GLN C NE2 1 
ATOM   4912 N  N   . LEU C 1 97  ? -51.421 73.586  17.818  1.00 51.89  ? 97  LEU C N   1 
ATOM   4913 C  CA  . LEU C 1 97  ? -51.334 72.378  18.656  1.00 47.17  ? 97  LEU C CA  1 
ATOM   4914 C  C   . LEU C 1 97  ? -51.996 71.102  18.066  1.00 51.07  ? 97  LEU C C   1 
ATOM   4915 O  O   . LEU C 1 97  ? -53.239 70.951  18.107  1.00 47.73  ? 97  LEU C O   1 
ATOM   4916 C  CB  . LEU C 1 97  ? -51.951 72.631  20.035  1.00 48.77  ? 97  LEU C CB  1 
ATOM   4917 C  CG  . LEU C 1 97  ? -52.108 71.455  21.027  1.00 51.35  ? 97  LEU C CG  1 
ATOM   4918 C  CD1 . LEU C 1 97  ? -51.987 71.884  22.472  1.00 51.21  ? 97  LEU C CD1 1 
ATOM   4919 C  CD2 . LEU C 1 97  ? -53.412 70.691  20.867  1.00 52.25  ? 97  LEU C CD2 1 
ATOM   4920 N  N   . HIS C 1 98  ? -51.163 70.154  17.617  1.00 49.61  ? 98  HIS C N   1 
ATOM   4921 C  CA  . HIS C 1 98  ? -51.625 68.865  17.064  1.00 42.82  ? 98  HIS C CA  1 
ATOM   4922 C  C   . HIS C 1 98  ? -51.086 67.614  17.744  1.00 47.31  ? 98  HIS C C   1 
ATOM   4923 O  O   . HIS C 1 98  ? -50.118 67.646  18.530  1.00 44.75  ? 98  HIS C O   1 
ATOM   4924 C  CB  . HIS C 1 98  ? -51.324 68.819  15.576  1.00 42.92  ? 98  HIS C CB  1 
ATOM   4925 C  CG  . HIS C 1 98  ? -49.858 68.670  15.259  1.00 41.55  ? 98  HIS C CG  1 
ATOM   4926 N  ND1 . HIS C 1 98  ? -49.089 69.703  14.881  1.00 40.82  ? 98  HIS C ND1 1 
ATOM   4927 C  CD2 . HIS C 1 98  ? -49.038 67.548  15.257  1.00 43.48  ? 98  HIS C CD2 1 
ATOM   4928 C  CE1 . HIS C 1 98  ? -47.832 69.275  14.664  1.00 38.47  ? 98  HIS C CE1 1 
ATOM   4929 N  NE2 . HIS C 1 98  ? -47.804 67.948  14.884  1.00 41.83  ? 98  HIS C NE2 1 
ATOM   4930 N  N   . LEU C 1 99  ? -51.706 66.475  17.429  1.00 48.47  ? 99  LEU C N   1 
ATOM   4931 C  CA  . LEU C 1 99  ? -51.347 65.210  18.088  1.00 46.07  ? 99  LEU C CA  1 
ATOM   4932 C  C   . LEU C 1 99  ? -51.040 64.066  17.154  1.00 40.91  ? 99  LEU C C   1 
ATOM   4933 O  O   . LEU C 1 99  ? -51.444 64.053  15.990  1.00 38.95  ? 99  LEU C O   1 
ATOM   4934 C  CB  . LEU C 1 99  ? -52.416 64.778  19.088  1.00 43.52  ? 99  LEU C CB  1 
ATOM   4935 C  CG  . LEU C 1 99  ? -52.363 65.564  20.390  1.00 45.93  ? 99  LEU C CG  1 
ATOM   4936 C  CD1 . LEU C 1 99  ? -53.054 66.912  20.198  1.00 47.22  ? 99  LEU C CD1 1 
ATOM   4937 C  CD2 . LEU C 1 99  ? -53.021 64.766  21.495  1.00 43.31  ? 99  LEU C CD2 1 
ATOM   4938 N  N   . HIS C 1 100 ? -50.304 63.112  17.713  1.00 41.00  ? 100 HIS C N   1 
ATOM   4939 C  CA  . HIS C 1 100 ? -50.011 61.841  17.076  1.00 37.64  ? 100 HIS C CA  1 
ATOM   4940 C  C   . HIS C 1 100 ? -50.329 60.790  18.045  1.00 37.85  ? 100 HIS C C   1 
ATOM   4941 O  O   . HIS C 1 100 ? -49.968 60.925  19.221  1.00 38.68  ? 100 HIS C O   1 
ATOM   4942 C  CB  . HIS C 1 100 ? -48.538 61.747  16.738  1.00 33.69  ? 100 HIS C CB  1 
ATOM   4943 C  CG  . HIS C 1 100 ? -48.101 62.774  15.759  1.00 32.91  ? 100 HIS C CG  1 
ATOM   4944 N  ND1 . HIS C 1 100 ? -48.086 62.549  14.454  1.00 36.09  ? 100 HIS C ND1 1 
ATOM   4945 C  CD2 . HIS C 1 100 ? -47.650 64.086  15.943  1.00 31.13  ? 100 HIS C CD2 1 
ATOM   4946 C  CE1 . HIS C 1 100 ? -47.651 63.682  13.803  1.00 33.64  ? 100 HIS C CE1 1 
ATOM   4947 N  NE2 . HIS C 1 100 ? -47.390 64.598  14.723  1.00 29.45  ? 100 HIS C NE2 1 
ATOM   4948 N  N   . TRP C 1 101 ? -50.948 59.707  17.545  1.00 39.59  ? 101 TRP C N   1 
ATOM   4949 C  CA  . TRP C 1 101 ? -51.423 58.592  18.350  1.00 40.70  ? 101 TRP C CA  1 
ATOM   4950 C  C   . TRP C 1 101 ? -51.677 57.321  17.542  1.00 47.72  ? 101 TRP C C   1 
ATOM   4951 O  O   . TRP C 1 101 ? -51.621 57.312  16.293  1.00 39.40  ? 101 TRP C O   1 
ATOM   4952 C  CB  . TRP C 1 101 ? -52.741 58.956  18.983  1.00 42.65  ? 101 TRP C CB  1 
ATOM   4953 C  CG  . TRP C 1 101 ? -53.832 59.139  17.947  1.00 46.19  ? 101 TRP C CG  1 
ATOM   4954 C  CD1 . TRP C 1 101 ? -54.661 58.164  17.397  1.00 49.09  ? 101 TRP C CD1 1 
ATOM   4955 C  CD2 . TRP C 1 101 ? -54.249 60.388  17.299  1.00 48.28  ? 101 TRP C CD2 1 
ATOM   4956 N  NE1 . TRP C 1 101 ? -55.529 58.714  16.478  1.00 45.82  ? 101 TRP C NE1 1 
ATOM   4957 C  CE2 . TRP C 1 101 ? -55.341 60.036  16.382  1.00 47.28  ? 101 TRP C CE2 1 
ATOM   4958 C  CE3 . TRP C 1 101 ? -53.862 61.707  17.398  1.00 48.05  ? 101 TRP C CE3 1 
ATOM   4959 C  CZ2 . TRP C 1 101 ? -55.983 60.986  15.610  1.00 48.28  ? 101 TRP C CZ2 1 
ATOM   4960 C  CZ3 . TRP C 1 101 ? -54.517 62.649  16.611  1.00 46.01  ? 101 TRP C CZ3 1 
ATOM   4961 C  CH2 . TRP C 1 101 ? -55.542 62.297  15.736  1.00 47.05  ? 101 TRP C CH2 1 
ATOM   4962 N  N   . SER C 1 102 ? -52.007 56.261  18.286  1.00 48.35  ? 102 SER C N   1 
ATOM   4963 C  CA  . SER C 1 102 ? -52.392 54.949  17.766  1.00 54.43  ? 102 SER C CA  1 
ATOM   4964 C  C   . SER C 1 102 ? -53.446 54.356  18.708  1.00 55.69  ? 102 SER C C   1 
ATOM   4965 O  O   . SER C 1 102 ? -53.933 55.040  19.618  1.00 55.89  ? 102 SER C O   1 
ATOM   4966 C  CB  . SER C 1 102 ? -51.166 54.022  17.745  1.00 57.07  ? 102 SER C CB  1 
ATOM   4967 O  OG  . SER C 1 102 ? -51.377 52.888  16.924  1.00 49.86  ? 102 SER C OG  1 
ATOM   4968 N  N   . ASP C 1 103 ? -53.785 53.082  18.504  1.00 57.99  ? 103 ASP C N   1 
ATOM   4969 C  CA  . ASP C 1 103 ? -54.714 52.368  19.403  1.00 54.12  ? 103 ASP C CA  1 
ATOM   4970 C  C   . ASP C 1 103 ? -54.049 51.475  20.463  1.00 52.97  ? 103 ASP C C   1 
ATOM   4971 O  O   . ASP C 1 103 ? -54.737 50.943  21.340  1.00 49.17  ? 103 ASP C O   1 
ATOM   4972 C  CB  . ASP C 1 103 ? -55.753 51.566  18.603  1.00 53.31  ? 103 ASP C CB  1 
ATOM   4973 C  CG  . ASP C 1 103 ? -55.139 50.764  17.440  1.00 49.26  ? 103 ASP C CG  1 
ATOM   4974 O  OD1 . ASP C 1 103 ? -53.916 50.507  17.419  1.00 48.20  ? 103 ASP C OD1 1 
ATOM   4975 O  OD2 . ASP C 1 103 ? -55.891 50.396  16.525  1.00 43.15  ? 103 ASP C OD2 1 
ATOM   4976 N  N   . LEU C 1 104 ? -52.724 51.331  20.401  1.00 52.94  ? 104 LEU C N   1 
ATOM   4977 C  CA  . LEU C 1 104 ? -51.995 50.463  21.343  1.00 56.86  ? 104 LEU C CA  1 
ATOM   4978 C  C   . LEU C 1 104 ? -51.060 51.212  22.293  1.00 60.32  ? 104 LEU C C   1 
ATOM   4979 O  O   . LEU C 1 104 ? -50.307 52.083  21.863  1.00 61.45  ? 104 LEU C O   1 
ATOM   4980 C  CB  . LEU C 1 104 ? -51.222 49.369  20.595  1.00 55.98  ? 104 LEU C CB  1 
ATOM   4981 C  CG  . LEU C 1 104 ? -52.011 48.170  20.035  1.00 58.33  ? 104 LEU C CG  1 
ATOM   4982 C  CD1 . LEU C 1 104 ? -51.301 47.551  18.832  1.00 57.01  ? 104 LEU C CD1 1 
ATOM   4983 C  CD2 . LEU C 1 104 ? -52.308 47.112  21.097  1.00 53.95  ? 104 LEU C CD2 1 
ATOM   4984 N  N   . PRO C 1 105 ? -51.054 50.822  23.582  1.00 59.29  ? 105 PRO C N   1 
ATOM   4985 C  CA  . PRO C 1 105 ? -50.444 51.655  24.619  1.00 60.12  ? 105 PRO C CA  1 
ATOM   4986 C  C   . PRO C 1 105 ? -48.979 51.947  24.328  1.00 61.83  ? 105 PRO C C   1 
ATOM   4987 O  O   . PRO C 1 105 ? -48.463 53.007  24.706  1.00 58.70  ? 105 PRO C O   1 
ATOM   4988 C  CB  . PRO C 1 105 ? -50.564 50.800  25.892  1.00 62.51  ? 105 PRO C CB  1 
ATOM   4989 C  CG  . PRO C 1 105 ? -51.475 49.666  25.554  1.00 58.34  ? 105 PRO C CG  1 
ATOM   4990 C  CD  . PRO C 1 105 ? -51.371 49.473  24.073  1.00 56.98  ? 105 PRO C CD  1 
ATOM   4991 N  N   . TYR C 1 106 ? -48.343 51.004  23.637  1.00 59.45  ? 106 TYR C N   1 
ATOM   4992 C  CA  . TYR C 1 106 ? -46.909 51.003  23.397  1.00 55.15  ? 106 TYR C CA  1 
ATOM   4993 C  C   . TYR C 1 106 ? -46.497 51.598  22.045  1.00 52.10  ? 106 TYR C C   1 
ATOM   4994 O  O   . TYR C 1 106 ? -45.334 51.479  21.674  1.00 56.82  ? 106 TYR C O   1 
ATOM   4995 C  CB  . TYR C 1 106 ? -46.345 49.575  23.533  1.00 57.02  ? 106 TYR C CB  1 
ATOM   4996 C  CG  . TYR C 1 106 ? -47.137 48.483  22.815  1.00 54.78  ? 106 TYR C CG  1 
ATOM   4997 C  CD1 . TYR C 1 106 ? -46.884 48.153  21.484  1.00 55.53  ? 106 TYR C CD1 1 
ATOM   4998 C  CD2 . TYR C 1 106 ? -48.138 47.780  23.481  1.00 58.38  ? 106 TYR C CD2 1 
ATOM   4999 C  CE1 . TYR C 1 106 ? -47.617 47.152  20.837  1.00 56.82  ? 106 TYR C CE1 1 
ATOM   5000 C  CE2 . TYR C 1 106 ? -48.875 46.777  22.848  1.00 58.66  ? 106 TYR C CE2 1 
ATOM   5001 C  CZ  . TYR C 1 106 ? -48.612 46.468  21.531  1.00 57.24  ? 106 TYR C CZ  1 
ATOM   5002 O  OH  . TYR C 1 106 ? -49.349 45.478  20.934  1.00 54.29  ? 106 TYR C OH  1 
ATOM   5003 N  N   . LYS C 1 107 ? -47.407 52.255  21.320  1.00 48.29  ? 107 LYS C N   1 
ATOM   5004 C  CA  . LYS C 1 107 ? -47.060 52.725  19.960  1.00 47.66  ? 107 LYS C CA  1 
ATOM   5005 C  C   . LYS C 1 107 ? -47.589 54.084  19.372  1.00 46.05  ? 107 LYS C C   1 
ATOM   5006 O  O   . LYS C 1 107 ? -47.442 54.323  18.179  1.00 44.83  ? 107 LYS C O   1 
ATOM   5007 C  CB  . LYS C 1 107 ? -47.294 51.607  18.952  1.00 49.45  ? 107 LYS C CB  1 
ATOM   5008 C  CG  . LYS C 1 107 ? -48.733 51.116  18.857  1.00 48.86  ? 107 LYS C CG  1 
ATOM   5009 C  CD  . LYS C 1 107 ? -48.861 50.005  17.808  1.00 46.90  ? 107 LYS C CD  1 
ATOM   5010 C  CE  . LYS C 1 107 ? -48.856 50.562  16.389  1.00 47.51  ? 107 LYS C CE  1 
ATOM   5011 N  NZ  . LYS C 1 107 ? -48.696 49.536  15.309  1.00 46.44  ? 107 LYS C NZ  1 
ATOM   5012 N  N   . GLY C 1 108 ? -48.147 54.986  20.171  1.00 47.88  ? 108 GLY C N   1 
ATOM   5013 C  CA  . GLY C 1 108 ? -48.658 56.284  19.597  1.00 45.03  ? 108 GLY C CA  1 
ATOM   5014 C  C   . GLY C 1 108 ? -47.696 57.466  19.345  1.00 40.45  ? 108 GLY C C   1 
ATOM   5015 O  O   . GLY C 1 108 ? -47.976 58.387  18.533  1.00 34.16  ? 108 GLY C O   1 
ATOM   5016 N  N   . SER C 1 109 ? -46.563 57.453  20.030  1.00 40.67  ? 109 SER C N   1 
ATOM   5017 C  CA  . SER C 1 109 ? -45.680 58.612  20.034  1.00 39.82  ? 109 SER C CA  1 
ATOM   5018 C  C   . SER C 1 109 ? -44.776 58.595  18.810  1.00 36.00  ? 109 SER C C   1 
ATOM   5019 O  O   . SER C 1 109 ? -44.501 57.536  18.236  1.00 33.60  ? 109 SER C O   1 
ATOM   5020 C  CB  . SER C 1 109 ? -44.889 58.667  21.350  1.00 42.14  ? 109 SER C CB  1 
ATOM   5021 O  OG  . SER C 1 109 ? -44.124 57.486  21.562  1.00 44.38  ? 109 SER C OG  1 
ATOM   5022 N  N   . GLU C 1 110 ? -44.354 59.765  18.364  1.00 35.19  ? 110 GLU C N   1 
ATOM   5023 C  CA  . GLU C 1 110 ? -43.322 59.817  17.313  1.00 35.37  ? 110 GLU C CA  1 
ATOM   5024 C  C   . GLU C 1 110 ? -41.983 59.571  17.992  1.00 37.12  ? 110 GLU C C   1 
ATOM   5025 O  O   . GLU C 1 110 ? -41.284 58.641  17.580  1.00 38.31  ? 110 GLU C O   1 
ATOM   5026 C  CB  . GLU C 1 110 ? -43.361 61.111  16.483  1.00 35.27  ? 110 GLU C CB  1 
ATOM   5027 C  CG  . GLU C 1 110 ? -44.699 61.341  15.775  1.00 34.09  ? 110 GLU C CG  1 
ATOM   5028 C  CD  . GLU C 1 110 ? -44.625 62.294  14.596  1.00 37.04  ? 110 GLU C CD  1 
ATOM   5029 O  OE1 . GLU C 1 110 ? -44.363 63.512  14.777  1.00 38.09  ? 110 GLU C OE1 1 
ATOM   5030 O  OE2 . GLU C 1 110 ? -44.860 61.842  13.462  1.00 41.97  ? 110 GLU C OE2 1 
ATOM   5031 N  N   . HIS C 1 111 ? -41.657 60.333  19.058  1.00 30.96  ? 111 HIS C N   1 
ATOM   5032 C  CA  . HIS C 1 111 ? -40.463 60.038  19.885  1.00 32.20  ? 111 HIS C CA  1 
ATOM   5033 C  C   . HIS C 1 111 ? -40.586 58.846  20.832  1.00 31.38  ? 111 HIS C C   1 
ATOM   5034 O  O   . HIS C 1 111 ? -41.694 58.456  21.209  1.00 29.31  ? 111 HIS C O   1 
ATOM   5035 C  CB  . HIS C 1 111 ? -40.000 61.264  20.666  1.00 31.40  ? 111 HIS C CB  1 
ATOM   5036 C  CG  . HIS C 1 111 ? -39.444 62.354  19.793  1.00 30.52  ? 111 HIS C CG  1 
ATOM   5037 N  ND1 . HIS C 1 111 ? -40.186 63.388  19.388  1.00 30.24  ? 111 HIS C ND1 1 
ATOM   5038 C  CD2 . HIS C 1 111 ? -38.185 62.520  19.231  1.00 31.90  ? 111 HIS C CD2 1 
ATOM   5039 C  CE1 . HIS C 1 111 ? -39.438 64.186  18.592  1.00 34.40  ? 111 HIS C CE1 1 
ATOM   5040 N  NE2 . HIS C 1 111 ? -38.212 63.646  18.500  1.00 32.48  ? 111 HIS C NE2 1 
ATOM   5041 N  N   . SER C 1 112 ? -39.451 58.294  21.261  1.00 28.93  ? 112 SER C N   1 
ATOM   5042 C  CA  . SER C 1 112 ? -39.477 57.268  22.305  1.00 35.05  ? 112 SER C CA  1 
ATOM   5043 C  C   . SER C 1 112 ? -38.440 57.548  23.402  1.00 33.37  ? 112 SER C C   1 
ATOM   5044 O  O   . SER C 1 112 ? -37.430 58.197  23.132  1.00 35.92  ? 112 SER C O   1 
ATOM   5045 C  CB  . SER C 1 112 ? -39.285 55.869  21.694  1.00 31.20  ? 112 SER C CB  1 
ATOM   5046 O  OG  . SER C 1 112 ? -38.000 55.770  21.113  1.00 31.22  ? 112 SER C OG  1 
ATOM   5047 N  N   . LEU C 1 113 ? -38.720 57.097  24.634  1.00 36.49  ? 113 LEU C N   1 
ATOM   5048 C  CA  . LEU C 1 113 ? -37.815 57.250  25.803  1.00 35.38  ? 113 LEU C CA  1 
ATOM   5049 C  C   . LEU C 1 113 ? -37.163 55.939  26.218  1.00 38.71  ? 113 LEU C C   1 
ATOM   5050 O  O   . LEU C 1 113 ? -37.781 55.143  26.908  1.00 41.83  ? 113 LEU C O   1 
ATOM   5051 C  CB  . LEU C 1 113 ? -38.538 57.827  27.032  1.00 36.58  ? 113 LEU C CB  1 
ATOM   5052 C  CG  . LEU C 1 113 ? -38.855 59.333  27.031  1.00 38.72  ? 113 LEU C CG  1 
ATOM   5053 C  CD1 . LEU C 1 113 ? -39.335 59.703  28.417  1.00 38.64  ? 113 LEU C CD1 1 
ATOM   5054 C  CD2 . LEU C 1 113 ? -37.676 60.210  26.604  1.00 37.36  ? 113 LEU C CD2 1 
ATOM   5055 N  N   . ASP C 1 114 ? -35.897 55.753  25.834  1.00 39.49  ? 114 ASP C N   1 
ATOM   5056 C  CA  . ASP C 1 114 ? -35.142 54.539  26.127  1.00 38.38  ? 114 ASP C CA  1 
ATOM   5057 C  C   . ASP C 1 114 ? -35.823 53.326  25.465  1.00 37.09  ? 114 ASP C C   1 
ATOM   5058 O  O   . ASP C 1 114 ? -35.859 52.246  26.049  1.00 35.85  ? 114 ASP C O   1 
ATOM   5059 C  CB  . ASP C 1 114 ? -35.052 54.286  27.635  1.00 41.89  ? 114 ASP C CB  1 
ATOM   5060 C  CG  . ASP C 1 114 ? -34.180 55.288  28.370  1.00 43.72  ? 114 ASP C CG  1 
ATOM   5061 O  OD1 . ASP C 1 114 ? -33.201 55.829  27.813  1.00 40.31  ? 114 ASP C OD1 1 
ATOM   5062 O  OD2 . ASP C 1 114 ? -34.477 55.505  29.558  1.00 48.21  ? 114 ASP C OD2 1 
ATOM   5063 N  N   . GLY C 1 115 ? -36.344 53.521  24.257  1.00 35.62  ? 115 GLY C N   1 
ATOM   5064 C  CA  . GLY C 1 115 ? -37.057 52.477  23.528  1.00 34.73  ? 115 GLY C CA  1 
ATOM   5065 C  C   . GLY C 1 115 ? -38.552 52.425  23.783  1.00 38.46  ? 115 GLY C C   1 
ATOM   5066 O  O   . GLY C 1 115 ? -39.288 51.762  23.038  1.00 36.19  ? 115 GLY C O   1 
ATOM   5067 N  N   . GLU C 1 116 ? -39.030 53.082  24.837  1.00 36.83  ? 116 GLU C N   1 
ATOM   5068 C  CA  . GLU C 1 116 ? -40.463 53.028  25.100  1.00 35.54  ? 116 GLU C CA  1 
ATOM   5069 C  C   . GLU C 1 116 ? -41.221 54.024  24.244  1.00 35.33  ? 116 GLU C C   1 
ATOM   5070 O  O   . GLU C 1 116 ? -40.886 55.216  24.217  1.00 38.92  ? 116 GLU C O   1 
ATOM   5071 C  CB  . GLU C 1 116 ? -40.760 53.237  26.583  1.00 36.28  ? 116 GLU C CB  1 
ATOM   5072 C  CG  . GLU C 1 116 ? -39.945 52.337  27.481  1.00 38.12  ? 116 GLU C CG  1 
ATOM   5073 C  CD  . GLU C 1 116 ? -40.602 52.081  28.822  1.00 41.21  ? 116 GLU C CD  1 
ATOM   5074 O  OE1 . GLU C 1 116 ? -40.234 52.769  29.785  1.00 40.68  ? 116 GLU C OE1 1 
ATOM   5075 O  OE2 . GLU C 1 116 ? -41.487 51.186  28.917  1.00 45.71  ? 116 GLU C OE2 1 
ATOM   5076 N  N   . HIS C 1 117 ? -42.258 53.555  23.557  1.00 34.86  ? 117 HIS C N   1 
ATOM   5077 C  CA  . HIS C 1 117 ? -43.177 54.442  22.848  1.00 34.65  ? 117 HIS C CA  1 
ATOM   5078 C  C   . HIS C 1 117 ? -44.396 54.638  23.672  1.00 36.97  ? 117 HIS C C   1 
ATOM   5079 O  O   . HIS C 1 117 ? -44.792 53.785  24.488  1.00 41.38  ? 117 HIS C O   1 
ATOM   5080 C  CB  . HIS C 1 117 ? -43.576 53.896  21.483  1.00 36.98  ? 117 HIS C CB  1 
ATOM   5081 C  CG  . HIS C 1 117 ? -42.474 53.878  20.479  1.00 35.88  ? 117 HIS C CG  1 
ATOM   5082 N  ND1 . HIS C 1 117 ? -42.550 54.548  19.344  1.00 41.05  ? 117 HIS C ND1 1 
ATOM   5083 C  CD2 . HIS C 1 117 ? -41.250 53.214  20.455  1.00 38.79  ? 117 HIS C CD2 1 
ATOM   5084 C  CE1 . HIS C 1 117 ? -41.434 54.357  18.621  1.00 36.66  ? 117 HIS C CE1 1 
ATOM   5085 N  NE2 . HIS C 1 117 ? -40.637 53.549  19.302  1.00 34.93  ? 117 HIS C NE2 1 
ATOM   5086 N  N   . PHE C 1 118 ? -45.030 55.782  23.491  1.00 37.49  ? 118 PHE C N   1 
ATOM   5087 C  CA  . PHE C 1 118 ? -46.141 56.113  24.349  1.00 36.65  ? 118 PHE C CA  1 
ATOM   5088 C  C   . PHE C 1 118 ? -47.453 56.122  23.596  1.00 35.25  ? 118 PHE C C   1 
ATOM   5089 O  O   . PHE C 1 118 ? -47.447 56.198  22.373  1.00 39.06  ? 118 PHE C O   1 
ATOM   5090 C  CB  . PHE C 1 118 ? -45.875 57.470  25.023  1.00 39.38  ? 118 PHE C CB  1 
ATOM   5091 C  CG  . PHE C 1 118 ? -44.962 57.373  26.202  1.00 38.10  ? 118 PHE C CG  1 
ATOM   5092 C  CD1 . PHE C 1 118 ? -43.597 57.169  26.027  1.00 37.35  ? 118 PHE C CD1 1 
ATOM   5093 C  CD2 . PHE C 1 118 ? -45.466 57.439  27.473  1.00 36.99  ? 118 PHE C CD2 1 
ATOM   5094 C  CE1 . PHE C 1 118 ? -42.751 57.067  27.110  1.00 35.06  ? 118 PHE C CE1 1 
ATOM   5095 C  CE2 . PHE C 1 118 ? -44.628 57.344  28.566  1.00 40.73  ? 118 PHE C CE2 1 
ATOM   5096 C  CZ  . PHE C 1 118 ? -43.266 57.162  28.386  1.00 42.84  ? 118 PHE C CZ  1 
ATOM   5097 N  N   . ALA C 1 119 ? -48.568 56.083  24.323  1.00 36.56  ? 119 ALA C N   1 
ATOM   5098 C  CA  . ALA C 1 119 ? -49.911 56.086  23.698  1.00 40.06  ? 119 ALA C CA  1 
ATOM   5099 C  C   . ALA C 1 119 ? -50.208 57.280  22.772  1.00 40.88  ? 119 ALA C C   1 
ATOM   5100 O  O   . ALA C 1 119 ? -50.858 57.120  21.750  1.00 38.44  ? 119 ALA C O   1 
ATOM   5101 C  CB  . ALA C 1 119 ? -50.993 55.967  24.757  1.00 44.95  ? 119 ALA C CB  1 
ATOM   5102 N  N   . MET C 1 120 ? -49.755 58.480  23.144  1.00 44.84  ? 120 MET C N   1 
ATOM   5103 C  CA  . MET C 1 120 ? -49.865 59.649  22.264  1.00 44.64  ? 120 MET C CA  1 
ATOM   5104 C  C   . MET C 1 120 ? -48.662 60.569  22.412  1.00 45.22  ? 120 MET C C   1 
ATOM   5105 O  O   . MET C 1 120 ? -48.021 60.574  23.456  1.00 46.60  ? 120 MET C O   1 
ATOM   5106 C  CB  . MET C 1 120 ? -51.103 60.468  22.629  1.00 46.97  ? 120 MET C CB  1 
ATOM   5107 C  CG  . MET C 1 120 ? -52.361 59.679  22.930  1.00 46.96  ? 120 MET C CG  1 
ATOM   5108 S  SD  . MET C 1 120 ? -53.776 60.779  23.053  1.00 51.81  ? 120 MET C SD  1 
ATOM   5109 C  CE  . MET C 1 120 ? -53.991 61.213  21.330  1.00 43.41  ? 120 MET C CE  1 
ATOM   5110 N  N   . GLU C 1 121 ? -48.385 61.382  21.395  1.00 46.18  ? 121 GLU C N   1 
ATOM   5111 C  CA  . GLU C 1 121 ? -47.486 62.541  21.573  1.00 46.38  ? 121 GLU C CA  1 
ATOM   5112 C  C   . GLU C 1 121 ? -48.208 63.842  21.207  1.00 43.81  ? 121 GLU C C   1 
ATOM   5113 O  O   . GLU C 1 121 ? -48.770 63.963  20.128  1.00 42.04  ? 121 GLU C O   1 
ATOM   5114 C  CB  . GLU C 1 121 ? -46.217 62.390  20.725  1.00 45.60  ? 121 GLU C CB  1 
ATOM   5115 C  CG  . GLU C 1 121 ? -45.067 63.327  21.075  1.00 44.12  ? 121 GLU C CG  1 
ATOM   5116 C  CD  . GLU C 1 121 ? -43.824 62.987  20.273  1.00 47.68  ? 121 GLU C CD  1 
ATOM   5117 O  OE1 . GLU C 1 121 ? -43.496 61.776  20.148  1.00 42.75  ? 121 GLU C OE1 1 
ATOM   5118 O  OE2 . GLU C 1 121 ? -43.176 63.910  19.746  1.00 44.27  ? 121 GLU C OE2 1 
ATOM   5119 N  N   . MET C 1 122 ? -48.185 64.808  22.120  1.00 47.83  ? 122 MET C N   1 
ATOM   5120 C  CA  . MET C 1 122 ? -48.811 66.122  21.894  1.00 46.32  ? 122 MET C CA  1 
ATOM   5121 C  C   . MET C 1 122 ? -47.729 67.092  21.479  1.00 44.98  ? 122 MET C C   1 
ATOM   5122 O  O   . MET C 1 122 ? -46.739 67.233  22.197  1.00 44.36  ? 122 MET C O   1 
ATOM   5123 C  CB  . MET C 1 122 ? -49.536 66.631  23.152  1.00 43.32  ? 122 MET C CB  1 
ATOM   5124 C  CG  . MET C 1 122 ? -50.107 68.058  23.023  1.00 48.16  ? 122 MET C CG  1 
ATOM   5125 S  SD  . MET C 1 122 ? -51.360 68.464  24.269  1.00 55.01  ? 122 MET C SD  1 
ATOM   5126 C  CE  . MET C 1 122 ? -50.418 68.594  25.775  1.00 47.44  ? 122 MET C CE  1 
ATOM   5127 N  N   . HIS C 1 123 ? -47.927 67.707  20.308  1.00 44.46  ? 123 HIS C N   1 
ATOM   5128 C  CA  . HIS C 1 123 ? -47.051 68.723  19.733  1.00 41.67  ? 123 HIS C CA  1 
ATOM   5129 C  C   . HIS C 1 123 ? -47.669 70.119  19.855  1.00 44.19  ? 123 HIS C C   1 
ATOM   5130 O  O   . HIS C 1 123 ? -48.774 70.359  19.368  1.00 39.39  ? 123 HIS C O   1 
ATOM   5131 C  CB  . HIS C 1 123 ? -46.800 68.415  18.253  1.00 39.38  ? 123 HIS C CB  1 
ATOM   5132 C  CG  . HIS C 1 123 ? -45.850 67.255  18.005  1.00 40.03  ? 123 HIS C CG  1 
ATOM   5133 N  ND1 . HIS C 1 123 ? -45.754 66.653  16.809  1.00 28.72  ? 123 HIS C ND1 1 
ATOM   5134 C  CD2 . HIS C 1 123 ? -44.942 66.591  18.859  1.00 36.12  ? 123 HIS C CD2 1 
ATOM   5135 C  CE1 . HIS C 1 123 ? -44.785 65.706  16.869  1.00 37.49  ? 123 HIS C CE1 1 
ATOM   5136 N  NE2 . HIS C 1 123 ? -44.294 65.670  18.118  1.00 33.54  ? 123 HIS C NE2 1 
ATOM   5137 N  N   . ILE C 1 124 ? -46.974 71.053  20.509  1.00 43.99  ? 124 ILE C N   1 
ATOM   5138 C  CA  . ILE C 1 124 ? -47.440 72.457  20.561  1.00 42.52  ? 124 ILE C CA  1 
ATOM   5139 C  C   . ILE C 1 124 ? -46.425 73.272  19.797  1.00 38.86  ? 124 ILE C C   1 
ATOM   5140 O  O   . ILE C 1 124 ? -45.276 73.329  20.190  1.00 39.28  ? 124 ILE C O   1 
ATOM   5141 C  CB  . ILE C 1 124 ? -47.592 72.971  21.994  1.00 45.81  ? 124 ILE C CB  1 
ATOM   5142 C  CG1 . ILE C 1 124 ? -48.561 72.061  22.754  1.00 44.63  ? 124 ILE C CG1 1 
ATOM   5143 C  CG2 . ILE C 1 124 ? -48.029 74.437  21.975  1.00 46.77  ? 124 ILE C CG2 1 
ATOM   5144 C  CD1 . ILE C 1 124 ? -49.044 72.578  24.091  1.00 48.17  ? 124 ILE C CD1 1 
ATOM   5145 N  N   . VAL C 1 125 ? -46.845 73.842  18.670  1.00 41.26  ? 125 VAL C N   1 
ATOM   5146 C  CA  . VAL C 1 125 ? -45.924 74.295  17.617  1.00 40.55  ? 125 VAL C CA  1 
ATOM   5147 C  C   . VAL C 1 125 ? -45.756 75.820  17.673  1.00 47.87  ? 125 VAL C C   1 
ATOM   5148 O  O   . VAL C 1 125 ? -46.752 76.541  17.856  1.00 45.33  ? 125 VAL C O   1 
ATOM   5149 C  CB  . VAL C 1 125 ? -46.449 73.888  16.227  1.00 37.12  ? 125 VAL C CB  1 
ATOM   5150 C  CG1 . VAL C 1 125 ? -45.457 74.211  15.116  1.00 33.85  ? 125 VAL C CG1 1 
ATOM   5151 C  CG2 . VAL C 1 125 ? -46.778 72.400  16.206  1.00 38.22  ? 125 VAL C CG2 1 
ATOM   5152 N  N   . HIS C 1 126 ? -44.504 76.290  17.531  1.00 49.79  ? 126 HIS C N   1 
ATOM   5153 C  CA  . HIS C 1 126 ? -44.154 77.730  17.607  1.00 52.14  ? 126 HIS C CA  1 
ATOM   5154 C  C   . HIS C 1 126 ? -43.129 78.135  16.589  1.00 56.47  ? 126 HIS C C   1 
ATOM   5155 O  O   . HIS C 1 126 ? -42.200 77.368  16.267  1.00 55.14  ? 126 HIS C O   1 
ATOM   5156 C  CB  . HIS C 1 126 ? -43.600 78.121  18.971  1.00 45.35  ? 126 HIS C CB  1 
ATOM   5157 C  CG  . HIS C 1 126 ? -44.383 77.601  20.147  1.00 45.73  ? 126 HIS C CG  1 
ATOM   5158 N  ND1 . HIS C 1 126 ? -44.166 76.371  20.683  1.00 50.26  ? 126 HIS C ND1 1 
ATOM   5159 C  CD2 . HIS C 1 126 ? -45.372 78.199  20.925  1.00 45.38  ? 126 HIS C CD2 1 
ATOM   5160 C  CE1 . HIS C 1 126 ? -44.989 76.190  21.744  1.00 46.63  ? 126 HIS C CE1 1 
ATOM   5161 N  NE2 . HIS C 1 126 ? -45.723 77.309  21.896  1.00 49.04  ? 126 HIS C NE2 1 
ATOM   5162 N  N   . GLU C 1 127 ? -43.273 79.378  16.113  1.00 65.27  ? 127 GLU C N   1 
ATOM   5163 C  CA  . GLU C 1 127 ? -42.325 80.028  15.189  1.00 61.45  ? 127 GLU C CA  1 
ATOM   5164 C  C   . GLU C 1 127 ? -41.556 81.086  15.989  1.00 58.02  ? 127 GLU C C   1 
ATOM   5165 O  O   . GLU C 1 127 ? -42.126 81.724  16.877  1.00 49.58  ? 127 GLU C O   1 
ATOM   5166 C  CB  . GLU C 1 127 ? -43.102 80.683  14.035  1.00 65.90  ? 127 GLU C CB  1 
ATOM   5167 C  CG  . GLU C 1 127 ? -42.378 80.760  12.693  1.00 70.12  ? 127 GLU C CG  1 
ATOM   5168 C  CD  . GLU C 1 127 ? -43.325 80.908  11.497  1.00 76.71  ? 127 GLU C CD  1 
ATOM   5169 O  OE1 . GLU C 1 127 ? -42.823 81.029  10.353  1.00 73.43  ? 127 GLU C OE1 1 
ATOM   5170 O  OE2 . GLU C 1 127 ? -44.570 80.900  11.689  1.00 77.16  ? 127 GLU C OE2 1 
ATOM   5171 N  N   . LYS C 1 128 ? -40.261 81.235  15.712  1.00 56.45  ? 128 LYS C N   1 
ATOM   5172 C  CA  . LYS C 1 128 ? -39.446 82.227  16.411  1.00 59.83  ? 128 LYS C CA  1 
ATOM   5173 C  C   . LYS C 1 128 ? -39.830 83.648  16.007  1.00 63.70  ? 128 LYS C C   1 
ATOM   5174 O  O   . LYS C 1 128 ? -39.662 84.032  14.841  1.00 66.21  ? 128 LYS C O   1 
ATOM   5175 C  CB  . LYS C 1 128 ? -37.959 82.009  16.127  1.00 58.52  ? 128 LYS C CB  1 
ATOM   5176 C  CG  . LYS C 1 128 ? -37.069 83.121  16.667  1.00 58.66  ? 128 LYS C CG  1 
ATOM   5177 C  CD  . LYS C 1 128 ? -35.688 83.080  16.039  1.00 57.57  ? 128 LYS C CD  1 
ATOM   5178 C  CE  . LYS C 1 128 ? -34.766 82.187  16.828  1.00 53.73  ? 128 LYS C CE  1 
ATOM   5179 N  NZ  . LYS C 1 128 ? -33.347 82.429  16.443  1.00 66.55  ? 128 LYS C NZ  1 
ATOM   5180 N  N   . GLU C 1 129 ? -40.342 84.418  16.965  1.00 66.55  ? 129 GLU C N   1 
ATOM   5181 C  CA  . GLU C 1 129 ? -40.651 85.831  16.722  1.00 75.66  ? 129 GLU C CA  1 
ATOM   5182 C  C   . GLU C 1 129 ? -39.525 86.494  15.925  1.00 77.11  ? 129 GLU C C   1 
ATOM   5183 O  O   . GLU C 1 129 ? -38.345 86.340  16.263  1.00 81.61  ? 129 GLU C O   1 
ATOM   5184 C  CB  . GLU C 1 129 ? -40.922 86.566  18.035  1.00 69.73  ? 129 GLU C CB  1 
ATOM   5185 C  CG  . GLU C 1 129 ? -42.175 86.052  18.734  1.00 70.61  ? 129 GLU C CG  1 
ATOM   5186 C  CD  . GLU C 1 129 ? -42.822 87.073  19.645  1.00 69.13  ? 129 GLU C CD  1 
ATOM   5187 O  OE1 . GLU C 1 129 ? -43.771 86.714  20.383  1.00 74.21  ? 129 GLU C OE1 1 
ATOM   5188 O  OE2 . GLU C 1 129 ? -42.385 88.237  19.627  1.00 69.60  ? 129 GLU C OE2 1 
ATOM   5189 N  N   . LYS C 1 130 ? -39.894 87.189  14.848  1.00 81.74  ? 130 LYS C N   1 
ATOM   5190 C  CA  . LYS C 1 130 ? -38.914 87.744  13.912  1.00 86.77  ? 130 LYS C CA  1 
ATOM   5191 C  C   . LYS C 1 130 ? -38.415 89.119  14.330  1.00 90.31  ? 130 LYS C C   1 
ATOM   5192 O  O   . LYS C 1 130 ? -39.141 89.886  14.964  1.00 92.35  ? 130 LYS C O   1 
ATOM   5193 C  CB  . LYS C 1 130 ? -39.486 87.795  12.492  1.00 86.99  ? 130 LYS C CB  1 
ATOM   5194 C  CG  . LYS C 1 130 ? -39.416 86.462  11.778  1.00 90.12  ? 130 LYS C CG  1 
ATOM   5195 C  CD  . LYS C 1 130 ? -40.387 86.387  10.615  1.00 92.94  ? 130 LYS C CD  1 
ATOM   5196 C  CE  . LYS C 1 130 ? -40.504 84.948  10.130  1.00 97.50  ? 130 LYS C CE  1 
ATOM   5197 N  NZ  . LYS C 1 130 ? -41.152 84.850  8.793   1.00 98.76  ? 130 LYS C NZ  1 
ATOM   5198 N  N   . GLY C 1 131 ? -37.166 89.412  13.971  1.00 94.93  ? 131 GLY C N   1 
ATOM   5199 C  CA  . GLY C 1 131 ? -36.568 90.731  14.186  1.00 96.96  ? 131 GLY C CA  1 
ATOM   5200 C  C   . GLY C 1 131 ? -36.171 90.991  15.623  1.00 94.41  ? 131 GLY C C   1 
ATOM   5201 O  O   . GLY C 1 131 ? -37.001 91.370  16.448  1.00 91.15  ? 131 GLY C O   1 
ATOM   5202 N  N   . PRO C 1 142 ? -30.998 78.535  9.710   1.00 68.69  ? 140 PRO C N   1 
ATOM   5203 C  CA  . PRO C 1 142 ? -32.121 78.785  10.650  1.00 65.40  ? 140 PRO C CA  1 
ATOM   5204 C  C   . PRO C 1 142 ? -32.453 77.566  11.397  1.00 65.77  ? 140 PRO C C   1 
ATOM   5205 O  O   . PRO C 1 142 ? -33.623 77.184  11.534  1.00 63.92  ? 140 PRO C O   1 
ATOM   5206 C  CB  . PRO C 1 142 ? -33.263 79.112  9.598   1.00 64.11  ? 140 PRO C CB  1 
ATOM   5207 C  CG  . PRO C 1 142 ? -32.851 78.461  8.304   1.00 67.10  ? 140 PRO C CG  1 
ATOM   5208 C  CD  . PRO C 1 142 ? -31.452 77.916  8.454   1.00 65.13  ? 140 PRO C CD  1 
ATOM   5209 N  N   . GLU C 1 143 ? -31.415 76.943  11.947  1.00 63.93  ? 141 GLU C N   1 
ATOM   5210 C  CA  . GLU C 1 143 ? -31.516 75.636  12.688  1.00 61.49  ? 141 GLU C CA  1 
ATOM   5211 C  C   . GLU C 1 143 ? -32.558 75.665  13.793  1.00 55.73  ? 141 GLU C C   1 
ATOM   5212 O  O   . GLU C 1 143 ? -33.043 74.602  14.179  1.00 46.61  ? 141 GLU C O   1 
ATOM   5213 C  CB  . GLU C 1 143 ? -30.132 75.110  13.014  1.00 65.57  ? 141 GLU C CB  1 
ATOM   5214 C  CG  . GLU C 1 143 ? -29.322 75.953  13.988  1.00 75.26  ? 141 GLU C CG  1 
ATOM   5215 C  CD  . GLU C 1 143 ? -28.048 75.263  14.464  1.00 77.77  ? 141 GLU C CD  1 
ATOM   5216 O  OE1 . GLU C 1 143 ? -27.478 74.436  13.709  1.00 81.05  ? 141 GLU C OE1 1 
ATOM   5217 O  OE2 . GLU C 1 143 ? -27.616 75.556  15.601  1.00 76.04  ? 141 GLU C OE2 1 
ATOM   5218 N  N   . ASP C 1 144 ? -32.896 76.846  14.318  1.00 55.85  ? 142 ASP C N   1 
ATOM   5219 C  CA  . ASP C 1 144 ? -33.992 76.979  15.240  1.00 50.54  ? 142 ASP C CA  1 
ATOM   5220 C  C   . ASP C 1 144 ? -35.214 77.836  14.938  1.00 48.89  ? 142 ASP C C   1 
ATOM   5221 O  O   . ASP C 1 144 ? -35.935 78.340  15.824  1.00 47.03  ? 142 ASP C O   1 
ATOM   5222 C  CB  . ASP C 1 144 ? -33.369 77.325  16.624  1.00 58.75  ? 142 ASP C CB  1 
ATOM   5223 C  CG  . ASP C 1 144 ? -32.587 78.614  16.583  1.00 63.69  ? 142 ASP C CG  1 
ATOM   5224 O  OD1 . ASP C 1 144 ? -33.213 79.676  16.769  1.00 68.46  ? 142 ASP C OD1 1 
ATOM   5225 O  OD2 . ASP C 1 144 ? -31.352 78.561  16.397  1.00 59.53  ? 142 ASP C OD2 1 
ATOM   5226 N  N   . GLU C 1 145 ? -35.471 77.957  13.645  1.00 50.43  ? 143 GLU C N   1 
ATOM   5227 C  CA  . GLU C 1 145 ? -36.663 78.633  13.156  1.00 57.95  ? 143 GLU C CA  1 
ATOM   5228 C  C   . GLU C 1 145 ? -37.926 78.263  13.957  1.00 57.31  ? 143 GLU C C   1 
ATOM   5229 O  O   . GLU C 1 145 ? -38.634 79.159  14.444  1.00 54.89  ? 143 GLU C O   1 
ATOM   5230 C  CB  . GLU C 1 145 ? -36.846 78.356  11.667  1.00 64.96  ? 143 GLU C CB  1 
ATOM   5231 C  CG  . GLU C 1 145 ? -37.259 79.573  10.844  1.00 74.15  ? 143 GLU C CG  1 
ATOM   5232 C  CD  . GLU C 1 145 ? -38.753 79.833  10.867  1.00 79.31  ? 143 GLU C CD  1 
ATOM   5233 O  OE1 . GLU C 1 145 ? -39.295 80.262  9.822   1.00 86.48  ? 143 GLU C OE1 1 
ATOM   5234 O  OE2 . GLU C 1 145 ? -39.388 79.608  11.918  1.00 75.69  ? 143 GLU C OE2 1 
ATOM   5235 N  N   . ILE C 1 146 ? -38.188 76.957  14.113  1.00 55.53  ? 144 ILE C N   1 
ATOM   5236 C  CA  . ILE C 1 146 ? -39.342 76.477  14.898  1.00 52.06  ? 144 ILE C CA  1 
ATOM   5237 C  C   . ILE C 1 146 ? -38.892 75.802  16.178  1.00 50.19  ? 144 ILE C C   1 
ATOM   5238 O  O   . ILE C 1 146 ? -37.851 75.177  16.207  1.00 55.39  ? 144 ILE C O   1 
ATOM   5239 C  CB  . ILE C 1 146 ? -40.234 75.494  14.088  1.00 51.96  ? 144 ILE C CB  1 
ATOM   5240 C  CG1 . ILE C 1 146 ? -41.081 76.264  13.092  1.00 47.31  ? 144 ILE C CG1 1 
ATOM   5241 C  CG2 . ILE C 1 146 ? -41.142 74.650  14.990  1.00 48.08  ? 144 ILE C CG2 1 
ATOM   5242 C  CD1 . ILE C 1 146 ? -40.351 76.511  11.799  1.00 43.18  ? 144 ILE C CD1 1 
ATOM   5243 N  N   . ALA C 1 147 ? -39.690 75.940  17.229  1.00 47.98  ? 145 ALA C N   1 
ATOM   5244 C  CA  . ALA C 1 147 ? -39.517 75.169  18.449  1.00 45.22  ? 145 ALA C CA  1 
ATOM   5245 C  C   . ALA C 1 147 ? -40.811 74.430  18.791  1.00 44.70  ? 145 ALA C C   1 
ATOM   5246 O  O   . ALA C 1 147 ? -41.858 75.049  18.895  1.00 42.92  ? 145 ALA C O   1 
ATOM   5247 C  CB  . ALA C 1 147 ? -39.136 76.081  19.589  1.00 47.91  ? 145 ALA C CB  1 
ATOM   5248 N  N   . VAL C 1 148 ? -40.739 73.111  18.960  1.00 42.98  ? 146 VAL C N   1 
ATOM   5249 C  CA  . VAL C 1 148 ? -41.940 72.315  19.275  1.00 39.77  ? 146 VAL C CA  1 
ATOM   5250 C  C   . VAL C 1 148 ? -41.887 71.873  20.736  1.00 37.06  ? 146 VAL C C   1 
ATOM   5251 O  O   . VAL C 1 148 ? -40.874 71.380  21.197  1.00 40.33  ? 146 VAL C O   1 
ATOM   5252 C  CB  . VAL C 1 148 ? -42.068 71.064  18.353  1.00 40.44  ? 146 VAL C CB  1 
ATOM   5253 C  CG1 . VAL C 1 148 ? -43.330 70.297  18.664  1.00 40.04  ? 146 VAL C CG1 1 
ATOM   5254 C  CG2 . VAL C 1 148 ? -42.093 71.438  16.884  1.00 39.42  ? 146 VAL C CG2 1 
ATOM   5255 N  N   . LEU C 1 149 ? -42.965 72.037  21.485  1.00 36.85  ? 147 LEU C N   1 
ATOM   5256 C  CA  . LEU C 1 149 ? -43.009 71.374  22.775  1.00 37.46  ? 147 LEU C CA  1 
ATOM   5257 C  C   . LEU C 1 149 ? -43.699 70.003  22.578  1.00 39.13  ? 147 LEU C C   1 
ATOM   5258 O  O   . LEU C 1 149 ? -44.864 69.935  22.187  1.00 36.85  ? 147 LEU C O   1 
ATOM   5259 C  CB  . LEU C 1 149 ? -43.693 72.233  23.821  1.00 38.38  ? 147 LEU C CB  1 
ATOM   5260 C  CG  . LEU C 1 149 ? -43.304 73.735  23.862  1.00 39.40  ? 147 LEU C CG  1 
ATOM   5261 C  CD1 . LEU C 1 149 ? -43.671 74.337  25.216  1.00 33.41  ? 147 LEU C CD1 1 
ATOM   5262 C  CD2 . LEU C 1 149 ? -41.841 74.041  23.492  1.00 37.24  ? 147 LEU C CD2 1 
ATOM   5263 N  N   . ALA C 1 150 ? -42.949 68.926  22.793  1.00 35.38  ? 148 ALA C N   1 
ATOM   5264 C  CA  . ALA C 1 150 ? -43.505 67.576  22.657  1.00 35.51  ? 148 ALA C CA  1 
ATOM   5265 C  C   . ALA C 1 150 ? -43.779 66.995  24.007  1.00 32.13  ? 148 ALA C C   1 
ATOM   5266 O  O   . ALA C 1 150 ? -42.862 66.854  24.802  1.00 31.34  ? 148 ALA C O   1 
ATOM   5267 C  CB  . ALA C 1 150 ? -42.558 66.671  21.866  1.00 30.51  ? 148 ALA C CB  1 
ATOM   5268 N  N   . PHE C 1 151 ? -45.042 66.649  24.259  1.00 34.83  ? 149 PHE C N   1 
ATOM   5269 C  CA  . PHE C 1 151 ? -45.434 65.944  25.494  1.00 36.97  ? 149 PHE C CA  1 
ATOM   5270 C  C   . PHE C 1 151 ? -45.947 64.516  25.223  1.00 39.17  ? 149 PHE C C   1 
ATOM   5271 O  O   . PHE C 1 151 ? -46.821 64.306  24.383  1.00 36.56  ? 149 PHE C O   1 
ATOM   5272 C  CB  . PHE C 1 151 ? -46.540 66.699  26.221  1.00 42.62  ? 149 PHE C CB  1 
ATOM   5273 C  CG  . PHE C 1 151 ? -46.230 68.158  26.498  1.00 45.51  ? 149 PHE C CG  1 
ATOM   5274 C  CD1 . PHE C 1 151 ? -46.140 69.088  25.462  1.00 46.00  ? 149 PHE C CD1 1 
ATOM   5275 C  CD2 . PHE C 1 151 ? -46.081 68.611  27.811  1.00 45.72  ? 149 PHE C CD2 1 
ATOM   5276 C  CE1 . PHE C 1 151 ? -45.871 70.429  25.727  1.00 52.52  ? 149 PHE C CE1 1 
ATOM   5277 C  CE2 . PHE C 1 151 ? -45.805 69.952  28.072  1.00 45.50  ? 149 PHE C CE2 1 
ATOM   5278 C  CZ  . PHE C 1 151 ? -45.710 70.859  27.034  1.00 45.49  ? 149 PHE C CZ  1 
ATOM   5279 N  N   . LEU C 1 152 ? -45.429 63.552  25.978  1.00 41.15  ? 150 LEU C N   1 
ATOM   5280 C  CA  . LEU C 1 152 ? -45.803 62.142  25.840  1.00 40.11  ? 150 LEU C CA  1 
ATOM   5281 C  C   . LEU C 1 152 ? -47.028 61.848  26.674  1.00 41.50  ? 150 LEU C C   1 
ATOM   5282 O  O   . LEU C 1 152 ? -47.108 62.291  27.827  1.00 42.42  ? 150 LEU C O   1 
ATOM   5283 C  CB  . LEU C 1 152 ? -44.661 61.241  26.321  1.00 36.27  ? 150 LEU C CB  1 
ATOM   5284 C  CG  . LEU C 1 152 ? -43.297 61.595  25.737  1.00 34.69  ? 150 LEU C CG  1 
ATOM   5285 C  CD1 . LEU C 1 152 ? -42.178 61.087  26.626  1.00 31.00  ? 150 LEU C CD1 1 
ATOM   5286 C  CD2 . LEU C 1 152 ? -43.203 61.071  24.309  1.00 36.99  ? 150 LEU C CD2 1 
ATOM   5287 N  N   . VAL C 1 153 ? -47.949 61.074  26.099  1.00 37.99  ? 151 VAL C N   1 
ATOM   5288 C  CA  . VAL C 1 153 ? -49.234 60.759  26.727  1.00 42.41  ? 151 VAL C CA  1 
ATOM   5289 C  C   . VAL C 1 153 ? -49.399 59.247  26.891  1.00 44.00  ? 151 VAL C C   1 
ATOM   5290 O  O   . VAL C 1 153 ? -49.311 58.505  25.910  1.00 44.44  ? 151 VAL C O   1 
ATOM   5291 C  CB  . VAL C 1 153 ? -50.419 61.290  25.882  1.00 43.97  ? 151 VAL C CB  1 
ATOM   5292 C  CG1 . VAL C 1 153 ? -51.754 61.020  26.574  1.00 42.74  ? 151 VAL C CG1 1 
ATOM   5293 C  CG2 . VAL C 1 153 ? -50.241 62.776  25.568  1.00 46.97  ? 151 VAL C CG2 1 
ATOM   5294 N  N   . GLU C 1 154 ? -49.623 58.806  28.124  1.00 44.20  ? 152 GLU C N   1 
ATOM   5295 C  CA  . GLU C 1 154 ? -49.925 57.406  28.410  1.00 53.47  ? 152 GLU C CA  1 
ATOM   5296 C  C   . GLU C 1 154 ? -51.287 57.340  29.068  1.00 55.33  ? 152 GLU C C   1 
ATOM   5297 O  O   . GLU C 1 154 ? -51.836 58.380  29.439  1.00 55.90  ? 152 GLU C O   1 
ATOM   5298 C  CB  . GLU C 1 154 ? -48.859 56.778  29.323  1.00 53.39  ? 152 GLU C CB  1 
ATOM   5299 C  CG  . GLU C 1 154 ? -48.925 57.173  30.799  1.00 53.62  ? 152 GLU C CG  1 
ATOM   5300 C  CD  . GLU C 1 154 ? -47.585 56.999  31.516  1.00 59.19  ? 152 GLU C CD  1 
ATOM   5301 O  OE1 . GLU C 1 154 ? -46.626 56.493  30.883  1.00 58.64  ? 152 GLU C OE1 1 
ATOM   5302 O  OE2 . GLU C 1 154 ? -47.474 57.382  32.710  1.00 59.18  ? 152 GLU C OE2 1 
ATOM   5303 N  N   . ALA C 1 155 ? -51.820 56.125  29.226  1.00 55.70  ? 153 ALA C N   1 
ATOM   5304 C  CA  . ALA C 1 155 ? -53.125 55.925  29.865  1.00 55.87  ? 153 ALA C CA  1 
ATOM   5305 C  C   . ALA C 1 155 ? -53.001 55.760  31.373  1.00 60.07  ? 153 ALA C C   1 
ATOM   5306 O  O   . ALA C 1 155 ? -52.267 54.902  31.852  1.00 64.25  ? 153 ALA C O   1 
ATOM   5307 C  CB  . ALA C 1 155 ? -53.870 54.738  29.248  1.00 53.85  ? 153 ALA C CB  1 
ATOM   5308 N  N   . GLY C 1 156 ? -53.718 56.596  32.114  1.00 62.66  ? 154 GLY C N   1 
ATOM   5309 C  CA  . GLY C 1 156 ? -53.827 56.445  33.556  1.00 70.17  ? 154 GLY C CA  1 
ATOM   5310 C  C   . GLY C 1 156 ? -55.224 55.956  33.896  1.00 74.67  ? 154 GLY C C   1 
ATOM   5311 O  O   . GLY C 1 156 ? -56.145 56.051  33.062  1.00 66.57  ? 154 GLY C O   1 
ATOM   5312 N  N   . THR C 1 157 ? -55.379 55.405  35.100  1.00 76.41  ? 155 THR C N   1 
ATOM   5313 C  CA  . THR C 1 157 ? -56.715 55.101  35.626  1.00 81.84  ? 155 THR C CA  1 
ATOM   5314 C  C   . THR C 1 157 ? -57.259 56.417  36.194  1.00 81.48  ? 155 THR C C   1 
ATOM   5315 O  O   . THR C 1 157 ? -57.108 56.688  37.388  1.00 73.83  ? 155 THR C O   1 
ATOM   5316 C  CB  . THR C 1 157 ? -56.726 53.939  36.673  1.00 84.97  ? 155 THR C CB  1 
ATOM   5317 O  OG1 . THR C 1 157 ? -55.923 54.271  37.817  1.00 76.01  ? 155 THR C OG1 1 
ATOM   5318 C  CG2 . THR C 1 157 ? -56.222 52.620  36.060  1.00 82.05  ? 155 THR C CG2 1 
ATOM   5319 N  N   . GLN C 1 158 ? -57.865 57.227  35.312  1.00 81.97  ? 156 GLN C N   1 
ATOM   5320 C  CA  . GLN C 1 158 ? -58.189 58.642  35.568  1.00 83.79  ? 156 GLN C CA  1 
ATOM   5321 C  C   . GLN C 1 158 ? -58.923 59.261  34.370  1.00 80.52  ? 156 GLN C C   1 
ATOM   5322 O  O   . GLN C 1 158 ? -58.570 58.989  33.229  1.00 81.21  ? 156 GLN C O   1 
ATOM   5323 C  CB  . GLN C 1 158 ? -56.905 59.401  35.934  1.00 88.10  ? 156 GLN C CB  1 
ATOM   5324 C  CG  . GLN C 1 158 ? -56.850 59.904  37.364  1.00 90.41  ? 156 GLN C CG  1 
ATOM   5325 C  CD  . GLN C 1 158 ? -57.744 61.107  37.584  1.00 90.90  ? 156 GLN C CD  1 
ATOM   5326 O  OE1 . GLN C 1 158 ? -58.564 61.119  38.500  1.00 92.26  ? 156 GLN C OE1 1 
ATOM   5327 N  NE2 . GLN C 1 158 ? -57.596 62.125  36.737  1.00 89.44  ? 156 GLN C NE2 1 
ATOM   5328 N  N   . VAL C 1 159 ? -59.920 60.108  34.608  1.00 80.78  ? 157 VAL C N   1 
ATOM   5329 C  CA  . VAL C 1 159 ? -60.424 60.954  33.513  1.00 81.02  ? 157 VAL C CA  1 
ATOM   5330 C  C   . VAL C 1 159 ? -59.851 62.336  33.821  1.00 80.48  ? 157 VAL C C   1 
ATOM   5331 O  O   . VAL C 1 159 ? -60.217 62.965  34.821  1.00 81.05  ? 157 VAL C O   1 
ATOM   5332 C  CB  . VAL C 1 159 ? -61.961 61.003  33.318  1.00 74.60  ? 157 VAL C CB  1 
ATOM   5333 C  CG1 . VAL C 1 159 ? -62.373 62.306  32.646  1.00 69.20  ? 157 VAL C CG1 1 
ATOM   5334 C  CG2 . VAL C 1 159 ? -62.427 59.825  32.472  1.00 70.96  ? 157 VAL C CG2 1 
ATOM   5335 N  N   . ASN C 1 160 ? -58.941 62.780  32.955  1.00 80.68  ? 158 ASN C N   1 
ATOM   5336 C  CA  . ASN C 1 160 ? -58.247 64.062  33.099  1.00 88.11  ? 158 ASN C CA  1 
ATOM   5337 C  C   . ASN C 1 160 ? -59.209 65.250  32.957  1.00 91.04  ? 158 ASN C C   1 
ATOM   5338 O  O   . ASN C 1 160 ? -59.742 65.503  31.868  1.00 87.48  ? 158 ASN C O   1 
ATOM   5339 C  CB  . ASN C 1 160 ? -57.095 64.148  32.086  1.00 85.95  ? 158 ASN C CB  1 
ATOM   5340 C  CG  . ASN C 1 160 ? -56.035 65.165  32.472  1.00 82.56  ? 158 ASN C CG  1 
ATOM   5341 O  OD1 . ASN C 1 160 ? -56.106 66.330  32.079  1.00 84.11  ? 158 ASN C OD1 1 
ATOM   5342 N  ND2 . ASN C 1 160 ? -55.027 64.718  33.214  1.00 80.41  ? 158 ASN C ND2 1 
ATOM   5343 N  N   . GLU C 1 161 ? -59.431 65.952  34.075  1.00 93.55  ? 159 GLU C N   1 
ATOM   5344 C  CA  . GLU C 1 161 ? -60.371 67.079  34.157  1.00 93.12  ? 159 GLU C CA  1 
ATOM   5345 C  C   . GLU C 1 161 ? -60.208 68.040  32.977  1.00 88.90  ? 159 GLU C C   1 
ATOM   5346 O  O   . GLU C 1 161 ? -61.081 68.117  32.107  1.00 86.96  ? 159 GLU C O   1 
ATOM   5347 C  CB  . GLU C 1 161 ? -60.191 67.830  35.486  1.00 98.54  ? 159 GLU C CB  1 
ATOM   5348 C  CG  . GLU C 1 161 ? -61.407 68.631  35.939  1.00 102.65 ? 159 GLU C CG  1 
ATOM   5349 C  CD  . GLU C 1 161 ? -62.306 67.854  36.890  1.00 106.28 ? 159 GLU C CD  1 
ATOM   5350 O  OE1 . GLU C 1 161 ? -63.400 67.430  36.467  1.00 105.45 ? 159 GLU C OE1 1 
ATOM   5351 O  OE2 . GLU C 1 161 ? -61.919 67.656  38.063  1.00 109.80 ? 159 GLU C OE2 1 
ATOM   5352 N  N   . GLY C 1 162 ? -59.069 68.733  32.946  1.00 80.62  ? 160 GLY C N   1 
ATOM   5353 C  CA  . GLY C 1 162 ? -58.767 69.735  31.934  1.00 72.12  ? 160 GLY C CA  1 
ATOM   5354 C  C   . GLY C 1 162 ? -58.818 69.280  30.489  1.00 68.60  ? 160 GLY C C   1 
ATOM   5355 O  O   . GLY C 1 162 ? -58.924 70.105  29.584  1.00 69.56  ? 160 GLY C O   1 
ATOM   5356 N  N   . PHE C 1 163 ? -58.761 67.973  30.253  1.00 72.83  ? 161 PHE C N   1 
ATOM   5357 C  CA  . PHE C 1 163 ? -58.687 67.478  28.873  1.00 69.15  ? 161 PHE C CA  1 
ATOM   5358 C  C   . PHE C 1 163 ? -60.037 67.274  28.191  1.00 70.34  ? 161 PHE C C   1 
ATOM   5359 O  O   . PHE C 1 163 ? -60.095 66.862  27.031  1.00 73.92  ? 161 PHE C O   1 
ATOM   5360 C  CB  . PHE C 1 163 ? -57.859 66.202  28.807  1.00 69.83  ? 161 PHE C CB  1 
ATOM   5361 C  CG  . PHE C 1 163 ? -56.745 66.267  27.804  1.00 67.41  ? 161 PHE C CG  1 
ATOM   5362 C  CD1 . PHE C 1 163 ? -55.471 66.677  28.196  1.00 67.66  ? 161 PHE C CD1 1 
ATOM   5363 C  CD2 . PHE C 1 163 ? -56.964 65.941  26.473  1.00 61.66  ? 161 PHE C CD2 1 
ATOM   5364 C  CE1 . PHE C 1 163 ? -54.430 66.741  27.279  1.00 66.84  ? 161 PHE C CE1 1 
ATOM   5365 C  CE2 . PHE C 1 163 ? -55.924 66.003  25.552  1.00 64.28  ? 161 PHE C CE2 1 
ATOM   5366 C  CZ  . PHE C 1 163 ? -54.656 66.405  25.956  1.00 61.31  ? 161 PHE C CZ  1 
ATOM   5367 N  N   . GLN C 1 164 ? -61.116 67.578  28.904  1.00 72.03  ? 162 GLN C N   1 
ATOM   5368 C  CA  . GLN C 1 164 ? -62.464 67.283  28.425  1.00 72.71  ? 162 GLN C CA  1 
ATOM   5369 C  C   . GLN C 1 164 ? -62.879 67.878  27.059  1.00 75.79  ? 162 GLN C C   1 
ATOM   5370 O  O   . GLN C 1 164 ? -63.234 67.115  26.157  1.00 80.31  ? 162 GLN C O   1 
ATOM   5371 C  CB  . GLN C 1 164 ? -63.495 67.586  29.518  1.00 74.91  ? 162 GLN C CB  1 
ATOM   5372 C  CG  . GLN C 1 164 ? -63.598 66.503  30.581  1.00 72.00  ? 162 GLN C CG  1 
ATOM   5373 C  CD  . GLN C 1 164 ? -64.215 65.210  30.048  1.00 74.38  ? 162 GLN C CD  1 
ATOM   5374 O  OE1 . GLN C 1 164 ? -63.768 64.656  29.038  1.00 68.26  ? 162 GLN C OE1 1 
ATOM   5375 N  NE2 . GLN C 1 164 ? -65.241 64.719  30.737  1.00 77.71  ? 162 GLN C NE2 1 
ATOM   5376 N  N   . PRO C 1 165 ? -62.824 69.220  26.893  1.00 70.35  ? 163 PRO C N   1 
ATOM   5377 C  CA  . PRO C 1 165 ? -63.413 69.848  25.685  1.00 71.51  ? 163 PRO C CA  1 
ATOM   5378 C  C   . PRO C 1 165 ? -62.769 69.480  24.320  1.00 73.44  ? 163 PRO C C   1 
ATOM   5379 O  O   . PRO C 1 165 ? -63.468 69.432  23.293  1.00 71.96  ? 163 PRO C O   1 
ATOM   5380 C  CB  . PRO C 1 165 ? -63.275 71.360  25.966  1.00 67.93  ? 163 PRO C CB  1 
ATOM   5381 C  CG  . PRO C 1 165 ? -63.049 71.466  27.436  1.00 68.28  ? 163 PRO C CG  1 
ATOM   5382 C  CD  . PRO C 1 165 ? -62.286 70.235  27.820  1.00 67.63  ? 163 PRO C CD  1 
ATOM   5383 N  N   . LEU C 1 166 ? -61.457 69.237  24.306  1.00 67.08  ? 164 LEU C N   1 
ATOM   5384 C  CA  . LEU C 1 166 ? -60.758 68.826  23.083  1.00 63.36  ? 164 LEU C CA  1 
ATOM   5385 C  C   . LEU C 1 166 ? -61.311 67.487  22.596  1.00 68.83  ? 164 LEU C C   1 
ATOM   5386 O  O   . LEU C 1 166 ? -61.484 67.272  21.387  1.00 68.70  ? 164 LEU C O   1 
ATOM   5387 C  CB  . LEU C 1 166 ? -59.246 68.751  23.342  1.00 62.54  ? 164 LEU C CB  1 
ATOM   5388 C  CG  . LEU C 1 166 ? -58.198 68.102  22.418  1.00 57.99  ? 164 LEU C CG  1 
ATOM   5389 C  CD1 . LEU C 1 166 ? -58.235 68.564  20.967  1.00 60.62  ? 164 LEU C CD1 1 
ATOM   5390 C  CD2 . LEU C 1 166 ? -56.815 68.362  22.992  1.00 58.64  ? 164 LEU C CD2 1 
ATOM   5391 N  N   . VAL C 1 167 ? -61.603 66.606  23.552  1.00 65.44  ? 165 VAL C N   1 
ATOM   5392 C  CA  . VAL C 1 167 ? -62.223 65.320  23.270  1.00 72.95  ? 165 VAL C CA  1 
ATOM   5393 C  C   . VAL C 1 167 ? -63.614 65.528  22.669  1.00 78.13  ? 165 VAL C C   1 
ATOM   5394 O  O   . VAL C 1 167 ? -63.934 64.969  21.614  1.00 77.13  ? 165 VAL C O   1 
ATOM   5395 C  CB  . VAL C 1 167 ? -62.317 64.431  24.536  1.00 73.20  ? 165 VAL C CB  1 
ATOM   5396 C  CG1 . VAL C 1 167 ? -62.835 63.049  24.174  1.00 70.30  ? 165 VAL C CG1 1 
ATOM   5397 C  CG2 . VAL C 1 167 ? -60.965 64.321  25.231  1.00 70.04  ? 165 VAL C CG2 1 
ATOM   5398 N  N   . GLU C 1 168 ? -64.426 66.345  23.338  1.00 82.21  ? 166 GLU C N   1 
ATOM   5399 C  CA  . GLU C 1 168 ? -65.787 66.629  22.884  1.00 80.39  ? 166 GLU C CA  1 
ATOM   5400 C  C   . GLU C 1 168 ? -65.807 67.327  21.533  1.00 81.26  ? 166 GLU C C   1 
ATOM   5401 O  O   . GLU C 1 168 ? -66.760 67.174  20.774  1.00 84.58  ? 166 GLU C O   1 
ATOM   5402 C  CB  . GLU C 1 168 ? -66.549 67.443  23.936  1.00 79.74  ? 166 GLU C CB  1 
ATOM   5403 C  CG  . GLU C 1 168 ? -67.169 66.581  25.030  1.00 79.52  ? 166 GLU C CG  1 
ATOM   5404 C  CD  . GLU C 1 168 ? -67.452 67.334  26.327  1.00 81.29  ? 166 GLU C CD  1 
ATOM   5405 O  OE1 . GLU C 1 168 ? -67.640 66.652  27.363  1.00 76.65  ? 166 GLU C OE1 1 
ATOM   5406 O  OE2 . GLU C 1 168 ? -67.485 68.590  26.318  1.00 76.24  ? 166 GLU C OE2 1 
ATOM   5407 N  N   . ALA C 1 169 ? -64.739 68.063  21.232  1.00 79.16  ? 167 ALA C N   1 
ATOM   5408 C  CA  . ALA C 1 169 ? -64.613 68.805  19.978  1.00 80.46  ? 167 ALA C CA  1 
ATOM   5409 C  C   . ALA C 1 169 ? -64.385 67.921  18.729  1.00 87.75  ? 167 ALA C C   1 
ATOM   5410 O  O   . ALA C 1 169 ? -64.286 68.421  17.601  1.00 91.45  ? 167 ALA C O   1 
ATOM   5411 C  CB  . ALA C 1 169 ? -63.513 69.849  20.107  1.00 73.85  ? 167 ALA C CB  1 
ATOM   5412 N  N   . LEU C 1 170 ? -64.317 66.611  18.927  1.00 85.65  ? 168 LEU C N   1 
ATOM   5413 C  CA  . LEU C 1 170 ? -64.013 65.690  17.830  1.00 84.32  ? 168 LEU C CA  1 
ATOM   5414 C  C   . LEU C 1 170 ? -65.265 65.032  17.243  1.00 83.40  ? 168 LEU C C   1 
ATOM   5415 O  O   . LEU C 1 170 ? -65.280 64.629  16.072  1.00 73.03  ? 168 LEU C O   1 
ATOM   5416 C  CB  . LEU C 1 170 ? -63.033 64.626  18.315  1.00 84.78  ? 168 LEU C CB  1 
ATOM   5417 C  CG  . LEU C 1 170 ? -61.699 65.155  18.845  1.00 81.41  ? 168 LEU C CG  1 
ATOM   5418 C  CD1 . LEU C 1 170 ? -61.138 64.273  19.950  1.00 77.52  ? 168 LEU C CD1 1 
ATOM   5419 C  CD2 . LEU C 1 170 ? -60.723 65.270  17.691  1.00 76.84  ? 168 LEU C CD2 1 
ATOM   5420 N  N   . SER C 1 171 ? -66.306 64.932  18.072  1.00 84.37  ? 169 SER C N   1 
ATOM   5421 C  CA  . SER C 1 171 ? -67.597 64.374  17.674  1.00 81.96  ? 169 SER C CA  1 
ATOM   5422 C  C   . SER C 1 171 ? -68.096 64.991  16.378  1.00 79.65  ? 169 SER C C   1 
ATOM   5423 O  O   . SER C 1 171 ? -68.775 64.323  15.602  1.00 79.59  ? 169 SER C O   1 
ATOM   5424 C  CB  . SER C 1 171 ? -68.633 64.600  18.777  1.00 82.34  ? 169 SER C CB  1 
ATOM   5425 O  OG  . SER C 1 171 ? -68.231 63.990  19.992  1.00 83.44  ? 169 SER C OG  1 
ATOM   5426 N  N   . ASN C 1 172 ? -67.725 66.255  16.146  1.00 83.13  ? 170 ASN C N   1 
ATOM   5427 C  CA  . ASN C 1 172 ? -68.244 67.047  15.027  1.00 80.11  ? 170 ASN C CA  1 
ATOM   5428 C  C   . ASN C 1 172 ? -67.246 67.404  13.904  1.00 84.78  ? 170 ASN C C   1 
ATOM   5429 O  O   . ASN C 1 172 ? -67.486 68.360  13.155  1.00 80.81  ? 170 ASN C O   1 
ATOM   5430 C  CB  . ASN C 1 172 ? -68.935 68.315  15.557  1.00 79.53  ? 170 ASN C CB  1 
ATOM   5431 C  CG  . ASN C 1 172 ? -69.940 68.018  16.664  1.00 80.91  ? 170 ASN C CG  1 
ATOM   5432 O  OD1 . ASN C 1 172 ? -71.062 67.562  16.404  1.00 69.60  ? 170 ASN C OD1 1 
ATOM   5433 N  ND2 . ASN C 1 172 ? -69.541 68.282  17.913  1.00 74.38  ? 170 ASN C ND2 1 
ATOM   5434 N  N   . ILE C 1 173 ? -66.146 66.650  13.776  1.00 86.54  ? 171 ILE C N   1 
ATOM   5435 C  CA  . ILE C 1 173 ? -65.180 66.849  12.659  1.00 87.00  ? 171 ILE C CA  1 
ATOM   5436 C  C   . ILE C 1 173 ? -64.593 65.586  11.971  1.00 93.66  ? 171 ILE C C   1 
ATOM   5437 O  O   . ILE C 1 173 ? -63.412 65.595  11.607  1.00 98.90  ? 171 ILE C O   1 
ATOM   5438 C  CB  . ILE C 1 173 ? -63.979 67.745  13.066  1.00 79.85  ? 171 ILE C CB  1 
ATOM   5439 C  CG1 . ILE C 1 173 ? -63.381 67.303  14.406  1.00 78.48  ? 171 ILE C CG1 1 
ATOM   5440 C  CG2 . ILE C 1 173 ? -64.372 69.211  13.090  1.00 78.94  ? 171 ILE C CG2 1 
ATOM   5441 C  CD1 . ILE C 1 173 ? -61.909 67.626  14.538  1.00 76.40  ? 171 ILE C CD1 1 
ATOM   5442 N  N   . PRO C 1 174 ? -65.400 64.517  11.763  1.00 89.10  ? 172 PRO C N   1 
ATOM   5443 C  CA  . PRO C 1 174 ? -64.823 63.246  11.288  1.00 88.92  ? 172 PRO C CA  1 
ATOM   5444 C  C   . PRO C 1 174 ? -63.997 63.309  9.990   1.00 94.51  ? 172 PRO C C   1 
ATOM   5445 O  O   . PRO C 1 174 ? -62.915 62.723  9.933   1.00 103.57 ? 172 PRO C O   1 
ATOM   5446 C  CB  . PRO C 1 174 ? -66.054 62.348  11.095  1.00 88.35  ? 172 PRO C CB  1 
ATOM   5447 C  CG  . PRO C 1 174 ? -67.076 62.910  12.015  1.00 86.94  ? 172 PRO C CG  1 
ATOM   5448 C  CD  . PRO C 1 174 ? -66.856 64.396  11.972  1.00 88.03  ? 172 PRO C CD  1 
ATOM   5449 N  N   . LYS C 1 175 ? -64.492 64.005  8.969   1.00 92.06  ? 173 LYS C N   1 
ATOM   5450 C  CA  . LYS C 1 175 ? -63.825 64.033  7.660   1.00 89.77  ? 173 LYS C CA  1 
ATOM   5451 C  C   . LYS C 1 175 ? -62.753 65.123  7.591   1.00 87.32  ? 173 LYS C C   1 
ATOM   5452 O  O   . LYS C 1 175 ? -62.770 66.066  8.390   1.00 86.97  ? 173 LYS C O   1 
ATOM   5453 C  CB  . LYS C 1 175 ? -64.850 64.232  6.529   1.00 100.05 ? 173 LYS C CB  1 
ATOM   5454 C  CG  . LYS C 1 175 ? -65.912 63.141  6.399   1.00 103.91 ? 173 LYS C CG  1 
ATOM   5455 C  CD  . LYS C 1 175 ? -67.120 63.632  5.608   1.00 103.97 ? 173 LYS C CD  1 
ATOM   5456 C  CE  . LYS C 1 175 ? -68.051 62.506  5.171   1.00 108.09 ? 173 LYS C CE  1 
ATOM   5457 N  NZ  . LYS C 1 175 ? -68.601 61.672  6.279   1.00 106.57 ? 173 LYS C NZ  1 
ATOM   5458 N  N   . PRO C 1 176 ? -61.806 64.994  6.641   1.00 84.51  ? 174 PRO C N   1 
ATOM   5459 C  CA  . PRO C 1 176 ? -60.819 66.071  6.365   1.00 84.56  ? 174 PRO C CA  1 
ATOM   5460 C  C   . PRO C 1 176 ? -61.626 67.354  6.039   1.00 77.83  ? 174 PRO C C   1 
ATOM   5461 O  O   . PRO C 1 176 ? -62.646 67.290  5.358   1.00 81.52  ? 174 PRO C O   1 
ATOM   5462 C  CB  . PRO C 1 176 ? -59.925 65.484  5.293   1.00 81.63  ? 174 PRO C CB  1 
ATOM   5463 C  CG  . PRO C 1 176 ? -60.605 64.263  4.790   1.00 83.71  ? 174 PRO C CG  1 
ATOM   5464 C  CD  . PRO C 1 176 ? -61.426 63.758  5.938   1.00 86.46  ? 174 PRO C CD  1 
ATOM   5465 N  N   . GLU C 1 177 ? -61.122 68.487  6.536   1.00 77.55  ? 175 GLU C N   1 
ATOM   5466 C  CA  . GLU C 1 177 ? -61.510 69.862  6.169   1.00 72.84  ? 175 GLU C CA  1 
ATOM   5467 C  C   . GLU C 1 177 ? -62.729 70.488  6.928   1.00 76.01  ? 175 GLU C C   1 
ATOM   5468 O  O   . GLU C 1 177 ? -63.235 71.538  6.538   1.00 80.62  ? 175 GLU C O   1 
ATOM   5469 C  CB  . GLU C 1 177 ? -61.991 69.990  4.714   1.00 72.68  ? 175 GLU C CB  1 
ATOM   5470 C  CG  . GLU C 1 177 ? -60.909 69.689  3.671   1.00 70.70  ? 175 GLU C CG  1 
ATOM   5471 C  CD  . GLU C 1 177 ? -59.735 70.647  3.730   1.00 72.40  ? 175 GLU C CD  1 
ATOM   5472 O  OE1 . GLU C 1 177 ? -59.918 71.833  3.385   1.00 70.31  ? 175 GLU C OE1 1 
ATOM   5473 O  OE2 . GLU C 1 177 ? -58.622 70.218  4.114   1.00 72.74  ? 175 GLU C OE2 1 
ATOM   5474 N  N   . MET C 1 178 ? -63.149 69.843  8.014   1.00 76.65  ? 176 MET C N   1 
ATOM   5475 C  CA  . MET C 1 178 ? -64.279 70.297  8.832   1.00 69.82  ? 176 MET C CA  1 
ATOM   5476 C  C   . MET C 1 178 ? -63.606 70.826  10.092  1.00 68.76  ? 176 MET C C   1 
ATOM   5477 O  O   . MET C 1 178 ? -62.587 70.274  10.509  1.00 67.62  ? 176 MET C O   1 
ATOM   5478 C  CB  . MET C 1 178 ? -65.251 69.173  9.214   1.00 69.26  ? 176 MET C CB  1 
ATOM   5479 C  CG  . MET C 1 178 ? -65.818 68.379  8.037   1.00 71.12  ? 176 MET C CG  1 
ATOM   5480 S  SD  . MET C 1 178 ? -66.362 66.694  8.439   1.00 77.97  ? 176 MET C SD  1 
ATOM   5481 C  CE  . MET C 1 178 ? -67.528 67.001  9.766   1.00 73.90  ? 176 MET C CE  1 
ATOM   5482 N  N   . SER C 1 179 ? -64.175 71.874  10.705  1.00 66.02  ? 177 SER C N   1 
ATOM   5483 C  CA  . SER C 1 179 ? -63.621 72.447  11.951  1.00 68.62  ? 177 SER C CA  1 
ATOM   5484 C  C   . SER C 1 179 ? -64.635 73.038  12.957  1.00 66.94  ? 177 SER C C   1 
ATOM   5485 O  O   . SER C 1 179 ? -65.106 74.161  12.793  1.00 69.60  ? 177 SER C O   1 
ATOM   5486 C  CB  . SER C 1 179 ? -62.516 73.465  11.650  1.00 69.58  ? 177 SER C CB  1 
ATOM   5487 O  OG  . SER C 1 179 ? -62.923 74.395  10.668  1.00 70.72  ? 177 SER C OG  1 
ATOM   5488 N  N   . THR C 1 180 ? -64.923 72.277  14.010  1.00 60.31  ? 178 THR C N   1 
ATOM   5489 C  CA  . THR C 1 180 ? -65.805 72.684  15.096  1.00 59.96  ? 178 THR C CA  1 
ATOM   5490 C  C   . THR C 1 180 ? -65.107 73.748  15.962  1.00 62.74  ? 178 THR C C   1 
ATOM   5491 O  O   . THR C 1 180 ? -64.055 74.274  15.584  1.00 65.41  ? 178 THR C O   1 
ATOM   5492 C  CB  . THR C 1 180 ? -66.228 71.445  15.935  1.00 64.31  ? 178 THR C CB  1 
ATOM   5493 O  OG1 . THR C 1 180 ? -67.462 71.689  16.621  1.00 73.29  ? 178 THR C OG1 1 
ATOM   5494 C  CG2 . THR C 1 180 ? -65.153 71.049  16.949  1.00 60.97  ? 178 THR C CG2 1 
ATOM   5495 N  N   . THR C 1 181 ? -65.692 74.073  17.111  1.00 57.63  ? 179 THR C N   1 
ATOM   5496 C  CA  . THR C 1 181 ? -65.106 75.058  18.004  1.00 61.35  ? 179 THR C CA  1 
ATOM   5497 C  C   . THR C 1 181 ? -64.982 74.443  19.373  1.00 65.38  ? 179 THR C C   1 
ATOM   5498 O  O   . THR C 1 181 ? -65.953 73.880  19.881  1.00 75.01  ? 179 THR C O   1 
ATOM   5499 C  CB  . THR C 1 181 ? -65.940 76.372  18.033  1.00 62.06  ? 179 THR C CB  1 
ATOM   5500 O  OG1 . THR C 1 181 ? -65.463 77.239  17.002  1.00 58.14  ? 179 THR C OG1 1 
ATOM   5501 C  CG2 . THR C 1 181 ? -65.837 77.111  19.392  1.00 55.32  ? 179 THR C CG2 1 
ATOM   5502 N  N   . MET C 1 182 ? -63.792 74.527  19.965  1.00 66.79  ? 180 MET C N   1 
ATOM   5503 C  CA  . MET C 1 182 ? -63.582 73.958  21.289  1.00 68.28  ? 180 MET C CA  1 
ATOM   5504 C  C   . MET C 1 182 ? -64.424 74.676  22.317  1.00 65.09  ? 180 MET C C   1 
ATOM   5505 O  O   . MET C 1 182 ? -64.729 75.861  22.175  1.00 64.69  ? 180 MET C O   1 
ATOM   5506 C  CB  . MET C 1 182 ? -62.106 73.978  21.700  1.00 72.62  ? 180 MET C CB  1 
ATOM   5507 C  CG  . MET C 1 182 ? -61.333 72.711  21.342  1.00 73.37  ? 180 MET C CG  1 
ATOM   5508 S  SD  . MET C 1 182 ? -59.765 72.530  22.227  1.00 71.57  ? 180 MET C SD  1 
ATOM   5509 C  CE  . MET C 1 182 ? -60.302 72.387  23.934  1.00 70.17  ? 180 MET C CE  1 
ATOM   5510 N  N   . ALA C 1 183 ? -64.809 73.941  23.349  1.00 70.63  ? 181 ALA C N   1 
ATOM   5511 C  CA  . ALA C 1 183 ? -65.541 74.526  24.457  1.00 69.96  ? 181 ALA C CA  1 
ATOM   5512 C  C   . ALA C 1 183 ? -64.579 75.401  25.235  1.00 70.03  ? 181 ALA C C   1 
ATOM   5513 O  O   . ALA C 1 183 ? -63.448 75.633  24.798  1.00 69.19  ? 181 ALA C O   1 
ATOM   5514 C  CB  . ALA C 1 183 ? -66.142 73.440  25.339  1.00 66.78  ? 181 ALA C CB  1 
ATOM   5515 N  N   . GLU C 1 184 ? -65.042 75.890  26.379  1.00 73.94  ? 182 GLU C N   1 
ATOM   5516 C  CA  . GLU C 1 184 ? -64.253 76.735  27.254  1.00 80.48  ? 182 GLU C CA  1 
ATOM   5517 C  C   . GLU C 1 184 ? -63.044 75.983  27.799  1.00 81.03  ? 182 GLU C C   1 
ATOM   5518 O  O   . GLU C 1 184 ? -63.197 74.997  28.525  1.00 84.17  ? 182 GLU C O   1 
ATOM   5519 C  CB  . GLU C 1 184 ? -65.126 77.241  28.401  1.00 86.54  ? 182 GLU C CB  1 
ATOM   5520 C  CG  . GLU C 1 184 ? -65.926 78.490  28.071  1.00 87.71  ? 182 GLU C CG  1 
ATOM   5521 C  CD  . GLU C 1 184 ? -65.098 79.750  28.215  1.00 85.48  ? 182 GLU C CD  1 
ATOM   5522 O  OE1 . GLU C 1 184 ? -64.200 79.978  27.376  1.00 81.11  ? 182 GLU C OE1 1 
ATOM   5523 O  OE2 . GLU C 1 184 ? -65.348 80.506  29.174  1.00 78.76  ? 182 GLU C OE2 1 
ATOM   5524 N  N   . SER C 1 185 ? -61.847 76.448  27.438  1.00 77.49  ? 183 SER C N   1 
ATOM   5525 C  CA  . SER C 1 185 ? -60.609 75.790  27.853  1.00 76.13  ? 183 SER C CA  1 
ATOM   5526 C  C   . SER C 1 185 ? -59.343 76.612  27.643  1.00 70.92  ? 183 SER C C   1 
ATOM   5527 O  O   . SER C 1 185 ? -59.257 77.440  26.733  1.00 66.98  ? 183 SER C O   1 
ATOM   5528 C  CB  . SER C 1 185 ? -60.445 74.462  27.122  1.00 76.66  ? 183 SER C CB  1 
ATOM   5529 O  OG  . SER C 1 185 ? -59.297 73.795  27.609  1.00 86.90  ? 183 SER C OG  1 
ATOM   5530 N  N   . SER C 1 186 ? -58.352 76.349  28.485  1.00 70.12  ? 184 SER C N   1 
ATOM   5531 C  CA  . SER C 1 186 ? -57.036 76.960  28.343  1.00 67.23  ? 184 SER C CA  1 
ATOM   5532 C  C   . SER C 1 186 ? -56.041 75.939  27.807  1.00 70.05  ? 184 SER C C   1 
ATOM   5533 O  O   . SER C 1 186 ? -56.434 74.870  27.319  1.00 75.61  ? 184 SER C O   1 
ATOM   5534 C  CB  . SER C 1 186 ? -56.558 77.522  29.681  1.00 70.87  ? 184 SER C CB  1 
ATOM   5535 O  OG  . SER C 1 186 ? -56.279 76.500  30.618  1.00 66.96  ? 184 SER C OG  1 
ATOM   5536 N  N   . LEU C 1 187 ? -54.758 76.274  27.900  1.00 63.68  ? 185 LEU C N   1 
ATOM   5537 C  CA  . LEU C 1 187 ? -53.682 75.383  27.485  1.00 58.53  ? 185 LEU C CA  1 
ATOM   5538 C  C   . LEU C 1 187 ? -53.084 74.710  28.707  1.00 62.60  ? 185 LEU C C   1 
ATOM   5539 O  O   . LEU C 1 187 ? -52.800 73.512  28.690  1.00 68.07  ? 185 LEU C O   1 
ATOM   5540 C  CB  . LEU C 1 187 ? -52.629 76.141  26.660  1.00 52.84  ? 185 LEU C CB  1 
ATOM   5541 C  CG  . LEU C 1 187 ? -53.110 76.628  25.278  1.00 46.28  ? 185 LEU C CG  1 
ATOM   5542 C  CD1 . LEU C 1 187 ? -52.065 77.463  24.561  1.00 50.30  ? 185 LEU C CD1 1 
ATOM   5543 C  CD2 . LEU C 1 187 ? -53.526 75.496  24.352  1.00 51.78  ? 185 LEU C CD2 1 
ATOM   5544 N  N   . LEU C 1 188 ? -52.935 75.480  29.780  1.00 66.30  ? 186 LEU C N   1 
ATOM   5545 C  CA  . LEU C 1 188 ? -52.536 74.960  31.088  1.00 65.28  ? 186 LEU C CA  1 
ATOM   5546 C  C   . LEU C 1 188 ? -53.385 73.740  31.475  1.00 68.34  ? 186 LEU C C   1 
ATOM   5547 O  O   . LEU C 1 188 ? -52.889 72.806  32.118  1.00 62.95  ? 186 LEU C O   1 
ATOM   5548 C  CB  . LEU C 1 188 ? -52.691 76.068  32.142  1.00 72.85  ? 186 LEU C CB  1 
ATOM   5549 C  CG  . LEU C 1 188 ? -51.681 76.311  33.279  1.00 71.90  ? 186 LEU C CG  1 
ATOM   5550 C  CD1 . LEU C 1 188 ? -50.365 76.870  32.761  1.00 67.90  ? 186 LEU C CD1 1 
ATOM   5551 C  CD2 . LEU C 1 188 ? -52.277 77.246  34.322  1.00 74.22  ? 186 LEU C CD2 1 
ATOM   5552 N  N   . ASP C 1 189 ? -54.660 73.764  31.067  1.00 67.48  ? 187 ASP C N   1 
ATOM   5553 C  CA  . ASP C 1 189 ? -55.626 72.693  31.330  1.00 68.03  ? 187 ASP C CA  1 
ATOM   5554 C  C   . ASP C 1 189 ? -55.182 71.333  30.791  1.00 69.41  ? 187 ASP C C   1 
ATOM   5555 O  O   . ASP C 1 189 ? -55.589 70.285  31.303  1.00 65.20  ? 187 ASP C O   1 
ATOM   5556 C  CB  . ASP C 1 189 ? -56.986 73.039  30.706  1.00 70.35  ? 187 ASP C CB  1 
ATOM   5557 C  CG  . ASP C 1 189 ? -57.734 74.121  31.470  1.00 68.76  ? 187 ASP C CG  1 
ATOM   5558 O  OD1 . ASP C 1 189 ? -57.248 74.556  32.536  1.00 67.67  ? 187 ASP C OD1 1 
ATOM   5559 O  OD2 . ASP C 1 189 ? -58.812 74.539  30.990  1.00 66.26  ? 187 ASP C OD2 1 
ATOM   5560 N  N   . LEU C 1 190 ? -54.351 71.352  29.754  1.00 67.58  ? 188 LEU C N   1 
ATOM   5561 C  CA  . LEU C 1 190 ? -53.972 70.120  29.064  1.00 67.35  ? 188 LEU C CA  1 
ATOM   5562 C  C   . LEU C 1 190 ? -52.720 69.435  29.632  1.00 66.30  ? 188 LEU C C   1 
ATOM   5563 O  O   . LEU C 1 190 ? -52.594 68.216  29.575  1.00 70.28  ? 188 LEU C O   1 
ATOM   5564 C  CB  . LEU C 1 190 ? -53.834 70.376  27.557  1.00 60.13  ? 188 LEU C CB  1 
ATOM   5565 C  CG  . LEU C 1 190 ? -55.040 71.004  26.840  1.00 54.81  ? 188 LEU C CG  1 
ATOM   5566 C  CD1 . LEU C 1 190 ? -54.613 71.526  25.486  1.00 43.47  ? 188 LEU C CD1 1 
ATOM   5567 C  CD2 . LEU C 1 190 ? -56.200 70.027  26.695  1.00 53.25  ? 188 LEU C CD2 1 
ATOM   5568 N  N   . LEU C 1 191 ? -51.825 70.227  30.209  1.00 66.46  ? 189 LEU C N   1 
ATOM   5569 C  CA  . LEU C 1 191 ? -50.493 69.769  30.619  1.00 66.88  ? 189 LEU C CA  1 
ATOM   5570 C  C   . LEU C 1 191 ? -50.401 69.312  32.103  1.00 67.35  ? 189 LEU C C   1 
ATOM   5571 O  O   . LEU C 1 191 ? -51.308 69.588  32.898  1.00 65.44  ? 189 LEU C O   1 
ATOM   5572 C  CB  . LEU C 1 191 ? -49.478 70.885  30.316  1.00 61.11  ? 189 LEU C CB  1 
ATOM   5573 C  CG  . LEU C 1 191 ? -49.740 71.656  29.011  1.00 59.32  ? 189 LEU C CG  1 
ATOM   5574 C  CD1 . LEU C 1 191 ? -49.033 72.998  28.975  1.00 54.31  ? 189 LEU C CD1 1 
ATOM   5575 C  CD2 . LEU C 1 191 ? -49.367 70.847  27.787  1.00 57.78  ? 189 LEU C CD2 1 
ATOM   5576 N  N   . PRO C 1 192 ? -49.315 68.593  32.473  1.00 66.94  ? 190 PRO C N   1 
ATOM   5577 C  CA  . PRO C 1 192 ? -49.124 68.261  33.898  1.00 69.13  ? 190 PRO C CA  1 
ATOM   5578 C  C   . PRO C 1 192 ? -48.740 69.506  34.690  1.00 71.85  ? 190 PRO C C   1 
ATOM   5579 O  O   . PRO C 1 192 ? -48.320 70.491  34.092  1.00 76.81  ? 190 PRO C O   1 
ATOM   5580 C  CB  . PRO C 1 192 ? -47.973 67.245  33.889  1.00 71.14  ? 190 PRO C CB  1 
ATOM   5581 C  CG  . PRO C 1 192 ? -47.293 67.403  32.567  1.00 68.95  ? 190 PRO C CG  1 
ATOM   5582 C  CD  . PRO C 1 192 ? -48.299 67.965  31.602  1.00 66.77  ? 190 PRO C CD  1 
ATOM   5583 N  N   . LYS C 1 193 ? -48.890 69.473  36.014  1.00 77.16  ? 191 LYS C N   1 
ATOM   5584 C  CA  . LYS C 1 193 ? -48.619 70.659  36.849  1.00 76.77  ? 191 LYS C CA  1 
ATOM   5585 C  C   . LYS C 1 193 ? -47.190 71.199  36.653  1.00 80.13  ? 191 LYS C C   1 
ATOM   5586 O  O   . LYS C 1 193 ? -46.220 70.458  36.776  1.00 80.20  ? 191 LYS C O   1 
ATOM   5587 C  CB  . LYS C 1 193 ? -48.978 70.386  38.312  1.00 77.60  ? 191 LYS C CB  1 
ATOM   5588 C  CG  . LYS C 1 193 ? -50.485 70.454  38.555  1.00 80.57  ? 191 LYS C CG  1 
ATOM   5589 C  CD  . LYS C 1 193 ? -50.960 69.631  39.746  1.00 78.90  ? 191 LYS C CD  1 
ATOM   5590 C  CE  . LYS C 1 193 ? -52.477 69.674  39.867  1.00 79.32  ? 191 LYS C CE  1 
ATOM   5591 N  NZ  . LYS C 1 193 ? -52.988 69.050  41.122  1.00 77.67  ? 191 LYS C NZ  1 
ATOM   5592 N  N   . GLU C 1 194 ? -47.081 72.490  36.335  1.00 81.24  ? 192 GLU C N   1 
ATOM   5593 C  CA  . GLU C 1 194 ? -45.900 73.030  35.637  1.00 84.58  ? 192 GLU C CA  1 
ATOM   5594 C  C   . GLU C 1 194 ? -44.534 72.860  36.328  1.00 84.84  ? 192 GLU C C   1 
ATOM   5595 O  O   . GLU C 1 194 ? -43.491 72.927  35.666  1.00 83.36  ? 192 GLU C O   1 
ATOM   5596 C  CB  . GLU C 1 194 ? -46.155 74.471  35.116  1.00 93.43  ? 192 GLU C CB  1 
ATOM   5597 C  CG  . GLU C 1 194 ? -45.827 75.637  36.049  1.00 96.89  ? 192 GLU C CG  1 
ATOM   5598 C  CD  . GLU C 1 194 ? -44.597 76.440  35.626  1.00 97.75  ? 192 GLU C CD  1 
ATOM   5599 O  OE1 . GLU C 1 194 ? -44.094 76.267  34.488  1.00 93.73  ? 192 GLU C OE1 1 
ATOM   5600 O  OE2 . GLU C 1 194 ? -44.128 77.264  36.444  1.00 100.97 ? 192 GLU C OE2 1 
ATOM   5601 N  N   . GLU C 1 195 ? -44.539 72.642  37.642  1.00 84.29  ? 193 GLU C N   1 
ATOM   5602 C  CA  . GLU C 1 195 ? -43.311 72.299  38.362  1.00 84.71  ? 193 GLU C CA  1 
ATOM   5603 C  C   . GLU C 1 195 ? -43.040 70.792  38.287  1.00 85.62  ? 193 GLU C C   1 
ATOM   5604 O  O   . GLU C 1 195 ? -42.249 70.249  39.062  1.00 85.99  ? 193 GLU C O   1 
ATOM   5605 C  CB  . GLU C 1 195 ? -43.341 72.815  39.807  1.00 87.58  ? 193 GLU C CB  1 
ATOM   5606 C  CG  . GLU C 1 195 ? -42.885 74.267  39.955  1.00 92.87  ? 193 GLU C CG  1 
ATOM   5607 C  CD  . GLU C 1 195 ? -43.098 74.837  41.359  1.00 98.68  ? 193 GLU C CD  1 
ATOM   5608 O  OE1 . GLU C 1 195 ? -43.133 74.051  42.333  1.00 103.72 ? 193 GLU C OE1 1 
ATOM   5609 O  OE2 . GLU C 1 195 ? -43.229 76.078  41.499  1.00 88.98  ? 193 GLU C OE2 1 
ATOM   5610 N  N   . LYS C 1 196 ? -43.742 70.129  37.364  1.00 87.30  ? 194 LYS C N   1 
ATOM   5611 C  CA  . LYS C 1 196 ? -43.382 68.801  36.848  1.00 86.04  ? 194 LYS C CA  1 
ATOM   5612 C  C   . LYS C 1 196 ? -42.657 69.011  35.515  1.00 81.57  ? 194 LYS C C   1 
ATOM   5613 O  O   . LYS C 1 196 ? -41.789 68.210  35.116  1.00 81.37  ? 194 LYS C O   1 
ATOM   5614 C  CB  . LYS C 1 196 ? -44.637 67.941  36.609  1.00 85.18  ? 194 LYS C CB  1 
ATOM   5615 C  CG  . LYS C 1 196 ? -44.943 66.857  37.643  1.00 86.23  ? 194 LYS C CG  1 
ATOM   5616 C  CD  . LYS C 1 196 ? -44.393 65.498  37.217  1.00 79.23  ? 194 LYS C CD  1 
ATOM   5617 C  CE  . LYS C 1 196 ? -45.465 64.419  37.220  1.00 75.75  ? 194 LYS C CE  1 
ATOM   5618 N  NZ  . LYS C 1 196 ? -45.944 64.072  38.585  1.00 72.62  ? 194 LYS C NZ  1 
ATOM   5619 N  N   . LEU C 1 197 ? -43.015 70.112  34.850  1.00 71.05  ? 195 LEU C N   1 
ATOM   5620 C  CA  . LEU C 1 197 ? -42.524 70.428  33.512  1.00 68.16  ? 195 LEU C CA  1 
ATOM   5621 C  C   . LEU C 1 197 ? -41.123 71.037  33.495  1.00 65.34  ? 195 LEU C C   1 
ATOM   5622 O  O   . LEU C 1 197 ? -40.717 71.667  32.516  1.00 67.90  ? 195 LEU C O   1 
ATOM   5623 C  CB  . LEU C 1 197 ? -43.542 71.293  32.758  1.00 68.21  ? 195 LEU C CB  1 
ATOM   5624 C  CG  . LEU C 1 197 ? -44.895 70.592  32.523  1.00 73.26  ? 195 LEU C CG  1 
ATOM   5625 C  CD1 . LEU C 1 197 ? -46.014 71.564  32.178  1.00 67.77  ? 195 LEU C CD1 1 
ATOM   5626 C  CD2 . LEU C 1 197 ? -44.791 69.495  31.467  1.00 69.74  ? 195 LEU C CD2 1 
ATOM   5627 N  N   . ARG C 1 198 ? -40.384 70.823  34.578  1.00 67.65  ? 196 ARG C N   1 
ATOM   5628 C  CA  . ARG C 1 198 ? -39.015 71.320  34.711  1.00 63.46  ? 196 ARG C CA  1 
ATOM   5629 C  C   . ARG C 1 198 ? -38.006 70.385  34.055  1.00 55.89  ? 196 ARG C C   1 
ATOM   5630 O  O   . ARG C 1 198 ? -36.977 70.852  33.563  1.00 51.05  ? 196 ARG C O   1 
ATOM   5631 C  CB  . ARG C 1 198 ? -38.647 71.620  36.184  1.00 63.53  ? 196 ARG C CB  1 
ATOM   5632 C  CG  . ARG C 1 198 ? -39.247 70.704  37.262  1.00 69.85  ? 196 ARG C CG  1 
ATOM   5633 C  CD  . ARG C 1 198 ? -38.303 69.588  37.704  1.00 73.13  ? 196 ARG C CD  1 
ATOM   5634 N  NE  . ARG C 1 198 ? -38.424 69.196  39.124  1.00 78.26  ? 196 ARG C NE  1 
ATOM   5635 C  CZ  . ARG C 1 198 ? -38.880 68.017  39.576  1.00 82.76  ? 196 ARG C CZ  1 
ATOM   5636 N  NH1 . ARG C 1 198 ? -38.927 67.770  40.884  1.00 70.77  ? 196 ARG C NH1 1 
ATOM   5637 N  NH2 . ARG C 1 198 ? -39.298 67.075  38.733  1.00 84.54  ? 196 ARG C NH2 1 
ATOM   5638 N  N   . HIS C 1 199 ? -38.317 69.085  34.040  1.00 52.20  ? 197 HIS C N   1 
ATOM   5639 C  CA  . HIS C 1 199 ? -37.456 68.057  33.408  1.00 51.61  ? 197 HIS C CA  1 
ATOM   5640 C  C   . HIS C 1 199 ? -37.851 67.820  31.991  1.00 47.21  ? 197 HIS C C   1 
ATOM   5641 O  O   . HIS C 1 199 ? -39.011 67.520  31.704  1.00 47.66  ? 197 HIS C O   1 
ATOM   5642 C  CB  . HIS C 1 199 ? -37.530 66.727  34.140  1.00 55.25  ? 197 HIS C CB  1 
ATOM   5643 C  CG  . HIS C 1 199 ? -36.765 66.686  35.438  1.00 57.06  ? 197 HIS C CG  1 
ATOM   5644 N  ND1 . HIS C 1 199 ? -35.412 66.705  35.492  1.00 61.47  ? 197 HIS C ND1 1 
ATOM   5645 C  CD2 . HIS C 1 199 ? -37.212 66.564  36.754  1.00 62.15  ? 197 HIS C CD2 1 
ATOM   5646 C  CE1 . HIS C 1 199 ? -35.018 66.622  36.782  1.00 62.16  ? 197 HIS C CE1 1 
ATOM   5647 N  NE2 . HIS C 1 199 ? -36.123 66.541  37.553  1.00 63.11  ? 197 HIS C NE2 1 
ATOM   5648 N  N   . TYR C 1 200 ? -36.891 67.938  31.086  1.00 41.97  ? 198 TYR C N   1 
ATOM   5649 C  CA  . TYR C 1 200 ? -37.163 67.720  29.671  1.00 40.14  ? 198 TYR C CA  1 
ATOM   5650 C  C   . TYR C 1 200 ? -35.861 67.528  28.961  1.00 39.10  ? 198 TYR C C   1 
ATOM   5651 O  O   . TYR C 1 200 ? -34.814 67.847  29.534  1.00 36.71  ? 198 TYR C O   1 
ATOM   5652 C  CB  . TYR C 1 200 ? -37.926 68.895  29.053  1.00 44.00  ? 198 TYR C CB  1 
ATOM   5653 C  CG  . TYR C 1 200 ? -37.242 70.248  29.161  1.00 46.55  ? 198 TYR C CG  1 
ATOM   5654 C  CD1 . TYR C 1 200 ? -36.386 70.708  28.159  1.00 47.76  ? 198 TYR C CD1 1 
ATOM   5655 C  CD2 . TYR C 1 200 ? -37.479 71.087  30.259  1.00 48.38  ? 198 TYR C CD2 1 
ATOM   5656 C  CE1 . TYR C 1 200 ? -35.772 71.954  28.256  1.00 46.33  ? 198 TYR C CE1 1 
ATOM   5657 C  CE2 . TYR C 1 200 ? -36.875 72.329  30.354  1.00 46.96  ? 198 TYR C CE2 1 
ATOM   5658 C  CZ  . TYR C 1 200 ? -36.029 72.752  29.349  1.00 46.06  ? 198 TYR C CZ  1 
ATOM   5659 O  OH  . TYR C 1 200 ? -35.439 73.985  29.451  1.00 52.28  ? 198 TYR C OH  1 
ATOM   5660 N  N   . PHE C 1 201 ? -35.945 66.991  27.732  1.00 37.95  ? 199 PHE C N   1 
ATOM   5661 C  CA  . PHE C 1 201 ? -34.793 66.731  26.837  1.00 36.64  ? 199 PHE C CA  1 
ATOM   5662 C  C   . PHE C 1 201 ? -34.794 67.755  25.710  1.00 36.14  ? 199 PHE C C   1 
ATOM   5663 O  O   . PHE C 1 201 ? -35.853 68.272  25.384  1.00 38.53  ? 199 PHE C O   1 
ATOM   5664 C  CB  . PHE C 1 201 ? -34.845 65.275  26.279  1.00 35.40  ? 199 PHE C CB  1 
ATOM   5665 C  CG  . PHE C 1 201 ? -34.949 64.234  27.363  1.00 34.74  ? 199 PHE C CG  1 
ATOM   5666 C  CD1 . PHE C 1 201 ? -33.819 63.687  27.917  1.00 31.78  ? 199 PHE C CD1 1 
ATOM   5667 C  CD2 . PHE C 1 201 ? -36.192 63.848  27.863  1.00 35.46  ? 199 PHE C CD2 1 
ATOM   5668 C  CE1 . PHE C 1 201 ? -33.895 62.803  28.970  1.00 34.08  ? 199 PHE C CE1 1 
ATOM   5669 C  CE2 . PHE C 1 201 ? -36.288 62.946  28.915  1.00 35.34  ? 199 PHE C CE2 1 
ATOM   5670 C  CZ  . PHE C 1 201 ? -35.132 62.413  29.472  1.00 33.19  ? 199 PHE C CZ  1 
ATOM   5671 N  N   . ARG C 1 202 ? -33.631 68.057  25.125  1.00 36.10  ? 200 ARG C N   1 
ATOM   5672 C  CA  . ARG C 1 202 ? -33.546 69.052  24.052  1.00 37.40  ? 200 ARG C CA  1 
ATOM   5673 C  C   . ARG C 1 202 ? -32.580 68.628  22.977  1.00 35.26  ? 200 ARG C C   1 
ATOM   5674 O  O   . ARG C 1 202 ? -31.485 68.168  23.282  1.00 43.32  ? 200 ARG C O   1 
ATOM   5675 C  CB  . ARG C 1 202 ? -33.082 70.420  24.584  1.00 41.75  ? 200 ARG C CB  1 
ATOM   5676 C  CG  . ARG C 1 202 ? -32.594 71.431  23.512  1.00 36.70  ? 200 ARG C CG  1 
ATOM   5677 C  CD  . ARG C 1 202 ? -33.739 72.238  22.921  1.00 37.72  ? 200 ARG C CD  1 
ATOM   5678 N  NE  . ARG C 1 202 ? -34.666 72.556  23.999  1.00 41.81  ? 200 ARG C NE  1 
ATOM   5679 C  CZ  . ARG C 1 202 ? -34.557 73.625  24.779  1.00 49.12  ? 200 ARG C CZ  1 
ATOM   5680 N  NH1 . ARG C 1 202 ? -33.594 74.525  24.548  1.00 50.25  ? 200 ARG C NH1 1 
ATOM   5681 N  NH2 . ARG C 1 202 ? -35.429 73.813  25.771  1.00 48.23  ? 200 ARG C NH2 1 
ATOM   5682 N  N   . TYR C 1 203 ? -32.949 68.818  21.724  1.00 34.75  ? 201 TYR C N   1 
ATOM   5683 C  CA  . TYR C 1 203 ? -32.048 68.472  20.634  1.00 37.19  ? 201 TYR C CA  1 
ATOM   5684 C  C   . TYR C 1 203 ? -32.412 69.261  19.391  1.00 38.95  ? 201 TYR C C   1 
ATOM   5685 O  O   . TYR C 1 203 ? -33.342 70.060  19.418  1.00 41.49  ? 201 TYR C O   1 
ATOM   5686 C  CB  . TYR C 1 203 ? -32.080 66.961  20.369  1.00 42.50  ? 201 TYR C CB  1 
ATOM   5687 C  CG  . TYR C 1 203 ? -33.309 66.488  19.615  1.00 41.02  ? 201 TYR C CG  1 
ATOM   5688 C  CD1 . TYR C 1 203 ? -34.505 66.167  20.285  1.00 39.77  ? 201 TYR C CD1 1 
ATOM   5689 C  CD2 . TYR C 1 203 ? -33.280 66.362  18.230  1.00 40.39  ? 201 TYR C CD2 1 
ATOM   5690 C  CE1 . TYR C 1 203 ? -35.626 65.731  19.583  1.00 36.11  ? 201 TYR C CE1 1 
ATOM   5691 C  CE2 . TYR C 1 203 ? -34.391 65.943  17.524  1.00 41.55  ? 201 TYR C CE2 1 
ATOM   5692 C  CZ  . TYR C 1 203 ? -35.560 65.622  18.201  1.00 39.05  ? 201 TYR C CZ  1 
ATOM   5693 O  OH  . TYR C 1 203 ? -36.644 65.216  17.449  1.00 37.68  ? 201 TYR C OH  1 
ATOM   5694 N  N   . LEU C 1 204 ? -31.682 69.069  18.300  1.00 42.75  ? 202 LEU C N   1 
ATOM   5695 C  CA  . LEU C 1 204 ? -31.940 69.871  17.112  1.00 47.73  ? 202 LEU C CA  1 
ATOM   5696 C  C   . LEU C 1 204 ? -32.327 68.979  15.962  1.00 53.93  ? 202 LEU C C   1 
ATOM   5697 O  O   . LEU C 1 204 ? -31.707 67.939  15.768  1.00 58.06  ? 202 LEU C O   1 
ATOM   5698 C  CB  . LEU C 1 204 ? -30.706 70.703  16.737  1.00 53.42  ? 202 LEU C CB  1 
ATOM   5699 C  CG  . LEU C 1 204 ? -30.437 72.046  17.452  1.00 53.78  ? 202 LEU C CG  1 
ATOM   5700 C  CD1 . LEU C 1 204 ? -29.213 72.735  16.863  1.00 47.85  ? 202 LEU C CD1 1 
ATOM   5701 C  CD2 . LEU C 1 204 ? -31.638 72.985  17.419  1.00 55.14  ? 202 LEU C CD2 1 
ATOM   5702 N  N   . GLY C 1 205 ? -33.345 69.377  15.194  1.00 58.85  ? 203 GLY C N   1 
ATOM   5703 C  CA  . GLY C 1 205 ? -33.820 68.545  14.083  1.00 58.05  ? 203 GLY C CA  1 
ATOM   5704 C  C   . GLY C 1 205 ? -34.859 69.129  13.139  1.00 58.65  ? 203 GLY C C   1 
ATOM   5705 O  O   . GLY C 1 205 ? -34.817 70.326  12.792  1.00 57.12  ? 203 GLY C O   1 
ATOM   5706 N  N   . SER C 1 206 ? -35.802 68.275  12.729  1.00 50.02  ? 204 SER C N   1 
ATOM   5707 C  CA  . SER C 1 206 ? -36.737 68.642  11.669  1.00 45.16  ? 204 SER C CA  1 
ATOM   5708 C  C   . SER C 1 206 ? -38.233 68.544  11.991  1.00 44.51  ? 204 SER C C   1 
ATOM   5709 O  O   . SER C 1 206 ? -38.638 68.170  13.104  1.00 46.57  ? 204 SER C O   1 
ATOM   5710 C  CB  . SER C 1 206 ? -36.394 67.913  10.365  1.00 44.65  ? 204 SER C CB  1 
ATOM   5711 O  OG  . SER C 1 206 ? -36.648 66.517  10.422  1.00 46.42  ? 204 SER C OG  1 
ATOM   5712 N  N   . LEU C 1 207 ? -39.033 68.967  11.011  1.00 46.02  ? 205 LEU C N   1 
ATOM   5713 C  CA  . LEU C 1 207 ? -40.463 68.671  10.929  1.00 48.02  ? 205 LEU C CA  1 
ATOM   5714 C  C   . LEU C 1 207 ? -40.594 67.167  10.658  1.00 46.44  ? 205 LEU C C   1 
ATOM   5715 O  O   . LEU C 1 207 ? -39.666 66.540  10.137  1.00 44.34  ? 205 LEU C O   1 
ATOM   5716 C  CB  . LEU C 1 207 ? -41.104 69.451  9.765   1.00 52.25  ? 205 LEU C CB  1 
ATOM   5717 C  CG  . LEU C 1 207 ? -41.356 70.970  9.705   1.00 55.68  ? 205 LEU C CG  1 
ATOM   5718 C  CD1 . LEU C 1 207 ? -40.247 71.794  10.340  1.00 55.27  ? 205 LEU C CD1 1 
ATOM   5719 C  CD2 . LEU C 1 207 ? -41.569 71.435  8.257   1.00 58.02  ? 205 LEU C CD2 1 
ATOM   5720 N  N   . THR C 1 208 ? -41.746 66.605  11.003  1.00 46.23  ? 206 THR C N   1 
ATOM   5721 C  CA  . THR C 1 208 ? -41.967 65.164  10.930  1.00 48.00  ? 206 THR C CA  1 
ATOM   5722 C  C   . THR C 1 208 ? -43.055 64.847  9.917   1.00 53.75  ? 206 THR C C   1 
ATOM   5723 O  O   . THR C 1 208 ? -43.525 63.707  9.834   1.00 52.18  ? 206 THR C O   1 
ATOM   5724 C  CB  . THR C 1 208 ? -42.455 64.591  12.271  1.00 41.49  ? 206 THR C CB  1 
ATOM   5725 O  OG1 . THR C 1 208 ? -43.724 65.176  12.592  1.00 33.11  ? 206 THR C OG1 1 
ATOM   5726 C  CG2 . THR C 1 208 ? -41.447 64.845  13.373  1.00 43.32  ? 206 THR C CG2 1 
ATOM   5727 N  N   . THR C 1 209 ? -43.477 65.888  9.206   1.00 59.76  ? 207 THR C N   1 
ATOM   5728 C  CA  . THR C 1 209 ? -44.267 65.783  7.994   1.00 59.45  ? 207 THR C CA  1 
ATOM   5729 C  C   . THR C 1 209 ? -43.478 66.514  6.903   1.00 61.19  ? 207 THR C C   1 
ATOM   5730 O  O   . THR C 1 209 ? -42.715 67.428  7.204   1.00 67.73  ? 207 THR C O   1 
ATOM   5731 C  CB  . THR C 1 209 ? -45.655 66.429  8.183   1.00 59.98  ? 207 THR C CB  1 
ATOM   5732 O  OG1 . THR C 1 209 ? -45.525 67.668  8.892   1.00 57.51  ? 207 THR C OG1 1 
ATOM   5733 C  CG2 . THR C 1 209 ? -46.568 65.512  8.983   1.00 61.38  ? 207 THR C CG2 1 
ATOM   5734 N  N   . PRO C 1 210 ? -43.634 66.104  5.632   1.00 65.13  ? 208 PRO C N   1 
ATOM   5735 C  CA  . PRO C 1 210 ? -42.938 66.768  4.514   1.00 65.75  ? 208 PRO C CA  1 
ATOM   5736 C  C   . PRO C 1 210 ? -43.124 68.288  4.501   1.00 60.99  ? 208 PRO C C   1 
ATOM   5737 O  O   . PRO C 1 210 ? -44.197 68.753  4.862   1.00 62.82  ? 208 PRO C O   1 
ATOM   5738 C  CB  . PRO C 1 210 ? -43.600 66.142  3.290   1.00 69.51  ? 208 PRO C CB  1 
ATOM   5739 C  CG  . PRO C 1 210 ? -43.939 64.755  3.749   1.00 66.96  ? 208 PRO C CG  1 
ATOM   5740 C  CD  . PRO C 1 210 ? -44.374 64.911  5.178   1.00 63.40  ? 208 PRO C CD  1 
ATOM   5741 N  N   . THR C 1 211 ? -42.103 69.051  4.088   1.00 61.09  ? 209 THR C N   1 
ATOM   5742 C  CA  . THR C 1 211 ? -40.850 68.495  3.532   1.00 64.50  ? 209 THR C CA  1 
ATOM   5743 C  C   . THR C 1 211 ? -39.724 68.231  4.540   1.00 65.05  ? 209 THR C C   1 
ATOM   5744 O  O   . THR C 1 211 ? -38.552 68.079  4.153   1.00 67.91  ? 209 THR C O   1 
ATOM   5745 C  CB  . THR C 1 211 ? -40.306 69.326  2.348   1.00 67.09  ? 209 THR C CB  1 
ATOM   5746 O  OG1 . THR C 1 211 ? -40.260 70.712  2.712   1.00 60.12  ? 209 THR C OG1 1 
ATOM   5747 C  CG2 . THR C 1 211 ? -41.170 69.111  1.080   1.00 61.99  ? 209 THR C CG2 1 
ATOM   5748 N  N   . CYS C 1 212 ? -40.100 68.142  5.818   1.00 65.88  ? 210 CYS C N   1 
ATOM   5749 C  CA  . CYS C 1 212 ? -39.205 67.731  6.902   1.00 63.42  ? 210 CYS C CA  1 
ATOM   5750 C  C   . CYS C 1 212 ? -37.990 68.680  7.054   1.00 69.66  ? 210 CYS C C   1 
ATOM   5751 O  O   . CYS C 1 212 ? -36.863 68.232  7.299   1.00 66.16  ? 210 CYS C O   1 
ATOM   5752 C  CB  . CYS C 1 212 ? -38.759 66.258  6.727   1.00 61.55  ? 210 CYS C CB  1 
ATOM   5753 S  SG  . CYS C 1 212 ? -39.919 65.093  5.938   1.00 52.86  ? 210 CYS C SG  1 
ATOM   5754 N  N   . ASP C 1 213 ? -38.241 69.988  6.920   1.00 72.02  ? 211 ASP C N   1 
ATOM   5755 C  CA  . ASP C 1 213 ? -37.196 71.030  6.945   1.00 70.01  ? 211 ASP C CA  1 
ATOM   5756 C  C   . ASP C 1 213 ? -36.363 70.993  8.223   1.00 70.09  ? 211 ASP C C   1 
ATOM   5757 O  O   . ASP C 1 213 ? -36.925 71.024  9.321   1.00 70.36  ? 211 ASP C O   1 
ATOM   5758 C  CB  . ASP C 1 213 ? -37.820 72.422  6.812   1.00 67.88  ? 211 ASP C CB  1 
ATOM   5759 C  CG  . ASP C 1 213 ? -38.690 72.564  5.579   1.00 71.58  ? 211 ASP C CG  1 
ATOM   5760 O  OD1 . ASP C 1 213 ? -38.203 73.114  4.561   1.00 68.64  ? 211 ASP C OD1 1 
ATOM   5761 O  OD2 . ASP C 1 213 ? -39.863 72.129  5.640   1.00 74.89  ? 211 ASP C OD2 1 
ATOM   5762 N  N   . GLU C 1 214 ? -35.035 70.952  8.086   1.00 62.88  ? 212 GLU C N   1 
ATOM   5763 C  CA  . GLU C 1 214 ? -34.148 70.818  9.248   1.00 58.81  ? 212 GLU C CA  1 
ATOM   5764 C  C   . GLU C 1 214 ? -34.023 72.139  10.033  1.00 61.23  ? 212 GLU C C   1 
ATOM   5765 O  O   . GLU C 1 214 ? -32.941 72.712  10.155  1.00 63.97  ? 212 GLU C O   1 
ATOM   5766 C  CB  . GLU C 1 214 ? -32.779 70.225  8.844   1.00 59.24  ? 212 GLU C CB  1 
ATOM   5767 C  CG  . GLU C 1 214 ? -32.890 68.850  8.200   1.00 53.68  ? 212 GLU C CG  1 
ATOM   5768 C  CD  . GLU C 1 214 ? -31.567 68.102  8.042   1.00 58.71  ? 212 GLU C CD  1 
ATOM   5769 O  OE1 . GLU C 1 214 ? -30.601 68.649  7.450   1.00 48.87  ? 212 GLU C OE1 1 
ATOM   5770 O  OE2 . GLU C 1 214 ? -31.511 66.916  8.466   1.00 63.73  ? 212 GLU C OE2 1 
ATOM   5771 N  N   . LYS C 1 215 ? -35.144 72.604  10.580  1.00 56.82  ? 213 LYS C N   1 
ATOM   5772 C  CA  . LYS C 1 215 ? -35.220 73.928  11.211  1.00 55.96  ? 213 LYS C CA  1 
ATOM   5773 C  C   . LYS C 1 215 ? -35.795 73.985  12.641  1.00 52.79  ? 213 LYS C C   1 
ATOM   5774 O  O   . LYS C 1 215 ? -36.071 75.081  13.143  1.00 52.53  ? 213 LYS C O   1 
ATOM   5775 C  CB  . LYS C 1 215 ? -36.032 74.877  10.316  1.00 58.60  ? 213 LYS C CB  1 
ATOM   5776 C  CG  . LYS C 1 215 ? -37.445 74.388  9.987   1.00 55.41  ? 213 LYS C CG  1 
ATOM   5777 C  CD  . LYS C 1 215 ? -38.424 75.530  9.715   1.00 57.65  ? 213 LYS C CD  1 
ATOM   5778 C  CE  . LYS C 1 215 ? -38.011 76.462  8.574   1.00 56.41  ? 213 LYS C CE  1 
ATOM   5779 N  NZ  . LYS C 1 215 ? -38.470 75.936  7.256   1.00 56.08  ? 213 LYS C NZ  1 
ATOM   5780 N  N   . VAL C 1 216 ? -35.958 72.837  13.305  1.00 47.72  ? 214 VAL C N   1 
ATOM   5781 C  CA  . VAL C 1 216 ? -36.679 72.791  14.602  1.00 43.77  ? 214 VAL C CA  1 
ATOM   5782 C  C   . VAL C 1 216 ? -35.786 72.627  15.832  1.00 41.45  ? 214 VAL C C   1 
ATOM   5783 O  O   . VAL C 1 216 ? -34.751 71.988  15.780  1.00 41.51  ? 214 VAL C O   1 
ATOM   5784 C  CB  . VAL C 1 216 ? -37.780 71.683  14.609  1.00 48.61  ? 214 VAL C CB  1 
ATOM   5785 C  CG1 . VAL C 1 216 ? -38.392 71.500  15.989  1.00 43.77  ? 214 VAL C CG1 1 
ATOM   5786 C  CG2 . VAL C 1 216 ? -38.876 72.026  13.620  1.00 51.37  ? 214 VAL C CG2 1 
ATOM   5787 N  N   . VAL C 1 217 ? -36.204 73.216  16.949  1.00 42.67  ? 215 VAL C N   1 
ATOM   5788 C  CA  . VAL C 1 217 ? -35.542 72.993  18.213  1.00 44.68  ? 215 VAL C CA  1 
ATOM   5789 C  C   . VAL C 1 217 ? -36.561 72.357  19.142  1.00 45.85  ? 215 VAL C C   1 
ATOM   5790 O  O   . VAL C 1 217 ? -37.512 72.995  19.628  1.00 45.82  ? 215 VAL C O   1 
ATOM   5791 C  CB  . VAL C 1 217 ? -34.829 74.253  18.800  1.00 49.90  ? 215 VAL C CB  1 
ATOM   5792 C  CG1 . VAL C 1 217 ? -35.728 75.484  18.831  1.00 49.24  ? 215 VAL C CG1 1 
ATOM   5793 C  CG2 . VAL C 1 217 ? -34.281 73.963  20.187  1.00 48.91  ? 215 VAL C CG2 1 
ATOM   5794 N  N   . TRP C 1 218 ? -36.345 71.059  19.340  1.00 46.43  ? 216 TRP C N   1 
ATOM   5795 C  CA  . TRP C 1 218 ? -37.284 70.182  19.985  1.00 40.22  ? 216 TRP C CA  1 
ATOM   5796 C  C   . TRP C 1 218 ? -37.138 70.234  21.437  1.00 39.64  ? 216 TRP C C   1 
ATOM   5797 O  O   . TRP C 1 218 ? -36.034 70.326  21.964  1.00 39.39  ? 216 TRP C O   1 
ATOM   5798 C  CB  . TRP C 1 218 ? -37.000 68.753  19.556  1.00 41.28  ? 216 TRP C CB  1 
ATOM   5799 C  CG  . TRP C 1 218 ? -37.607 68.437  18.221  1.00 40.86  ? 216 TRP C CG  1 
ATOM   5800 C  CD1 . TRP C 1 218 ? -36.975 68.407  16.975  1.00 40.24  ? 216 TRP C CD1 1 
ATOM   5801 C  CD2 . TRP C 1 218 ? -39.005 68.095  17.956  1.00 39.81  ? 216 TRP C CD2 1 
ATOM   5802 N  NE1 . TRP C 1 218 ? -37.865 68.073  15.987  1.00 40.37  ? 216 TRP C NE1 1 
ATOM   5803 C  CE2 . TRP C 1 218 ? -39.108 67.883  16.511  1.00 41.61  ? 216 TRP C CE2 1 
ATOM   5804 C  CE3 . TRP C 1 218 ? -40.141 67.975  18.736  1.00 42.94  ? 216 TRP C CE3 1 
ATOM   5805 C  CZ2 . TRP C 1 218 ? -40.307 67.556  15.903  1.00 41.15  ? 216 TRP C CZ2 1 
ATOM   5806 C  CZ3 . TRP C 1 218 ? -41.340 67.622  18.113  1.00 40.42  ? 216 TRP C CZ3 1 
ATOM   5807 C  CH2 . TRP C 1 218 ? -41.417 67.431  16.732  1.00 41.38  ? 216 TRP C CH2 1 
ATOM   5808 N  N   . THR C 1 219 ? -38.275 70.143  22.098  1.00 36.55  ? 217 THR C N   1 
ATOM   5809 C  CA  . THR C 1 219 ? -38.323 69.983  23.521  1.00 35.85  ? 217 THR C CA  1 
ATOM   5810 C  C   . THR C 1 219 ? -39.292 68.831  23.793  1.00 34.17  ? 217 THR C C   1 
ATOM   5811 O  O   . THR C 1 219 ? -40.482 68.923  23.508  1.00 33.90  ? 217 THR C O   1 
ATOM   5812 C  CB  . THR C 1 219 ? -38.809 71.271  24.209  1.00 34.39  ? 217 THR C CB  1 
ATOM   5813 O  OG1 . THR C 1 219 ? -37.888 72.315  23.891  1.00 41.76  ? 217 THR C OG1 1 
ATOM   5814 C  CG2 . THR C 1 219 ? -38.881 71.096  25.700  1.00 30.20  ? 217 THR C CG2 1 
ATOM   5815 N  N   . VAL C 1 220 ? -38.757 67.772  24.377  1.00 32.76  ? 218 VAL C N   1 
ATOM   5816 C  CA  . VAL C 1 220 ? -39.526 66.610  24.684  1.00 31.53  ? 218 VAL C CA  1 
ATOM   5817 C  C   . VAL C 1 220 ? -39.550 66.510  26.208  1.00 31.90  ? 218 VAL C C   1 
ATOM   5818 O  O   . VAL C 1 220 ? -38.511 66.389  26.821  1.00 33.50  ? 218 VAL C O   1 
ATOM   5819 C  CB  . VAL C 1 220 ? -38.925 65.331  24.005  1.00 28.46  ? 218 VAL C CB  1 
ATOM   5820 C  CG1 . VAL C 1 220 ? -39.803 64.128  24.293  1.00 24.48  ? 218 VAL C CG1 1 
ATOM   5821 C  CG2 . VAL C 1 220 ? -38.842 65.514  22.501  1.00 27.12  ? 218 VAL C CG2 1 
ATOM   5822 N  N   . PHE C 1 221 ? -40.731 66.580  26.815  1.00 36.18  ? 219 PHE C N   1 
ATOM   5823 C  CA  . PHE C 1 221 ? -40.822 66.605  28.282  1.00 40.06  ? 219 PHE C CA  1 
ATOM   5824 C  C   . PHE C 1 221 ? -40.714 65.202  28.884  1.00 43.79  ? 219 PHE C C   1 
ATOM   5825 O  O   . PHE C 1 221 ? -41.296 64.245  28.365  1.00 44.30  ? 219 PHE C O   1 
ATOM   5826 C  CB  . PHE C 1 221 ? -42.106 67.332  28.711  1.00 44.85  ? 219 PHE C CB  1 
ATOM   5827 C  CG  . PHE C 1 221 ? -42.032 68.835  28.520  1.00 47.81  ? 219 PHE C CG  1 
ATOM   5828 C  CD1 . PHE C 1 221 ? -42.255 69.408  27.266  1.00 51.63  ? 219 PHE C CD1 1 
ATOM   5829 C  CD2 . PHE C 1 221 ? -41.679 69.661  29.574  1.00 50.09  ? 219 PHE C CD2 1 
ATOM   5830 C  CE1 . PHE C 1 221 ? -42.155 70.782  27.076  1.00 59.56  ? 219 PHE C CE1 1 
ATOM   5831 C  CE2 . PHE C 1 221 ? -41.569 71.033  29.396  1.00 54.76  ? 219 PHE C CE2 1 
ATOM   5832 C  CZ  . PHE C 1 221 ? -41.809 71.599  28.144  1.00 58.22  ? 219 PHE C CZ  1 
ATOM   5833 N  N   . ARG C 1 222 ? -39.950 65.076  29.960  1.00 49.39  ? 220 ARG C N   1 
ATOM   5834 C  CA  . ARG C 1 222 ? -39.722 63.782  30.591  1.00 54.41  ? 220 ARG C CA  1 
ATOM   5835 C  C   . ARG C 1 222 ? -41.022 63.150  31.076  1.00 55.90  ? 220 ARG C C   1 
ATOM   5836 O  O   . ARG C 1 222 ? -41.230 61.933  30.953  1.00 51.61  ? 220 ARG C O   1 
ATOM   5837 C  CB  . ARG C 1 222 ? -38.728 63.913  31.754  1.00 57.90  ? 220 ARG C CB  1 
ATOM   5838 C  CG  . ARG C 1 222 ? -38.235 62.592  32.329  1.00 58.33  ? 220 ARG C CG  1 
ATOM   5839 C  CD  . ARG C 1 222 ? -37.425 62.802  33.607  1.00 68.09  ? 220 ARG C CD  1 
ATOM   5840 N  NE  . ARG C 1 222 ? -38.259 62.972  34.808  1.00 72.11  ? 220 ARG C NE  1 
ATOM   5841 C  CZ  . ARG C 1 222 ? -37.801 63.267  36.030  1.00 70.24  ? 220 ARG C CZ  1 
ATOM   5842 N  NH1 . ARG C 1 222 ? -36.502 63.446  36.254  1.00 65.52  ? 220 ARG C NH1 1 
ATOM   5843 N  NH2 . ARG C 1 222 ? -38.652 63.396  37.038  1.00 70.29  ? 220 ARG C NH2 1 
ATOM   5844 N  N   . GLU C 1 223 ? -41.904 63.983  31.607  1.00 56.70  ? 221 GLU C N   1 
ATOM   5845 C  CA  . GLU C 1 223 ? -43.091 63.477  32.279  1.00 59.12  ? 221 GLU C CA  1 
ATOM   5846 C  C   . GLU C 1 223 ? -44.345 63.467  31.393  1.00 55.33  ? 221 GLU C C   1 
ATOM   5847 O  O   . GLU C 1 223 ? -44.612 64.419  30.675  1.00 52.57  ? 221 GLU C O   1 
ATOM   5848 C  CB  . GLU C 1 223 ? -43.305 64.228  33.595  1.00 66.70  ? 221 GLU C CB  1 
ATOM   5849 C  CG  . GLU C 1 223 ? -42.443 63.693  34.739  1.00 65.06  ? 221 GLU C CG  1 
ATOM   5850 C  CD  . GLU C 1 223 ? -42.970 62.382  35.302  1.00 65.76  ? 221 GLU C CD  1 
ATOM   5851 O  OE1 . GLU C 1 223 ? -44.196 62.141  35.186  1.00 71.27  ? 221 GLU C OE1 1 
ATOM   5852 O  OE2 . GLU C 1 223 ? -42.170 61.590  35.854  1.00 62.61  ? 221 GLU C OE2 1 
ATOM   5853 N  N   . PRO C 1 224 ? -45.080 62.346  31.403  1.00 57.37  ? 222 PRO C N   1 
ATOM   5854 C  CA  . PRO C 1 224 ? -46.220 62.180  30.524  1.00 55.65  ? 222 PRO C CA  1 
ATOM   5855 C  C   . PRO C 1 224 ? -47.549 62.741  31.033  1.00 56.65  ? 222 PRO C C   1 
ATOM   5856 O  O   . PRO C 1 224 ? -47.715 62.977  32.229  1.00 61.99  ? 222 PRO C O   1 
ATOM   5857 C  CB  . PRO C 1 224 ? -46.312 60.655  30.379  1.00 57.81  ? 222 PRO C CB  1 
ATOM   5858 C  CG  . PRO C 1 224 ? -45.773 60.139  31.657  1.00 51.65  ? 222 PRO C CG  1 
ATOM   5859 C  CD  . PRO C 1 224 ? -44.642 61.057  31.975  1.00 54.90  ? 222 PRO C CD  1 
ATOM   5860 N  N   . ILE C 1 225 ? -48.476 62.919  30.091  1.00 57.43  ? 223 ILE C N   1 
ATOM   5861 C  CA  . ILE C 1 225 ? -49.869 63.298  30.321  1.00 55.17  ? 223 ILE C CA  1 
ATOM   5862 C  C   . ILE C 1 225 ? -50.780 62.076  30.566  1.00 61.00  ? 223 ILE C C   1 
ATOM   5863 O  O   . ILE C 1 225 ? -50.708 61.074  29.849  1.00 59.19  ? 223 ILE C O   1 
ATOM   5864 C  CB  . ILE C 1 225 ? -50.367 64.069  29.088  1.00 54.48  ? 223 ILE C CB  1 
ATOM   5865 C  CG1 . ILE C 1 225 ? -49.767 65.476  29.084  1.00 49.58  ? 223 ILE C CG1 1 
ATOM   5866 C  CG2 . ILE C 1 225 ? -51.892 64.130  29.030  1.00 56.74  ? 223 ILE C CG2 1 
ATOM   5867 C  CD1 . ILE C 1 225 ? -49.685 66.071  27.703  1.00 52.44  ? 223 ILE C CD1 1 
ATOM   5868 N  N   . GLN C 1 226 ? -51.642 62.144  31.572  1.00 63.05  ? 224 GLN C N   1 
ATOM   5869 C  CA  . GLN C 1 226 ? -52.577 61.048  31.786  1.00 64.69  ? 224 GLN C CA  1 
ATOM   5870 C  C   . GLN C 1 226 ? -53.942 61.349  31.179  1.00 66.34  ? 224 GLN C C   1 
ATOM   5871 O  O   . GLN C 1 226 ? -54.605 62.307  31.557  1.00 68.19  ? 224 GLN C O   1 
ATOM   5872 C  CB  . GLN C 1 226 ? -52.719 60.732  33.271  1.00 71.85  ? 224 GLN C CB  1 
ATOM   5873 C  CG  . GLN C 1 226 ? -51.571 59.948  33.898  1.00 73.02  ? 224 GLN C CG  1 
ATOM   5874 C  CD  . GLN C 1 226 ? -51.540 60.111  35.419  1.00 76.18  ? 224 GLN C CD  1 
ATOM   5875 O  OE1 . GLN C 1 226 ? -51.488 61.239  35.929  1.00 77.80  ? 224 GLN C OE1 1 
ATOM   5876 N  NE2 . GLN C 1 226 ? -51.579 58.989  36.152  1.00 66.36  ? 224 GLN C NE2 1 
ATOM   5877 N  N   . LEU C 1 227 ? -54.345 60.541  30.212  1.00 67.32  ? 225 LEU C N   1 
ATOM   5878 C  CA  . LEU C 1 227 ? -55.726 60.532  29.758  1.00 71.23  ? 225 LEU C CA  1 
ATOM   5879 C  C   . LEU C 1 227 ? -56.271 59.188  30.135  1.00 80.25  ? 225 LEU C C   1 
ATOM   5880 O  O   . LEU C 1 227 ? -55.511 58.214  30.186  1.00 82.06  ? 225 LEU C O   1 
ATOM   5881 C  CB  . LEU C 1 227 ? -55.832 60.676  28.244  1.00 65.03  ? 225 LEU C CB  1 
ATOM   5882 C  CG  . LEU C 1 227 ? -55.316 61.942  27.569  1.00 66.19  ? 225 LEU C CG  1 
ATOM   5883 C  CD1 . LEU C 1 227 ? -55.827 62.005  26.145  1.00 67.29  ? 225 LEU C CD1 1 
ATOM   5884 C  CD2 . LEU C 1 227 ? -55.726 63.180  28.341  1.00 66.98  ? 225 LEU C CD2 1 
ATOM   5885 N  N   . HIS C 1 228 ? -57.575 59.107  30.391  1.00 81.66  ? 226 HIS C N   1 
ATOM   5886 C  CA  . HIS C 1 228 ? -58.143 57.797  30.627  1.00 85.43  ? 226 HIS C CA  1 
ATOM   5887 C  C   . HIS C 1 228 ? -58.001 56.969  29.399  1.00 80.41  ? 226 HIS C C   1 
ATOM   5888 O  O   . HIS C 1 228 ? -58.059 57.489  28.274  1.00 65.99  ? 226 HIS C O   1 
ATOM   5889 C  CB  . HIS C 1 228 ? -59.595 57.815  31.095  1.00 92.99  ? 226 HIS C CB  1 
ATOM   5890 C  CG  . HIS C 1 228 ? -60.025 56.504  31.727  1.00 98.28  ? 226 HIS C CG  1 
ATOM   5891 N  ND1 . HIS C 1 228 ? -60.832 55.630  31.105  1.00 95.39  ? 226 HIS C ND1 1 
ATOM   5892 C  CD2 . HIS C 1 228 ? -59.669 55.913  32.945  1.00 101.50 ? 226 HIS C CD2 1 
ATOM   5893 C  CE1 . HIS C 1 228 ? -61.014 54.547  31.891  1.00 103.76 ? 226 HIS C CE1 1 
ATOM   5894 N  NE2 . HIS C 1 228 ? -60.300 54.724  33.017  1.00 102.58 ? 226 HIS C NE2 1 
ATOM   5895 N  N   . ARG C 1 229 ? -57.778 55.675  29.633  1.00 79.29  ? 227 ARG C N   1 
ATOM   5896 C  CA  . ARG C 1 229 ? -57.762 54.660  28.595  1.00 77.87  ? 227 ARG C CA  1 
ATOM   5897 C  C   . ARG C 1 229 ? -58.863 54.978  27.587  1.00 77.59  ? 227 ARG C C   1 
ATOM   5898 O  O   . ARG C 1 229 ? -58.695 54.804  26.374  1.00 78.94  ? 227 ARG C O   1 
ATOM   5899 C  CB  . ARG C 1 229 ? -57.947 53.284  29.253  1.00 82.45  ? 227 ARG C CB  1 
ATOM   5900 C  CG  . ARG C 1 229 ? -58.488 52.183  28.361  1.00 88.09  ? 227 ARG C CG  1 
ATOM   5901 C  CD  . ARG C 1 229 ? -58.389 50.823  29.039  1.00 90.93  ? 227 ARG C CD  1 
ATOM   5902 N  NE  . ARG C 1 229 ? -59.421 49.895  28.571  1.00 94.85  ? 227 ARG C NE  1 
ATOM   5903 C  CZ  . ARG C 1 229 ? -59.541 49.445  27.320  1.00 97.80  ? 227 ARG C CZ  1 
ATOM   5904 N  NH1 . ARG C 1 229 ? -58.699 49.837  26.369  1.00 95.41  ? 227 ARG C NH1 1 
ATOM   5905 N  NH2 . ARG C 1 229 ? -60.517 48.601  27.014  1.00 98.46  ? 227 ARG C NH2 1 
ATOM   5906 N  N   . GLU C 1 230 ? -59.971 55.490  28.118  1.00 75.51  ? 228 GLU C N   1 
ATOM   5907 C  CA  . GLU C 1 230 ? -61.138 55.880  27.342  1.00 75.13  ? 228 GLU C CA  1 
ATOM   5908 C  C   . GLU C 1 230 ? -60.936 57.214  26.621  1.00 72.10  ? 228 GLU C C   1 
ATOM   5909 O  O   . GLU C 1 230 ? -61.259 57.331  25.431  1.00 68.03  ? 228 GLU C O   1 
ATOM   5910 C  CB  . GLU C 1 230 ? -62.373 55.942  28.250  1.00 82.05  ? 228 GLU C CB  1 
ATOM   5911 C  CG  . GLU C 1 230 ? -62.800 54.598  28.835  1.00 77.09  ? 228 GLU C CG  1 
ATOM   5912 C  CD  . GLU C 1 230 ? -63.689 53.815  27.898  1.00 75.56  ? 228 GLU C CD  1 
ATOM   5913 O  OE1 . GLU C 1 230 ? -64.630 54.414  27.333  1.00 75.57  ? 228 GLU C OE1 1 
ATOM   5914 O  OE2 . GLU C 1 230 ? -63.448 52.601  27.734  1.00 76.02  ? 228 GLU C OE2 1 
ATOM   5915 N  N   . GLN C 1 231 ? -60.414 58.213  27.343  1.00 74.58  ? 229 GLN C N   1 
ATOM   5916 C  CA  . GLN C 1 231 ? -60.101 59.532  26.746  1.00 69.34  ? 229 GLN C CA  1 
ATOM   5917 C  C   . GLN C 1 231 ? -59.183 59.349  25.542  1.00 65.38  ? 229 GLN C C   1 
ATOM   5918 O  O   . GLN C 1 231 ? -59.497 59.820  24.447  1.00 70.10  ? 229 GLN C O   1 
ATOM   5919 C  CB  . GLN C 1 231 ? -59.466 60.490  27.766  1.00 67.68  ? 229 GLN C CB  1 
ATOM   5920 C  CG  . GLN C 1 231 ? -60.377 60.944  28.891  1.00 64.91  ? 229 GLN C CG  1 
ATOM   5921 C  CD  . GLN C 1 231 ? -59.846 62.166  29.620  1.00 71.83  ? 229 GLN C CD  1 
ATOM   5922 O  OE1 . GLN C 1 231 ? -58.806 62.111  30.289  1.00 71.63  ? 229 GLN C OE1 1 
ATOM   5923 N  NE2 . GLN C 1 231 ? -60.567 63.286  29.503  1.00 69.27  ? 229 GLN C NE2 1 
ATOM   5924 N  N   . ILE C 1 232 ? -58.077 58.624  25.748  1.00 63.28  ? 230 ILE C N   1 
ATOM   5925 C  CA  . ILE C 1 232 ? -57.110 58.305  24.677  1.00 62.03  ? 230 ILE C CA  1 
ATOM   5926 C  C   . ILE C 1 232 ? -57.775 57.655  23.465  1.00 58.70  ? 230 ILE C C   1 
ATOM   5927 O  O   . ILE C 1 232 ? -57.546 58.075  22.333  1.00 57.46  ? 230 ILE C O   1 
ATOM   5928 C  CB  . ILE C 1 232 ? -55.934 57.412  25.194  1.00 59.68  ? 230 ILE C CB  1 
ATOM   5929 C  CG1 . ILE C 1 232 ? -55.075 58.187  26.187  1.00 60.33  ? 230 ILE C CG1 1 
ATOM   5930 C  CG2 . ILE C 1 232 ? -55.045 56.934  24.056  1.00 57.37  ? 230 ILE C CG2 1 
ATOM   5931 C  CD1 . ILE C 1 232 ? -53.909 57.402  26.735  1.00 63.14  ? 230 ILE C CD1 1 
ATOM   5932 N  N   . LEU C 1 233 ? -58.597 56.631  23.704  1.00 61.36  ? 231 LEU C N   1 
ATOM   5933 C  CA  . LEU C 1 233 ? -59.221 55.885  22.603  1.00 60.24  ? 231 LEU C CA  1 
ATOM   5934 C  C   . LEU C 1 233 ? -60.270 56.665  21.759  1.00 60.76  ? 231 LEU C C   1 
ATOM   5935 O  O   . LEU C 1 233 ? -60.469 56.358  20.584  1.00 57.72  ? 231 LEU C O   1 
ATOM   5936 C  CB  . LEU C 1 233 ? -59.738 54.531  23.096  1.00 62.20  ? 231 LEU C CB  1 
ATOM   5937 C  CG  . LEU C 1 233 ? -58.677 53.418  23.051  1.00 61.96  ? 231 LEU C CG  1 
ATOM   5938 C  CD1 . LEU C 1 233 ? -58.767 52.471  24.244  1.00 63.10  ? 231 LEU C CD1 1 
ATOM   5939 C  CD2 . LEU C 1 233 ? -58.751 52.649  21.739  1.00 61.95  ? 231 LEU C CD2 1 
ATOM   5940 N  N   . ALA C 1 234 ? -60.913 57.678  22.343  1.00 62.65  ? 232 ALA C N   1 
ATOM   5941 C  CA  . ALA C 1 234 ? -61.809 58.584  21.582  1.00 62.34  ? 232 ALA C CA  1 
ATOM   5942 C  C   . ALA C 1 234 ? -61.215 59.099  20.257  1.00 63.06  ? 232 ALA C C   1 
ATOM   5943 O  O   . ALA C 1 234 ? -61.898 59.089  19.215  1.00 66.95  ? 232 ALA C O   1 
ATOM   5944 C  CB  . ALA C 1 234 ? -62.261 59.750  22.451  1.00 58.81  ? 232 ALA C CB  1 
ATOM   5945 N  N   . PHE C 1 235 ? -59.951 59.537  20.302  1.00 59.91  ? 233 PHE C N   1 
ATOM   5946 C  CA  . PHE C 1 235 ? -59.229 60.035  19.116  1.00 58.22  ? 233 PHE C CA  1 
ATOM   5947 C  C   . PHE C 1 235 ? -59.197 59.046  17.955  1.00 54.98  ? 233 PHE C C   1 
ATOM   5948 O  O   . PHE C 1 235 ? -59.381 59.440  16.817  1.00 53.37  ? 233 PHE C O   1 
ATOM   5949 C  CB  . PHE C 1 235 ? -57.787 60.439  19.472  1.00 57.38  ? 233 PHE C CB  1 
ATOM   5950 C  CG  . PHE C 1 235 ? -57.681 61.627  20.396  1.00 49.88  ? 233 PHE C CG  1 
ATOM   5951 C  CD1 . PHE C 1 235 ? -57.700 61.459  21.783  1.00 50.94  ? 233 PHE C CD1 1 
ATOM   5952 C  CD2 . PHE C 1 235 ? -57.528 62.899  19.884  1.00 45.48  ? 233 PHE C CD2 1 
ATOM   5953 C  CE1 . PHE C 1 235 ? -57.589 62.546  22.646  1.00 51.50  ? 233 PHE C CE1 1 
ATOM   5954 C  CE2 . PHE C 1 235 ? -57.399 63.990  20.736  1.00 52.09  ? 233 PHE C CE2 1 
ATOM   5955 C  CZ  . PHE C 1 235 ? -57.440 63.822  22.119  1.00 49.12  ? 233 PHE C CZ  1 
ATOM   5956 N  N   . SER C 1 236 ? -58.966 57.764  18.257  1.00 64.90  ? 234 SER C N   1 
ATOM   5957 C  CA  . SER C 1 236 ? -58.784 56.719  17.225  1.00 68.07  ? 234 SER C CA  1 
ATOM   5958 C  C   . SER C 1 236 ? -60.069 56.312  16.523  1.00 79.89  ? 234 SER C C   1 
ATOM   5959 O  O   . SER C 1 236 ? -60.062 55.995  15.326  1.00 89.14  ? 234 SER C O   1 
ATOM   5960 C  CB  . SER C 1 236 ? -58.070 55.479  17.781  1.00 69.67  ? 234 SER C CB  1 
ATOM   5961 O  OG  . SER C 1 236 ? -58.409 55.217  19.140  1.00 67.35  ? 234 SER C OG  1 
ATOM   5962 N  N   . GLN C 1 237 ? -61.168 56.314  17.269  1.00 81.79  ? 235 GLN C N   1 
ATOM   5963 C  CA  . GLN C 1 237 ? -62.467 55.959  16.713  1.00 82.23  ? 235 GLN C CA  1 
ATOM   5964 C  C   . GLN C 1 237 ? -63.203 57.172  16.129  1.00 83.17  ? 235 GLN C C   1 
ATOM   5965 O  O   . GLN C 1 237 ? -63.459 57.222  14.917  1.00 83.10  ? 235 GLN C O   1 
ATOM   5966 C  CB  . GLN C 1 237 ? -63.300 55.222  17.764  1.00 79.41  ? 235 GLN C CB  1 
ATOM   5967 C  CG  . GLN C 1 237 ? -62.887 53.762  17.898  1.00 80.19  ? 235 GLN C CG  1 
ATOM   5968 C  CD  . GLN C 1 237 ? -63.004 53.233  19.313  1.00 82.40  ? 235 GLN C CD  1 
ATOM   5969 O  OE1 . GLN C 1 237 ? -63.589 53.883  20.184  1.00 83.72  ? 235 GLN C OE1 1 
ATOM   5970 N  NE2 . GLN C 1 237 ? -62.445 52.043  19.553  1.00 74.50  ? 235 GLN C NE2 1 
ATOM   5971 N  N   . LYS C 1 238 ? -63.486 58.159  16.985  1.00 80.46  ? 236 LYS C N   1 
ATOM   5972 C  CA  . LYS C 1 238 ? -64.298 59.325  16.620  1.00 72.96  ? 236 LYS C CA  1 
ATOM   5973 C  C   . LYS C 1 238 ? -63.648 60.273  15.599  1.00 73.18  ? 236 LYS C C   1 
ATOM   5974 O  O   . LYS C 1 238 ? -64.170 61.366  15.354  1.00 74.41  ? 236 LYS C O   1 
ATOM   5975 C  CB  . LYS C 1 238 ? -64.760 60.079  17.880  1.00 70.91  ? 236 LYS C CB  1 
ATOM   5976 C  CG  . LYS C 1 238 ? -65.744 59.316  18.768  1.00 72.21  ? 236 LYS C CG  1 
ATOM   5977 C  CD  . LYS C 1 238 ? -67.117 59.107  18.112  1.00 68.56  ? 236 LYS C CD  1 
ATOM   5978 C  CE  . LYS C 1 238 ? -67.310 57.699  17.533  1.00 72.50  ? 236 LYS C CE  1 
ATOM   5979 N  NZ  . LYS C 1 238 ? -67.330 56.596  18.549  1.00 61.91  ? 236 LYS C NZ  1 
ATOM   5980 N  N   . LEU C 1 239 ? -62.523 59.846  15.008  1.00 71.78  ? 237 LEU C N   1 
ATOM   5981 C  CA  . LEU C 1 239 ? -61.868 60.562  13.896  1.00 65.32  ? 237 LEU C CA  1 
ATOM   5982 C  C   . LEU C 1 239 ? -61.547 59.632  12.731  1.00 61.99  ? 237 LEU C C   1 
ATOM   5983 O  O   . LEU C 1 239 ? -61.545 58.418  12.912  1.00 64.99  ? 237 LEU C O   1 
ATOM   5984 C  CB  . LEU C 1 239 ? -60.613 61.303  14.356  1.00 63.81  ? 237 LEU C CB  1 
ATOM   5985 C  CG  . LEU C 1 239 ? -60.781 62.803  14.605  1.00 67.82  ? 237 LEU C CG  1 
ATOM   5986 C  CD1 . LEU C 1 239 ? -59.417 63.441  14.810  1.00 60.87  ? 237 LEU C CD1 1 
ATOM   5987 C  CD2 . LEU C 1 239 ? -61.520 63.485  13.459  1.00 66.20  ? 237 LEU C CD2 1 
ATOM   5988 N  N   . TYR C 1 240 ? -61.278 60.202  11.553  1.00 54.83  ? 238 TYR C N   1 
ATOM   5989 C  CA  . TYR C 1 240 ? -61.226 59.438  10.308  1.00 58.94  ? 238 TYR C CA  1 
ATOM   5990 C  C   . TYR C 1 240 ? -60.320 60.084  9.276   1.00 60.61  ? 238 TYR C C   1 
ATOM   5991 O  O   . TYR C 1 240 ? -60.511 61.256  8.918   1.00 60.47  ? 238 TYR C O   1 
ATOM   5992 C  CB  . TYR C 1 240 ? -62.633 59.369  9.695   1.00 67.76  ? 238 TYR C CB  1 
ATOM   5993 C  CG  . TYR C 1 240 ? -63.341 58.037  9.715   1.00 69.58  ? 238 TYR C CG  1 
ATOM   5994 C  CD1 . TYR C 1 240 ? -64.321 57.757  10.673  1.00 74.47  ? 238 TYR C CD1 1 
ATOM   5995 C  CD2 . TYR C 1 240 ? -63.066 57.073  8.747   1.00 72.33  ? 238 TYR C CD2 1 
ATOM   5996 C  CE1 . TYR C 1 240 ? -64.990 56.540  10.675  1.00 75.60  ? 238 TYR C CE1 1 
ATOM   5997 C  CE2 . TYR C 1 240 ? -63.717 55.850  8.746   1.00 74.20  ? 238 TYR C CE2 1 
ATOM   5998 C  CZ  . TYR C 1 240 ? -64.685 55.593  9.701   1.00 78.40  ? 238 TYR C CZ  1 
ATOM   5999 O  OH  . TYR C 1 240 ? -65.341 54.384  9.673   1.00 82.58  ? 238 TYR C OH  1 
ATOM   6000 N  N   . TYR C 1 241 ? -59.376 59.311  8.748   1.00 61.48  ? 239 TYR C N   1 
ATOM   6001 C  CA  . TYR C 1 241 ? -58.431 59.817  7.727   1.00 68.45  ? 239 TYR C CA  1 
ATOM   6002 C  C   . TYR C 1 241 ? -59.073 60.244  6.409   1.00 65.06  ? 239 TYR C C   1 
ATOM   6003 O  O   . TYR C 1 241 ? -58.385 60.792  5.541   1.00 57.01  ? 239 TYR C O   1 
ATOM   6004 C  CB  . TYR C 1 241 ? -57.412 58.750  7.344   1.00 64.87  ? 239 TYR C CB  1 
ATOM   6005 C  CG  . TYR C 1 241 ? -56.167 58.613  8.182   1.00 69.58  ? 239 TYR C CG  1 
ATOM   6006 C  CD1 . TYR C 1 241 ? -55.027 59.362  7.905   1.00 71.03  ? 239 TYR C CD1 1 
ATOM   6007 C  CD2 . TYR C 1 241 ? -56.101 57.668  9.201   1.00 70.39  ? 239 TYR C CD2 1 
ATOM   6008 C  CE1 . TYR C 1 241 ? -53.866 59.189  8.640   1.00 69.02  ? 239 TYR C CE1 1 
ATOM   6009 C  CE2 . TYR C 1 241 ? -54.953 57.497  9.946   1.00 69.42  ? 239 TYR C CE2 1 
ATOM   6010 C  CZ  . TYR C 1 241 ? -53.841 58.255  9.655   1.00 70.69  ? 239 TYR C CZ  1 
ATOM   6011 O  OH  . TYR C 1 241 ? -52.714 58.072  10.396  1.00 71.52  ? 239 TYR C OH  1 
ATOM   6012 N  N   . ASP C 1 242 ? -60.360 59.948  6.233   1.00 67.45  ? 240 ASP C N   1 
ATOM   6013 C  CA  . ASP C 1 242 ? -60.995 60.112  4.921   1.00 73.88  ? 240 ASP C CA  1 
ATOM   6014 C  C   . ASP C 1 242 ? -62.449 60.605  4.988   1.00 75.11  ? 240 ASP C C   1 
ATOM   6015 O  O   . ASP C 1 242 ? -63.110 60.498  6.034   1.00 76.26  ? 240 ASP C O   1 
ATOM   6016 C  CB  . ASP C 1 242 ? -60.880 58.808  4.103   1.00 76.35  ? 240 ASP C CB  1 
ATOM   6017 C  CG  . ASP C 1 242 ? -61.876 57.732  4.543   1.00 76.73  ? 240 ASP C CG  1 
ATOM   6018 O  OD1 . ASP C 1 242 ? -62.078 57.527  5.769   1.00 71.48  ? 240 ASP C OD1 1 
ATOM   6019 O  OD2 . ASP C 1 242 ? -62.452 57.084  3.642   1.00 74.70  ? 240 ASP C OD2 1 
ATOM   6020 N  N   . LYS C 1 243 ? -62.926 61.142  3.864   1.00 71.47  ? 241 LYS C N   1 
ATOM   6021 C  CA  . LYS C 1 243 ? -64.303 61.638  3.733   1.00 74.61  ? 241 LYS C CA  1 
ATOM   6022 C  C   . LYS C 1 243 ? -65.298 60.484  3.611   1.00 72.63  ? 241 LYS C C   1 
ATOM   6023 O  O   . LYS C 1 243 ? -66.275 60.406  4.363   1.00 70.87  ? 241 LYS C O   1 
ATOM   6024 C  CB  . LYS C 1 243 ? -64.429 62.574  2.522   1.00 76.83  ? 241 LYS C CB  1 
ATOM   6025 C  CG  . LYS C 1 243 ? -63.452 63.743  2.519   1.00 76.48  ? 241 LYS C CG  1 
ATOM   6026 C  CD  . LYS C 1 243 ? -63.192 64.233  1.106   1.00 77.25  ? 241 LYS C CD  1 
ATOM   6027 C  CE  . LYS C 1 243 ? -62.719 65.676  1.092   1.00 77.75  ? 241 LYS C CE  1 
ATOM   6028 N  NZ  . LYS C 1 243 ? -62.624 66.194  -0.301  1.00 80.81  ? 241 LYS C NZ  1 
ATOM   6029 N  N   . GLU C 1 244 ? -65.020 59.585  2.668   1.00 73.13  ? 242 GLU C N   1 
ATOM   6030 C  CA  . GLU C 1 244 ? -65.834 58.386  2.421   1.00 73.79  ? 242 GLU C CA  1 
ATOM   6031 C  C   . GLU C 1 244 ? -66.067 57.494  3.659   1.00 76.24  ? 242 GLU C C   1 
ATOM   6032 O  O   . GLU C 1 244 ? -66.993 56.681  3.675   1.00 74.33  ? 242 GLU C O   1 
ATOM   6033 C  CB  . GLU C 1 244 ? -65.176 57.484  1.364   1.00 64.61  ? 242 GLU C CB  1 
ATOM   6034 C  CG  . GLU C 1 244 ? -64.694 58.172  0.088   1.00 64.12  ? 242 GLU C CG  1 
ATOM   6035 C  CD  . GLU C 1 244 ? -63.310 58.802  0.230   1.00 66.71  ? 242 GLU C CD  1 
ATOM   6036 O  OE1 . GLU C 1 244 ? -62.299 58.067  0.249   1.00 67.47  ? 242 GLU C OE1 1 
ATOM   6037 O  OE2 . GLU C 1 244 ? -63.225 60.042  0.313   1.00 64.18  ? 242 GLU C OE2 1 
ATOM   6038 N  N   . GLN C 1 245 ? -65.236 57.676  4.688   1.00 76.02  ? 243 GLN C N   1 
ATOM   6039 C  CA  . GLN C 1 245 ? -65.182 56.789  5.857   1.00 76.26  ? 243 GLN C CA  1 
ATOM   6040 C  C   . GLN C 1 245 ? -64.718 55.349  5.553   1.00 78.57  ? 243 GLN C C   1 
ATOM   6041 O  O   . GLN C 1 245 ? -65.444 54.374  5.774   1.00 75.90  ? 243 GLN C O   1 
ATOM   6042 C  CB  . GLN C 1 245 ? -66.520 56.850  6.617   1.00 74.42  ? 243 GLN C CB  1 
ATOM   6043 C  CG  . GLN C 1 245 ? -66.471 57.630  7.930   1.00 70.09  ? 243 GLN C CG  1 
ATOM   6044 C  CD  . GLN C 1 245 ? -66.761 59.115  7.814   1.00 71.76  ? 243 GLN C CD  1 
ATOM   6045 O  OE1 . GLN C 1 245 ? -67.405 59.696  8.693   1.00 64.46  ? 243 GLN C OE1 1 
ATOM   6046 N  NE2 . GLN C 1 245 ? -66.291 59.741  6.741   1.00 77.31  ? 243 GLN C NE2 1 
ATOM   6047 N  N   . THR C 1 246 ? -63.488 55.240  5.044   1.00 84.92  ? 244 THR C N   1 
ATOM   6048 C  CA  . THR C 1 246 ? -62.840 53.949  4.750   1.00 87.59  ? 244 THR C CA  1 
ATOM   6049 C  C   . THR C 1 246 ? -61.551 53.684  5.562   1.00 90.36  ? 244 THR C C   1 
ATOM   6050 O  O   . THR C 1 246 ? -60.987 52.589  5.476   1.00 97.02  ? 244 THR C O   1 
ATOM   6051 C  CB  . THR C 1 246 ? -62.551 53.751  3.233   1.00 90.05  ? 244 THR C CB  1 
ATOM   6052 O  OG1 . THR C 1 246 ? -61.908 54.914  2.689   1.00 91.45  ? 244 THR C OG1 1 
ATOM   6053 C  CG2 . THR C 1 246 ? -63.841 53.469  2.456   1.00 94.30  ? 244 THR C CG2 1 
ATOM   6054 N  N   . VAL C 1 247 ? -61.088 54.671  6.339   1.00 82.75  ? 245 VAL C N   1 
ATOM   6055 C  CA  . VAL C 1 247 ? -59.885 54.517  7.177   1.00 74.19  ? 245 VAL C CA  1 
ATOM   6056 C  C   . VAL C 1 247 ? -59.974 55.328  8.477   1.00 72.02  ? 245 VAL C C   1 
ATOM   6057 O  O   . VAL C 1 247 ? -59.894 56.554  8.443   1.00 75.78  ? 245 VAL C O   1 
ATOM   6058 C  CB  . VAL C 1 247 ? -58.587 54.940  6.441   1.00 75.15  ? 245 VAL C CB  1 
ATOM   6059 C  CG1 . VAL C 1 247 ? -57.437 54.032  6.845   1.00 80.18  ? 245 VAL C CG1 1 
ATOM   6060 C  CG2 . VAL C 1 247 ? -58.747 54.936  4.928   1.00 72.75  ? 245 VAL C CG2 1 
ATOM   6061 N  N   . SER C 1 248 ? -60.143 54.648  9.614   1.00 64.96  ? 246 SER C N   1 
ATOM   6062 C  CA  . SER C 1 248 ? -60.107 55.286  10.943  1.00 66.74  ? 246 SER C CA  1 
ATOM   6063 C  C   . SER C 1 248 ? -58.738 55.913  11.247  1.00 63.71  ? 246 SER C C   1 
ATOM   6064 O  O   . SER C 1 248 ? -57.721 55.404  10.770  1.00 58.94  ? 246 SER C O   1 
ATOM   6065 C  CB  . SER C 1 248 ? -60.460 54.275  12.040  1.00 67.36  ? 246 SER C CB  1 
ATOM   6066 O  OG  . SER C 1 248 ? -61.838 54.326  12.377  1.00 66.79  ? 246 SER C OG  1 
ATOM   6067 N  N   . MET C 1 249 ? -58.728 57.003  12.035  1.00 61.41  ? 247 MET C N   1 
ATOM   6068 C  CA  . MET C 1 249 ? -57.514 57.819  12.307  1.00 52.15  ? 247 MET C CA  1 
ATOM   6069 C  C   . MET C 1 249 ? -56.697 57.248  13.454  1.00 50.05  ? 247 MET C C   1 
ATOM   6070 O  O   . MET C 1 249 ? -57.178 57.131  14.583  1.00 50.16  ? 247 MET C O   1 
ATOM   6071 C  CB  . MET C 1 249 ? -57.849 59.304  12.564  1.00 48.07  ? 247 MET C CB  1 
ATOM   6072 C  CG  . MET C 1 249 ? -56.677 60.251  12.318  1.00 51.56  ? 247 MET C CG  1 
ATOM   6073 S  SD  . MET C 1 249 ? -56.960 62.043  12.572  1.00 54.39  ? 247 MET C SD  1 
ATOM   6074 C  CE  . MET C 1 249 ? -56.938 62.630  10.887  1.00 52.66  ? 247 MET C CE  1 
ATOM   6075 N  N   . LYS C 1 250 ? -55.453 56.888  13.146  1.00 51.55  ? 248 LYS C N   1 
ATOM   6076 C  CA  . LYS C 1 250 ? -54.526 56.250  14.096  1.00 43.67  ? 248 LYS C CA  1 
ATOM   6077 C  C   . LYS C 1 250 ? -53.205 56.004  13.360  1.00 40.81  ? 248 LYS C C   1 
ATOM   6078 O  O   . LYS C 1 250 ? -53.161 56.081  12.128  1.00 39.48  ? 248 LYS C O   1 
ATOM   6079 C  CB  . LYS C 1 250 ? -55.118 54.935  14.640  1.00 49.18  ? 248 LYS C CB  1 
ATOM   6080 C  CG  . LYS C 1 250 ? -55.278 53.804  13.602  1.00 50.13  ? 248 LYS C CG  1 
ATOM   6081 C  CD  . LYS C 1 250 ? -55.687 52.519  14.298  1.00 50.26  ? 248 LYS C CD  1 
ATOM   6082 C  CE  . LYS C 1 250 ? -55.607 51.299  13.403  1.00 52.25  ? 248 LYS C CE  1 
ATOM   6083 N  NZ  . LYS C 1 250 ? -55.334 50.106  14.272  1.00 49.92  ? 248 LYS C NZ  1 
ATOM   6084 N  N   . ASP C 1 251 ? -52.136 55.687  14.094  1.00 39.32  ? 249 ASP C N   1 
ATOM   6085 C  CA  . ASP C 1 251 ? -50.784 55.557  13.491  1.00 40.10  ? 249 ASP C CA  1 
ATOM   6086 C  C   . ASP C 1 251 ? -50.364 56.653  12.527  1.00 36.23  ? 249 ASP C C   1 
ATOM   6087 O  O   . ASP C 1 251 ? -49.597 56.426  11.576  1.00 35.06  ? 249 ASP C O   1 
ATOM   6088 C  CB  . ASP C 1 251 ? -50.580 54.194  12.839  1.00 40.21  ? 249 ASP C CB  1 
ATOM   6089 C  CG  . ASP C 1 251 ? -51.074 53.119  13.679  1.00 38.65  ? 249 ASP C CG  1 
ATOM   6090 O  OD1 . ASP C 1 251 ? -50.435 52.850  14.715  1.00 39.15  ? 249 ASP C OD1 1 
ATOM   6091 O  OD2 . ASP C 1 251 ? -52.134 52.577  13.321  1.00 45.26  ? 249 ASP C OD2 1 
ATOM   6092 N  N   . ASN C 1 252 ? -50.807 57.867  12.805  1.00 40.21  ? 250 ASN C N   1 
ATOM   6093 C  CA  . ASN C 1 252 ? -50.259 59.021  12.114  1.00 38.43  ? 250 ASN C CA  1 
ATOM   6094 C  C   . ASN C 1 252 ? -48.897 59.368  12.712  1.00 40.78  ? 250 ASN C C   1 
ATOM   6095 O  O   . ASN C 1 252 ? -48.764 60.390  13.395  1.00 38.70  ? 250 ASN C O   1 
ATOM   6096 C  CB  . ASN C 1 252 ? -51.213 60.203  12.266  1.00 39.71  ? 250 ASN C CB  1 
ATOM   6097 C  CG  . ASN C 1 252 ? -51.610 60.448  13.715  1.00 42.36  ? 250 ASN C CG  1 
ATOM   6098 O  OD1 . ASN C 1 252 ? -51.272 59.669  14.607  1.00 41.29  ? 250 ASN C OD1 1 
ATOM   6099 N  ND2 . ASN C 1 252 ? -52.323 61.543  13.957  1.00 43.21  ? 250 ASN C ND2 1 
ATOM   6100 N  N   . VAL C 1 253 ? -47.895 58.514  12.482  1.00 40.08  ? 251 VAL C N   1 
ATOM   6101 C  CA  . VAL C 1 253 ? -46.542 58.749  13.000  1.00 43.13  ? 251 VAL C CA  1 
ATOM   6102 C  C   . VAL C 1 253 ? -45.435 58.466  11.966  1.00 45.49  ? 251 VAL C C   1 
ATOM   6103 O  O   . VAL C 1 253 ? -45.543 57.533  11.161  1.00 43.36  ? 251 VAL C O   1 
ATOM   6104 C  CB  . VAL C 1 253 ? -46.233 57.979  14.323  1.00 42.70  ? 251 VAL C CB  1 
ATOM   6105 C  CG1 . VAL C 1 253 ? -47.484 57.516  15.062  1.00 35.07  ? 251 VAL C CG1 1 
ATOM   6106 C  CG2 . VAL C 1 253 ? -45.324 56.815  14.062  1.00 42.57  ? 251 VAL C CG2 1 
ATOM   6107 N  N   . ARG C 1 254 ? -44.370 59.268  11.999  1.00 41.89  ? 252 ARG C N   1 
ATOM   6108 C  CA  . ARG C 1 254 ? -43.179 58.981  11.201  1.00 39.74  ? 252 ARG C CA  1 
ATOM   6109 C  C   . ARG C 1 254 ? -42.325 57.987  11.966  1.00 41.63  ? 252 ARG C C   1 
ATOM   6110 O  O   . ARG C 1 254 ? -42.087 58.185  13.169  1.00 46.33  ? 252 ARG C O   1 
ATOM   6111 C  CB  . ARG C 1 254 ? -42.386 60.259  10.922  1.00 37.99  ? 252 ARG C CB  1 
ATOM   6112 C  CG  . ARG C 1 254 ? -41.435 60.182  9.728   1.00 38.29  ? 252 ARG C CG  1 
ATOM   6113 C  CD  . ARG C 1 254 ? -40.525 61.401  9.643   1.00 37.73  ? 252 ARG C CD  1 
ATOM   6114 N  NE  . ARG C 1 254 ? -39.693 61.423  8.429   1.00 41.79  ? 252 ARG C NE  1 
ATOM   6115 C  CZ  . ARG C 1 254 ? -38.757 62.342  8.166   1.00 43.21  ? 252 ARG C CZ  1 
ATOM   6116 N  NH1 . ARG C 1 254 ? -38.541 63.342  9.025   1.00 43.07  ? 252 ARG C NH1 1 
ATOM   6117 N  NH2 . ARG C 1 254 ? -38.045 62.277  7.035   1.00 44.35  ? 252 ARG C NH2 1 
ATOM   6118 N  N   . PRO C 1 255 ? -41.863 56.907  11.299  1.00 40.97  ? 253 PRO C N   1 
ATOM   6119 C  CA  . PRO C 1 255 ? -40.875 55.987  11.901  1.00 41.42  ? 253 PRO C CA  1 
ATOM   6120 C  C   . PRO C 1 255 ? -39.661 56.729  12.472  1.00 44.20  ? 253 PRO C C   1 
ATOM   6121 O  O   . PRO C 1 255 ? -39.498 57.913  12.226  1.00 45.63  ? 253 PRO C O   1 
ATOM   6122 C  CB  . PRO C 1 255 ? -40.454 55.094  10.718  1.00 40.82  ? 253 PRO C CB  1 
ATOM   6123 C  CG  . PRO C 1 255 ? -40.978 55.779  9.481   1.00 43.37  ? 253 PRO C CG  1 
ATOM   6124 C  CD  . PRO C 1 255 ? -42.235 56.464  9.945   1.00 43.36  ? 253 PRO C CD  1 
ATOM   6125 N  N   . LEU C 1 256 ? -38.808 56.037  13.216  1.00 43.74  ? 254 LEU C N   1 
ATOM   6126 C  CA  . LEU C 1 256 ? -37.728 56.696  13.933  1.00 42.59  ? 254 LEU C CA  1 
ATOM   6127 C  C   . LEU C 1 256 ? -36.567 57.031  13.006  1.00 48.14  ? 254 LEU C C   1 
ATOM   6128 O  O   . LEU C 1 256 ? -36.263 56.278  12.073  1.00 47.69  ? 254 LEU C O   1 
ATOM   6129 C  CB  . LEU C 1 256 ? -37.230 55.807  15.070  1.00 39.49  ? 254 LEU C CB  1 
ATOM   6130 C  CG  . LEU C 1 256 ? -38.116 55.713  16.304  1.00 35.42  ? 254 LEU C CG  1 
ATOM   6131 C  CD1 . LEU C 1 256 ? -37.739 54.532  17.207  1.00 34.72  ? 254 LEU C CD1 1 
ATOM   6132 C  CD2 . LEU C 1 256 ? -38.098 57.022  17.070  1.00 37.72  ? 254 LEU C CD2 1 
ATOM   6133 N  N   . GLN C 1 257 ? -35.925 58.163  13.274  1.00 45.82  ? 255 GLN C N   1 
ATOM   6134 C  CA  . GLN C 1 257 ? -34.725 58.568  12.544  1.00 52.17  ? 255 GLN C CA  1 
ATOM   6135 C  C   . GLN C 1 257 ? -33.502 58.394  13.449  1.00 47.64  ? 255 GLN C C   1 
ATOM   6136 O  O   . GLN C 1 257 ? -33.635 58.326  14.669  1.00 48.89  ? 255 GLN C O   1 
ATOM   6137 C  CB  . GLN C 1 257 ? -34.859 60.026  12.047  1.00 55.13  ? 255 GLN C CB  1 
ATOM   6138 C  CG  . GLN C 1 257 ? -36.124 60.325  11.238  1.00 52.98  ? 255 GLN C CG  1 
ATOM   6139 C  CD  . GLN C 1 257 ? -36.232 59.497  9.960   1.00 57.41  ? 255 GLN C CD  1 
ATOM   6140 O  OE1 . GLN C 1 257 ? -35.395 59.601  9.058   1.00 55.61  ? 255 GLN C OE1 1 
ATOM   6141 N  NE2 . GLN C 1 257 ? -37.274 58.672  9.876   1.00 54.84  ? 255 GLN C NE2 1 
ATOM   6142 N  N   . GLN C 1 258 ? -32.312 58.313  12.867  1.00 51.40  ? 256 GLN C N   1 
ATOM   6143 C  CA  . GLN C 1 258 ? -31.105 58.146  13.683  1.00 50.53  ? 256 GLN C CA  1 
ATOM   6144 C  C   . GLN C 1 258 ? -30.495 59.481  14.030  1.00 51.04  ? 256 GLN C C   1 
ATOM   6145 O  O   . GLN C 1 258 ? -30.593 60.431  13.254  1.00 52.52  ? 256 GLN C O   1 
ATOM   6146 C  CB  . GLN C 1 258 ? -30.070 57.243  13.010  1.00 56.90  ? 256 GLN C CB  1 
ATOM   6147 C  CG  . GLN C 1 258 ? -29.936 57.404  11.506  1.00 58.08  ? 256 GLN C CG  1 
ATOM   6148 C  CD  . GLN C 1 258 ? -30.787 56.416  10.737  1.00 59.82  ? 256 GLN C CD  1 
ATOM   6149 O  OE1 . GLN C 1 258 ? -30.650 56.291  9.525   1.00 60.99  ? 256 GLN C OE1 1 
ATOM   6150 N  NE2 . GLN C 1 258 ? -31.674 55.709  11.437  1.00 56.90  ? 256 GLN C NE2 1 
ATOM   6151 N  N   . LEU C 1 259 ? -29.876 59.545  15.204  1.00 50.73  ? 257 LEU C N   1 
ATOM   6152 C  CA  . LEU C 1 259 ? -29.319 60.782  15.736  1.00 54.87  ? 257 LEU C CA  1 
ATOM   6153 C  C   . LEU C 1 259 ? -28.159 61.250  14.866  1.00 62.02  ? 257 LEU C C   1 
ATOM   6154 O  O   . LEU C 1 259 ? -28.088 62.432  14.502  1.00 59.05  ? 257 LEU C O   1 
ATOM   6155 C  CB  . LEU C 1 259 ? -28.877 60.588  17.188  1.00 51.91  ? 257 LEU C CB  1 
ATOM   6156 C  CG  . LEU C 1 259 ? -28.522 61.792  18.060  1.00 49.76  ? 257 LEU C CG  1 
ATOM   6157 C  CD1 . LEU C 1 259 ? -29.718 62.706  18.346  1.00 44.79  ? 257 LEU C CD1 1 
ATOM   6158 C  CD2 . LEU C 1 259 ? -27.892 61.284  19.348  1.00 50.59  ? 257 LEU C CD2 1 
ATOM   6159 N  N   . GLY C 1 260 ? -27.292 60.301  14.499  1.00 65.29  ? 258 GLY C N   1 
ATOM   6160 C  CA  . GLY C 1 260 ? -26.135 60.571  13.660  1.00 70.86  ? 258 GLY C CA  1 
ATOM   6161 C  C   . GLY C 1 260 ? -25.235 61.596  14.317  1.00 75.36  ? 258 GLY C C   1 
ATOM   6162 O  O   . GLY C 1 260 ? -24.509 61.291  15.269  1.00 77.81  ? 258 GLY C O   1 
ATOM   6163 N  N   . GLN C 1 261 ? -25.325 62.826  13.828  1.00 83.12  ? 259 GLN C N   1 
ATOM   6164 C  CA  . GLN C 1 261 ? -24.428 63.901  14.243  1.00 85.54  ? 259 GLN C CA  1 
ATOM   6165 C  C   . GLN C 1 261 ? -24.667 64.455  15.664  1.00 82.32  ? 259 GLN C C   1 
ATOM   6166 O  O   . GLN C 1 261 ? -23.715 64.616  16.433  1.00 83.00  ? 259 GLN C O   1 
ATOM   6167 C  CB  . GLN C 1 261 ? -24.475 65.031  13.210  1.00 85.05  ? 259 GLN C CB  1 
ATOM   6168 C  CG  . GLN C 1 261 ? -23.149 65.747  13.015  1.00 88.83  ? 259 GLN C CG  1 
ATOM   6169 C  CD  . GLN C 1 261 ? -22.195 64.999  12.099  1.00 86.48  ? 259 GLN C CD  1 
ATOM   6170 O  OE1 . GLN C 1 261 ? -22.102 63.765  12.133  1.00 84.51  ? 259 GLN C OE1 1 
ATOM   6171 N  NE2 . GLN C 1 261 ? -21.475 65.749  11.271  1.00 80.03  ? 259 GLN C NE2 1 
ATOM   6172 N  N   . ARG C 1 262 ? -25.928 64.717  16.010  1.00 70.99  ? 260 ARG C N   1 
ATOM   6173 C  CA  . ARG C 1 262 ? -26.263 65.494  17.206  1.00 68.09  ? 260 ARG C CA  1 
ATOM   6174 C  C   . ARG C 1 262 ? -26.034 64.741  18.496  1.00 63.53  ? 260 ARG C C   1 
ATOM   6175 O  O   . ARG C 1 262 ? -25.620 63.589  18.507  1.00 66.76  ? 260 ARG C O   1 
ATOM   6176 C  CB  . ARG C 1 262 ? -27.732 65.940  17.171  1.00 71.67  ? 260 ARG C CB  1 
ATOM   6177 C  CG  . ARG C 1 262 ? -28.150 66.660  15.903  1.00 81.09  ? 260 ARG C CG  1 
ATOM   6178 C  CD  . ARG C 1 262 ? -29.602 66.362  15.559  1.00 88.41  ? 260 ARG C CD  1 
ATOM   6179 N  NE  . ARG C 1 262 ? -29.822 65.029  14.983  1.00 91.85  ? 260 ARG C NE  1 
ATOM   6180 C  CZ  . ARG C 1 262 ? -30.976 64.613  14.451  1.00 90.05  ? 260 ARG C CZ  1 
ATOM   6181 N  NH1 . ARG C 1 262 ? -32.031 65.421  14.402  1.00 87.90  ? 260 ARG C NH1 1 
ATOM   6182 N  NH2 . ARG C 1 262 ? -31.076 63.388  13.955  1.00 84.95  ? 260 ARG C NH2 1 
ATOM   6183 N  N   . THR C 1 263 ? -26.306 65.424  19.592  1.00 62.31  ? 261 THR C N   1 
ATOM   6184 C  CA  . THR C 1 263 ? -26.503 64.789  20.881  1.00 60.39  ? 261 THR C CA  1 
ATOM   6185 C  C   . THR C 1 263 ? -27.731 65.445  21.480  1.00 54.74  ? 261 THR C C   1 
ATOM   6186 O  O   . THR C 1 263 ? -28.282 66.403  20.930  1.00 51.60  ? 261 THR C O   1 
ATOM   6187 C  CB  . THR C 1 263 ? -25.295 64.984  21.835  1.00 63.26  ? 261 THR C CB  1 
ATOM   6188 O  OG1 . THR C 1 263 ? -24.901 66.362  21.842  1.00 61.80  ? 261 THR C OG1 1 
ATOM   6189 C  CG2 . THR C 1 263 ? -24.105 64.130  21.401  1.00 66.66  ? 261 THR C CG2 1 
ATOM   6190 N  N   . VAL C 1 264 ? -28.148 64.936  22.625  1.00 52.93  ? 262 VAL C N   1 
ATOM   6191 C  CA  . VAL C 1 264 ? -29.313 65.454  23.273  1.00 48.35  ? 262 VAL C CA  1 
ATOM   6192 C  C   . VAL C 1 264 ? -28.897 65.946  24.642  1.00 47.18  ? 262 VAL C C   1 
ATOM   6193 O  O   . VAL C 1 264 ? -28.032 65.342  25.266  1.00 44.79  ? 262 VAL C O   1 
ATOM   6194 C  CB  . VAL C 1 264 ? -30.399 64.359  23.376  1.00 47.94  ? 262 VAL C CB  1 
ATOM   6195 C  CG1 . VAL C 1 264 ? -31.666 64.927  23.994  1.00 43.29  ? 262 VAL C CG1 1 
ATOM   6196 C  CG2 . VAL C 1 264 ? -30.694 63.774  21.992  1.00 43.29  ? 262 VAL C CG2 1 
ATOM   6197 N  N   . ILE C 1 265 ? -29.484 67.060  25.077  1.00 47.07  ? 263 ILE C N   1 
ATOM   6198 C  CA  . ILE C 1 265 ? -29.262 67.601  26.430  1.00 46.50  ? 263 ILE C CA  1 
ATOM   6199 C  C   . ILE C 1 265 ? -30.558 67.580  27.219  1.00 44.89  ? 263 ILE C C   1 
ATOM   6200 O  O   . ILE C 1 265 ? -31.642 67.426  26.644  1.00 45.15  ? 263 ILE C O   1 
ATOM   6201 C  CB  . ILE C 1 265 ? -28.698 69.059  26.428  1.00 50.95  ? 263 ILE C CB  1 
ATOM   6202 C  CG1 . ILE C 1 265 ? -29.244 69.896  25.244  1.00 49.97  ? 263 ILE C CG1 1 
ATOM   6203 C  CG2 . ILE C 1 265 ? -27.171 69.036  26.482  1.00 50.82  ? 263 ILE C CG2 1 
ATOM   6204 C  CD1 . ILE C 1 265 ? -28.619 71.284  25.062  1.00 46.53  ? 263 ILE C CD1 1 
ATOM   6205 N  N   . LYS C 1 266 ? -30.455 67.751  28.528  1.00 44.31  ? 264 LYS C N   1 
ATOM   6206 C  CA  . LYS C 1 266 ? -31.636 67.766  29.378  1.00 47.48  ? 264 LYS C CA  1 
ATOM   6207 C  C   . LYS C 1 266 ? -31.498 68.745  30.536  1.00 44.56  ? 264 LYS C C   1 
ATOM   6208 O  O   . LYS C 1 266 ? -30.437 68.908  31.099  1.00 45.78  ? 264 LYS C O   1 
ATOM   6209 C  CB  . LYS C 1 266 ? -31.947 66.365  29.935  1.00 46.62  ? 264 LYS C CB  1 
ATOM   6210 C  CG  . LYS C 1 266 ? -30.995 65.902  31.024  1.00 51.07  ? 264 LYS C CG  1 
ATOM   6211 C  CD  . LYS C 1 266 ? -31.699 65.033  32.054  1.00 56.16  ? 264 LYS C CD  1 
ATOM   6212 C  CE  . LYS C 1 266 ? -30.744 63.957  32.560  1.00 59.95  ? 264 LYS C CE  1 
ATOM   6213 N  NZ  . LYS C 1 266 ? -30.362 62.991  31.477  1.00 55.75  ? 264 LYS C NZ  1 
ATOM   6214 N  N   . SER C 1 267 ? -32.599 69.371  30.900  1.00 45.37  ? 265 SER C N   1 
ATOM   6215 C  CA  . SER C 1 267 ? -32.653 70.129  32.137  1.00 51.23  ? 265 SER C CA  1 
ATOM   6216 C  C   . SER C 1 267 ? -32.569 69.142  33.311  1.00 54.95  ? 265 SER C C   1 
ATOM   6217 O  O   . SER C 1 267 ? -33.164 68.054  33.291  1.00 68.42  ? 265 SER C O   1 
ATOM   6218 C  CB  . SER C 1 267 ? -33.966 70.864  32.205  1.00 45.33  ? 265 SER C CB  1 
ATOM   6219 O  OG  . SER C 1 267 ? -34.974 69.921  32.505  1.00 49.61  ? 265 SER C OG  1 
ATOM   6220 O  OXT . SER C 1 267 ? -31.911 69.405  34.312  1.00 56.40  ? 265 SER C OXT 1 
ATOM   6221 N  N   . HIS D 1 5   ? -36.989 100.065 16.925  1.00 99.77  ? 5   HIS D N   1 
ATOM   6222 C  CA  . HIS D 1 5   ? -38.287 99.743  16.263  1.00 99.28  ? 5   HIS D CA  1 
ATOM   6223 C  C   . HIS D 1 5   ? -38.609 100.702 15.157  1.00 93.91  ? 5   HIS D C   1 
ATOM   6224 O  O   . HIS D 1 5   ? -38.074 101.817 15.108  1.00 90.67  ? 5   HIS D O   1 
ATOM   6225 C  CB  . HIS D 1 5   ? -39.423 99.722  17.280  1.00 104.27 ? 5   HIS D CB  1 
ATOM   6226 C  CG  . HIS D 1 5   ? -39.598 98.390  17.968  1.00 116.24 ? 5   HIS D CG  1 
ATOM   6227 N  ND1 . HIS D 1 5   ? -40.228 97.351  17.385  1.00 120.31 ? 5   HIS D ND1 1 
ATOM   6228 C  CD2 . HIS D 1 5   ? -39.206 97.954  19.233  1.00 117.64 ? 5   HIS D CD2 1 
ATOM   6229 C  CE1 . HIS D 1 5   ? -40.237 96.300  18.229  1.00 120.97 ? 5   HIS D CE1 1 
ATOM   6230 N  NE2 . HIS D 1 5   ? -39.611 96.670  19.360  1.00 122.18 ? 5   HIS D NE2 1 
ATOM   6231 N  N   . TRP D 1 6   ? -39.492 100.267 14.259  1.00 85.84  ? 6   TRP D N   1 
ATOM   6232 C  CA  . TRP D 1 6   ? -39.941 101.095 13.139  1.00 75.43  ? 6   TRP D CA  1 
ATOM   6233 C  C   . TRP D 1 6   ? -41.204 101.828 13.489  1.00 70.64  ? 6   TRP D C   1 
ATOM   6234 O  O   . TRP D 1 6   ? -42.024 101.336 14.272  1.00 68.07  ? 6   TRP D O   1 
ATOM   6235 C  CB  . TRP D 1 6   ? -40.136 100.256 11.870  1.00 69.83  ? 6   TRP D CB  1 
ATOM   6236 C  CG  . TRP D 1 6   ? -41.219 99.207  11.981  1.00 64.17  ? 6   TRP D CG  1 
ATOM   6237 C  CD1 . TRP D 1 6   ? -41.064 97.852  12.269  1.00 59.08  ? 6   TRP D CD1 1 
ATOM   6238 C  CD2 . TRP D 1 6   ? -42.663 99.394  11.807  1.00 58.31  ? 6   TRP D CD2 1 
ATOM   6239 N  NE1 . TRP D 1 6   ? -42.270 97.218  12.286  1.00 58.25  ? 6   TRP D NE1 1 
ATOM   6240 C  CE2 . TRP D 1 6   ? -43.272 98.084  12.022  1.00 55.81  ? 6   TRP D CE2 1 
ATOM   6241 C  CE3 . TRP D 1 6   ? -43.480 100.478 11.517  1.00 58.10  ? 6   TRP D CE3 1 
ATOM   6242 C  CZ2 . TRP D 1 6   ? -44.639 97.888  11.941  1.00 58.44  ? 6   TRP D CZ2 1 
ATOM   6243 C  CZ3 . TRP D 1 6   ? -44.858 100.274 11.441  1.00 58.76  ? 6   TRP D CZ3 1 
ATOM   6244 C  CH2 . TRP D 1 6   ? -45.425 99.007  11.645  1.00 58.96  ? 6   TRP D CH2 1 
ATOM   6245 N  N   . CYS D 1 7   ? -41.375 103.004 12.891  1.00 66.54  ? 7   CYS D N   1 
ATOM   6246 C  CA  . CYS D 1 7   ? -42.521 103.854 13.170  1.00 67.90  ? 7   CYS D CA  1 
ATOM   6247 C  C   . CYS D 1 7   ? -43.155 104.459 11.912  1.00 64.95  ? 7   CYS D C   1 
ATOM   6248 O  O   . CYS D 1 7   ? -42.483 104.666 10.900  1.00 69.86  ? 7   CYS D O   1 
ATOM   6249 C  CB  . CYS D 1 7   ? -42.111 104.970 14.135  1.00 65.84  ? 7   CYS D CB  1 
ATOM   6250 S  SG  . CYS D 1 7   ? -40.817 106.039 13.459  1.00 84.72  ? 7   CYS D SG  1 
ATOM   6251 N  N   . TYR D 1 8   ? -44.455 104.729 11.998  1.00 57.98  ? 8   TYR D N   1 
ATOM   6252 C  CA  . TYR D 1 8   ? -45.146 105.617 11.076  1.00 59.08  ? 8   TYR D CA  1 
ATOM   6253 C  C   . TYR D 1 8   ? -44.646 107.070 11.290  1.00 65.36  ? 8   TYR D C   1 
ATOM   6254 O  O   . TYR D 1 8   ? -43.944 107.328 12.272  1.00 68.89  ? 8   TYR D O   1 
ATOM   6255 C  CB  . TYR D 1 8   ? -46.658 105.480 11.298  1.00 49.74  ? 8   TYR D CB  1 
ATOM   6256 C  CG  . TYR D 1 8   ? -47.183 104.166 10.763  1.00 50.76  ? 8   TYR D CG  1 
ATOM   6257 C  CD1 . TYR D 1 8   ? -47.034 103.844 9.403   1.00 47.74  ? 8   TYR D CD1 1 
ATOM   6258 C  CD2 . TYR D 1 8   ? -47.808 103.221 11.607  1.00 46.41  ? 8   TYR D CD2 1 
ATOM   6259 C  CE1 . TYR D 1 8   ? -47.481 102.629 8.891   1.00 51.44  ? 8   TYR D CE1 1 
ATOM   6260 C  CE2 . TYR D 1 8   ? -48.270 101.994 11.100  1.00 50.81  ? 8   TYR D CE2 1 
ATOM   6261 C  CZ  . TYR D 1 8   ? -48.101 101.704 9.739   1.00 48.68  ? 8   TYR D CZ  1 
ATOM   6262 O  OH  . TYR D 1 8   ? -48.552 100.524 9.200   1.00 50.69  ? 8   TYR D OH  1 
ATOM   6263 N  N   . GLU D 1 9   ? -44.975 108.008 10.391  1.00 65.23  ? 9   GLU D N   1 
ATOM   6264 C  CA  . GLU D 1 9   ? -44.448 109.397 10.517  1.00 66.54  ? 9   GLU D CA  1 
ATOM   6265 C  C   . GLU D 1 9   ? -44.983 110.073 11.766  1.00 64.27  ? 9   GLU D C   1 
ATOM   6266 O  O   . GLU D 1 9   ? -44.292 110.875 12.382  1.00 70.30  ? 9   GLU D O   1 
ATOM   6267 C  CB  . GLU D 1 9   ? -44.754 110.293 9.297   1.00 66.68  ? 9   GLU D CB  1 
ATOM   6268 C  CG  . GLU D 1 9   ? -44.460 109.720 7.904   1.00 73.60  ? 9   GLU D CG  1 
ATOM   6269 C  CD  . GLU D 1 9   ? -42.983 109.597 7.552   1.00 79.46  ? 9   GLU D CD  1 
ATOM   6270 O  OE1 . GLU D 1 9   ? -42.669 109.430 6.344   1.00 84.91  ? 9   GLU D OE1 1 
ATOM   6271 O  OE2 . GLU D 1 9   ? -42.132 109.660 8.463   1.00 78.01  ? 9   GLU D OE2 1 
ATOM   6272 N  N   . VAL D 1 10  ? -46.207 109.712 12.139  1.00 63.42  ? 10  VAL D N   1 
ATOM   6273 C  CA  . VAL D 1 10  ? -46.934 110.355 13.224  1.00 62.27  ? 10  VAL D CA  1 
ATOM   6274 C  C   . VAL D 1 10  ? -46.406 109.998 14.606  1.00 65.52  ? 10  VAL D C   1 
ATOM   6275 O  O   . VAL D 1 10  ? -46.274 110.870 15.463  1.00 71.03  ? 10  VAL D O   1 
ATOM   6276 C  CB  . VAL D 1 10  ? -48.448 110.046 13.160  1.00 55.00  ? 10  VAL D CB  1 
ATOM   6277 C  CG1 . VAL D 1 10  ? -48.701 108.544 13.184  1.00 50.17  ? 10  VAL D CG1 1 
ATOM   6278 C  CG2 . VAL D 1 10  ? -49.177 110.744 14.300  1.00 54.03  ? 10  VAL D CG2 1 
ATOM   6279 N  N   . GLN D 1 11  ? -46.134 108.716 14.829  1.00 66.64  ? 11  GLN D N   1 
ATOM   6280 C  CA  . GLN D 1 11  ? -45.691 108.256 16.143  1.00 67.91  ? 11  GLN D CA  1 
ATOM   6281 C  C   . GLN D 1 11  ? -44.276 108.729 16.469  1.00 68.76  ? 11  GLN D C   1 
ATOM   6282 O  O   . GLN D 1 11  ? -43.915 108.822 17.641  1.00 65.93  ? 11  GLN D O   1 
ATOM   6283 C  CB  . GLN D 1 11  ? -45.861 106.730 16.328  1.00 67.15  ? 11  GLN D CB  1 
ATOM   6284 C  CG  . GLN D 1 11  ? -45.549 105.845 15.125  1.00 69.03  ? 11  GLN D CG  1 
ATOM   6285 C  CD  . GLN D 1 11  ? -45.955 104.382 15.332  1.00 71.94  ? 11  GLN D CD  1 
ATOM   6286 O  OE1 . GLN D 1 11  ? -46.999 104.080 15.923  1.00 69.52  ? 11  GLN D OE1 1 
ATOM   6287 N  NE2 . GLN D 1 11  ? -45.129 103.468 14.841  1.00 63.30  ? 11  GLN D NE2 1 
ATOM   6288 N  N   . ALA D 1 12  ? -43.495 109.069 15.438  1.00 70.83  ? 12  ALA D N   1 
ATOM   6289 C  CA  . ALA D 1 12  ? -42.176 109.688 15.639  1.00 72.08  ? 12  ALA D CA  1 
ATOM   6290 C  C   . ALA D 1 12  ? -42.305 111.051 16.333  1.00 74.07  ? 12  ALA D C   1 
ATOM   6291 O  O   . ALA D 1 12  ? -41.363 111.536 16.964  1.00 66.14  ? 12  ALA D O   1 
ATOM   6292 C  CB  . ALA D 1 12  ? -41.437 109.820 14.323  1.00 65.02  ? 12  ALA D CB  1 
ATOM   6293 N  N   . GLU D 1 13  ? -43.489 111.649 16.212  1.00 78.64  ? 13  GLU D N   1 
ATOM   6294 C  CA  . GLU D 1 13  ? -43.821 112.874 16.920  1.00 84.66  ? 13  GLU D CA  1 
ATOM   6295 C  C   . GLU D 1 13  ? -44.272 112.520 18.342  1.00 89.21  ? 13  GLU D C   1 
ATOM   6296 O  O   . GLU D 1 13  ? -43.539 112.739 19.315  1.00 88.05  ? 13  GLU D O   1 
ATOM   6297 C  CB  . GLU D 1 13  ? -44.911 113.660 16.160  1.00 80.11  ? 13  GLU D CB  1 
ATOM   6298 C  CG  . GLU D 1 13  ? -44.808 115.185 16.261  1.00 79.72  ? 13  GLU D CG  1 
ATOM   6299 C  CD  . GLU D 1 13  ? -45.728 115.818 17.305  1.00 79.31  ? 13  GLU D CD  1 
ATOM   6300 O  OE1 . GLU D 1 13  ? -46.737 115.182 17.696  1.00 80.88  ? 13  GLU D OE1 1 
ATOM   6301 O  OE2 . GLU D 1 13  ? -45.450 116.970 17.730  1.00 67.14  ? 13  GLU D OE2 1 
ATOM   6302 N  N   . SER D 1 14  ? -45.450 111.908 18.438  1.00 91.18  ? 14  SER D N   1 
ATOM   6303 C  CA  . SER D 1 14  ? -46.229 111.862 19.680  1.00 91.85  ? 14  SER D CA  1 
ATOM   6304 C  C   . SER D 1 14  ? -45.606 111.198 20.921  1.00 88.09  ? 14  SER D C   1 
ATOM   6305 O  O   . SER D 1 14  ? -46.217 111.227 21.994  1.00 84.50  ? 14  SER D O   1 
ATOM   6306 C  CB  . SER D 1 14  ? -47.625 111.283 19.405  1.00 96.35  ? 14  SER D CB  1 
ATOM   6307 O  OG  . SER D 1 14  ? -48.521 111.585 20.466  1.00 97.51  ? 14  SER D OG  1 
ATOM   6308 N  N   . SER D 1 15  ? -44.418 110.605 20.796  1.00 86.10  ? 15  SER D N   1 
ATOM   6309 C  CA  . SER D 1 15  ? -43.746 110.038 21.977  1.00 84.31  ? 15  SER D CA  1 
ATOM   6310 C  C   . SER D 1 15  ? -42.261 110.397 22.048  1.00 87.74  ? 15  SER D C   1 
ATOM   6311 O  O   . SER D 1 15  ? -41.536 110.294 21.053  1.00 82.65  ? 15  SER D O   1 
ATOM   6312 C  CB  . SER D 1 15  ? -43.959 108.518 22.079  1.00 78.42  ? 15  SER D CB  1 
ATOM   6313 O  OG  . SER D 1 15  ? -42.857 107.787 21.560  1.00 73.64  ? 15  SER D OG  1 
ATOM   6314 N  N   . ASN D 1 16  ? -41.826 110.812 23.241  1.00 94.83  ? 16  ASN D N   1 
ATOM   6315 C  CA  . ASN D 1 16  ? -40.460 111.292 23.487  1.00 96.23  ? 16  ASN D CA  1 
ATOM   6316 C  C   . ASN D 1 16  ? -39.447 110.142 23.565  1.00 97.32  ? 16  ASN D C   1 
ATOM   6317 O  O   . ASN D 1 16  ? -38.873 109.875 24.627  1.00 91.31  ? 16  ASN D O   1 
ATOM   6318 C  CB  . ASN D 1 16  ? -40.410 112.149 24.765  1.00 98.30  ? 16  ASN D CB  1 
ATOM   6319 C  CG  . ASN D 1 16  ? -41.489 113.228 24.809  1.00 97.73  ? 16  ASN D CG  1 
ATOM   6320 O  OD1 . ASN D 1 16  ? -41.729 113.940 23.827  1.00 99.37  ? 16  ASN D OD1 1 
ATOM   6321 N  ND2 . ASN D 1 16  ? -42.136 113.362 25.966  1.00 94.80  ? 16  ASN D ND2 1 
ATOM   6322 N  N   . TYR D 1 17  ? -39.237 109.484 22.421  1.00 98.28  ? 17  TYR D N   1 
ATOM   6323 C  CA  . TYR D 1 17  ? -38.431 108.262 22.310  1.00 97.29  ? 17  TYR D CA  1 
ATOM   6324 C  C   . TYR D 1 17  ? -37.865 108.044 20.906  1.00 101.40 ? 17  TYR D C   1 
ATOM   6325 O  O   . TYR D 1 17  ? -38.430 108.554 19.932  1.00 107.35 ? 17  TYR D O   1 
ATOM   6326 C  CB  . TYR D 1 17  ? -39.272 107.047 22.700  1.00 98.58  ? 17  TYR D CB  1 
ATOM   6327 C  CG  . TYR D 1 17  ? -39.078 106.649 24.131  1.00 97.38  ? 17  TYR D CG  1 
ATOM   6328 C  CD1 . TYR D 1 17  ? -38.038 105.794 24.498  1.00 96.43  ? 17  TYR D CD1 1 
ATOM   6329 C  CD2 . TYR D 1 17  ? -39.920 107.137 25.123  1.00 96.62  ? 17  TYR D CD2 1 
ATOM   6330 C  CE1 . TYR D 1 17  ? -37.843 105.432 25.817  1.00 94.68  ? 17  TYR D CE1 1 
ATOM   6331 C  CE2 . TYR D 1 17  ? -39.737 106.782 26.446  1.00 96.72  ? 17  TYR D CE2 1 
ATOM   6332 C  CZ  . TYR D 1 17  ? -38.700 105.931 26.785  1.00 96.57  ? 17  TYR D CZ  1 
ATOM   6333 O  OH  . TYR D 1 17  ? -38.521 105.584 28.100  1.00 96.76  ? 17  TYR D OH  1 
ATOM   6334 N  N   . PRO D 1 18  ? -36.753 107.273 20.791  1.00 101.74 ? 18  PRO D N   1 
ATOM   6335 C  CA  . PRO D 1 18  ? -36.182 106.935 19.471  1.00 95.95  ? 18  PRO D CA  1 
ATOM   6336 C  C   . PRO D 1 18  ? -37.204 106.301 18.519  1.00 90.96  ? 18  PRO D C   1 
ATOM   6337 O  O   . PRO D 1 18  ? -38.281 105.884 18.958  1.00 85.67  ? 18  PRO D O   1 
ATOM   6338 C  CB  . PRO D 1 18  ? -35.052 105.938 19.804  1.00 95.31  ? 18  PRO D CB  1 
ATOM   6339 C  CG  . PRO D 1 18  ? -35.201 105.601 21.254  1.00 96.32  ? 18  PRO D CG  1 
ATOM   6340 C  CD  . PRO D 1 18  ? -35.909 106.763 21.889  1.00 100.61 ? 18  PRO D CD  1 
ATOM   6341 N  N   . CYS D 1 19  ? -36.855 106.236 17.232  1.00 86.10  ? 19  CYS D N   1 
ATOM   6342 C  CA  . CYS D 1 19  ? -37.768 105.786 16.167  1.00 81.10  ? 19  CYS D CA  1 
ATOM   6343 C  C   . CYS D 1 19  ? -37.016 105.438 14.884  1.00 84.13  ? 19  CYS D C   1 
ATOM   6344 O  O   . CYS D 1 19  ? -35.781 105.430 14.850  1.00 84.25  ? 19  CYS D O   1 
ATOM   6345 C  CB  . CYS D 1 19  ? -38.812 106.870 15.852  1.00 75.24  ? 19  CYS D CB  1 
ATOM   6346 S  SG  . CYS D 1 19  ? -40.488 106.522 16.425  1.00 70.93  ? 19  CYS D SG  1 
ATOM   6347 N  N   . LEU D 1 20  ? -37.780 105.158 13.831  1.00 81.67  ? 20  LEU D N   1 
ATOM   6348 C  CA  . LEU D 1 20  ? -37.243 104.867 12.509  1.00 75.60  ? 20  LEU D CA  1 
ATOM   6349 C  C   . LEU D 1 20  ? -38.386 104.994 11.511  1.00 71.63  ? 20  LEU D C   1 
ATOM   6350 O  O   . LEU D 1 20  ? -39.140 104.049 11.282  1.00 67.84  ? 20  LEU D O   1 
ATOM   6351 C  CB  . LEU D 1 20  ? -36.643 103.460 12.470  1.00 79.24  ? 20  LEU D CB  1 
ATOM   6352 C  CG  . LEU D 1 20  ? -35.380 103.207 11.644  1.00 79.83  ? 20  LEU D CG  1 
ATOM   6353 C  CD1 . LEU D 1 20  ? -35.662 103.337 10.160  1.00 79.08  ? 20  LEU D CD1 1 
ATOM   6354 C  CD2 . LEU D 1 20  ? -34.237 104.126 12.054  1.00 82.40  ? 20  LEU D CD2 1 
ATOM   6355 N  N   . VAL D 1 21  ? -38.504 106.187 10.942  1.00 60.97  ? 21  VAL D N   1 
ATOM   6356 C  CA  . VAL D 1 21  ? -39.634 106.577 10.114  1.00 59.71  ? 21  VAL D CA  1 
ATOM   6357 C  C   . VAL D 1 21  ? -39.559 106.027 8.674   1.00 59.63  ? 21  VAL D C   1 
ATOM   6358 O  O   . VAL D 1 21  ? -38.465 105.782 8.165   1.00 58.73  ? 21  VAL D O   1 
ATOM   6359 C  CB  . VAL D 1 21  ? -39.811 108.113 10.136  1.00 56.25  ? 21  VAL D CB  1 
ATOM   6360 C  CG1 . VAL D 1 21  ? -40.238 108.557 11.527  1.00 51.78  ? 21  VAL D CG1 1 
ATOM   6361 C  CG2 . VAL D 1 21  ? -38.533 108.838 9.699   1.00 51.92  ? 21  VAL D CG2 1 
ATOM   6362 N  N   . PRO D 1 22  ? -40.725 105.849 8.018   1.00 57.85  ? 22  PRO D N   1 
ATOM   6363 C  CA  . PRO D 1 22  ? -40.873 105.185 6.719   1.00 59.12  ? 22  PRO D CA  1 
ATOM   6364 C  C   . PRO D 1 22  ? -39.754 105.363 5.691   1.00 60.60  ? 22  PRO D C   1 
ATOM   6365 O  O   . PRO D 1 22  ? -39.332 104.382 5.092   1.00 63.69  ? 22  PRO D O   1 
ATOM   6366 C  CB  . PRO D 1 22  ? -42.191 105.742 6.201   1.00 55.54  ? 22  PRO D CB  1 
ATOM   6367 C  CG  . PRO D 1 22  ? -42.998 105.863 7.450   1.00 62.96  ? 22  PRO D CG  1 
ATOM   6368 C  CD  . PRO D 1 22  ? -42.042 106.263 8.542   1.00 55.88  ? 22  PRO D CD  1 
ATOM   6369 N  N   . VAL D 1 23  ? -39.276 106.586 5.489   1.00 61.13  ? 23  VAL D N   1 
ATOM   6370 C  CA  . VAL D 1 23  ? -38.223 106.830 4.500   1.00 61.75  ? 23  VAL D CA  1 
ATOM   6371 C  C   . VAL D 1 23  ? -36.883 106.213 4.913   1.00 61.85  ? 23  VAL D C   1 
ATOM   6372 O  O   . VAL D 1 23  ? -35.999 105.965 4.077   1.00 58.30  ? 23  VAL D O   1 
ATOM   6373 C  CB  . VAL D 1 23  ? -38.048 108.332 4.195   1.00 62.68  ? 23  VAL D CB  1 
ATOM   6374 C  CG1 . VAL D 1 23  ? -39.379 108.942 3.765   1.00 58.15  ? 23  VAL D CG1 1 
ATOM   6375 C  CG2 . VAL D 1 23  ? -37.449 109.064 5.393   1.00 65.28  ? 23  VAL D CG2 1 
ATOM   6376 N  N   . LYS D 1 24  ? -36.746 105.957 6.207   1.00 61.12  ? 24  LYS D N   1 
ATOM   6377 C  CA  . LYS D 1 24  ? -35.506 105.436 6.752   1.00 63.64  ? 24  LYS D CA  1 
ATOM   6378 C  C   . LYS D 1 24  ? -35.585 103.932 6.981   1.00 67.16  ? 24  LYS D C   1 
ATOM   6379 O  O   . LYS D 1 24  ? -34.558 103.284 7.193   1.00 72.34  ? 24  LYS D O   1 
ATOM   6380 C  CB  . LYS D 1 24  ? -35.151 106.174 8.044   1.00 63.55  ? 24  LYS D CB  1 
ATOM   6381 C  CG  . LYS D 1 24  ? -34.901 107.654 7.833   1.00 60.09  ? 24  LYS D CG  1 
ATOM   6382 C  CD  . LYS D 1 24  ? -34.900 108.421 9.138   1.00 60.27  ? 24  LYS D CD  1 
ATOM   6383 C  CE  . LYS D 1 24  ? -34.936 109.915 8.862   1.00 61.93  ? 24  LYS D CE  1 
ATOM   6384 N  NZ  . LYS D 1 24  ? -34.801 110.744 10.092  1.00 57.42  ? 24  LYS D NZ  1 
ATOM   6385 N  N   . TRP D 1 25  ? -36.802 103.390 6.912   1.00 66.84  ? 25  TRP D N   1 
ATOM   6386 C  CA  . TRP D 1 25  ? -37.075 101.966 7.154   1.00 69.44  ? 25  TRP D CA  1 
ATOM   6387 C  C   . TRP D 1 25  ? -36.026 101.026 6.616   1.00 72.04  ? 25  TRP D C   1 
ATOM   6388 O  O   . TRP D 1 25  ? -35.485 101.221 5.504   1.00 66.97  ? 25  TRP D O   1 
ATOM   6389 C  CB  . TRP D 1 25  ? -38.476 101.573 6.666   1.00 62.60  ? 25  TRP D CB  1 
ATOM   6390 C  CG  . TRP D 1 25  ? -39.600 101.970 7.608   1.00 63.40  ? 25  TRP D CG  1 
ATOM   6391 C  CD1 . TRP D 1 25  ? -39.483 102.499 8.890   1.00 66.13  ? 25  TRP D CD1 1 
ATOM   6392 C  CD2 . TRP D 1 25  ? -41.060 101.847 7.389   1.00 58.40  ? 25  TRP D CD2 1 
ATOM   6393 N  NE1 . TRP D 1 25  ? -40.722 102.730 9.444   1.00 68.31  ? 25  TRP D NE1 1 
ATOM   6394 C  CE2 . TRP D 1 25  ? -41.703 102.354 8.605   1.00 61.29  ? 25  TRP D CE2 1 
ATOM   6395 C  CE3 . TRP D 1 25  ? -41.858 101.396 6.347   1.00 58.85  ? 25  TRP D CE3 1 
ATOM   6396 C  CZ2 . TRP D 1 25  ? -43.082 102.394 8.748   1.00 61.39  ? 25  TRP D CZ2 1 
ATOM   6397 C  CZ3 . TRP D 1 25  ? -43.248 101.439 6.505   1.00 57.33  ? 25  TRP D CZ3 1 
ATOM   6398 C  CH2 . TRP D 1 25  ? -43.844 101.927 7.676   1.00 56.07  ? 25  TRP D CH2 1 
ATOM   6399 N  N   . GLY D 1 26  ? -35.736 100.004 7.430   1.00 77.64  ? 26  GLY D N   1 
ATOM   6400 C  CA  . GLY D 1 26  ? -34.708 98.998  7.150   1.00 75.03  ? 26  GLY D CA  1 
ATOM   6401 C  C   . GLY D 1 26  ? -35.284 97.623  6.879   1.00 75.31  ? 26  GLY D C   1 
ATOM   6402 O  O   . GLY D 1 26  ? -36.166 97.153  7.603   1.00 74.13  ? 26  GLY D O   1 
ATOM   6403 N  N   . GLY D 1 27  ? -34.763 96.985  5.834   1.00 76.26  ? 27  GLY D N   1 
ATOM   6404 C  CA  . GLY D 1 27  ? -35.250 95.696  5.335   1.00 77.25  ? 27  GLY D CA  1 
ATOM   6405 C  C   . GLY D 1 27  ? -35.171 95.813  3.824   1.00 77.76  ? 27  GLY D C   1 
ATOM   6406 O  O   . GLY D 1 27  ? -34.152 96.244  3.278   1.00 78.37  ? 27  GLY D O   1 
ATOM   6407 N  N   . ASN D 1 28  ? -36.252 95.447  3.145   1.00 74.06  ? 28  ASN D N   1 
ATOM   6408 C  CA  . ASN D 1 28  ? -36.355 95.662  1.700   1.00 73.71  ? 28  ASN D CA  1 
ATOM   6409 C  C   . ASN D 1 28  ? -36.875 97.047  1.300   1.00 73.20  ? 28  ASN D C   1 
ATOM   6410 O  O   . ASN D 1 28  ? -36.832 97.434  0.128   1.00 67.07  ? 28  ASN D O   1 
ATOM   6411 C  CB  . ASN D 1 28  ? -37.234 94.559  1.107   1.00 72.03  ? 28  ASN D CB  1 
ATOM   6412 C  CG  . ASN D 1 28  ? -36.698 93.172  1.398   1.00 74.07  ? 28  ASN D CG  1 
ATOM   6413 O  OD1 . ASN D 1 28  ? -35.556 92.852  1.062   1.00 74.43  ? 28  ASN D OD1 1 
ATOM   6414 N  ND2 . ASN D 1 28  ? -37.514 92.344  2.028   1.00 67.11  ? 28  ASN D ND2 1 
ATOM   6415 N  N   . CYS D 1 29  ? -37.338 97.788  2.306   1.00 69.51  ? 29  CYS D N   1 
ATOM   6416 C  CA  . CYS D 1 29  ? -38.083 99.029  2.129   1.00 66.96  ? 29  CYS D CA  1 
ATOM   6417 C  C   . CYS D 1 29  ? -37.596 99.952  1.029   1.00 64.30  ? 29  CYS D C   1 
ATOM   6418 O  O   . CYS D 1 29  ? -38.391 100.697 0.457   1.00 63.64  ? 29  CYS D O   1 
ATOM   6419 C  CB  . CYS D 1 29  ? -38.170 99.787  3.457   1.00 68.82  ? 29  CYS D CB  1 
ATOM   6420 S  SG  . CYS D 1 29  ? -39.219 98.967  4.684   1.00 69.61  ? 29  CYS D SG  1 
ATOM   6421 N  N   . GLN D 1 30  ? -36.303 99.897  0.727   1.00 65.54  ? 30  GLN D N   1 
ATOM   6422 C  CA  . GLN D 1 30  ? -35.701 100.873 -0.186  1.00 67.60  ? 30  GLN D CA  1 
ATOM   6423 C  C   . GLN D 1 30  ? -35.646 100.402 -1.634  1.00 67.33  ? 30  GLN D C   1 
ATOM   6424 O  O   . GLN D 1 30  ? -35.156 101.134 -2.500  1.00 69.06  ? 30  GLN D O   1 
ATOM   6425 C  CB  . GLN D 1 30  ? -34.308 101.314 0.295   1.00 68.78  ? 30  GLN D CB  1 
ATOM   6426 C  CG  . GLN D 1 30  ? -34.227 101.765 1.753   1.00 73.70  ? 30  GLN D CG  1 
ATOM   6427 C  CD  . GLN D 1 30  ? -35.219 102.869 2.125   1.00 80.75  ? 30  GLN D CD  1 
ATOM   6428 O  OE1 . GLN D 1 30  ? -35.484 103.789 1.343   1.00 77.63  ? 30  GLN D OE1 1 
ATOM   6429 N  NE2 . GLN D 1 30  ? -35.762 102.785 3.343   1.00 84.46  ? 30  GLN D NE2 1 
ATOM   6430 N  N   . LYS D 1 31  ? -36.162 99.194  -1.887  1.00 69.58  ? 31  LYS D N   1 
ATOM   6431 C  CA  . LYS D 1 31  ? -36.134 98.573  -3.223  1.00 72.84  ? 31  LYS D CA  1 
ATOM   6432 C  C   . LYS D 1 31  ? -37.200 99.150  -4.152  1.00 73.07  ? 31  LYS D C   1 
ATOM   6433 O  O   . LYS D 1 31  ? -38.062 99.916  -3.716  1.00 75.53  ? 31  LYS D O   1 
ATOM   6434 C  CB  . LYS D 1 31  ? -36.272 97.048  -3.122  1.00 77.44  ? 31  LYS D CB  1 
ATOM   6435 C  CG  . LYS D 1 31  ? -35.019 96.318  -2.657  1.00 74.39  ? 31  LYS D CG  1 
ATOM   6436 C  CD  . LYS D 1 31  ? -35.402 95.038  -1.934  1.00 75.61  ? 31  LYS D CD  1 
ATOM   6437 C  CE  . LYS D 1 31  ? -34.192 94.172  -1.636  1.00 76.88  ? 31  LYS D CE  1 
ATOM   6438 N  NZ  . LYS D 1 31  ? -34.611 92.761  -1.416  1.00 75.44  ? 31  LYS D NZ  1 
ATOM   6439 N  N   . ASP D 1 32  ? -37.141 98.762  -5.426  1.00 73.49  ? 32  ASP D N   1 
ATOM   6440 C  CA  . ASP D 1 32  ? -37.945 99.381  -6.488  1.00 66.99  ? 32  ASP D CA  1 
ATOM   6441 C  C   . ASP D 1 32  ? -39.329 98.769  -6.783  1.00 62.31  ? 32  ASP D C   1 
ATOM   6442 O  O   . ASP D 1 32  ? -39.963 99.178  -7.765  1.00 61.91  ? 32  ASP D O   1 
ATOM   6443 C  CB  . ASP D 1 32  ? -37.143 99.408  -7.804  1.00 75.10  ? 32  ASP D CB  1 
ATOM   6444 C  CG  . ASP D 1 32  ? -36.148 100.563 -7.883  1.00 79.24  ? 32  ASP D CG  1 
ATOM   6445 O  OD1 . ASP D 1 32  ? -36.480 101.691 -7.453  1.00 86.56  ? 32  ASP D OD1 1 
ATOM   6446 O  OD2 . ASP D 1 32  ? -35.032 100.343 -8.407  1.00 76.98  ? 32  ASP D OD2 1 
ATOM   6447 N  N   . ARG D 1 33  ? -39.809 97.815  -5.982  1.00 52.02  ? 33  ARG D N   1 
ATOM   6448 C  CA  . ARG D 1 33  ? -41.086 97.137  -6.315  1.00 54.73  ? 33  ARG D CA  1 
ATOM   6449 C  C   . ARG D 1 33  ? -42.157 97.233  -5.199  1.00 56.19  ? 33  ARG D C   1 
ATOM   6450 O  O   . ARG D 1 33  ? -42.897 96.264  -4.920  1.00 46.08  ? 33  ARG D O   1 
ATOM   6451 C  CB  . ARG D 1 33  ? -40.843 95.661  -6.708  1.00 57.61  ? 33  ARG D CB  1 
ATOM   6452 C  CG  . ARG D 1 33  ? -40.219 95.445  -8.085  1.00 60.81  ? 33  ARG D CG  1 
ATOM   6453 C  CD  . ARG D 1 33  ? -39.926 93.977  -8.414  1.00 56.58  ? 33  ARG D CD  1 
ATOM   6454 N  NE  . ARG D 1 33  ? -41.074 93.070  -8.291  1.00 53.75  ? 33  ARG D NE  1 
ATOM   6455 C  CZ  . ARG D 1 33  ? -42.043 92.922  -9.194  1.00 58.01  ? 33  ARG D CZ  1 
ATOM   6456 N  NH1 . ARG D 1 33  ? -42.037 93.626  -10.323 1.00 59.54  ? 33  ARG D NH1 1 
ATOM   6457 N  NH2 . ARG D 1 33  ? -43.033 92.065  -8.962  1.00 53.24  ? 33  ARG D NH2 1 
ATOM   6458 N  N   . GLN D 1 34  ? -42.265 98.420  -4.607  1.00 51.00  ? 34  GLN D N   1 
ATOM   6459 C  CA  . GLN D 1 34  ? -42.911 98.583  -3.310  1.00 50.68  ? 34  GLN D CA  1 
ATOM   6460 C  C   . GLN D 1 34  ? -44.372 99.009  -3.364  1.00 50.04  ? 34  GLN D C   1 
ATOM   6461 O  O   . GLN D 1 34  ? -44.854 99.495  -4.378  1.00 45.67  ? 34  GLN D O   1 
ATOM   6462 C  CB  . GLN D 1 34  ? -42.107 99.573  -2.480  1.00 48.09  ? 34  GLN D CB  1 
ATOM   6463 C  CG  . GLN D 1 34  ? -40.712 99.079  -2.155  1.00 50.36  ? 34  GLN D CG  1 
ATOM   6464 C  CD  . GLN D 1 34  ? -40.684 98.140  -0.962  1.00 49.49  ? 34  GLN D CD  1 
ATOM   6465 O  OE1 . GLN D 1 34  ? -40.450 98.573  0.150   1.00 49.39  ? 34  GLN D OE1 1 
ATOM   6466 N  NE2 . GLN D 1 34  ? -40.913 96.849  -1.191  1.00 50.37  ? 34  GLN D NE2 1 
ATOM   6467 N  N   . SER D 1 35  ? -45.075 98.801  -2.257  1.00 50.16  ? 35  SER D N   1 
ATOM   6468 C  CA  . SER D 1 35  ? -46.467 99.217  -2.119  1.00 45.68  ? 35  SER D CA  1 
ATOM   6469 C  C   . SER D 1 35  ? -46.515 100.195 -0.946  1.00 42.83  ? 35  SER D C   1 
ATOM   6470 O  O   . SER D 1 35  ? -45.653 100.120 -0.075  1.00 39.96  ? 35  SER D O   1 
ATOM   6471 C  CB  . SER D 1 35  ? -47.347 97.995  -1.830  1.00 48.03  ? 35  SER D CB  1 
ATOM   6472 O  OG  . SER D 1 35  ? -47.762 97.352  -3.026  1.00 44.70  ? 35  SER D OG  1 
ATOM   6473 N  N   . PRO D 1 36  ? -47.514 101.105 -0.904  1.00 40.75  ? 36  PRO D N   1 
ATOM   6474 C  CA  . PRO D 1 36  ? -48.606 101.239 -1.844  1.00 36.78  ? 36  PRO D CA  1 
ATOM   6475 C  C   . PRO D 1 36  ? -48.253 102.181 -3.001  1.00 36.01  ? 36  PRO D C   1 
ATOM   6476 O  O   . PRO D 1 36  ? -47.205 102.823 -2.978  1.00 37.38  ? 36  PRO D O   1 
ATOM   6477 C  CB  . PRO D 1 36  ? -49.704 101.833 -0.964  1.00 34.30  ? 36  PRO D CB  1 
ATOM   6478 C  CG  . PRO D 1 36  ? -48.936 102.807 -0.122  1.00 35.78  ? 36  PRO D CG  1 
ATOM   6479 C  CD  . PRO D 1 36  ? -47.692 102.040 0.235   1.00 38.79  ? 36  PRO D CD  1 
ATOM   6480 N  N   . ILE D 1 37  ? -49.132 102.235 -3.995  1.00 34.33  ? 37  ILE D N   1 
ATOM   6481 C  CA  . ILE D 1 37  ? -48.994 103.076 -5.175  1.00 34.74  ? 37  ILE D CA  1 
ATOM   6482 C  C   . ILE D 1 37  ? -50.311 103.766 -5.412  1.00 32.45  ? 37  ILE D C   1 
ATOM   6483 O  O   . ILE D 1 37  ? -51.358 103.373 -4.875  1.00 27.67  ? 37  ILE D O   1 
ATOM   6484 C  CB  . ILE D 1 37  ? -48.756 102.276 -6.506  1.00 35.00  ? 37  ILE D CB  1 
ATOM   6485 C  CG1 . ILE D 1 37  ? -49.630 101.028 -6.581  1.00 35.37  ? 37  ILE D CG1 1 
ATOM   6486 C  CG2 . ILE D 1 37  ? -47.288 101.919 -6.700  1.00 37.69  ? 37  ILE D CG2 1 
ATOM   6487 C  CD1 . ILE D 1 37  ? -50.121 100.686 -7.977  1.00 40.48  ? 37  ILE D CD1 1 
ATOM   6488 N  N   . ASN D 1 38  ? -50.249 104.776 -6.263  1.00 32.06  ? 38  ASN D N   1 
ATOM   6489 C  CA  . ASN D 1 38  ? -51.433 105.348 -6.836  1.00 31.59  ? 38  ASN D CA  1 
ATOM   6490 C  C   . ASN D 1 38  ? -51.721 104.629 -8.159  1.00 33.78  ? 38  ASN D C   1 
ATOM   6491 O  O   . ASN D 1 38  ? -50.785 104.219 -8.865  1.00 30.97  ? 38  ASN D O   1 
ATOM   6492 C  CB  . ASN D 1 38  ? -51.178 106.845 -6.977  1.00 31.74  ? 38  ASN D CB  1 
ATOM   6493 C  CG  . ASN D 1 38  ? -52.147 107.523 -7.861  1.00 32.25  ? 38  ASN D CG  1 
ATOM   6494 O  OD1 . ASN D 1 38  ? -53.288 107.762 -7.485  1.00 43.19  ? 38  ASN D OD1 1 
ATOM   6495 N  ND2 . ASN D 1 38  ? -51.700 107.867 -9.047  1.00 31.23  ? 38  ASN D ND2 1 
ATOM   6496 N  N   . ILE D 1 39  ? -53.012 104.503 -8.487  1.00 35.36  ? 39  ILE D N   1 
ATOM   6497 C  CA  . ILE D 1 39  ? -53.519 103.688 -9.586  1.00 36.58  ? 39  ILE D CA  1 
ATOM   6498 C  C   . ILE D 1 39  ? -54.282 104.587 -10.539 1.00 37.21  ? 39  ILE D C   1 
ATOM   6499 O  O   . ILE D 1 39  ? -55.309 105.165 -10.154 1.00 38.42  ? 39  ILE D O   1 
ATOM   6500 C  CB  . ILE D 1 39  ? -54.473 102.562 -9.053  1.00 37.67  ? 39  ILE D CB  1 
ATOM   6501 C  CG1 . ILE D 1 39  ? -53.764 101.664 -8.040  1.00 36.60  ? 39  ILE D CG1 1 
ATOM   6502 C  CG2 . ILE D 1 39  ? -55.036 101.692 -10.170 1.00 35.58  ? 39  ILE D CG2 1 
ATOM   6503 C  CD1 . ILE D 1 39  ? -54.654 100.557 -7.496  1.00 34.31  ? 39  ILE D CD1 1 
ATOM   6504 N  N   . VAL D 1 40  ? -53.795 104.709 -11.782 1.00 38.89  ? 40  VAL D N   1 
ATOM   6505 C  CA  . VAL D 1 40  ? -54.466 105.560 -12.766 1.00 39.18  ? 40  VAL D CA  1 
ATOM   6506 C  C   . VAL D 1 40  ? -55.504 104.709 -13.494 1.00 42.50  ? 40  VAL D C   1 
ATOM   6507 O  O   . VAL D 1 40  ? -55.142 103.870 -14.324 1.00 40.01  ? 40  VAL D O   1 
ATOM   6508 C  CB  . VAL D 1 40  ? -53.495 106.277 -13.759 1.00 38.06  ? 40  VAL D CB  1 
ATOM   6509 C  CG1 . VAL D 1 40  ? -54.251 107.305 -14.590 1.00 39.97  ? 40  VAL D CG1 1 
ATOM   6510 C  CG2 . VAL D 1 40  ? -52.311 106.949 -13.056 1.00 36.70  ? 40  VAL D CG2 1 
ATOM   6511 N  N   . THR D 1 41  ? -56.792 104.912 -13.176 1.00 45.20  ? 41  THR D N   1 
ATOM   6512 C  CA  . THR D 1 41  ? -57.831 103.992 -13.655 1.00 47.93  ? 41  THR D CA  1 
ATOM   6513 C  C   . THR D 1 41  ? -57.825 103.815 -15.178 1.00 52.54  ? 41  THR D C   1 
ATOM   6514 O  O   . THR D 1 41  ? -57.976 102.690 -15.669 1.00 52.61  ? 41  THR D O   1 
ATOM   6515 C  CB  . THR D 1 41  ? -59.259 104.276 -13.118 1.00 43.73  ? 41  THR D CB  1 
ATOM   6516 O  OG1 . THR D 1 41  ? -59.744 105.541 -13.589 1.00 41.24  ? 41  THR D OG1 1 
ATOM   6517 C  CG2 . THR D 1 41  ? -59.299 104.189 -11.567 1.00 41.96  ? 41  THR D CG2 1 
ATOM   6518 N  N   . THR D 1 42  ? -57.587 104.914 -15.897 1.00 48.24  ? 42  THR D N   1 
ATOM   6519 C  CA  . THR D 1 42  ? -57.550 104.943 -17.366 1.00 44.40  ? 42  THR D CA  1 
ATOM   6520 C  C   . THR D 1 42  ? -56.419 104.135 -18.008 1.00 49.06  ? 42  THR D C   1 
ATOM   6521 O  O   . THR D 1 42  ? -56.555 103.681 -19.152 1.00 46.31  ? 42  THR D O   1 
ATOM   6522 C  CB  . THR D 1 42  ? -57.392 106.389 -17.868 1.00 46.59  ? 42  THR D CB  1 
ATOM   6523 O  OG1 . THR D 1 42  ? -56.370 107.050 -17.097 1.00 44.97  ? 42  THR D OG1 1 
ATOM   6524 C  CG2 . THR D 1 42  ? -58.705 107.157 -17.776 1.00 43.04  ? 42  THR D CG2 1 
ATOM   6525 N  N   . LYS D 1 43  ? -55.310 103.968 -17.277 1.00 48.05  ? 43  LYS D N   1 
ATOM   6526 C  CA  . LYS D 1 43  ? -54.110 103.281 -17.783 1.00 47.21  ? 43  LYS D CA  1 
ATOM   6527 C  C   . LYS D 1 43  ? -53.991 101.813 -17.360 1.00 47.42  ? 43  LYS D C   1 
ATOM   6528 O  O   . LYS D 1 43  ? -52.953 101.183 -17.555 1.00 44.60  ? 43  LYS D O   1 
ATOM   6529 C  CB  . LYS D 1 43  ? -52.844 104.034 -17.341 1.00 44.61  ? 43  LYS D CB  1 
ATOM   6530 C  CG  . LYS D 1 43  ? -52.718 105.393 -18.014 1.00 44.03  ? 43  LYS D CG  1 
ATOM   6531 C  CD  . LYS D 1 43  ? -51.332 105.985 -17.874 1.00 40.79  ? 43  LYS D CD  1 
ATOM   6532 C  CE  . LYS D 1 43  ? -51.357 107.469 -18.247 1.00 41.39  ? 43  LYS D CE  1 
ATOM   6533 N  NZ  . LYS D 1 43  ? -50.147 108.151 -17.734 1.00 35.63  ? 43  LYS D NZ  1 
ATOM   6534 N  N   . ALA D 1 44  ? -55.028 101.288 -16.727 1.00 49.49  ? 44  ALA D N   1 
ATOM   6535 C  CA  . ALA D 1 44  ? -55.034 99.869  -16.371 1.00 47.64  ? 44  ALA D CA  1 
ATOM   6536 C  C   . ALA D 1 44  ? -55.980 99.175  -17.342 1.00 45.63  ? 44  ALA D C   1 
ATOM   6537 O  O   . ALA D 1 44  ? -57.169 99.501  -17.403 1.00 43.95  ? 44  ALA D O   1 
ATOM   6538 C  CB  . ALA D 1 44  ? -55.472 99.675  -14.928 1.00 47.05  ? 44  ALA D CB  1 
ATOM   6539 N  N   . LYS D 1 45  ? -55.427 98.275  -18.148 1.00 47.84  ? 45  LYS D N   1 
ATOM   6540 C  CA  . LYS D 1 45  ? -56.200 97.583  -19.195 1.00 51.65  ? 45  LYS D CA  1 
ATOM   6541 C  C   . LYS D 1 45  ? -56.816 96.275  -18.720 1.00 48.71  ? 45  LYS D C   1 
ATOM   6542 O  O   . LYS D 1 45  ? -56.311 95.633  -17.780 1.00 47.94  ? 45  LYS D O   1 
ATOM   6543 C  CB  . LYS D 1 45  ? -55.379 97.379  -20.481 1.00 53.01  ? 45  LYS D CB  1 
ATOM   6544 C  CG  . LYS D 1 45  ? -53.895 97.706  -20.361 1.00 55.02  ? 45  LYS D CG  1 
ATOM   6545 C  CD  . LYS D 1 45  ? -53.252 97.954  -21.718 1.00 54.79  ? 45  LYS D CD  1 
ATOM   6546 C  CE  . LYS D 1 45  ? -53.658 99.282  -22.353 1.00 56.75  ? 45  LYS D CE  1 
ATOM   6547 N  NZ  . LYS D 1 45  ? -52.645 99.697  -23.371 1.00 55.59  ? 45  LYS D NZ  1 
ATOM   6548 N  N   . VAL D 1 46  ? -57.916 95.896  -19.370 1.00 47.77  ? 46  VAL D N   1 
ATOM   6549 C  CA  . VAL D 1 46  ? -58.657 94.681  -19.010 1.00 53.59  ? 46  VAL D CA  1 
ATOM   6550 C  C   . VAL D 1 46  ? -57.767 93.468  -19.308 1.00 54.45  ? 46  VAL D C   1 
ATOM   6551 O  O   . VAL D 1 46  ? -57.108 93.425  -20.356 1.00 58.06  ? 46  VAL D O   1 
ATOM   6552 C  CB  . VAL D 1 46  ? -60.018 94.605  -19.754 1.00 58.34  ? 46  VAL D CB  1 
ATOM   6553 C  CG1 . VAL D 1 46  ? -60.865 93.434  -19.255 1.00 60.35  ? 46  VAL D CG1 1 
ATOM   6554 C  CG2 . VAL D 1 46  ? -60.794 95.910  -19.598 1.00 54.17  ? 46  VAL D CG2 1 
ATOM   6555 N  N   . ASP D 1 47  ? -57.687 92.523  -18.376 1.00 51.20  ? 47  ASP D N   1 
ATOM   6556 C  CA  . ASP D 1 47  ? -56.826 91.358  -18.577 1.00 55.08  ? 47  ASP D CA  1 
ATOM   6557 C  C   . ASP D 1 47  ? -57.668 90.132  -18.882 1.00 62.55  ? 47  ASP D C   1 
ATOM   6558 O  O   . ASP D 1 47  ? -57.149 89.149  -19.420 1.00 63.82  ? 47  ASP D O   1 
ATOM   6559 C  CB  . ASP D 1 47  ? -55.806 91.207  -17.451 1.00 55.71  ? 47  ASP D CB  1 
ATOM   6560 C  CG  . ASP D 1 47  ? -54.668 90.246  -17.800 1.00 61.77  ? 47  ASP D CG  1 
ATOM   6561 O  OD1 . ASP D 1 47  ? -54.676 89.111  -17.278 1.00 63.49  ? 47  ASP D OD1 1 
ATOM   6562 O  OD2 . ASP D 1 47  ? -53.754 90.622  -18.573 1.00 65.63  ? 47  ASP D OD2 1 
ATOM   6563 N  N   . LYS D 1 48  ? -58.961 90.206  -18.535 1.00 60.78  ? 48  LYS D N   1 
ATOM   6564 C  CA  . LYS D 1 48  ? -59.977 89.214  -18.929 1.00 64.19  ? 48  LYS D CA  1 
ATOM   6565 C  C   . LYS D 1 48  ? -59.817 87.945  -18.080 1.00 61.26  ? 48  LYS D C   1 
ATOM   6566 O  O   . LYS D 1 48  ? -60.775 87.513  -17.439 1.00 61.70  ? 48  LYS D O   1 
ATOM   6567 C  CB  . LYS D 1 48  ? -60.032 88.943  -20.433 1.00 69.23  ? 48  LYS D CB  1 
ATOM   6568 C  CG  . LYS D 1 48  ? -61.158 89.661  -21.152 1.00 69.85  ? 48  LYS D CG  1 
ATOM   6569 C  CD  . LYS D 1 48  ? -61.043 89.446  -22.652 1.00 71.00  ? 48  LYS D CD  1 
ATOM   6570 C  CE  . LYS D 1 48  ? -62.370 89.710  -23.342 1.00 76.22  ? 48  LYS D CE  1 
ATOM   6571 N  NZ  . LYS D 1 48  ? -62.183 89.885  -24.807 1.00 75.01  ? 48  LYS D NZ  1 
ATOM   6572 N  N   . LYS D 1 49  ? -58.614 87.366  -18.103 1.00 58.30  ? 49  LYS D N   1 
ATOM   6573 C  CA  . LYS D 1 49  ? -58.209 86.211  -17.293 1.00 60.00  ? 49  LYS D CA  1 
ATOM   6574 C  C   . LYS D 1 49  ? -58.577 86.309  -15.814 1.00 59.51  ? 49  LYS D C   1 
ATOM   6575 O  O   . LYS D 1 49  ? -58.661 85.294  -15.137 1.00 58.81  ? 49  LYS D O   1 
ATOM   6576 C  CB  . LYS D 1 49  ? -56.692 85.985  -17.392 1.00 58.67  ? 49  LYS D CB  1 
ATOM   6577 C  CG  . LYS D 1 49  ? -56.182 85.750  -18.802 1.00 61.89  ? 49  LYS D CG  1 
ATOM   6578 C  CD  . LYS D 1 49  ? -54.737 86.213  -18.939 1.00 64.92  ? 49  LYS D CD  1 
ATOM   6579 C  CE  . LYS D 1 49  ? -54.629 87.265  -20.034 1.00 62.16  ? 49  LYS D CE  1 
ATOM   6580 N  NZ  . LYS D 1 49  ? -53.536 86.954  -20.998 1.00 67.03  ? 49  LYS D NZ  1 
ATOM   6581 N  N   . LEU D 1 50  ? -58.771 87.532  -15.317 1.00 57.62  ? 50  LEU D N   1 
ATOM   6582 C  CA  . LEU D 1 50  ? -59.050 87.749  -13.907 1.00 51.62  ? 50  LEU D CA  1 
ATOM   6583 C  C   . LEU D 1 50  ? -60.543 87.867  -13.762 1.00 50.28  ? 50  LEU D C   1 
ATOM   6584 O  O   . LEU D 1 50  ? -61.109 88.963  -13.747 1.00 53.24  ? 50  LEU D O   1 
ATOM   6585 C  CB  . LEU D 1 50  ? -58.388 89.028  -13.402 1.00 51.47  ? 50  LEU D CB  1 
ATOM   6586 C  CG  . LEU D 1 50  ? -57.271 89.705  -14.178 1.00 49.07  ? 50  LEU D CG  1 
ATOM   6587 C  CD1 . LEU D 1 50  ? -57.329 91.196  -13.881 1.00 47.81  ? 50  LEU D CD1 1 
ATOM   6588 C  CD2 . LEU D 1 50  ? -55.926 89.100  -13.824 1.00 46.15  ? 50  LEU D CD2 1 
ATOM   6589 N  N   . GLY D 1 51  ? -61.187 86.722  -13.682 1.00 45.13  ? 51  GLY D N   1 
ATOM   6590 C  CA  . GLY D 1 51  ? -62.617 86.669  -13.467 1.00 45.46  ? 51  GLY D CA  1 
ATOM   6591 C  C   . GLY D 1 51  ? -62.916 86.816  -11.991 1.00 47.89  ? 51  GLY D C   1 
ATOM   6592 O  O   . GLY D 1 51  ? -62.051 87.224  -11.209 1.00 47.63  ? 51  GLY D O   1 
ATOM   6593 N  N   . ARG D 1 52  ? -64.127 86.421  -11.616 1.00 50.04  ? 52  ARG D N   1 
ATOM   6594 C  CA  . ARG D 1 52  ? -64.529 86.558  -10.205 1.00 52.47  ? 52  ARG D CA  1 
ATOM   6595 C  C   . ARG D 1 52  ? -63.785 85.718  -9.137  1.00 49.43  ? 52  ARG D C   1 
ATOM   6596 O  O   . ARG D 1 52  ? -62.958 84.866  -9.453  1.00 51.30  ? 52  ARG D O   1 
ATOM   6597 C  CB  . ARG D 1 52  ? -66.075 86.500  -10.092 1.00 53.51  ? 52  ARG D CB  1 
ATOM   6598 C  CG  . ARG D 1 52  ? -66.739 87.789  -10.602 1.00 58.51  ? 52  ARG D CG  1 
ATOM   6599 C  CD  . ARG D 1 52  ? -68.252 87.706  -10.798 1.00 64.52  ? 52  ARG D CD  1 
ATOM   6600 N  NE  . ARG D 1 52  ? -68.646 86.574  -11.637 1.00 66.59  ? 52  ARG D NE  1 
ATOM   6601 C  CZ  . ARG D 1 52  ? -68.897 86.637  -12.944 1.00 68.73  ? 52  ARG D CZ  1 
ATOM   6602 N  NH1 . ARG D 1 52  ? -68.816 87.798  -13.599 1.00 62.61  ? 52  ARG D NH1 1 
ATOM   6603 N  NH2 . ARG D 1 52  ? -69.238 85.528  -13.598 1.00 67.44  ? 52  ARG D NH2 1 
ATOM   6604 N  N   . PHE D 1 53  ? -64.061 85.995  -7.869  1.00 47.18  ? 53  PHE D N   1 
ATOM   6605 C  CA  . PHE D 1 53  ? -63.376 85.323  -6.770  1.00 50.92  ? 53  PHE D CA  1 
ATOM   6606 C  C   . PHE D 1 53  ? -64.326 84.290  -6.130  1.00 56.78  ? 53  PHE D C   1 
ATOM   6607 O  O   . PHE D 1 53  ? -65.538 84.550  -6.005  1.00 51.38  ? 53  PHE D O   1 
ATOM   6608 C  CB  . PHE D 1 53  ? -62.919 86.341  -5.704  1.00 42.52  ? 53  PHE D CB  1 
ATOM   6609 C  CG  . PHE D 1 53  ? -61.591 87.038  -5.997  1.00 42.96  ? 53  PHE D CG  1 
ATOM   6610 C  CD1 . PHE D 1 53  ? -61.562 88.341  -6.511  1.00 42.84  ? 53  PHE D CD1 1 
ATOM   6611 C  CD2 . PHE D 1 53  ? -60.373 86.436  -5.682  1.00 40.38  ? 53  PHE D CD2 1 
ATOM   6612 C  CE1 . PHE D 1 53  ? -60.359 89.003  -6.738  1.00 40.13  ? 53  PHE D CE1 1 
ATOM   6613 C  CE2 . PHE D 1 53  ? -59.167 87.089  -5.913  1.00 43.83  ? 53  PHE D CE2 1 
ATOM   6614 C  CZ  . PHE D 1 53  ? -59.160 88.377  -6.448  1.00 42.02  ? 53  PHE D CZ  1 
ATOM   6615 N  N   . PHE D 1 54  ? -63.794 83.131  -5.719  1.00 61.06  ? 54  PHE D N   1 
ATOM   6616 C  CA  . PHE D 1 54  ? -64.620 82.160  -4.975  1.00 66.76  ? 54  PHE D CA  1 
ATOM   6617 C  C   . PHE D 1 54  ? -64.359 82.296  -3.495  1.00 66.53  ? 54  PHE D C   1 
ATOM   6618 O  O   . PHE D 1 54  ? -63.210 82.228  -3.047  1.00 61.73  ? 54  PHE D O   1 
ATOM   6619 C  CB  . PHE D 1 54  ? -64.415 80.696  -5.417  1.00 68.35  ? 54  PHE D CB  1 
ATOM   6620 C  CG  . PHE D 1 54  ? -64.001 80.544  -6.846  1.00 71.61  ? 54  PHE D CG  1 
ATOM   6621 C  CD1 . PHE D 1 54  ? -64.813 80.999  -7.879  1.00 69.21  ? 54  PHE D CD1 1 
ATOM   6622 C  CD2 . PHE D 1 54  ? -62.783 79.947  -7.162  1.00 74.90  ? 54  PHE D CD2 1 
ATOM   6623 C  CE1 . PHE D 1 54  ? -64.401 80.867  -9.193  1.00 75.77  ? 54  PHE D CE1 1 
ATOM   6624 C  CE2 . PHE D 1 54  ? -62.370 79.802  -8.482  1.00 76.29  ? 54  PHE D CE2 1 
ATOM   6625 C  CZ  . PHE D 1 54  ? -63.181 80.267  -9.500  1.00 75.65  ? 54  PHE D CZ  1 
ATOM   6626 N  N   . PHE D 1 55  ? -65.440 82.474  -2.742  1.00 75.72  ? 55  PHE D N   1 
ATOM   6627 C  CA  . PHE D 1 55  ? -65.330 82.732  -1.309  1.00 81.67  ? 55  PHE D CA  1 
ATOM   6628 C  C   . PHE D 1 55  ? -65.781 81.579  -0.422  1.00 84.11  ? 55  PHE D C   1 
ATOM   6629 O  O   . PHE D 1 55  ? -66.928 81.527  0.043   1.00 82.17  ? 55  PHE D O   1 
ATOM   6630 C  CB  . PHE D 1 55  ? -66.010 84.065  -0.928  1.00 86.17  ? 55  PHE D CB  1 
ATOM   6631 C  CG  . PHE D 1 55  ? -65.247 85.280  -1.394  1.00 83.43  ? 55  PHE D CG  1 
ATOM   6632 C  CD1 . PHE D 1 55  ? -63.963 85.538  -0.911  1.00 79.50  ? 55  PHE D CD1 1 
ATOM   6633 C  CD2 . PHE D 1 55  ? -65.795 86.147  -2.335  1.00 76.50  ? 55  PHE D CD2 1 
ATOM   6634 C  CE1 . PHE D 1 55  ? -63.250 86.637  -1.356  1.00 78.10  ? 55  PHE D CE1 1 
ATOM   6635 C  CE2 . PHE D 1 55  ? -65.083 87.252  -2.780  1.00 72.99  ? 55  PHE D CE2 1 
ATOM   6636 C  CZ  . PHE D 1 55  ? -63.812 87.496  -2.291  1.00 73.05  ? 55  PHE D CZ  1 
ATOM   6637 N  N   . SER D 1 56  ? -64.847 80.654  -0.202  1.00 80.22  ? 56  SER D N   1 
ATOM   6638 C  CA  . SER D 1 56  ? -65.033 79.553  0.734   1.00 80.21  ? 56  SER D CA  1 
ATOM   6639 C  C   . SER D 1 56  ? -64.389 79.864  2.094   1.00 78.49  ? 56  SER D C   1 
ATOM   6640 O  O   . SER D 1 56  ? -63.260 80.381  2.179   1.00 68.20  ? 56  SER D O   1 
ATOM   6641 C  CB  . SER D 1 56  ? -64.490 78.251  0.143   1.00 79.32  ? 56  SER D CB  1 
ATOM   6642 O  OG  . SER D 1 56  ? -64.933 78.097  -1.194  1.00 72.28  ? 56  SER D OG  1 
ATOM   6643 N  N   . GLY D 1 57  ? -65.124 79.543  3.155   1.00 80.59  ? 57  GLY D N   1 
ATOM   6644 C  CA  . GLY D 1 57  ? -64.750 79.956  4.501   1.00 78.82  ? 57  GLY D CA  1 
ATOM   6645 C  C   . GLY D 1 57  ? -64.883 81.467  4.608   1.00 76.85  ? 57  GLY D C   1 
ATOM   6646 O  O   . GLY D 1 57  ? -63.936 82.150  4.989   1.00 66.57  ? 57  GLY D O   1 
ATOM   6647 N  N   . TYR D 1 58  ? -66.058 81.980  4.235   1.00 77.58  ? 58  TYR D N   1 
ATOM   6648 C  CA  . TYR D 1 58  ? -66.373 83.408  4.332   1.00 73.68  ? 58  TYR D CA  1 
ATOM   6649 C  C   . TYR D 1 58  ? -67.804 83.647  4.838   1.00 74.81  ? 58  TYR D C   1 
ATOM   6650 O  O   . TYR D 1 58  ? -68.006 84.470  5.722   1.00 77.64  ? 58  TYR D O   1 
ATOM   6651 C  CB  . TYR D 1 58  ? -66.113 84.144  2.998   1.00 69.31  ? 58  TYR D CB  1 
ATOM   6652 C  CG  . TYR D 1 58  ? -64.709 84.744  2.852   1.00 65.31  ? 58  TYR D CG  1 
ATOM   6653 C  CD1 . TYR D 1 58  ? -63.609 83.937  2.559   1.00 60.42  ? 58  TYR D CD1 1 
ATOM   6654 C  CD2 . TYR D 1 58  ? -64.490 86.124  2.985   1.00 64.38  ? 58  TYR D CD2 1 
ATOM   6655 C  CE1 . TYR D 1 58  ? -62.335 84.465  2.428   1.00 55.93  ? 58  TYR D CE1 1 
ATOM   6656 C  CE2 . TYR D 1 58  ? -63.215 86.672  2.845   1.00 57.19  ? 58  TYR D CE2 1 
ATOM   6657 C  CZ  . TYR D 1 58  ? -62.133 85.844  2.566   1.00 63.05  ? 58  TYR D CZ  1 
ATOM   6658 O  OH  . TYR D 1 58  ? -60.841 86.370  2.420   1.00 55.01  ? 58  TYR D OH  1 
ATOM   6659 N  N   . ASP D 1 59  ? -68.786 82.921  4.304   1.00 71.26  ? 59  ASP D N   1 
ATOM   6660 C  CA  . ASP D 1 59  ? -70.187 83.104  4.722   1.00 69.95  ? 59  ASP D CA  1 
ATOM   6661 C  C   . ASP D 1 59  ? -70.507 82.533  6.111   1.00 72.72  ? 59  ASP D C   1 
ATOM   6662 O  O   . ASP D 1 59  ? -71.667 82.559  6.547   1.00 69.57  ? 59  ASP D O   1 
ATOM   6663 C  CB  . ASP D 1 59  ? -71.151 82.520  3.675   1.00 69.52  ? 59  ASP D CB  1 
ATOM   6664 C  CG  . ASP D 1 59  ? -71.051 80.995  3.557   1.00 72.30  ? 59  ASP D CG  1 
ATOM   6665 O  OD1 . ASP D 1 59  ? -69.941 80.429  3.689   1.00 71.85  ? 59  ASP D OD1 1 
ATOM   6666 O  OD2 . ASP D 1 59  ? -72.098 80.356  3.333   1.00 65.59  ? 59  ASP D OD2 1 
ATOM   6667 N  N   . LYS D 1 60  ? -69.474 82.064  6.816   1.00 70.06  ? 60  LYS D N   1 
ATOM   6668 C  CA  . LYS D 1 60  ? -69.651 81.265  8.022   1.00 64.80  ? 60  LYS D CA  1 
ATOM   6669 C  C   . LYS D 1 60  ? -69.550 82.009  9.362   1.00 63.68  ? 60  LYS D C   1 
ATOM   6670 O  O   . LYS D 1 60  ? -68.471 82.089  9.972   1.00 56.75  ? 60  LYS D O   1 
ATOM   6671 C  CB  . LYS D 1 60  ? -68.668 80.087  7.992   1.00 69.66  ? 60  LYS D CB  1 
ATOM   6672 C  CG  . LYS D 1 60  ? -69.080 78.876  8.835   1.00 73.85  ? 60  LYS D CG  1 
ATOM   6673 C  CD  . LYS D 1 60  ? -67.940 77.870  8.998   1.00 70.02  ? 60  LYS D CD  1 
ATOM   6674 C  CE  . LYS D 1 60  ? -66.949 78.299  10.083  1.00 69.36  ? 60  LYS D CE  1 
ATOM   6675 N  NZ  . LYS D 1 60  ? -65.597 77.676  9.920   1.00 63.93  ? 60  LYS D NZ  1 
ATOM   6676 N  N   . LYS D 1 61  ? -70.695 82.511  9.822   1.00 63.69  ? 61  LYS D N   1 
ATOM   6677 C  CA  . LYS D 1 61  ? -70.862 83.091  11.169  1.00 68.41  ? 61  LYS D CA  1 
ATOM   6678 C  C   . LYS D 1 61  ? -70.016 82.414  12.247  1.00 69.42  ? 61  LYS D C   1 
ATOM   6679 O  O   . LYS D 1 61  ? -69.973 81.185  12.350  1.00 73.66  ? 61  LYS D O   1 
ATOM   6680 C  CB  . LYS D 1 61  ? -72.342 83.101  11.580  1.00 71.13  ? 61  LYS D CB  1 
ATOM   6681 C  CG  . LYS D 1 61  ? -73.180 84.193  10.915  1.00 71.16  ? 61  LYS D CG  1 
ATOM   6682 C  CD  . LYS D 1 61  ? -73.324 85.393  11.840  1.00 70.97  ? 61  LYS D CD  1 
ATOM   6683 C  CE  . LYS D 1 61  ? -73.488 86.695  11.073  1.00 59.73  ? 61  LYS D CE  1 
ATOM   6684 N  NZ  . LYS D 1 61  ? -72.897 87.771  11.895  1.00 56.92  ? 61  LYS D NZ  1 
ATOM   6685 N  N   . GLN D 1 62  ? -69.359 83.238  13.056  1.00 72.16  ? 62  GLN D N   1 
ATOM   6686 C  CA  . GLN D 1 62  ? -68.183 82.825  13.808  1.00 68.97  ? 62  GLN D CA  1 
ATOM   6687 C  C   . GLN D 1 62  ? -67.804 83.926  14.796  1.00 70.54  ? 62  GLN D C   1 
ATOM   6688 O  O   . GLN D 1 62  ? -68.183 85.087  14.616  1.00 67.36  ? 62  GLN D O   1 
ATOM   6689 C  CB  . GLN D 1 62  ? -67.028 82.637  12.819  1.00 69.49  ? 62  GLN D CB  1 
ATOM   6690 C  CG  . GLN D 1 62  ? -65.965 81.637  13.228  1.00 69.96  ? 62  GLN D CG  1 
ATOM   6691 C  CD  . GLN D 1 62  ? -65.159 81.122  12.050  1.00 69.42  ? 62  GLN D CD  1 
ATOM   6692 O  OE1 . GLN D 1 62  ? -64.090 80.540  12.229  1.00 75.44  ? 62  GLN D OE1 1 
ATOM   6693 N  NE2 . GLN D 1 62  ? -65.670 81.325  10.838  1.00 65.84  ? 62  GLN D NE2 1 
ATOM   6694 N  N   . THR D 1 63  ? -67.070 83.557  15.845  1.00 71.09  ? 63  THR D N   1 
ATOM   6695 C  CA  . THR D 1 63  ? -66.343 84.534  16.652  1.00 68.87  ? 63  THR D CA  1 
ATOM   6696 C  C   . THR D 1 63  ? -64.917 84.576  16.095  1.00 69.24  ? 63  THR D C   1 
ATOM   6697 O  O   . THR D 1 63  ? -64.525 83.702  15.300  1.00 63.56  ? 63  THR D O   1 
ATOM   6698 C  CB  . THR D 1 63  ? -66.352 84.190  18.165  1.00 74.54  ? 63  THR D CB  1 
ATOM   6699 O  OG1 . THR D 1 63  ? -65.810 82.879  18.374  1.00 66.40  ? 63  THR D OG1 1 
ATOM   6700 C  CG2 . THR D 1 63  ? -67.785 84.264  18.746  1.00 73.93  ? 63  THR D CG2 1 
ATOM   6701 N  N   . TRP D 1 64  ? -64.146 85.596  16.460  1.00 61.94  ? 64  TRP D N   1 
ATOM   6702 C  CA  . TRP D 1 64  ? -62.742 85.639  16.027  1.00 59.47  ? 64  TRP D CA  1 
ATOM   6703 C  C   . TRP D 1 64  ? -61.964 86.323  17.096  1.00 55.28  ? 64  TRP D C   1 
ATOM   6704 O  O   . TRP D 1 64  ? -62.534 87.131  17.825  1.00 62.69  ? 64  TRP D O   1 
ATOM   6705 C  CB  . TRP D 1 64  ? -62.540 86.387  14.703  1.00 53.25  ? 64  TRP D CB  1 
ATOM   6706 C  CG  . TRP D 1 64  ? -63.570 86.154  13.614  1.00 48.51  ? 64  TRP D CG  1 
ATOM   6707 C  CD1 . TRP D 1 64  ? -64.884 86.619  13.567  1.00 46.13  ? 64  TRP D CD1 1 
ATOM   6708 C  CD2 . TRP D 1 64  ? -63.383 85.428  12.342  1.00 46.24  ? 64  TRP D CD2 1 
ATOM   6709 N  NE1 . TRP D 1 64  ? -65.504 86.225  12.406  1.00 45.56  ? 64  TRP D NE1 1 
ATOM   6710 C  CE2 . TRP D 1 64  ? -64.661 85.507  11.630  1.00 45.77  ? 64  TRP D CE2 1 
ATOM   6711 C  CE3 . TRP D 1 64  ? -62.325 84.739  11.755  1.00 44.23  ? 64  TRP D CE3 1 
ATOM   6712 C  CZ2 . TRP D 1 64  ? -64.848 84.916  10.387  1.00 45.78  ? 64  TRP D CZ2 1 
ATOM   6713 C  CZ3 . TRP D 1 64  ? -62.529 84.148  10.505  1.00 46.51  ? 64  TRP D CZ3 1 
ATOM   6714 C  CH2 . TRP D 1 64  ? -63.759 84.236  9.839   1.00 48.78  ? 64  TRP D CH2 1 
ATOM   6715 N  N   . THR D 1 65  ? -60.670 86.013  17.201  1.00 54.38  ? 65  THR D N   1 
ATOM   6716 C  CA  . THR D 1 65  ? -59.743 86.829  17.975  1.00 58.22  ? 65  THR D CA  1 
ATOM   6717 C  C   . THR D 1 65  ? -59.470 88.118  17.174  1.00 63.43  ? 65  THR D C   1 
ATOM   6718 O  O   . THR D 1 65  ? -58.571 88.158  16.341  1.00 64.07  ? 65  THR D O   1 
ATOM   6719 C  CB  . THR D 1 65  ? -58.380 86.133  18.252  1.00 61.46  ? 65  THR D CB  1 
ATOM   6720 O  OG1 . THR D 1 65  ? -58.544 84.723  18.481  1.00 63.50  ? 65  THR D OG1 1 
ATOM   6721 C  CG2 . THR D 1 65  ? -57.684 86.765  19.464  1.00 64.45  ? 65  THR D CG2 1 
ATOM   6722 N  N   . VAL D 1 66  ? -60.274 89.154  17.394  1.00 67.36  ? 66  VAL D N   1 
ATOM   6723 C  CA  . VAL D 1 66  ? -59.898 90.495  16.967  1.00 63.88  ? 66  VAL D CA  1 
ATOM   6724 C  C   . VAL D 1 66  ? -59.002 91.053  18.060  1.00 61.77  ? 66  VAL D C   1 
ATOM   6725 O  O   . VAL D 1 66  ? -59.289 90.864  19.246  1.00 58.08  ? 66  VAL D O   1 
ATOM   6726 C  CB  . VAL D 1 66  ? -61.122 91.404  16.710  1.00 65.99  ? 66  VAL D CB  1 
ATOM   6727 C  CG1 . VAL D 1 66  ? -62.101 91.379  17.871  1.00 68.82  ? 66  VAL D CG1 1 
ATOM   6728 C  CG2 . VAL D 1 66  ? -60.684 92.833  16.429  1.00 68.66  ? 66  VAL D CG2 1 
ATOM   6729 N  N   . GLN D 1 67  ? -57.908 91.705  17.671  1.00 60.79  ? 67  GLN D N   1 
ATOM   6730 C  CA  . GLN D 1 67  ? -56.996 92.287  18.655  1.00 63.95  ? 67  GLN D CA  1 
ATOM   6731 C  C   . GLN D 1 67  ? -56.205 93.518  18.196  1.00 68.78  ? 67  GLN D C   1 
ATOM   6732 O  O   . GLN D 1 67  ? -56.137 93.821  17.001  1.00 69.84  ? 67  GLN D O   1 
ATOM   6733 C  CB  . GLN D 1 67  ? -56.041 91.220  19.187  1.00 61.60  ? 67  GLN D CB  1 
ATOM   6734 C  CG  . GLN D 1 67  ? -54.792 90.969  18.357  1.00 53.40  ? 67  GLN D CG  1 
ATOM   6735 C  CD  . GLN D 1 67  ? -54.347 89.537  18.529  1.00 48.20  ? 67  GLN D CD  1 
ATOM   6736 O  OE1 . GLN D 1 67  ? -55.165 88.681  18.871  1.00 52.68  ? 67  GLN D OE1 1 
ATOM   6737 N  NE2 . GLN D 1 67  ? -53.065 89.258  18.303  1.00 46.87  ? 67  GLN D NE2 1 
ATOM   6738 N  N   . ASN D 1 68  ? -55.631 94.221  19.177  1.00 64.05  ? 68  ASN D N   1 
ATOM   6739 C  CA  . ASN D 1 68  ? -54.687 95.299  18.951  1.00 61.04  ? 68  ASN D CA  1 
ATOM   6740 C  C   . ASN D 1 68  ? -53.277 94.749  18.921  1.00 60.91  ? 68  ASN D C   1 
ATOM   6741 O  O   . ASN D 1 68  ? -52.964 93.808  19.650  1.00 67.78  ? 68  ASN D O   1 
ATOM   6742 C  CB  . ASN D 1 68  ? -54.801 96.341  20.065  1.00 62.79  ? 68  ASN D CB  1 
ATOM   6743 C  CG  . ASN D 1 68  ? -54.199 97.683  19.681  1.00 62.47  ? 68  ASN D CG  1 
ATOM   6744 O  OD1 . ASN D 1 68  ? -53.253 97.761  18.886  1.00 61.16  ? 68  ASN D OD1 1 
ATOM   6745 N  ND2 . ASN D 1 68  ? -54.753 98.756  20.239  1.00 60.08  ? 68  ASN D ND2 1 
ATOM   6746 N  N   . ASN D 1 69  ? -52.426 95.360  18.094  1.00 62.57  ? 69  ASN D N   1 
ATOM   6747 C  CA  . ASN D 1 69  ? -51.039 94.918  17.878  1.00 59.44  ? 69  ASN D CA  1 
ATOM   6748 C  C   . ASN D 1 69  ? -50.027 96.066  17.876  1.00 56.49  ? 69  ASN D C   1 
ATOM   6749 O  O   . ASN D 1 69  ? -48.842 95.866  17.598  1.00 52.84  ? 69  ASN D O   1 
ATOM   6750 C  CB  . ASN D 1 69  ? -50.953 94.188  16.541  1.00 62.47  ? 69  ASN D CB  1 
ATOM   6751 C  CG  . ASN D 1 69  ? -51.153 95.129  15.352  1.00 74.36  ? 69  ASN D CG  1 
ATOM   6752 O  OD1 . ASN D 1 69  ? -52.034 96.001  15.374  1.00 61.24  ? 69  ASN D OD1 1 
ATOM   6753 N  ND2 . ASN D 1 69  ? -50.330 94.959  14.307  1.00 73.41  ? 69  ASN D ND2 1 
ATOM   6754 N  N   . GLY D 1 70  ? -50.503 97.273  18.171  1.00 56.80  ? 70  GLY D N   1 
ATOM   6755 C  CA  . GLY D 1 70  ? -49.665 98.462  18.147  1.00 57.75  ? 70  GLY D CA  1 
ATOM   6756 C  C   . GLY D 1 70  ? -49.696 99.244  16.838  1.00 60.15  ? 70  GLY D C   1 
ATOM   6757 O  O   . GLY D 1 70  ? -49.349 100.435 16.822  1.00 55.97  ? 70  GLY D O   1 
ATOM   6758 N  N   . HIS D 1 71  ? -50.109 98.593  15.745  1.00 55.57  ? 71  HIS D N   1 
ATOM   6759 C  CA  . HIS D 1 71  ? -50.159 99.245  14.420  1.00 51.91  ? 71  HIS D CA  1 
ATOM   6760 C  C   . HIS D 1 71  ? -51.530 99.284  13.811  1.00 50.31  ? 71  HIS D C   1 
ATOM   6761 O  O   . HIS D 1 71  ? -51.821 100.131 12.965  1.00 47.79  ? 71  HIS D O   1 
ATOM   6762 C  CB  . HIS D 1 71  ? -49.175 98.571  13.479  1.00 58.49  ? 71  HIS D CB  1 
ATOM   6763 C  CG  . HIS D 1 71  ? -47.807 98.368  14.090  1.00 59.29  ? 71  HIS D CG  1 
ATOM   6764 N  ND1 . HIS D 1 71  ? -47.014 99.402  14.450  1.00 63.28  ? 71  HIS D ND1 1 
ATOM   6765 C  CD2 . HIS D 1 71  ? -47.109 97.204  14.408  1.00 61.84  ? 71  HIS D CD2 1 
ATOM   6766 C  CE1 . HIS D 1 71  ? -45.865 98.926  14.971  1.00 60.77  ? 71  HIS D CE1 1 
ATOM   6767 N  NE2 . HIS D 1 71  ? -45.921 97.579  14.942  1.00 62.83  ? 71  HIS D NE2 1 
ATOM   6768 N  N   . SER D 1 72  ? -52.412 98.397  14.268  1.00 46.30  ? 72  SER D N   1 
ATOM   6769 C  CA  . SER D 1 72  ? -53.691 98.202  13.606  1.00 46.45  ? 72  SER D CA  1 
ATOM   6770 C  C   . SER D 1 72  ? -54.735 97.497  14.498  1.00 47.78  ? 72  SER D C   1 
ATOM   6771 O  O   . SER D 1 72  ? -54.437 97.067  15.617  1.00 59.43  ? 72  SER D O   1 
ATOM   6772 C  CB  . SER D 1 72  ? -53.434 97.413  12.301  1.00 40.57  ? 72  SER D CB  1 
ATOM   6773 O  OG  . SER D 1 72  ? -54.555 97.469  11.455  1.00 40.29  ? 72  SER D OG  1 
ATOM   6774 N  N   . VAL D 1 73  ? -55.970 97.389  14.029  1.00 52.71  ? 73  VAL D N   1 
ATOM   6775 C  CA  . VAL D 1 73  ? -56.856 96.370  14.585  1.00 52.98  ? 73  VAL D CA  1 
ATOM   6776 C  C   . VAL D 1 73  ? -56.767 95.087  13.734  1.00 57.91  ? 73  VAL D C   1 
ATOM   6777 O  O   . VAL D 1 73  ? -57.352 95.008  12.656  1.00 55.81  ? 73  VAL D O   1 
ATOM   6778 C  CB  . VAL D 1 73  ? -58.300 96.858  14.717  1.00 55.07  ? 73  VAL D CB  1 
ATOM   6779 C  CG1 . VAL D 1 73  ? -58.807 97.446  13.415  1.00 55.15  ? 73  VAL D CG1 1 
ATOM   6780 C  CG2 . VAL D 1 73  ? -59.193 95.720  15.183  1.00 60.08  ? 73  VAL D CG2 1 
ATOM   6781 N  N   . MET D 1 74  ? -56.012 94.097  14.218  1.00 63.27  ? 74  MET D N   1 
ATOM   6782 C  CA  . MET D 1 74  ? -55.796 92.829  13.496  1.00 59.44  ? 74  MET D CA  1 
ATOM   6783 C  C   . MET D 1 74  ? -56.604 91.640  14.026  1.00 67.04  ? 74  MET D C   1 
ATOM   6784 O  O   . MET D 1 74  ? -56.294 91.062  15.089  1.00 64.62  ? 74  MET D O   1 
ATOM   6785 C  CB  . MET D 1 74  ? -54.313 92.464  13.453  1.00 58.13  ? 74  MET D CB  1 
ATOM   6786 C  CG  . MET D 1 74  ? -54.025 91.112  12.803  1.00 53.18  ? 74  MET D CG  1 
ATOM   6787 S  SD  . MET D 1 74  ? -52.351 90.587  13.142  1.00 63.22  ? 74  MET D SD  1 
ATOM   6788 C  CE  . MET D 1 74  ? -51.491 91.241  11.716  1.00 60.39  ? 74  MET D CE  1 
ATOM   6789 N  N   . MET D 1 75  ? -57.624 91.260  13.262  1.00 68.46  ? 75  MET D N   1 
ATOM   6790 C  CA  . MET D 1 75  ? -58.392 90.061  13.570  1.00 62.40  ? 75  MET D CA  1 
ATOM   6791 C  C   . MET D 1 75  ? -57.894 88.832  12.789  1.00 62.06  ? 75  MET D C   1 
ATOM   6792 O  O   . MET D 1 75  ? -57.699 88.879  11.563  1.00 55.64  ? 75  MET D O   1 
ATOM   6793 C  CB  . MET D 1 75  ? -59.889 90.303  13.400  1.00 58.69  ? 75  MET D CB  1 
ATOM   6794 C  CG  . MET D 1 75  ? -60.332 90.569  11.992  1.00 56.83  ? 75  MET D CG  1 
ATOM   6795 S  SD  . MET D 1 75  ? -62.114 90.649  11.862  1.00 63.88  ? 75  MET D SD  1 
ATOM   6796 C  CE  . MET D 1 75  ? -62.488 88.922  11.573  1.00 59.78  ? 75  MET D CE  1 
ATOM   6797 N  N   . LEU D 1 76  ? -57.701 87.741  13.534  1.00 62.24  ? 76  LEU D N   1 
ATOM   6798 C  CA  . LEU D 1 76  ? -57.019 86.545  13.057  1.00 57.35  ? 76  LEU D CA  1 
ATOM   6799 C  C   . LEU D 1 76  ? -57.923 85.566  12.295  1.00 57.75  ? 76  LEU D C   1 
ATOM   6800 O  O   . LEU D 1 76  ? -59.098 85.350  12.644  1.00 52.69  ? 76  LEU D O   1 
ATOM   6801 C  CB  . LEU D 1 76  ? -56.288 85.859  14.219  1.00 60.54  ? 76  LEU D CB  1 
ATOM   6802 C  CG  . LEU D 1 76  ? -54.853 86.346  14.484  1.00 63.23  ? 76  LEU D CG  1 
ATOM   6803 C  CD1 . LEU D 1 76  ? -54.522 86.418  15.970  1.00 62.65  ? 76  LEU D CD1 1 
ATOM   6804 C  CD2 . LEU D 1 76  ? -53.826 85.501  13.722  1.00 62.38  ? 76  LEU D CD2 1 
ATOM   6805 N  N   . LEU D 1 77  ? -57.373 85.030  11.241  1.00 55.35  ? 77  LEU D N   1 
ATOM   6806 C  CA  . LEU D 1 77  ? -58.150 84.139  10.345  1.00 65.31  ? 77  LEU D CA  1 
ATOM   6807 C  C   . LEU D 1 77  ? -57.482 82.910  9.674   1.00 71.79  ? 77  LEU D C   1 
ATOM   6808 O  O   . LEU D 1 77  ? -58.202 82.096  9.081   1.00 77.12  ? 77  LEU D O   1 
ATOM   6809 C  CB  . LEU D 1 77  ? -58.855 84.952  9.251   1.00 66.94  ? 77  LEU D CB  1 
ATOM   6810 C  CG  . LEU D 1 77  ? -58.815 86.475  9.313   1.00 61.64  ? 77  LEU D CG  1 
ATOM   6811 C  CD1 . LEU D 1 77  ? -58.427 87.062  7.966   1.00 60.02  ? 77  LEU D CD1 1 
ATOM   6812 C  CD2 . LEU D 1 77  ? -60.170 87.002  9.757   1.00 64.02  ? 77  LEU D CD2 1 
ATOM   6813 N  N   . GLU D 1 78  ? -56.162 82.790  9.772   1.00 76.48  ? 78  GLU D N   1 
ATOM   6814 C  CA  . GLU D 1 78  ? -55.442 81.707  9.113   1.00 75.16  ? 78  GLU D CA  1 
ATOM   6815 C  C   . GLU D 1 78  ? -56.066 80.355  9.442   1.00 72.96  ? 78  GLU D C   1 
ATOM   6816 O  O   . GLU D 1 78  ? -56.740 80.203  10.461  1.00 73.12  ? 78  GLU D O   1 
ATOM   6817 C  CB  . GLU D 1 78  ? -53.967 81.718  9.519   1.00 76.60  ? 78  GLU D CB  1 
ATOM   6818 C  CG  . GLU D 1 78  ? -53.476 80.406  10.108  1.00 79.77  ? 78  GLU D CG  1 
ATOM   6819 C  CD  . GLU D 1 78  ? -52.451 80.608  11.207  1.00 84.32  ? 78  GLU D CD  1 
ATOM   6820 O  OE1 . GLU D 1 78  ? -51.631 79.693  11.433  1.00 86.30  ? 78  GLU D OE1 1 
ATOM   6821 O  OE2 . GLU D 1 78  ? -52.466 81.681  11.845  1.00 92.14  ? 78  GLU D OE2 1 
ATOM   6822 N  N   . ASN D 1 79  ? -55.839 79.375  8.573   1.00 65.44  ? 79  ASN D N   1 
ATOM   6823 C  CA  . ASN D 1 79  ? -56.381 78.036  8.769   1.00 64.58  ? 79  ASN D CA  1 
ATOM   6824 C  C   . ASN D 1 79  ? -57.890 78.054  8.992   1.00 65.61  ? 79  ASN D C   1 
ATOM   6825 O  O   . ASN D 1 79  ? -58.477 77.059  9.417   1.00 62.68  ? 79  ASN D O   1 
ATOM   6826 C  CB  . ASN D 1 79  ? -55.685 77.342  9.942   1.00 65.74  ? 79  ASN D CB  1 
ATOM   6827 C  CG  . ASN D 1 79  ? -54.638 76.344  9.489   1.00 71.68  ? 79  ASN D CG  1 
ATOM   6828 O  OD1 . ASN D 1 79  ? -54.786 75.698  8.451   1.00 72.96  ? 79  ASN D OD1 1 
ATOM   6829 N  ND2 . ASN D 1 79  ? -53.570 76.212  10.268  1.00 72.92  ? 79  ASN D ND2 1 
ATOM   6830 N  N   . LYS D 1 80  ? -58.511 79.192  8.701   1.00 63.70  ? 80  LYS D N   1 
ATOM   6831 C  CA  . LYS D 1 80  ? -59.957 79.347  8.868   1.00 58.49  ? 80  LYS D CA  1 
ATOM   6832 C  C   . LYS D 1 80  ? -60.657 79.730  7.564   1.00 55.75  ? 80  LYS D C   1 
ATOM   6833 O  O   . LYS D 1 80  ? -61.881 79.559  7.439   1.00 56.21  ? 80  LYS D O   1 
ATOM   6834 C  CB  . LYS D 1 80  ? -60.265 80.466  9.870   1.00 65.34  ? 80  LYS D CB  1 
ATOM   6835 C  CG  . LYS D 1 80  ? -60.440 80.084  11.319  1.00 62.43  ? 80  LYS D CG  1 
ATOM   6836 C  CD  . LYS D 1 80  ? -61.354 81.122  11.955  1.00 65.92  ? 80  LYS D CD  1 
ATOM   6837 C  CE  . LYS D 1 80  ? -61.059 81.351  13.430  1.00 69.35  ? 80  LYS D CE  1 
ATOM   6838 N  NZ  . LYS D 1 80  ? -62.058 82.278  14.034  1.00 70.98  ? 80  LYS D NZ  1 
ATOM   6839 N  N   . ALA D 1 81  ? -59.916 80.304  6.615   1.00 51.47  ? 81  ALA D N   1 
ATOM   6840 C  CA  . ALA D 1 81  ? -60.561 80.967  5.472   1.00 46.65  ? 81  ALA D CA  1 
ATOM   6841 C  C   . ALA D 1 81  ? -59.772 80.781  4.200   1.00 41.89  ? 81  ALA D C   1 
ATOM   6842 O  O   . ALA D 1 81  ? -58.554 80.538  4.242   1.00 41.23  ? 81  ALA D O   1 
ATOM   6843 C  CB  . ALA D 1 81  ? -60.728 82.456  5.757   1.00 47.45  ? 81  ALA D CB  1 
ATOM   6844 N  N   . SER D 1 82  ? -60.432 80.929  3.066   1.00 35.75  ? 82  SER D N   1 
ATOM   6845 C  CA  . SER D 1 82  ? -59.696 80.603  1.839   1.00 42.09  ? 82  SER D CA  1 
ATOM   6846 C  C   . SER D 1 82  ? -60.234 81.281  0.621   1.00 39.26  ? 82  SER D C   1 
ATOM   6847 O  O   . SER D 1 82  ? -61.445 81.479  0.505   1.00 37.96  ? 82  SER D O   1 
ATOM   6848 C  CB  . SER D 1 82  ? -59.745 79.083  1.600   1.00 46.49  ? 82  SER D CB  1 
ATOM   6849 O  OG  . SER D 1 82  ? -61.056 78.697  1.172   1.00 48.96  ? 82  SER D OG  1 
ATOM   6850 N  N   . ILE D 1 83  ? -59.356 81.593  -0.331  1.00 37.27  ? 83  ILE D N   1 
ATOM   6851 C  CA  . ILE D 1 83  ? -59.836 82.231  -1.542  1.00 37.50  ? 83  ILE D CA  1 
ATOM   6852 C  C   . ILE D 1 83  ? -59.232 81.564  -2.751  1.00 38.01  ? 83  ILE D C   1 
ATOM   6853 O  O   . ILE D 1 83  ? -58.113 81.086  -2.689  1.00 39.16  ? 83  ILE D O   1 
ATOM   6854 C  CB  . ILE D 1 83  ? -59.514 83.770  -1.612  1.00 36.12  ? 83  ILE D CB  1 
ATOM   6855 C  CG1 . ILE D 1 83  ? -58.015 84.062  -1.746  1.00 32.76  ? 83  ILE D CG1 1 
ATOM   6856 C  CG2 . ILE D 1 83  ? -60.115 84.518  -0.423  1.00 41.39  ? 83  ILE D CG2 1 
ATOM   6857 C  CD1 . ILE D 1 83  ? -57.676 85.544  -1.783  1.00 34.88  ? 83  ILE D CD1 1 
ATOM   6858 N  N   . SER D 1 84  ? -59.958 81.602  -3.858  1.00 37.84  ? 84  SER D N   1 
ATOM   6859 C  CA  . SER D 1 84  ? -59.376 81.237  -5.134  1.00 42.67  ? 84  SER D CA  1 
ATOM   6860 C  C   . SER D 1 84  ? -60.166 82.012  -6.175  1.00 47.01  ? 84  SER D C   1 
ATOM   6861 O  O   . SER D 1 84  ? -61.175 82.670  -5.842  1.00 50.70  ? 84  SER D O   1 
ATOM   6862 C  CB  . SER D 1 84  ? -59.511 79.712  -5.367  1.00 43.50  ? 84  SER D CB  1 
ATOM   6863 O  OG  . SER D 1 84  ? -60.863 79.391  -5.581  1.00 40.30  ? 84  SER D OG  1 
ATOM   6864 N  N   . GLY D 1 85  ? -59.722 81.913  -7.422  1.00 40.83  ? 85  GLY D N   1 
ATOM   6865 C  CA  . GLY D 1 85  ? -60.324 82.618  -8.527  1.00 44.07  ? 85  GLY D CA  1 
ATOM   6866 C  C   . GLY D 1 85  ? -59.565 83.909  -8.661  1.00 39.26  ? 85  GLY D C   1 
ATOM   6867 O  O   . GLY D 1 85  ? -58.494 84.054  -8.064  1.00 39.57  ? 85  GLY D O   1 
ATOM   6868 N  N   . GLY D 1 86  ? -60.102 84.826  -9.456  1.00 43.14  ? 86  GLY D N   1 
ATOM   6869 C  CA  . GLY D 1 86  ? -59.504 86.168  -9.626  1.00 40.14  ? 86  GLY D CA  1 
ATOM   6870 C  C   . GLY D 1 86  ? -58.096 86.181  -10.196 1.00 43.35  ? 86  GLY D C   1 
ATOM   6871 O  O   . GLY D 1 86  ? -57.336 87.109  -9.936  1.00 41.35  ? 86  GLY D O   1 
ATOM   6872 N  N   . GLY D 1 87  ? -57.719 85.141  -10.953 1.00 48.99  ? 87  GLY D N   1 
ATOM   6873 C  CA  . GLY D 1 87  ? -56.415 85.115  -11.671 1.00 38.88  ? 87  GLY D CA  1 
ATOM   6874 C  C   . GLY D 1 87  ? -55.259 84.651  -10.823 1.00 38.79  ? 87  GLY D C   1 
ATOM   6875 O  O   . GLY D 1 87  ? -54.092 84.795  -11.192 1.00 37.65  ? 87  GLY D O   1 
ATOM   6876 N  N   . LEU D 1 88  ? -55.610 84.100  -9.669  1.00 41.22  ? 88  LEU D N   1 
ATOM   6877 C  CA  . LEU D 1 88  ? -54.673 83.646  -8.683  1.00 45.73  ? 88  LEU D CA  1 
ATOM   6878 C  C   . LEU D 1 88  ? -54.188 82.262  -9.095  1.00 53.60  ? 88  LEU D C   1 
ATOM   6879 O  O   . LEU D 1 88  ? -55.014 81.415  -9.450  1.00 51.63  ? 88  LEU D O   1 
ATOM   6880 C  CB  . LEU D 1 88  ? -55.383 83.556  -7.314  1.00 48.32  ? 88  LEU D CB  1 
ATOM   6881 C  CG  . LEU D 1 88  ? -55.572 84.798  -6.408  1.00 48.67  ? 88  LEU D CG  1 
ATOM   6882 C  CD1 . LEU D 1 88  ? -56.391 84.463  -5.165  1.00 45.66  ? 88  LEU D CD1 1 
ATOM   6883 C  CD2 . LEU D 1 88  ? -54.219 85.366  -6.010  1.00 48.54  ? 88  LEU D CD2 1 
ATOM   6884 N  N   . PRO D 1 89  ? -52.859 82.024  -9.051  1.00 57.54  ? 89  PRO D N   1 
ATOM   6885 C  CA  . PRO D 1 89  ? -52.323 80.675  -9.292  1.00 62.66  ? 89  PRO D CA  1 
ATOM   6886 C  C   . PRO D 1 89  ? -53.050 79.485  -8.648  1.00 65.04  ? 89  PRO D C   1 
ATOM   6887 O  O   . PRO D 1 89  ? -53.659 78.695  -9.359  1.00 68.46  ? 89  PRO D O   1 
ATOM   6888 C  CB  . PRO D 1 89  ? -50.920 80.747  -8.678  1.00 58.71  ? 89  PRO D CB  1 
ATOM   6889 C  CG  . PRO D 1 89  ? -50.522 82.183  -8.836  1.00 58.46  ? 89  PRO D CG  1 
ATOM   6890 C  CD  . PRO D 1 89  ? -51.775 83.022  -8.956  1.00 57.30  ? 89  PRO D CD  1 
ATOM   6891 N  N   . ALA D 1 90  ? -53.000 79.386  -7.324  1.00 67.09  ? 90  ALA D N   1 
ATOM   6892 C  CA  . ALA D 1 90  ? -53.663 78.325  -6.586  1.00 64.82  ? 90  ALA D CA  1 
ATOM   6893 C  C   . ALA D 1 90  ? -54.743 79.006  -5.759  1.00 65.31  ? 90  ALA D C   1 
ATOM   6894 O  O   . ALA D 1 90  ? -55.029 80.180  -5.963  1.00 64.63  ? 90  ALA D O   1 
ATOM   6895 C  CB  . ALA D 1 90  ? -52.712 77.566  -5.680  1.00 68.18  ? 90  ALA D CB  1 
ATOM   6896 N  N   . PRO D 1 91  ? -55.395 78.252  -4.857  1.00 66.50  ? 91  PRO D N   1 
ATOM   6897 C  CA  . PRO D 1 91  ? -56.103 78.930  -3.778  1.00 60.79  ? 91  PRO D CA  1 
ATOM   6898 C  C   . PRO D 1 91  ? -55.118 79.522  -2.771  1.00 58.43  ? 91  PRO D C   1 
ATOM   6899 O  O   . PRO D 1 91  ? -53.959 79.088  -2.715  1.00 58.44  ? 91  PRO D O   1 
ATOM   6900 C  CB  . PRO D 1 91  ? -56.913 77.801  -3.136  1.00 62.68  ? 91  PRO D CB  1 
ATOM   6901 C  CG  . PRO D 1 91  ? -57.166 76.857  -4.263  1.00 62.70  ? 91  PRO D CG  1 
ATOM   6902 C  CD  . PRO D 1 91  ? -55.860 76.859  -5.011  1.00 64.85  ? 91  PRO D CD  1 
ATOM   6903 N  N   . TYR D 1 92  ? -55.576 80.519  -2.009  1.00 48.89  ? 92  TYR D N   1 
ATOM   6904 C  CA  . TYR D 1 92  ? -54.769 81.173  -0.991  1.00 47.03  ? 92  TYR D CA  1 
ATOM   6905 C  C   . TYR D 1 92  ? -55.383 81.028  0.405   1.00 46.96  ? 92  TYR D C   1 
ATOM   6906 O  O   . TYR D 1 92  ? -56.608 81.157  0.563   1.00 50.33  ? 92  TYR D O   1 
ATOM   6907 C  CB  . TYR D 1 92  ? -54.591 82.652  -1.361  1.00 49.11  ? 92  TYR D CB  1 
ATOM   6908 C  CG  . TYR D 1 92  ? -53.481 82.880  -2.353  1.00 45.72  ? 92  TYR D CG  1 
ATOM   6909 C  CD1 . TYR D 1 92  ? -53.617 82.483  -3.685  1.00 45.60  ? 92  TYR D CD1 1 
ATOM   6910 C  CD2 . TYR D 1 92  ? -52.276 83.450  -1.965  1.00 43.57  ? 92  TYR D CD2 1 
ATOM   6911 C  CE1 . TYR D 1 92  ? -52.599 82.657  -4.596  1.00 34.30  ? 92  TYR D CE1 1 
ATOM   6912 C  CE2 . TYR D 1 92  ? -51.259 83.629  -2.890  1.00 45.47  ? 92  TYR D CE2 1 
ATOM   6913 C  CZ  . TYR D 1 92  ? -51.440 83.214  -4.203  1.00 38.36  ? 92  TYR D CZ  1 
ATOM   6914 O  OH  . TYR D 1 92  ? -50.449 83.385  -5.134  1.00 39.49  ? 92  TYR D OH  1 
ATOM   6915 N  N   . GLN D 1 93  ? -54.554 80.751  1.416   1.00 46.51  ? 93  GLN D N   1 
ATOM   6916 C  CA  . GLN D 1 93  ? -55.062 80.700  2.826   1.00 53.73  ? 93  GLN D CA  1 
ATOM   6917 C  C   . GLN D 1 93  ? -54.989 81.986  3.660   1.00 49.11  ? 93  GLN D C   1 
ATOM   6918 O  O   . GLN D 1 93  ? -53.953 82.634  3.692   1.00 51.14  ? 93  GLN D O   1 
ATOM   6919 C  CB  . GLN D 1 93  ? -54.394 79.578  3.608   1.00 58.76  ? 93  GLN D CB  1 
ATOM   6920 C  CG  . GLN D 1 93  ? -55.352 78.465  3.966   1.00 59.58  ? 93  GLN D CG  1 
ATOM   6921 C  CD  . GLN D 1 93  ? -54.776 77.136  3.574   1.00 63.84  ? 93  GLN D CD  1 
ATOM   6922 O  OE1 . GLN D 1 93  ? -54.950 76.141  4.277   1.00 66.91  ? 93  GLN D OE1 1 
ATOM   6923 N  NE2 . GLN D 1 93  ? -54.063 77.111  2.446   1.00 59.00  ? 93  GLN D NE2 1 
ATOM   6924 N  N   . ALA D 1 94  ? -56.063 82.281  4.396   1.00 46.67  ? 94  ALA D N   1 
ATOM   6925 C  CA  . ALA D 1 94  ? -56.350 83.639  4.920   1.00 46.02  ? 94  ALA D CA  1 
ATOM   6926 C  C   . ALA D 1 94  ? -55.590 84.123  6.165   1.00 50.01  ? 94  ALA D C   1 
ATOM   6927 O  O   . ALA D 1 94  ? -56.226 84.467  7.177   1.00 47.52  ? 94  ALA D O   1 
ATOM   6928 C  CB  . ALA D 1 94  ? -57.855 83.792  5.135   1.00 45.79  ? 94  ALA D CB  1 
ATOM   6929 N  N   . LYS D 1 95  ? -54.251 84.182  6.080   1.00 46.56  ? 95  LYS D N   1 
ATOM   6930 C  CA  . LYS D 1 95  ? -53.385 84.429  7.232   1.00 48.99  ? 95  LYS D CA  1 
ATOM   6931 C  C   . LYS D 1 95  ? -53.934 85.416  8.294   1.00 54.22  ? 95  LYS D C   1 
ATOM   6932 O  O   . LYS D 1 95  ? -54.003 85.080  9.474   1.00 56.92  ? 95  LYS D O   1 
ATOM   6933 C  CB  . LYS D 1 95  ? -51.976 84.838  6.778   1.00 51.36  ? 95  LYS D CB  1 
ATOM   6934 C  CG  . LYS D 1 95  ? -51.089 83.701  6.285   1.00 52.12  ? 95  LYS D CG  1 
ATOM   6935 C  CD  . LYS D 1 95  ? -50.444 82.907  7.414   1.00 56.16  ? 95  LYS D CD  1 
ATOM   6936 C  CE  . LYS D 1 95  ? -49.936 81.567  6.887   1.00 61.19  ? 95  LYS D CE  1 
ATOM   6937 N  NZ  . LYS D 1 95  ? -49.338 80.712  7.945   1.00 58.22  ? 95  LYS D NZ  1 
ATOM   6938 N  N   . GLN D 1 96  ? -54.306 86.629  7.869   1.00 60.31  ? 96  GLN D N   1 
ATOM   6939 C  CA  . GLN D 1 96  ? -54.917 87.641  8.764   1.00 55.47  ? 96  GLN D CA  1 
ATOM   6940 C  C   . GLN D 1 96  ? -55.598 88.762  7.976   1.00 51.06  ? 96  GLN D C   1 
ATOM   6941 O  O   . GLN D 1 96  ? -55.288 88.935  6.795   1.00 43.49  ? 96  GLN D O   1 
ATOM   6942 C  CB  . GLN D 1 96  ? -53.873 88.215  9.748   1.00 52.65  ? 96  GLN D CB  1 
ATOM   6943 C  CG  . GLN D 1 96  ? -52.524 88.573  9.137   1.00 54.20  ? 96  GLN D CG  1 
ATOM   6944 C  CD  . GLN D 1 96  ? -52.403 90.064  8.901   1.00 54.07  ? 96  GLN D CD  1 
ATOM   6945 O  OE1 . GLN D 1 96  ? -53.347 90.806  9.134   1.00 53.37  ? 96  GLN D OE1 1 
ATOM   6946 N  NE2 . GLN D 1 96  ? -51.237 90.509  8.455   1.00 54.83  ? 96  GLN D NE2 1 
ATOM   6947 N  N   . LEU D 1 97  ? -56.508 89.495  8.640   1.00 46.68  ? 97  LEU D N   1 
ATOM   6948 C  CA  . LEU D 1 97  ? -57.139 90.732  8.138   1.00 52.04  ? 97  LEU D CA  1 
ATOM   6949 C  C   . LEU D 1 97  ? -56.867 91.972  9.042   1.00 54.54  ? 97  LEU D C   1 
ATOM   6950 O  O   . LEU D 1 97  ? -57.086 91.888  10.249  1.00 57.27  ? 97  LEU D O   1 
ATOM   6951 C  CB  . LEU D 1 97  ? -58.653 90.514  8.003   1.00 51.24  ? 97  LEU D CB  1 
ATOM   6952 C  CG  . LEU D 1 97  ? -59.627 91.685  7.816   1.00 51.56  ? 97  LEU D CG  1 
ATOM   6953 C  CD1 . LEU D 1 97  ? -60.934 91.206  7.220   1.00 48.49  ? 97  LEU D CD1 1 
ATOM   6954 C  CD2 . LEU D 1 97  ? -59.927 92.426  9.114   1.00 52.11  ? 97  LEU D CD2 1 
ATOM   6955 N  N   . HIS D 1 98  ? -56.433 93.111  8.461   1.00 53.14  ? 98  HIS D N   1 
ATOM   6956 C  CA  . HIS D 1 98  ? -56.177 94.380  9.219   1.00 46.20  ? 98  HIS D CA  1 
ATOM   6957 C  C   . HIS D 1 98  ? -56.517 95.663  8.486   1.00 43.47  ? 98  HIS D C   1 
ATOM   6958 O  O   . HIS D 1 98  ? -56.756 95.647  7.285   1.00 39.56  ? 98  HIS D O   1 
ATOM   6959 C  CB  . HIS D 1 98  ? -54.748 94.430  9.753   1.00 45.47  ? 98  HIS D CB  1 
ATOM   6960 C  CG  . HIS D 1 98  ? -53.692 94.685  8.701   1.00 50.16  ? 98  HIS D CG  1 
ATOM   6961 N  ND1 . HIS D 1 98  ? -53.220 93.713  7.898   1.00 49.52  ? 98  HIS D ND1 1 
ATOM   6962 C  CD2 . HIS D 1 98  ? -52.970 95.849  8.378   1.00 47.98  ? 98  HIS D CD2 1 
ATOM   6963 C  CE1 . HIS D 1 98  ? -52.268 94.221  7.084   1.00 48.77  ? 98  HIS D CE1 1 
ATOM   6964 N  NE2 . HIS D 1 98  ? -52.120 95.533  7.380   1.00 46.75  ? 98  HIS D NE2 1 
ATOM   6965 N  N   . LEU D 1 99  ? -56.565 96.788  9.206   1.00 42.60  ? 99  LEU D N   1 
ATOM   6966 C  CA  . LEU D 1 99  ? -56.952 98.076  8.598   1.00 36.76  ? 99  LEU D CA  1 
ATOM   6967 C  C   . LEU D 1 99  ? -55.944 99.180  8.766   1.00 36.45  ? 99  LEU D C   1 
ATOM   6968 O  O   . LEU D 1 99  ? -55.096 99.147  9.656   1.00 39.26  ? 99  LEU D O   1 
ATOM   6969 C  CB  . LEU D 1 99  ? -58.368 98.545  9.008   1.00 36.72  ? 99  LEU D CB  1 
ATOM   6970 C  CG  . LEU D 1 99  ? -59.526 97.716  8.428   1.00 37.64  ? 99  LEU D CG  1 
ATOM   6971 C  CD1 . LEU D 1 99  ? -59.816 96.492  9.285   1.00 36.88  ? 99  LEU D CD1 1 
ATOM   6972 C  CD2 . LEU D 1 99  ? -60.799 98.493  8.199   1.00 37.14  ? 99  LEU D CD2 1 
ATOM   6973 N  N   . HIS D 1 100 ? -56.023 100.131 7.830   1.00 37.08  ? 100 HIS D N   1 
ATOM   6974 C  CA  . HIS D 1 100 ? -55.280 101.374 7.840   1.00 31.94  ? 100 HIS D CA  1 
ATOM   6975 C  C   . HIS D 1 100 ? -56.319 102.434 7.781   1.00 33.57  ? 100 HIS D C   1 
ATOM   6976 O  O   . HIS D 1 100 ? -57.337 102.253 7.082   1.00 34.06  ? 100 HIS D O   1 
ATOM   6977 C  CB  . HIS D 1 100 ? -54.371 101.461 6.624   1.00 27.91  ? 100 HIS D CB  1 
ATOM   6978 C  CG  . HIS D 1 100 ? -53.291 100.385 6.596   1.00 26.09  ? 100 HIS D CG  1 
ATOM   6979 N  ND1 . HIS D 1 100 ? -52.068 100.567 7.124   1.00 26.08  ? 100 HIS D ND1 1 
ATOM   6980 C  CD2 . HIS D 1 100 ? -53.301 99.085  6.092   1.00 23.90  ? 100 HIS D CD2 1 
ATOM   6981 C  CE1 . HIS D 1 100 ? -51.322 99.440  6.961   1.00 24.25  ? 100 HIS D CE1 1 
ATOM   6982 N  NE2 . HIS D 1 100 ? -52.063 98.555  6.307   1.00 21.57  ? 100 HIS D NE2 1 
ATOM   6983 N  N   . TRP D 1 101 ? -56.108 103.551 8.509   1.00 34.75  ? 101 TRP D N   1 
ATOM   6984 C  CA  . TRP D 1 101 ? -57.104 104.636 8.535   1.00 34.81  ? 101 TRP D CA  1 
ATOM   6985 C  C   . TRP D 1 101 ? -56.640 105.998 9.047   1.00 32.20  ? 101 TRP D C   1 
ATOM   6986 O  O   . TRP D 1 101 ? -55.584 106.137 9.624   1.00 31.66  ? 101 TRP D O   1 
ATOM   6987 C  CB  . TRP D 1 101 ? -58.331 104.185 9.325   1.00 33.34  ? 101 TRP D CB  1 
ATOM   6988 C  CG  . TRP D 1 101 ? -58.037 103.973 10.785  1.00 40.72  ? 101 TRP D CG  1 
ATOM   6989 C  CD1 . TRP D 1 101 ? -57.927 104.939 11.767  1.00 40.59  ? 101 TRP D CD1 1 
ATOM   6990 C  CD2 . TRP D 1 101 ? -57.781 102.694 11.489  1.00 45.60  ? 101 TRP D CD2 1 
ATOM   6991 N  NE1 . TRP D 1 101 ? -57.641 104.368 12.982  1.00 42.70  ? 101 TRP D NE1 1 
ATOM   6992 C  CE2 . TRP D 1 101 ? -57.556 103.042 12.892  1.00 43.12  ? 101 TRP D CE2 1 
ATOM   6993 C  CE3 . TRP D 1 101 ? -57.755 101.354 11.113  1.00 49.71  ? 101 TRP D CE3 1 
ATOM   6994 C  CZ2 . TRP D 1 101 ? -57.288 102.090 13.850  1.00 45.13  ? 101 TRP D CZ2 1 
ATOM   6995 C  CZ3 . TRP D 1 101 ? -57.495 100.399 12.094  1.00 48.57  ? 101 TRP D CZ3 1 
ATOM   6996 C  CH2 . TRP D 1 101 ? -57.259 100.758 13.428  1.00 46.20  ? 101 TRP D CH2 1 
ATOM   6997 N  N   . SER D 1 102 ? -57.480 107.007 8.868   1.00 38.75  ? 102 SER D N   1 
ATOM   6998 C  CA  . SER D 1 102 ? -57.249 108.335 9.467   1.00 41.57  ? 102 SER D CA  1 
ATOM   6999 C  C   . SER D 1 102 ? -58.550 108.913 10.056  1.00 47.07  ? 102 SER D C   1 
ATOM   7000 O  O   . SER D 1 102 ? -59.605 108.277 9.967   1.00 46.86  ? 102 SER D O   1 
ATOM   7001 C  CB  . SER D 1 102 ? -56.653 109.291 8.416   1.00 40.73  ? 102 SER D CB  1 
ATOM   7002 O  OG  . SER D 1 102 ? -56.151 110.459 9.050   1.00 38.27  ? 102 SER D OG  1 
ATOM   7003 N  N   . ASP D 1 103 ? -58.477 110.114 10.649  1.00 51.55  ? 103 ASP D N   1 
ATOM   7004 C  CA  . ASP D 1 103 ? -59.675 110.816 11.149  1.00 53.10  ? 103 ASP D CA  1 
ATOM   7005 C  C   . ASP D 1 103 ? -60.282 111.780 10.105  1.00 56.26  ? 103 ASP D C   1 
ATOM   7006 O  O   . ASP D 1 103 ? -61.326 112.399 10.340  1.00 57.13  ? 103 ASP D O   1 
ATOM   7007 C  CB  . ASP D 1 103 ? -59.350 111.565 12.449  1.00 56.55  ? 103 ASP D CB  1 
ATOM   7008 C  CG  . ASP D 1 103 ? -58.130 112.485 12.314  1.00 53.28  ? 103 ASP D CG  1 
ATOM   7009 O  OD1 . ASP D 1 103 ? -57.782 112.835 11.173  1.00 57.19  ? 103 ASP D OD1 1 
ATOM   7010 O  OD2 . ASP D 1 103 ? -57.504 112.841 13.334  1.00 46.61  ? 103 ASP D OD2 1 
ATOM   7011 N  N   . LEU D 1 104 ? -59.621 111.893 8.957   1.00 53.78  ? 104 LEU D N   1 
ATOM   7012 C  CA  . LEU D 1 104 ? -60.065 112.772 7.869   1.00 55.89  ? 104 LEU D CA  1 
ATOM   7013 C  C   . LEU D 1 104 ? -60.417 111.938 6.618   1.00 55.38  ? 104 LEU D C   1 
ATOM   7014 O  O   . LEU D 1 104 ? -59.634 111.101 6.195   1.00 51.31  ? 104 LEU D O   1 
ATOM   7015 C  CB  . LEU D 1 104 ? -58.992 113.839 7.562   1.00 50.41  ? 104 LEU D CB  1 
ATOM   7016 C  CG  . LEU D 1 104 ? -58.793 115.062 8.487   1.00 54.79  ? 104 LEU D CG  1 
ATOM   7017 C  CD1 . LEU D 1 104 ? -57.462 115.761 8.239   1.00 54.16  ? 104 LEU D CD1 1 
ATOM   7018 C  CD2 . LEU D 1 104 ? -59.930 116.073 8.343   1.00 53.51  ? 104 LEU D CD2 1 
ATOM   7019 N  N   . PRO D 1 105 ? -61.599 112.187 6.027   1.00 55.17  ? 105 PRO D N   1 
ATOM   7020 C  CA  . PRO D 1 105 ? -62.206 111.391 4.951   1.00 52.80  ? 105 PRO D CA  1 
ATOM   7021 C  C   . PRO D 1 105 ? -61.361 111.212 3.664   1.00 54.35  ? 105 PRO D C   1 
ATOM   7022 O  O   . PRO D 1 105 ? -61.496 110.197 2.931   1.00 49.41  ? 105 PRO D O   1 
ATOM   7023 C  CB  . PRO D 1 105 ? -63.507 112.146 4.652   1.00 56.69  ? 105 PRO D CB  1 
ATOM   7024 C  CG  . PRO D 1 105 ? -63.311 113.534 5.211   1.00 53.94  ? 105 PRO D CG  1 
ATOM   7025 C  CD  . PRO D 1 105 ? -62.451 113.330 6.416   1.00 53.87  ? 105 PRO D CD  1 
ATOM   7026 N  N   . TYR D 1 106 ? -60.492 112.180 3.417   1.00 48.85  ? 106 TYR D N   1 
ATOM   7027 C  CA  . TYR D 1 106 ? -59.672 112.218 2.215   1.00 44.71  ? 106 TYR D CA  1 
ATOM   7028 C  C   . TYR D 1 106 ? -58.258 111.697 2.474   1.00 44.15  ? 106 TYR D C   1 
ATOM   7029 O  O   . TYR D 1 106 ? -57.373 111.903 1.655   1.00 45.19  ? 106 TYR D O   1 
ATOM   7030 C  CB  . TYR D 1 106 ? -59.609 113.665 1.692   1.00 47.72  ? 106 TYR D CB  1 
ATOM   7031 C  CG  . TYR D 1 106 ? -58.890 114.634 2.631   1.00 43.19  ? 106 TYR D CG  1 
ATOM   7032 C  CD1 . TYR D 1 106 ? -57.511 114.523 2.831   1.00 42.33  ? 106 TYR D CD1 1 
ATOM   7033 C  CD2 . TYR D 1 106 ? -59.580 115.669 3.302   1.00 42.48  ? 106 TYR D CD2 1 
ATOM   7034 C  CE1 . TYR D 1 106 ? -56.836 115.370 3.689   1.00 44.01  ? 106 TYR D CE1 1 
ATOM   7035 C  CE2 . TYR D 1 106 ? -58.896 116.554 4.165   1.00 40.43  ? 106 TYR D CE2 1 
ATOM   7036 C  CZ  . TYR D 1 106 ? -57.523 116.390 4.351   1.00 40.66  ? 106 TYR D CZ  1 
ATOM   7037 O  OH  . TYR D 1 106 ? -56.759 117.196 5.180   1.00 38.88  ? 106 TYR D OH  1 
ATOM   7038 N  N   . LYS D 1 107 ? -58.035 111.010 3.593   1.00 43.09  ? 107 LYS D N   1 
ATOM   7039 C  CA  . LYS D 1 107 ? -56.662 110.692 4.023   1.00 42.30  ? 107 LYS D CA  1 
ATOM   7040 C  C   . LYS D 1 107 ? -56.366 109.274 4.582   1.00 42.02  ? 107 LYS D C   1 
ATOM   7041 O  O   . LYS D 1 107 ? -55.214 108.996 4.980   1.00 44.37  ? 107 LYS D O   1 
ATOM   7042 C  CB  . LYS D 1 107 ? -56.222 111.737 5.064   1.00 49.27  ? 107 LYS D CB  1 
ATOM   7043 C  CG  . LYS D 1 107 ? -54.714 111.886 5.238   1.00 50.94  ? 107 LYS D CG  1 
ATOM   7044 C  CD  . LYS D 1 107 ? -54.370 112.248 6.675   1.00 52.03  ? 107 LYS D CD  1 
ATOM   7045 C  CE  . LYS D 1 107 ? -54.116 113.740 6.829   1.00 48.28  ? 107 LYS D CE  1 
ATOM   7046 N  NZ  . LYS D 1 107 ? -53.033 113.899 7.842   1.00 49.19  ? 107 LYS D NZ  1 
ATOM   7047 N  N   . GLY D 1 108 ? -57.339 108.366 4.633   1.00 39.56  ? 108 GLY D N   1 
ATOM   7048 C  CA  . GLY D 1 108 ? -57.066 107.060 5.360   1.00 40.79  ? 108 GLY D CA  1 
ATOM   7049 C  C   . GLY D 1 108 ? -56.470 105.822 4.652   1.00 37.96  ? 108 GLY D C   1 
ATOM   7050 O  O   . GLY D 1 108 ? -55.896 104.917 5.298   1.00 34.59  ? 108 GLY D O   1 
ATOM   7051 N  N   . SER D 1 109 ? -56.641 105.738 3.338   1.00 32.25  ? 109 SER D N   1 
ATOM   7052 C  CA  . SER D 1 109 ? -56.196 104.536 2.589   1.00 32.81  ? 109 SER D CA  1 
ATOM   7053 C  C   . SER D 1 109 ? -54.676 104.504 2.368   1.00 31.72  ? 109 SER D C   1 
ATOM   7054 O  O   . SER D 1 109 ? -54.020 105.561 2.434   1.00 29.25  ? 109 SER D O   1 
ATOM   7055 C  CB  . SER D 1 109 ? -56.946 104.469 1.258   1.00 32.85  ? 109 SER D CB  1 
ATOM   7056 O  OG  . SER D 1 109 ? -56.789 105.697 0.524   1.00 33.86  ? 109 SER D OG  1 
ATOM   7057 N  N   . GLU D 1 110 ? -54.094 103.324 2.105   1.00 33.25  ? 110 GLU D N   1 
ATOM   7058 C  CA  . GLU D 1 110 ? -52.695 103.315 1.623   1.00 32.60  ? 110 GLU D CA  1 
ATOM   7059 C  C   . GLU D 1 110 ? -52.621 103.554 0.108   1.00 34.76  ? 110 GLU D C   1 
ATOM   7060 O  O   . GLU D 1 110 ? -51.816 104.367 -0.324  1.00 35.99  ? 110 GLU D O   1 
ATOM   7061 C  CB  . GLU D 1 110 ? -51.877 102.113 2.075   1.00 33.12  ? 110 GLU D CB  1 
ATOM   7062 C  CG  . GLU D 1 110 ? -51.950 101.888 3.582   1.00 41.07  ? 110 GLU D CG  1 
ATOM   7063 C  CD  . GLU D 1 110 ? -50.872 100.974 4.100   1.00 42.54  ? 110 GLU D CD  1 
ATOM   7064 O  OE1 . GLU D 1 110 ? -50.980 99.742  3.871   1.00 49.60  ? 110 GLU D OE1 1 
ATOM   7065 O  OE2 . GLU D 1 110 ? -49.922 101.472 4.746   1.00 39.37  ? 110 GLU D OE2 1 
ATOM   7066 N  N   . HIS D 1 111 ? -53.453 102.851 -0.680  1.00 33.30  ? 111 HIS D N   1 
ATOM   7067 C  CA  . HIS D 1 111 ? -53.616 103.110 -2.142  1.00 31.92  ? 111 HIS D CA  1 
ATOM   7068 C  C   . HIS D 1 111 ? -54.492 104.312 -2.429  1.00 34.29  ? 111 HIS D C   1 
ATOM   7069 O  O   . HIS D 1 111 ? -55.366 104.673 -1.602  1.00 33.62  ? 111 HIS D O   1 
ATOM   7070 C  CB  . HIS D 1 111 ? -54.190 101.865 -2.838  1.00 31.88  ? 111 HIS D CB  1 
ATOM   7071 C  CG  . HIS D 1 111 ? -53.279 100.658 -2.693  1.00 30.75  ? 111 HIS D CG  1 
ATOM   7072 N  ND1 . HIS D 1 111 ? -53.336 99.851  -1.636  1.00 27.36  ? 111 HIS D ND1 1 
ATOM   7073 C  CD2 . HIS D 1 111 ? -52.184 100.259 -3.435  1.00 30.57  ? 111 HIS D CD2 1 
ATOM   7074 C  CE1 . HIS D 1 111 ? -52.353 98.948  -1.713  1.00 33.76  ? 111 HIS D CE1 1 
ATOM   7075 N  NE2 . HIS D 1 111 ? -51.632 99.213  -2.807  1.00 31.59  ? 111 HIS D NE2 1 
ATOM   7076 N  N   . SER D 1 112 ? -54.317 104.894 -3.619  1.00 31.30  ? 112 SER D N   1 
ATOM   7077 C  CA  . SER D 1 112 ? -55.245 105.873 -4.155  1.00 28.06  ? 112 SER D CA  1 
ATOM   7078 C  C   . SER D 1 112 ? -55.679 105.533 -5.555  1.00 27.32  ? 112 SER D C   1 
ATOM   7079 O  O   . SER D 1 112 ? -54.885 104.999 -6.344  1.00 29.21  ? 112 SER D O   1 
ATOM   7080 C  CB  . SER D 1 112 ? -54.610 107.284 -4.161  1.00 32.12  ? 112 SER D CB  1 
ATOM   7081 O  OG  . SER D 1 112 ? -53.254 107.249 -4.603  1.00 27.81  ? 112 SER D OG  1 
ATOM   7082 N  N   . LEU D 1 113 ? -56.922 105.877 -5.887  1.00 25.81  ? 113 LEU D N   1 
ATOM   7083 C  CA  . LEU D 1 113 ? -57.426 105.748 -7.253  1.00 32.09  ? 113 LEU D CA  1 
ATOM   7084 C  C   . LEU D 1 113 ? -57.459 107.144 -7.905  1.00 34.45  ? 113 LEU D C   1 
ATOM   7085 O  O   . LEU D 1 113 ? -58.235 107.998 -7.496  1.00 31.90  ? 113 LEU D O   1 
ATOM   7086 C  CB  . LEU D 1 113 ? -58.842 105.146 -7.261  1.00 33.39  ? 113 LEU D CB  1 
ATOM   7087 C  CG  . LEU D 1 113 ? -59.108 103.768 -6.640  1.00 30.34  ? 113 LEU D CG  1 
ATOM   7088 C  CD1 . LEU D 1 113 ? -60.565 103.399 -6.770  1.00 31.51  ? 113 LEU D CD1 1 
ATOM   7089 C  CD2 . LEU D 1 113 ? -58.219 102.688 -7.252  1.00 32.63  ? 113 LEU D CD2 1 
ATOM   7090 N  N   . ASP D 1 114 ? -56.616 107.379 -8.910  1.00 37.54  ? 114 ASP D N   1 
ATOM   7091 C  CA  . ASP D 1 114 ? -56.598 108.688 -9.575  1.00 36.53  ? 114 ASP D CA  1 
ATOM   7092 C  C   . ASP D 1 114 ? -56.416 109.853 -8.575  1.00 36.45  ? 114 ASP D C   1 
ATOM   7093 O  O   . ASP D 1 114 ? -57.052 110.896 -8.693  1.00 37.95  ? 114 ASP D O   1 
ATOM   7094 C  CB  . ASP D 1 114 ? -57.881 108.889 -10.407 1.00 35.60  ? 114 ASP D CB  1 
ATOM   7095 C  CG  . ASP D 1 114 ? -58.011 107.867 -11.544 1.00 35.10  ? 114 ASP D CG  1 
ATOM   7096 O  OD1 . ASP D 1 114 ? -56.986 107.467 -12.146 1.00 32.23  ? 114 ASP D OD1 1 
ATOM   7097 O  OD2 . ASP D 1 114 ? -59.150 107.487 -11.839 1.00 34.02  ? 114 ASP D OD2 1 
ATOM   7098 N  N   . GLY D 1 115 ? -55.555 109.636 -7.589  1.00 36.08  ? 115 GLY D N   1 
ATOM   7099 C  CA  . GLY D 1 115 ? -55.263 110.613 -6.581  1.00 36.67  ? 115 GLY D CA  1 
ATOM   7100 C  C   . GLY D 1 115 ? -56.201 110.707 -5.393  1.00 39.96  ? 115 GLY D C   1 
ATOM   7101 O  O   . GLY D 1 115 ? -55.858 111.383 -4.416  1.00 46.62  ? 115 GLY D O   1 
ATOM   7102 N  N   . GLU D 1 116 ? -57.381 110.097 -5.436  1.00 36.20  ? 116 GLU D N   1 
ATOM   7103 C  CA  . GLU D 1 116 ? -58.198 110.060 -4.209  1.00 37.06  ? 116 GLU D CA  1 
ATOM   7104 C  C   . GLU D 1 116 ? -57.757 108.979 -3.216  1.00 35.19  ? 116 GLU D C   1 
ATOM   7105 O  O   . GLU D 1 116 ? -57.598 107.819 -3.560  1.00 34.41  ? 116 GLU D O   1 
ATOM   7106 C  CB  . GLU D 1 116 ? -59.685 109.906 -4.490  1.00 40.06  ? 116 GLU D CB  1 
ATOM   7107 C  CG  . GLU D 1 116 ? -60.203 110.834 -5.563  1.00 49.58  ? 116 GLU D CG  1 
ATOM   7108 C  CD  . GLU D 1 116 ? -61.701 110.774 -5.691  1.00 54.57  ? 116 GLU D CD  1 
ATOM   7109 O  OE1 . GLU D 1 116 ? -62.240 109.657 -5.867  1.00 63.24  ? 116 GLU D OE1 1 
ATOM   7110 O  OE2 . GLU D 1 116 ? -62.333 111.848 -5.607  1.00 59.21  ? 116 GLU D OE2 1 
ATOM   7111 N  N   . HIS D 1 117 ? -57.529 109.404 -1.985  1.00 34.36  ? 117 HIS D N   1 
ATOM   7112 C  CA  . HIS D 1 117 ? -57.398 108.556 -0.850  1.00 34.53  ? 117 HIS D CA  1 
ATOM   7113 C  C   . HIS D 1 117 ? -58.753 108.493 -0.180  1.00 35.80  ? 117 HIS D C   1 
ATOM   7114 O  O   . HIS D 1 117 ? -59.600 109.374 -0.314  1.00 35.19  ? 117 HIS D O   1 
ATOM   7115 C  CB  . HIS D 1 117 ? -56.319 109.083 0.093   1.00 36.33  ? 117 HIS D CB  1 
ATOM   7116 C  CG  . HIS D 1 117 ? -54.980 109.292 -0.569  1.00 35.72  ? 117 HIS D CG  1 
ATOM   7117 N  ND1 . HIS D 1 117 ? -53.834 108.738 -0.098  1.00 39.30  ? 117 HIS D ND1 1 
ATOM   7118 C  CD2 . HIS D 1 117 ? -54.633 109.997 -1.726  1.00 34.30  ? 117 HIS D CD2 1 
ATOM   7119 C  CE1 . HIS D 1 117 ? -52.811 109.084 -0.900  1.00 37.85  ? 117 HIS D CE1 1 
ATOM   7120 N  NE2 . HIS D 1 117 ? -53.305 109.857 -1.900  1.00 34.74  ? 117 HIS D NE2 1 
ATOM   7121 N  N   . PHE D 1 118 ? -58.995 107.401 0.516   1.00 38.42  ? 118 PHE D N   1 
ATOM   7122 C  CA  . PHE D 1 118 ? -60.293 107.148 1.081   1.00 30.88  ? 118 PHE D CA  1 
ATOM   7123 C  C   . PHE D 1 118 ? -60.146 107.148 2.585   1.00 31.26  ? 118 PHE D C   1 
ATOM   7124 O  O   . PHE D 1 118 ? -59.027 107.257 3.119   1.00 33.20  ? 118 PHE D O   1 
ATOM   7125 C  CB  . PHE D 1 118 ? -60.774 105.794 0.581   1.00 33.31  ? 118 PHE D CB  1 
ATOM   7126 C  CG  . PHE D 1 118 ? -61.322 105.833 -0.821  1.00 32.80  ? 118 PHE D CG  1 
ATOM   7127 C  CD1 . PHE D 1 118 ? -60.460 105.749 -1.939  1.00 33.84  ? 118 PHE D CD1 1 
ATOM   7128 C  CD2 . PHE D 1 118 ? -62.658 105.983 -1.023  1.00 27.67  ? 118 PHE D CD2 1 
ATOM   7129 C  CE1 . PHE D 1 118 ? -60.965 105.793 -3.222  1.00 31.61  ? 118 PHE D CE1 1 
ATOM   7130 C  CE2 . PHE D 1 118 ? -63.168 105.997 -2.295  1.00 35.22  ? 118 PHE D CE2 1 
ATOM   7131 C  CZ  . PHE D 1 118 ? -62.326 105.903 -3.396  1.00 34.38  ? 118 PHE D CZ  1 
ATOM   7132 N  N   . ALA D 1 119 ? -61.269 107.006 3.274   1.00 31.66  ? 119 ALA D N   1 
ATOM   7133 C  CA  . ALA D 1 119 ? -61.302 107.125 4.742   1.00 33.29  ? 119 ALA D CA  1 
ATOM   7134 C  C   . ALA D 1 119 ? -60.566 105.996 5.467   1.00 32.59  ? 119 ALA D C   1 
ATOM   7135 O  O   . ALA D 1 119 ? -59.902 106.236 6.467   1.00 31.57  ? 119 ALA D O   1 
ATOM   7136 C  CB  . ALA D 1 119 ? -62.747 107.233 5.207   1.00 36.58  ? 119 ALA D CB  1 
ATOM   7137 N  N   . MET D 1 120 ? -60.700 104.761 4.960   1.00 30.07  ? 120 MET D N   1 
ATOM   7138 C  CA  . MET D 1 120 ? -59.937 103.650 5.461   1.00 33.54  ? 120 MET D CA  1 
ATOM   7139 C  C   . MET D 1 120 ? -59.515 102.691 4.329   1.00 34.47  ? 120 MET D C   1 
ATOM   7140 O  O   . MET D 1 120 ? -60.144 102.645 3.269   1.00 41.30  ? 120 MET D O   1 
ATOM   7141 C  CB  . MET D 1 120 ? -60.749 102.821 6.486   1.00 36.32  ? 120 MET D CB  1 
ATOM   7142 C  CG  . MET D 1 120 ? -61.718 103.568 7.426   1.00 39.95  ? 120 MET D CG  1 
ATOM   7143 S  SD  . MET D 1 120 ? -62.420 102.388 8.627   1.00 41.27  ? 120 MET D SD  1 
ATOM   7144 C  CE  . MET D 1 120 ? -60.912 101.837 9.409   1.00 33.61  ? 120 MET D CE  1 
ATOM   7145 N  N   . GLU D 1 121 ? -58.492 101.885 4.597   1.00 32.22  ? 121 GLU D N   1 
ATOM   7146 C  CA  . GLU D 1 121 ? -58.195 100.771 3.737   1.00 38.04  ? 121 GLU D CA  1 
ATOM   7147 C  C   . GLU D 1 121 ? -58.105 99.459  4.494   1.00 37.01  ? 121 GLU D C   1 
ATOM   7148 O  O   . GLU D 1 121 ? -57.306 99.327  5.408   1.00 38.76  ? 121 GLU D O   1 
ATOM   7149 C  CB  . GLU D 1 121 ? -56.882 101.017 3.000   1.00 37.22  ? 121 GLU D CB  1 
ATOM   7150 C  CG  . GLU D 1 121 ? -56.535 99.918  2.020   1.00 38.61  ? 121 GLU D CG  1 
ATOM   7151 C  CD  . GLU D 1 121 ? -55.595 100.402 0.963   1.00 37.36  ? 121 GLU D CD  1 
ATOM   7152 O  OE1 . GLU D 1 121 ? -55.747 101.581 0.559   1.00 38.54  ? 121 GLU D OE1 1 
ATOM   7153 O  OE2 . GLU D 1 121 ? -54.712 99.625  0.557   1.00 33.58  ? 121 GLU D OE2 1 
ATOM   7154 N  N   . MET D 1 122 ? -58.884 98.475  4.054   1.00 42.44  ? 122 MET D N   1 
ATOM   7155 C  CA  . MET D 1 122 ? -58.934 97.157  4.702   1.00 41.92  ? 122 MET D CA  1 
ATOM   7156 C  C   . MET D 1 122 ? -58.066 96.186  3.952   1.00 42.62  ? 122 MET D C   1 
ATOM   7157 O  O   . MET D 1 122 ? -58.158 96.084  2.727   1.00 47.08  ? 122 MET D O   1 
ATOM   7158 C  CB  . MET D 1 122 ? -60.377 96.633  4.770   1.00 42.59  ? 122 MET D CB  1 
ATOM   7159 C  CG  . MET D 1 122 ? -60.535 95.127  5.033   1.00 41.49  ? 122 MET D CG  1 
ATOM   7160 S  SD  . MET D 1 122 ? -62.097 94.819  5.893   1.00 45.86  ? 122 MET D SD  1 
ATOM   7161 C  CE  . MET D 1 122 ? -63.275 94.802  4.549   1.00 36.53  ? 122 MET D CE  1 
ATOM   7162 N  N   . HIS D 1 123 ? -57.224 95.479  4.700   1.00 40.38  ? 123 HIS D N   1 
ATOM   7163 C  CA  . HIS D 1 123 ? -56.406 94.433  4.166   1.00 39.71  ? 123 HIS D CA  1 
ATOM   7164 C  C   . HIS D 1 123 ? -56.843 93.080  4.694   1.00 43.38  ? 123 HIS D C   1 
ATOM   7165 O  O   . HIS D 1 123 ? -56.899 92.888  5.902   1.00 42.98  ? 123 HIS D O   1 
ATOM   7166 C  CB  . HIS D 1 123 ? -54.947 94.686  4.518   1.00 38.65  ? 123 HIS D CB  1 
ATOM   7167 C  CG  . HIS D 1 123 ? -54.337 95.874  3.794   1.00 40.87  ? 123 HIS D CG  1 
ATOM   7168 N  ND1 . HIS D 1 123 ? -53.157 96.446  4.185   1.00 35.22  ? 123 HIS D ND1 1 
ATOM   7169 C  CD2 . HIS D 1 123 ? -54.798 96.609  2.686   1.00 31.75  ? 123 HIS D CD2 1 
ATOM   7170 C  CE1 . HIS D 1 123 ? -52.853 97.427  3.300   1.00 38.10  ? 123 HIS D CE1 1 
ATOM   7171 N  NE2 . HIS D 1 123 ? -53.883 97.540  2.411   1.00 33.79  ? 123 HIS D NE2 1 
ATOM   7172 N  N   . ILE D 1 124 ? -57.172 92.149  3.790   1.00 46.34  ? 124 ILE D N   1 
ATOM   7173 C  CA  . ILE D 1 124 ? -57.433 90.738  4.138   1.00 45.03  ? 124 ILE D CA  1 
ATOM   7174 C  C   . ILE D 1 124 ? -56.348 89.929  3.462   1.00 44.83  ? 124 ILE D C   1 
ATOM   7175 O  O   . ILE D 1 124 ? -56.350 89.782  2.236   1.00 45.80  ? 124 ILE D O   1 
ATOM   7176 C  CB  . ILE D 1 124 ? -58.807 90.215  3.654   1.00 48.39  ? 124 ILE D CB  1 
ATOM   7177 C  CG1 . ILE D 1 124 ? -59.852 91.322  3.680   1.00 46.07  ? 124 ILE D CG1 1 
ATOM   7178 C  CG2 . ILE D 1 124 ? -59.259 89.025  4.501   1.00 47.29  ? 124 ILE D CG2 1 
ATOM   7179 C  CD1 . ILE D 1 124 ? -61.269 90.837  3.505   1.00 44.46  ? 124 ILE D CD1 1 
ATOM   7180 N  N   . VAL D 1 125 ? -55.429 89.427  4.283   1.00 42.24  ? 125 VAL D N   1 
ATOM   7181 C  CA  . VAL D 1 125 ? -54.150 88.851  3.883   1.00 43.65  ? 125 VAL D CA  1 
ATOM   7182 C  C   . VAL D 1 125 ? -54.302 87.310  3.729   1.00 47.80  ? 125 VAL D C   1 
ATOM   7183 O  O   . VAL D 1 125 ? -55.037 86.679  4.502   1.00 45.13  ? 125 VAL D O   1 
ATOM   7184 C  CB  . VAL D 1 125 ? -53.091 89.262  4.945   1.00 39.85  ? 125 VAL D CB  1 
ATOM   7185 C  CG1 . VAL D 1 125 ? -51.723 88.626  4.746   1.00 39.11  ? 125 VAL D CG1 1 
ATOM   7186 C  CG2 . VAL D 1 125 ? -52.940 90.786  4.946   1.00 43.14  ? 125 VAL D CG2 1 
ATOM   7187 N  N   . HIS D 1 126 ? -53.638 86.740  2.714   1.00 47.98  ? 126 HIS D N   1 
ATOM   7188 C  CA  . HIS D 1 126 ? -53.655 85.282  2.411   1.00 48.85  ? 126 HIS D CA  1 
ATOM   7189 C  C   . HIS D 1 126 ? -52.307 84.844  1.954   1.00 47.75  ? 126 HIS D C   1 
ATOM   7190 O  O   . HIS D 1 126 ? -51.552 85.671  1.432   1.00 42.22  ? 126 HIS D O   1 
ATOM   7191 C  CB  . HIS D 1 126 ? -54.656 84.942  1.318   1.00 42.89  ? 126 HIS D CB  1 
ATOM   7192 C  CG  . HIS D 1 126 ? -56.028 85.472  1.565   1.00 42.22  ? 126 HIS D CG  1 
ATOM   7193 N  ND1 . HIS D 1 126 ? -56.367 86.740  1.287   1.00 44.84  ? 126 HIS D ND1 1 
ATOM   7194 C  CD2 . HIS D 1 126 ? -57.166 84.861  2.072   1.00 41.12  ? 126 HIS D CD2 1 
ATOM   7195 C  CE1 . HIS D 1 126 ? -57.657 86.936  1.614   1.00 45.21  ? 126 HIS D CE1 1 
ATOM   7196 N  NE2 . HIS D 1 126 ? -58.146 85.783  2.088   1.00 46.38  ? 126 HIS D NE2 1 
ATOM   7197 N  N   . GLU D 1 127 ? -51.992 83.549  2.132   1.00 54.16  ? 127 GLU D N   1 
ATOM   7198 C  CA  . GLU D 1 127 ? -50.671 82.972  1.746   1.00 58.30  ? 127 GLU D CA  1 
ATOM   7199 C  C   . GLU D 1 127 ? -50.769 81.838  0.695   1.00 57.56  ? 127 GLU D C   1 
ATOM   7200 O  O   . GLU D 1 127 ? -51.767 81.096  0.691   1.00 51.34  ? 127 GLU D O   1 
ATOM   7201 C  CB  . GLU D 1 127 ? -49.901 82.511  2.997   1.00 64.37  ? 127 GLU D CB  1 
ATOM   7202 C  CG  . GLU D 1 127 ? -48.384 82.451  2.821   1.00 73.80  ? 127 GLU D CG  1 
ATOM   7203 C  CD  . GLU D 1 127 ? -47.599 82.787  4.092   1.00 84.92  ? 127 GLU D CD  1 
ATOM   7204 O  OE1 . GLU D 1 127 ? -46.594 82.092  4.367   1.00 89.52  ? 127 GLU D OE1 1 
ATOM   7205 O  OE2 . GLU D 1 127 ? -47.968 83.747  4.814   1.00 79.80  ? 127 GLU D OE2 1 
ATOM   7206 N  N   . LYS D 1 128 ? -49.757 81.731  -0.195  1.00 57.45  ? 128 LYS D N   1 
ATOM   7207 C  CA  . LYS D 1 128 ? -49.830 80.827  -1.383  1.00 65.68  ? 128 LYS D CA  1 
ATOM   7208 C  C   . LYS D 1 128 ? -49.698 79.372  -1.005  1.00 63.39  ? 128 LYS D C   1 
ATOM   7209 O  O   . LYS D 1 128 ? -48.693 78.983  -0.420  1.00 58.58  ? 128 LYS D O   1 
ATOM   7210 C  CB  . LYS D 1 128 ? -48.806 81.159  -2.497  1.00 66.77  ? 128 LYS D CB  1 
ATOM   7211 C  CG  . LYS D 1 128 ? -48.852 80.199  -3.695  1.00 58.94  ? 128 LYS D CG  1 
ATOM   7212 C  CD  . LYS D 1 128 ? -47.476 79.954  -4.339  1.00 60.37  ? 128 LYS D CD  1 
ATOM   7213 C  CE  . LYS D 1 128 ? -47.295 80.740  -5.641  1.00 59.91  ? 128 LYS D CE  1 
ATOM   7214 N  NZ  . LYS D 1 128 ? -45.892 80.884  -6.164  1.00 53.04  ? 128 LYS D NZ  1 
ATOM   7215 N  N   . GLU D 1 129 ? -50.717 78.592  -1.375  1.00 67.41  ? 129 GLU D N   1 
ATOM   7216 C  CA  . GLU D 1 129 ? -50.826 77.179  -1.009  1.00 71.33  ? 129 GLU D CA  1 
ATOM   7217 C  C   . GLU D 1 129 ? -49.502 76.439  -1.159  1.00 71.37  ? 129 GLU D C   1 
ATOM   7218 O  O   . GLU D 1 129 ? -48.727 76.689  -2.095  1.00 64.71  ? 129 GLU D O   1 
ATOM   7219 C  CB  . GLU D 1 129 ? -51.919 76.476  -1.831  1.00 70.02  ? 129 GLU D CB  1 
ATOM   7220 C  CG  . GLU D 1 129 ? -52.666 75.400  -1.052  1.00 75.14  ? 129 GLU D CG  1 
ATOM   7221 C  CD  . GLU D 1 129 ? -53.308 74.342  -1.944  1.00 78.31  ? 129 GLU D CD  1 
ATOM   7222 O  OE1 . GLU D 1 129 ? -54.561 74.262  -1.966  1.00 73.16  ? 129 GLU D OE1 1 
ATOM   7223 O  OE2 . GLU D 1 129 ? -52.564 73.584  -2.617  1.00 77.86  ? 129 GLU D OE2 1 
ATOM   7224 N  N   . LYS D 1 130 ? -49.251 75.537  -0.214  1.00 73.55  ? 130 LYS D N   1 
ATOM   7225 C  CA  . LYS D 1 130 ? -48.044 74.714  -0.213  1.00 75.71  ? 130 LYS D CA  1 
ATOM   7226 C  C   . LYS D 1 130 ? -48.337 73.321  -0.809  1.00 77.06  ? 130 LYS D C   1 
ATOM   7227 O  O   . LYS D 1 130 ? -49.361 73.130  -1.484  1.00 68.15  ? 130 LYS D O   1 
ATOM   7228 C  CB  . LYS D 1 130 ? -47.490 74.584  1.215   1.00 77.83  ? 130 LYS D CB  1 
ATOM   7229 C  CG  . LYS D 1 130 ? -47.634 75.831  2.089   1.00 78.64  ? 130 LYS D CG  1 
ATOM   7230 C  CD  . LYS D 1 130 ? -47.501 75.480  3.567   1.00 75.96  ? 130 LYS D CD  1 
ATOM   7231 C  CE  . LYS D 1 130 ? -47.050 76.671  4.399   1.00 73.94  ? 130 LYS D CE  1 
ATOM   7232 N  NZ  . LYS D 1 130 ? -46.576 76.235  5.743   1.00 64.07  ? 130 LYS D NZ  1 
ATOM   7233 N  N   . GLY D 1 131 ? -47.429 72.370  -0.554  1.00 81.25  ? 131 GLY D N   1 
ATOM   7234 C  CA  . GLY D 1 131 ? -47.568 70.970  -0.968  1.00 73.75  ? 131 GLY D CA  1 
ATOM   7235 C  C   . GLY D 1 131 ? -47.740 70.790  -2.462  1.00 73.36  ? 131 GLY D C   1 
ATOM   7236 O  O   . GLY D 1 131 ? -48.859 70.629  -2.947  1.00 70.14  ? 131 GLY D O   1 
ATOM   7237 N  N   . PRO D 1 142 ? -40.549 84.214  -4.995  1.00 60.39  ? 140 PRO D N   1 
ATOM   7238 C  CA  . PRO D 1 142 ? -41.782 84.245  -5.760  1.00 60.16  ? 140 PRO D CA  1 
ATOM   7239 C  C   . PRO D 1 142 ? -42.522 85.584  -5.581  1.00 63.77  ? 140 PRO D C   1 
ATOM   7240 O  O   . PRO D 1 142 ? -43.026 85.886  -4.483  1.00 62.54  ? 140 PRO D O   1 
ATOM   7241 C  CB  . PRO D 1 142 ? -42.593 83.093  -5.151  1.00 61.46  ? 140 PRO D CB  1 
ATOM   7242 C  CG  . PRO D 1 142 ? -42.063 82.934  -3.753  1.00 60.21  ? 140 PRO D CG  1 
ATOM   7243 C  CD  . PRO D 1 142 ? -40.776 83.720  -3.628  1.00 59.28  ? 140 PRO D CD  1 
ATOM   7244 N  N   . GLU D 1 143 ? -42.583 86.359  -6.661  1.00 58.68  ? 141 GLU D N   1 
ATOM   7245 C  CA  . GLU D 1 143 ? -43.157 87.697  -6.643  1.00 61.83  ? 141 GLU D CA  1 
ATOM   7246 C  C   . GLU D 1 143 ? -44.607 87.710  -6.185  1.00 61.55  ? 141 GLU D C   1 
ATOM   7247 O  O   . GLU D 1 143 ? -45.123 88.756  -5.765  1.00 72.04  ? 141 GLU D O   1 
ATOM   7248 C  CB  . GLU D 1 143 ? -42.997 88.381  -8.010  1.00 64.88  ? 141 GLU D CB  1 
ATOM   7249 C  CG  . GLU D 1 143 ? -42.893 87.429  -9.201  1.00 68.97  ? 141 GLU D CG  1 
ATOM   7250 C  CD  . GLU D 1 143 ? -42.864 88.152  -10.539 1.00 68.17  ? 141 GLU D CD  1 
ATOM   7251 O  OE1 . GLU D 1 143 ? -42.021 89.073  -10.700 1.00 65.29  ? 141 GLU D OE1 1 
ATOM   7252 O  OE2 . GLU D 1 143 ? -43.684 87.794  -11.422 1.00 61.41  ? 141 GLU D OE2 1 
ATOM   7253 N  N   . ASP D 1 144 ? -45.247 86.544  -6.229  1.00 55.96  ? 142 ASP D N   1 
ATOM   7254 C  CA  . ASP D 1 144 ? -46.634 86.413  -5.830  1.00 48.17  ? 142 ASP D CA  1 
ATOM   7255 C  C   . ASP D 1 144 ? -46.879 85.503  -4.620  1.00 46.06  ? 142 ASP D C   1 
ATOM   7256 O  O   . ASP D 1 144 ? -47.984 85.014  -4.420  1.00 43.30  ? 142 ASP D O   1 
ATOM   7257 C  CB  . ASP D 1 144 ? -47.534 86.056  -7.030  1.00 52.82  ? 142 ASP D CB  1 
ATOM   7258 C  CG  . ASP D 1 144 ? -47.166 84.715  -7.726  1.00 54.09  ? 142 ASP D CG  1 
ATOM   7259 O  OD1 . ASP D 1 144 ? -46.135 84.079  -7.405  1.00 48.16  ? 142 ASP D OD1 1 
ATOM   7260 O  OD2 . ASP D 1 144 ? -47.941 84.310  -8.628  1.00 52.10  ? 142 ASP D OD2 1 
ATOM   7261 N  N   . GLU D 1 145 ? -45.851 85.323  -3.802  1.00 46.28  ? 143 GLU D N   1 
ATOM   7262 C  CA  . GLU D 1 145 ? -45.933 84.559  -2.530  1.00 52.52  ? 143 GLU D CA  1 
ATOM   7263 C  C   . GLU D 1 145 ? -47.206 84.732  -1.662  1.00 54.58  ? 143 GLU D C   1 
ATOM   7264 O  O   . GLU D 1 145 ? -47.837 83.731  -1.237  1.00 54.41  ? 143 GLU D O   1 
ATOM   7265 C  CB  . GLU D 1 145 ? -44.682 84.857  -1.681  1.00 53.20  ? 143 GLU D CB  1 
ATOM   7266 C  CG  . GLU D 1 145 ? -44.056 83.637  -1.011  1.00 62.84  ? 143 GLU D CG  1 
ATOM   7267 C  CD  . GLU D 1 145 ? -44.510 83.437  0.420   1.00 63.42  ? 143 GLU D CD  1 
ATOM   7268 O  OE1 . GLU D 1 145 ? -43.622 83.232  1.275   1.00 58.87  ? 143 GLU D OE1 1 
ATOM   7269 O  OE2 . GLU D 1 145 ? -45.742 83.489  0.685   1.00 60.84  ? 143 GLU D OE2 1 
ATOM   7270 N  N   . ILE D 1 146 ? -47.558 85.986  -1.352  1.00 51.57  ? 144 ILE D N   1 
ATOM   7271 C  CA  . ILE D 1 146 ? -48.832 86.249  -0.664  1.00 52.42  ? 144 ILE D CA  1 
ATOM   7272 C  C   . ILE D 1 146 ? -49.785 87.095  -1.520  1.00 47.75  ? 144 ILE D C   1 
ATOM   7273 O  O   . ILE D 1 146 ? -49.370 87.872  -2.381  1.00 44.49  ? 144 ILE D O   1 
ATOM   7274 C  CB  . ILE D 1 146 ? -48.647 86.925  0.719   1.00 57.58  ? 144 ILE D CB  1 
ATOM   7275 C  CG1 . ILE D 1 146 ? -48.138 88.360  0.557   1.00 58.60  ? 144 ILE D CG1 1 
ATOM   7276 C  CG2 . ILE D 1 146 ? -47.752 86.115  1.662   1.00 50.37  ? 144 ILE D CG2 1 
ATOM   7277 C  CD1 . ILE D 1 146 ? -48.716 89.279  1.605   1.00 59.12  ? 144 ILE D CD1 1 
ATOM   7278 N  N   . ALA D 1 147 ? -51.078 86.930  -1.283  1.00 49.60  ? 145 ALA D N   1 
ATOM   7279 C  CA  . ALA D 1 147 ? -52.066 87.747  -1.975  1.00 44.88  ? 145 ALA D CA  1 
ATOM   7280 C  C   . ALA D 1 147 ? -52.744 88.584  -0.943  1.00 45.97  ? 145 ALA D C   1 
ATOM   7281 O  O   . ALA D 1 147 ? -53.359 88.042  -0.022  1.00 43.42  ? 145 ALA D O   1 
ATOM   7282 C  CB  . ALA D 1 147 ? -53.107 86.875  -2.670  1.00 50.05  ? 145 ALA D CB  1 
ATOM   7283 N  N   . VAL D 1 148 ? -52.671 89.903  -1.075  1.00 41.72  ? 146 VAL D N   1 
ATOM   7284 C  CA  . VAL D 1 148 ? -53.497 90.700  -0.180  1.00 37.96  ? 146 VAL D CA  1 
ATOM   7285 C  C   . VAL D 1 148 ? -54.760 91.111  -0.925  1.00 33.59  ? 146 VAL D C   1 
ATOM   7286 O  O   . VAL D 1 148 ? -54.675 91.563  -2.069  1.00 35.99  ? 146 VAL D O   1 
ATOM   7287 C  CB  . VAL D 1 148 ? -52.722 91.921  0.380   1.00 40.28  ? 146 VAL D CB  1 
ATOM   7288 C  CG1 . VAL D 1 148 ? -53.659 92.873  1.105   1.00 34.96  ? 146 VAL D CG1 1 
ATOM   7289 C  CG2 . VAL D 1 148 ? -51.600 91.477  1.292   1.00 37.91  ? 146 VAL D CG2 1 
ATOM   7290 N  N   . LEU D 1 149 ? -55.926 90.970  -0.296  1.00 33.62  ? 147 LEU D N   1 
ATOM   7291 C  CA  . LEU D 1 149 ? -57.130 91.575  -0.852  1.00 36.92  ? 147 LEU D CA  1 
ATOM   7292 C  C   . LEU D 1 149 ? -57.418 92.924  -0.147  1.00 41.93  ? 147 LEU D C   1 
ATOM   7293 O  O   . LEU D 1 149 ? -57.514 92.968  1.109   1.00 42.07  ? 147 LEU D O   1 
ATOM   7294 C  CB  . LEU D 1 149 ? -58.337 90.653  -0.718  1.00 36.40  ? 147 LEU D CB  1 
ATOM   7295 C  CG  . LEU D 1 149 ? -58.438 89.276  -1.392  1.00 37.21  ? 147 LEU D CG  1 
ATOM   7296 C  CD1 . LEU D 1 149 ? -59.852 88.778  -1.123  1.00 37.08  ? 147 LEU D CD1 1 
ATOM   7297 C  CD2 . LEU D 1 149 ? -58.147 89.283  -2.896  1.00 36.44  ? 147 LEU D CD2 1 
ATOM   7298 N  N   . ALA D 1 150 ? -57.567 93.997  -0.942  1.00 36.32  ? 148 ALA D N   1 
ATOM   7299 C  CA  . ALA D 1 150 ? -57.601 95.374  -0.406  1.00 37.16  ? 148 ALA D CA  1 
ATOM   7300 C  C   . ALA D 1 150 ? -58.867 96.106  -0.766  1.00 37.39  ? 148 ALA D C   1 
ATOM   7301 O  O   . ALA D 1 150 ? -59.163 96.274  -1.946  1.00 38.93  ? 148 ALA D O   1 
ATOM   7302 C  CB  . ALA D 1 150 ? -56.380 96.161  -0.865  1.00 34.34  ? 148 ALA D CB  1 
ATOM   7303 N  N   . PHE D 1 151 ? -59.616 96.531  0.262   1.00 36.82  ? 149 PHE D N   1 
ATOM   7304 C  CA  . PHE D 1 151 ? -60.888 97.248  0.076   1.00 41.74  ? 149 PHE D CA  1 
ATOM   7305 C  C   . PHE D 1 151 ? -60.829 98.699  0.587   1.00 40.32  ? 149 PHE D C   1 
ATOM   7306 O  O   . PHE D 1 151 ? -60.638 98.925  1.772   1.00 42.10  ? 149 PHE D O   1 
ATOM   7307 C  CB  . PHE D 1 151 ? -62.025 96.520  0.804   1.00 44.68  ? 149 PHE D CB  1 
ATOM   7308 C  CG  . PHE D 1 151 ? -62.311 95.146  0.258   1.00 46.76  ? 149 PHE D CG  1 
ATOM   7309 C  CD1 . PHE D 1 151 ? -61.375 94.115  0.391   1.00 46.58  ? 149 PHE D CD1 1 
ATOM   7310 C  CD2 . PHE D 1 151 ? -63.504 94.891  -0.400  1.00 47.51  ? 149 PHE D CD2 1 
ATOM   7311 C  CE1 . PHE D 1 151 ? -61.633 92.857  -0.135  1.00 54.03  ? 149 PHE D CE1 1 
ATOM   7312 C  CE2 . PHE D 1 151 ? -63.775 93.634  -0.927  1.00 48.34  ? 149 PHE D CE2 1 
ATOM   7313 C  CZ  . PHE D 1 151 ? -62.837 92.618  -0.796  1.00 50.77  ? 149 PHE D CZ  1 
ATOM   7314 N  N   . LEU D 1 152 ? -61.018 99.674  -0.295  1.00 39.77  ? 150 LEU D N   1 
ATOM   7315 C  CA  . LEU D 1 152 ? -61.162 101.082 0.150   1.00 40.79  ? 150 LEU D CA  1 
ATOM   7316 C  C   . LEU D 1 152 ? -62.497 101.321 0.858   1.00 42.02  ? 150 LEU D C   1 
ATOM   7317 O  O   . LEU D 1 152 ? -63.544 100.824 0.404   1.00 40.49  ? 150 LEU D O   1 
ATOM   7318 C  CB  . LEU D 1 152 ? -61.097 102.032 -1.034  1.00 38.35  ? 150 LEU D CB  1 
ATOM   7319 C  CG  . LEU D 1 152 ? -59.893 101.807 -1.933  1.00 40.16  ? 150 LEU D CG  1 
ATOM   7320 C  CD1 . LEU D 1 152 ? -60.242 102.116 -3.374  1.00 33.85  ? 150 LEU D CD1 1 
ATOM   7321 C  CD2 . LEU D 1 152 ? -58.727 102.629 -1.424  1.00 41.08  ? 150 LEU D CD2 1 
ATOM   7322 N  N   . VAL D 1 153 ? -62.463 102.122 1.929   1.00 40.81  ? 151 VAL D N   1 
ATOM   7323 C  CA  . VAL D 1 153 ? -63.668 102.437 2.692   1.00 42.75  ? 151 VAL D CA  1 
ATOM   7324 C  C   . VAL D 1 153 ? -63.924 103.953 2.738   1.00 46.81  ? 151 VAL D C   1 
ATOM   7325 O  O   . VAL D 1 153 ? -63.046 104.721 3.125   1.00 42.37  ? 151 VAL D O   1 
ATOM   7326 C  CB  . VAL D 1 153 ? -63.567 101.940 4.153   1.00 45.71  ? 151 VAL D CB  1 
ATOM   7327 C  CG1 . VAL D 1 153 ? -64.834 102.294 4.922   1.00 47.65  ? 151 VAL D CG1 1 
ATOM   7328 C  CG2 . VAL D 1 153 ? -63.309 100.438 4.217   1.00 46.34  ? 151 VAL D CG2 1 
ATOM   7329 N  N   . GLU D 1 154 ? -65.133 104.357 2.370   1.00 50.48  ? 152 GLU D N   1 
ATOM   7330 C  CA  . GLU D 1 154 ? -65.578 105.741 2.510   1.00 55.55  ? 152 GLU D CA  1 
ATOM   7331 C  C   . GLU D 1 154 ? -66.822 105.878 3.428   1.00 62.30  ? 152 GLU D C   1 
ATOM   7332 O  O   . GLU D 1 154 ? -67.542 104.900 3.711   1.00 58.10  ? 152 GLU D O   1 
ATOM   7333 C  CB  . GLU D 1 154 ? -65.843 106.358 1.132   1.00 54.79  ? 152 GLU D CB  1 
ATOM   7334 C  CG  . GLU D 1 154 ? -67.190 106.008 0.529   1.00 53.10  ? 152 GLU D CG  1 
ATOM   7335 C  CD  . GLU D 1 154 ? -67.234 106.143 -0.984  1.00 59.42  ? 152 GLU D CD  1 
ATOM   7336 O  OE1 . GLU D 1 154 ? -66.215 106.543 -1.604  1.00 59.40  ? 152 GLU D OE1 1 
ATOM   7337 O  OE2 . GLU D 1 154 ? -68.302 105.825 -1.562  1.00 60.70  ? 152 GLU D OE2 1 
ATOM   7338 N  N   . ALA D 1 155 ? -67.062 107.101 3.884   1.00 62.00  ? 153 ALA D N   1 
ATOM   7339 C  CA  . ALA D 1 155 ? -68.221 107.400 4.695   1.00 62.40  ? 153 ALA D CA  1 
ATOM   7340 C  C   . ALA D 1 155 ? -69.472 107.479 3.828   1.00 67.06  ? 153 ALA D C   1 
ATOM   7341 O  O   . ALA D 1 155 ? -69.413 107.940 2.687   1.00 71.97  ? 153 ALA D O   1 
ATOM   7342 C  CB  . ALA D 1 155 ? -68.006 108.698 5.453   1.00 65.15  ? 153 ALA D CB  1 
ATOM   7343 N  N   . GLY D 1 156 ? -70.595 107.005 4.362   1.00 64.94  ? 154 GLY D N   1 
ATOM   7344 C  CA  . GLY D 1 156 ? -71.883 107.123 3.684   1.00 61.82  ? 154 GLY D CA  1 
ATOM   7345 C  C   . GLY D 1 156 ? -73.035 107.375 4.648   1.00 65.56  ? 154 GLY D C   1 
ATOM   7346 O  O   . GLY D 1 156 ? -72.819 107.615 5.849   1.00 62.19  ? 154 GLY D O   1 
ATOM   7347 N  N   . THR D 1 157 ? -74.252 107.298 4.106   1.00 65.87  ? 155 THR D N   1 
ATOM   7348 C  CA  . THR D 1 157 ? -75.515 107.489 4.837   1.00 69.27  ? 155 THR D CA  1 
ATOM   7349 C  C   . THR D 1 157 ? -75.683 106.972 6.266   1.00 73.68  ? 155 THR D C   1 
ATOM   7350 O  O   . THR D 1 157 ? -75.865 107.758 7.196   1.00 74.29  ? 155 THR D O   1 
ATOM   7351 C  CB  . THR D 1 157 ? -76.710 106.871 4.069   1.00 68.08  ? 155 THR D CB  1 
ATOM   7352 O  OG1 . THR D 1 157 ? -76.725 107.352 2.715   1.00 70.51  ? 155 THR D OG1 1 
ATOM   7353 C  CG2 . THR D 1 157 ? -78.042 107.202 4.754   1.00 66.63  ? 155 THR D CG2 1 
ATOM   7354 N  N   . GLN D 1 158 ? -75.603 105.655 6.435   1.00 75.81  ? 156 GLN D N   1 
ATOM   7355 C  CA  . GLN D 1 158 ? -76.093 105.031 7.658   1.00 80.53  ? 156 GLN D CA  1 
ATOM   7356 C  C   . GLN D 1 158 ? -75.234 103.854 8.076   1.00 79.03  ? 156 GLN D C   1 
ATOM   7357 O  O   . GLN D 1 158 ? -74.468 103.313 7.278   1.00 82.39  ? 156 GLN D O   1 
ATOM   7358 C  CB  . GLN D 1 158 ? -77.598 104.712 7.660   1.00 88.47  ? 156 GLN D CB  1 
ATOM   7359 C  CG  . GLN D 1 158 ? -78.050 103.694 6.612   1.00 86.73  ? 156 GLN D CG  1 
ATOM   7360 C  CD  . GLN D 1 158 ? -79.537 103.369 6.704   1.00 86.38  ? 156 GLN D CD  1 
ATOM   7361 O  OE1 . GLN D 1 158 ? -79.932 102.194 6.708   1.00 78.84  ? 156 GLN D OE1 1 
ATOM   7362 N  NE2 . GLN D 1 158 ? -80.371 104.410 6.779   1.00 83.26  ? 156 GLN D NE2 1 
ATOM   7363 N  N   . VAL D 1 159 ? -75.407 103.462 9.338   1.00 74.27  ? 157 VAL D N   1 
ATOM   7364 C  CA  . VAL D 1 159 ? -74.716 102.324 9.965   1.00 74.89  ? 157 VAL D CA  1 
ATOM   7365 C  C   . VAL D 1 159 ? -74.690 101.055 9.086   1.00 77.94  ? 157 VAL D C   1 
ATOM   7366 O  O   . VAL D 1 159 ? -75.742 100.560 8.669   1.00 81.89  ? 157 VAL D O   1 
ATOM   7367 C  CB  . VAL D 1 159 ? -75.355 102.002 11.345  1.00 68.96  ? 157 VAL D CB  1 
ATOM   7368 C  CG1 . VAL D 1 159 ? -74.476 101.056 12.147  1.00 70.47  ? 157 VAL D CG1 1 
ATOM   7369 C  CG2 . VAL D 1 159 ? -75.596 103.278 12.142  1.00 58.75  ? 157 VAL D CG2 1 
ATOM   7370 N  N   . ASN D 1 160 ? -73.480 100.557 8.800   1.00 76.08  ? 158 ASN D N   1 
ATOM   7371 C  CA  . ASN D 1 160 ? -73.274 99.283  8.090   1.00 73.51  ? 158 ASN D CA  1 
ATOM   7372 C  C   . ASN D 1 160 ? -73.373 98.111  9.077   1.00 72.55  ? 158 ASN D C   1 
ATOM   7373 O  O   . ASN D 1 160 ? -72.645 98.067  10.078  1.00 60.39  ? 158 ASN D O   1 
ATOM   7374 C  CB  . ASN D 1 160 ? -71.910 99.273  7.371   1.00 72.73  ? 158 ASN D CB  1 
ATOM   7375 C  CG  . ASN D 1 160 ? -71.815 98.223  6.259   1.00 75.66  ? 158 ASN D CG  1 
ATOM   7376 O  OD1 . ASN D 1 160 ? -70.817 98.178  5.530   1.00 69.66  ? 158 ASN D OD1 1 
ATOM   7377 N  ND2 . ASN D 1 160 ? -72.846 97.382  6.116   1.00 71.63  ? 158 ASN D ND2 1 
ATOM   7378 N  N   . GLU D 1 161 ? -74.268 97.165  8.779   1.00 75.91  ? 159 GLU D N   1 
ATOM   7379 C  CA  . GLU D 1 161 ? -74.626 96.105  9.722   1.00 77.25  ? 159 GLU D CA  1 
ATOM   7380 C  C   . GLU D 1 161 ? -73.685 94.896  9.725   1.00 77.85  ? 159 GLU D C   1 
ATOM   7381 O  O   . GLU D 1 161 ? -74.042 93.829  10.224  1.00 77.54  ? 159 GLU D O   1 
ATOM   7382 C  CB  . GLU D 1 161 ? -76.083 95.655  9.516   1.00 80.00  ? 159 GLU D CB  1 
ATOM   7383 C  CG  . GLU D 1 161 ? -77.153 96.684  9.874   1.00 82.15  ? 159 GLU D CG  1 
ATOM   7384 C  CD  . GLU D 1 161 ? -76.795 97.547  11.080  1.00 84.30  ? 159 GLU D CD  1 
ATOM   7385 O  OE1 . GLU D 1 161 ? -76.840 97.065  12.233  1.00 77.45  ? 159 GLU D OE1 1 
ATOM   7386 O  OE2 . GLU D 1 161 ? -76.475 98.734  10.869  1.00 90.86  ? 159 GLU D OE2 1 
ATOM   7387 N  N   . GLY D 1 162 ? -72.484 95.053  9.181   1.00 74.99  ? 160 GLY D N   1 
ATOM   7388 C  CA  . GLY D 1 162 ? -71.497 93.974  9.243   1.00 73.99  ? 160 GLY D CA  1 
ATOM   7389 C  C   . GLY D 1 162 ? -70.370 94.305  10.204  1.00 73.17  ? 160 GLY D C   1 
ATOM   7390 O  O   . GLY D 1 162 ? -69.901 93.442  10.975  1.00 66.34  ? 160 GLY D O   1 
ATOM   7391 N  N   . PHE D 1 163 ? -69.967 95.575  10.170  1.00 60.89  ? 161 PHE D N   1 
ATOM   7392 C  CA  . PHE D 1 163 ? -68.779 96.039  10.864  1.00 62.96  ? 161 PHE D CA  1 
ATOM   7393 C  C   . PHE D 1 163 ? -68.909 96.141  12.373  1.00 59.21  ? 161 PHE D C   1 
ATOM   7394 O  O   . PHE D 1 163 ? -67.905 96.158  13.078  1.00 64.71  ? 161 PHE D O   1 
ATOM   7395 C  CB  . PHE D 1 163 ? -68.304 97.374  10.274  1.00 58.91  ? 161 PHE D CB  1 
ATOM   7396 C  CG  . PHE D 1 163 ? -67.086 97.248  9.400   1.00 58.98  ? 161 PHE D CG  1 
ATOM   7397 C  CD1 . PHE D 1 163 ? -67.188 96.766  8.095   1.00 57.66  ? 161 PHE D CD1 1 
ATOM   7398 C  CD2 . PHE D 1 163 ? -65.835 97.613  9.879   1.00 58.23  ? 161 PHE D CD2 1 
ATOM   7399 C  CE1 . PHE D 1 163 ? -66.066 96.645  7.298   1.00 56.69  ? 161 PHE D CE1 1 
ATOM   7400 C  CE2 . PHE D 1 163 ? -64.708 97.501  9.078   1.00 54.33  ? 161 PHE D CE2 1 
ATOM   7401 C  CZ  . PHE D 1 163 ? -64.826 97.015  7.790   1.00 51.77  ? 161 PHE D CZ  1 
ATOM   7402 N  N   . GLN D 1 164 ? -70.141 96.205  12.860  1.00 69.68  ? 162 GLN D N   1 
ATOM   7403 C  CA  . GLN D 1 164 ? -70.426 96.278  14.304  1.00 71.82  ? 162 GLN D CA  1 
ATOM   7404 C  C   . GLN D 1 164 ? -69.577 95.343  15.211  1.00 69.35  ? 162 GLN D C   1 
ATOM   7405 O  O   . GLN D 1 164 ? -68.876 95.830  16.111  1.00 66.22  ? 162 GLN D O   1 
ATOM   7406 C  CB  . GLN D 1 164 ? -71.929 96.105  14.551  1.00 74.47  ? 162 GLN D CB  1 
ATOM   7407 C  CG  . GLN D 1 164 ? -72.793 97.113  13.806  1.00 80.34  ? 162 GLN D CG  1 
ATOM   7408 C  CD  . GLN D 1 164 ? -72.856 98.463  14.506  1.00 89.64  ? 162 GLN D CD  1 
ATOM   7409 O  OE1 . GLN D 1 164 ? -73.903 98.847  15.039  1.00 90.91  ? 162 GLN D OE1 1 
ATOM   7410 N  NE2 . GLN D 1 164 ? -71.732 99.188  14.520  1.00 88.92  ? 162 GLN D NE2 1 
ATOM   7411 N  N   . PRO D 1 165 ? -69.613 94.008  14.968  1.00 67.42  ? 163 PRO D N   1 
ATOM   7412 C  CA  . PRO D 1 165 ? -68.823 93.110  15.823  1.00 63.84  ? 163 PRO D CA  1 
ATOM   7413 C  C   . PRO D 1 165 ? -67.368 93.563  15.967  1.00 66.02  ? 163 PRO D C   1 
ATOM   7414 O  O   . PRO D 1 165 ? -66.826 93.543  17.073  1.00 64.99  ? 163 PRO D O   1 
ATOM   7415 C  CB  . PRO D 1 165 ? -68.907 91.765  15.091  1.00 62.67  ? 163 PRO D CB  1 
ATOM   7416 C  CG  . PRO D 1 165 ? -70.205 91.818  14.369  1.00 60.89  ? 163 PRO D CG  1 
ATOM   7417 C  CD  . PRO D 1 165 ? -70.385 93.254  13.955  1.00 63.42  ? 163 PRO D CD  1 
ATOM   7418 N  N   . LEU D 1 166 ? -66.760 93.976  14.852  1.00 61.71  ? 164 LEU D N   1 
ATOM   7419 C  CA  . LEU D 1 166 ? -65.418 94.538  14.833  1.00 56.19  ? 164 LEU D CA  1 
ATOM   7420 C  C   . LEU D 1 166 ? -65.391 95.913  15.488  1.00 55.94  ? 164 LEU D C   1 
ATOM   7421 O  O   . LEU D 1 166 ? -64.525 96.175  16.321  1.00 57.03  ? 164 LEU D O   1 
ATOM   7422 C  CB  . LEU D 1 166 ? -64.908 94.634  13.386  1.00 56.58  ? 164 LEU D CB  1 
ATOM   7423 C  CG  . LEU D 1 166 ? -63.450 95.066  13.173  1.00 57.75  ? 164 LEU D CG  1 
ATOM   7424 C  CD1 . LEU D 1 166 ? -62.470 93.969  13.550  1.00 59.95  ? 164 LEU D CD1 1 
ATOM   7425 C  CD2 . LEU D 1 166 ? -63.218 95.471  11.731  1.00 58.15  ? 164 LEU D CD2 1 
ATOM   7426 N  N   . VAL D 1 167 ? -66.332 96.781  15.101  1.00 57.12  ? 165 VAL D N   1 
ATOM   7427 C  CA  . VAL D 1 167 ? -66.441 98.147  15.638  1.00 61.85  ? 165 VAL D CA  1 
ATOM   7428 C  C   . VAL D 1 167 ? -66.574 98.125  17.156  1.00 67.20  ? 165 VAL D C   1 
ATOM   7429 O  O   . VAL D 1 167 ? -65.687 98.595  17.867  1.00 65.03  ? 165 VAL D O   1 
ATOM   7430 C  CB  . VAL D 1 167 ? -67.640 98.944  15.033  1.00 61.22  ? 165 VAL D CB  1 
ATOM   7431 C  CG1 . VAL D 1 167 ? -67.918 100.202 15.843  1.00 61.43  ? 165 VAL D CG1 1 
ATOM   7432 C  CG2 . VAL D 1 167 ? -67.392 99.331  13.579  1.00 57.02  ? 165 VAL D CG2 1 
ATOM   7433 N  N   . GLU D 1 168 ? -67.681 97.569  17.646  1.00 71.57  ? 166 GLU D N   1 
ATOM   7434 C  CA  . GLU D 1 168 ? -67.960 97.544  19.082  1.00 72.39  ? 166 GLU D CA  1 
ATOM   7435 C  C   . GLU D 1 168 ? -66.817 96.891  19.862  1.00 70.70  ? 166 GLU D C   1 
ATOM   7436 O  O   . GLU D 1 168 ? -66.409 97.405  20.901  1.00 71.76  ? 166 GLU D O   1 
ATOM   7437 C  CB  . GLU D 1 168 ? -69.330 96.908  19.364  1.00 71.71  ? 166 GLU D CB  1 
ATOM   7438 C  CG  . GLU D 1 168 ? -70.472 97.921  19.236  1.00 76.45  ? 166 GLU D CG  1 
ATOM   7439 C  CD  . GLU D 1 168 ? -71.847 97.325  18.921  1.00 81.86  ? 166 GLU D CD  1 
ATOM   7440 O  OE1 . GLU D 1 168 ? -72.852 97.834  19.465  1.00 83.54  ? 166 GLU D OE1 1 
ATOM   7441 O  OE2 . GLU D 1 168 ? -71.949 96.372  18.115  1.00 83.62  ? 166 GLU D OE2 1 
ATOM   7442 N  N   . ALA D 1 169 ? -66.259 95.814  19.307  1.00 69.61  ? 167 ALA D N   1 
ATOM   7443 C  CA  . ALA D 1 169 ? -65.203 95.028  19.962  1.00 74.43  ? 167 ALA D CA  1 
ATOM   7444 C  C   . ALA D 1 169 ? -63.890 95.775  20.199  1.00 73.65  ? 167 ALA D C   1 
ATOM   7445 O  O   . ALA D 1 169 ? -62.991 95.256  20.860  1.00 71.91  ? 167 ALA D O   1 
ATOM   7446 C  CB  . ALA D 1 169 ? -64.937 93.741  19.191  1.00 71.44  ? 167 ALA D CB  1 
ATOM   7447 N  N   . LEU D 1 170 ? -63.782 96.985  19.658  1.00 79.73  ? 168 LEU D N   1 
ATOM   7448 C  CA  . LEU D 1 170 ? -62.594 97.816  19.858  1.00 82.15  ? 168 LEU D CA  1 
ATOM   7449 C  C   . LEU D 1 170 ? -62.504 98.330  21.302  1.00 83.53  ? 168 LEU D C   1 
ATOM   7450 O  O   . LEU D 1 170 ? -61.400 98.539  21.833  1.00 76.18  ? 168 LEU D O   1 
ATOM   7451 C  CB  . LEU D 1 170 ? -62.568 98.973  18.855  1.00 80.24  ? 168 LEU D CB  1 
ATOM   7452 C  CG  . LEU D 1 170 ? -62.536 98.627  17.355  1.00 79.71  ? 168 LEU D CG  1 
ATOM   7453 C  CD1 . LEU D 1 170 ? -62.701 99.870  16.491  1.00 77.99  ? 168 LEU D CD1 1 
ATOM   7454 C  CD2 . LEU D 1 170 ? -61.270 97.875  16.968  1.00 77.11  ? 168 LEU D CD2 1 
ATOM   7455 N  N   . SER D 1 171 ? -63.678 98.503  21.922  1.00 90.91  ? 169 SER D N   1 
ATOM   7456 C  CA  . SER D 1 171 ? -63.830 98.941  23.322  1.00 89.94  ? 169 SER D CA  1 
ATOM   7457 C  C   . SER D 1 171 ? -62.892 98.217  24.283  1.00 88.85  ? 169 SER D C   1 
ATOM   7458 O  O   . SER D 1 171 ? -62.348 98.828  25.206  1.00 82.42  ? 169 SER D O   1 
ATOM   7459 C  CB  . SER D 1 171 ? -65.280 98.734  23.793  1.00 90.17  ? 169 SER D CB  1 
ATOM   7460 O  OG  . SER D 1 171 ? -66.180 99.601  23.121  1.00 83.76  ? 169 SER D OG  1 
ATOM   7461 N  N   . ASN D 1 172 ? -62.693 96.922  24.039  1.00 89.06  ? 170 ASN D N   1 
ATOM   7462 C  CA  . ASN D 1 172 ? -61.959 96.064  24.960  1.00 86.76  ? 170 ASN D CA  1 
ATOM   7463 C  C   . ASN D 1 172 ? -60.550 95.695  24.494  1.00 89.70  ? 170 ASN D C   1 
ATOM   7464 O  O   . ASN D 1 172 ? -60.020 94.663  24.903  1.00 93.37  ? 170 ASN D O   1 
ATOM   7465 C  CB  . ASN D 1 172 ? -62.782 94.806  25.262  1.00 83.02  ? 170 ASN D CB  1 
ATOM   7466 C  CG  . ASN D 1 172 ? -64.267 95.105  25.409  1.00 82.42  ? 170 ASN D CG  1 
ATOM   7467 O  OD1 . ASN D 1 172 ? -64.713 95.632  26.436  1.00 81.59  ? 170 ASN D OD1 1 
ATOM   7468 N  ND2 . ASN D 1 172 ? -65.040 94.780  24.372  1.00 69.62  ? 170 ASN D ND2 1 
ATOM   7469 N  N   . ILE D 1 173 ? -59.954 96.536  23.643  1.00 90.38  ? 171 ILE D N   1 
ATOM   7470 C  CA  . ILE D 1 173 ? -58.538 96.403  23.241  1.00 89.65  ? 171 ILE D CA  1 
ATOM   7471 C  C   . ILE D 1 173 ? -57.895 97.726  22.806  1.00 87.70  ? 171 ILE D C   1 
ATOM   7472 O  O   . ILE D 1 173 ? -57.300 97.795  21.726  1.00 88.31  ? 171 ILE D O   1 
ATOM   7473 C  CB  . ILE D 1 173 ? -58.319 95.397  22.080  1.00 90.39  ? 171 ILE D CB  1 
ATOM   7474 C  CG1 . ILE D 1 173 ? -59.420 95.533  21.021  1.00 89.29  ? 171 ILE D CG1 1 
ATOM   7475 C  CG2 . ILE D 1 173 ? -58.171 93.973  22.596  1.00 87.47  ? 171 ILE D CG2 1 
ATOM   7476 C  CD1 . ILE D 1 173 ? -58.882 95.535  19.608  1.00 86.72  ? 171 ILE D CD1 1 
ATOM   7477 N  N   . PRO D 1 174 ? -58.004 98.780  23.636  1.00 87.24  ? 172 PRO D N   1 
ATOM   7478 C  CA  . PRO D 1 174 ? -57.323 100.032 23.287  1.00 79.52  ? 172 PRO D CA  1 
ATOM   7479 C  C   . PRO D 1 174 ? -55.791 100.027 23.461  1.00 78.59  ? 172 PRO D C   1 
ATOM   7480 O  O   . PRO D 1 174 ? -55.115 100.841 22.835  1.00 81.18  ? 172 PRO D O   1 
ATOM   7481 C  CB  . PRO D 1 174 ? -57.979 101.059 24.214  1.00 81.73  ? 172 PRO D CB  1 
ATOM   7482 C  CG  . PRO D 1 174 ? -58.482 100.267 25.369  1.00 82.47  ? 172 PRO D CG  1 
ATOM   7483 C  CD  . PRO D 1 174 ? -58.875 98.933  24.816  1.00 86.22  ? 172 PRO D CD  1 
ATOM   7484 N  N   . LYS D 1 175 ? -55.253 99.141  24.297  1.00 78.16  ? 173 LYS D N   1 
ATOM   7485 C  CA  . LYS D 1 175 ? -53.794 99.018  24.487  1.00 81.24  ? 173 LYS D CA  1 
ATOM   7486 C  C   . LYS D 1 175 ? -53.155 98.081  23.460  1.00 81.07  ? 173 LYS D C   1 
ATOM   7487 O  O   . LYS D 1 175 ? -53.842 97.231  22.890  1.00 88.15  ? 173 LYS D O   1 
ATOM   7488 C  CB  . LYS D 1 175 ? -53.465 98.455  25.883  1.00 87.39  ? 173 LYS D CB  1 
ATOM   7489 C  CG  . LYS D 1 175 ? -53.267 99.458  27.008  1.00 90.11  ? 173 LYS D CG  1 
ATOM   7490 C  CD  . LYS D 1 175 ? -52.378 98.845  28.085  1.00 93.76  ? 173 LYS D CD  1 
ATOM   7491 C  CE  . LYS D 1 175 ? -52.277 99.714  29.331  1.00 97.54  ? 173 LYS D CE  1 
ATOM   7492 N  NZ  . LYS D 1 175 ? -53.525 99.695  30.149  1.00 101.53 ? 173 LYS D NZ  1 
ATOM   7493 N  N   . PRO D 1 176 ? -51.833 98.217  23.233  1.00 78.18  ? 174 PRO D N   1 
ATOM   7494 C  CA  . PRO D 1 176 ? -51.079 97.180  22.514  1.00 78.82  ? 174 PRO D CA  1 
ATOM   7495 C  C   . PRO D 1 176 ? -51.080 95.832  23.237  1.00 79.39  ? 174 PRO D C   1 
ATOM   7496 O  O   . PRO D 1 176 ? -51.431 95.762  24.416  1.00 84.59  ? 174 PRO D O   1 
ATOM   7497 C  CB  . PRO D 1 176 ? -49.654 97.742  22.477  1.00 72.74  ? 174 PRO D CB  1 
ATOM   7498 C  CG  . PRO D 1 176 ? -49.828 99.211  22.546  1.00 71.46  ? 174 PRO D CG  1 
ATOM   7499 C  CD  . PRO D 1 176 ? -51.042 99.451  23.400  1.00 76.71  ? 174 PRO D CD  1 
ATOM   7500 N  N   . GLU D 1 177 ? -50.701 94.775  22.518  1.00 78.21  ? 175 GLU D N   1 
ATOM   7501 C  CA  . GLU D 1 177 ? -50.517 93.427  23.080  1.00 75.75  ? 175 GLU D CA  1 
ATOM   7502 C  C   . GLU D 1 177 ? -51.809 92.805  23.579  1.00 69.60  ? 175 GLU D C   1 
ATOM   7503 O  O   . GLU D 1 177 ? -51.814 91.652  23.979  1.00 61.58  ? 175 GLU D O   1 
ATOM   7504 C  CB  . GLU D 1 177 ? -49.483 93.425  24.226  1.00 84.89  ? 175 GLU D CB  1 
ATOM   7505 C  CG  . GLU D 1 177 ? -48.097 93.977  23.890  1.00 92.29  ? 175 GLU D CG  1 
ATOM   7506 C  CD  . GLU D 1 177 ? -47.129 92.924  23.366  1.00 94.92  ? 175 GLU D CD  1 
ATOM   7507 O  OE1 . GLU D 1 177 ? -46.119 92.646  24.052  1.00 95.24  ? 175 GLU D OE1 1 
ATOM   7508 O  OE2 . GLU D 1 177 ? -47.367 92.375  22.269  1.00 99.45  ? 175 GLU D OE2 1 
ATOM   7509 N  N   . MET D 1 178 ? -52.893 93.574  23.558  1.00 73.67  ? 176 MET D N   1 
ATOM   7510 C  CA  . MET D 1 178 ? -54.164 93.164  24.150  1.00 76.06  ? 176 MET D CA  1 
ATOM   7511 C  C   . MET D 1 178 ? -55.026 92.368  23.191  1.00 80.21  ? 176 MET D C   1 
ATOM   7512 O  O   . MET D 1 178 ? -55.258 92.811  22.066  1.00 85.59  ? 176 MET D O   1 
ATOM   7513 C  CB  . MET D 1 178 ? -54.954 94.392  24.557  1.00 80.97  ? 176 MET D CB  1 
ATOM   7514 C  CG  . MET D 1 178 ? -54.584 94.981  25.903  1.00 86.96  ? 176 MET D CG  1 
ATOM   7515 S  SD  . MET D 1 178 ? -55.853 96.172  26.388  1.00 96.29  ? 176 MET D SD  1 
ATOM   7516 C  CE  . MET D 1 178 ? -57.260 95.092  26.650  1.00 97.53  ? 176 MET D CE  1 
ATOM   7517 N  N   . SER D 1 179 ? -55.516 91.213  23.647  1.00 79.70  ? 177 SER D N   1 
ATOM   7518 C  CA  . SER D 1 179 ? -56.438 90.353  22.874  1.00 75.98  ? 177 SER D CA  1 
ATOM   7519 C  C   . SER D 1 179 ? -57.902 90.534  23.287  1.00 73.47  ? 177 SER D C   1 
ATOM   7520 O  O   . SER D 1 179 ? -58.182 90.945  24.411  1.00 75.75  ? 177 SER D O   1 
ATOM   7521 C  CB  . SER D 1 179 ? -56.060 88.872  23.035  1.00 76.72  ? 177 SER D CB  1 
ATOM   7522 O  OG  . SER D 1 179 ? -55.474 88.341  21.859  1.00 76.67  ? 177 SER D OG  1 
ATOM   7523 N  N   . THR D 1 180 ? -58.827 90.226  22.380  1.00 64.57  ? 178 THR D N   1 
ATOM   7524 C  CA  . THR D 1 180 ? -60.249 90.157  22.729  1.00 64.84  ? 178 THR D CA  1 
ATOM   7525 C  C   . THR D 1 180 ? -60.984 89.185  21.789  1.00 66.04  ? 178 THR D C   1 
ATOM   7526 O  O   . THR D 1 180 ? -60.324 88.342  21.157  1.00 68.68  ? 178 THR D O   1 
ATOM   7527 C  CB  . THR D 1 180 ? -60.915 91.556  22.862  1.00 69.37  ? 178 THR D CB  1 
ATOM   7528 O  OG1 . THR D 1 180 ? -62.146 91.440  23.580  1.00 69.04  ? 178 THR D OG1 1 
ATOM   7529 C  CG2 . THR D 1 180 ? -61.181 92.209  21.505  1.00 70.77  ? 178 THR D CG2 1 
ATOM   7530 N  N   . THR D 1 181 ? -62.320 89.264  21.720  1.00 61.07  ? 179 THR D N   1 
ATOM   7531 C  CA  . THR D 1 181 ? -63.118 88.262  20.992  1.00 62.13  ? 179 THR D CA  1 
ATOM   7532 C  C   . THR D 1 181 ? -64.390 88.841  20.367  1.00 66.03  ? 179 THR D C   1 
ATOM   7533 O  O   . THR D 1 181 ? -65.335 89.200  21.061  1.00 62.66  ? 179 THR D O   1 
ATOM   7534 C  CB  . THR D 1 181 ? -63.505 87.041  21.878  1.00 62.58  ? 179 THR D CB  1 
ATOM   7535 O  OG1 . THR D 1 181 ? -62.582 86.899  22.974  1.00 53.89  ? 179 THR D OG1 1 
ATOM   7536 C  CG2 . THR D 1 181 ? -63.547 85.752  21.041  1.00 56.36  ? 179 THR D CG2 1 
ATOM   7537 N  N   . MET D 1 182 ? -64.408 88.894  19.037  1.00 73.49  ? 180 MET D N   1 
ATOM   7538 C  CA  . MET D 1 182 ? -65.491 89.518  18.285  1.00 73.46  ? 180 MET D CA  1 
ATOM   7539 C  C   . MET D 1 182 ? -66.748 88.671  18.387  1.00 73.56  ? 180 MET D C   1 
ATOM   7540 O  O   . MET D 1 182 ? -66.664 87.451  18.506  1.00 77.80  ? 180 MET D O   1 
ATOM   7541 C  CB  . MET D 1 182 ? -65.074 89.656  16.814  1.00 74.53  ? 180 MET D CB  1 
ATOM   7542 C  CG  . MET D 1 182 ? -65.710 90.823  16.073  1.00 70.80  ? 180 MET D CG  1 
ATOM   7543 S  SD  . MET D 1 182 ? -65.020 91.102  14.426  1.00 66.29  ? 180 MET D SD  1 
ATOM   7544 C  CE  . MET D 1 182 ? -65.988 89.961  13.441  1.00 70.23  ? 180 MET D CE  1 
ATOM   7545 N  N   . ALA D 1 183 ? -67.909 89.312  18.330  1.00 74.82  ? 181 ALA D N   1 
ATOM   7546 C  CA  . ALA D 1 183 ? -69.181 88.588  18.328  1.00 71.09  ? 181 ALA D CA  1 
ATOM   7547 C  C   . ALA D 1 183 ? -69.338 87.674  17.105  1.00 73.21  ? 181 ALA D C   1 
ATOM   7548 O  O   . ALA D 1 183 ? -68.546 87.731  16.154  1.00 68.43  ? 181 ALA D O   1 
ATOM   7549 C  CB  . ALA D 1 183 ? -70.346 89.568  18.416  1.00 73.26  ? 181 ALA D CB  1 
ATOM   7550 N  N   . GLU D 1 184 ? -70.372 86.835  17.165  1.00 74.87  ? 182 GLU D N   1 
ATOM   7551 C  CA  . GLU D 1 184 ? -70.793 85.934  16.093  1.00 73.46  ? 182 GLU D CA  1 
ATOM   7552 C  C   . GLU D 1 184 ? -71.011 86.637  14.757  1.00 68.79  ? 182 GLU D C   1 
ATOM   7553 O  O   . GLU D 1 184 ? -72.029 87.311  14.552  1.00 62.12  ? 182 GLU D O   1 
ATOM   7554 C  CB  . GLU D 1 184 ? -72.072 85.215  16.517  1.00 78.66  ? 182 GLU D CB  1 
ATOM   7555 C  CG  . GLU D 1 184 ? -71.888 83.749  16.853  1.00 86.56  ? 182 GLU D CG  1 
ATOM   7556 C  CD  . GLU D 1 184 ? -72.358 82.860  15.725  1.00 92.72  ? 182 GLU D CD  1 
ATOM   7557 O  OE1 . GLU D 1 184 ? -71.516 82.140  15.146  1.00 94.38  ? 182 GLU D OE1 1 
ATOM   7558 O  OE2 . GLU D 1 184 ? -73.572 82.898  15.410  1.00 97.21  ? 182 GLU D OE2 1 
ATOM   7559 N  N   . SER D 1 185 ? -70.057 86.461  13.845  1.00 66.80  ? 183 SER D N   1 
ATOM   7560 C  CA  . SER D 1 185 ? -70.060 87.223  12.595  1.00 70.06  ? 183 SER D CA  1 
ATOM   7561 C  C   . SER D 1 185 ? -69.334 86.567  11.430  1.00 67.77  ? 183 SER D C   1 
ATOM   7562 O  O   . SER D 1 185 ? -68.223 86.077  11.575  1.00 67.35  ? 183 SER D O   1 
ATOM   7563 C  CB  . SER D 1 185 ? -69.500 88.623  12.821  1.00 61.34  ? 183 SER D CB  1 
ATOM   7564 O  OG  . SER D 1 185 ? -70.237 89.543  12.040  1.00 62.54  ? 183 SER D OG  1 
ATOM   7565 N  N   . SER D 1 186 ? -69.978 86.589  10.267  1.00 73.14  ? 184 SER D N   1 
ATOM   7566 C  CA  . SER D 1 186 ? -69.406 86.022  9.048   1.00 70.96  ? 184 SER D CA  1 
ATOM   7567 C  C   . SER D 1 186 ? -68.453 87.029  8.425   1.00 69.27  ? 184 SER D C   1 
ATOM   7568 O  O   . SER D 1 186 ? -68.438 88.201  8.815   1.00 77.14  ? 184 SER D O   1 
ATOM   7569 C  CB  . SER D 1 186 ? -70.510 85.626  8.057   1.00 74.72  ? 184 SER D CB  1 
ATOM   7570 O  OG  . SER D 1 186 ? -71.156 86.759  7.501   1.00 73.43  ? 184 SER D OG  1 
ATOM   7571 N  N   . LEU D 1 187 ? -67.642 86.570  7.478   1.00 62.87  ? 185 LEU D N   1 
ATOM   7572 C  CA  . LEU D 1 187 ? -66.666 87.432  6.823   1.00 59.25  ? 185 LEU D CA  1 
ATOM   7573 C  C   . LEU D 1 187 ? -67.313 88.213  5.685   1.00 60.00  ? 185 LEU D C   1 
ATOM   7574 O  O   . LEU D 1 187 ? -66.731 89.173  5.180   1.00 63.69  ? 185 LEU D O   1 
ATOM   7575 C  CB  . LEU D 1 187 ? -65.443 86.642  6.315   1.00 50.70  ? 185 LEU D CB  1 
ATOM   7576 C  CG  . LEU D 1 187 ? -64.122 86.546  7.112   1.00 53.06  ? 185 LEU D CG  1 
ATOM   7577 C  CD1 . LEU D 1 187 ? -63.035 85.775  6.359   1.00 42.41  ? 185 LEU D CD1 1 
ATOM   7578 C  CD2 . LEU D 1 187 ? -63.568 87.895  7.549   1.00 47.27  ? 185 LEU D CD2 1 
ATOM   7579 N  N   . LEU D 1 188 ? -68.514 87.798  5.293   1.00 65.79  ? 186 LEU D N   1 
ATOM   7580 C  CA  . LEU D 1 188 ? -69.252 88.438  4.206   1.00 68.03  ? 186 LEU D CA  1 
ATOM   7581 C  C   . LEU D 1 188 ? -70.004 89.636  4.749   1.00 71.85  ? 186 LEU D C   1 
ATOM   7582 O  O   . LEU D 1 188 ? -70.486 90.481  3.981   1.00 74.51  ? 186 LEU D O   1 
ATOM   7583 C  CB  . LEU D 1 188 ? -70.235 87.451  3.561   1.00 74.61  ? 186 LEU D CB  1 
ATOM   7584 C  CG  . LEU D 1 188 ? -70.552 87.571  2.065   1.00 74.55  ? 186 LEU D CG  1 
ATOM   7585 C  CD1 . LEU D 1 188 ? -69.308 87.328  1.210   1.00 78.52  ? 186 LEU D CD1 1 
ATOM   7586 C  CD2 . LEU D 1 188 ? -71.658 86.597  1.684   1.00 72.36  ? 186 LEU D CD2 1 
ATOM   7587 N  N   . ASP D 1 189 ? -70.104 89.697  6.078   1.00 71.86  ? 187 ASP D N   1 
ATOM   7588 C  CA  . ASP D 1 189 ? -70.672 90.858  6.778   1.00 73.70  ? 187 ASP D CA  1 
ATOM   7589 C  C   . ASP D 1 189 ? -69.859 92.116  6.517   1.00 71.23  ? 187 ASP D C   1 
ATOM   7590 O  O   . ASP D 1 189 ? -70.392 93.218  6.534   1.00 71.25  ? 187 ASP D O   1 
ATOM   7591 C  CB  . ASP D 1 189 ? -70.727 90.602  8.287   1.00 69.03  ? 187 ASP D CB  1 
ATOM   7592 C  CG  . ASP D 1 189 ? -71.737 89.541  8.661   1.00 67.96  ? 187 ASP D CG  1 
ATOM   7593 O  OD1 . ASP D 1 189 ? -72.888 89.612  8.167   1.00 65.42  ? 187 ASP D OD1 1 
ATOM   7594 O  OD2 . ASP D 1 189 ? -71.369 88.641  9.443   1.00 66.27  ? 187 ASP D OD2 1 
ATOM   7595 N  N   . LEU D 1 190 ? -68.563 91.924  6.288   1.00 71.88  ? 188 LEU D N   1 
ATOM   7596 C  CA  . LEU D 1 190 ? -67.613 93.014  6.074   1.00 73.56  ? 188 LEU D CA  1 
ATOM   7597 C  C   . LEU D 1 190 ? -67.436 93.291  4.591   1.00 76.54  ? 188 LEU D C   1 
ATOM   7598 O  O   . LEU D 1 190 ? -67.120 94.421  4.196   1.00 74.31  ? 188 LEU D O   1 
ATOM   7599 C  CB  . LEU D 1 190 ? -66.249 92.676  6.701   1.00 66.60  ? 188 LEU D CB  1 
ATOM   7600 C  CG  . LEU D 1 190 ? -66.195 92.198  8.163   1.00 61.91  ? 188 LEU D CG  1 
ATOM   7601 C  CD1 . LEU D 1 190 ? -64.755 92.079  8.656   1.00 55.68  ? 188 LEU D CD1 1 
ATOM   7602 C  CD2 . LEU D 1 190 ? -67.009 93.103  9.084   1.00 61.71  ? 188 LEU D CD2 1 
ATOM   7603 N  N   . LEU D 1 191 ? -67.647 92.250  3.785   1.00 75.36  ? 189 LEU D N   1 
ATOM   7604 C  CA  . LEU D 1 191 ? -67.457 92.321  2.337   1.00 75.51  ? 189 LEU D CA  1 
ATOM   7605 C  C   . LEU D 1 191 ? -68.747 92.617  1.572   1.00 74.90  ? 189 LEU D C   1 
ATOM   7606 O  O   . LEU D 1 191 ? -69.627 91.744  1.461   1.00 70.65  ? 189 LEU D O   1 
ATOM   7607 C  CB  . LEU D 1 191 ? -66.789 91.051  1.805   1.00 76.94  ? 189 LEU D CB  1 
ATOM   7608 C  CG  . LEU D 1 191 ? -65.332 90.801  2.194   1.00 71.63  ? 189 LEU D CG  1 
ATOM   7609 C  CD1 . LEU D 1 191 ? -64.699 90.022  1.055   1.00 70.57  ? 189 LEU D CD1 1 
ATOM   7610 C  CD2 . LEU D 1 191 ? -64.567 92.092  2.461   1.00 65.83  ? 189 LEU D CD2 1 
ATOM   7611 N  N   . PRO D 1 192 ? -68.836 93.845  1.024   1.00 72.67  ? 190 PRO D N   1 
ATOM   7612 C  CA  . PRO D 1 192 ? -69.984 94.468  0.372   1.00 71.36  ? 190 PRO D CA  1 
ATOM   7613 C  C   . PRO D 1 192 ? -70.716 93.486  -0.534  1.00 73.06  ? 190 PRO D C   1 
ATOM   7614 O  O   . PRO D 1 192 ? -70.075 92.730  -1.272  1.00 75.26  ? 190 PRO D O   1 
ATOM   7615 C  CB  . PRO D 1 192 ? -69.351 95.638  -0.409  1.00 74.77  ? 190 PRO D CB  1 
ATOM   7616 C  CG  . PRO D 1 192 ? -67.868 95.389  -0.403  1.00 71.08  ? 190 PRO D CG  1 
ATOM   7617 C  CD  . PRO D 1 192 ? -67.634 94.688  0.896   1.00 73.01  ? 190 PRO D CD  1 
ATOM   7618 N  N   . LYS D 1 193 ? -72.048 93.506  -0.474  1.00 72.52  ? 191 LYS D N   1 
ATOM   7619 C  CA  . LYS D 1 193 ? -72.884 92.543  -1.209  1.00 77.46  ? 191 LYS D CA  1 
ATOM   7620 C  C   . LYS D 1 193 ? -72.034 92.303  -2.478  1.00 80.31  ? 191 LYS D C   1 
ATOM   7621 O  O   . LYS D 1 193 ? -71.711 93.239  -3.220  1.00 77.34  ? 191 LYS D O   1 
ATOM   7622 C  CB  . LYS D 1 193 ? -74.338 93.035  -1.323  1.00 72.76  ? 191 LYS D CB  1 
ATOM   7623 C  CG  . LYS D 1 193 ? -75.297 92.405  -0.324  1.00 63.29  ? 191 LYS D CG  1 
ATOM   7624 C  CD  . LYS D 1 193 ? -76.550 91.908  -1.039  1.00 64.68  ? 191 LYS D CD  1 
ATOM   7625 C  CE  . LYS D 1 193 ? -77.465 91.065  -0.151  1.00 64.62  ? 191 LYS D CE  1 
ATOM   7626 N  NZ  . LYS D 1 193 ? -78.573 91.839  0.491   1.00 54.98  ? 191 LYS D NZ  1 
ATOM   7627 N  N   . GLU D 1 194 ? -71.644 91.045  -2.643  1.00 83.48  ? 192 GLU D N   1 
ATOM   7628 C  CA  . GLU D 1 194 ? -70.744 90.667  -3.720  1.00 79.82  ? 192 GLU D CA  1 
ATOM   7629 C  C   . GLU D 1 194 ? -71.420 90.860  -5.066  1.00 77.47  ? 192 GLU D C   1 
ATOM   7630 O  O   . GLU D 1 194 ? -72.578 91.287  -5.122  1.00 76.85  ? 192 GLU D O   1 
ATOM   7631 C  CB  . GLU D 1 194 ? -70.248 89.229  -3.548  1.00 81.25  ? 192 GLU D CB  1 
ATOM   7632 C  CG  . GLU D 1 194 ? -71.346 88.181  -3.500  1.00 83.41  ? 192 GLU D CG  1 
ATOM   7633 C  CD  . GLU D 1 194 ? -70.927 86.883  -4.159  1.00 83.76  ? 192 GLU D CD  1 
ATOM   7634 O  OE1 . GLU D 1 194 ? -70.838 86.850  -5.404  1.00 80.16  ? 192 GLU D OE1 1 
ATOM   7635 O  OE2 . GLU D 1 194 ? -70.683 85.896  -3.434  1.00 77.12  ? 192 GLU D OE2 1 
ATOM   7636 N  N   . GLU D 1 195 ? -70.684 90.552  -6.123  1.00 68.22  ? 193 GLU D N   1 
ATOM   7637 C  CA  . GLU D 1 195 ? -71.161 90.829  -7.478  1.00 73.98  ? 193 GLU D CA  1 
ATOM   7638 C  C   . GLU D 1 195 ? -70.897 92.224  -8.043  1.00 76.80  ? 193 GLU D C   1 
ATOM   7639 O  O   . GLU D 1 195 ? -71.121 92.458  -9.239  1.00 73.98  ? 193 GLU D O   1 
ATOM   7640 C  CB  . GLU D 1 195 ? -72.655 90.501  -7.552  1.00 72.74  ? 193 GLU D CB  1 
ATOM   7641 C  CG  . GLU D 1 195 ? -73.160 90.284  -8.968  1.00 67.98  ? 193 GLU D CG  1 
ATOM   7642 N  N   . LYS D 1 196 ? -70.412 93.112  -7.170  1.00 73.67  ? 194 LYS D N   1 
ATOM   7643 C  CA  . LYS D 1 196 ? -69.751 94.364  -7.535  1.00 70.44  ? 194 LYS D CA  1 
ATOM   7644 C  C   . LYS D 1 196 ? -68.308 94.197  -7.036  1.00 65.07  ? 194 LYS D C   1 
ATOM   7645 O  O   . LYS D 1 196 ? -67.554 95.167  -6.924  1.00 52.94  ? 194 LYS D O   1 
ATOM   7646 C  CB  . LYS D 1 196 ? -70.425 95.619  -6.960  1.00 75.40  ? 194 LYS D CB  1 
ATOM   7647 C  CG  . LYS D 1 196 ? -70.657 95.646  -5.450  1.00 78.32  ? 194 LYS D CG  1 
ATOM   7648 C  CD  . LYS D 1 196 ? -71.438 96.893  -5.035  1.00 76.34  ? 194 LYS D CD  1 
ATOM   7649 C  CE  . LYS D 1 196 ? -72.680 97.094  -5.896  1.00 73.94  ? 194 LYS D CE  1 
ATOM   7650 N  NZ  . LYS D 1 196 ? -73.731 97.869  -5.183  1.00 75.12  ? 194 LYS D NZ  1 
ATOM   7651 N  N   . LEU D 1 197 ? -67.936 92.946  -6.749  1.00 58.51  ? 195 LEU D N   1 
ATOM   7652 C  CA  . LEU D 1 197 ? -66.545 92.595  -6.507  1.00 54.08  ? 195 LEU D CA  1 
ATOM   7653 C  C   . LEU D 1 197 ? -65.864 92.199  -7.831  1.00 54.25  ? 195 LEU D C   1 
ATOM   7654 O  O   . LEU D 1 197 ? -64.691 91.803  -7.877  1.00 57.12  ? 195 LEU D O   1 
ATOM   7655 C  CB  . LEU D 1 197 ? -66.448 91.531  -5.407  1.00 54.11  ? 195 LEU D CB  1 
ATOM   7656 C  CG  . LEU D 1 197 ? -66.942 92.008  -4.028  1.00 55.40  ? 195 LEU D CG  1 
ATOM   7657 C  CD1 . LEU D 1 197 ? -66.922 90.890  -3.004  1.00 59.45  ? 195 LEU D CD1 1 
ATOM   7658 C  CD2 . LEU D 1 197 ? -66.158 93.209  -3.505  1.00 55.04  ? 195 LEU D CD2 1 
ATOM   7659 N  N   . ARG D 1 198 ? -66.610 92.386  -8.914  1.00 56.23  ? 196 ARG D N   1 
ATOM   7660 C  CA  . ARG D 1 198 ? -66.208 91.999  -10.262 1.00 59.56  ? 196 ARG D CA  1 
ATOM   7661 C  C   . ARG D 1 198 ? -65.107 92.932  -10.746 1.00 53.33  ? 196 ARG D C   1 
ATOM   7662 O  O   . ARG D 1 198 ? -64.252 92.535  -11.535 1.00 51.99  ? 196 ARG D O   1 
ATOM   7663 C  CB  . ARG D 1 198 ? -67.438 92.066  -11.196 1.00 63.79  ? 196 ARG D CB  1 
ATOM   7664 C  CG  . ARG D 1 198 ? -67.505 91.036  -12.320 1.00 62.65  ? 196 ARG D CG  1 
ATOM   7665 C  CD  . ARG D 1 198 ? -67.205 91.623  -13.694 1.00 68.36  ? 196 ARG D CD  1 
ATOM   7666 N  NE  . ARG D 1 198 ? -67.926 92.872  -13.952 1.00 71.61  ? 196 ARG D NE  1 
ATOM   7667 C  CZ  . ARG D 1 198 ? -69.016 93.000  -14.710 1.00 78.22  ? 196 ARG D CZ  1 
ATOM   7668 N  NH1 . ARG D 1 198 ? -69.562 91.950  -15.320 1.00 76.17  ? 196 ARG D NH1 1 
ATOM   7669 N  NH2 . ARG D 1 198 ? -69.566 94.200  -14.865 1.00 83.82  ? 196 ARG D NH2 1 
ATOM   7670 N  N   . HIS D 1 199 ? -65.139 94.166  -10.242 1.00 50.60  ? 197 HIS D N   1 
ATOM   7671 C  CA  . HIS D 1 199 ? -64.213 95.217  -10.662 1.00 42.38  ? 197 HIS D CA  1 
ATOM   7672 C  C   . HIS D 1 199 ? -63.074 95.409  -9.708  1.00 38.22  ? 197 HIS D C   1 
ATOM   7673 O  O   . HIS D 1 199 ? -63.263 95.826  -8.558  1.00 36.69  ? 197 HIS D O   1 
ATOM   7674 C  CB  . HIS D 1 199 ? -64.975 96.525  -10.900 1.00 45.53  ? 197 HIS D CB  1 
ATOM   7675 C  CG  . HIS D 1 199 ? -65.847 96.500  -12.138 1.00 49.84  ? 197 HIS D CG  1 
ATOM   7676 N  ND1 . HIS D 1 199 ? -65.339 96.642  -13.388 1.00 51.87  ? 197 HIS D ND1 1 
ATOM   7677 C  CD2 . HIS D 1 199 ? -67.235 96.333  -12.290 1.00 54.00  ? 197 HIS D CD2 1 
ATOM   7678 C  CE1 . HIS D 1 199 ? -66.349 96.570  -14.293 1.00 58.83  ? 197 HIS D CE1 1 
ATOM   7679 N  NE2 . HIS D 1 199 ? -67.509 96.389  -13.620 1.00 55.06  ? 197 HIS D NE2 1 
ATOM   7680 N  N   . TYR D 1 200 ? -61.873 95.087  -10.170 1.00 35.06  ? 198 TYR D N   1 
ATOM   7681 C  CA  . TYR D 1 200 ? -60.669 95.256  -9.371  1.00 32.77  ? 198 TYR D CA  1 
ATOM   7682 C  C   . TYR D 1 200 ? -59.435 95.530  -10.207 1.00 35.82  ? 198 TYR D C   1 
ATOM   7683 O  O   . TYR D 1 200 ? -59.398 95.240  -11.424 1.00 36.11  ? 198 TYR D O   1 
ATOM   7684 C  CB  . TYR D 1 200 ? -60.422 94.073  -8.417  1.00 35.57  ? 198 TYR D CB  1 
ATOM   7685 C  CG  . TYR D 1 200 ? -60.157 92.717  -9.079  1.00 39.28  ? 198 TYR D CG  1 
ATOM   7686 C  CD1 . TYR D 1 200 ? -58.901 92.386  -9.588  1.00 36.36  ? 198 TYR D CD1 1 
ATOM   7687 C  CD2 . TYR D 1 200 ? -61.155 91.750  -9.136  1.00 37.90  ? 198 TYR D CD2 1 
ATOM   7688 C  CE1 . TYR D 1 200 ? -58.672 91.151  -10.182 1.00 37.84  ? 198 TYR D CE1 1 
ATOM   7689 C  CE2 . TYR D 1 200 ? -60.924 90.510  -9.710  1.00 39.78  ? 198 TYR D CE2 1 
ATOM   7690 C  CZ  . TYR D 1 200 ? -59.684 90.215  -10.234 1.00 41.41  ? 198 TYR D CZ  1 
ATOM   7691 O  OH  . TYR D 1 200 ? -59.475 88.972  -10.818 1.00 39.47  ? 198 TYR D OH  1 
ATOM   7692 N  N   . PHE D 1 201 ? -58.435 96.095  -9.528  1.00 33.33  ? 199 PHE D N   1 
ATOM   7693 C  CA  . PHE D 1 201 ? -57.099 96.321  -10.048 1.00 31.12  ? 199 PHE D CA  1 
ATOM   7694 C  C   . PHE D 1 201 ? -56.167 95.378  -9.393  1.00 31.63  ? 199 PHE D C   1 
ATOM   7695 O  O   . PHE D 1 201 ? -56.429 94.903  -8.284  1.00 37.09  ? 199 PHE D O   1 
ATOM   7696 C  CB  . PHE D 1 201 ? -56.613 97.751  -9.707  1.00 30.93  ? 199 PHE D CB  1 
ATOM   7697 C  CG  . PHE D 1 201 ? -57.563 98.785  -10.115 1.00 29.76  ? 199 PHE D CG  1 
ATOM   7698 C  CD1 . PHE D 1 201 ? -57.530 99.298  -11.404 1.00 32.27  ? 199 PHE D CD1 1 
ATOM   7699 C  CD2 . PHE D 1 201 ? -58.579 99.198  -9.231  1.00 31.58  ? 199 PHE D CD2 1 
ATOM   7700 C  CE1 . PHE D 1 201 ? -58.473 100.224 -11.800 1.00 32.45  ? 199 PHE D CE1 1 
ATOM   7701 C  CE2 . PHE D 1 201 ? -59.512 100.119 -9.621  1.00 26.95  ? 199 PHE D CE2 1 
ATOM   7702 C  CZ  . PHE D 1 201 ? -59.463 100.632 -10.902 1.00 32.34  ? 199 PHE D CZ  1 
ATOM   7703 N  N   . ARG D 1 202 ? -55.044 95.143  -10.058 1.00 32.68  ? 200 ARG D N   1 
ATOM   7704 C  CA  . ARG D 1 202 ? -54.136 94.091  -9.723  1.00 32.69  ? 200 ARG D CA  1 
ATOM   7705 C  C   . ARG D 1 202 ? -52.752 94.485  -10.161 1.00 32.58  ? 200 ARG D C   1 
ATOM   7706 O  O   . ARG D 1 202 ? -52.561 95.021  -11.255 1.00 37.87  ? 200 ARG D O   1 
ATOM   7707 C  CB  . ARG D 1 202 ? -54.594 92.828  -10.479 1.00 39.00  ? 200 ARG D CB  1 
ATOM   7708 C  CG  . ARG D 1 202 ? -53.541 91.761  -10.808 1.00 35.34  ? 200 ARG D CG  1 
ATOM   7709 C  CD  . ARG D 1 202 ? -53.159 90.896  -9.631  1.00 36.64  ? 200 ARG D CD  1 
ATOM   7710 N  NE  . ARG D 1 202 ? -54.306 90.575  -8.768  1.00 40.18  ? 200 ARG D NE  1 
ATOM   7711 C  CZ  . ARG D 1 202 ? -55.089 89.504  -8.902  1.00 44.21  ? 200 ARG D CZ  1 
ATOM   7712 N  NH1 . ARG D 1 202 ? -54.863 88.614  -9.875  1.00 37.96  ? 200 ARG D NH1 1 
ATOM   7713 N  NH2 . ARG D 1 202 ? -56.111 89.325  -8.063  1.00 42.61  ? 200 ARG D NH2 1 
ATOM   7714 N  N   . TYR D 1 203 ? -51.770 94.193  -9.337  1.00 32.30  ? 201 TYR D N   1 
ATOM   7715 C  CA  . TYR D 1 203 ? -50.415 94.516  -9.683  1.00 35.07  ? 201 TYR D CA  1 
ATOM   7716 C  C   . TYR D 1 203 ? -49.602 93.751  -8.680  1.00 37.22  ? 201 TYR D C   1 
ATOM   7717 O  O   . TYR D 1 203 ? -50.150 93.185  -7.719  1.00 37.33  ? 201 TYR D O   1 
ATOM   7718 C  CB  . TYR D 1 203 ? -50.132 96.045  -9.634  1.00 39.27  ? 201 TYR D CB  1 
ATOM   7719 C  CG  . TYR D 1 203 ? -50.003 96.621  -8.228  1.00 38.24  ? 201 TYR D CG  1 
ATOM   7720 C  CD1 . TYR D 1 203 ? -51.127 97.090  -7.527  1.00 38.43  ? 201 TYR D CD1 1 
ATOM   7721 C  CD2 . TYR D 1 203 ? -48.759 96.689  -7.596  1.00 37.02  ? 201 TYR D CD2 1 
ATOM   7722 C  CE1 . TYR D 1 203 ? -50.994 97.613  -6.241  1.00 36.33  ? 201 TYR D CE1 1 
ATOM   7723 C  CE2 . TYR D 1 203 ? -48.623 97.191  -6.310  1.00 38.08  ? 201 TYR D CE2 1 
ATOM   7724 C  CZ  . TYR D 1 203 ? -49.732 97.649  -5.637  1.00 38.30  ? 201 TYR D CZ  1 
ATOM   7725 O  OH  . TYR D 1 203 ? -49.571 98.128  -4.348  1.00 42.76  ? 201 TYR D OH  1 
ATOM   7726 N  N   . LEU D 1 204 ? -48.298 93.738  -8.917  1.00 41.24  ? 202 LEU D N   1 
ATOM   7727 C  CA  . LEU D 1 204 ? -47.351 93.038  -8.091  1.00 46.64  ? 202 LEU D CA  1 
ATOM   7728 C  C   . LEU D 1 204 ? -46.544 94.051  -7.331  1.00 49.34  ? 202 LEU D C   1 
ATOM   7729 O  O   . LEU D 1 204 ? -46.092 95.059  -7.899  1.00 49.23  ? 202 LEU D O   1 
ATOM   7730 C  CB  . LEU D 1 204 ? -46.441 92.148  -8.961  1.00 51.58  ? 202 LEU D CB  1 
ATOM   7731 C  CG  . LEU D 1 204 ? -47.137 90.870  -9.491  1.00 56.10  ? 202 LEU D CG  1 
ATOM   7732 C  CD1 . LEU D 1 204 ? -46.483 90.270  -10.747 1.00 57.76  ? 202 LEU D CD1 1 
ATOM   7733 C  CD2 . LEU D 1 204 ? -47.286 89.826  -8.394  1.00 53.27  ? 202 LEU D CD2 1 
ATOM   7734 N  N   . GLY D 1 205 ? -46.361 93.770  -6.042  1.00 54.89  ? 203 GLY D N   1 
ATOM   7735 C  CA  . GLY D 1 205 ? -45.636 94.661  -5.154  1.00 51.86  ? 203 GLY D CA  1 
ATOM   7736 C  C   . GLY D 1 205 ? -45.241 94.040  -3.838  1.00 50.60  ? 203 GLY D C   1 
ATOM   7737 O  O   . GLY D 1 205 ? -45.003 92.829  -3.768  1.00 53.40  ? 203 GLY D O   1 
ATOM   7738 N  N   . SER D 1 206 ? -45.206 94.870  -2.786  1.00 49.17  ? 204 SER D N   1 
ATOM   7739 C  CA  . SER D 1 206 ? -44.664 94.450  -1.490  1.00 49.75  ? 204 SER D CA  1 
ATOM   7740 C  C   . SER D 1 206 ? -45.637 94.540  -0.319  1.00 49.02  ? 204 SER D C   1 
ATOM   7741 O  O   . SER D 1 206 ? -46.810 94.887  -0.500  1.00 44.93  ? 204 SER D O   1 
ATOM   7742 C  CB  . SER D 1 206 ? -43.372 95.207  -1.147  1.00 51.94  ? 204 SER D CB  1 
ATOM   7743 O  OG  . SER D 1 206 ? -43.637 96.454  -0.513  1.00 58.47  ? 204 SER D OG  1 
ATOM   7744 N  N   . LEU D 1 207 ? -45.134 94.171  0.865   1.00 48.79  ? 205 LEU D N   1 
ATOM   7745 C  CA  . LEU D 1 207 ? -45.783 94.475  2.153   1.00 53.27  ? 205 LEU D CA  1 
ATOM   7746 C  C   . LEU D 1 207 ? -45.626 95.976  2.427   1.00 47.43  ? 205 LEU D C   1 
ATOM   7747 O  O   . LEU D 1 207 ? -44.635 96.583  2.010   1.00 42.88  ? 205 LEU D O   1 
ATOM   7748 C  CB  . LEU D 1 207 ? -45.121 93.700  3.294   1.00 56.85  ? 205 LEU D CB  1 
ATOM   7749 C  CG  . LEU D 1 207 ? -45.420 92.228  3.567   1.00 58.73  ? 205 LEU D CG  1 
ATOM   7750 C  CD1 . LEU D 1 207 ? -44.342 91.662  4.492   1.00 57.36  ? 205 LEU D CD1 1 
ATOM   7751 C  CD2 . LEU D 1 207 ? -46.821 92.046  4.165   1.00 60.80  ? 205 LEU D CD2 1 
ATOM   7752 N  N   . THR D 1 208 ? -46.591 96.560  3.130   1.00 50.28  ? 206 THR D N   1 
ATOM   7753 C  CA  . THR D 1 208 ? -46.558 98.001  3.440   1.00 50.15  ? 206 THR D CA  1 
ATOM   7754 C  C   . THR D 1 208 ? -45.944 98.329  4.792   1.00 54.62  ? 206 THR D C   1 
ATOM   7755 O  O   . THR D 1 208 ? -46.022 99.474  5.245   1.00 58.89  ? 206 THR D O   1 
ATOM   7756 C  CB  . THR D 1 208 ? -47.962 98.624  3.399   1.00 45.33  ? 206 THR D CB  1 
ATOM   7757 O  OG1 . THR D 1 208 ? -48.791 97.998  4.380   1.00 42.47  ? 206 THR D OG1 1 
ATOM   7758 C  CG2 . THR D 1 208 ? -48.583 98.451  2.018   1.00 45.81  ? 206 THR D CG2 1 
ATOM   7759 N  N   . THR D 1 209 ? -45.375 97.314  5.442   1.00 59.72  ? 207 THR D N   1 
ATOM   7760 C  CA  . THR D 1 209 ? -44.639 97.466  6.699   1.00 57.61  ? 207 THR D CA  1 
ATOM   7761 C  C   . THR D 1 209 ? -43.322 96.710  6.604   1.00 57.82  ? 207 THR D C   1 
ATOM   7762 O  O   . THR D 1 209 ? -43.195 95.801  5.788   1.00 66.02  ? 207 THR D O   1 
ATOM   7763 C  CB  . THR D 1 209 ? -45.418 96.873  7.871   1.00 59.23  ? 207 THR D CB  1 
ATOM   7764 O  OG1 . THR D 1 209 ? -45.668 95.487  7.613   1.00 56.87  ? 207 THR D OG1 1 
ATOM   7765 C  CG2 . THR D 1 209 ? -46.735 97.618  8.071   1.00 60.89  ? 207 THR D CG2 1 
ATOM   7766 N  N   . PRO D 1 210 ? -42.331 97.076  7.435   1.00 58.26  ? 208 PRO D N   1 
ATOM   7767 C  CA  . PRO D 1 210 ? -41.080 96.319  7.458   1.00 54.68  ? 208 PRO D CA  1 
ATOM   7768 C  C   . PRO D 1 210 ? -41.330 94.820  7.669   1.00 57.44  ? 208 PRO D C   1 
ATOM   7769 O  O   . PRO D 1 210 ? -42.165 94.455  8.503   1.00 56.67  ? 208 PRO D O   1 
ATOM   7770 C  CB  . PRO D 1 210 ? -40.334 96.931  8.641   1.00 58.19  ? 208 PRO D CB  1 
ATOM   7771 C  CG  . PRO D 1 210 ? -40.814 98.348  8.690   1.00 57.83  ? 208 PRO D CG  1 
ATOM   7772 C  CD  . PRO D 1 210 ? -42.252 98.298  8.263   1.00 57.98  ? 208 PRO D CD  1 
ATOM   7773 N  N   . THR D 1 211 ? -40.598 93.965  6.948   1.00 54.23  ? 209 THR D N   1 
ATOM   7774 C  CA  . THR D 1 211 ? -39.405 94.391  6.210   1.00 57.46  ? 209 THR D CA  1 
ATOM   7775 C  C   . THR D 1 211 ? -39.585 94.586  4.692   1.00 59.40  ? 209 THR D C   1 
ATOM   7776 O  O   . THR D 1 211 ? -38.602 94.537  3.937   1.00 61.80  ? 209 THR D O   1 
ATOM   7777 C  CB  . THR D 1 211 ? -38.177 93.499  6.519   1.00 61.01  ? 209 THR D CB  1 
ATOM   7778 O  OG1 . THR D 1 211 ? -37.923 92.620  5.416   1.00 62.45  ? 209 THR D OG1 1 
ATOM   7779 C  CG2 . THR D 1 211 ? -38.386 92.693  7.823   1.00 59.28  ? 209 THR D CG2 1 
ATOM   7780 N  N   . CYS D 1 212 ? -40.832 94.819  4.270   1.00 54.55  ? 210 CYS D N   1 
ATOM   7781 C  CA  . CYS D 1 212 ? -41.172 95.247  2.904   1.00 57.40  ? 210 CYS D CA  1 
ATOM   7782 C  C   . CYS D 1 212 ? -40.864 94.247  1.773   1.00 59.55  ? 210 CYS D C   1 
ATOM   7783 O  O   . CYS D 1 212 ? -40.543 94.662  0.647   1.00 63.97  ? 210 CYS D O   1 
ATOM   7784 C  CB  . CYS D 1 212 ? -40.534 96.605  2.578   1.00 60.20  ? 210 CYS D CB  1 
ATOM   7785 S  SG  . CYS D 1 212 ? -40.903 97.949  3.739   1.00 62.08  ? 210 CYS D SG  1 
ATOM   7786 N  N   . ASP D 1 213 ? -40.992 92.948  2.059   1.00 54.60  ? 211 ASP D N   1 
ATOM   7787 C  CA  . ASP D 1 213 ? -40.691 91.904  1.074   1.00 54.34  ? 211 ASP D CA  1 
ATOM   7788 C  C   . ASP D 1 213 ? -41.568 92.007  -0.170  1.00 54.33  ? 211 ASP D C   1 
ATOM   7789 O  O   . ASP D 1 213 ? -42.760 92.254  -0.073  1.00 53.79  ? 211 ASP D O   1 
ATOM   7790 C  CB  . ASP D 1 213 ? -40.845 90.536  1.715   1.00 54.95  ? 211 ASP D CB  1 
ATOM   7791 C  CG  . ASP D 1 213 ? -40.096 90.430  3.024   1.00 53.81  ? 211 ASP D CG  1 
ATOM   7792 O  OD1 . ASP D 1 213 ? -39.074 91.130  3.174   1.00 53.87  ? 211 ASP D OD1 1 
ATOM   7793 O  OD2 . ASP D 1 213 ? -40.540 89.662  3.905   1.00 52.61  ? 211 ASP D OD2 1 
ATOM   7794 N  N   . GLU D 1 214 ? -40.971 91.813  -1.338  1.00 57.41  ? 212 GLU D N   1 
ATOM   7795 C  CA  . GLU D 1 214 ? -41.675 92.027  -2.590  1.00 56.23  ? 212 GLU D CA  1 
ATOM   7796 C  C   . GLU D 1 214 ? -42.315 90.748  -3.121  1.00 63.10  ? 212 GLU D C   1 
ATOM   7797 O  O   . GLU D 1 214 ? -42.015 90.282  -4.223  1.00 68.48  ? 212 GLU D O   1 
ATOM   7798 C  CB  . GLU D 1 214 ? -40.742 92.688  -3.594  1.00 59.12  ? 212 GLU D CB  1 
ATOM   7799 C  CG  . GLU D 1 214 ? -40.109 93.949  -3.030  1.00 60.24  ? 212 GLU D CG  1 
ATOM   7800 C  CD  . GLU D 1 214 ? -39.314 94.736  -4.045  1.00 66.62  ? 212 GLU D CD  1 
ATOM   7801 O  OE1 . GLU D 1 214 ? -38.656 94.116  -4.911  1.00 65.15  ? 212 GLU D OE1 1 
ATOM   7802 O  OE2 . GLU D 1 214 ? -39.339 95.989  -3.965  1.00 69.42  ? 212 GLU D OE2 1 
ATOM   7803 N  N   . LYS D 1 215 ? -43.237 90.213  -2.324  1.00 62.18  ? 213 LYS D N   1 
ATOM   7804 C  CA  . LYS D 1 215 ? -43.811 88.890  -2.531  1.00 53.66  ? 213 LYS D CA  1 
ATOM   7805 C  C   . LYS D 1 215 ? -45.355 88.885  -2.594  1.00 51.54  ? 213 LYS D C   1 
ATOM   7806 O  O   . LYS D 1 215 ? -46.011 87.858  -2.380  1.00 47.93  ? 213 LYS D O   1 
ATOM   7807 C  CB  . LYS D 1 215 ? -43.308 87.970  -1.418  1.00 55.60  ? 213 LYS D CB  1 
ATOM   7808 C  CG  . LYS D 1 215 ? -43.807 88.312  -0.023  1.00 54.20  ? 213 LYS D CG  1 
ATOM   7809 C  CD  . LYS D 1 215 ? -43.340 87.261  0.967   1.00 53.70  ? 213 LYS D CD  1 
ATOM   7810 C  CE  . LYS D 1 215 ? -44.138 87.345  2.246   1.00 56.37  ? 213 LYS D CE  1 
ATOM   7811 N  NZ  . LYS D 1 215 ? -43.385 86.707  3.363   1.00 62.16  ? 213 LYS D NZ  1 
ATOM   7812 N  N   . VAL D 1 216 ? -45.928 90.033  -2.932  1.00 46.90  ? 214 VAL D N   1 
ATOM   7813 C  CA  . VAL D 1 216 ? -47.364 90.236  -2.781  1.00 44.82  ? 214 VAL D CA  1 
ATOM   7814 C  C   . VAL D 1 216 ? -48.065 90.396  -4.116  1.00 42.45  ? 214 VAL D C   1 
ATOM   7815 O  O   . VAL D 1 216 ? -47.556 91.084  -5.026  1.00 48.39  ? 214 VAL D O   1 
ATOM   7816 C  CB  . VAL D 1 216 ? -47.645 91.492  -1.911  1.00 42.40  ? 214 VAL D CB  1 
ATOM   7817 C  CG1 . VAL D 1 216 ? -49.086 91.531  -1.453  1.00 39.78  ? 214 VAL D CG1 1 
ATOM   7818 C  CG2 . VAL D 1 216 ? -46.736 91.491  -0.697  1.00 47.42  ? 214 VAL D CG2 1 
ATOM   7819 N  N   . VAL D 1 217 ? -49.247 89.788  -4.220  1.00 43.55  ? 215 VAL D N   1 
ATOM   7820 C  CA  . VAL D 1 217 ? -50.120 90.022  -5.370  1.00 44.95  ? 215 VAL D CA  1 
ATOM   7821 C  C   . VAL D 1 217 ? -51.356 90.788  -4.927  1.00 46.28  ? 215 VAL D C   1 
ATOM   7822 O  O   . VAL D 1 217 ? -52.363 90.192  -4.470  1.00 40.33  ? 215 VAL D O   1 
ATOM   7823 C  CB  . VAL D 1 217 ? -50.466 88.749  -6.233  1.00 48.03  ? 215 VAL D CB  1 
ATOM   7824 C  CG1 . VAL D 1 217 ? -51.124 87.642  -5.431  1.00 49.56  ? 215 VAL D CG1 1 
ATOM   7825 C  CG2 . VAL D 1 217 ? -51.360 89.113  -7.423  1.00 47.37  ? 215 VAL D CG2 1 
ATOM   7826 N  N   . TRP D 1 218 ? -51.265 92.112  -5.104  1.00 39.15  ? 216 TRP D N   1 
ATOM   7827 C  CA  . TRP D 1 218 ? -52.328 93.012  -4.715  1.00 39.75  ? 216 TRP D CA  1 
ATOM   7828 C  C   . TRP D 1 218 ? -53.575 92.911  -5.527  1.00 38.30  ? 216 TRP D C   1 
ATOM   7829 O  O   . TRP D 1 218 ? -53.565 92.783  -6.766  1.00 35.99  ? 216 TRP D O   1 
ATOM   7830 C  CB  . TRP D 1 218 ? -51.829 94.447  -4.765  1.00 38.46  ? 216 TRP D CB  1 
ATOM   7831 C  CG  . TRP D 1 218 ? -50.917 94.717  -3.628  1.00 38.18  ? 216 TRP D CG  1 
ATOM   7832 C  CD1 . TRP D 1 218 ? -49.504 94.711  -3.616  1.00 38.15  ? 216 TRP D CD1 1 
ATOM   7833 C  CD2 . TRP D 1 218 ? -51.325 95.046  -2.268  1.00 38.22  ? 216 TRP D CD2 1 
ATOM   7834 N  NE1 . TRP D 1 218 ? -49.034 95.006  -2.360  1.00 37.70  ? 216 TRP D NE1 1 
ATOM   7835 C  CE2 . TRP D 1 218 ? -50.091 95.219  -1.499  1.00 38.45  ? 216 TRP D CE2 1 
ATOM   7836 C  CE3 . TRP D 1 218 ? -52.560 95.213  -1.628  1.00 39.34  ? 216 TRP D CE3 1 
ATOM   7837 C  CZ2 . TRP D 1 218 ? -50.111 95.556  -0.150  1.00 37.14  ? 216 TRP D CZ2 1 
ATOM   7838 C  CZ3 . TRP D 1 218 ? -52.559 95.554  -0.263  1.00 36.30  ? 216 TRP D CZ3 1 
ATOM   7839 C  CH2 . TRP D 1 218 ? -51.363 95.702  0.451   1.00 33.12  ? 216 TRP D CH2 1 
ATOM   7840 N  N   . THR D 1 219 ? -54.678 92.977  -4.812  1.00 40.38  ? 217 THR D N   1 
ATOM   7841 C  CA  . THR D 1 219 ? -55.961 93.167  -5.427  1.00 42.46  ? 217 THR D CA  1 
ATOM   7842 C  C   . THR D 1 219 ? -56.635 94.377  -4.755  1.00 39.85  ? 217 THR D C   1 
ATOM   7843 O  O   . THR D 1 219 ? -56.887 94.387  -3.566  1.00 38.24  ? 217 THR D O   1 
ATOM   7844 C  CB  . THR D 1 219 ? -56.809 91.882  -5.344  1.00 42.57  ? 217 THR D CB  1 
ATOM   7845 O  OG1 . THR D 1 219 ? -56.058 90.791  -5.899  1.00 44.56  ? 217 THR D OG1 1 
ATOM   7846 C  CG2 . THR D 1 219 ? -58.118 92.037  -6.091  1.00 40.22  ? 217 THR D CG2 1 
ATOM   7847 N  N   . VAL D 1 220 ? -56.916 95.394  -5.549  1.00 39.40  ? 218 VAL D N   1 
ATOM   7848 C  CA  . VAL D 1 220 ? -57.559 96.595  -5.068  1.00 34.51  ? 218 VAL D CA  1 
ATOM   7849 C  C   . VAL D 1 220 ? -58.959 96.615  -5.669  1.00 31.39  ? 218 VAL D C   1 
ATOM   7850 O  O   . VAL D 1 220 ? -59.121 96.681  -6.872  1.00 34.18  ? 218 VAL D O   1 
ATOM   7851 C  CB  . VAL D 1 220 ? -56.682 97.857  -5.401  1.00 32.99  ? 218 VAL D CB  1 
ATOM   7852 C  CG1 . VAL D 1 220 ? -57.424 99.145  -5.120  1.00 33.20  ? 218 VAL D CG1 1 
ATOM   7853 C  CG2 . VAL D 1 220 ? -55.389 97.843  -4.609  1.00 28.75  ? 218 VAL D CG2 1 
ATOM   7854 N  N   . PHE D 1 221 ? -59.978 96.518  -4.820  1.00 35.79  ? 219 PHE D N   1 
ATOM   7855 C  CA  . PHE D 1 221 ? -61.367 96.547  -5.269  1.00 38.41  ? 219 PHE D CA  1 
ATOM   7856 C  C   . PHE D 1 221 ? -61.865 97.988  -5.468  1.00 43.72  ? 219 PHE D C   1 
ATOM   7857 O  O   . PHE D 1 221 ? -61.571 98.905  -4.677  1.00 40.02  ? 219 PHE D O   1 
ATOM   7858 C  CB  . PHE D 1 221 ? -62.272 95.757  -4.307  1.00 45.02  ? 219 PHE D CB  1 
ATOM   7859 C  CG  . PHE D 1 221 ? -61.990 94.274  -4.308  1.00 45.80  ? 219 PHE D CG  1 
ATOM   7860 C  CD1 . PHE D 1 221 ? -61.002 93.736  -3.482  1.00 47.22  ? 219 PHE D CD1 1 
ATOM   7861 C  CD2 . PHE D 1 221 ? -62.680 93.421  -5.165  1.00 46.67  ? 219 PHE D CD2 1 
ATOM   7862 C  CE1 . PHE D 1 221 ? -60.719 92.373  -3.508  1.00 46.84  ? 219 PHE D CE1 1 
ATOM   7863 C  CE2 . PHE D 1 221 ? -62.397 92.059  -5.199  1.00 44.25  ? 219 PHE D CE2 1 
ATOM   7864 C  CZ  . PHE D 1 221 ? -61.409 91.541  -4.376  1.00 43.27  ? 219 PHE D CZ  1 
ATOM   7865 N  N   . ARG D 1 222 ? -62.649 98.159  -6.520  1.00 42.58  ? 220 ARG D N   1 
ATOM   7866 C  CA  . ARG D 1 222 ? -62.953 99.468  -7.041  1.00 46.98  ? 220 ARG D CA  1 
ATOM   7867 C  C   . ARG D 1 222 ? -64.112 100.125 -6.319  1.00 49.75  ? 220 ARG D C   1 
ATOM   7868 O  O   . ARG D 1 222 ? -64.040 101.309 -5.995  1.00 47.20  ? 220 ARG D O   1 
ATOM   7869 C  CB  . ARG D 1 222 ? -63.214 99.378  -8.538  1.00 45.49  ? 220 ARG D CB  1 
ATOM   7870 C  CG  . ARG D 1 222 ? -63.676 100.661 -9.194  1.00 47.88  ? 220 ARG D CG  1 
ATOM   7871 C  CD  . ARG D 1 222 ? -64.162 100.356 -10.599 1.00 50.13  ? 220 ARG D CD  1 
ATOM   7872 N  NE  . ARG D 1 222 ? -65.562 99.938  -10.638 1.00 49.48  ? 220 ARG D NE  1 
ATOM   7873 C  CZ  . ARG D 1 222 ? -66.366 100.141 -11.678 1.00 52.40  ? 220 ARG D CZ  1 
ATOM   7874 N  NH1 . ARG D 1 222 ? -65.908 100.775 -12.766 1.00 46.20  ? 220 ARG D NH1 1 
ATOM   7875 N  NH2 . ARG D 1 222 ? -67.635 99.730  -11.627 1.00 48.04  ? 220 ARG D NH2 1 
ATOM   7876 N  N   . GLU D 1 223 ? -65.178 99.375  -6.060  1.00 50.88  ? 221 GLU D N   1 
ATOM   7877 C  CA  . GLU D 1 223 ? -66.309 99.962  -5.362  1.00 56.07  ? 221 GLU D CA  1 
ATOM   7878 C  C   . GLU D 1 223 ? -66.061 99.807  -3.848  1.00 52.20  ? 221 GLU D C   1 
ATOM   7879 O  O   . GLU D 1 223 ? -65.837 98.700  -3.370  1.00 60.09  ? 221 GLU D O   1 
ATOM   7880 C  CB  . GLU D 1 223 ? -67.641 99.374  -5.862  1.00 61.17  ? 221 GLU D CB  1 
ATOM   7881 C  CG  . GLU D 1 223 ? -67.715 99.141  -7.383  1.00 65.01  ? 221 GLU D CG  1 
ATOM   7882 C  CD  . GLU D 1 223 ? -68.204 100.342 -8.210  1.00 68.80  ? 221 GLU D CD  1 
ATOM   7883 O  OE1 . GLU D 1 223 ? -68.123 101.501 -7.749  1.00 66.96  ? 221 GLU D OE1 1 
ATOM   7884 O  OE2 . GLU D 1 223 ? -68.673 100.130 -9.351  1.00 68.11  ? 221 GLU D OE2 1 
ATOM   7885 N  N   . PRO D 1 224 ? -66.010 100.937 -3.111  1.00 53.11  ? 222 PRO D N   1 
ATOM   7886 C  CA  . PRO D 1 224 ? -65.623 100.990 -1.693  1.00 53.65  ? 222 PRO D CA  1 
ATOM   7887 C  C   . PRO D 1 224 ? -66.702 100.552 -0.714  1.00 51.00  ? 222 PRO D C   1 
ATOM   7888 O  O   . PRO D 1 224 ? -67.877 100.579 -1.066  1.00 52.46  ? 222 PRO D O   1 
ATOM   7889 C  CB  . PRO D 1 224 ? -65.322 102.478 -1.476  1.00 51.59  ? 222 PRO D CB  1 
ATOM   7890 C  CG  . PRO D 1 224 ? -66.163 103.170 -2.475  1.00 53.88  ? 222 PRO D CG  1 
ATOM   7891 C  CD  . PRO D 1 224 ? -66.122 102.288 -3.685  1.00 52.15  ? 222 PRO D CD  1 
ATOM   7892 N  N   . ILE D 1 225 ? -66.304 100.164 0.502   1.00 46.61  ? 223 ILE D N   1 
ATOM   7893 C  CA  . ILE D 1 225 ? -67.276 99.849  1.553   1.00 46.55  ? 223 ILE D CA  1 
ATOM   7894 C  C   . ILE D 1 225 ? -67.798 101.142 2.198   1.00 49.73  ? 223 ILE D C   1 
ATOM   7895 O  O   . ILE D 1 225 ? -67.023 102.067 2.466   1.00 48.32  ? 223 ILE D O   1 
ATOM   7896 C  CB  . ILE D 1 225 ? -66.703 98.972  2.690   1.00 47.75  ? 223 ILE D CB  1 
ATOM   7897 C  CG1 . ILE D 1 225 ? -65.920 97.770  2.149   1.00 44.94  ? 223 ILE D CG1 1 
ATOM   7898 C  CG2 . ILE D 1 225 ? -67.839 98.447  3.575   1.00 45.47  ? 223 ILE D CG2 1 
ATOM   7899 C  CD1 . ILE D 1 225 ? -64.947 97.206  3.152   1.00 37.68  ? 223 ILE D CD1 1 
ATOM   7900 N  N   . GLN D 1 226 ? -69.100 101.202 2.461   1.00 49.11  ? 224 GLN D N   1 
ATOM   7901 C  CA  . GLN D 1 226 ? -69.680 102.416 3.012   1.00 51.47  ? 224 GLN D CA  1 
ATOM   7902 C  C   . GLN D 1 226 ? -69.994 102.261 4.470   1.00 55.05  ? 224 GLN D C   1 
ATOM   7903 O  O   . GLN D 1 226 ? -70.995 101.650 4.838   1.00 55.87  ? 224 GLN D O   1 
ATOM   7904 C  CB  . GLN D 1 226 ? -70.933 102.830 2.263   1.00 53.53  ? 224 GLN D CB  1 
ATOM   7905 C  CG  . GLN D 1 226 ? -70.648 103.431 0.907   1.00 55.98  ? 224 GLN D CG  1 
ATOM   7906 C  CD  . GLN D 1 226 ? -71.921 103.800 0.201   1.00 55.36  ? 224 GLN D CD  1 
ATOM   7907 O  OE1 . GLN D 1 226 ? -72.255 103.229 -0.841  1.00 60.54  ? 224 GLN D OE1 1 
ATOM   7908 N  NE2 . GLN D 1 226 ? -72.656 104.740 0.772   1.00 49.27  ? 224 GLN D NE2 1 
ATOM   7909 N  N   . LEU D 1 227 ? -69.124 102.799 5.309   1.00 54.95  ? 225 LEU D N   1 
ATOM   7910 C  CA  . LEU D 1 227 ? -69.433 102.852 6.705   1.00 61.07  ? 225 LEU D CA  1 
ATOM   7911 C  C   . LEU D 1 227 ? -70.031 104.217 7.020   1.00 71.92  ? 225 LEU D C   1 
ATOM   7912 O  O   . LEU D 1 227 ? -69.753 105.210 6.331   1.00 69.91  ? 225 LEU D O   1 
ATOM   7913 C  CB  . LEU D 1 227 ? -68.182 102.639 7.538   1.00 63.30  ? 225 LEU D CB  1 
ATOM   7914 C  CG  . LEU D 1 227 ? -67.277 101.406 7.439   1.00 62.53  ? 225 LEU D CG  1 
ATOM   7915 C  CD1 . LEU D 1 227 ? -66.626 101.219 8.803   1.00 54.34  ? 225 LEU D CD1 1 
ATOM   7916 C  CD2 . LEU D 1 227 ? -67.996 100.135 6.995   1.00 60.31  ? 225 LEU D CD2 1 
ATOM   7917 N  N   . HIS D 1 228 ? -70.860 104.259 8.058   1.00 75.91  ? 226 HIS D N   1 
ATOM   7918 C  CA  . HIS D 1 228 ? -71.313 105.517 8.613   1.00 77.72  ? 226 HIS D CA  1 
ATOM   7919 C  C   . HIS D 1 228 ? -70.156 106.211 9.273   1.00 78.98  ? 226 HIS D C   1 
ATOM   7920 O  O   . HIS D 1 228 ? -69.268 105.555 9.831   1.00 79.60  ? 226 HIS D O   1 
ATOM   7921 C  CB  . HIS D 1 228 ? -72.432 105.289 9.615   1.00 79.44  ? 226 HIS D CB  1 
ATOM   7922 C  CG  . HIS D 1 228 ? -73.028 106.559 10.126  1.00 78.89  ? 226 HIS D CG  1 
ATOM   7923 N  ND1 . HIS D 1 228 ? -73.962 107.239 9.443   1.00 80.24  ? 226 HIS D ND1 1 
ATOM   7924 C  CD2 . HIS D 1 228 ? -72.750 107.303 11.272  1.00 82.58  ? 226 HIS D CD2 1 
ATOM   7925 C  CE1 . HIS D 1 228 ? -74.291 108.354 10.126  1.00 83.48  ? 226 HIS D CE1 1 
ATOM   7926 N  NE2 . HIS D 1 228 ? -73.547 108.391 11.247  1.00 83.24  ? 226 HIS D NE2 1 
ATOM   7927 N  N   . ARG D 1 229 ? -70.161 107.543 9.212   1.00 79.63  ? 227 ARG D N   1 
ATOM   7928 C  CA  . ARG D 1 229 ? -69.097 108.367 9.790   1.00 81.49  ? 227 ARG D CA  1 
ATOM   7929 C  C   . ARG D 1 229 ? -68.670 107.917 11.191  1.00 83.61  ? 227 ARG D C   1 
ATOM   7930 O  O   . ARG D 1 229 ? -67.473 107.786 11.467  1.00 87.91  ? 227 ARG D O   1 
ATOM   7931 C  CB  . ARG D 1 229 ? -69.506 109.848 9.805   1.00 85.59  ? 227 ARG D CB  1 
ATOM   7932 C  CG  . ARG D 1 229 ? -68.552 110.745 10.592  1.00 84.16  ? 227 ARG D CG  1 
ATOM   7933 C  CD  . ARG D 1 229 ? -69.034 112.181 10.721  1.00 75.42  ? 227 ARG D CD  1 
ATOM   7934 N  NE  . ARG D 1 229 ? -68.240 112.921 11.707  1.00 75.54  ? 227 ARG D NE  1 
ATOM   7935 C  CZ  . ARG D 1 229 ? -67.064 113.501 11.464  1.00 75.67  ? 227 ARG D CZ  1 
ATOM   7936 N  NH1 . ARG D 1 229 ? -66.504 113.431 10.261  1.00 78.25  ? 227 ARG D NH1 1 
ATOM   7937 N  NH2 . ARG D 1 229 ? -66.433 114.147 12.436  1.00 74.47  ? 227 ARG D NH2 1 
ATOM   7938 N  N   . GLU D 1 230 ? -69.650 107.677 12.061  1.00 86.43  ? 228 GLU D N   1 
ATOM   7939 C  CA  . GLU D 1 230 ? -69.391 107.275 13.450  1.00 84.54  ? 228 GLU D CA  1 
ATOM   7940 C  C   . GLU D 1 230 ? -68.507 106.031 13.556  1.00 76.71  ? 228 GLU D C   1 
ATOM   7941 O  O   . GLU D 1 230 ? -67.533 106.022 14.320  1.00 71.60  ? 228 GLU D O   1 
ATOM   7942 C  CB  . GLU D 1 230 ? -70.710 107.069 14.206  1.00 93.52  ? 228 GLU D CB  1 
ATOM   7943 C  CG  . GLU D 1 230 ? -71.446 108.361 14.545  1.00 97.55  ? 228 GLU D CG  1 
ATOM   7944 C  CD  . GLU D 1 230 ? -72.954 108.192 14.610  1.00 98.26  ? 228 GLU D CD  1 
ATOM   7945 O  OE1 . GLU D 1 230 ? -73.430 107.151 15.117  1.00 98.13  ? 228 GLU D OE1 1 
ATOM   7946 O  OE2 . GLU D 1 230 ? -73.668 109.111 14.155  1.00 102.18 ? 228 GLU D OE2 1 
ATOM   7947 N  N   . GLN D 1 231 ? -68.835 105.003 12.769  1.00 71.20  ? 229 GLN D N   1 
ATOM   7948 C  CA  . GLN D 1 231 ? -68.110 103.718 12.797  1.00 69.13  ? 229 GLN D CA  1 
ATOM   7949 C  C   . GLN D 1 231 ? -66.635 103.888 12.424  1.00 70.53  ? 229 GLN D C   1 
ATOM   7950 O  O   . GLN D 1 231 ? -65.757 103.262 13.026  1.00 70.75  ? 229 GLN D O   1 
ATOM   7951 C  CB  . GLN D 1 231 ? -68.755 102.664 11.876  1.00 63.90  ? 229 GLN D CB  1 
ATOM   7952 C  CG  . GLN D 1 231 ? -70.269 102.528 11.959  1.00 61.56  ? 229 GLN D CG  1 
ATOM   7953 C  CD  . GLN D 1 231 ? -70.784 101.249 11.314  1.00 66.95  ? 229 GLN D CD  1 
ATOM   7954 O  OE1 . GLN D 1 231 ? -71.592 101.290 10.381  1.00 64.98  ? 229 GLN D OE1 1 
ATOM   7955 N  NE2 . GLN D 1 231 ? -70.318 100.102 11.812  1.00 63.60  ? 229 GLN D NE2 1 
ATOM   7956 N  N   . ILE D 1 232 ? -66.376 104.738 11.430  1.00 66.35  ? 230 ILE D N   1 
ATOM   7957 C  CA  . ILE D 1 232 ? -65.014 105.020 10.992  1.00 58.85  ? 230 ILE D CA  1 
ATOM   7958 C  C   . ILE D 1 232 ? -64.253 105.698 12.121  1.00 55.44  ? 230 ILE D C   1 
ATOM   7959 O  O   . ILE D 1 232 ? -63.195 105.216 12.548  1.00 51.07  ? 230 ILE D O   1 
ATOM   7960 C  CB  . ILE D 1 232 ? -65.005 105.861 9.688   1.00 58.84  ? 230 ILE D CB  1 
ATOM   7961 C  CG1 . ILE D 1 232 ? -65.512 105.010 8.504   1.00 56.44  ? 230 ILE D CG1 1 
ATOM   7962 C  CG2 . ILE D 1 232 ? -63.622 106.433 9.411   1.00 58.73  ? 230 ILE D CG2 1 
ATOM   7963 C  CD1 . ILE D 1 232 ? -66.044 105.803 7.323   1.00 57.52  ? 230 ILE D CD1 1 
ATOM   7964 N  N   . LEU D 1 233 ? -64.821 106.802 12.608  1.00 57.33  ? 231 LEU D N   1 
ATOM   7965 C  CA  . LEU D 1 233 ? -64.262 107.557 13.731  1.00 61.33  ? 231 LEU D CA  1 
ATOM   7966 C  C   . LEU D 1 233 ? -64.012 106.693 14.962  1.00 55.73  ? 231 LEU D C   1 
ATOM   7967 O  O   . LEU D 1 233 ? -62.964 106.801 15.612  1.00 60.56  ? 231 LEU D O   1 
ATOM   7968 C  CB  . LEU D 1 233 ? -65.171 108.733 14.083  1.00 66.22  ? 231 LEU D CB  1 
ATOM   7969 C  CG  . LEU D 1 233 ? -64.707 110.125 13.642  1.00 70.50  ? 231 LEU D CG  1 
ATOM   7970 C  CD1 . LEU D 1 233 ? -65.906 111.037 13.448  1.00 64.08  ? 231 LEU D CD1 1 
ATOM   7971 C  CD2 . LEU D 1 233 ? -63.715 110.720 14.644  1.00 74.18  ? 231 LEU D CD2 1 
ATOM   7972 N  N   . ALA D 1 234 ? -64.972 105.833 15.270  1.00 53.96  ? 232 ALA D N   1 
ATOM   7973 C  CA  . ALA D 1 234 ? -64.791 104.788 16.289  1.00 56.03  ? 232 ALA D CA  1 
ATOM   7974 C  C   . ALA D 1 234 ? -63.408 104.102 16.294  1.00 50.77  ? 232 ALA D C   1 
ATOM   7975 O  O   . ALA D 1 234 ? -62.941 103.679 17.358  1.00 42.85  ? 232 ALA D O   1 
ATOM   7976 C  CB  . ALA D 1 234 ? -65.894 103.747 16.181  1.00 57.75  ? 232 ALA D CB  1 
ATOM   7977 N  N   . PHE D 1 235 ? -62.765 103.986 15.125  1.00 44.85  ? 233 PHE D N   1 
ATOM   7978 C  CA  . PHE D 1 235 ? -61.454 103.320 15.058  1.00 47.93  ? 233 PHE D CA  1 
ATOM   7979 C  C   . PHE D 1 235 ? -60.313 104.127 15.646  1.00 47.53  ? 233 PHE D C   1 
ATOM   7980 O  O   . PHE D 1 235 ? -59.364 103.541 16.155  1.00 51.76  ? 233 PHE D O   1 
ATOM   7981 C  CB  . PHE D 1 235 ? -61.076 102.868 13.635  1.00 45.47  ? 233 PHE D CB  1 
ATOM   7982 C  CG  . PHE D 1 235 ? -61.761 101.615 13.198  1.00 41.76  ? 233 PHE D CG  1 
ATOM   7983 C  CD1 . PHE D 1 235 ? -63.088 101.646 12.776  1.00 45.37  ? 233 PHE D CD1 1 
ATOM   7984 C  CD2 . PHE D 1 235 ? -61.101 100.420 13.212  1.00 39.68  ? 233 PHE D CD2 1 
ATOM   7985 C  CE1 . PHE D 1 235 ? -63.740 100.493 12.369  1.00 44.67  ? 233 PHE D CE1 1 
ATOM   7986 C  CE2 . PHE D 1 235 ? -61.743 99.264  12.802  1.00 45.94  ? 233 PHE D CE2 1 
ATOM   7987 C  CZ  . PHE D 1 235 ? -63.065 99.297  12.382  1.00 41.85  ? 233 PHE D CZ  1 
ATOM   7988 N  N   . SER D 1 236 ? -60.369 105.455 15.544  1.00 53.29  ? 234 SER D N   1 
ATOM   7989 C  CA  . SER D 1 236 ? -59.353 106.289 16.214  1.00 52.43  ? 234 SER D CA  1 
ATOM   7990 C  C   . SER D 1 236 ? -59.881 106.940 17.509  1.00 55.25  ? 234 SER D C   1 
ATOM   7991 O  O   . SER D 1 236 ? -59.097 107.186 18.434  1.00 58.08  ? 234 SER D O   1 
ATOM   7992 C  CB  . SER D 1 236 ? -58.693 107.308 15.263  1.00 48.41  ? 234 SER D CB  1 
ATOM   7993 O  OG  . SER D 1 236 ? -59.191 108.622 15.406  1.00 45.99  ? 234 SER D OG  1 
ATOM   7994 N  N   . GLN D 1 237 ? -61.192 107.189 17.584  1.00 53.45  ? 235 GLN D N   1 
ATOM   7995 C  CA  . GLN D 1 237 ? -61.815 107.592 18.872  1.00 58.37  ? 235 GLN D CA  1 
ATOM   7996 C  C   . GLN D 1 237 ? -61.617 106.566 20.015  1.00 62.20  ? 235 GLN D C   1 
ATOM   7997 O  O   . GLN D 1 237 ? -61.336 106.957 21.151  1.00 65.25  ? 235 GLN D O   1 
ATOM   7998 C  CB  . GLN D 1 237 ? -63.289 108.008 18.712  1.00 58.44  ? 235 GLN D CB  1 
ATOM   7999 C  CG  . GLN D 1 237 ? -63.466 109.521 18.550  1.00 58.65  ? 235 GLN D CG  1 
ATOM   8000 C  CD  . GLN D 1 237 ? -64.914 110.011 18.681  1.00 64.01  ? 235 GLN D CD  1 
ATOM   8001 O  OE1 . GLN D 1 237 ? -65.754 109.784 17.792  1.00 58.97  ? 235 GLN D OE1 1 
ATOM   8002 N  NE2 . GLN D 1 237 ? -65.204 110.717 19.784  1.00 59.17  ? 235 GLN D NE2 1 
ATOM   8003 N  N   . LYS D 1 238 ? -61.697 105.279 19.670  1.00 63.57  ? 236 LYS D N   1 
ATOM   8004 C  CA  . LYS D 1 238 ? -61.602 104.145 20.602  1.00 68.31  ? 236 LYS D CA  1 
ATOM   8005 C  C   . LYS D 1 238 ? -60.348 103.297 20.640  1.00 72.82  ? 236 LYS D C   1 
ATOM   8006 O  O   . LYS D 1 238 ? -60.445 102.176 21.053  1.00 78.79  ? 236 LYS D O   1 
ATOM   8007 C  CB  . LYS D 1 238 ? -62.693 103.103 20.313  1.00 61.45  ? 236 LYS D CB  1 
ATOM   8008 C  CG  . LYS D 1 238 ? -64.118 103.567 20.406  1.00 56.62  ? 236 LYS D CG  1 
ATOM   8009 C  CD  . LYS D 1 238 ? -64.553 103.569 21.842  1.00 58.71  ? 236 LYS D CD  1 
ATOM   8010 C  CE  . LYS D 1 238 ? -65.862 104.301 22.003  1.00 65.39  ? 236 LYS D CE  1 
ATOM   8011 N  NZ  . LYS D 1 238 ? -66.349 104.231 23.398  1.00 64.18  ? 236 LYS D NZ  1 
ATOM   8012 N  N   . LEU D 1 239 ? -59.197 103.744 20.196  1.00 72.63  ? 237 LEU D N   1 
ATOM   8013 C  CA  . LEU D 1 239 ? -58.094 102.805 20.105  1.00 73.30  ? 237 LEU D CA  1 
ATOM   8014 C  C   . LEU D 1 239 ? -56.884 103.644 20.196  1.00 66.51  ? 237 LEU D C   1 
ATOM   8015 O  O   . LEU D 1 239 ? -56.964 104.772 19.784  1.00 66.26  ? 237 LEU D O   1 
ATOM   8016 C  CB  . LEU D 1 239 ? -58.110 102.138 18.743  1.00 76.45  ? 237 LEU D CB  1 
ATOM   8017 C  CG  . LEU D 1 239 ? -58.675 100.748 18.518  1.00 84.29  ? 237 LEU D CG  1 
ATOM   8018 C  CD1 . LEU D 1 239 ? -59.276 100.688 17.136  1.00 83.36  ? 237 LEU D CD1 1 
ATOM   8019 C  CD2 . LEU D 1 239 ? -57.610 99.670  18.664  1.00 84.13  ? 237 LEU D CD2 1 
ATOM   8020 N  N   . TYR D 1 240 ? -55.766 103.147 20.721  1.00 63.94  ? 238 TYR D N   1 
ATOM   8021 C  CA  . TYR D 1 240 ? -54.654 104.075 20.946  1.00 62.91  ? 238 TYR D CA  1 
ATOM   8022 C  C   . TYR D 1 240 ? -53.344 103.385 20.646  1.00 61.42  ? 238 TYR D C   1 
ATOM   8023 O  O   . TYR D 1 240 ? -53.222 102.188 20.872  1.00 61.51  ? 238 TYR D O   1 
ATOM   8024 C  CB  . TYR D 1 240 ? -54.634 104.553 22.410  1.00 69.02  ? 238 TYR D CB  1 
ATOM   8025 C  CG  . TYR D 1 240 ? -55.826 105.390 22.790  1.00 74.26  ? 238 TYR D CG  1 
ATOM   8026 C  CD1 . TYR D 1 240 ? -56.944 104.811 23.383  1.00 76.53  ? 238 TYR D CD1 1 
ATOM   8027 C  CD2 . TYR D 1 240 ? -55.847 106.760 22.535  1.00 78.37  ? 238 TYR D CD2 1 
ATOM   8028 C  CE1 . TYR D 1 240 ? -58.049 105.576 23.719  1.00 80.71  ? 238 TYR D CE1 1 
ATOM   8029 C  CE2 . TYR D 1 240 ? -56.950 107.533 22.859  1.00 84.04  ? 238 TYR D CE2 1 
ATOM   8030 C  CZ  . TYR D 1 240 ? -58.049 106.937 23.451  1.00 83.64  ? 238 TYR D CZ  1 
ATOM   8031 O  OH  . TYR D 1 240 ? -59.147 107.703 23.777  1.00 84.42  ? 238 TYR D OH  1 
ATOM   8032 N  N   . TYR D 1 241 ? -52.356 104.137 20.167  1.00 63.49  ? 239 TYR D N   1 
ATOM   8033 C  CA  . TYR D 1 241 ? -51.022 103.578 19.888  1.00 63.79  ? 239 TYR D CA  1 
ATOM   8034 C  C   . TYR D 1 241 ? -50.263 103.158 21.149  1.00 70.27  ? 239 TYR D C   1 
ATOM   8035 O  O   . TYR D 1 241 ? -49.331 102.349 21.070  1.00 66.95  ? 239 TYR D O   1 
ATOM   8036 C  CB  . TYR D 1 241 ? -50.126 104.578 19.140  1.00 63.11  ? 239 TYR D CB  1 
ATOM   8037 C  CG  . TYR D 1 241 ? -50.298 104.691 17.630  1.00 59.44  ? 239 TYR D CG  1 
ATOM   8038 C  CD1 . TYR D 1 241 ? -50.093 103.596 16.793  1.00 55.50  ? 239 TYR D CD1 1 
ATOM   8039 C  CD2 . TYR D 1 241 ? -50.628 105.920 17.045  1.00 58.47  ? 239 TYR D CD2 1 
ATOM   8040 C  CE1 . TYR D 1 241 ? -50.236 103.716 15.419  1.00 58.71  ? 239 TYR D CE1 1 
ATOM   8041 C  CE2 . TYR D 1 241 ? -50.777 106.051 15.677  1.00 58.44  ? 239 TYR D CE2 1 
ATOM   8042 C  CZ  . TYR D 1 241 ? -50.574 104.948 14.868  1.00 55.49  ? 239 TYR D CZ  1 
ATOM   8043 O  OH  . TYR D 1 241 ? -50.719 105.092 13.526  1.00 43.02  ? 239 TYR D OH  1 
ATOM   8044 N  N   . ASP D 1 242 ? -50.642 103.729 22.294  1.00 71.67  ? 240 ASP D N   1 
ATOM   8045 C  CA  . ASP D 1 242 ? -49.835 103.640 23.517  1.00 75.57  ? 240 ASP D CA  1 
ATOM   8046 C  C   . ASP D 1 242 ? -50.575 103.007 24.698  1.00 74.90  ? 240 ASP D C   1 
ATOM   8047 O  O   . ASP D 1 242 ? -51.804 103.101 24.798  1.00 75.90  ? 240 ASP D O   1 
ATOM   8048 C  CB  . ASP D 1 242 ? -49.295 105.033 23.909  1.00 73.56  ? 240 ASP D CB  1 
ATOM   8049 C  CG  . ASP D 1 242 ? -50.408 106.073 24.152  1.00 73.39  ? 240 ASP D CG  1 
ATOM   8050 O  OD1 . ASP D 1 242 ? -51.564 105.876 23.696  1.00 69.91  ? 240 ASP D OD1 1 
ATOM   8051 O  OD2 . ASP D 1 242 ? -50.110 107.109 24.789  1.00 69.87  ? 240 ASP D OD2 1 
ATOM   8052 N  N   . LYS D 1 243 ? -49.807 102.363 25.579  1.00 77.90  ? 241 LYS D N   1 
ATOM   8053 C  CA  . LYS D 1 243 ? -50.305 101.862 26.874  1.00 79.55  ? 241 LYS D CA  1 
ATOM   8054 C  C   . LYS D 1 243 ? -50.917 103.000 27.709  1.00 74.33  ? 241 LYS D C   1 
ATOM   8055 O  O   . LYS D 1 243 ? -51.913 102.810 28.403  1.00 70.70  ? 241 LYS D O   1 
ATOM   8056 C  CB  . LYS D 1 243 ? -49.179 101.187 27.669  1.00 77.86  ? 241 LYS D CB  1 
ATOM   8057 C  CG  . LYS D 1 243 ? -48.141 100.432 26.838  1.00 84.36  ? 241 LYS D CG  1 
ATOM   8058 C  CD  . LYS D 1 243 ? -46.932 101.300 26.476  1.00 82.99  ? 241 LYS D CD  1 
ATOM   8059 C  CE  . LYS D 1 243 ? -45.714 100.460 26.083  1.00 80.91  ? 241 LYS D CE  1 
ATOM   8060 N  NZ  . LYS D 1 243 ? -44.957 99.917  27.252  1.00 70.31  ? 241 LYS D NZ  1 
ATOM   8061 N  N   . GLU D 1 244 ? -50.309 104.181 27.608  1.00 76.89  ? 242 GLU D N   1 
ATOM   8062 C  CA  . GLU D 1 244 ? -50.789 105.409 28.250  1.00 78.38  ? 242 GLU D CA  1 
ATOM   8063 C  C   . GLU D 1 244 ? -52.198 105.812 27.803  1.00 79.04  ? 242 GLU D C   1 
ATOM   8064 O  O   . GLU D 1 244 ? -52.918 106.486 28.552  1.00 78.52  ? 242 GLU D O   1 
ATOM   8065 C  CB  . GLU D 1 244 ? -49.826 106.564 27.958  1.00 73.59  ? 242 GLU D CB  1 
ATOM   8066 C  CG  . GLU D 1 244 ? -48.516 106.548 28.737  1.00 74.88  ? 242 GLU D CG  1 
ATOM   8067 C  CD  . GLU D 1 244 ? -47.616 105.357 28.431  1.00 71.91  ? 242 GLU D CD  1 
ATOM   8068 O  OE1 . GLU D 1 244 ? -47.897 104.567 27.501  1.00 69.87  ? 242 GLU D OE1 1 
ATOM   8069 O  OE2 . GLU D 1 244 ? -46.609 105.208 29.142  1.00 67.76  ? 242 GLU D OE2 1 
ATOM   8070 N  N   . GLN D 1 245 ? -52.575 105.394 26.589  1.00 76.48  ? 243 GLN D N   1 
ATOM   8071 C  CA  . GLN D 1 245 ? -53.838 105.793 25.928  1.00 72.94  ? 243 GLN D CA  1 
ATOM   8072 C  C   . GLN D 1 245 ? -53.927 107.301 25.658  1.00 67.59  ? 243 GLN D C   1 
ATOM   8073 O  O   . GLN D 1 245 ? -55.016 107.871 25.661  1.00 57.33  ? 243 GLN D O   1 
ATOM   8074 C  CB  . GLN D 1 245 ? -55.078 105.307 26.696  1.00 68.72  ? 243 GLN D CB  1 
ATOM   8075 C  CG  . GLN D 1 245 ? -55.238 103.799 26.774  1.00 70.13  ? 243 GLN D CG  1 
ATOM   8076 C  CD  . GLN D 1 245 ? -56.536 103.400 27.465  1.00 69.88  ? 243 GLN D CD  1 
ATOM   8077 O  OE1 . GLN D 1 245 ? -57.439 102.825 26.848  1.00 59.95  ? 243 GLN D OE1 1 
ATOM   8078 N  NE2 . GLN D 1 245 ? -56.641 103.722 28.752  1.00 69.62  ? 243 GLN D NE2 1 
ATOM   8079 N  N   . THR D 1 246 ? -52.776 107.927 25.419  1.00 68.39  ? 244 THR D N   1 
ATOM   8080 C  CA  . THR D 1 246 ? -52.707 109.350 25.075  1.00 73.31  ? 244 THR D CA  1 
ATOM   8081 C  C   . THR D 1 246 ? -52.801 109.593 23.562  1.00 72.52  ? 244 THR D C   1 
ATOM   8082 O  O   . THR D 1 246 ? -53.400 110.587 23.130  1.00 70.64  ? 244 THR D O   1 
ATOM   8083 C  CB  . THR D 1 246 ? -51.403 110.015 25.589  1.00 74.58  ? 244 THR D CB  1 
ATOM   8084 O  OG1 . THR D 1 246 ? -50.272 109.519 24.852  1.00 70.71  ? 244 THR D OG1 1 
ATOM   8085 C  CG2 . THR D 1 246 ? -51.208 109.766 27.083  1.00 71.87  ? 244 THR D CG2 1 
ATOM   8086 N  N   . VAL D 1 247 ? -52.205 108.685 22.779  1.00 65.82  ? 245 VAL D N   1 
ATOM   8087 C  CA  . VAL D 1 247 ? -52.031 108.852 21.323  1.00 57.09  ? 245 VAL D CA  1 
ATOM   8088 C  C   . VAL D 1 247 ? -53.086 108.083 20.532  1.00 53.59  ? 245 VAL D C   1 
ATOM   8089 O  O   . VAL D 1 247 ? -53.003 106.850 20.407  1.00 52.92  ? 245 VAL D O   1 
ATOM   8090 C  CB  . VAL D 1 247 ? -50.634 108.366 20.854  1.00 52.55  ? 245 VAL D CB  1 
ATOM   8091 C  CG1 . VAL D 1 247 ? -50.306 108.929 19.479  1.00 49.73  ? 245 VAL D CG1 1 
ATOM   8092 C  CG2 . VAL D 1 247 ? -49.547 108.708 21.864  1.00 50.84  ? 245 VAL D CG2 1 
ATOM   8093 N  N   . SER D 1 248 ? -54.066 108.802 19.984  1.00 53.56  ? 246 SER D N   1 
ATOM   8094 C  CA  . SER D 1 248 ? -55.144 108.146 19.254  1.00 54.32  ? 246 SER D CA  1 
ATOM   8095 C  C   . SER D 1 248 ? -54.605 107.420 18.017  1.00 54.31  ? 246 SER D C   1 
ATOM   8096 O  O   . SER D 1 248 ? -53.641 107.871 17.385  1.00 49.75  ? 246 SER D O   1 
ATOM   8097 C  CB  . SER D 1 248 ? -56.272 109.124 18.915  1.00 59.04  ? 246 SER D CB  1 
ATOM   8098 O  OG  . SER D 1 248 ? -57.153 109.288 20.024  1.00 59.84  ? 246 SER D OG  1 
ATOM   8099 N  N   . MET D 1 249 ? -55.216 106.283 17.698  1.00 52.12  ? 247 MET D N   1 
ATOM   8100 C  CA  . MET D 1 249 ? -54.730 105.429 16.615  1.00 47.28  ? 247 MET D CA  1 
ATOM   8101 C  C   . MET D 1 249 ? -55.185 105.947 15.262  1.00 46.07  ? 247 MET D C   1 
ATOM   8102 O  O   . MET D 1 249 ? -56.391 105.944 14.966  1.00 42.28  ? 247 MET D O   1 
ATOM   8103 C  CB  . MET D 1 249 ? -55.193 103.991 16.810  1.00 46.08  ? 247 MET D CB  1 
ATOM   8104 C  CG  . MET D 1 249 ? -54.050 103.023 16.574  1.00 49.88  ? 247 MET D CG  1 
ATOM   8105 S  SD  . MET D 1 249 ? -54.554 101.359 16.072  1.00 49.59  ? 247 MET D SD  1 
ATOM   8106 C  CE  . MET D 1 249 ? -52.971 100.575 16.360  1.00 42.35  ? 247 MET D CE  1 
ATOM   8107 N  N   . LYS D 1 250 ? -54.228 106.403 14.447  1.00 43.19  ? 248 LYS D N   1 
ATOM   8108 C  CA  . LYS D 1 250 ? -54.552 107.078 13.180  1.00 41.42  ? 248 LYS D CA  1 
ATOM   8109 C  C   . LYS D 1 250 ? -53.358 107.194 12.256  1.00 40.28  ? 248 LYS D C   1 
ATOM   8110 O  O   . LYS D 1 250 ? -52.209 107.054 12.678  1.00 41.09  ? 248 LYS D O   1 
ATOM   8111 C  CB  . LYS D 1 250 ? -55.147 108.478 13.438  1.00 48.44  ? 248 LYS D CB  1 
ATOM   8112 C  CG  . LYS D 1 250 ? -54.214 109.513 14.075  1.00 49.72  ? 248 LYS D CG  1 
ATOM   8113 C  CD  . LYS D 1 250 ? -54.507 110.879 13.446  1.00 48.27  ? 248 LYS D CD  1 
ATOM   8114 C  CE  . LYS D 1 250 ? -54.198 112.088 14.328  1.00 45.75  ? 248 LYS D CE  1 
ATOM   8115 N  NZ  . LYS D 1 250 ? -55.074 113.208 13.869  1.00 45.19  ? 248 LYS D NZ  1 
ATOM   8116 N  N   . ASP D 1 251 ? -53.620 107.453 10.979  1.00 43.95  ? 249 ASP D N   1 
ATOM   8117 C  CA  . ASP D 1 251 ? -52.517 107.584 10.007  1.00 40.50  ? 249 ASP D CA  1 
ATOM   8118 C  C   . ASP D 1 251 ? -51.486 106.473 10.159  1.00 35.42  ? 249 ASP D C   1 
ATOM   8119 O  O   . ASP D 1 251 ? -50.278 106.679 10.045  1.00 32.15  ? 249 ASP D O   1 
ATOM   8120 C  CB  . ASP D 1 251 ? -51.856 108.976 10.125  1.00 41.42  ? 249 ASP D CB  1 
ATOM   8121 C  CG  . ASP D 1 251 ? -52.864 110.079 10.184  1.00 40.83  ? 249 ASP D CG  1 
ATOM   8122 O  OD1 . ASP D 1 251 ? -53.747 110.153 9.306   1.00 39.93  ? 249 ASP D OD1 1 
ATOM   8123 O  OD2 . ASP D 1 251 ? -52.799 110.867 11.141  1.00 46.97  ? 249 ASP D OD2 1 
ATOM   8124 N  N   . ASN D 1 252 ? -51.975 105.269 10.419  1.00 37.11  ? 250 ASN D N   1 
ATOM   8125 C  CA  . ASN D 1 252 ? -51.133 104.107 10.292  1.00 38.21  ? 250 ASN D CA  1 
ATOM   8126 C  C   . ASN D 1 252 ? -50.986 103.713 8.811   1.00 38.75  ? 250 ASN D C   1 
ATOM   8127 O  O   . ASN D 1 252 ? -51.185 102.556 8.436   1.00 39.53  ? 250 ASN D O   1 
ATOM   8128 C  CB  . ASN D 1 252 ? -51.655 102.935 11.163  1.00 39.46  ? 250 ASN D CB  1 
ATOM   8129 C  CG  . ASN D 1 252 ? -53.135 102.686 10.998  1.00 38.60  ? 250 ASN D CG  1 
ATOM   8130 O  OD1 . ASN D 1 252 ? -53.852 103.452 10.355  1.00 45.88  ? 250 ASN D OD1 1 
ATOM   8131 N  ND2 . ASN D 1 252 ? -53.609 101.608 11.596  1.00 41.29  ? 250 ASN D ND2 1 
ATOM   8132 N  N   . VAL D 1 253 ? -50.603 104.686 7.983   1.00 39.96  ? 251 VAL D N   1 
ATOM   8133 C  CA  . VAL D 1 253 ? -50.416 104.478 6.551   1.00 39.55  ? 251 VAL D CA  1 
ATOM   8134 C  C   . VAL D 1 253 ? -49.036 104.838 6.000   1.00 41.20  ? 251 VAL D C   1 
ATOM   8135 O  O   . VAL D 1 253 ? -48.507 105.888 6.293   1.00 37.87  ? 251 VAL D O   1 
ATOM   8136 C  CB  . VAL D 1 253 ? -51.575 105.071 5.706   1.00 38.24  ? 251 VAL D CB  1 
ATOM   8137 C  CG1 . VAL D 1 253 ? -52.688 105.674 6.548   1.00 29.54  ? 251 VAL D CG1 1 
ATOM   8138 C  CG2 . VAL D 1 253 ? -51.108 105.939 4.553   1.00 34.52  ? 251 VAL D CG2 1 
ATOM   8139 N  N   . ARG D 1 254 ? -48.477 103.962 5.173   1.00 40.29  ? 252 ARG D N   1 
ATOM   8140 C  CA  . ARG D 1 254 ? -47.189 104.212 4.555   1.00 40.68  ? 252 ARG D CA  1 
ATOM   8141 C  C   . ARG D 1 254 ? -47.366 105.137 3.353   1.00 41.15  ? 252 ARG D C   1 
ATOM   8142 O  O   . ARG D 1 254 ? -48.312 104.963 2.606   1.00 45.99  ? 252 ARG D O   1 
ATOM   8143 C  CB  . ARG D 1 254 ? -46.596 102.870 4.128   1.00 43.24  ? 252 ARG D CB  1 
ATOM   8144 C  CG  . ARG D 1 254 ? -45.090 102.877 3.922   1.00 45.88  ? 252 ARG D CG  1 
ATOM   8145 C  CD  . ARG D 1 254 ? -44.683 101.690 3.079   1.00 47.62  ? 252 ARG D CD  1 
ATOM   8146 N  NE  . ARG D 1 254 ? -43.278 101.763 2.720   1.00 51.63  ? 252 ARG D NE  1 
ATOM   8147 C  CZ  . ARG D 1 254 ? -42.668 100.902 1.918   1.00 53.22  ? 252 ARG D CZ  1 
ATOM   8148 N  NH1 . ARG D 1 254 ? -43.351 99.894  1.387   1.00 54.66  ? 252 ARG D NH1 1 
ATOM   8149 N  NH2 . ARG D 1 254 ? -41.379 101.051 1.637   1.00 48.78  ? 252 ARG D NH2 1 
ATOM   8150 N  N   . PRO D 1 255 ? -46.487 106.154 3.184   1.00 42.63  ? 253 PRO D N   1 
ATOM   8151 C  CA  . PRO D 1 255 ? -46.506 107.070 2.012   1.00 41.14  ? 253 PRO D CA  1 
ATOM   8152 C  C   . PRO D 1 255 ? -46.335 106.297 0.691   1.00 47.50  ? 253 PRO D C   1 
ATOM   8153 O  O   . PRO D 1 255 ? -45.899 105.134 0.698   1.00 47.49  ? 253 PRO D O   1 
ATOM   8154 C  CB  . PRO D 1 255 ? -45.289 107.970 2.237   1.00 40.09  ? 253 PRO D CB  1 
ATOM   8155 C  CG  . PRO D 1 255 ? -44.402 107.191 3.162   1.00 41.21  ? 253 PRO D CG  1 
ATOM   8156 C  CD  . PRO D 1 255 ? -45.342 106.436 4.070   1.00 43.07  ? 253 PRO D CD  1 
ATOM   8157 N  N   . LEU D 1 256 ? -46.657 106.950 -0.425  1.00 44.63  ? 254 LEU D N   1 
ATOM   8158 C  CA  . LEU D 1 256 ? -46.798 106.293 -1.711  1.00 42.59  ? 254 LEU D CA  1 
ATOM   8159 C  C   . LEU D 1 256 ? -45.486 105.996 -2.423  1.00 48.32  ? 254 LEU D C   1 
ATOM   8160 O  O   . LEU D 1 256 ? -44.656 106.881 -2.650  1.00 52.77  ? 254 LEU D O   1 
ATOM   8161 C  CB  . LEU D 1 256 ? -47.665 107.147 -2.630  1.00 39.69  ? 254 LEU D CB  1 
ATOM   8162 C  CG  . LEU D 1 256 ? -49.146 107.247 -2.334  1.00 36.41  ? 254 LEU D CG  1 
ATOM   8163 C  CD1 . LEU D 1 256 ? -49.702 108.489 -3.013  1.00 36.92  ? 254 LEU D CD1 1 
ATOM   8164 C  CD2 . LEU D 1 256 ? -49.909 105.994 -2.783  1.00 32.99  ? 254 LEU D CD2 1 
ATOM   8165 N  N   . GLN D 1 257 ? -45.337 104.739 -2.814  1.00 52.63  ? 255 GLN D N   1 
ATOM   8166 C  CA  . GLN D 1 257 ? -44.222 104.290 -3.662  1.00 49.13  ? 255 GLN D CA  1 
ATOM   8167 C  C   . GLN D 1 257 ? -44.505 104.454 -5.157  1.00 49.81  ? 255 GLN D C   1 
ATOM   8168 O  O   . GLN D 1 257 ? -45.653 104.653 -5.563  1.00 46.24  ? 255 GLN D O   1 
ATOM   8169 C  CB  . GLN D 1 257 ? -43.897 102.833 -3.336  1.00 48.37  ? 255 GLN D CB  1 
ATOM   8170 C  CG  . GLN D 1 257 ? -43.929 102.528 -1.851  1.00 48.22  ? 255 GLN D CG  1 
ATOM   8171 C  CD  . GLN D 1 257 ? -43.060 103.475 -1.035  1.00 51.79  ? 255 GLN D CD  1 
ATOM   8172 O  OE1 . GLN D 1 257 ? -41.953 103.851 -1.448  1.00 44.44  ? 255 GLN D OE1 1 
ATOM   8173 N  NE2 . GLN D 1 257 ? -43.565 103.871 0.133   1.00 51.47  ? 255 GLN D NE2 1 
ATOM   8174 N  N   . GLN D 1 258 ? -43.448 104.386 -5.972  1.00 54.87  ? 256 GLN D N   1 
ATOM   8175 C  CA  . GLN D 1 258 ? -43.569 104.547 -7.426  1.00 56.29  ? 256 GLN D CA  1 
ATOM   8176 C  C   . GLN D 1 258 ? -43.804 103.217 -8.113  1.00 54.43  ? 256 GLN D C   1 
ATOM   8177 O  O   . GLN D 1 258 ? -43.247 102.203 -7.707  1.00 53.94  ? 256 GLN D O   1 
ATOM   8178 C  CB  . GLN D 1 258 ? -42.322 105.202 -8.032  1.00 62.94  ? 256 GLN D CB  1 
ATOM   8179 C  CG  . GLN D 1 258 ? -41.016 104.967 -7.270  1.00 72.01  ? 256 GLN D CG  1 
ATOM   8180 C  CD  . GLN D 1 258 ? -40.568 106.183 -6.450  1.00 74.50  ? 256 GLN D CD  1 
ATOM   8181 O  OE1 . GLN D 1 258 ? -39.666 106.082 -5.610  1.00 75.63  ? 256 GLN D OE1 1 
ATOM   8182 N  NE2 . GLN D 1 258 ? -41.194 107.341 -6.698  1.00 68.45  ? 256 GLN D NE2 1 
ATOM   8183 N  N   . LEU D 1 259 ? -44.626 103.229 -9.160  1.00 57.57  ? 257 LEU D N   1 
ATOM   8184 C  CA  . LEU D 1 259 ? -44.846 102.042 -9.993  1.00 61.23  ? 257 LEU D CA  1 
ATOM   8185 C  C   . LEU D 1 259 ? -43.499 101.412 -10.354 1.00 65.99  ? 257 LEU D C   1 
ATOM   8186 O  O   . LEU D 1 259 ? -43.294 100.201 -10.155 1.00 69.83  ? 257 LEU D O   1 
ATOM   8187 C  CB  . LEU D 1 259 ? -45.633 102.403 -11.257 1.00 58.35  ? 257 LEU D CB  1 
ATOM   8188 C  CG  . LEU D 1 259 ? -46.629 101.394 -11.838 1.00 57.46  ? 257 LEU D CG  1 
ATOM   8189 C  CD1 . LEU D 1 259 ? -47.487 100.750 -10.748 1.00 55.31  ? 257 LEU D CD1 1 
ATOM   8190 C  CD2 . LEU D 1 259 ? -47.498 102.058 -12.897 1.00 52.07  ? 257 LEU D CD2 1 
ATOM   8191 N  N   . GLY D 1 260 ? -42.571 102.258 -10.813 1.00 63.09  ? 258 GLY D N   1 
ATOM   8192 C  CA  . GLY D 1 260 ? -41.282 101.804 -11.306 1.00 64.62  ? 258 GLY D CA  1 
ATOM   8193 C  C   . GLY D 1 260 ? -41.533 101.041 -12.592 1.00 65.89  ? 258 GLY D C   1 
ATOM   8194 O  O   . GLY D 1 260 ? -42.403 101.419 -13.382 1.00 62.02  ? 258 GLY D O   1 
ATOM   8195 N  N   . GLN D 1 261 ? -40.809 99.941  -12.777 1.00 65.58  ? 259 GLN D N   1 
ATOM   8196 C  CA  . GLN D 1 261 ? -40.924 99.144  -13.997 1.00 69.07  ? 259 GLN D CA  1 
ATOM   8197 C  C   . GLN D 1 261 ? -42.024 98.095  -13.827 1.00 68.00  ? 259 GLN D C   1 
ATOM   8198 O  O   . GLN D 1 261 ? -41.763 96.883  -13.823 1.00 77.12  ? 259 GLN D O   1 
ATOM   8199 C  CB  . GLN D 1 261 ? -39.567 98.530  -14.366 1.00 69.76  ? 259 GLN D CB  1 
ATOM   8200 C  CG  . GLN D 1 261 ? -38.612 99.464  -15.123 1.00 76.36  ? 259 GLN D CG  1 
ATOM   8201 C  CD  . GLN D 1 261 ? -38.498 100.892 -14.573 1.00 77.17  ? 259 GLN D CD  1 
ATOM   8202 O  OE1 . GLN D 1 261 ? -38.719 101.869 -15.305 1.00 68.27  ? 259 GLN D OE1 1 
ATOM   8203 N  NE2 . GLN D 1 261 ? -38.138 101.021 -13.290 1.00 76.82  ? 259 GLN D NE2 1 
ATOM   8204 N  N   . ARG D 1 262 ? -43.253 98.590  -13.676 1.00 57.47  ? 260 ARG D N   1 
ATOM   8205 C  CA  . ARG D 1 262 ? -44.428 97.770  -13.388 1.00 57.57  ? 260 ARG D CA  1 
ATOM   8206 C  C   . ARG D 1 262 ? -45.627 98.355  -14.089 1.00 53.03  ? 260 ARG D C   1 
ATOM   8207 O  O   . ARG D 1 262 ? -45.592 99.493  -14.549 1.00 54.92  ? 260 ARG D O   1 
ATOM   8208 C  CB  . ARG D 1 262 ? -44.721 97.739  -11.874 1.00 61.89  ? 260 ARG D CB  1 
ATOM   8209 C  CG  . ARG D 1 262 ? -43.799 96.842  -11.057 1.00 64.24  ? 260 ARG D CG  1 
ATOM   8210 C  CD  . ARG D 1 262 ? -44.275 96.720  -9.623  1.00 65.83  ? 260 ARG D CD  1 
ATOM   8211 N  NE  . ARG D 1 262 ? -43.937 97.913  -8.848  1.00 71.79  ? 260 ARG D NE  1 
ATOM   8212 C  CZ  . ARG D 1 262 ? -44.385 98.190  -7.621  1.00 67.41  ? 260 ARG D CZ  1 
ATOM   8213 N  NH1 . ARG D 1 262 ? -45.222 97.368  -6.986  1.00 59.56  ? 260 ARG D NH1 1 
ATOM   8214 N  NH2 . ARG D 1 262 ? -43.990 99.311  -7.031  1.00 61.11  ? 260 ARG D NH2 1 
ATOM   8215 N  N   . THR D 1 263 ? -46.704 97.580  -14.161 1.00 56.06  ? 261 THR D N   1 
ATOM   8216 C  CA  . THR D 1 263 ? -47.966 98.079  -14.711 1.00 51.28  ? 261 THR D CA  1 
ATOM   8217 C  C   . THR D 1 263 ? -49.161 97.501  -13.915 1.00 47.70  ? 261 THR D C   1 
ATOM   8218 O  O   . THR D 1 263 ? -49.018 96.525  -13.173 1.00 42.46  ? 261 THR D O   1 
ATOM   8219 C  CB  . THR D 1 263 ? -48.085 97.855  -16.264 1.00 55.52  ? 261 THR D CB  1 
ATOM   8220 O  OG1 . THR D 1 263 ? -48.990 96.782  -16.574 1.00 53.85  ? 261 THR D OG1 1 
ATOM   8221 C  CG2 . THR D 1 263 ? -46.702 97.589  -16.940 1.00 55.45  ? 261 THR D CG2 1 
ATOM   8222 N  N   . VAL D 1 264 ? -50.327 98.124  -14.060 1.00 44.27  ? 262 VAL D N   1 
ATOM   8223 C  CA  . VAL D 1 264 ? -51.538 97.621  -13.419 1.00 44.13  ? 262 VAL D CA  1 
ATOM   8224 C  C   . VAL D 1 264 ? -52.586 97.138  -14.424 1.00 45.20  ? 262 VAL D C   1 
ATOM   8225 O  O   . VAL D 1 264 ? -52.751 97.741  -15.490 1.00 38.21  ? 262 VAL D O   1 
ATOM   8226 C  CB  . VAL D 1 264 ? -52.149 98.685  -12.482 1.00 42.81  ? 262 VAL D CB  1 
ATOM   8227 C  CG1 . VAL D 1 264 ? -53.407 98.157  -11.798 1.00 42.73  ? 262 VAL D CG1 1 
ATOM   8228 C  CG2 . VAL D 1 264 ? -51.114 99.116  -11.450 1.00 40.85  ? 262 VAL D CG2 1 
ATOM   8229 N  N   . ILE D 1 265 ? -53.290 96.053  -14.058 1.00 45.52  ? 263 ILE D N   1 
ATOM   8230 C  CA  . ILE D 1 265 ? -54.406 95.514  -14.836 1.00 41.39  ? 263 ILE D CA  1 
ATOM   8231 C  C   . ILE D 1 265 ? -55.734 95.533  -14.084 1.00 44.02  ? 263 ILE D C   1 
ATOM   8232 O  O   . ILE D 1 265 ? -55.787 95.542  -12.855 1.00 46.29  ? 263 ILE D O   1 
ATOM   8233 C  CB  . ILE D 1 265 ? -54.133 94.064  -15.352 1.00 42.52  ? 263 ILE D CB  1 
ATOM   8234 C  CG1 . ILE D 1 265 ? -53.691 93.122  -14.224 1.00 38.95  ? 263 ILE D CG1 1 
ATOM   8235 C  CG2 . ILE D 1 265 ? -53.101 94.062  -16.484 1.00 42.14  ? 263 ILE D CG2 1 
ATOM   8236 C  CD1 . ILE D 1 265 ? -53.372 91.687  -14.663 1.00 44.10  ? 263 ILE D CD1 1 
ATOM   8237 N  N   . LYS D 1 266 ? -56.819 95.555  -14.833 1.00 45.97  ? 264 LYS D N   1 
ATOM   8238 C  CA  . LYS D 1 266 ? -58.111 95.405  -14.217 1.00 49.18  ? 264 LYS D CA  1 
ATOM   8239 C  C   . LYS D 1 266 ? -58.876 94.202  -14.757 1.00 48.17  ? 264 LYS D C   1 
ATOM   8240 O  O   . LYS D 1 266 ? -58.376 93.461  -15.609 1.00 57.44  ? 264 LYS D O   1 
ATOM   8241 C  CB  . LYS D 1 266 ? -58.930 96.718  -14.256 1.00 46.98  ? 264 LYS D CB  1 
ATOM   8242 C  CG  . LYS D 1 266 ? -59.227 97.328  -15.614 1.00 47.36  ? 264 LYS D CG  1 
ATOM   8243 C  CD  . LYS D 1 266 ? -59.687 98.767  -15.398 1.00 47.48  ? 264 LYS D CD  1 
ATOM   8244 C  CE  . LYS D 1 266 ? -60.248 99.425  -16.646 1.00 46.22  ? 264 LYS D CE  1 
ATOM   8245 N  NZ  . LYS D 1 266 ? -60.308 100.907 -16.450 1.00 50.13  ? 264 LYS D NZ  1 
ATOM   8246 N  N   . SER D 1 267 ? -60.075 94.022  -14.226 1.00 50.33  ? 265 SER D N   1 
ATOM   8247 C  CA  . SER D 1 267 ? -60.932 92.887  -14.481 1.00 54.34  ? 265 SER D CA  1 
ATOM   8248 C  C   . SER D 1 267 ? -62.191 93.380  -15.183 1.00 58.10  ? 265 SER D C   1 
ATOM   8249 O  O   . SER D 1 267 ? -62.899 94.264  -14.682 1.00 56.61  ? 265 SER D O   1 
ATOM   8250 C  CB  . SER D 1 267 ? -61.321 92.238  -13.146 1.00 53.39  ? 265 SER D CB  1 
ATOM   8251 O  OG  . SER D 1 267 ? -62.285 93.026  -12.448 1.00 48.95  ? 265 SER D OG  1 
ATOM   8252 O  OXT . SER D 1 267 ? -62.538 92.901  -16.258 1.00 62.28  ? 265 SER D OXT 1 
HETATM 8253 ZN ZN  . ZN  E 2 .   ? -1.061  1.481   10.055  1.00 23.92  ? 301 ZN  A ZN  1 
HETATM 8254 C  C13 . 6CC F 3 .   ? -3.074  5.721   6.978   1.00 47.60  ? 302 6CC A C13 1 
HETATM 8255 CL CL1 . 6CC F 3 .   ? 3.311   5.650   10.171  1.00 35.58  ? 302 6CC A CL1 1 
HETATM 8256 C  C5  . 6CC F 3 .   ? 1.717   5.976   9.407   1.00 29.91  ? 302 6CC A C5  1 
HETATM 8257 C  C6  . 6CC F 3 .   ? 0.858   4.957   8.978   1.00 32.25  ? 302 6CC A C6  1 
HETATM 8258 S  S7  . 6CC F 3 .   ? 1.336   3.270   9.238   1.00 30.78  ? 302 6CC A S7  1 
HETATM 8259 O  O9  . 6CC F 3 .   ? 1.607   3.100   10.777  1.00 29.94  ? 302 6CC A O9  1 
HETATM 8260 O  O10 . 6CC F 3 .   ? 2.728   3.022   8.635   1.00 26.63  ? 302 6CC A O10 1 
HETATM 8261 N  N8  . 6CC F 3 .   ? 0.184   2.133   8.744   1.00 26.15  ? 302 6CC A N8  1 
HETATM 8262 C  C2  . 6CC F 3 .   ? -0.397  5.181   8.353   1.00 34.38  ? 302 6CC A C2  1 
HETATM 8263 C  C4  . 6CC F 3 .   ? 1.258   7.303   9.154   1.00 35.02  ? 302 6CC A C4  1 
HETATM 8264 C  C3  . 6CC F 3 .   ? 0.000   7.530   8.525   1.00 35.44  ? 302 6CC A C3  1 
HETATM 8265 C  C1  . 6CC F 3 .   ? -0.854  6.479   8.110   1.00 37.95  ? 302 6CC A C1  1 
HETATM 8266 C  C12 . 6CC F 3 .   ? -2.191  6.725   7.462   1.00 41.23  ? 302 6CC A C12 1 
HETATM 8267 N  N16 . 6CC F 3 .   ? -2.688  8.000   7.306   1.00 51.53  ? 302 6CC A N16 1 
HETATM 8268 C  C15 . 6CC F 3 .   ? -3.905  8.023   6.703   1.00 52.10  ? 302 6CC A C15 1 
HETATM 8269 N  N17 . 6CC F 3 .   ? -4.583  9.230   6.449   1.00 53.86  ? 302 6CC A N17 1 
HETATM 8270 S  S14 . 6CC F 3 .   ? -4.425  6.491   6.368   1.00 51.87  ? 302 6CC A S14 1 
HETATM 8271 ZN ZN  . ZN  G 2 .   ? -30.407 33.482  18.367  1.00 26.31  ? 301 ZN  B ZN  1 
HETATM 8272 C  C13 . 6CC H 3 .   ? -31.505 29.587  15.253  1.00 44.97  ? 302 6CC B C13 1 
HETATM 8273 CL CL1 . 6CC H 3 .   ? -32.196 29.108  22.096  1.00 38.89  ? 302 6CC B CL1 1 
HETATM 8274 C  C5  . 6CC H 3 .   ? -32.157 28.868  20.345  1.00 30.19  ? 302 6CC B C5  1 
HETATM 8275 C  C6  . 6CC H 3 .   ? -32.086 29.972  19.536  1.00 29.74  ? 302 6CC B C6  1 
HETATM 8276 S  S7  . 6CC H 3 .   ? -32.033 31.667  20.169  1.00 29.61  ? 302 6CC B S7  1 
HETATM 8277 O  O9  . 6CC H 3 .   ? -31.018 31.880  21.217  1.00 25.93  ? 302 6CC B O9  1 
HETATM 8278 O  O10 . 6CC H 3 .   ? -33.391 32.098  20.759  1.00 24.05  ? 302 6CC B O10 1 
HETATM 8279 N  N8  . 6CC H 3 .   ? -31.717 32.771  18.814  1.00 30.03  ? 302 6CC B N8  1 
HETATM 8280 C  C2  . 6CC H 3 .   ? -32.064 29.802  18.141  1.00 31.00  ? 302 6CC B C2  1 
HETATM 8281 C  C4  . 6CC H 3 .   ? -32.162 27.580  19.738  1.00 32.95  ? 302 6CC B C4  1 
HETATM 8282 C  C3  . 6CC H 3 .   ? -32.140 27.405  18.341  1.00 31.00  ? 302 6CC B C3  1 
HETATM 8283 C  C1  . 6CC H 3 .   ? -32.087 28.539  17.518  1.00 36.48  ? 302 6CC B C1  1 
HETATM 8284 C  C12 . 6CC H 3 .   ? -32.030 28.508  16.020  1.00 39.05  ? 302 6CC B C12 1 
HETATM 8285 N  N16 . 6CC H 3 .   ? -32.485 27.450  15.256  1.00 47.15  ? 302 6CC B N16 1 
HETATM 8286 C  C15 . 6CC H 3 .   ? -32.352 27.685  13.924  1.00 47.85  ? 302 6CC B C15 1 
HETATM 8287 N  N17 . 6CC H 3 .   ? -32.737 26.793  12.919  1.00 57.38  ? 302 6CC B N17 1 
HETATM 8288 S  S14 . 6CC H 3 .   ? -31.681 29.158  13.651  1.00 42.26  ? 302 6CC B S14 1 
HETATM 8289 ZN ZN  . ZN  I 2 .   ? -46.433 66.721  15.095  1.00 42.12  ? 301 ZN  C ZN  1 
HETATM 8290 C  C13 . 6CC J 3 .   ? -49.156 69.571  11.172  1.00 81.30  ? 302 6CC C C13 1 
HETATM 8291 CL CL1 . 6CC J 3 .   ? -42.876 71.442  12.859  1.00 65.00  ? 302 6CC C CL1 1 
HETATM 8292 C  C5  . 6CC J 3 .   ? -44.405 70.970  12.137  1.00 63.14  ? 302 6CC C C5  1 
HETATM 8293 C  C6  . 6CC J 3 .   ? -45.084 69.773  12.495  1.00 54.23  ? 302 6CC C C6  1 
HETATM 8294 S  S7  . 6CC J 3 .   ? -44.509 68.586  13.724  1.00 49.43  ? 302 6CC C S7  1 
HETATM 8295 O  O9  . 6CC J 3 .   ? -44.855 69.008  15.172  1.00 38.30  ? 302 6CC C O9  1 
HETATM 8296 O  O10 . 6CC J 3 .   ? -42.960 68.468  13.667  1.00 37.65  ? 302 6CC C O10 1 
HETATM 8297 N  N8  . 6CC J 3 .   ? -45.191 66.940  13.708  1.00 33.84  ? 302 6CC C N8  1 
HETATM 8298 C  C2  . 6CC J 3 .   ? -46.287 69.499  11.868  1.00 62.44  ? 302 6CC C C2  1 
HETATM 8299 C  C4  . 6CC J 3 .   ? -44.935 71.840  11.176  1.00 63.86  ? 302 6CC C C4  1 
HETATM 8300 C  C3  . 6CC J 3 .   ? -46.149 71.543  10.559  1.00 71.48  ? 302 6CC C C3  1 
HETATM 8301 C  C1  . 6CC J 3 .   ? -46.811 70.364  10.908  1.00 70.08  ? 302 6CC C C1  1 
HETATM 8302 C  C12 . 6CC J 3 .   ? -48.092 69.975  10.333  1.00 78.75  ? 302 6CC C C12 1 
HETATM 8303 N  N16 . 6CC J 3 .   ? -48.331 69.955  8.977   1.00 81.74  ? 302 6CC C N16 1 
HETATM 8304 C  C15 . 6CC J 3 .   ? -49.584 69.528  8.722   1.00 90.31  ? 302 6CC C C15 1 
HETATM 8305 N  N17 . 6CC J 3 .   ? -50.130 69.394  7.432   1.00 98.98  ? 302 6CC C N17 1 
HETATM 8306 S  S14 . 6CC J 3 .   ? -50.371 69.189  10.126  1.00 93.65  ? 302 6CC C S14 1 
HETATM 8307 ZN ZN  . ZN  K 2 .   ? -51.733 96.433  5.522   1.00 36.75  ? 301 ZN  D ZN  1 
HETATM 8308 O  O   . HOH L 4 .   ? -5.259  5.881   32.459  1.00 33.49  ? 401 HOH A O   1 
HETATM 8309 O  O   . HOH L 4 .   ? -6.985  -8.747  4.269   1.00 50.92  ? 402 HOH A O   1 
HETATM 8310 O  O   . HOH L 4 .   ? 0.471   -7.907  4.956   1.00 23.76  ? 403 HOH A O   1 
HETATM 8311 O  O   . HOH L 4 .   ? -20.507 11.688  14.157  1.00 47.00  ? 404 HOH A O   1 
HETATM 8312 O  O   . HOH L 4 .   ? 9.183   2.109   16.829  1.00 32.61  ? 405 HOH A O   1 
HETATM 8313 O  O   . HOH L 4 .   ? -12.351 1.344   -8.595  1.00 51.86  ? 406 HOH A O   1 
HETATM 8314 O  O   . HOH L 4 .   ? 0.133   10.355  10.717  1.00 31.96  ? 407 HOH A O   1 
HETATM 8315 O  O   . HOH L 4 .   ? -5.064  -4.902  -0.109  1.00 26.47  ? 408 HOH A O   1 
HETATM 8316 O  O   . HOH L 4 .   ? 3.785   -17.132 15.382  1.00 43.10  ? 409 HOH A O   1 
HETATM 8317 O  O   . HOH L 4 .   ? 12.561  -10.221 23.160  1.00 38.00  ? 410 HOH A O   1 
HETATM 8318 O  O   . HOH L 4 .   ? -7.993  14.213  20.214  1.00 29.13  ? 411 HOH A O   1 
HETATM 8319 O  O   . HOH L 4 .   ? 8.293   -10.200 4.457   1.00 25.33  ? 412 HOH A O   1 
HETATM 8320 O  O   . HOH L 4 .   ? -8.471  -13.927 16.595  1.00 31.87  ? 413 HOH A O   1 
HETATM 8321 O  O   . HOH L 4 .   ? -0.854  8.118   4.219   1.00 47.58  ? 414 HOH A O   1 
HETATM 8322 O  O   . HOH L 4 .   ? 16.641  -10.640 10.887  1.00 41.01  ? 415 HOH A O   1 
HETATM 8323 O  O   . HOH L 4 .   ? 0.247   3.276   -10.982 1.00 51.30  ? 416 HOH A O   1 
HETATM 8324 O  O   . HOH L 4 .   ? -3.700  8.896   27.505  1.00 33.12  ? 417 HOH A O   1 
HETATM 8325 O  O   . HOH L 4 .   ? 3.919   -13.684 28.800  1.00 67.35  ? 418 HOH A O   1 
HETATM 8326 O  O   . HOH L 4 .   ? 12.048  -11.757 9.229   1.00 33.57  ? 419 HOH A O   1 
HETATM 8327 O  O   . HOH L 4 .   ? 14.832  16.491  22.074  1.00 48.60  ? 420 HOH A O   1 
HETATM 8328 O  O   . HOH L 4 .   ? 17.955  -5.331  27.412  1.00 40.87  ? 421 HOH A O   1 
HETATM 8329 O  O   . HOH L 4 .   ? 1.032   -10.394 1.299   1.00 31.41  ? 422 HOH A O   1 
HETATM 8330 O  O   . HOH L 4 .   ? -5.225  -7.576  25.977  1.00 37.08  ? 423 HOH A O   1 
HETATM 8331 O  O   . HOH L 4 .   ? 15.950  -4.491  -5.128  1.00 49.49  ? 424 HOH A O   1 
HETATM 8332 O  O   . HOH L 4 .   ? 10.670  -3.865  0.688   1.00 43.20  ? 425 HOH A O   1 
HETATM 8333 O  O   . HOH L 4 .   ? 5.980   -12.190 0.358   1.00 44.02  ? 426 HOH A O   1 
HETATM 8334 O  O   . HOH L 4 .   ? 9.509   -2.120  27.045  1.00 39.01  ? 427 HOH A O   1 
HETATM 8335 O  O   . HOH L 4 .   ? 6.396   17.597  10.920  1.00 56.98  ? 428 HOH A O   1 
HETATM 8336 O  O   . HOH L 4 .   ? -10.785 3.366   24.303  1.00 38.26  ? 429 HOH A O   1 
HETATM 8337 O  O   . HOH L 4 .   ? 15.218  2.639   5.754   1.00 44.84  ? 430 HOH A O   1 
HETATM 8338 O  O   . HOH L 4 .   ? 3.294   10.423  32.493  1.00 49.87  ? 431 HOH A O   1 
HETATM 8339 O  O   . HOH L 4 .   ? 2.977   -14.580 6.403   1.00 27.87  ? 432 HOH A O   1 
HETATM 8340 O  O   . HOH L 4 .   ? -23.556 -3.536  5.565   1.00 55.19  ? 433 HOH A O   1 
HETATM 8341 O  O   . HOH L 4 .   ? -3.147  -7.772  2.033   1.00 37.82  ? 434 HOH A O   1 
HETATM 8342 O  O   . HOH L 4 .   ? 1.979   -2.356  -1.952  1.00 33.46  ? 435 HOH A O   1 
HETATM 8343 O  O   . HOH L 4 .   ? 8.973   -14.548 28.418  1.00 54.80  ? 436 HOH A O   1 
HETATM 8344 O  O   . HOH L 4 .   ? 11.357  7.464   0.841   1.00 46.43  ? 437 HOH A O   1 
HETATM 8345 O  O   . HOH L 4 .   ? -4.218  9.837   1.832   1.00 46.70  ? 438 HOH A O   1 
HETATM 8346 O  O   . HOH L 4 .   ? -9.366  -12.370 26.969  1.00 42.59  ? 439 HOH A O   1 
HETATM 8347 O  O   . HOH L 4 .   ? -4.526  -0.976  31.487  1.00 47.40  ? 440 HOH A O   1 
HETATM 8348 O  O   . HOH L 4 .   ? 13.943  -8.391  28.056  1.00 40.50  ? 441 HOH A O   1 
HETATM 8349 O  O   . HOH L 4 .   ? -2.888  -6.675  -3.344  1.00 42.25  ? 442 HOH A O   1 
HETATM 8350 O  O   . HOH L 4 .   ? -16.473 1.884   29.510  1.00 42.04  ? 443 HOH A O   1 
HETATM 8351 O  O   . HOH L 4 .   ? 19.411  -3.147  8.377   1.00 31.84  ? 444 HOH A O   1 
HETATM 8352 O  O   . HOH L 4 .   ? 3.019   10.761  4.429   1.00 39.04  ? 445 HOH A O   1 
HETATM 8353 O  O   . HOH L 4 .   ? 10.851  -13.750 19.990  1.00 64.25  ? 446 HOH A O   1 
HETATM 8354 O  O   . HOH L 4 .   ? 21.837  -7.330  13.637  1.00 40.61  ? 447 HOH A O   1 
HETATM 8355 O  O   . HOH L 4 .   ? 7.122   -12.276 3.502   1.00 28.74  ? 448 HOH A O   1 
HETATM 8356 O  O   . HOH L 4 .   ? 20.420  2.700   4.239   1.00 45.14  ? 449 HOH A O   1 
HETATM 8357 O  O   . HOH L 4 .   ? 14.311  8.102   0.964   1.00 53.17  ? 450 HOH A O   1 
HETATM 8358 O  O   . HOH L 4 .   ? -1.343  -19.388 7.108   1.00 37.52  ? 451 HOH A O   1 
HETATM 8359 O  O   . HOH M 4 .   ? -15.901 19.511  14.639  1.00 21.40  ? 401 HOH B O   1 
HETATM 8360 O  O   . HOH M 4 .   ? -44.317 45.169  32.438  1.00 41.82  ? 402 HOH B O   1 
HETATM 8361 O  O   . HOH M 4 .   ? -45.752 37.161  19.195  1.00 27.49  ? 403 HOH B O   1 
HETATM 8362 O  O   . HOH M 4 .   ? -32.394 43.681  11.252  1.00 34.36  ? 404 HOH B O   1 
HETATM 8363 O  O   . HOH M 4 .   ? -32.073 34.424  36.945  1.00 39.53  ? 405 HOH B O   1 
HETATM 8364 O  O   . HOH M 4 .   ? -24.135 20.430  19.532  1.00 26.29  ? 406 HOH B O   1 
HETATM 8365 O  O   . HOH M 4 .   ? -31.465 32.832  12.802  1.00 31.14  ? 407 HOH B O   1 
HETATM 8366 O  O   . HOH M 4 .   ? -9.334  32.235  18.202  1.00 52.39  ? 408 HOH B O   1 
HETATM 8367 O  O   . HOH M 4 .   ? -13.951 22.674  25.094  1.00 30.47  ? 409 HOH B O   1 
HETATM 8368 O  O   . HOH M 4 .   ? -4.962  32.641  8.575   1.00 45.30  ? 410 HOH B O   1 
HETATM 8369 O  O   . HOH M 4 .   ? -35.678 42.833  17.255  1.00 25.84  ? 411 HOH B O   1 
HETATM 8370 O  O   . HOH M 4 .   ? -36.404 42.551  12.742  1.00 36.82  ? 412 HOH B O   1 
HETATM 8371 O  O   . HOH M 4 .   ? -39.896 45.263  23.983  1.00 29.85  ? 413 HOH B O   1 
HETATM 8372 O  O   . HOH M 4 .   ? -39.484 48.680  25.880  1.00 38.28  ? 414 HOH B O   1 
HETATM 8373 O  O   . HOH M 4 .   ? -11.892 24.626  31.800  1.00 40.04  ? 415 HOH B O   1 
HETATM 8374 O  O   . HOH M 4 .   ? -18.175 16.002  23.006  1.00 48.51  ? 416 HOH B O   1 
HETATM 8375 O  O   . HOH M 4 .   ? -38.768 45.207  15.927  1.00 35.09  ? 417 HOH B O   1 
HETATM 8376 O  O   . HOH M 4 .   ? -44.269 38.540  24.440  1.00 38.99  ? 418 HOH B O   1 
HETATM 8377 O  O   . HOH M 4 .   ? -10.113 44.872  2.408   1.00 51.50  ? 419 HOH B O   1 
HETATM 8378 O  O   . HOH M 4 .   ? -44.176 46.799  28.884  1.00 46.82  ? 420 HOH B O   1 
HETATM 8379 O  O   . HOH M 4 .   ? -39.567 31.337  30.402  1.00 42.56  ? 421 HOH B O   1 
HETATM 8380 O  O   . HOH M 4 .   ? -9.712  18.231  24.439  1.00 44.61  ? 422 HOH B O   1 
HETATM 8381 O  O   . HOH M 4 .   ? -33.421 50.078  15.069  1.00 45.90  ? 423 HOH B O   1 
HETATM 8382 O  O   . HOH M 4 .   ? -42.954 44.044  16.581  1.00 44.02  ? 424 HOH B O   1 
HETATM 8383 O  O   . HOH M 4 .   ? -13.995 43.009  21.815  1.00 51.52  ? 425 HOH B O   1 
HETATM 8384 O  O   . HOH M 4 .   ? -9.983  49.087  19.404  1.00 60.07  ? 426 HOH B O   1 
HETATM 8385 O  O   . HOH M 4 .   ? -32.113 27.936  -1.338  1.00 49.59  ? 427 HOH B O   1 
HETATM 8386 O  O   . HOH M 4 .   ? -17.793 19.878  7.892   1.00 40.87  ? 428 HOH B O   1 
HETATM 8387 O  O   . HOH M 4 .   ? -37.647 26.903  7.439   1.00 42.04  ? 429 HOH B O   1 
HETATM 8388 O  O   . HOH M 4 .   ? -14.776 44.214  25.758  1.00 43.68  ? 430 HOH B O   1 
HETATM 8389 O  O   . HOH M 4 .   ? -43.497 44.986  21.360  1.00 40.15  ? 431 HOH B O   1 
HETATM 8390 O  O   . HOH M 4 .   ? -16.723 27.371  -1.000  1.00 45.95  ? 432 HOH B O   1 
HETATM 8391 O  O   . HOH M 4 .   ? -35.497 30.624  1.531   1.00 48.45  ? 433 HOH B O   1 
HETATM 8392 O  O   . HOH M 4 .   ? -8.413  30.408  10.418  1.00 40.55  ? 434 HOH B O   1 
HETATM 8393 O  O   . HOH M 4 .   ? -7.911  20.612  18.604  1.00 36.43  ? 435 HOH B O   1 
HETATM 8394 O  O   . HOH M 4 .   ? -45.161 32.484  34.710  1.00 46.39  ? 436 HOH B O   1 
HETATM 8395 O  O   . HOH M 4 .   ? -41.452 38.015  35.894  1.00 33.42  ? 437 HOH B O   1 
HETATM 8396 O  O   . HOH M 4 .   ? -36.029 44.213  15.107  1.00 32.86  ? 438 HOH B O   1 
HETATM 8397 O  O   . HOH M 4 .   ? -35.690 51.130  16.671  1.00 43.41  ? 439 HOH B O   1 
HETATM 8398 O  O   . HOH M 4 .   ? -42.094 46.460  4.894   1.00 52.48  ? 440 HOH B O   1 
HETATM 8399 O  O   . HOH M 4 .   ? -3.540  24.713  13.987  1.00 36.49  ? 441 HOH B O   1 
HETATM 8400 O  O   . HOH M 4 .   ? -20.220 53.411  22.816  1.00 57.46  ? 442 HOH B O   1 
HETATM 8401 O  O   . HOH M 4 .   ? -40.030 47.215  22.400  1.00 31.41  ? 443 HOH B O   1 
HETATM 8402 O  O   . HOH M 4 .   ? -22.158 47.242  2.948   1.00 41.42  ? 444 HOH B O   1 
HETATM 8403 O  O   . HOH M 4 .   ? -8.510  21.753  31.033  1.00 55.69  ? 445 HOH B O   1 
HETATM 8404 O  O   . HOH N 4 .   ? -41.783 56.884  15.835  1.00 39.63  ? 401 HOH C O   1 
HETATM 8405 O  O   . HOH N 4 .   ? -31.503 55.001  29.493  1.00 41.43  ? 402 HOH C O   1 
HETATM 8406 O  O   . HOH N 4 .   ? -23.299 78.999  27.545  1.00 63.08  ? 403 HOH C O   1 
HETATM 8407 O  O   . HOH N 4 .   ? -63.828 54.149  22.837  1.00 60.10  ? 404 HOH C O   1 
HETATM 8408 O  O   . HOH N 4 .   ? -40.296 89.017  21.134  1.00 50.19  ? 405 HOH C O   1 
HETATM 8409 O  O   . HOH N 4 .   ? -47.756 54.383  26.949  1.00 43.18  ? 406 HOH C O   1 
HETATM 8410 O  O   . HOH N 4 .   ? -36.991 55.902  30.561  1.00 35.22  ? 407 HOH C O   1 
HETATM 8411 O  O   . HOH N 4 .   ? -52.050 50.413  15.335  1.00 40.14  ? 408 HOH C O   1 
HETATM 8412 O  O   . HOH N 4 .   ? -38.409 49.409  21.706  1.00 36.57  ? 409 HOH C O   1 
HETATM 8413 O  O   . HOH N 4 .   ? -47.853 54.023  14.947  1.00 46.80  ? 410 HOH C O   1 
HETATM 8414 O  O   . HOH N 4 .   ? -50.022 64.433  11.515  1.00 35.28  ? 411 HOH C O   1 
HETATM 8415 O  O   . HOH N 4 .   ? -44.928 54.284  12.500  1.00 38.74  ? 412 HOH C O   1 
HETATM 8416 O  O   . HOH N 4 .   ? -54.160 53.096  24.451  1.00 44.67  ? 413 HOH C O   1 
HETATM 8417 O  O   . HOH O 4 .   ? -49.897 106.168 0.894   1.00 26.67  ? 401 HOH D O   1 
HETATM 8418 O  O   . HOH O 4 .   ? -53.177 88.216  -11.887 1.00 40.39  ? 402 HOH D O   1 
HETATM 8419 O  O   . HOH O 4 .   ? -46.539 107.768 8.130   1.00 36.26  ? 403 HOH D O   1 
HETATM 8420 O  O   . HOH O 4 .   ? -47.616 105.874 -7.191  1.00 35.75  ? 404 HOH D O   1 
HETATM 8421 O  O   . HOH O 4 .   ? -63.080 83.583  18.620  1.00 60.15  ? 405 HOH D O   1 
HETATM 8422 O  O   . HOH O 4 .   ? -54.031 113.537 -4.612  1.00 36.90  ? 406 HOH D O   1 
HETATM 8423 O  O   . HOH O 4 .   ? -52.513 110.266 -4.670  1.00 33.80  ? 407 HOH D O   1 
HETATM 8424 O  O   . HOH O 4 .   ? -51.848 109.423 7.126   1.00 40.85  ? 408 HOH D O   1 
HETATM 8425 O  O   . HOH O 4 .   ? -62.828 110.099 8.311   1.00 62.43  ? 409 HOH D O   1 
HETATM 8426 O  O   . HOH O 4 .   ? -42.097 113.592 11.363  1.00 47.25  ? 410 HOH D O   1 
HETATM 8427 O  O   . HOH O 4 .   ? -50.663 93.944  10.741  1.00 48.04  ? 411 HOH D O   1 
# 
