data_4WUP
# 
_entry.id   4WUP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.383 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   4WUP         pdb_00004wup 10.2210/pdb4wup/pdb 
WWPDB D_1000204539 ?            ?                   
# 
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 2015-07-01 
2 'Structure model' 1 1 2018-03-07 
3 'Structure model' 1 2 2024-01-10 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Database references'    
4 3 'Structure model' 'Derived calculations'   
5 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' diffrn_source                 
2 3 'Structure model' chem_comp_atom                
3 3 'Structure model' chem_comp_bond                
4 3 'Structure model' database_2                    
5 3 'Structure model' pdbx_initial_refinement_model 
6 3 'Structure model' struct_conn                   
# 
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' '_diffrn_source.pdbx_synchrotron_site' 
2  3 'Structure model' '_database_2.pdbx_DOI'                 
3  3 'Structure model' '_database_2.pdbx_database_accession'  
4  3 'Structure model' '_struct_conn.pdbx_dist_value'         
5  3 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id' 
6  3 'Structure model' '_struct_conn.ptnr1_auth_asym_id'      
7  3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'      
8  3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'       
9  3 'Structure model' '_struct_conn.ptnr1_label_asym_id'     
10 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'     
11 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'     
12 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'      
13 3 'Structure model' '_struct_conn.ptnr2_auth_asym_id'      
14 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'      
15 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'       
16 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'     
17 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'     
18 3 '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                        4WUP 
_pdbx_database_status.recvd_initial_deposition_date   2014-11-03 
_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            ? 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          4WR7 
_pdbx_database_related.content_type   unspecified 
# 
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                   NE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biophys.Chem. 
_citation.journal_id_ASTM           BICIAZ 
_citation.journal_id_CSD            0829 
_citation.journal_id_ISSN           0301-4622 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            205 
_citation.language                  ? 
_citation.page_first                51 
_citation.page_last                 65 
_citation.title                     
;Intrinsic thermodynamics of 4-substituted-2,3,5,6-tetrafluorobenzenesulfonamide binding to carbonic anhydrases by isothermal titration calorimetry.
;
_citation.year                      2015 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bpc.2015.05.009 
_citation.pdbx_database_id_PubMed   26079542 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zubriene, A.'      1  ? 
primary 'Smirnoviene, J.'   2  ? 
primary 'Smirnov, A.'       3  ? 
primary 'Morkunaite, V.'    4  ? 
primary 'Michailoviene, V.' 5  ? 
primary 'Jachno, J.'        6  ? 
primary 'Juozapaitiene, V.' 7  ? 
primary 'Norvaisas, P.'     8  ? 
primary 'Manakova, E.'      9  ? 
primary 'Grazulis, S.'      10 ? 
primary 'Matulis, D.'       11 ? 
# 
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 1'                           28835.105 2   4.2.1.1 ? 'UNP residues 3-261' ? 
2 non-polymer syn 'ZINC ION'                                       65.409    2   ?       ? 
'4-[(2-Hydroxyethyl)thio]benzenesulfonamide' ? 
3 non-polymer syn '4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' 233.308   2   ?       ? Zn ? 
4 non-polymer syn 'ACETATE ION'                                    59.044    1   ?       ? 'ACETATE ION' ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                          106.120   1   ?       ? 'DI(HYDROXYETHYL)ETHER' ? 
6 water       nat water                                            18.015    370 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase I,Carbonic anhydrase B,CAB,Carbonic anhydrase I,CA-I' 
# 
_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       
;MSPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLK
GGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKV
LDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVP
MQHNNRPTQPLKGRTVRASF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLK
GGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKV
LDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVP
MQHNNRPTQPLKGRTVRASF
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                       ZN  
3 '4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' 3UF 
4 'ACETATE ION'                                    ACT 
5 'DI(HYDROXYETHYL)ETHER'                          PEG 
6 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   SER n 
1 3   PRO n 
1 4   ASP n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   ASP n 
1 9   ASP n 
1 10  LYS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  GLN n 
1 16  TRP n 
1 17  SER n 
1 18  LYS n 
1 19  LEU n 
1 20  TYR n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  ASN n 
1 25  GLY n 
1 26  ASN n 
1 27  ASN n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  LYS n 
1 35  THR n 
1 36  SER n 
1 37  GLU n 
1 38  THR n 
1 39  LYS n 
1 40  HIS n 
1 41  ASP n 
1 42  THR n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  ILE n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASN n 
1 53  PRO n 
1 54  ALA n 
1 55  THR n 
1 56  ALA n 
1 57  LYS n 
1 58  GLU n 
1 59  ILE n 
1 60  ILE n 
1 61  ASN n 
1 62  VAL n 
1 63  GLY n 
1 64  HIS n 
1 65  SER n 
1 66  PHE n 
1 67  HIS n 
1 68  VAL n 
1 69  ASN n 
1 70  PHE n 
1 71  GLU n 
1 72  ASP n 
1 73  ASN n 
1 74  ASP n 
1 75  ASN n 
1 76  ARG n 
1 77  SER n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  PHE n 
1 85  SER n 
1 86  ASP n 
1 87  SER n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  PHE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 THR n 
1 101 ASN n 
1 102 GLU n 
1 103 HIS n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 GLY n 
1 112 VAL n 
1 113 LYS n 
1 114 TYR n 
1 115 SER n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 VAL n 
1 121 ALA n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 SER n 
1 126 ALA n 
1 127 LYS n 
1 128 TYR n 
1 129 SER n 
1 130 SER n 
1 131 LEU n 
1 132 ALA n 
1 133 GLU n 
1 134 ALA n 
1 135 ALA n 
1 136 SER n 
1 137 LYS n 
1 138 ALA n 
1 139 ASP n 
1 140 GLY n 
1 141 LEU n 
1 142 ALA n 
1 143 VAL n 
1 144 ILE n 
1 145 GLY n 
1 146 VAL n 
1 147 LEU n 
1 148 MET n 
1 149 LYS n 
1 150 VAL n 
1 151 GLY n 
1 152 GLU n 
1 153 ALA n 
1 154 ASN n 
1 155 PRO n 
1 156 LYS n 
1 157 LEU n 
1 158 GLN n 
1 159 LYS n 
1 160 VAL n 
1 161 LEU n 
1 162 ASP n 
1 163 ALA n 
1 164 LEU n 
1 165 GLN n 
1 166 ALA n 
1 167 ILE n 
1 168 LYS n 
1 169 THR n 
1 170 LYS n 
1 171 GLY n 
1 172 LYS n 
1 173 ARG n 
1 174 ALA n 
1 175 PRO n 
1 176 PHE n 
1 177 THR n 
1 178 ASN n 
1 179 PHE n 
1 180 ASP n 
1 181 PRO n 
1 182 SER n 
1 183 THR n 
1 184 LEU n 
1 185 LEU n 
1 186 PRO n 
1 187 SER n 
1 188 SER n 
1 189 LEU n 
1 190 ASP n 
1 191 PHE n 
1 192 TRP n 
1 193 THR n 
1 194 TYR n 
1 195 PRO n 
1 196 GLY n 
1 197 SER n 
1 198 LEU n 
1 199 THR n 
1 200 HIS n 
1 201 PRO n 
1 202 PRO n 
1 203 LEU n 
1 204 TYR n 
1 205 GLU n 
1 206 SER n 
1 207 VAL n 
1 208 THR n 
1 209 TRP n 
1 210 ILE n 
1 211 ILE n 
1 212 CYS n 
1 213 LYS n 
1 214 GLU n 
1 215 SER n 
1 216 ILE n 
1 217 SER n 
1 218 VAL n 
1 219 SER n 
1 220 SER n 
1 221 GLU n 
1 222 GLN n 
1 223 LEU n 
1 224 ALA n 
1 225 GLN n 
1 226 PHE n 
1 227 ARG n 
1 228 SER n 
1 229 LEU n 
1 230 LEU n 
1 231 SER n 
1 232 ASN n 
1 233 VAL n 
1 234 GLU n 
1 235 GLY n 
1 236 ASP n 
1 237 ASN n 
1 238 ALA n 
1 239 VAL n 
1 240 PRO n 
1 241 MET n 
1 242 GLN n 
1 243 HIS n 
1 244 ASN n 
1 245 ASN n 
1 246 ARG n 
1 247 PRO n 
1 248 THR n 
1 249 GLN n 
1 250 PRO n 
1 251 LEU n 
1 252 LYS n 
1 253 GLY n 
1 254 ARG n 
1 255 THR n 
1 256 VAL n 
1 257 ARG n 
1 258 ALA n 
1 259 SER n 
1 260 PHE 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                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
3UF non-polymer         . '4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' ? 'C8 H11 N O3 S2' 233.308 
ACT non-polymer         . 'ACETATE ION'                                    ? 'C2 H3 O2 -1'    59.044  
ALA 'L-peptide linking' y ALANINE                                          ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                         ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                       ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                  ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                         ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                        ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                  ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                          ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                        ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                            ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                       ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                          ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                           ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                       ? 'C5 H11 N O2 S'  149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                          ? 'C4 H10 O3'      106.120 
PHE 'L-peptide linking' y PHENYLALANINE                                    ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                          ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                           ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                        ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                       ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                         ? 'C9 H11 N O3'    181.189 
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   SER 2   2   ?   ?   ?   A . n 
A 1 3   PRO 3   3   ?   ?   ?   A . n 
A 1 4   ASP 4   4   ?   ?   ?   A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   ASP 8   8   8   ASP ASP A . n 
A 1 9   ASP 9   9   9   ASP ASP A . n 
A 1 10  LYS 10  10  10  LYS LYS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  SER 17  17  17  SER SER A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  TYR 20  20  20  TYR TYR A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  ASN 24  24  24  ASN ASN A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  ASN 27  27  27  ASN ASN A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  THR 38  38  38  THR THR A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  HIS 40  40  40  HIS HIS A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  THR 42  42  42  THR THR A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASN 52  52  52  ASN ASN A . n 
A 1 53  PRO 53  53  53  PRO PRO A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  HIS 67  67  67  HIS HIS A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  ASN 69  69  69  ASN ASN A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  ASN 73  73  73  ASN ASN A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  PHE 84  84  84  PHE PHE A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  SER 87  87  87  SER SER A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  PHE 91  91  91  PHE PHE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 THR 100 100 100 THR THR A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 HIS 103 103 103 HIS HIS A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 SER 125 125 125 SER SER A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 TYR 128 128 128 TYR TYR A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 ALA 138 138 138 ALA ALA A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 VAL 143 143 143 VAL VAL A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 VAL 146 146 146 VAL VAL A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 MET 148 148 148 MET MET A . n 
A 1 149 LYS 149 149 149 LYS LYS A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 GLU 152 152 152 GLU GLU A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 ASN 154 154 154 ASN ASN A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 GLN 158 158 158 GLN GLN A . n 
A 1 159 LYS 159 159 159 LYS LYS A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 GLN 165 165 165 GLN GLN A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 LYS 170 170 170 LYS LYS A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 LYS 172 172 172 LYS LYS A . n 
A 1 173 ARG 173 173 173 ARG ARG A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 PHE 176 176 176 PHE PHE A . n 
A 1 177 THR 177 177 177 THR THR A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 PHE 179 179 179 PHE PHE A . n 
A 1 180 ASP 180 180 180 ASP ASP A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 THR 183 183 183 THR THR A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 PRO 186 186 186 PRO PRO A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 SER 188 188 188 SER SER A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 ASP 190 190 190 ASP ASP A . n 
A 1 191 PHE 191 191 191 PHE PHE A . n 
A 1 192 TRP 192 192 192 TRP TRP A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 TYR 194 194 194 TYR TYR A . n 
A 1 195 PRO 195 195 195 PRO PRO A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 HIS 200 200 200 HIS HIS A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 TYR 204 204 204 TYR TYR A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 THR 208 208 208 THR THR A . n 
A 1 209 TRP 209 209 209 TRP TRP A . n 
A 1 210 ILE 210 210 210 ILE ILE A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 CYS 212 212 212 CYS CYS A . n 
A 1 213 LYS 213 213 213 LYS LYS A . n 
A 1 214 GLU 214 214 214 GLU GLU A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 SER 217 217 217 SER SER A . n 
A 1 218 VAL 218 218 218 VAL VAL A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 GLN 222 222 222 GLN GLN A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 GLN 225 225 225 GLN GLN A . n 
A 1 226 PHE 226 226 226 PHE PHE A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 SER 228 228 228 SER SER A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 ASN 232 232 232 ASN ASN A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 GLU 234 234 234 GLU GLU A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 ASN 237 237 237 ASN ASN A . n 
A 1 238 ALA 238 238 238 ALA ALA A . n 
A 1 239 VAL 239 239 239 VAL VAL A . n 
A 1 240 PRO 240 240 240 PRO PRO A . n 
A 1 241 MET 241 241 241 MET MET A . n 
A 1 242 GLN 242 242 242 GLN GLN A . n 
A 1 243 HIS 243 243 243 HIS HIS A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 ARG 246 246 246 ARG ARG A . n 
A 1 247 PRO 247 247 247 PRO PRO A . n 
A 1 248 THR 248 248 248 THR THR A . n 
A 1 249 GLN 249 249 249 GLN GLN A . n 
A 1 250 PRO 250 250 250 PRO PRO A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 LYS 252 252 252 LYS LYS A . n 
A 1 253 GLY 253 253 253 GLY GLY A . n 
A 1 254 ARG 254 254 254 ARG ARG A . n 
A 1 255 THR 255 255 255 THR THR A . n 
A 1 256 VAL 256 256 256 VAL VAL A . n 
A 1 257 ARG 257 257 257 ARG ARG A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 SER 259 259 259 SER SER A . n 
A 1 260 PHE 260 260 260 PHE PHE A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   PRO 3   3   ?   ?   ?   B . n 
B 1 4   ASP 4   4   4   ASP ASP B . n 
B 1 5   TRP 5   5   5   TRP TRP B . n 
B 1 6   GLY 6   6   6   GLY GLY B . n 
B 1 7   TYR 7   7   7   TYR TYR B . n 
B 1 8   ASP 8   8   8   ASP ASP B . n 
B 1 9   ASP 9   9   9   ASP ASP B . n 
B 1 10  LYS 10  10  10  LYS LYS B . n 
B 1 11  ASN 11  11  11  ASN ASN B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  TRP 16  16  16  TRP TRP B . n 
B 1 17  SER 17  17  17  SER SER B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  LEU 19  19  19  LEU LEU B . n 
B 1 20  TYR 20  20  20  TYR TYR B . n 
B 1 21  PRO 21  21  21  PRO PRO B . n 
B 1 22  ILE 22  22  22  ILE ILE B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  ASN 24  24  24  ASN ASN B . n 
B 1 25  GLY 25  25  25  GLY GLY B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  ASN 27  27  27  ASN ASN B . n 
B 1 28  GLN 28  28  28  GLN GLN B . n 
B 1 29  SER 29  29  29  SER SER B . n 
B 1 30  PRO 30  30  30  PRO PRO B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  ASP 32  32  32  ASP ASP B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  LYS 34  34  34  LYS LYS B . n 
B 1 35  THR 35  35  35  THR THR B . n 
B 1 36  SER 36  36  36  SER SER B . n 
B 1 37  GLU 37  37  37  GLU GLU B . n 
B 1 38  THR 38  38  38  THR THR B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  HIS 40  40  40  HIS HIS B . n 
B 1 41  ASP 41  41  41  ASP ASP B . n 
B 1 42  THR 42  42  42  THR THR B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  LEU 44  44  44  LEU LEU B . n 
B 1 45  LYS 45  45  45  LYS LYS B . n 
B 1 46  PRO 46  46  46  PRO PRO B . n 
B 1 47  ILE 47  47  47  ILE ILE B . n 
B 1 48  SER 48  48  48  SER SER B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  SER 50  50  50  SER SER B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASN 52  52  52  ASN ASN B . n 
B 1 53  PRO 53  53  53  PRO PRO B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  THR 55  55  55  THR THR B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  LYS 57  57  57  LYS LYS B . n 
B 1 58  GLU 58  58  58  GLU GLU B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  ILE 60  60  60  ILE ILE B . n 
B 1 61  ASN 61  61  61  ASN ASN B . n 
B 1 62  VAL 62  62  62  VAL VAL B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  HIS 67  67  67  HIS HIS B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  ASN 69  69  69  ASN ASN B . n 
B 1 70  PHE 70  70  70  PHE PHE B . n 
B 1 71  GLU 71  71  71  GLU GLU B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  ASN 73  73  73  ASN ASN B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  ASN 75  75  75  ASN ASN B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  SER 77  77  77  SER SER B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  LEU 79  79  79  LEU LEU B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  PRO 83  83  83  PRO PRO B . n 
B 1 84  PHE 84  84  84  PHE PHE B . n 
B 1 85  SER 85  85  85  SER SER B . n 
B 1 86  ASP 86  86  86  ASP ASP B . n 
B 1 87  SER 87  87  87  SER SER B . n 
B 1 88  TYR 88  88  88  TYR TYR B . n 
B 1 89  ARG 89  89  89  ARG ARG B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  PHE 91  91  91  PHE PHE B . n 
B 1 92  GLN 92  92  92  GLN GLN B . n 
B 1 93  PHE 93  93  93  PHE PHE B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  HIS 96  96  96  HIS HIS B . n 
B 1 97  TRP 97  97  97  TRP TRP B . n 
B 1 98  GLY 98  98  98  GLY GLY B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 THR 100 100 100 THR THR B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 GLU 102 102 102 GLU GLU B . n 
B 1 103 HIS 103 103 103 HIS HIS B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 GLU 106 106 106 GLU GLU B . n 
B 1 107 HIS 107 107 107 HIS HIS B . n 
B 1 108 THR 108 108 108 THR THR B . n 
B 1 109 VAL 109 109 109 VAL VAL B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 GLY 111 111 111 GLY GLY B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 GLU 117 117 117 GLU GLU B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 HIS 122 122 122 HIS HIS B . n 
B 1 123 TRP 123 123 123 TRP TRP B . n 
B 1 124 ASN 124 124 124 ASN ASN B . n 
B 1 125 SER 125 125 125 SER SER B . n 
B 1 126 ALA 126 126 126 ALA ALA B . n 
B 1 127 LYS 127 127 127 LYS LYS B . n 
B 1 128 TYR 128 128 128 TYR TYR B . n 
B 1 129 SER 129 129 129 SER SER B . n 
B 1 130 SER 130 130 130 SER SER B . n 
B 1 131 LEU 131 131 131 LEU LEU B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ALA 135 135 135 ALA ALA B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 ALA 138 138 138 ALA ALA B . n 
B 1 139 ASP 139 139 139 ASP ASP B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ALA 142 142 142 ALA ALA B . n 
B 1 143 VAL 143 143 143 VAL VAL B . n 
B 1 144 ILE 144 144 144 ILE ILE B . n 
B 1 145 GLY 145 145 145 GLY GLY B . n 
B 1 146 VAL 146 146 146 VAL VAL B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 MET 148 148 148 MET MET B . n 
B 1 149 LYS 149 149 149 LYS LYS B . n 
B 1 150 VAL 150 150 150 VAL VAL B . n 
B 1 151 GLY 151 151 151 GLY GLY B . n 
B 1 152 GLU 152 152 152 GLU GLU B . n 
B 1 153 ALA 153 153 153 ALA ALA B . n 
B 1 154 ASN 154 154 154 ASN ASN B . n 
B 1 155 PRO 155 155 155 PRO PRO B . n 
B 1 156 LYS 156 156 156 LYS LYS B . n 
B 1 157 LEU 157 157 157 LEU LEU B . n 
B 1 158 GLN 158 158 158 GLN GLN B . n 
B 1 159 LYS 159 159 159 LYS LYS B . n 
B 1 160 VAL 160 160 160 VAL VAL B . n 
B 1 161 LEU 161 161 161 LEU LEU B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 ALA 163 163 163 ALA ALA B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 GLN 165 165 165 GLN GLN B . n 
B 1 166 ALA 166 166 166 ALA ALA B . n 
B 1 167 ILE 167 167 167 ILE ILE B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 LYS 170 170 170 LYS LYS B . n 
B 1 171 GLY 171 171 171 GLY GLY B . n 
B 1 172 LYS 172 172 172 LYS LYS B . n 
B 1 173 ARG 173 173 173 ARG ARG B . n 
B 1 174 ALA 174 174 174 ALA ALA B . n 
B 1 175 PRO 175 175 175 PRO PRO B . n 
B 1 176 PHE 176 176 176 PHE PHE B . n 
B 1 177 THR 177 177 177 THR THR B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 PHE 179 179 179 PHE PHE B . n 
B 1 180 ASP 180 180 180 ASP ASP B . n 
B 1 181 PRO 181 181 181 PRO PRO B . n 
B 1 182 SER 182 182 182 SER SER B . n 
B 1 183 THR 183 183 183 THR THR B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 LEU 185 185 185 LEU LEU B . n 
B 1 186 PRO 186 186 186 PRO PRO B . n 
B 1 187 SER 187 187 187 SER SER B . n 
B 1 188 SER 188 188 188 SER SER B . n 
B 1 189 LEU 189 189 189 LEU LEU B . n 
B 1 190 ASP 190 190 190 ASP ASP B . n 
B 1 191 PHE 191 191 191 PHE PHE B . n 
B 1 192 TRP 192 192 192 TRP TRP B . n 
B 1 193 THR 193 193 193 THR THR B . n 
B 1 194 TYR 194 194 194 TYR TYR B . n 
B 1 195 PRO 195 195 195 PRO PRO B . n 
B 1 196 GLY 196 196 196 GLY GLY B . n 
B 1 197 SER 197 197 197 SER SER B . n 
B 1 198 LEU 198 198 198 LEU LEU B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 HIS 200 200 200 HIS HIS B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 PRO 202 202 202 PRO PRO B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 TYR 204 204 204 TYR TYR B . n 
B 1 205 GLU 205 205 205 GLU GLU B . n 
B 1 206 SER 206 206 206 SER SER B . n 
B 1 207 VAL 207 207 207 VAL VAL B . n 
B 1 208 THR 208 208 208 THR THR B . n 
B 1 209 TRP 209 209 209 TRP TRP B . n 
B 1 210 ILE 210 210 210 ILE ILE B . n 
B 1 211 ILE 211 211 211 ILE ILE B . n 
B 1 212 CYS 212 212 212 CYS CYS B . n 
B 1 213 LYS 213 213 213 LYS LYS B . n 
B 1 214 GLU 214 214 214 GLU GLU B . n 
B 1 215 SER 215 215 215 SER SER B . n 
B 1 216 ILE 216 216 216 ILE ILE B . n 
B 1 217 SER 217 217 217 SER SER B . n 
B 1 218 VAL 218 218 218 VAL VAL B . n 
B 1 219 SER 219 219 219 SER SER B . n 
B 1 220 SER 220 220 220 SER SER B . n 
B 1 221 GLU 221 221 221 GLU GLU B . n 
B 1 222 GLN 222 222 222 GLN GLN B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 GLN 225 225 225 GLN GLN B . n 
B 1 226 PHE 226 226 226 PHE PHE B . n 
B 1 227 ARG 227 227 227 ARG ARG B . n 
B 1 228 SER 228 228 228 SER SER B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 SER 231 231 231 SER SER B . n 
B 1 232 ASN 232 232 232 ASN ASN B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 GLU 234 234 234 GLU GLU B . n 
B 1 235 GLY 235 235 235 GLY GLY B . n 
B 1 236 ASP 236 236 236 ASP ASP B . n 
B 1 237 ASN 237 237 237 ASN ASN B . n 
B 1 238 ALA 238 238 238 ALA ALA B . n 
B 1 239 VAL 239 239 239 VAL VAL B . n 
B 1 240 PRO 240 240 240 PRO PRO B . n 
B 1 241 MET 241 241 241 MET MET B . n 
B 1 242 GLN 242 242 242 GLN GLN B . n 
B 1 243 HIS 243 243 243 HIS HIS B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
B 1 246 ARG 246 246 246 ARG ARG B . n 
B 1 247 PRO 247 247 247 PRO PRO B . n 
B 1 248 THR 248 248 248 THR THR B . n 
B 1 249 GLN 249 249 249 GLN GLN B . n 
B 1 250 PRO 250 250 250 PRO PRO B . n 
B 1 251 LEU 251 251 251 LEU LEU B . n 
B 1 252 LYS 252 252 252 LYS LYS B . n 
B 1 253 GLY 253 253 253 GLY GLY B . n 
B 1 254 ARG 254 254 254 ARG ARG B . n 
B 1 255 THR 255 255 255 THR THR B . n 
B 1 256 VAL 256 256 256 VAL VAL B . n 
B 1 257 ARG 257 257 257 ARG ARG B . n 
B 1 258 ALA 258 258 258 ALA ALA B . n 
B 1 259 SER 259 259 259 SER SER B . n 
B 1 260 PHE 260 260 260 PHE PHE B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ZN  1   301 1   ZN  ZN  A . 
D 3 3UF 1   302 1   3UF V13 A . 
E 4 ACT 1   303 2   ACT ACT A . 
F 2 ZN  1   301 2   ZN  ZN  B . 
G 3 3UF 1   302 2   3UF V13 B . 
H 5 PEG 1   303 1   PEG PEG B . 
I 6 HOH 1   401 84  HOH HOH A . 
I 6 HOH 2   402 318 HOH HOH A . 
I 6 HOH 3   403 260 HOH HOH A . 
I 6 HOH 4   404 290 HOH HOH A . 
I 6 HOH 5   405 248 HOH HOH A . 
I 6 HOH 6   406 42  HOH HOH A . 
I 6 HOH 7   407 132 HOH HOH A . 
I 6 HOH 8   408 99  HOH HOH A . 
I 6 HOH 9   409 76  HOH HOH A . 
I 6 HOH 10  410 161 HOH HOH A . 
I 6 HOH 11  411 209 HOH HOH A . 
I 6 HOH 12  412 247 HOH HOH A . 
I 6 HOH 13  413 267 HOH HOH A . 
I 6 HOH 14  414 20  HOH HOH A . 
I 6 HOH 15  415 189 HOH HOH A . 
I 6 HOH 16  416 299 HOH HOH A . 
I 6 HOH 17  417 34  HOH HOH A . 
I 6 HOH 18  418 4   HOH HOH A . 
I 6 HOH 19  419 195 HOH HOH A . 
I 6 HOH 20  420 155 HOH HOH A . 
I 6 HOH 21  421 272 HOH HOH A . 
I 6 HOH 22  422 85  HOH HOH A . 
I 6 HOH 23  423 47  HOH HOH A . 
I 6 HOH 24  424 192 HOH HOH A . 
I 6 HOH 25  425 107 HOH HOH A . 
I 6 HOH 26  426 40  HOH HOH A . 
I 6 HOH 27  427 353 HOH HOH A . 
I 6 HOH 28  428 126 HOH HOH A . 
I 6 HOH 29  429 194 HOH HOH A . 
I 6 HOH 30  430 265 HOH HOH A . 
I 6 HOH 31  431 255 HOH HOH A . 
I 6 HOH 32  432 273 HOH HOH A . 
I 6 HOH 33  433 154 HOH HOH A . 
I 6 HOH 34  434 29  HOH HOH A . 
I 6 HOH 35  435 228 HOH HOH A . 
I 6 HOH 36  436 67  HOH HOH A . 
I 6 HOH 37  437 338 HOH HOH A . 
I 6 HOH 38  438 58  HOH HOH A . 
I 6 HOH 39  439 354 HOH HOH A . 
I 6 HOH 40  440 134 HOH HOH A . 
I 6 HOH 41  441 312 HOH HOH A . 
I 6 HOH 42  442 294 HOH HOH A . 
I 6 HOH 43  443 205 HOH HOH A . 
I 6 HOH 44  444 61  HOH HOH A . 
I 6 HOH 45  445 125 HOH HOH A . 
I 6 HOH 46  446 295 HOH HOH A . 
I 6 HOH 47  447 105 HOH HOH A . 
I 6 HOH 48  448 166 HOH HOH A . 
I 6 HOH 49  449 245 HOH HOH A . 
I 6 HOH 50  450 106 HOH HOH A . 
I 6 HOH 51  451 256 HOH HOH A . 
I 6 HOH 52  452 242 HOH HOH A . 
I 6 HOH 53  453 331 HOH HOH A . 
I 6 HOH 54  454 363 HOH HOH A . 
I 6 HOH 55  455 350 HOH HOH A . 
I 6 HOH 56  456 233 HOH HOH A . 
I 6 HOH 57  457 2   HOH HOH A . 
I 6 HOH 58  458 5   HOH HOH A . 
I 6 HOH 59  459 6   HOH HOH A . 
I 6 HOH 60  460 19  HOH HOH A . 
I 6 HOH 61  461 23  HOH HOH A . 
I 6 HOH 62  462 24  HOH HOH A . 
I 6 HOH 63  463 25  HOH HOH A . 
I 6 HOH 64  464 26  HOH HOH A . 
I 6 HOH 65  465 27  HOH HOH A . 
I 6 HOH 66  466 37  HOH HOH A . 
I 6 HOH 67  467 41  HOH HOH A . 
I 6 HOH 68  468 48  HOH HOH A . 
I 6 HOH 69  469 51  HOH HOH A . 
I 6 HOH 70  470 53  HOH HOH A . 
I 6 HOH 71  471 55  HOH HOH A . 
I 6 HOH 72  472 56  HOH HOH A . 
I 6 HOH 73  473 64  HOH HOH A . 
I 6 HOH 74  474 66  HOH HOH A . 
I 6 HOH 75  475 68  HOH HOH A . 
I 6 HOH 76  476 70  HOH HOH A . 
I 6 HOH 77  477 71  HOH HOH A . 
I 6 HOH 78  478 72  HOH HOH A . 
I 6 HOH 79  479 74  HOH HOH A . 
I 6 HOH 80  480 79  HOH HOH A . 
I 6 HOH 81  481 80  HOH HOH A . 
I 6 HOH 82  482 82  HOH HOH A . 
I 6 HOH 83  483 88  HOH HOH A . 
I 6 HOH 84  484 90  HOH HOH A . 
I 6 HOH 85  485 91  HOH HOH A . 
I 6 HOH 86  486 94  HOH HOH A . 
I 6 HOH 87  487 95  HOH HOH A . 
I 6 HOH 88  488 96  HOH HOH A . 
I 6 HOH 89  489 98  HOH HOH A . 
I 6 HOH 90  490 100 HOH HOH A . 
I 6 HOH 91  491 101 HOH HOH A . 
I 6 HOH 92  492 104 HOH HOH A . 
I 6 HOH 93  493 108 HOH HOH A . 
I 6 HOH 94  494 109 HOH HOH A . 
I 6 HOH 95  495 113 HOH HOH A . 
I 6 HOH 96  496 114 HOH HOH A . 
I 6 HOH 97  497 118 HOH HOH A . 
I 6 HOH 98  498 124 HOH HOH A . 
I 6 HOH 99  499 129 HOH HOH A . 
I 6 HOH 100 500 136 HOH HOH A . 
I 6 HOH 101 501 138 HOH HOH A . 
I 6 HOH 102 502 139 HOH HOH A . 
I 6 HOH 103 503 141 HOH HOH A . 
I 6 HOH 104 504 143 HOH HOH A . 
I 6 HOH 105 505 150 HOH HOH A . 
I 6 HOH 106 506 152 HOH HOH A . 
I 6 HOH 107 507 158 HOH HOH A . 
I 6 HOH 108 508 159 HOH HOH A . 
I 6 HOH 109 509 162 HOH HOH A . 
I 6 HOH 110 510 163 HOH HOH A . 
I 6 HOH 111 511 168 HOH HOH A . 
I 6 HOH 112 512 169 HOH HOH A . 
I 6 HOH 113 513 174 HOH HOH A . 
I 6 HOH 114 514 176 HOH HOH A . 
I 6 HOH 115 515 177 HOH HOH A . 
I 6 HOH 116 516 179 HOH HOH A . 
I 6 HOH 117 517 186 HOH HOH A . 
I 6 HOH 118 518 188 HOH HOH A . 
I 6 HOH 119 519 191 HOH HOH A . 
I 6 HOH 120 520 196 HOH HOH A . 
I 6 HOH 121 521 197 HOH HOH A . 
I 6 HOH 122 522 199 HOH HOH A . 
I 6 HOH 123 523 200 HOH HOH A . 
I 6 HOH 124 524 206 HOH HOH A . 
I 6 HOH 125 525 207 HOH HOH A . 
I 6 HOH 126 526 211 HOH HOH A . 
I 6 HOH 127 527 213 HOH HOH A . 
I 6 HOH 128 528 214 HOH HOH A . 
I 6 HOH 129 529 216 HOH HOH A . 
I 6 HOH 130 530 217 HOH HOH A . 
I 6 HOH 131 531 218 HOH HOH A . 
I 6 HOH 132 532 223 HOH HOH A . 
I 6 HOH 133 533 224 HOH HOH A . 
I 6 HOH 134 534 232 HOH HOH A . 
I 6 HOH 135 535 235 HOH HOH A . 
I 6 HOH 136 536 238 HOH HOH A . 
I 6 HOH 137 537 241 HOH HOH A . 
I 6 HOH 138 538 243 HOH HOH A . 
I 6 HOH 139 539 244 HOH HOH A . 
I 6 HOH 140 540 249 HOH HOH A . 
I 6 HOH 141 541 253 HOH HOH A . 
I 6 HOH 142 542 261 HOH HOH A . 
I 6 HOH 143 543 263 HOH HOH A . 
I 6 HOH 144 544 274 HOH HOH A . 
I 6 HOH 145 545 275 HOH HOH A . 
I 6 HOH 146 546 276 HOH HOH A . 
I 6 HOH 147 547 280 HOH HOH A . 
I 6 HOH 148 548 284 HOH HOH A . 
I 6 HOH 149 549 285 HOH HOH A . 
I 6 HOH 150 550 287 HOH HOH A . 
I 6 HOH 151 551 288 HOH HOH A . 
I 6 HOH 152 552 296 HOH HOH A . 
I 6 HOH 153 553 297 HOH HOH A . 
I 6 HOH 154 554 298 HOH HOH A . 
I 6 HOH 155 555 300 HOH HOH A . 
I 6 HOH 156 556 301 HOH HOH A . 
I 6 HOH 157 557 302 HOH HOH A . 
I 6 HOH 158 558 303 HOH HOH A . 
I 6 HOH 159 559 311 HOH HOH A . 
I 6 HOH 160 560 313 HOH HOH A . 
I 6 HOH 161 561 314 HOH HOH A . 
I 6 HOH 162 562 315 HOH HOH A . 
I 6 HOH 163 563 316 HOH HOH A . 
I 6 HOH 164 564 317 HOH HOH A . 
I 6 HOH 165 565 319 HOH HOH A . 
I 6 HOH 166 566 320 HOH HOH A . 
I 6 HOH 167 567 322 HOH HOH A . 
I 6 HOH 168 568 323 HOH HOH A . 
I 6 HOH 169 569 355 HOH HOH A . 
I 6 HOH 170 570 356 HOH HOH A . 
I 6 HOH 171 571 361 HOH HOH A . 
I 6 HOH 172 572 362 HOH HOH A . 
J 6 HOH 1   401 180 HOH HOH B . 
J 6 HOH 2   402 282 HOH HOH B . 
J 6 HOH 3   403 246 HOH HOH B . 
J 6 HOH 4   404 93  HOH HOH B . 
J 6 HOH 5   405 269 HOH HOH B . 
J 6 HOH 6   406 184 HOH HOH B . 
J 6 HOH 7   407 229 HOH HOH B . 
J 6 HOH 8   408 210 HOH HOH B . 
J 6 HOH 9   409 30  HOH HOH B . 
J 6 HOH 10  410 54  HOH HOH B . 
J 6 HOH 11  411 73  HOH HOH B . 
J 6 HOH 12  412 336 HOH HOH B . 
J 6 HOH 13  413 289 HOH HOH B . 
J 6 HOH 14  414 28  HOH HOH B . 
J 6 HOH 15  415 309 HOH HOH B . 
J 6 HOH 16  416 222 HOH HOH B . 
J 6 HOH 17  417 360 HOH HOH B . 
J 6 HOH 18  418 359 HOH HOH B . 
J 6 HOH 19  419 266 HOH HOH B . 
J 6 HOH 20  420 219 HOH HOH B . 
J 6 HOH 21  421 173 HOH HOH B . 
J 6 HOH 22  422 190 HOH HOH B . 
J 6 HOH 23  423 38  HOH HOH B . 
J 6 HOH 24  424 36  HOH HOH B . 
J 6 HOH 25  425 351 HOH HOH B . 
J 6 HOH 26  426 208 HOH HOH B . 
J 6 HOH 27  427 160 HOH HOH B . 
J 6 HOH 28  428 349 HOH HOH B . 
J 6 HOH 29  429 281 HOH HOH B . 
J 6 HOH 30  430 123 HOH HOH B . 
J 6 HOH 31  431 262 HOH HOH B . 
J 6 HOH 32  432 202 HOH HOH B . 
J 6 HOH 33  433 187 HOH HOH B . 
J 6 HOH 34  434 92  HOH HOH B . 
J 6 HOH 35  435 175 HOH HOH B . 
J 6 HOH 36  436 310 HOH HOH B . 
J 6 HOH 37  437 9   HOH HOH B . 
J 6 HOH 38  438 307 HOH HOH B . 
J 6 HOH 39  439 286 HOH HOH B . 
J 6 HOH 40  440 185 HOH HOH B . 
J 6 HOH 41  441 324 HOH HOH B . 
J 6 HOH 42  442 358 HOH HOH B . 
J 6 HOH 43  443 181 HOH HOH B . 
J 6 HOH 44  444 259 HOH HOH B . 
J 6 HOH 45  445 137 HOH HOH B . 
J 6 HOH 46  446 226 HOH HOH B . 
J 6 HOH 47  447 117 HOH HOH B . 
J 6 HOH 48  448 156 HOH HOH B . 
J 6 HOH 49  449 366 HOH HOH B . 
J 6 HOH 50  450 225 HOH HOH B . 
J 6 HOH 51  451 183 HOH HOH B . 
J 6 HOH 52  452 264 HOH HOH B . 
J 6 HOH 53  453 348 HOH HOH B . 
J 6 HOH 54  454 334 HOH HOH B . 
J 6 HOH 55  455 172 HOH HOH B . 
J 6 HOH 56  456 352 HOH HOH B . 
J 6 HOH 57  457 291 HOH HOH B . 
J 6 HOH 58  458 103 HOH HOH B . 
J 6 HOH 59  459 279 HOH HOH B . 
J 6 HOH 60  460 369 HOH HOH B . 
J 6 HOH 61  461 270 HOH HOH B . 
J 6 HOH 62  462 321 HOH HOH B . 
J 6 HOH 63  463 221 HOH HOH B . 
J 6 HOH 64  464 254 HOH HOH B . 
J 6 HOH 65  465 271 HOH HOH B . 
J 6 HOH 66  466 1   HOH HOH B . 
J 6 HOH 67  467 3   HOH HOH B . 
J 6 HOH 68  468 7   HOH HOH B . 
J 6 HOH 69  469 8   HOH HOH B . 
J 6 HOH 70  470 10  HOH HOH B . 
J 6 HOH 71  471 11  HOH HOH B . 
J 6 HOH 72  472 12  HOH HOH B . 
J 6 HOH 73  473 13  HOH HOH B . 
J 6 HOH 74  474 14  HOH HOH B . 
J 6 HOH 75  475 15  HOH HOH B . 
J 6 HOH 76  476 16  HOH HOH B . 
J 6 HOH 77  477 17  HOH HOH B . 
J 6 HOH 78  478 18  HOH HOH B . 
J 6 HOH 79  479 21  HOH HOH B . 
J 6 HOH 80  480 22  HOH HOH B . 
J 6 HOH 81  481 31  HOH HOH B . 
J 6 HOH 82  482 32  HOH HOH B . 
J 6 HOH 83  483 33  HOH HOH B . 
J 6 HOH 84  484 35  HOH HOH B . 
J 6 HOH 85  485 39  HOH HOH B . 
J 6 HOH 86  486 43  HOH HOH B . 
J 6 HOH 87  487 44  HOH HOH B . 
J 6 HOH 88  488 45  HOH HOH B . 
J 6 HOH 89  489 46  HOH HOH B . 
J 6 HOH 90  490 49  HOH HOH B . 
J 6 HOH 91  491 50  HOH HOH B . 
J 6 HOH 92  492 52  HOH HOH B . 
J 6 HOH 93  493 57  HOH HOH B . 
J 6 HOH 94  494 59  HOH HOH B . 
J 6 HOH 95  495 60  HOH HOH B . 
J 6 HOH 96  496 62  HOH HOH B . 
J 6 HOH 97  497 63  HOH HOH B . 
J 6 HOH 98  498 65  HOH HOH B . 
J 6 HOH 99  499 69  HOH HOH B . 
J 6 HOH 100 500 75  HOH HOH B . 
J 6 HOH 101 501 77  HOH HOH B . 
J 6 HOH 102 502 78  HOH HOH B . 
J 6 HOH 103 503 81  HOH HOH B . 
J 6 HOH 104 504 83  HOH HOH B . 
J 6 HOH 105 505 86  HOH HOH B . 
J 6 HOH 106 506 87  HOH HOH B . 
J 6 HOH 107 507 89  HOH HOH B . 
J 6 HOH 108 508 97  HOH HOH B . 
J 6 HOH 109 509 102 HOH HOH B . 
J 6 HOH 110 510 110 HOH HOH B . 
J 6 HOH 111 511 111 HOH HOH B . 
J 6 HOH 112 512 112 HOH HOH B . 
J 6 HOH 113 513 115 HOH HOH B . 
J 6 HOH 114 514 116 HOH HOH B . 
J 6 HOH 115 515 119 HOH HOH B . 
J 6 HOH 116 516 120 HOH HOH B . 
J 6 HOH 117 517 121 HOH HOH B . 
J 6 HOH 118 518 122 HOH HOH B . 
J 6 HOH 119 519 127 HOH HOH B . 
J 6 HOH 120 520 128 HOH HOH B . 
J 6 HOH 121 521 130 HOH HOH B . 
J 6 HOH 122 522 131 HOH HOH B . 
J 6 HOH 123 523 133 HOH HOH B . 
J 6 HOH 124 524 135 HOH HOH B . 
J 6 HOH 125 525 140 HOH HOH B . 
J 6 HOH 126 526 142 HOH HOH B . 
J 6 HOH 127 527 144 HOH HOH B . 
J 6 HOH 128 528 145 HOH HOH B . 
J 6 HOH 129 529 146 HOH HOH B . 
J 6 HOH 130 530 147 HOH HOH B . 
J 6 HOH 131 531 148 HOH HOH B . 
J 6 HOH 132 532 149 HOH HOH B . 
J 6 HOH 133 533 151 HOH HOH B . 
J 6 HOH 134 534 153 HOH HOH B . 
J 6 HOH 135 535 157 HOH HOH B . 
J 6 HOH 136 536 164 HOH HOH B . 
J 6 HOH 137 537 165 HOH HOH B . 
J 6 HOH 138 538 167 HOH HOH B . 
J 6 HOH 139 539 170 HOH HOH B . 
J 6 HOH 140 540 171 HOH HOH B . 
J 6 HOH 141 541 178 HOH HOH B . 
J 6 HOH 142 542 182 HOH HOH B . 
J 6 HOH 143 543 193 HOH HOH B . 
J 6 HOH 144 544 198 HOH HOH B . 
J 6 HOH 145 545 201 HOH HOH B . 
J 6 HOH 146 546 203 HOH HOH B . 
J 6 HOH 147 547 204 HOH HOH B . 
J 6 HOH 148 548 212 HOH HOH B . 
J 6 HOH 149 549 215 HOH HOH B . 
J 6 HOH 150 550 220 HOH HOH B . 
J 6 HOH 151 551 227 HOH HOH B . 
J 6 HOH 152 552 230 HOH HOH B . 
J 6 HOH 153 553 231 HOH HOH B . 
J 6 HOH 154 554 234 HOH HOH B . 
J 6 HOH 155 555 236 HOH HOH B . 
J 6 HOH 156 556 237 HOH HOH B . 
J 6 HOH 157 557 239 HOH HOH B . 
J 6 HOH 158 558 240 HOH HOH B . 
J 6 HOH 159 559 250 HOH HOH B . 
J 6 HOH 160 560 251 HOH HOH B . 
J 6 HOH 161 561 252 HOH HOH B . 
J 6 HOH 162 562 257 HOH HOH B . 
J 6 HOH 163 563 258 HOH HOH B . 
J 6 HOH 164 564 268 HOH HOH B . 
J 6 HOH 165 565 277 HOH HOH B . 
J 6 HOH 166 566 278 HOH HOH B . 
J 6 HOH 167 567 283 HOH HOH B . 
J 6 HOH 168 568 292 HOH HOH B . 
J 6 HOH 169 569 293 HOH HOH B . 
J 6 HOH 170 570 304 HOH HOH B . 
J 6 HOH 171 571 305 HOH HOH B . 
J 6 HOH 172 572 306 HOH HOH B . 
J 6 HOH 173 573 308 HOH HOH B . 
J 6 HOH 174 574 325 HOH HOH B . 
J 6 HOH 175 575 326 HOH HOH B . 
J 6 HOH 176 576 327 HOH HOH B . 
J 6 HOH 177 577 328 HOH HOH B . 
J 6 HOH 178 578 329 HOH HOH B . 
J 6 HOH 179 579 330 HOH HOH B . 
J 6 HOH 180 580 332 HOH HOH B . 
J 6 HOH 181 581 333 HOH HOH B . 
J 6 HOH 182 582 335 HOH HOH B . 
J 6 HOH 183 583 337 HOH HOH B . 
J 6 HOH 184 584 339 HOH HOH B . 
J 6 HOH 185 585 340 HOH HOH B . 
J 6 HOH 186 586 341 HOH HOH B . 
J 6 HOH 187 587 342 HOH HOH B . 
J 6 HOH 188 588 343 HOH HOH B . 
J 6 HOH 189 589 344 HOH HOH B . 
J 6 HOH 190 590 345 HOH HOH B . 
J 6 HOH 191 591 346 HOH HOH B . 
J 6 HOH 192 592 347 HOH HOH B . 
J 6 HOH 193 593 357 HOH HOH B . 
J 6 HOH 194 594 364 HOH HOH B . 
J 6 HOH 195 595 365 HOH HOH B . 
J 6 HOH 196 596 367 HOH HOH B . 
J 6 HOH 197 597 368 HOH HOH B . 
J 6 HOH 198 598 370 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 14 ? CD  ? A GLU 14 CD  
2  1 Y 1 A GLU 14 ? OE1 ? A GLU 14 OE1 
3  1 Y 1 A GLU 14 ? OE2 ? A GLU 14 OE2 
4  1 Y 1 A LYS 39 ? CG  ? A LYS 39 CG  
5  1 Y 1 A LYS 39 ? CD  ? A LYS 39 CD  
6  1 Y 1 A LYS 39 ? CE  ? A LYS 39 CE  
7  1 Y 1 A LYS 39 ? NZ  ? A LYS 39 NZ  
8  1 Y 1 A THR 42 ? CB  ? A THR 42 CB  
9  1 Y 1 A THR 42 ? OG1 ? A THR 42 OG1 
10 1 Y 1 A THR 42 ? CG2 ? A THR 42 CG2 
11 1 Y 1 A LYS 45 ? CE  ? A LYS 45 CE  
12 1 Y 1 A LYS 45 ? NZ  ? A LYS 45 NZ  
13 1 Y 1 A LYS 57 ? NZ  ? A LYS 57 NZ  
14 1 Y 1 B LYS 34 ? CD  ? B LYS 34 CD  
15 1 Y 1 B LYS 34 ? CE  ? B LYS 34 CE  
16 1 Y 1 B LYS 34 ? NZ  ? B LYS 34 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        1 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .        3 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.6.0117 4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        5 
# 
_cell.entry_id           4WUP 
_cell.length_a           63.332 
_cell.length_b           71.284 
_cell.length_c           120.719 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         4WUP 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   4WUP 
_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            2.37 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         47.6 
_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              8.5 
_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: 0.1M TrisHCl (pH 8.5), 
0.2M ammonium acetate and 24% of PEG4000
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-01-08 
# 
_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            23.016 
_reflns.entry_id                         4WUP 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.750 
_reflns.d_resolution_low                 71.284 
_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                       55864 
_reflns.number_obs                       55864 
_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             100.000 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  13.100 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.085 
_reflns.pdbx_netI_over_av_sigmaI         4.004 
_reflns.pdbx_netI_over_sigmaI            16.600 
_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                  0.091 
_reflns.pdbx_Rpim_I_all                  0.025 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         733336 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
1.75 1.84  ? 2.1 106147 ? ? 8022 ? 100.00 ? ? ? 0.370 0.345 ? ? ? ? ? ? ? ? 13.20 0.345 ? ? 6.30  0.37 0.10 ? 1  1 ? ? 
1.84 1.96  ? 3.1 100562 ? ? 7593 ? 99.90  ? ? ? 0.243 0.228 ? ? ? ? ? ? ? ? 13.20 0.228 ? ? 8.70  0.24 0.07 ? 2  ? ? ? 
1.96 2.09  ? 4.4 94283  ? ? 7192 ? 100.00 ? ? ? 0.168 0.157 ? ? ? ? ? ? ? ? 13.10 0.157 ? ? 11.70 0.17 0.05 ? 3  ? ? ? 
2.09 2.26  ? 5.3 88430  ? ? 6712 ? 100.00 ? ? ? 0.129 0.120 ? ? ? ? ? ? ? ? 13.20 0.120 ? ? 14.60 0.13 0.04 ? 4  ? ? ? 
2.26 2.47  ? 6.3 79525  ? ? 6183 ? 99.90  ? ? ? 0.106 0.099 ? ? ? ? ? ? ? ? 12.90 0.099 ? ? 17.00 0.11 0.03 ? 5  ? ? ? 
2.47 2.77  ? 6.8 74757  ? ? 5610 ? 99.90  ? ? ? 0.093 0.087 ? ? ? ? ? ? ? ? 13.30 0.087 ? ? 20.50 0.09 0.03 ? 6  ? ? ? 
2.77 3.20  ? 7.0 67161  ? ? 4994 ? 100.00 ? ? ? 0.086 0.081 ? ? ? ? ? ? ? ? 13.40 0.081 ? ? 25.00 0.09 0.02 ? 7  ? ? ? 
3.20 3.91  ? 7.2 55776  ? ? 4245 ? 100.00 ? ? ? 0.080 0.076 ? ? ? ? ? ? ? ? 13.10 0.076 ? ? 29.80 0.08 0.02 ? 8  ? ? ? 
3.91 5.53  ? 7.2 43639  ? ? 3354 ? 100.00 ? ? ? 0.074 0.070 ? ? ? ? ? ? ? ? 13.00 0.070 ? ? 31.00 0.07 0.02 ? 9  ? ? ? 
5.53 71.28 ? 5.9 23056  ? ? 1959 ? 99.90  ? ? ? 0.072 0.068 ? ? ? ? ? ? ? ? 11.80 0.068 ? ? 28.20 0.07 0.02 ? 10 ? ? ? 
# 
_refine.aniso_B[1][1]                            0.370 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][2]                            1.120 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            -1.490 
_refine.B_iso_max                                82.00 
_refine.B_iso_mean                               24.864 
_refine.B_iso_min                                10.58 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.943 
_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                                 4WUP 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.750 
_refine.ls_d_res_low                             60.360 
_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                     55767 
_refine.ls_number_reflns_R_free                  5608 
_refine.ls_number_reflns_R_work                  50159 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.870 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.189 
_refine.ls_R_factor_R_free                       0.232 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.185 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      0.249 
_refine.ls_wR_factor_R_work                      0.196 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      1CAB 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.126 
_refine.pdbx_overall_ESU_R_Free                  0.126 
_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             0.126 
_refine.overall_SU_R_free                        0.126 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   0.836 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4023 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         41 
_refine_hist.number_atoms_solvent             370 
_refine_hist.number_atoms_total               4434 
_refine_hist.d_res_high                       1.750 
_refine_hist.d_res_low                        60.360 
# 
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' ? 0.020  0.020  4269 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.012  1.940  5820 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.094  5.000  531  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 38.496 24.718 195  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.878 15.000 662  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 15.040 15.000 14   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.162  0.200  615  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.021  3331 ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.750 
_refine_ls_shell.d_res_low                        1.795 
_refine_ls_shell.number_reflns_all                4029 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             411 
_refine_ls_shell.number_reflns_R_work             3618 
_refine_ls_shell.percent_reflns_obs               99.800 
_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                  0.277 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.222 
_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                 ? 
# 
_struct.entry_id                     4WUP 
_struct.title                        
'Crystal structure of human carbonic anhydrase isozyme I with 4-[(2-Hydroxyethyl)thio]benzenesulfonamide' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        4WUP 
_struct_keywords.text            'drug design, lyase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 5 ? 
I N N 6 ? 
J N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH1_HUMAN 
_struct_ref.pdbx_db_accession          P00915 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKG
GPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVL
DALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPM
QHNNRPTQPLKGRTVRASF
;
_struct_ref.pdbx_align_begin           3 
# 
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 4WUP A 2 ? 260 ? P00915 3 ? 261 ? 2 260 
2 1 4WUP B 2 ? 260 ? P00915 3 ? 261 ? 2 260 
# 
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 4WUP MET A 1 ? UNP P00915 ? ? 'initiating methionine' 1 1 
2 4WUP MET B 1 ? UNP P00915 ? ? 'initiating methionine' 1 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 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,C,D,E,I 
2 1 B,F,G,H,J 
# 
_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 GLY A 12  ? LEU A 19  ? GLY A 12  LEU A 19  5 ? 8  
HELX_P HELX_P2  AA2 TYR A 20  ? GLY A 25  ? TYR A 20  GLY A 25  5 ? 6  
HELX_P HELX_P3  AA3 LYS A 34  ? THR A 38  ? LYS A 34  THR A 38  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 52  ? ALA A 54  ? ASN A 52  ALA A 54  5 ? 3  
HELX_P HELX_P5  AA5 SER A 130 ? ALA A 135 ? SER A 130 ALA A 135 1 ? 6  
HELX_P HELX_P6  AA6 ASN A 154 ? LYS A 156 ? ASN A 154 LYS A 156 5 ? 3  
HELX_P HELX_P7  AA7 LEU A 157 ? LEU A 164 ? LEU A 157 LEU A 164 1 ? 8  
HELX_P HELX_P8  AA8 GLN A 165 ? ILE A 167 ? GLN A 165 ILE A 167 5 ? 3  
HELX_P HELX_P9  AA9 ASP A 180 ? LEU A 185 ? ASP A 180 LEU A 185 5 ? 6  
HELX_P HELX_P10 AB1 SER A 219 ? LEU A 229 ? SER A 219 LEU A 229 1 ? 11 
HELX_P HELX_P11 AB2 GLY B 12  ? LEU B 19  ? GLY B 12  LEU B 19  5 ? 8  
HELX_P HELX_P12 AB3 TYR B 20  ? GLY B 25  ? TYR B 20  GLY B 25  5 ? 6  
HELX_P HELX_P13 AB4 LYS B 34  ? THR B 38  ? LYS B 34  THR B 38  5 ? 5  
HELX_P HELX_P14 AB5 ASN B 52  ? ALA B 54  ? ASN B 52  ALA B 54  5 ? 3  
HELX_P HELX_P15 AB6 SER B 130 ? ALA B 135 ? SER B 130 ALA B 135 1 ? 6  
HELX_P HELX_P16 AB7 ASN B 154 ? LYS B 156 ? ASN B 154 LYS B 156 5 ? 3  
HELX_P HELX_P17 AB8 LEU B 157 ? LEU B 164 ? LEU B 157 LEU B 164 1 ? 8  
HELX_P HELX_P18 AB9 GLN B 165 ? ILE B 167 ? GLN B 165 ILE B 167 5 ? 3  
HELX_P HELX_P19 AC1 ASP B 180 ? LEU B 185 ? ASP B 180 LEU B 185 5 ? 6  
HELX_P HELX_P20 AC2 SER B 219 ? SER B 228 ? SER B 219 SER B 228 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 
metalc1  metalc ? ? A HIS 94  NE2 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
metalc2  metalc ? ? A HIS 96  NE2 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc3  metalc ? ? A HIS 119 ND1 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
metalc4  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D 3UF . S2 B ? A ZN  301 A 3UF 302 1_555 ? ? ? ? ? ? ? 2.992 ? ? 
metalc5  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D 3UF . N3 A ? A ZN  301 A 3UF 302 1_555 ? ? ? ? ? ? ? 1.740 ? ? 
metalc6  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D 3UF . N3 B ? A ZN  301 A 3UF 302 1_555 ? ? ? ? ? ? ? 1.731 ? ? 
metalc7  metalc ? ? B HIS 94  NE2 ? ? ? 1_555 F ZN  . ZN ? ? B HIS 94  B ZN  301 1_555 ? ? ? ? ? ? ? 1.993 ? ? 
metalc8  metalc ? ? B HIS 96  NE2 ? ? ? 1_555 F ZN  . ZN ? ? B HIS 96  B ZN  301 1_555 ? ? ? ? ? ? ? 2.004 ? ? 
metalc9  metalc ? ? B HIS 119 ND1 ? ? ? 1_555 F ZN  . ZN ? ? B HIS 119 B ZN  301 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
metalc10 metalc ? ? F ZN  .   ZN  ? ? ? 1_555 G 3UF . N3 ? ? B ZN  301 B 3UF 302 1_555 ? ? ? ? ? ? ? 1.931 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 105.5 ? 
2  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 109.0 ? 
3  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.2  ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 S2  B D 3UF .   ? A 3UF 302 ? 1_555 99.1  ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 S2  B D 3UF .   ? A 3UF 302 ? 1_555 141.2 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 S2  B D 3UF .   ? A 3UF 302 ? 1_555 101.6 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N3  A D 3UF .   ? A 3UF 302 ? 1_555 116.3 ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N3  A D 3UF .   ? A 3UF 302 ? 1_555 111.9 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N3  A D 3UF .   ? A 3UF 302 ? 1_555 114.2 ? 
10 S2  B D 3UF .   ? A 3UF 302 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N3  A D 3UF .   ? A 3UF 302 ? 1_555 29.3  ? 
11 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N3  B D 3UF .   ? A 3UF 302 ? 1_555 117.2 ? 
12 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N3  B D 3UF .   ? A 3UF 302 ? 1_555 111.5 ? 
13 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N3  B D 3UF .   ? A 3UF 302 ? 1_555 113.5 ? 
14 S2  B D 3UF .   ? A 3UF 302 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N3  B D 3UF .   ? A 3UF 302 ? 1_555 29.7  ? 
15 N3  A D 3UF .   ? A 3UF 302 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N3  B D 3UF .   ? A 3UF 302 ? 1_555 1.0   ? 
16 NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 105.4 ? 
17 NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 110.4 ? 
18 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 96.1  ? 
19 NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 N3  ? G 3UF .   ? B 3UF 302 ? 1_555 115.4 ? 
20 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 N3  ? G 3UF .   ? B 3UF 302 ? 1_555 110.2 ? 
21 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 ZN ? F ZN . ? B ZN 301 ? 1_555 N3  ? G 3UF .   ? B 3UF 302 ? 1_555 117.0 ? 
# 
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 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 7.23  
2 PRO 201 A . ? PRO 201 A PRO 202 A ? PRO 202 A 1 12.40 
3 SER 29  B . ? SER 29  B PRO 30  B ? PRO 30  B 1 -2.45 
4 PRO 201 B . ? PRO 201 B PRO 202 B ? PRO 202 B 1 12.26 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? HIS A 40  ? LYS A 39  HIS A 40  
AA2 2  ARG A 257 ? ALA A 258 ? ARG A 257 ALA A 258 
AA2 3  PHE A 191 ? GLY A 196 ? PHE A 191 GLY A 196 
AA2 4  VAL A 207 ? CYS A 212 ? VAL A 207 CYS A 212 
AA2 5  LEU A 141 ? VAL A 150 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  ALA A 56  ? ASN A 61  ? ALA A 56  ASN A 61  
AA2 10 ARG A 173 ? PRO A 175 ? ARG A 173 PRO A 175 
AA3 1  ILE A 47  ? SER A 50  ? ILE A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 141 ? VAL A 150 ? LEU A 141 VAL A 150 
AA3 6  ILE A 216 ? VAL A 218 ? ILE A 216 VAL A 218 
AA4 1  ASP B 32  ? ILE B 33  ? ASP B 32  ILE B 33  
AA4 2  THR B 108 ? VAL B 109 ? THR B 108 VAL B 109 
AA5 1  LYS B 39  ? HIS B 40  ? LYS B 39  HIS B 40  
AA5 2  ARG B 257 ? ALA B 258 ? ARG B 257 ALA B 258 
AA5 3  PHE B 191 ? GLY B 196 ? PHE B 191 GLY B 196 
AA5 4  VAL B 207 ? CYS B 212 ? VAL B 207 CYS B 212 
AA5 5  LEU B 141 ? VAL B 150 ? LEU B 141 VAL B 150 
AA5 6  ALA B 116 ? ASN B 124 ? ALA B 116 ASN B 124 
AA5 7  TYR B 88  ? TRP B 97  ? TYR B 88  TRP B 97  
AA5 8  PHE B 66  ? PHE B 70  ? PHE B 66  PHE B 70  
AA5 9  ALA B 56  ? ASN B 61  ? ALA B 56  ASN B 61  
AA5 10 ARG B 173 ? PRO B 175 ? ARG B 173 PRO B 175 
AA6 1  ILE B 47  ? SER B 50  ? ILE B 47  SER B 50  
AA6 2  VAL B 78  ? GLY B 81  ? VAL B 78  GLY B 81  
AA6 3  TYR B 88  ? TRP B 97  ? TYR B 88  TRP B 97  
AA6 4  ALA B 116 ? ASN B 124 ? ALA B 116 ASN B 124 
AA6 5  LEU B 141 ? VAL B 150 ? LEU B 141 VAL B 150 
AA6 6  ILE B 216 ? VAL B 218 ? ILE B 216 VAL B 218 
# 
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 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 258 ? O ALA A 258 
AA2 2 3  O ARG A 257 ? O ARG A 257 N THR A 193 ? N THR A 193 
AA2 3 4  N GLY A 196 ? N GLY A 196 O VAL A 207 ? O VAL A 207 
AA2 4 5  O ILE A 210 ? O ILE A 210 N GLY A 145 ? N GLY A 145 
AA2 5 6  O MET A 148 ? O MET A 148 N ALA A 116 ? N ALA A 116 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O ASN A 69  ? O ASN A 69  N GLU A 58  ? N GLU A 58  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 174 ? O ALA A 174 
AA3 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N ALA A 116 ? N ALA A 116 O MET A 148 ? O MET A 148 
AA3 5 6  N LYS A 149 ? N LYS A 149 O ILE A 216 ? O ILE A 216 
AA4 1 2  N ILE B 33  ? N ILE B 33  O THR B 108 ? O THR B 108 
AA5 1 2  N LYS B 39  ? N LYS B 39  O ALA B 258 ? O ALA B 258 
AA5 2 3  O ARG B 257 ? O ARG B 257 N THR B 193 ? N THR B 193 
AA5 3 4  N GLY B 196 ? N GLY B 196 O VAL B 207 ? O VAL B 207 
AA5 4 5  O CYS B 212 ? O CYS B 212 N GLY B 145 ? N GLY B 145 
AA5 5 6  O MET B 148 ? O MET B 148 N ALA B 116 ? N ALA B 116 
AA5 6 7  O ALA B 121 ? O ALA B 121 N GLN B 92  ? N GLN B 92  
AA5 7 8  O PHE B 93  ? O PHE B 93  N VAL B 68  ? N VAL B 68  
AA5 8 9  O ASN B 69  ? O ASN B 69  N GLU B 58  ? N GLU B 58  
AA5 9 10 N ILE B 59  ? N ILE B 59  O ALA B 174 ? O ALA B 174 
AA6 1 2  N SER B 48  ? N SER B 48  O LYS B 80  ? O LYS B 80  
AA6 2 3  N LEU B 79  ? N LEU B 79  O TYR B 88  ? O TYR B 88  
AA6 3 4  N GLN B 92  ? N GLN B 92  O ALA B 121 ? O ALA B 121 
AA6 4 5  N ALA B 116 ? N ALA B 116 O MET B 148 ? O MET B 148 
AA6 5 6  N LYS B 149 ? N LYS B 149 O ILE B 216 ? O ILE B 216 
# 
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 3UF 302 ? 10 'binding site for residue 3UF A 302' 
AC3 Software A ACT 303 ? 2  'binding site for residue ACT A 303' 
AC4 Software B ZN  301 ? 4  'binding site for residue ZN B 301'  
AC5 Software B 3UF 302 ? 9  'binding site for residue 3UF B 302' 
AC6 Software B PEG 303 ? 3  'binding site for residue PEG B 303' 
# 
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 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  3UF D .   ? 3UF A 302 . ? 1_555 ? 
5  AC2 10 HIS A 94  ? HIS A 94  . ? 1_555 ? 
6  AC2 10 HIS A 96  ? HIS A 96  . ? 1_555 ? 
7  AC2 10 HIS A 119 ? HIS A 119 . ? 1_555 ? 
8  AC2 10 ALA A 135 ? ALA A 135 . ? 1_555 ? 
9  AC2 10 VAL A 143 ? VAL A 143 . ? 1_555 ? 
10 AC2 10 LEU A 198 ? LEU A 198 . ? 1_555 ? 
11 AC2 10 THR A 199 ? THR A 199 . ? 1_555 ? 
12 AC2 10 HIS A 200 ? HIS A 200 . ? 1_555 ? 
13 AC2 10 TRP A 209 ? TRP A 209 . ? 1_555 ? 
14 AC2 10 ZN  C .   ? ZN  A 301 . ? 1_555 ? 
15 AC3 2  TYR A 204 ? TYR A 204 . ? 1_555 ? 
16 AC3 2  TYR B 204 ? TYR B 204 . ? 3_545 ? 
17 AC4 4  HIS B 94  ? HIS B 94  . ? 1_555 ? 
18 AC4 4  HIS B 96  ? HIS B 96  . ? 1_555 ? 
19 AC4 4  HIS B 119 ? HIS B 119 . ? 1_555 ? 
20 AC4 4  3UF G .   ? 3UF B 302 . ? 1_555 ? 
21 AC5 9  HIS B 94  ? HIS B 94  . ? 1_555 ? 
22 AC5 9  HIS B 96  ? HIS B 96  . ? 1_555 ? 
23 AC5 9  HIS B 119 ? HIS B 119 . ? 1_555 ? 
24 AC5 9  VAL B 143 ? VAL B 143 . ? 1_555 ? 
25 AC5 9  LEU B 198 ? LEU B 198 . ? 1_555 ? 
26 AC5 9  THR B 199 ? THR B 199 . ? 1_555 ? 
27 AC5 9  HIS B 200 ? HIS B 200 . ? 1_555 ? 
28 AC5 9  TRP B 209 ? TRP B 209 . ? 1_555 ? 
29 AC5 9  ZN  F .   ? ZN  B 301 . ? 1_555 ? 
30 AC6 3  LYS B 170 ? LYS B 170 . ? 1_555 ? 
31 AC6 3  GLY B 171 ? GLY B 171 . ? 1_555 ? 
32 AC6 3  HOH J .   ? HOH B 478 . ? 1_555 ? 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG A HIS 64  ? ? CD2 A HIS 64  ? ? 1.411 1.354 0.057 0.009 N 
2 1 CG A HIS 243 ? ? CD2 A HIS 243 ? ? 1.412 1.354 0.058 0.009 N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             C 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             GLY 
_pdbx_validate_rmsd_angle.auth_seq_id_1              82 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             N 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_2              83 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_3              83 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                128.96 
_pdbx_validate_rmsd_angle.angle_target_value         119.30 
_pdbx_validate_rmsd_angle.angle_deviation            9.66 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.50 
_pdbx_validate_rmsd_angle.linker_flag                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 65  ? ? -172.11 -171.57 
2 1 ASN A 75  ? ? -94.41  31.92   
3 1 ASN A 244 ? ? -159.59 31.73   
4 1 SER B 65  ? ? -167.25 -165.92 
5 1 ASN B 75  ? ? -94.53  44.04   
6 1 ASN B 244 ? ? -159.62 38.58   
# 
_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 SER 2 ? A SER 2 
3 1 Y 1 A PRO 3 ? A PRO 3 
4 1 Y 1 A ASP 4 ? A ASP 4 
5 1 Y 1 B MET 1 ? B MET 1 
6 1 Y 1 B SER 2 ? B SER 2 
7 1 Y 1 B PRO 3 ? B PRO 3 
# 
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 
3UF C6   C  Y N 1   
3UF C5   C  Y N 2   
3UF O4   O  N N 3   
3UF S2   S  N N 4   
3UF O1   O  N N 5   
3UF N3   N  N N 6   
3UF C10  C  Y N 7   
3UF C9   C  Y N 8   
3UF C8   C  Y N 9   
3UF C7   C  Y N 10  
3UF S11  S  N N 11  
3UF C12  C  N N 12  
3UF C13  C  N N 13  
3UF O14  O  N N 14  
3UF H1   H  N N 15  
3UF H2   H  N N 16  
3UF H3   H  N N 17  
3UF H4   H  N N 18  
3UF H5   H  N N 19  
3UF H6   H  N N 20  
3UF H7   H  N N 21  
3UF H8   H  N N 22  
3UF H9   H  N N 23  
3UF H10  H  N N 24  
3UF H11  H  N N 25  
ACT C    C  N N 26  
ACT O    O  N N 27  
ACT OXT  O  N N 28  
ACT CH3  C  N N 29  
ACT H1   H  N N 30  
ACT H2   H  N N 31  
ACT H3   H  N N 32  
ALA N    N  N N 33  
ALA CA   C  N S 34  
ALA C    C  N N 35  
ALA O    O  N N 36  
ALA CB   C  N N 37  
ALA OXT  O  N N 38  
ALA H    H  N N 39  
ALA H2   H  N N 40  
ALA HA   H  N N 41  
ALA HB1  H  N N 42  
ALA HB2  H  N N 43  
ALA HB3  H  N N 44  
ALA HXT  H  N N 45  
ARG N    N  N N 46  
ARG CA   C  N S 47  
ARG C    C  N N 48  
ARG O    O  N N 49  
ARG CB   C  N N 50  
ARG CG   C  N N 51  
ARG CD   C  N N 52  
ARG NE   N  N N 53  
ARG CZ   C  N N 54  
ARG NH1  N  N N 55  
ARG NH2  N  N N 56  
ARG OXT  O  N N 57  
ARG H    H  N N 58  
ARG H2   H  N N 59  
ARG HA   H  N N 60  
ARG HB2  H  N N 61  
ARG HB3  H  N N 62  
ARG HG2  H  N N 63  
ARG HG3  H  N N 64  
ARG HD2  H  N N 65  
ARG HD3  H  N N 66  
ARG HE   H  N N 67  
ARG HH11 H  N N 68  
ARG HH12 H  N N 69  
ARG HH21 H  N N 70  
ARG HH22 H  N N 71  
ARG HXT  H  N N 72  
ASN N    N  N N 73  
ASN CA   C  N S 74  
ASN C    C  N N 75  
ASN O    O  N N 76  
ASN CB   C  N N 77  
ASN CG   C  N N 78  
ASN OD1  O  N N 79  
ASN ND2  N  N N 80  
ASN OXT  O  N N 81  
ASN H    H  N N 82  
ASN H2   H  N N 83  
ASN HA   H  N N 84  
ASN HB2  H  N N 85  
ASN HB3  H  N N 86  
ASN HD21 H  N N 87  
ASN HD22 H  N N 88  
ASN HXT  H  N N 89  
ASP N    N  N N 90  
ASP CA   C  N S 91  
ASP C    C  N N 92  
ASP O    O  N N 93  
ASP CB   C  N N 94  
ASP CG   C  N N 95  
ASP OD1  O  N N 96  
ASP OD2  O  N N 97  
ASP OXT  O  N N 98  
ASP H    H  N N 99  
ASP H2   H  N N 100 
ASP HA   H  N N 101 
ASP HB2  H  N N 102 
ASP HB3  H  N N 103 
ASP HD2  H  N N 104 
ASP HXT  H  N N 105 
CYS N    N  N N 106 
CYS CA   C  N R 107 
CYS C    C  N N 108 
CYS O    O  N N 109 
CYS CB   C  N N 110 
CYS SG   S  N N 111 
CYS OXT  O  N N 112 
CYS H    H  N N 113 
CYS H2   H  N N 114 
CYS HA   H  N N 115 
CYS HB2  H  N N 116 
CYS HB3  H  N N 117 
CYS HG   H  N N 118 
CYS HXT  H  N N 119 
GLN N    N  N N 120 
GLN CA   C  N S 121 
GLN C    C  N N 122 
GLN O    O  N N 123 
GLN CB   C  N N 124 
GLN CG   C  N N 125 
GLN CD   C  N N 126 
GLN OE1  O  N N 127 
GLN NE2  N  N N 128 
GLN OXT  O  N N 129 
GLN H    H  N N 130 
GLN H2   H  N N 131 
GLN HA   H  N N 132 
GLN HB2  H  N N 133 
GLN HB3  H  N N 134 
GLN HG2  H  N N 135 
GLN HG3  H  N N 136 
GLN HE21 H  N N 137 
GLN HE22 H  N N 138 
GLN HXT  H  N N 139 
GLU N    N  N N 140 
GLU CA   C  N S 141 
GLU C    C  N N 142 
GLU O    O  N N 143 
GLU CB   C  N N 144 
GLU CG   C  N N 145 
GLU CD   C  N N 146 
GLU OE1  O  N N 147 
GLU OE2  O  N N 148 
GLU OXT  O  N N 149 
GLU H    H  N N 150 
GLU H2   H  N N 151 
GLU HA   H  N N 152 
GLU HB2  H  N N 153 
GLU HB3  H  N N 154 
GLU HG2  H  N N 155 
GLU HG3  H  N N 156 
GLU HE2  H  N N 157 
GLU HXT  H  N N 158 
GLY N    N  N N 159 
GLY CA   C  N N 160 
GLY C    C  N N 161 
GLY O    O  N N 162 
GLY OXT  O  N N 163 
GLY H    H  N N 164 
GLY H2   H  N N 165 
GLY HA2  H  N N 166 
GLY HA3  H  N N 167 
GLY HXT  H  N N 168 
HIS N    N  N N 169 
HIS CA   C  N S 170 
HIS C    C  N N 171 
HIS O    O  N N 172 
HIS CB   C  N N 173 
HIS CG   C  Y N 174 
HIS ND1  N  Y N 175 
HIS CD2  C  Y N 176 
HIS CE1  C  Y N 177 
HIS NE2  N  Y N 178 
HIS OXT  O  N N 179 
HIS H    H  N N 180 
HIS H2   H  N N 181 
HIS HA   H  N N 182 
HIS HB2  H  N N 183 
HIS HB3  H  N N 184 
HIS HD1  H  N N 185 
HIS HD2  H  N N 186 
HIS HE1  H  N N 187 
HIS HE2  H  N N 188 
HIS HXT  H  N N 189 
HOH O    O  N N 190 
HOH H1   H  N N 191 
HOH H2   H  N N 192 
ILE N    N  N N 193 
ILE CA   C  N S 194 
ILE C    C  N N 195 
ILE O    O  N N 196 
ILE CB   C  N S 197 
ILE CG1  C  N N 198 
ILE CG2  C  N N 199 
ILE CD1  C  N N 200 
ILE OXT  O  N N 201 
ILE H    H  N N 202 
ILE H2   H  N N 203 
ILE HA   H  N N 204 
ILE HB   H  N N 205 
ILE HG12 H  N N 206 
ILE HG13 H  N N 207 
ILE HG21 H  N N 208 
ILE HG22 H  N N 209 
ILE HG23 H  N N 210 
ILE HD11 H  N N 211 
ILE HD12 H  N N 212 
ILE HD13 H  N N 213 
ILE HXT  H  N N 214 
LEU N    N  N N 215 
LEU CA   C  N S 216 
LEU C    C  N N 217 
LEU O    O  N N 218 
LEU CB   C  N N 219 
LEU CG   C  N N 220 
LEU CD1  C  N N 221 
LEU CD2  C  N N 222 
LEU OXT  O  N N 223 
LEU H    H  N N 224 
LEU H2   H  N N 225 
LEU HA   H  N N 226 
LEU HB2  H  N N 227 
LEU HB3  H  N N 228 
LEU HG   H  N N 229 
LEU HD11 H  N N 230 
LEU HD12 H  N N 231 
LEU HD13 H  N N 232 
LEU HD21 H  N N 233 
LEU HD22 H  N N 234 
LEU HD23 H  N N 235 
LEU HXT  H  N N 236 
LYS N    N  N N 237 
LYS CA   C  N S 238 
LYS C    C  N N 239 
LYS O    O  N N 240 
LYS CB   C  N N 241 
LYS CG   C  N N 242 
LYS CD   C  N N 243 
LYS CE   C  N N 244 
LYS NZ   N  N N 245 
LYS OXT  O  N N 246 
LYS H    H  N N 247 
LYS H2   H  N N 248 
LYS HA   H  N N 249 
LYS HB2  H  N N 250 
LYS HB3  H  N N 251 
LYS HG2  H  N N 252 
LYS HG3  H  N N 253 
LYS HD2  H  N N 254 
LYS HD3  H  N N 255 
LYS HE2  H  N N 256 
LYS HE3  H  N N 257 
LYS HZ1  H  N N 258 
LYS HZ2  H  N N 259 
LYS HZ3  H  N N 260 
LYS HXT  H  N N 261 
MET N    N  N N 262 
MET CA   C  N S 263 
MET C    C  N N 264 
MET O    O  N N 265 
MET CB   C  N N 266 
MET CG   C  N N 267 
MET SD   S  N N 268 
MET CE   C  N N 269 
MET OXT  O  N N 270 
MET H    H  N N 271 
MET H2   H  N N 272 
MET HA   H  N N 273 
MET HB2  H  N N 274 
MET HB3  H  N N 275 
MET HG2  H  N N 276 
MET HG3  H  N N 277 
MET HE1  H  N N 278 
MET HE2  H  N N 279 
MET HE3  H  N N 280 
MET HXT  H  N N 281 
PEG C1   C  N N 282 
PEG O1   O  N N 283 
PEG C2   C  N N 284 
PEG O2   O  N N 285 
PEG C3   C  N N 286 
PEG C4   C  N N 287 
PEG O4   O  N N 288 
PEG H11  H  N N 289 
PEG H12  H  N N 290 
PEG HO1  H  N N 291 
PEG H21  H  N N 292 
PEG H22  H  N N 293 
PEG H31  H  N N 294 
PEG H32  H  N N 295 
PEG H41  H  N N 296 
PEG H42  H  N N 297 
PEG HO4  H  N N 298 
PHE N    N  N N 299 
PHE CA   C  N S 300 
PHE C    C  N N 301 
PHE O    O  N N 302 
PHE CB   C  N N 303 
PHE CG   C  Y N 304 
PHE CD1  C  Y N 305 
PHE CD2  C  Y N 306 
PHE CE1  C  Y N 307 
PHE CE2  C  Y N 308 
PHE CZ   C  Y N 309 
PHE OXT  O  N N 310 
PHE H    H  N N 311 
PHE H2   H  N N 312 
PHE HA   H  N N 313 
PHE HB2  H  N N 314 
PHE HB3  H  N N 315 
PHE HD1  H  N N 316 
PHE HD2  H  N N 317 
PHE HE1  H  N N 318 
PHE HE2  H  N N 319 
PHE HZ   H  N N 320 
PHE HXT  H  N N 321 
PRO N    N  N N 322 
PRO CA   C  N S 323 
PRO C    C  N N 324 
PRO O    O  N N 325 
PRO CB   C  N N 326 
PRO CG   C  N N 327 
PRO CD   C  N N 328 
PRO OXT  O  N N 329 
PRO H    H  N N 330 
PRO HA   H  N N 331 
PRO HB2  H  N N 332 
PRO HB3  H  N N 333 
PRO HG2  H  N N 334 
PRO HG3  H  N N 335 
PRO HD2  H  N N 336 
PRO HD3  H  N N 337 
PRO HXT  H  N N 338 
SER N    N  N N 339 
SER CA   C  N S 340 
SER C    C  N N 341 
SER O    O  N N 342 
SER CB   C  N N 343 
SER OG   O  N N 344 
SER OXT  O  N N 345 
SER H    H  N N 346 
SER H2   H  N N 347 
SER HA   H  N N 348 
SER HB2  H  N N 349 
SER HB3  H  N N 350 
SER HG   H  N N 351 
SER HXT  H  N N 352 
THR N    N  N N 353 
THR CA   C  N S 354 
THR C    C  N N 355 
THR O    O  N N 356 
THR CB   C  N R 357 
THR OG1  O  N N 358 
THR CG2  C  N N 359 
THR OXT  O  N N 360 
THR H    H  N N 361 
THR H2   H  N N 362 
THR HA   H  N N 363 
THR HB   H  N N 364 
THR HG1  H  N N 365 
THR HG21 H  N N 366 
THR HG22 H  N N 367 
THR HG23 H  N N 368 
THR HXT  H  N N 369 
TRP N    N  N N 370 
TRP CA   C  N S 371 
TRP C    C  N N 372 
TRP O    O  N N 373 
TRP CB   C  N N 374 
TRP CG   C  Y N 375 
TRP CD1  C  Y N 376 
TRP CD2  C  Y N 377 
TRP NE1  N  Y N 378 
TRP CE2  C  Y N 379 
TRP CE3  C  Y N 380 
TRP CZ2  C  Y N 381 
TRP CZ3  C  Y N 382 
TRP CH2  C  Y N 383 
TRP OXT  O  N N 384 
TRP H    H  N N 385 
TRP H2   H  N N 386 
TRP HA   H  N N 387 
TRP HB2  H  N N 388 
TRP HB3  H  N N 389 
TRP HD1  H  N N 390 
TRP HE1  H  N N 391 
TRP HE3  H  N N 392 
TRP HZ2  H  N N 393 
TRP HZ3  H  N N 394 
TRP HH2  H  N N 395 
TRP HXT  H  N N 396 
TYR N    N  N N 397 
TYR CA   C  N S 398 
TYR C    C  N N 399 
TYR O    O  N N 400 
TYR CB   C  N N 401 
TYR CG   C  Y N 402 
TYR CD1  C  Y N 403 
TYR CD2  C  Y N 404 
TYR CE1  C  Y N 405 
TYR CE2  C  Y N 406 
TYR CZ   C  Y N 407 
TYR OH   O  N N 408 
TYR OXT  O  N N 409 
TYR H    H  N N 410 
TYR H2   H  N N 411 
TYR HA   H  N N 412 
TYR HB2  H  N N 413 
TYR HB3  H  N N 414 
TYR HD1  H  N N 415 
TYR HD2  H  N N 416 
TYR HE1  H  N N 417 
TYR HE2  H  N N 418 
TYR HH   H  N N 419 
TYR HXT  H  N N 420 
VAL N    N  N N 421 
VAL CA   C  N S 422 
VAL C    C  N N 423 
VAL O    O  N N 424 
VAL CB   C  N N 425 
VAL CG1  C  N N 426 
VAL CG2  C  N N 427 
VAL OXT  O  N N 428 
VAL H    H  N N 429 
VAL H2   H  N N 430 
VAL HA   H  N N 431 
VAL HB   H  N N 432 
VAL HG11 H  N N 433 
VAL HG12 H  N N 434 
VAL HG13 H  N N 435 
VAL HG21 H  N N 436 
VAL HG22 H  N N 437 
VAL HG23 H  N N 438 
VAL HXT  H  N N 439 
ZN  ZN   ZN N N 440 
# 
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 
3UF O14 C13  sing N N 1   
3UF C13 C12  sing N N 2   
3UF S11 C12  sing N N 3   
3UF S11 C8   sing N N 4   
3UF C8  C7   doub Y N 5   
3UF C8  C9   sing Y N 6   
3UF C7  C6   sing Y N 7   
3UF C9  C10  doub Y N 8   
3UF C6  C5   doub Y N 9   
3UF C10 C5   sing Y N 10  
3UF C5  S2   sing N N 11  
3UF N3  S2   sing N N 12  
3UF S2  O4   doub N N 13  
3UF S2  O1   doub N N 14  
3UF C6  H1   sing N N 15  
3UF N3  H2   sing N N 16  
3UF N3  H3   sing N N 17  
3UF C10 H4   sing N N 18  
3UF C9  H5   sing N N 19  
3UF C7  H6   sing N N 20  
3UF C12 H7   sing N N 21  
3UF C12 H8   sing N N 22  
3UF C13 H9   sing N N 23  
3UF C13 H10  sing N N 24  
3UF O14 H11  sing N N 25  
ACT C   O    doub N N 26  
ACT C   OXT  sing N N 27  
ACT C   CH3  sing N N 28  
ACT CH3 H1   sing N N 29  
ACT CH3 H2   sing N N 30  
ACT CH3 H3   sing N N 31  
ALA N   CA   sing N N 32  
ALA N   H    sing N N 33  
ALA N   H2   sing N N 34  
ALA CA  C    sing N N 35  
ALA CA  CB   sing N N 36  
ALA CA  HA   sing N N 37  
ALA C   O    doub N N 38  
ALA C   OXT  sing N N 39  
ALA CB  HB1  sing N N 40  
ALA CB  HB2  sing N N 41  
ALA CB  HB3  sing N N 42  
ALA OXT HXT  sing N N 43  
ARG N   CA   sing N N 44  
ARG N   H    sing N N 45  
ARG N   H2   sing N N 46  
ARG CA  C    sing N N 47  
ARG CA  CB   sing N N 48  
ARG CA  HA   sing N N 49  
ARG C   O    doub N N 50  
ARG C   OXT  sing N N 51  
ARG CB  CG   sing N N 52  
ARG CB  HB2  sing N N 53  
ARG CB  HB3  sing N N 54  
ARG CG  CD   sing N N 55  
ARG CG  HG2  sing N N 56  
ARG CG  HG3  sing N N 57  
ARG CD  NE   sing N N 58  
ARG CD  HD2  sing N N 59  
ARG CD  HD3  sing N N 60  
ARG NE  CZ   sing N N 61  
ARG NE  HE   sing N N 62  
ARG CZ  NH1  sing N N 63  
ARG CZ  NH2  doub N N 64  
ARG NH1 HH11 sing N N 65  
ARG NH1 HH12 sing N N 66  
ARG NH2 HH21 sing N N 67  
ARG NH2 HH22 sing N N 68  
ARG OXT HXT  sing N N 69  
ASN N   CA   sing N N 70  
ASN N   H    sing N N 71  
ASN N   H2   sing N N 72  
ASN CA  C    sing N N 73  
ASN CA  CB   sing N N 74  
ASN CA  HA   sing N N 75  
ASN C   O    doub N N 76  
ASN C   OXT  sing N N 77  
ASN CB  CG   sing N N 78  
ASN CB  HB2  sing N N 79  
ASN CB  HB3  sing N N 80  
ASN CG  OD1  doub N N 81  
ASN CG  ND2  sing N N 82  
ASN ND2 HD21 sing N N 83  
ASN ND2 HD22 sing N N 84  
ASN OXT HXT  sing N N 85  
ASP N   CA   sing N N 86  
ASP N   H    sing N N 87  
ASP N   H2   sing N N 88  
ASP CA  C    sing N N 89  
ASP CA  CB   sing N N 90  
ASP CA  HA   sing N N 91  
ASP C   O    doub N N 92  
ASP C   OXT  sing N N 93  
ASP CB  CG   sing N N 94  
ASP CB  HB2  sing N N 95  
ASP CB  HB3  sing N N 96  
ASP CG  OD1  doub N N 97  
ASP CG  OD2  sing N N 98  
ASP OD2 HD2  sing N N 99  
ASP OXT HXT  sing N N 100 
CYS N   CA   sing N N 101 
CYS N   H    sing N N 102 
CYS N   H2   sing N N 103 
CYS CA  C    sing N N 104 
CYS CA  CB   sing N N 105 
CYS CA  HA   sing N N 106 
CYS C   O    doub N N 107 
CYS C   OXT  sing N N 108 
CYS CB  SG   sing N N 109 
CYS CB  HB2  sing N N 110 
CYS CB  HB3  sing N N 111 
CYS SG  HG   sing N N 112 
CYS OXT HXT  sing N N 113 
GLN N   CA   sing N N 114 
GLN N   H    sing N N 115 
GLN N   H2   sing N N 116 
GLN CA  C    sing N N 117 
GLN CA  CB   sing N N 118 
GLN CA  HA   sing N N 119 
GLN C   O    doub N N 120 
GLN C   OXT  sing N N 121 
GLN CB  CG   sing N N 122 
GLN CB  HB2  sing N N 123 
GLN CB  HB3  sing N N 124 
GLN CG  CD   sing N N 125 
GLN CG  HG2  sing N N 126 
GLN CG  HG3  sing N N 127 
GLN CD  OE1  doub N N 128 
GLN CD  NE2  sing N N 129 
GLN NE2 HE21 sing N N 130 
GLN NE2 HE22 sing N N 131 
GLN OXT HXT  sing N N 132 
GLU N   CA   sing N N 133 
GLU N   H    sing N N 134 
GLU N   H2   sing N N 135 
GLU CA  C    sing N N 136 
GLU CA  CB   sing N N 137 
GLU CA  HA   sing N N 138 
GLU C   O    doub N N 139 
GLU C   OXT  sing N N 140 
GLU CB  CG   sing N N 141 
GLU CB  HB2  sing N N 142 
GLU CB  HB3  sing N N 143 
GLU CG  CD   sing N N 144 
GLU CG  HG2  sing N N 145 
GLU CG  HG3  sing N N 146 
GLU CD  OE1  doub N N 147 
GLU CD  OE2  sing N N 148 
GLU OE2 HE2  sing N N 149 
GLU OXT HXT  sing N N 150 
GLY N   CA   sing N N 151 
GLY N   H    sing N N 152 
GLY N   H2   sing N N 153 
GLY CA  C    sing N N 154 
GLY CA  HA2  sing N N 155 
GLY CA  HA3  sing N N 156 
GLY C   O    doub N N 157 
GLY C   OXT  sing N N 158 
GLY OXT HXT  sing N N 159 
HIS N   CA   sing N N 160 
HIS N   H    sing N N 161 
HIS N   H2   sing N N 162 
HIS CA  C    sing N N 163 
HIS CA  CB   sing N N 164 
HIS CA  HA   sing N N 165 
HIS C   O    doub N N 166 
HIS C   OXT  sing N N 167 
HIS CB  CG   sing N N 168 
HIS CB  HB2  sing N N 169 
HIS CB  HB3  sing N N 170 
HIS CG  ND1  sing Y N 171 
HIS CG  CD2  doub Y N 172 
HIS ND1 CE1  doub Y N 173 
HIS ND1 HD1  sing N N 174 
HIS CD2 NE2  sing Y N 175 
HIS CD2 HD2  sing N N 176 
HIS CE1 NE2  sing Y N 177 
HIS CE1 HE1  sing N N 178 
HIS NE2 HE2  sing N N 179 
HIS OXT HXT  sing N N 180 
HOH O   H1   sing N N 181 
HOH O   H2   sing N N 182 
ILE N   CA   sing N N 183 
ILE N   H    sing N N 184 
ILE N   H2   sing N N 185 
ILE CA  C    sing N N 186 
ILE CA  CB   sing N N 187 
ILE CA  HA   sing N N 188 
ILE C   O    doub N N 189 
ILE C   OXT  sing N N 190 
ILE CB  CG1  sing N N 191 
ILE CB  CG2  sing N N 192 
ILE CB  HB   sing N N 193 
ILE CG1 CD1  sing N N 194 
ILE CG1 HG12 sing N N 195 
ILE CG1 HG13 sing N N 196 
ILE CG2 HG21 sing N N 197 
ILE CG2 HG22 sing N N 198 
ILE CG2 HG23 sing N N 199 
ILE CD1 HD11 sing N N 200 
ILE CD1 HD12 sing N N 201 
ILE CD1 HD13 sing N N 202 
ILE OXT HXT  sing N N 203 
LEU N   CA   sing N N 204 
LEU N   H    sing N N 205 
LEU N   H2   sing N N 206 
LEU CA  C    sing N N 207 
LEU CA  CB   sing N N 208 
LEU CA  HA   sing N N 209 
LEU C   O    doub N N 210 
LEU C   OXT  sing N N 211 
LEU CB  CG   sing N N 212 
LEU CB  HB2  sing N N 213 
LEU CB  HB3  sing N N 214 
LEU CG  CD1  sing N N 215 
LEU CG  CD2  sing N N 216 
LEU CG  HG   sing N N 217 
LEU CD1 HD11 sing N N 218 
LEU CD1 HD12 sing N N 219 
LEU CD1 HD13 sing N N 220 
LEU CD2 HD21 sing N N 221 
LEU CD2 HD22 sing N N 222 
LEU CD2 HD23 sing N N 223 
LEU OXT HXT  sing N N 224 
LYS N   CA   sing N N 225 
LYS N   H    sing N N 226 
LYS N   H2   sing N N 227 
LYS CA  C    sing N N 228 
LYS CA  CB   sing N N 229 
LYS CA  HA   sing N N 230 
LYS C   O    doub N N 231 
LYS C   OXT  sing N N 232 
LYS CB  CG   sing N N 233 
LYS CB  HB2  sing N N 234 
LYS CB  HB3  sing N N 235 
LYS CG  CD   sing N N 236 
LYS CG  HG2  sing N N 237 
LYS CG  HG3  sing N N 238 
LYS CD  CE   sing N N 239 
LYS CD  HD2  sing N N 240 
LYS CD  HD3  sing N N 241 
LYS CE  NZ   sing N N 242 
LYS CE  HE2  sing N N 243 
LYS CE  HE3  sing N N 244 
LYS NZ  HZ1  sing N N 245 
LYS NZ  HZ2  sing N N 246 
LYS NZ  HZ3  sing N N 247 
LYS OXT HXT  sing N N 248 
MET N   CA   sing N N 249 
MET N   H    sing N N 250 
MET N   H2   sing N N 251 
MET CA  C    sing N N 252 
MET CA  CB   sing N N 253 
MET CA  HA   sing N N 254 
MET C   O    doub N N 255 
MET C   OXT  sing N N 256 
MET CB  CG   sing N N 257 
MET CB  HB2  sing N N 258 
MET CB  HB3  sing N N 259 
MET CG  SD   sing N N 260 
MET CG  HG2  sing N N 261 
MET CG  HG3  sing N N 262 
MET SD  CE   sing N N 263 
MET CE  HE1  sing N N 264 
MET CE  HE2  sing N N 265 
MET CE  HE3  sing N N 266 
MET OXT HXT  sing N N 267 
PEG C1  O1   sing N N 268 
PEG C1  C2   sing N N 269 
PEG C1  H11  sing N N 270 
PEG C1  H12  sing N N 271 
PEG O1  HO1  sing N N 272 
PEG C2  O2   sing N N 273 
PEG C2  H21  sing N N 274 
PEG C2  H22  sing N N 275 
PEG O2  C3   sing N N 276 
PEG C3  C4   sing N N 277 
PEG C3  H31  sing N N 278 
PEG C3  H32  sing N N 279 
PEG C4  O4   sing N N 280 
PEG C4  H41  sing N N 281 
PEG C4  H42  sing N N 282 
PEG O4  HO4  sing N N 283 
PHE N   CA   sing N N 284 
PHE N   H    sing N N 285 
PHE N   H2   sing N N 286 
PHE CA  C    sing N N 287 
PHE CA  CB   sing N N 288 
PHE CA  HA   sing N N 289 
PHE C   O    doub N N 290 
PHE C   OXT  sing N N 291 
PHE CB  CG   sing N N 292 
PHE CB  HB2  sing N N 293 
PHE CB  HB3  sing N N 294 
PHE CG  CD1  doub Y N 295 
PHE CG  CD2  sing Y N 296 
PHE CD1 CE1  sing Y N 297 
PHE CD1 HD1  sing N N 298 
PHE CD2 CE2  doub Y N 299 
PHE CD2 HD2  sing N N 300 
PHE CE1 CZ   doub Y N 301 
PHE CE1 HE1  sing N N 302 
PHE CE2 CZ   sing Y N 303 
PHE CE2 HE2  sing N N 304 
PHE CZ  HZ   sing N N 305 
PHE OXT HXT  sing N N 306 
PRO N   CA   sing N N 307 
PRO N   CD   sing N N 308 
PRO N   H    sing N N 309 
PRO CA  C    sing N N 310 
PRO CA  CB   sing N N 311 
PRO CA  HA   sing N N 312 
PRO C   O    doub N N 313 
PRO C   OXT  sing N N 314 
PRO CB  CG   sing N N 315 
PRO CB  HB2  sing N N 316 
PRO CB  HB3  sing N N 317 
PRO CG  CD   sing N N 318 
PRO CG  HG2  sing N N 319 
PRO CG  HG3  sing N N 320 
PRO CD  HD2  sing N N 321 
PRO CD  HD3  sing N N 322 
PRO OXT HXT  sing N N 323 
SER N   CA   sing N N 324 
SER N   H    sing N N 325 
SER N   H2   sing N N 326 
SER CA  C    sing N N 327 
SER CA  CB   sing N N 328 
SER CA  HA   sing N N 329 
SER C   O    doub N N 330 
SER C   OXT  sing N N 331 
SER CB  OG   sing N N 332 
SER CB  HB2  sing N N 333 
SER CB  HB3  sing N N 334 
SER OG  HG   sing N N 335 
SER OXT HXT  sing N N 336 
THR N   CA   sing N N 337 
THR N   H    sing N N 338 
THR N   H2   sing N N 339 
THR CA  C    sing N N 340 
THR CA  CB   sing N N 341 
THR CA  HA   sing N N 342 
THR C   O    doub N N 343 
THR C   OXT  sing N N 344 
THR CB  OG1  sing N N 345 
THR CB  CG2  sing N N 346 
THR CB  HB   sing N N 347 
THR OG1 HG1  sing N N 348 
THR CG2 HG21 sing N N 349 
THR CG2 HG22 sing N N 350 
THR CG2 HG23 sing N N 351 
THR OXT HXT  sing N N 352 
TRP N   CA   sing N N 353 
TRP N   H    sing N N 354 
TRP N   H2   sing N N 355 
TRP CA  C    sing N N 356 
TRP CA  CB   sing N N 357 
TRP CA  HA   sing N N 358 
TRP C   O    doub N N 359 
TRP C   OXT  sing N N 360 
TRP CB  CG   sing N N 361 
TRP CB  HB2  sing N N 362 
TRP CB  HB3  sing N N 363 
TRP CG  CD1  doub Y N 364 
TRP CG  CD2  sing Y N 365 
TRP CD1 NE1  sing Y N 366 
TRP CD1 HD1  sing N N 367 
TRP CD2 CE2  doub Y N 368 
TRP CD2 CE3  sing Y N 369 
TRP NE1 CE2  sing Y N 370 
TRP NE1 HE1  sing N N 371 
TRP CE2 CZ2  sing Y N 372 
TRP CE3 CZ3  doub Y N 373 
TRP CE3 HE3  sing N N 374 
TRP CZ2 CH2  doub Y N 375 
TRP CZ2 HZ2  sing N N 376 
TRP CZ3 CH2  sing Y N 377 
TRP CZ3 HZ3  sing N N 378 
TRP CH2 HH2  sing N N 379 
TRP OXT HXT  sing N N 380 
TYR N   CA   sing N N 381 
TYR N   H    sing N N 382 
TYR N   H2   sing N N 383 
TYR CA  C    sing N N 384 
TYR CA  CB   sing N N 385 
TYR CA  HA   sing N N 386 
TYR C   O    doub N N 387 
TYR C   OXT  sing N N 388 
TYR CB  CG   sing N N 389 
TYR CB  HB2  sing N N 390 
TYR CB  HB3  sing N N 391 
TYR CG  CD1  doub Y N 392 
TYR CG  CD2  sing Y N 393 
TYR CD1 CE1  sing Y N 394 
TYR CD1 HD1  sing N N 395 
TYR CD2 CE2  doub Y N 396 
TYR CD2 HD2  sing N N 397 
TYR CE1 CZ   doub Y N 398 
TYR CE1 HE1  sing N N 399 
TYR CE2 CZ   sing Y N 400 
TYR CE2 HE2  sing N N 401 
TYR CZ  OH   sing N N 402 
TYR OH  HH   sing N N 403 
TYR OXT HXT  sing N N 404 
VAL N   CA   sing N N 405 
VAL N   H    sing N N 406 
VAL N   H2   sing N N 407 
VAL CA  C    sing N N 408 
VAL CA  CB   sing N N 409 
VAL CA  HA   sing N N 410 
VAL C   O    doub N N 411 
VAL C   OXT  sing N N 412 
VAL CB  CG1  sing N N 413 
VAL CB  CG2  sing N N 414 
VAL CB  HB   sing N N 415 
VAL CG1 HG11 sing N N 416 
VAL CG1 HG12 sing N N 417 
VAL CG1 HG13 sing N N 418 
VAL CG2 HG21 sing N N 419 
VAL CG2 HG22 sing N N 420 
VAL CG2 HG23 sing N N 421 
VAL OXT HXT  sing N N 422 
# 
_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   1CAB 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    4WUP 
_atom_sites.fract_transf_matrix[1][1]   0.015790 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014028 
_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]   0.008284 
_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  
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   . TRP A 1 5   ? 16.326  45.540 7.711  1.00 28.60 ? 5   TRP A N   1 
ATOM   2    C  CA  . TRP A 1 5   ? 16.935  45.756 9.073  1.00 25.81 ? 5   TRP A CA  1 
ATOM   3    C  C   . TRP A 1 5   ? 18.222  45.003 9.348  1.00 25.57 ? 5   TRP A C   1 
ATOM   4    O  O   . TRP A 1 5   ? 18.550  43.925 8.758  1.00 29.32 ? 5   TRP A O   1 
ATOM   5    C  CB  . TRP A 1 5   ? 15.884  45.497 10.172 1.00 23.46 ? 5   TRP A CB  1 
ATOM   6    C  CG  . TRP A 1 5   ? 15.633  44.039 10.383 1.00 24.42 ? 5   TRP A CG  1 
ATOM   7    C  CD1 . TRP A 1 5   ? 14.685  43.230 9.766  1.00 24.05 ? 5   TRP A CD1 1 
ATOM   8    C  CD2 . TRP A 1 5   ? 16.382  43.162 11.299 1.00 20.94 ? 5   TRP A CD2 1 
ATOM   9    N  NE1 . TRP A 1 5   ? 14.787  41.925 10.238 1.00 22.43 ? 5   TRP A NE1 1 
ATOM   10   C  CE2 . TRP A 1 5   ? 15.797  41.831 11.168 1.00 23.27 ? 5   TRP A CE2 1 
ATOM   11   C  CE3 . TRP A 1 5   ? 17.437  43.356 12.148 1.00 22.88 ? 5   TRP A CE3 1 
ATOM   12   C  CZ2 . TRP A 1 5   ? 16.284  40.741 11.889 1.00 20.97 ? 5   TRP A CZ2 1 
ATOM   13   C  CZ3 . TRP A 1 5   ? 17.950  42.252 12.867 1.00 21.82 ? 5   TRP A CZ3 1 
ATOM   14   C  CH2 . TRP A 1 5   ? 17.369  40.970 12.741 1.00 21.95 ? 5   TRP A CH2 1 
ATOM   15   N  N   . GLY A 1 6   ? 18.998  45.558 10.259 1.00 25.00 ? 6   GLY A N   1 
ATOM   16   C  CA  . GLY A 1 6   ? 20.272  44.969 10.646 1.00 23.22 ? 6   GLY A CA  1 
ATOM   17   C  C   . GLY A 1 6   ? 20.756  45.543 11.990 1.00 23.74 ? 6   GLY A C   1 
ATOM   18   O  O   . GLY A 1 6   ? 19.951  45.985 12.845 1.00 23.18 ? 6   GLY A O   1 
ATOM   19   N  N   . TYR A 1 7   ? 22.079  45.506 12.152 1.00 25.65 ? 7   TYR A N   1 
ATOM   20   C  CA  . TYR A 1 7   ? 22.722  46.074 13.331 1.00 27.87 ? 7   TYR A CA  1 
ATOM   21   C  C   . TYR A 1 7   ? 23.697  47.204 12.997 1.00 36.19 ? 7   TYR A C   1 
ATOM   22   O  O   . TYR A 1 7   ? 24.298  47.751 13.893 1.00 39.66 ? 7   TYR A O   1 
ATOM   23   C  CB  . TYR A 1 7   ? 23.445  44.969 14.093 1.00 26.27 ? 7   TYR A CB  1 
ATOM   24   C  CG  . TYR A 1 7   ? 22.440  44.030 14.722 1.00 25.90 ? 7   TYR A CG  1 
ATOM   25   C  CD1 . TYR A 1 7   ? 22.122  42.829 14.121 1.00 25.20 ? 7   TYR A CD1 1 
ATOM   26   C  CD2 . TYR A 1 7   ? 21.815  44.367 15.967 1.00 24.14 ? 7   TYR A CD2 1 
ATOM   27   C  CE1 . TYR A 1 7   ? 21.186  41.976 14.718 1.00 22.58 ? 7   TYR A CE1 1 
ATOM   28   C  CE2 . TYR A 1 7   ? 20.874  43.536 16.566 1.00 22.45 ? 7   TYR A CE2 1 
ATOM   29   C  CZ  . TYR A 1 7   ? 20.589  42.313 15.918 1.00 22.90 ? 7   TYR A CZ  1 
ATOM   30   O  OH  . TYR A 1 7   ? 19.704  41.385 16.423 1.00 21.12 ? 7   TYR A OH  1 
ATOM   31   N  N   . ASP A 1 8   ? 23.850  47.535 11.715 1.00 36.14 ? 8   ASP A N   1 
ATOM   32   C  CA  . ASP A 1 8   ? 24.774  48.606 11.333 1.00 39.72 ? 8   ASP A CA  1 
ATOM   33   C  C   . ASP A 1 8   ? 24.177  49.962 11.640 1.00 40.47 ? 8   ASP A C   1 
ATOM   34   O  O   . ASP A 1 8   ? 23.041  50.072 12.113 1.00 36.87 ? 8   ASP A O   1 
ATOM   35   C  CB  . ASP A 1 8   ? 25.249  48.461 9.870  1.00 41.01 ? 8   ASP A CB  1 
ATOM   36   C  CG  . ASP A 1 8   ? 26.021  47.161 9.642  1.00 48.43 ? 8   ASP A CG  1 
ATOM   37   O  OD1 . ASP A 1 8   ? 25.692  46.389 8.704  1.00 48.63 ? 8   ASP A OD1 1 
ATOM   38   O  OD2 . ASP A 1 8   ? 26.952  46.890 10.435 1.00 53.61 ? 8   ASP A OD2 1 
ATOM   39   N  N   . ASP A 1 9   ? 24.945  51.013 11.375 1.00 44.53 ? 9   ASP A N   1 
ATOM   40   C  CA  . ASP A 1 9   ? 24.472  52.354 11.666 1.00 48.32 ? 9   ASP A CA  1 
ATOM   41   C  C   . ASP A 1 9   ? 23.175  52.734 10.948 1.00 39.29 ? 9   ASP A C   1 
ATOM   42   O  O   . ASP A 1 9   ? 22.281  53.329 11.548 1.00 45.43 ? 9   ASP A O   1 
ATOM   43   C  CB  . ASP A 1 9   ? 25.566  53.395 11.412 1.00 55.86 ? 9   ASP A CB  1 
ATOM   44   C  CG  . ASP A 1 9   ? 26.262  53.828 12.693 1.00 70.39 ? 9   ASP A CG  1 
ATOM   45   O  OD1 . ASP A 1 9   ? 27.502  53.698 12.773 1.00 75.56 ? 9   ASP A OD1 1 
ATOM   46   O  OD2 . ASP A 1 9   ? 25.566  54.283 13.626 1.00 73.12 ? 9   ASP A OD2 1 
ATOM   47   N  N   . LYS A 1 10  ? 23.067  52.412 9.663  1.00 36.05 ? 10  LYS A N   1 
ATOM   48   C  CA  . LYS A 1 10  ? 21.882  52.811 8.911  1.00 36.19 ? 10  LYS A CA  1 
ATOM   49   C  C   . LYS A 1 10  ? 20.626  51.986 9.150  1.00 36.60 ? 10  LYS A C   1 
ATOM   50   O  O   . LYS A 1 10  ? 19.490  52.515 9.129  1.00 35.07 ? 10  LYS A O   1 
ATOM   51   C  CB  . LYS A 1 10  ? 22.161  52.829 7.417  1.00 39.29 ? 10  LYS A CB  1 
ATOM   52   C  CG  . LYS A 1 10  ? 21.201  53.754 6.654  1.00 42.11 ? 10  LYS A CG  1 
ATOM   53   C  CD  . LYS A 1 10  ? 22.093  54.717 5.854  1.00 45.01 ? 10  LYS A CD  1 
ATOM   54   C  CE  . LYS A 1 10  ? 21.516  55.169 4.536  1.00 45.01 ? 10  LYS A CE  1 
ATOM   55   N  NZ  . LYS A 1 10  ? 22.708  55.325 3.653  1.00 30.90 ? 10  LYS A NZ  1 
ATOM   56   N  N   . ASN A 1 11  ? 20.805  50.691 9.383  1.00 32.10 ? 11  ASN A N   1 
ATOM   57   C  CA  . ASN A 1 11  ? 19.596  49.836 9.470  1.00 30.73 ? 11  ASN A CA  1 
ATOM   58   C  C   . ASN A 1 11  ? 19.407  49.265 10.897 1.00 33.38 ? 11  ASN A C   1 
ATOM   59   O  O   . ASN A 1 11  ? 18.614  48.341 11.104 1.00 27.87 ? 11  ASN A O   1 
ATOM   60   C  CB  . ASN A 1 11  ? 19.712  48.714 8.450  1.00 31.85 ? 11  ASN A CB  1 
ATOM   61   C  CG  . ASN A 1 11  ? 20.949  47.856 8.653  1.00 29.55 ? 11  ASN A CG  1 
ATOM   62   O  OD1 . ASN A 1 11  ? 21.719  48.046 9.591  1.00 31.41 ? 11  ASN A OD1 1 
ATOM   63   N  ND2 . ASN A 1 11  ? 21.137  46.865 7.754  1.00 30.22 ? 11  ASN A ND2 1 
ATOM   64   N  N   . GLY A 1 12  ? 20.129  49.835 11.859 1.00 31.14 ? 12  GLY A N   1 
ATOM   65   C  CA  . GLY A 1 12  ? 20.326  49.142 13.136 1.00 25.70 ? 12  GLY A CA  1 
ATOM   66   C  C   . GLY A 1 12  ? 19.327  49.585 14.180 1.00 25.81 ? 12  GLY A C   1 
ATOM   67   O  O   . GLY A 1 12  ? 18.345  50.301 13.871 1.00 25.98 ? 12  GLY A O   1 
ATOM   68   N  N   . PRO A 1 13  ? 19.548  49.140 15.444 1.00 24.75 ? 13  PRO A N   1 
ATOM   69   C  CA  . PRO A 1 13  ? 18.539  49.302 16.485 1.00 24.74 ? 13  PRO A CA  1 
ATOM   70   C  C   . PRO A 1 13  ? 18.011  50.708 16.660 1.00 29.44 ? 13  PRO A C   1 
ATOM   71   O  O   . PRO A 1 13  ? 16.812  50.880 16.886 1.00 27.24 ? 13  PRO A O   1 
ATOM   72   C  CB  . PRO A 1 13  ? 19.253  48.822 17.745 1.00 25.75 ? 13  PRO A CB  1 
ATOM   73   C  CG  . PRO A 1 13  ? 20.140  47.772 17.226 1.00 22.77 ? 13  PRO A CG  1 
ATOM   74   C  CD  . PRO A 1 13  ? 20.607  48.194 15.854 1.00 26.59 ? 13  PRO A CD  1 
ATOM   75   N  N   . GLU A 1 14  ? 18.870  51.722 16.571 1.00 36.73 ? 14  GLU A N   1 
ATOM   76   C  CA  . GLU A 1 14  ? 18.379  53.100 16.809 1.00 38.09 ? 14  GLU A CA  1 
ATOM   77   C  C   . GLU A 1 14  ? 17.380  53.582 15.750 1.00 36.76 ? 14  GLU A C   1 
ATOM   78   O  O   . GLU A 1 14  ? 16.649  54.543 15.990 1.00 34.23 ? 14  GLU A O   1 
ATOM   79   C  CB  . GLU A 1 14  ? 19.530  54.122 17.032 1.00 47.32 ? 14  GLU A CB  1 
ATOM   80   C  CG  . GLU A 1 14  ? 19.726  54.513 18.504 1.00 58.46 ? 14  GLU A CG  1 
ATOM   81   N  N   . GLN A 1 15  ? 17.343  52.852 14.629 1.00 33.14 ? 15  GLN A N   1 
ATOM   82   C  CA  . GLN A 1 15  ? 16.505  53.128 13.451 1.00 33.33 ? 15  GLN A CA  1 
ATOM   83   C  C   . GLN A 1 15  ? 15.308  52.188 13.264 1.00 33.04 ? 15  GLN A C   1 
ATOM   84   O  O   . GLN A 1 15  ? 14.486  52.467 12.390 1.00 26.57 ? 15  GLN A O   1 
ATOM   85   C  CB  . GLN A 1 15  ? 17.321  53.004 12.146 1.00 38.17 ? 15  GLN A CB  1 
ATOM   86   C  CG  . GLN A 1 15  ? 18.619  53.783 12.114 1.00 45.46 ? 15  GLN A CG  1 
ATOM   87   C  CD  . GLN A 1 15  ? 18.484  55.229 12.619 1.00 46.02 ? 15  GLN A CD  1 
ATOM   88   O  OE1 . GLN A 1 15  ? 17.419  55.855 12.486 1.00 43.95 ? 15  GLN A OE1 1 
ATOM   89   N  NE2 . GLN A 1 15  ? 19.577  55.770 13.194 1.00 47.15 ? 15  GLN A NE2 1 
ATOM   90   N  N   . TRP A 1 16  ? 15.193  51.099 14.044 1.00 29.93 ? 16  TRP A N   1 
ATOM   91   C  CA  . TRP A 1 16  ? 14.094  50.125 13.804 1.00 26.01 ? 16  TRP A CA  1 
ATOM   92   C  C   . TRP A 1 16  ? 12.692  50.637 13.903 1.00 28.50 ? 16  TRP A C   1 
ATOM   93   O  O   . TRP A 1 16  ? 11.754  50.095 13.266 1.00 25.57 ? 16  TRP A O   1 
ATOM   94   C  CB  . TRP A 1 16  ? 14.236  48.899 14.729 1.00 24.00 ? 16  TRP A CB  1 
ATOM   95   C  CG  . TRP A 1 16  ? 15.444  48.086 14.491 1.00 21.64 ? 16  TRP A CG  1 
ATOM   96   C  CD1 . TRP A 1 16  ? 16.221  48.053 13.374 1.00 21.75 ? 16  TRP A CD1 1 
ATOM   97   C  CD2 . TRP A 1 16  ? 15.986  47.050 15.366 1.00 21.06 ? 16  TRP A CD2 1 
ATOM   98   N  NE1 . TRP A 1 16  ? 17.211  47.092 13.454 1.00 19.74 ? 16  TRP A NE1 1 
ATOM   99   C  CE2 . TRP A 1 16  ? 17.132  46.476 14.661 1.00 21.83 ? 16  TRP A CE2 1 
ATOM   100  C  CE3 . TRP A 1 16  ? 15.673  46.590 16.642 1.00 21.91 ? 16  TRP A CE3 1 
ATOM   101  C  CZ2 . TRP A 1 16  ? 17.936  45.470 15.221 1.00 21.27 ? 16  TRP A CZ2 1 
ATOM   102  C  CZ3 . TRP A 1 16  ? 16.470  45.583 17.183 1.00 20.74 ? 16  TRP A CZ3 1 
ATOM   103  C  CH2 . TRP A 1 16  ? 17.569  45.021 16.481 1.00 18.34 ? 16  TRP A CH2 1 
ATOM   104  N  N   . SER A 1 17  ? 12.487  51.684 14.693 1.00 25.52 ? 17  SER A N   1 
ATOM   105  C  CA  . SER A 1 17  ? 11.116  52.151 14.947 1.00 24.78 ? 17  SER A CA  1 
ATOM   106  C  C   . SER A 1 17  ? 10.459  52.717 13.668 1.00 24.27 ? 17  SER A C   1 
ATOM   107  O  O   . SER A 1 17  ? 9.230   52.736 13.601 1.00 25.87 ? 17  SER A O   1 
ATOM   108  C  CB  . SER A 1 17  ? 11.095  53.187 16.073 1.00 24.49 ? 17  SER A CB  1 
ATOM   109  O  OG  . SER A 1 17  ? 11.828  54.322 15.604 1.00 26.53 ? 17  SER A OG  1 
ATOM   110  N  N   . LYS A 1 18  ? 11.254  53.067 12.654 1.00 26.84 ? 18  LYS A N   1 
ATOM   111  C  CA  . LYS A 1 18  ? 10.717  53.770 11.442 1.00 29.60 ? 18  LYS A CA  1 
ATOM   112  C  C   . LYS A 1 18  ? 9.795   52.760 10.756 1.00 30.42 ? 18  LYS A C   1 
ATOM   113  O  O   . LYS A 1 18  ? 8.660   53.076 10.399 1.00 36.65 ? 18  LYS A O   1 
ATOM   114  C  CB  . LYS A 1 18  ? 11.853  54.199 10.506 1.00 30.20 ? 18  LYS A CB  1 
ATOM   115  C  CG  . LYS A 1 18  ? 12.636  55.425 10.988 1.00 33.16 ? 18  LYS A CG  1 
ATOM   116  C  CD  . LYS A 1 18  ? 13.864  55.622 10.113 1.00 36.41 ? 18  LYS A CD  1 
ATOM   117  C  CE  . LYS A 1 18  ? 14.655  56.865 10.450 1.00 39.90 ? 18  LYS A CE  1 
ATOM   118  N  NZ  . LYS A 1 18  ? 15.951  56.778 9.715  1.00 38.77 ? 18  LYS A NZ  1 
ATOM   119  N  N   . LEU A 1 19  ? 10.296  51.523 10.645 1.00 33.12 ? 19  LEU A N   1 
ATOM   120  C  CA  . LEU A 1 19  ? 9.531   50.381 10.058 1.00 29.77 ? 19  LEU A CA  1 
ATOM   121  C  C   . LEU A 1 19  ? 8.720   49.527 11.071 1.00 29.64 ? 19  LEU A C   1 
ATOM   122  O  O   . LEU A 1 19  ? 7.686   48.930 10.733 1.00 25.29 ? 19  LEU A O   1 
ATOM   123  C  CB  . LEU A 1 19  ? 10.475  49.477 9.248  1.00 32.76 ? 19  LEU A CB  1 
ATOM   124  C  CG  . LEU A 1 19  ? 11.374  50.113 8.151  1.00 38.83 ? 19  LEU A CG  1 
ATOM   125  C  CD1 . LEU A 1 19  ? 12.592  49.271 7.806  1.00 39.37 ? 19  LEU A CD1 1 
ATOM   126  C  CD2 . LEU A 1 19  ? 10.619  50.539 6.887  1.00 43.93 ? 19  LEU A CD2 1 
ATOM   127  N  N   . TYR A 1 20  ? 9.210   49.417 12.308 1.00 24.74 ? 20  TYR A N   1 
ATOM   128  C  CA  . TYR A 1 20  ? 8.477   48.684 13.351 1.00 23.89 ? 20  TYR A CA  1 
ATOM   129  C  C   . TYR A 1 20  ? 8.270   49.583 14.509 1.00 26.50 ? 20  TYR A C   1 
ATOM   130  O  O   . TYR A 1 20  ? 9.168   49.625 15.398 1.00 21.79 ? 20  TYR A O   1 
ATOM   131  C  CB  . TYR A 1 20  ? 9.295   47.442 13.841 1.00 21.92 ? 20  TYR A CB  1 
ATOM   132  C  CG  . TYR A 1 20  ? 9.792   46.627 12.653 1.00 25.71 ? 20  TYR A CG  1 
ATOM   133  C  CD1 . TYR A 1 20  ? 10.985  46.916 12.054 1.00 27.73 ? 20  TYR A CD1 1 
ATOM   134  C  CD2 . TYR A 1 20  ? 9.005   45.585 12.148 1.00 31.30 ? 20  TYR A CD2 1 
ATOM   135  C  CE1 . TYR A 1 20  ? 11.406  46.218 10.923 1.00 32.41 ? 20  TYR A CE1 1 
ATOM   136  C  CE2 . TYR A 1 20  ? 9.392   44.883 11.033 1.00 28.27 ? 20  TYR A CE2 1 
ATOM   137  C  CZ  . TYR A 1 20  ? 10.606  45.181 10.442 1.00 28.06 ? 20  TYR A CZ  1 
ATOM   138  O  OH  . TYR A 1 20  ? 11.007  44.451 9.316  1.00 35.22 ? 20  TYR A OH  1 
ATOM   139  N  N   . PRO A 1 21  ? 7.097   50.251 14.569 1.00 24.93 ? 21  PRO A N   1 
ATOM   140  C  CA  . PRO A 1 21  ? 6.798   51.266 15.610 1.00 27.27 ? 21  PRO A CA  1 
ATOM   141  C  C   . PRO A 1 21  ? 6.724   50.675 17.015 1.00 28.97 ? 21  PRO A C   1 
ATOM   142  O  O   . PRO A 1 21  ? 6.926   51.421 17.968 1.00 26.17 ? 21  PRO A O   1 
ATOM   143  C  CB  . PRO A 1 21  ? 5.395   51.784 15.200 1.00 30.04 ? 21  PRO A CB  1 
ATOM   144  C  CG  . PRO A 1 21  ? 5.400   51.649 13.699 1.00 26.79 ? 21  PRO A CG  1 
ATOM   145  C  CD  . PRO A 1 21  ? 6.158   50.343 13.424 1.00 26.20 ? 21  PRO A CD  1 
ATOM   146  N  N   . ILE A 1 22  ? 6.464   49.340 17.142 1.00 26.66 ? 22  ILE A N   1 
ATOM   147  C  CA  . ILE A 1 22  ? 6.500   48.660 18.419 1.00 24.64 ? 22  ILE A CA  1 
ATOM   148  C  C   . ILE A 1 22  ? 7.898   48.815 19.128 1.00 21.98 ? 22  ILE A C   1 
ATOM   149  O  O   . ILE A 1 22  ? 7.955   48.629 20.341 1.00 25.97 ? 22  ILE A O   1 
ATOM   150  C  CB  . ILE A 1 22  ? 6.031   47.158 18.321 1.00 21.96 ? 22  ILE A CB  1 
ATOM   151  C  CG1 . ILE A 1 22  ? 5.522   46.651 19.676 1.00 24.16 ? 22  ILE A CG1 1 
ATOM   152  C  CG2 . ILE A 1 22  ? 7.159   46.249 17.809 1.00 25.51 ? 22  ILE A CG2 1 
ATOM   153  C  CD1 . ILE A 1 22  ? 4.241   47.305 20.247 1.00 24.17 ? 22  ILE A CD1 1 
ATOM   154  N  N   . ALA A 1 23  ? 8.951   49.181 18.400 1.00 22.02 ? 23  ALA A N   1 
ATOM   155  C  CA  . ALA A 1 23  ? 10.311  49.351 18.963 1.00 22.94 ? 23  ALA A CA  1 
ATOM   156  C  C   . ALA A 1 23  ? 10.274  50.318 20.151 1.00 27.49 ? 23  ALA A C   1 
ATOM   157  O  O   . ALA A 1 23  ? 11.065  50.197 21.082 1.00 26.93 ? 23  ALA A O   1 
ATOM   158  C  CB  . ALA A 1 23  ? 11.300  49.801 17.933 1.00 23.85 ? 23  ALA A CB  1 
ATOM   159  N  N   . ASN A 1 24  ? 9.347   51.252 20.118 1.00 27.29 ? 24  ASN A N   1 
ATOM   160  C  CA  . ASN A 1 24  ? 9.150   52.173 21.266 1.00 28.93 ? 24  ASN A CA  1 
ATOM   161  C  C   . ASN A 1 24  ? 8.023   51.802 22.205 1.00 30.66 ? 24  ASN A C   1 
ATOM   162  O  O   . ASN A 1 24  ? 7.517   52.668 22.905 1.00 32.48 ? 24  ASN A O   1 
ATOM   163  C  CB  . ASN A 1 24  ? 8.928   53.608 20.778 1.00 29.18 ? 24  ASN A CB  1 
ATOM   164  C  CG  . ASN A 1 24  ? 10.105  54.148 19.966 1.00 30.30 ? 24  ASN A CG  1 
ATOM   165  O  OD1 . ASN A 1 24  ? 9.891   54.822 18.960 1.00 35.89 ? 24  ASN A OD1 1 
ATOM   166  N  ND2 . ASN A 1 24  ? 11.342  53.855 20.384 1.00 31.43 ? 24  ASN A ND2 1 
ATOM   167  N  N   . GLY A 1 25  ? 7.622   50.527 22.246 1.00 29.51 ? 25  GLY A N   1 
ATOM   168  C  CA  . GLY A 1 25  ? 6.474   50.093 23.024 1.00 27.88 ? 25  GLY A CA  1 
ATOM   169  C  C   . GLY A 1 25  ? 6.786   49.997 24.508 1.00 26.16 ? 25  GLY A C   1 
ATOM   170  O  O   . GLY A 1 25  ? 7.873   50.409 24.915 1.00 29.56 ? 25  GLY A O   1 
ATOM   171  N  N   . ASN A 1 26  ? 5.856   49.423 25.274 1.00 25.43 ? 26  ASN A N   1 
ATOM   172  C  CA  . ASN A 1 26  ? 5.943   49.410 26.717 1.00 25.85 ? 26  ASN A CA  1 
ATOM   173  C  C   . ASN A 1 26  ? 6.545   48.131 27.212 1.00 25.44 ? 26  ASN A C   1 
ATOM   174  O  O   . ASN A 1 26  ? 6.798   48.013 28.391 1.00 24.20 ? 26  ASN A O   1 
ATOM   175  C  CB  . ASN A 1 26  ? 4.579   49.625 27.347 1.00 29.65 ? 26  ASN A CB  1 
ATOM   176  C  CG  . ASN A 1 26  ? 4.092   51.032 27.142 1.00 33.44 ? 26  ASN A CG  1 
ATOM   177  O  OD1 . ASN A 1 26  ? 4.899   51.968 27.021 1.00 37.08 ? 26  ASN A OD1 1 
ATOM   178  N  ND2 . ASN A 1 26  ? 2.790   51.186 27.031 1.00 33.94 ? 26  ASN A ND2 1 
ATOM   179  N  N   . ASN A 1 27  ? 6.725   47.143 26.320 1.00 24.34 ? 27  ASN A N   1 
ATOM   180  C  CA  . ASN A 1 27  ? 7.249   45.844 26.751 1.00 23.68 ? 27  ASN A CA  1 
ATOM   181  C  C   . ASN A 1 27  ? 8.421   45.376 25.890 1.00 22.23 ? 27  ASN A C   1 
ATOM   182  O  O   . ASN A 1 27  ? 8.436   44.186 25.499 1.00 23.24 ? 27  ASN A O   1 
ATOM   183  C  CB  . ASN A 1 27  ? 6.168   44.747 26.715 1.00 24.48 ? 27  ASN A CB  1 
ATOM   184  C  CG  . ASN A 1 27  ? 4.942   45.090 27.557 1.00 28.44 ? 27  ASN A CG  1 
ATOM   185  O  OD1 . ASN A 1 27  ? 3.989   45.735 27.073 1.00 33.53 ? 27  ASN A OD1 1 
ATOM   186  N  ND2 . ASN A 1 27  ? 4.973   44.738 28.784 1.00 28.34 ? 27  ASN A ND2 1 
ATOM   187  N  N   . GLN A 1 28  ? 9.355   46.273 25.601 1.00 20.57 ? 28  GLN A N   1 
ATOM   188  C  CA  . GLN A 1 28  ? 10.514  45.955 24.728 1.00 19.56 ? 28  GLN A CA  1 
ATOM   189  C  C   . GLN A 1 28  ? 11.665  45.341 25.472 1.00 21.44 ? 28  GLN A C   1 
ATOM   190  O  O   . GLN A 1 28  ? 11.840  45.567 26.661 1.00 18.01 ? 28  GLN A O   1 
ATOM   191  C  CB  . GLN A 1 28  ? 10.972  47.194 24.013 1.00 21.28 ? 28  GLN A CB  1 
ATOM   192  C  CG  . GLN A 1 28  ? 9.942   47.625 22.963 1.00 21.96 ? 28  GLN A CG  1 
ATOM   193  C  CD  . GLN A 1 28  ? 9.832   46.571 21.878 1.00 20.80 ? 28  GLN A CD  1 
ATOM   194  O  OE1 . GLN A 1 28  ? 10.767  46.387 21.134 1.00 21.68 ? 28  GLN A OE1 1 
ATOM   195  N  NE2 . GLN A 1 28  ? 8.708   45.861 21.830 1.00 20.46 ? 28  GLN A NE2 1 
ATOM   196  N  N   . SER A 1 29  ? 12.407  44.489 24.772 1.00 21.03 ? 29  SER A N   1 
ATOM   197  C  CA  . SER A 1 29  ? 13.547  43.729 25.400 1.00 19.31 ? 29  SER A CA  1 
ATOM   198  C  C   . SER A 1 29  ? 14.743  43.972 24.535 1.00 18.94 ? 29  SER A C   1 
ATOM   199  O  O   . SER A 1 29  ? 14.601  44.214 23.335 1.00 19.12 ? 29  SER A O   1 
ATOM   200  C  CB  . SER A 1 29  ? 13.222  42.245 25.416 1.00 17.51 ? 29  SER A CB  1 
ATOM   201  O  OG  . SER A 1 29  ? 12.200  41.945 26.329 1.00 16.27 ? 29  SER A OG  1 
ATOM   202  N  N   . PRO A 1 30  ? 15.995  43.879 25.079 1.00 17.72 ? 30  PRO A N   1 
ATOM   203  C  CA  . PRO A 1 30  ? 16.235  43.405 26.429 1.00 18.36 ? 30  PRO A CA  1 
ATOM   204  C  C   . PRO A 1 30  ? 16.155  44.598 27.396 1.00 19.63 ? 30  PRO A C   1 
ATOM   205  O  O   . PRO A 1 30  ? 15.826  45.698 27.020 1.00 19.54 ? 30  PRO A O   1 
ATOM   206  C  CB  . PRO A 1 30  ? 17.697  42.989 26.368 1.00 16.66 ? 30  PRO A CB  1 
ATOM   207  C  CG  . PRO A 1 30  ? 18.320  43.951 25.383 1.00 19.34 ? 30  PRO A CG  1 
ATOM   208  C  CD  . PRO A 1 30  ? 17.245  43.934 24.293 1.00 18.83 ? 30  PRO A CD  1 
ATOM   209  N  N   . VAL A 1 31  ? 16.511  44.310 28.637 1.00 17.59 ? 31  VAL A N   1 
ATOM   210  C  CA  . VAL A 1 31  ? 16.410  45.336 29.715 1.00 19.81 ? 31  VAL A CA  1 
ATOM   211  C  C   . VAL A 1 31  ? 17.668  45.178 30.582 1.00 19.50 ? 31  VAL A C   1 
ATOM   212  O  O   . VAL A 1 31  ? 18.255  44.117 30.608 1.00 17.92 ? 31  VAL A O   1 
ATOM   213  C  CB  . VAL A 1 31  ? 15.106  45.210 30.578 1.00 16.32 ? 31  VAL A CB  1 
ATOM   214  C  CG1 . VAL A 1 31  ? 13.832  45.489 29.740 1.00 16.41 ? 31  VAL A CG1 1 
ATOM   215  C  CG2 . VAL A 1 31  ? 15.002  43.883 31.339 1.00 16.56 ? 31  VAL A CG2 1 
ATOM   216  N  N   . ASP A 1 32  ? 18.005  46.256 31.271 1.00 20.34 ? 32  ASP A N   1 
ATOM   217  C  CA  . ASP A 1 32  ? 18.904  46.189 32.459 1.00 22.90 ? 32  ASP A CA  1 
ATOM   218  C  C   . ASP A 1 32  ? 18.120  45.747 33.692 1.00 23.00 ? 32  ASP A C   1 
ATOM   219  O  O   . ASP A 1 32  ? 17.071  46.342 34.074 1.00 26.77 ? 32  ASP A O   1 
ATOM   220  C  CB  . ASP A 1 32  ? 19.523  47.530 32.728 1.00 22.66 ? 32  ASP A CB  1 
ATOM   221  C  CG  . ASP A 1 32  ? 20.510  47.477 33.914 1.00 27.15 ? 32  ASP A CG  1 
ATOM   222  O  OD1 . ASP A 1 32  ? 20.407  48.355 34.819 1.00 28.58 ? 32  ASP A OD1 1 
ATOM   223  O  OD2 . ASP A 1 32  ? 21.330  46.537 33.931 1.00 23.00 ? 32  ASP A OD2 1 
ATOM   224  N  N   . ILE A 1 33  ? 18.588  44.686 34.322 1.00 21.58 ? 33  ILE A N   1 
ATOM   225  C  CA  . ILE A 1 33  ? 17.932  44.133 35.476 1.00 19.00 ? 33  ILE A CA  1 
ATOM   226  C  C   . ILE A 1 33  ? 18.623  44.786 36.682 1.00 24.53 ? 33  ILE A C   1 
ATOM   227  O  O   . ILE A 1 33  ? 19.788  44.530 36.948 1.00 22.45 ? 33  ILE A O   1 
ATOM   228  C  CB  . ILE A 1 33  ? 18.143  42.618 35.568 1.00 21.52 ? 33  ILE A CB  1 
ATOM   229  C  CG1 . ILE A 1 33  ? 17.359  41.930 34.420 1.00 20.68 ? 33  ILE A CG1 1 
ATOM   230  C  CG2 . ILE A 1 33  ? 17.540  42.047 36.862 1.00 20.79 ? 33  ILE A CG2 1 
ATOM   231  C  CD1 . ILE A 1 33  ? 17.453  40.425 34.410 1.00 23.51 ? 33  ILE A CD1 1 
ATOM   232  N  N   . LYS A 1 34  ? 17.872  45.620 37.403 1.00 23.36 ? 34  LYS A N   1 
ATOM   233  C  CA  . LYS A 1 34  ? 18.407  46.292 38.622 1.00 25.43 ? 34  LYS A CA  1 
ATOM   234  C  C   . LYS A 1 34  ? 18.001  45.474 39.845 1.00 22.65 ? 34  LYS A C   1 
ATOM   235  O  O   . LYS A 1 34  ? 16.783  45.377 40.182 1.00 24.08 ? 34  LYS A O   1 
ATOM   236  C  CB  . LYS A 1 34  ? 17.861  47.702 38.691 1.00 24.58 ? 34  LYS A CB  1 
ATOM   237  C  CG  . LYS A 1 34  ? 18.535  48.653 37.734 1.00 32.72 ? 34  LYS A CG  1 
ATOM   238  C  CD  . LYS A 1 34  ? 17.746  49.956 37.566 1.00 38.54 ? 34  LYS A CD  1 
ATOM   239  C  CE  . LYS A 1 34  ? 18.488  50.920 36.637 1.00 39.72 ? 34  LYS A CE  1 
ATOM   240  N  NZ  . LYS A 1 34  ? 18.699  50.292 35.271 1.00 40.16 ? 34  LYS A NZ  1 
ATOM   241  N  N   . THR A 1 35  ? 18.969  44.813 40.499 1.00 21.99 ? 35  THR A N   1 
ATOM   242  C  CA  . THR A 1 35  ? 18.594  43.739 41.424 1.00 23.35 ? 35  THR A CA  1 
ATOM   243  C  C   . THR A 1 35  ? 17.981  44.318 42.726 1.00 27.08 ? 35  THR A C   1 
ATOM   244  O  O   . THR A 1 35  ? 17.239  43.606 43.415 1.00 28.21 ? 35  THR A O   1 
ATOM   245  C  CB  . THR A 1 35  ? 19.799  42.832 41.750 1.00 27.49 ? 35  THR A CB  1 
ATOM   246  O  OG1 . THR A 1 35  ? 20.913  43.667 42.155 1.00 28.96 ? 35  THR A OG1 1 
ATOM   247  C  CG2 . THR A 1 35  ? 20.225  42.087 40.509 1.00 29.43 ? 35  THR A CG2 1 
ATOM   248  N  N   . SER A 1 36  ? 18.284  45.582 43.008 1.00 28.31 ? 36  SER A N   1 
ATOM   249  C  CA  . SER A 1 36  ? 17.701  46.303 44.198 1.00 31.21 ? 36  SER A CA  1 
ATOM   250  C  C   . SER A 1 36  ? 16.217  46.580 43.946 1.00 34.42 ? 36  SER A C   1 
ATOM   251  O  O   . SER A 1 36  ? 15.429  46.715 44.897 1.00 38.39 ? 36  SER A O   1 
ATOM   252  C  CB  . SER A 1 36  ? 18.458  47.610 44.484 1.00 27.95 ? 36  SER A CB  1 
ATOM   253  O  OG  . SER A 1 36  ? 18.226  48.585 43.468 1.00 36.73 ? 36  SER A OG  1 
ATOM   254  N  N   . GLU A 1 37  ? 15.826  46.620 42.660 1.00 31.03 ? 37  GLU A N   1 
ATOM   255  C  CA  . GLU A 1 37  ? 14.422  46.830 42.264 1.00 29.82 ? 37  GLU A CA  1 
ATOM   256  C  C   . GLU A 1 37  ? 13.577  45.577 41.888 1.00 30.28 ? 37  GLU A C   1 
ATOM   257  O  O   . GLU A 1 37  ? 12.388  45.699 41.560 1.00 29.90 ? 37  GLU A O   1 
ATOM   258  C  CB  . GLU A 1 37  ? 14.330  47.924 41.178 1.00 29.67 ? 37  GLU A CB  1 
ATOM   259  C  CG  . GLU A 1 37  ? 14.931  49.277 41.507 1.00 33.03 ? 37  GLU A CG  1 
ATOM   260  C  CD  . GLU A 1 37  ? 14.740  50.311 40.385 1.00 40.59 ? 37  GLU A CD  1 
ATOM   261  O  OE1 . GLU A 1 37  ? 13.978  50.051 39.429 1.00 42.91 ? 37  GLU A OE1 1 
ATOM   262  O  OE2 . GLU A 1 37  ? 15.357  51.409 40.420 1.00 36.96 ? 37  GLU A OE2 1 
ATOM   263  N  N   . THR A 1 38  ? 14.151  44.379 41.968 1.00 28.81 ? 38  THR A N   1 
ATOM   264  C  CA  . THR A 1 38  ? 13.438  43.153 41.656 1.00 29.30 ? 38  THR A CA  1 
ATOM   265  C  C   . THR A 1 38  ? 12.509  42.743 42.780 1.00 35.92 ? 38  THR A C   1 
ATOM   266  O  O   . THR A 1 38  ? 12.776  43.015 43.953 1.00 37.44 ? 38  THR A O   1 
ATOM   267  C  CB  . THR A 1 38  ? 14.395  41.960 41.363 1.00 28.72 ? 38  THR A CB  1 
ATOM   268  O  OG1 . THR A 1 38  ? 15.289  41.711 42.496 1.00 27.23 ? 38  THR A OG1 1 
ATOM   269  C  CG2 . THR A 1 38  ? 15.223  42.322 40.179 1.00 25.15 ? 38  THR A CG2 1 
ATOM   270  N  N   . LYS A 1 39  ? 11.435  42.050 42.449 1.00 35.48 ? 39  LYS A N   1 
ATOM   271  C  CA  . LYS A 1 39  ? 10.624  41.535 43.535 1.00 38.93 ? 39  LYS A CA  1 
ATOM   272  C  C   . LYS A 1 39  ? 10.660  40.036 43.674 1.00 40.80 ? 39  LYS A C   1 
ATOM   273  O  O   . LYS A 1 39  ? 10.330  39.297 42.728 1.00 36.40 ? 39  LYS A O   1 
ATOM   274  C  CB  . LYS A 1 39  ? 9.193   42.074 43.465 1.00 46.06 ? 39  LYS A CB  1 
ATOM   275  N  N   . HIS A 1 40  ? 11.070  39.578 44.862 1.00 41.12 ? 40  HIS A N   1 
ATOM   276  C  CA  . HIS A 1 40  ? 11.111  38.144 45.152 1.00 50.10 ? 40  HIS A CA  1 
ATOM   277  C  C   . HIS A 1 40  ? 9.684   37.682 45.170 1.00 49.70 ? 40  HIS A C   1 
ATOM   278  O  O   . HIS A 1 40  ? 8.842   38.270 45.831 1.00 59.09 ? 40  HIS A O   1 
ATOM   279  C  CB  . HIS A 1 40  ? 11.856  37.843 46.468 1.00 56.55 ? 40  HIS A CB  1 
ATOM   280  C  CG  . HIS A 1 40  ? 11.861  36.375 46.847 1.00 66.08 ? 40  HIS A CG  1 
ATOM   281  N  ND1 . HIS A 1 40  ? 12.508  35.435 46.122 1.00 71.70 ? 40  HIS A ND1 1 
ATOM   282  C  CD2 . HIS A 1 40  ? 11.256  35.696 47.912 1.00 77.97 ? 40  HIS A CD2 1 
ATOM   283  C  CE1 . HIS A 1 40  ? 12.332  34.214 46.688 1.00 72.11 ? 40  HIS A CE1 1 
ATOM   284  N  NE2 . HIS A 1 40  ? 11.564  34.373 47.781 1.00 80.69 ? 40  HIS A NE2 1 
ATOM   285  N  N   . ASP A 1 41  ? 9.383   36.659 44.387 1.00 50.90 ? 41  ASP A N   1 
ATOM   286  C  CA  . ASP A 1 41  ? 8.044   36.135 44.287 1.00 46.78 ? 41  ASP A CA  1 
ATOM   287  C  C   . ASP A 1 41  ? 8.050   34.626 44.553 1.00 51.20 ? 41  ASP A C   1 
ATOM   288  O  O   . ASP A 1 41  ? 8.764   33.867 43.884 1.00 51.65 ? 41  ASP A O   1 
ATOM   289  C  CB  . ASP A 1 41  ? 7.453   36.484 42.929 1.00 48.84 ? 41  ASP A CB  1 
ATOM   290  C  CG  . ASP A 1 41  ? 6.055   35.963 42.758 1.00 54.97 ? 41  ASP A CG  1 
ATOM   291  O  OD1 . ASP A 1 41  ? 5.727   34.911 43.362 1.00 61.29 ? 41  ASP A OD1 1 
ATOM   292  O  OD2 . ASP A 1 41  ? 5.281   36.602 42.005 1.00 55.17 ? 41  ASP A OD2 1 
ATOM   293  N  N   . THR A 1 42  ? 7.250   34.206 45.546 1.00 51.42 ? 42  THR A N   1 
ATOM   294  C  CA  . THR A 1 42  ? 7.263   32.831 46.056 1.00 51.78 ? 42  THR A CA  1 
ATOM   295  C  C   . THR A 1 42  ? 6.273   31.906 45.337 1.00 47.23 ? 42  THR A C   1 
ATOM   296  O  O   . THR A 1 42  ? 6.318   30.675 45.534 1.00 47.48 ? 42  THR A O   1 
ATOM   297  N  N   . SER A 1 43  ? 5.383   32.472 44.520 1.00 49.35 ? 43  SER A N   1 
ATOM   298  C  CA  . SER A 1 43  ? 4.498   31.646 43.675 1.00 48.74 ? 43  SER A CA  1 
ATOM   299  C  C   . SER A 1 43  ? 5.219   31.002 42.441 1.00 51.01 ? 43  SER A C   1 
ATOM   300  O  O   . SER A 1 43  ? 4.725   29.994 41.890 1.00 46.27 ? 43  SER A O   1 
ATOM   301  C  CB  . SER A 1 43  ? 3.288   32.437 43.210 1.00 50.26 ? 43  SER A CB  1 
ATOM   302  O  OG  . SER A 1 43  ? 3.677   33.420 42.270 1.00 54.66 ? 43  SER A OG  1 
ATOM   303  N  N   . LEU A 1 44  ? 6.347   31.603 42.011 1.00 46.39 ? 44  LEU A N   1 
ATOM   304  C  CA  . LEU A 1 44  ? 7.243   31.042 40.961 1.00 40.33 ? 44  LEU A CA  1 
ATOM   305  C  C   . LEU A 1 44  ? 7.731   29.654 41.298 1.00 38.89 ? 44  LEU A C   1 
ATOM   306  O  O   . LEU A 1 44  ? 8.366   29.451 42.317 1.00 47.56 ? 44  LEU A O   1 
ATOM   307  C  CB  . LEU A 1 44  ? 8.471   31.935 40.722 1.00 35.35 ? 44  LEU A CB  1 
ATOM   308  C  CG  . LEU A 1 44  ? 8.239   33.325 40.113 1.00 35.13 ? 44  LEU A CG  1 
ATOM   309  C  CD1 . LEU A 1 44  ? 9.512   34.144 40.100 1.00 32.10 ? 44  LEU A CD1 1 
ATOM   310  C  CD2 . LEU A 1 44  ? 7.625   33.263 38.719 1.00 32.64 ? 44  LEU A CD2 1 
ATOM   311  N  N   . LYS A 1 45  ? 7.453   28.696 40.427 1.00 35.78 ? 45  LYS A N   1 
ATOM   312  C  CA  . LYS A 1 45  ? 8.006   27.374 40.557 1.00 35.57 ? 45  LYS A CA  1 
ATOM   313  C  C   . LYS A 1 45  ? 9.416   27.289 39.897 1.00 32.16 ? 45  LYS A C   1 
ATOM   314  O  O   . LYS A 1 45  ? 9.833   28.223 39.161 1.00 31.27 ? 45  LYS A O   1 
ATOM   315  C  CB  . LYS A 1 45  ? 7.015   26.355 39.995 1.00 39.47 ? 45  LYS A CB  1 
ATOM   316  C  CG  . LYS A 1 45  ? 5.692   26.393 40.735 1.00 42.87 ? 45  LYS A CG  1 
ATOM   317  C  CD  . LYS A 1 45  ? 4.621   25.590 40.020 1.00 55.85 ? 45  LYS A CD  1 
ATOM   318  N  N   . PRO A 1 46  ? 10.161  26.204 40.175 1.00 33.60 ? 46  PRO A N   1 
ATOM   319  C  CA  . PRO A 1 46  ? 11.427  26.088 39.447 1.00 34.94 ? 46  PRO A CA  1 
ATOM   320  C  C   . PRO A 1 46  ? 11.149  25.815 37.959 1.00 32.41 ? 46  PRO A C   1 
ATOM   321  O  O   . PRO A 1 46  ? 10.102  25.283 37.609 1.00 28.95 ? 46  PRO A O   1 
ATOM   322  C  CB  . PRO A 1 46  ? 12.089  24.845 40.066 1.00 34.69 ? 46  PRO A CB  1 
ATOM   323  C  CG  . PRO A 1 46  ? 11.479  24.775 41.463 1.00 38.19 ? 46  PRO A CG  1 
ATOM   324  C  CD  . PRO A 1 46  ? 10.050  25.203 41.259 1.00 37.59 ? 46  PRO A CD  1 
ATOM   325  N  N   . ILE A 1 47  ? 12.101  26.208 37.118 1.00 33.14 ? 47  ILE A N   1 
ATOM   326  C  CA  . ILE A 1 47  ? 12.086  25.952 35.665 1.00 29.57 ? 47  ILE A CA  1 
ATOM   327  C  C   . ILE A 1 47  ? 12.395  24.470 35.458 1.00 28.38 ? 47  ILE A C   1 
ATOM   328  O  O   . ILE A 1 47  ? 13.333  23.950 36.026 1.00 30.26 ? 47  ILE A O   1 
ATOM   329  C  CB  . ILE A 1 47  ? 13.161  26.867 35.007 1.00 28.92 ? 47  ILE A CB  1 
ATOM   330  C  CG1 . ILE A 1 47  ? 12.616  28.280 34.888 1.00 31.60 ? 47  ILE A CG1 1 
ATOM   331  C  CG2 . ILE A 1 47  ? 13.715  26.317 33.692 1.00 33.79 ? 47  ILE A CG2 1 
ATOM   332  C  CD1 . ILE A 1 47  ? 11.336  28.395 34.134 1.00 28.48 ? 47  ILE A CD1 1 
ATOM   333  N  N   . SER A 1 48  ? 11.612  23.797 34.632 1.00 27.32 ? 48  SER A N   1 
ATOM   334  C  CA  . SER A 1 48  ? 11.905  22.429 34.247 1.00 33.08 ? 48  SER A CA  1 
ATOM   335  C  C   . SER A 1 48  ? 12.087  22.408 32.719 1.00 27.38 ? 48  SER A C   1 
ATOM   336  O  O   . SER A 1 48  ? 11.140  22.743 31.978 1.00 28.43 ? 48  SER A O   1 
ATOM   337  C  CB  . SER A 1 48  ? 10.794  21.481 34.733 1.00 36.27 ? 48  SER A CB  1 
ATOM   338  O  OG  . SER A 1 48  ? 10.310  20.620 33.717 1.00 47.49 ? 48  SER A OG  1 
ATOM   339  N  N   . VAL A 1 49  ? 13.294  22.037 32.280 1.00 25.19 ? 49  VAL A N   1 
ATOM   340  C  CA  . VAL A 1 49  ? 13.473  21.677 30.829 1.00 25.69 ? 49  VAL A CA  1 
ATOM   341  C  C   . VAL A 1 49  ? 13.684  20.193 30.580 1.00 25.57 ? 49  VAL A C   1 
ATOM   342  O  O   . VAL A 1 49  ? 14.380  19.508 31.348 1.00 27.21 ? 49  VAL A O   1 
ATOM   343  C  CB  . VAL A 1 49  ? 14.519  22.511 30.073 1.00 25.02 ? 49  VAL A CB  1 
ATOM   344  C  CG1 . VAL A 1 49  ? 14.083  23.948 30.051 1.00 26.59 ? 49  VAL A CG1 1 
ATOM   345  C  CG2 . VAL A 1 49  ? 15.929  22.340 30.656 1.00 28.42 ? 49  VAL A CG2 1 
ATOM   346  N  N   . SER A 1 50  ? 13.055  19.674 29.511 1.00 25.23 ? 50  SER A N   1 
ATOM   347  C  CA  . SER A 1 50  ? 13.225  18.256 29.135 1.00 24.04 ? 50  SER A CA  1 
ATOM   348  C  C   . SER A 1 50  ? 13.236  18.242 27.612 1.00 25.25 ? 50  SER A C   1 
ATOM   349  O  O   . SER A 1 50  ? 12.186  18.311 26.998 1.00 26.07 ? 50  SER A O   1 
ATOM   350  C  CB  . SER A 1 50  ? 12.009  17.464 29.619 1.00 30.40 ? 50  SER A CB  1 
ATOM   351  O  OG  . SER A 1 50  ? 12.190  16.082 29.361 1.00 34.16 ? 50  SER A OG  1 
ATOM   352  N  N   . TYR A 1 51  ? 14.413  18.159 27.029 1.00 25.10 ? 51  TYR A N   1 
ATOM   353  C  CA  . TYR A 1 51  ? 14.595  18.244 25.573 1.00 23.32 ? 51  TYR A CA  1 
ATOM   354  C  C   . TYR A 1 51  ? 15.154  16.944 25.080 1.00 27.15 ? 51  TYR A C   1 
ATOM   355  O  O   . TYR A 1 51  ? 16.132  16.458 25.631 1.00 32.49 ? 51  TYR A O   1 
ATOM   356  C  CB  . TYR A 1 51  ? 15.664  19.293 25.248 1.00 22.26 ? 51  TYR A CB  1 
ATOM   357  C  CG  . TYR A 1 51  ? 15.406  20.735 25.695 1.00 20.31 ? 51  TYR A CG  1 
ATOM   358  C  CD1 . TYR A 1 51  ? 16.477  21.539 26.087 1.00 17.94 ? 51  TYR A CD1 1 
ATOM   359  C  CD2 . TYR A 1 51  ? 14.135  21.244 25.779 1.00 19.73 ? 51  TYR A CD2 1 
ATOM   360  C  CE1 . TYR A 1 51  ? 16.293  22.858 26.468 1.00 20.54 ? 51  TYR A CE1 1 
ATOM   361  C  CE2 . TYR A 1 51  ? 13.905  22.572 26.183 1.00 17.73 ? 51  TYR A CE2 1 
ATOM   362  C  CZ  . TYR A 1 51  ? 14.995  23.380 26.531 1.00 17.98 ? 51  TYR A CZ  1 
ATOM   363  O  OH  . TYR A 1 51  ? 14.961  24.681 26.952 1.00 18.27 ? 51  TYR A OH  1 
ATOM   364  N  N   . ASN A 1 52  ? 14.601  16.434 23.988 1.00 25.39 ? 52  ASN A N   1 
ATOM   365  C  CA  . ASN A 1 52  ? 15.013  15.189 23.333 1.00 23.01 ? 52  ASN A CA  1 
ATOM   366  C  C   . ASN A 1 52  ? 16.009  15.548 22.220 1.00 21.50 ? 52  ASN A C   1 
ATOM   367  O  O   . ASN A 1 52  ? 15.692  16.375 21.330 1.00 22.46 ? 52  ASN A O   1 
ATOM   368  C  CB  . ASN A 1 52  ? 13.735  14.550 22.786 1.00 24.94 ? 52  ASN A CB  1 
ATOM   369  C  CG  . ASN A 1 52  ? 13.973  13.211 22.164 1.00 24.75 ? 52  ASN A CG  1 
ATOM   370  O  OD1 . ASN A 1 52  ? 15.042  12.927 21.625 1.00 26.71 ? 52  ASN A OD1 1 
ATOM   371  N  ND2 . ASN A 1 52  ? 12.954  12.378 22.213 1.00 25.57 ? 52  ASN A ND2 1 
ATOM   372  N  N   . PRO A 1 53  ? 17.259  15.025 22.268 1.00 22.91 ? 53  PRO A N   1 
ATOM   373  C  CA  . PRO A 1 53  ? 18.277  15.387 21.287 1.00 21.73 ? 53  PRO A CA  1 
ATOM   374  C  C   . PRO A 1 53  ? 17.889  15.030 19.833 1.00 21.46 ? 53  PRO A C   1 
ATOM   375  O  O   . PRO A 1 53  ? 18.356  15.658 18.968 1.00 23.95 ? 53  PRO A O   1 
ATOM   376  C  CB  . PRO A 1 53  ? 19.528  14.592 21.738 1.00 26.01 ? 53  PRO A CB  1 
ATOM   377  C  CG  . PRO A 1 53  ? 18.966  13.422 22.443 1.00 27.17 ? 53  PRO A CG  1 
ATOM   378  C  CD  . PRO A 1 53  ? 17.723  13.928 23.145 1.00 24.26 ? 53  PRO A CD  1 
ATOM   379  N  N   . ALA A 1 54  ? 17.003  14.059 19.643 1.00 25.85 ? 54  ALA A N   1 
ATOM   380  C  CA  . ALA A 1 54  ? 16.449  13.696 18.324 1.00 25.53 ? 54  ALA A CA  1 
ATOM   381  C  C   . ALA A 1 54  ? 15.634  14.858 17.674 1.00 28.17 ? 54  ALA A C   1 
ATOM   382  O  O   . ALA A 1 54  ? 15.412  14.847 16.448 1.00 26.62 ? 54  ALA A O   1 
ATOM   383  C  CB  . ALA A 1 54  ? 15.593  12.441 18.469 1.00 25.81 ? 54  ALA A CB  1 
ATOM   384  N  N   . THR A 1 55  ? 15.184  15.853 18.453 1.00 24.78 ? 55  THR A N   1 
ATOM   385  C  CA  . THR A 1 55  ? 14.532  17.016 17.804 1.00 23.68 ? 55  THR A CA  1 
ATOM   386  C  C   . THR A 1 55  ? 15.503  18.032 17.176 1.00 22.57 ? 55  THR A C   1 
ATOM   387  O  O   . THR A 1 55  ? 15.062  18.950 16.457 1.00 20.29 ? 55  THR A O   1 
ATOM   388  C  CB  . THR A 1 55  ? 13.611  17.772 18.785 1.00 22.85 ? 55  THR A CB  1 
ATOM   389  O  OG1 . THR A 1 55  ? 14.418  18.249 19.878 1.00 20.57 ? 55  THR A OG1 1 
ATOM   390  C  CG2 . THR A 1 55  ? 12.542  16.866 19.391 1.00 23.90 ? 55  THR A CG2 1 
ATOM   391  N  N   . ALA A 1 56  ? 16.811  17.950 17.425 1.00 21.10 ? 56  ALA A N   1 
ATOM   392  C  CA  . ALA A 1 56  ? 17.734  18.914 16.795 1.00 19.12 ? 56  ALA A CA  1 
ATOM   393  C  C   . ALA A 1 56  ? 17.672  18.705 15.227 1.00 20.54 ? 56  ALA A C   1 
ATOM   394  O  O   . ALA A 1 56  ? 17.713  17.557 14.767 1.00 20.35 ? 56  ALA A O   1 
ATOM   395  C  CB  . ALA A 1 56  ? 19.160  18.758 17.322 1.00 18.31 ? 56  ALA A CB  1 
ATOM   396  N  N   . LYS A 1 57  ? 17.534  19.778 14.458 1.00 18.52 ? 57  LYS A N   1 
ATOM   397  C  CA  . LYS A 1 57  ? 17.277  19.641 13.010 1.00 22.37 ? 57  LYS A CA  1 
ATOM   398  C  C   . LYS A 1 57  ? 18.360  20.262 12.102 1.00 22.62 ? 57  LYS A C   1 
ATOM   399  O  O   . LYS A 1 57  ? 18.923  19.574 11.245 1.00 24.93 ? 57  LYS A O   1 
ATOM   400  C  CB  . LYS A 1 57  ? 15.868  20.163 12.661 1.00 25.61 ? 57  LYS A CB  1 
ATOM   401  C  CG  . LYS A 1 57  ? 15.477  19.871 11.225 1.00 34.25 ? 57  LYS A CG  1 
ATOM   402  C  CD  . LYS A 1 57  ? 14.025  20.249 10.975 1.00 39.05 ? 57  LYS A CD  1 
ATOM   403  C  CE  . LYS A 1 57  ? 13.822  21.737 10.809 1.00 45.16 ? 57  LYS A CE  1 
ATOM   404  N  N   . GLU A 1 58  ? 18.660  21.557 12.246 1.00 18.75 ? 58  GLU A N   1 
ATOM   405  C  CA  . GLU A 1 58  ? 19.423  22.245 11.236 1.00 19.01 ? 58  GLU A CA  1 
ATOM   406  C  C   . GLU A 1 58  ? 20.084  23.458 11.861 1.00 20.71 ? 58  GLU A C   1 
ATOM   407  O  O   . GLU A 1 58  ? 19.608  23.997 12.825 1.00 20.59 ? 58  GLU A O   1 
ATOM   408  C  CB  . GLU A 1 58  ? 18.386  22.629 10.123 1.00 21.84 ? 58  GLU A CB  1 
ATOM   409  C  CG  . GLU A 1 58  ? 18.912  23.139 8.815  1.00 34.48 ? 58  GLU A CG  1 
ATOM   410  C  CD  . GLU A 1 58  ? 17.751  23.339 7.838  1.00 36.26 ? 58  GLU A CD  1 
ATOM   411  O  OE1 . GLU A 1 58  ? 18.021  23.175 6.604  1.00 43.09 ? 58  GLU A OE1 1 
ATOM   412  O  OE2 . GLU A 1 58  ? 16.597  23.603 8.318  1.00 30.28 ? 58  GLU A OE2 1 
ATOM   413  N  N   . ILE A 1 59  ? 21.227  23.830 11.324 1.00 18.91 ? 59  ILE A N   1 
ATOM   414  C  CA  . ILE A 1 59  ? 21.879  25.112 11.661 1.00 18.86 ? 59  ILE A CA  1 
ATOM   415  C  C   . ILE A 1 59  ? 21.928  26.019 10.428 1.00 19.89 ? 59  ILE A C   1 
ATOM   416  O  O   . ILE A 1 59  ? 22.194  25.495 9.278  1.00 23.67 ? 59  ILE A O   1 
ATOM   417  C  CB  . ILE A 1 59  ? 23.225  24.796 12.320 1.00 17.12 ? 59  ILE A CB  1 
ATOM   418  C  CG1 . ILE A 1 59  ? 23.850  26.097 12.814 1.00 15.62 ? 59  ILE A CG1 1 
ATOM   419  C  CG2 . ILE A 1 59  ? 24.165  24.085 11.352 1.00 20.42 ? 59  ILE A CG2 1 
ATOM   420  C  CD1 . ILE A 1 59  ? 25.072  25.855 13.698 1.00 15.62 ? 59  ILE A CD1 1 
ATOM   421  N  N   . ILE A 1 60  ? 21.617  27.304 10.595 1.00 19.34 ? 60  ILE A N   1 
ATOM   422  C  CA  . ILE A 1 60  ? 21.393  28.246 9.488  1.00 19.71 ? 60  ILE A CA  1 
ATOM   423  C  C   . ILE A 1 60  ? 22.068  29.566 9.757  1.00 22.70 ? 60  ILE A C   1 
ATOM   424  O  O   . ILE A 1 60  ? 21.878  30.184 10.826 1.00 22.09 ? 60  ILE A O   1 
ATOM   425  C  CB  . ILE A 1 60  ? 19.872  28.609 9.303  1.00 23.24 ? 60  ILE A CB  1 
ATOM   426  C  CG1 . ILE A 1 60  ? 19.024  27.332 9.338  1.00 30.14 ? 60  ILE A CG1 1 
ATOM   427  C  CG2 . ILE A 1 60  ? 19.673  29.470 8.033  1.00 23.11 ? 60  ILE A CG2 1 
ATOM   428  C  CD1 . ILE A 1 60  ? 17.559  27.529 9.058  1.00 35.84 ? 60  ILE A CD1 1 
ATOM   429  N  N   . ASN A 1 61  ? 22.792  30.068 8.747  1.00 21.37 ? 61  ASN A N   1 
ATOM   430  C  CA  . ASN A 1 61  ? 23.352  31.377 8.748  1.00 21.58 ? 61  ASN A CA  1 
ATOM   431  C  C   . ASN A 1 61  ? 22.297  32.315 8.213  1.00 24.22 ? 61  ASN A C   1 
ATOM   432  O  O   . ASN A 1 61  ? 21.916  32.251 7.005  1.00 22.40 ? 61  ASN A O   1 
ATOM   433  C  CB  . ASN A 1 61  ? 24.630  31.433 7.890  1.00 20.87 ? 61  ASN A CB  1 
ATOM   434  C  CG  . ASN A 1 61  ? 25.281  32.806 7.846  1.00 17.42 ? 61  ASN A CG  1 
ATOM   435  O  OD1 . ASN A 1 61  ? 24.660  33.897 7.802  1.00 21.40 ? 61  ASN A OD1 1 
ATOM   436  N  ND2 . ASN A 1 61  ? 26.632  32.791 7.885  1.00 19.86 ? 61  ASN A ND2 1 
ATOM   437  N  N   . VAL A 1 62  ? 21.792  33.188 9.089  1.00 22.32 ? 62  VAL A N   1 
ATOM   438  C  CA  . VAL A 1 62  ? 20.750  34.139 8.694  1.00 22.61 ? 62  VAL A CA  1 
ATOM   439  C  C   . VAL A 1 62  ? 21.259  35.564 8.464  1.00 20.10 ? 62  VAL A C   1 
ATOM   440  O  O   . VAL A 1 62  ? 20.499  36.542 8.560  1.00 26.35 ? 62  VAL A O   1 
ATOM   441  C  CB  . VAL A 1 62  ? 19.514  34.111 9.676  1.00 22.40 ? 62  VAL A CB  1 
ATOM   442  C  CG1 . VAL A 1 62  ? 18.872  32.736 9.711  1.00 24.25 ? 62  VAL A CG1 1 
ATOM   443  C  CG2 . VAL A 1 62  ? 19.918  34.503 11.103 1.00 23.34 ? 62  VAL A CG2 1 
ATOM   444  N  N   . GLY A 1 63  ? 22.551  35.728 8.147  1.00 22.85 ? 63  GLY A N   1 
ATOM   445  C  CA  . GLY A 1 63  ? 23.078  37.026 7.788  1.00 23.08 ? 63  GLY A CA  1 
ATOM   446  C  C   . GLY A 1 63  ? 23.525  37.886 8.946  1.00 26.54 ? 63  GLY A C   1 
ATOM   447  O  O   . GLY A 1 63  ? 24.698  38.228 9.026  1.00 27.09 ? 63  GLY A O   1 
ATOM   448  N  N   . HIS A 1 64  ? 22.616  38.130 9.910  1.00 26.96 ? 64  HIS A N   1 
ATOM   449  C  CA  . HIS A 1 64  ? 22.938  38.900 11.140 1.00 25.78 ? 64  HIS A CA  1 
ATOM   450  C  C   . HIS A 1 64  ? 23.356  38.025 12.328 1.00 24.76 ? 64  HIS A C   1 
ATOM   451  O  O   . HIS A 1 64  ? 23.905  38.555 13.308 1.00 22.57 ? 64  HIS A O   1 
ATOM   452  C  CB  . HIS A 1 64  ? 21.747  39.759 11.543 1.00 29.08 ? 64  HIS A CB  1 
ATOM   453  C  CG  . HIS A 1 64  ? 20.512  38.966 11.790 1.00 27.59 ? 64  HIS A CG  1 
ATOM   454  N  ND1 . HIS A 1 64  ? 20.196  38.438 13.059 1.00 24.80 ? 64  HIS A ND1 1 
ATOM   455  C  CD2 . HIS A 1 64  ? 19.480  38.566 10.915 1.00 27.95 ? 64  HIS A CD2 1 
ATOM   456  C  CE1 . HIS A 1 64  ? 19.026  37.743 12.958 1.00 27.30 ? 64  HIS A CE1 1 
ATOM   457  N  NE2 . HIS A 1 64  ? 18.593  37.816 11.641 1.00 27.07 ? 64  HIS A NE2 1 
ATOM   458  N  N   . SER A 1 65  ? 23.182  36.713 12.196 1.00 20.81 ? 65  SER A N   1 
ATOM   459  C  CA  . SER A 1 65  ? 23.394  35.729 13.241 1.00 20.33 ? 65  SER A CA  1 
ATOM   460  C  C   . SER A 1 65  ? 23.280  34.334 12.648 1.00 21.64 ? 65  SER A C   1 
ATOM   461  O  O   . SER A 1 65  ? 23.238  34.150 11.394 1.00 20.81 ? 65  SER A O   1 
ATOM   462  C  CB  . SER A 1 65  ? 22.270  35.931 14.277 1.00 24.04 ? 65  SER A CB  1 
ATOM   463  O  OG  . SER A 1 65  ? 22.579  35.136 15.429 1.00 22.84 ? 65  SER A OG  1 
ATOM   464  N  N   . PHE A 1 66  ? 23.275  33.301 13.485 1.00 16.73 ? 66  PHE A N   1 
ATOM   465  C  CA  . PHE A 1 66  ? 23.017  31.955 13.054 1.00 16.81 ? 66  PHE A CA  1 
ATOM   466  C  C   . PHE A 1 66  ? 22.026  31.354 14.028 1.00 18.70 ? 66  PHE A C   1 
ATOM   467  O  O   . PHE A 1 66  ? 22.009  31.809 15.191 1.00 18.53 ? 66  PHE A O   1 
ATOM   468  C  CB  . PHE A 1 66  ? 24.281  31.086 12.917 1.00 18.27 ? 66  PHE A CB  1 
ATOM   469  C  CG  . PHE A 1 66  ? 24.917  30.684 14.216 1.00 17.95 ? 66  PHE A CG  1 
ATOM   470  C  CD1 . PHE A 1 66  ? 24.583  29.462 14.815 1.00 20.89 ? 66  PHE A CD1 1 
ATOM   471  C  CD2 . PHE A 1 66  ? 25.815  31.549 14.817 1.00 20.08 ? 66  PHE A CD2 1 
ATOM   472  C  CE1 . PHE A 1 66  ? 25.183  29.106 16.048 1.00 21.54 ? 66  PHE A CE1 1 
ATOM   473  C  CE2 . PHE A 1 66  ? 26.455  31.173 16.014 1.00 19.69 ? 66  PHE A CE2 1 
ATOM   474  C  CZ  . PHE A 1 66  ? 26.122  29.982 16.633 1.00 16.64 ? 66  PHE A CZ  1 
ATOM   475  N  N   A HIS A 1 67  ? 21.235  30.363 13.600 0.50 17.50 ? 67  HIS A N   1 
ATOM   476  N  N   B HIS A 1 67  ? 21.302  30.327 13.649 0.50 17.04 ? 67  HIS A N   1 
ATOM   477  C  CA  A HIS A 1 67  ? 20.196  29.722 14.429 0.50 17.90 ? 67  HIS A CA  1 
ATOM   478  C  CA  B HIS A 1 67  ? 20.557  29.688 14.688 0.50 17.18 ? 67  HIS A CA  1 
ATOM   479  C  C   A HIS A 1 67  ? 20.394  28.262 14.388 0.50 17.66 ? 67  HIS A C   1 
ATOM   480  C  C   B HIS A 1 67  ? 20.367  28.272 14.409 0.50 17.33 ? 67  HIS A C   1 
ATOM   481  O  O   A HIS A 1 67  ? 20.809  27.766 13.329 0.50 18.88 ? 67  HIS A O   1 
ATOM   482  O  O   B HIS A 1 67  ? 20.585  27.814 13.273 0.50 18.76 ? 67  HIS A O   1 
ATOM   483  C  CB  A HIS A 1 67  ? 18.808  29.917 13.795 0.50 20.19 ? 67  HIS A CB  1 
ATOM   484  C  CB  B HIS A 1 67  ? 19.281  30.460 15.005 0.50 19.02 ? 67  HIS A CB  1 
ATOM   485  C  CG  A HIS A 1 67  ? 18.331  31.315 13.798 0.50 22.53 ? 67  HIS A CG  1 
ATOM   486  C  CG  B HIS A 1 67  ? 18.308  30.552 13.856 0.50 20.45 ? 67  HIS A CG  1 
ATOM   487  N  ND1 A HIS A 1 67  ? 17.226  31.699 13.140 0.50 22.60 ? 67  HIS A ND1 1 
ATOM   488  N  ND1 B HIS A 1 67  ? 17.869  31.727 13.380 0.50 21.93 ? 67  HIS A ND1 1 
ATOM   489  C  CD2 A HIS A 1 67  ? 18.840  32.450 14.417 0.50 25.28 ? 67  HIS A CD2 1 
ATOM   490  C  CD2 B HIS A 1 67  ? 17.701  29.570 13.091 0.50 22.88 ? 67  HIS A CD2 1 
ATOM   491  C  CE1 A HIS A 1 67  ? 17.034  33.021 13.327 0.50 24.91 ? 67  HIS A CE1 1 
ATOM   492  C  CE1 B HIS A 1 67  ? 16.993  31.521 12.386 0.50 23.73 ? 67  HIS A CE1 1 
ATOM   493  N  NE2 A HIS A 1 67  ? 18.003  33.473 14.134 0.50 24.83 ? 67  HIS A NE2 1 
ATOM   494  N  NE2 B HIS A 1 67  ? 16.895  30.202 12.186 0.50 23.79 ? 67  HIS A NE2 1 
ATOM   495  N  N   . VAL A 1 68  ? 20.053  27.544 15.470 1.00 17.13 ? 68  VAL A N   1 
ATOM   496  C  CA  . VAL A 1 68  ? 19.924  26.062 15.452 1.00 15.97 ? 68  VAL A CA  1 
ATOM   497  C  C   . VAL A 1 68  ? 18.455  25.780 15.688 1.00 18.03 ? 68  VAL A C   1 
ATOM   498  O  O   . VAL A 1 68  ? 17.851  26.180 16.724 1.00 17.33 ? 68  VAL A O   1 
ATOM   499  C  CB  . VAL A 1 68  ? 20.801  25.291 16.471 1.00 15.93 ? 68  VAL A CB  1 
ATOM   500  C  CG1 . VAL A 1 68  ? 20.429  23.788 16.447 1.00 14.99 ? 68  VAL A CG1 1 
ATOM   501  C  CG2 . VAL A 1 68  ? 22.294  25.487 16.193 1.00 17.93 ? 68  VAL A CG2 1 
ATOM   502  N  N   . ASN A 1 69  ? 17.826  25.215 14.665 1.00 15.80 ? 69  ASN A N   1 
ATOM   503  C  CA  . ASN A 1 69  ? 16.378  24.886 14.713 1.00 18.40 ? 69  ASN A CA  1 
ATOM   504  C  C   . ASN A 1 69  ? 16.103  23.468 15.127 1.00 16.92 ? 69  ASN A C   1 
ATOM   505  O  O   . ASN A 1 69  ? 16.935  22.573 14.858 1.00 19.61 ? 69  ASN A O   1 
ATOM   506  C  CB  . ASN A 1 69  ? 15.724  25.156 13.320 1.00 19.33 ? 69  ASN A CB  1 
ATOM   507  C  CG  . ASN A 1 69  ? 15.621  26.636 12.991 1.00 23.53 ? 69  ASN A CG  1 
ATOM   508  O  OD1 . ASN A 1 69  ? 15.490  27.501 13.876 1.00 26.42 ? 69  ASN A OD1 1 
ATOM   509  N  ND2 . ASN A 1 69  ? 15.725  26.931 11.700 1.00 29.50 ? 69  ASN A ND2 1 
ATOM   510  N  N   . PHE A 1 70  ? 14.965  23.276 15.804 1.00 17.96 ? 70  PHE A N   1 
ATOM   511  C  CA  . PHE A 1 70  ? 14.462  21.990 16.260 1.00 17.38 ? 70  PHE A CA  1 
ATOM   512  C  C   . PHE A 1 70  ? 13.098  21.619 15.627 1.00 21.40 ? 70  PHE A C   1 
ATOM   513  O  O   . PHE A 1 70  ? 12.231  22.505 15.421 1.00 19.83 ? 70  PHE A O   1 
ATOM   514  C  CB  . PHE A 1 70  ? 14.321  22.065 17.794 1.00 19.82 ? 70  PHE A CB  1 
ATOM   515  C  CG  . PHE A 1 70  ? 15.667  22.153 18.472 1.00 15.84 ? 70  PHE A CG  1 
ATOM   516  C  CD1 . PHE A 1 70  ? 16.234  21.040 19.060 1.00 17.49 ? 70  PHE A CD1 1 
ATOM   517  C  CD2 . PHE A 1 70  ? 16.374  23.345 18.468 1.00 18.97 ? 70  PHE A CD2 1 
ATOM   518  C  CE1 . PHE A 1 70  ? 17.507  21.086 19.654 1.00 18.07 ? 70  PHE A CE1 1 
ATOM   519  C  CE2 . PHE A 1 70  ? 17.647  23.405 19.029 1.00 17.88 ? 70  PHE A CE2 1 
ATOM   520  C  CZ  . PHE A 1 70  ? 18.219  22.271 19.599 1.00 18.78 ? 70  PHE A CZ  1 
ATOM   521  N  N   . GLU A 1 71  ? 12.905  20.319 15.360 1.00 18.42 ? 71  GLU A N   1 
ATOM   522  C  CA  . GLU A 1 71  ? 11.566  19.826 15.016 1.00 21.73 ? 71  GLU A CA  1 
ATOM   523  C  C   . GLU A 1 71  ? 10.616  20.198 16.130 1.00 20.86 ? 71  GLU A C   1 
ATOM   524  O  O   . GLU A 1 71  ? 10.897  19.914 17.301 1.00 20.77 ? 71  GLU A O   1 
ATOM   525  C  CB  . GLU A 1 71  ? 11.585  18.280 14.968 1.00 22.41 ? 71  GLU A CB  1 
ATOM   526  C  CG  . GLU A 1 71  ? 12.664  17.785 14.013 1.00 25.90 ? 71  GLU A CG  1 
ATOM   527  C  CD  . GLU A 1 71  ? 12.585  16.280 13.704 1.00 30.21 ? 71  GLU A CD  1 
ATOM   528  O  OE1 . GLU A 1 71  ? 11.821  15.555 14.357 1.00 33.06 ? 71  GLU A OE1 1 
ATOM   529  O  OE2 . GLU A 1 71  ? 13.297  15.830 12.782 1.00 34.82 ? 71  GLU A OE2 1 
ATOM   530  N  N   . ASP A 1 72  ? 9.441   20.708 15.759 1.00 21.56 ? 72  ASP A N   1 
ATOM   531  C  CA  . ASP A 1 72  ? 8.493   21.134 16.783 1.00 20.10 ? 72  ASP A CA  1 
ATOM   532  C  C   . ASP A 1 72  ? 7.068   20.722 16.485 1.00 24.00 ? 72  ASP A C   1 
ATOM   533  O  O   . ASP A 1 72  ? 6.115   21.461 16.788 1.00 22.68 ? 72  ASP A O   1 
ATOM   534  C  CB  . ASP A 1 72  ? 8.564   22.635 16.991 1.00 19.86 ? 72  ASP A CB  1 
ATOM   535  C  CG  . ASP A 1 72  ? 8.116   23.439 15.727 1.00 25.60 ? 72  ASP A CG  1 
ATOM   536  O  OD1 . ASP A 1 72  ? 7.850   24.640 15.849 1.00 22.88 ? 72  ASP A OD1 1 
ATOM   537  O  OD2 . ASP A 1 72  ? 8.035   22.874 14.603 1.00 22.87 ? 72  ASP A OD2 1 
ATOM   538  N  N   . ASN A 1 73  ? 6.950   19.504 15.963 1.00 24.00 ? 73  ASN A N   1 
ATOM   539  C  CA  . ASN A 1 73  ? 5.649   18.899 15.645 1.00 28.29 ? 73  ASN A CA  1 
ATOM   540  C  C   . ASN A 1 73  ? 4.956   18.234 16.829 1.00 30.51 ? 73  ASN A C   1 
ATOM   541  O  O   . ASN A 1 73  ? 3.737   17.964 16.770 1.00 33.99 ? 73  ASN A O   1 
ATOM   542  C  CB  . ASN A 1 73  ? 5.843   17.893 14.528 1.00 28.53 ? 73  ASN A CB  1 
ATOM   543  C  CG  . ASN A 1 73  ? 6.933   16.913 14.836 1.00 34.90 ? 73  ASN A CG  1 
ATOM   544  O  OD1 . ASN A 1 73  ? 8.132   17.186 14.624 1.00 30.53 ? 73  ASN A OD1 1 
ATOM   545  N  ND2 . ASN A 1 73  ? 6.528   15.727 15.328 1.00 31.55 ? 73  ASN A ND2 1 
ATOM   546  N  N   . ASP A 1 74  ? 5.688   17.990 17.908 1.00 28.71 ? 74  ASP A N   1 
ATOM   547  C  CA  . ASP A 1 74  ? 5.079   17.452 19.114 1.00 28.14 ? 74  ASP A CA  1 
ATOM   548  C  C   . ASP A 1 74  ? 5.810   17.932 20.358 1.00 28.85 ? 74  ASP A C   1 
ATOM   549  O  O   . ASP A 1 74  ? 6.738   18.756 20.242 1.00 28.73 ? 74  ASP A O   1 
ATOM   550  C  CB  . ASP A 1 74  ? 5.064   15.914 19.076 1.00 29.36 ? 74  ASP A CB  1 
ATOM   551  C  CG  . ASP A 1 74  ? 6.456   15.290 18.929 1.00 34.94 ? 74  ASP A CG  1 
ATOM   552  O  OD1 . ASP A 1 74  ? 7.515   15.917 19.237 1.00 31.21 ? 74  ASP A OD1 1 
ATOM   553  O  OD2 . ASP A 1 74  ? 6.499   14.096 18.564 1.00 35.51 ? 74  ASP A OD2 1 
ATOM   554  N  N   . ASN A 1 75  ? 5.432   17.388 21.515 1.00 28.38 ? 75  ASN A N   1 
ATOM   555  C  CA  . ASN A 1 75  ? 5.985   17.842 22.792 1.00 31.83 ? 75  ASN A CA  1 
ATOM   556  C  C   . ASN A 1 75  ? 7.181   17.034 23.292 1.00 28.16 ? 75  ASN A C   1 
ATOM   557  O  O   . ASN A 1 75  ? 7.362   16.870 24.481 1.00 30.32 ? 75  ASN A O   1 
ATOM   558  C  CB  . ASN A 1 75  ? 4.896   17.933 23.863 1.00 33.22 ? 75  ASN A CB  1 
ATOM   559  C  CG  . ASN A 1 75  ? 4.207   19.296 23.891 1.00 38.99 ? 75  ASN A CG  1 
ATOM   560  O  OD1 . ASN A 1 75  ? 4.558   20.213 23.162 1.00 39.65 ? 75  ASN A OD1 1 
ATOM   561  N  ND2 . ASN A 1 75  ? 3.231   19.433 24.762 1.00 44.72 ? 75  ASN A ND2 1 
ATOM   562  N  N   . ARG A 1 76  ? 7.992   16.508 22.390 1.00 30.43 ? 76  ARG A N   1 
ATOM   563  C  CA  . ARG A 1 76  ? 9.241   15.850 22.778 1.00 26.62 ? 76  ARG A CA  1 
ATOM   564  C  C   . ARG A 1 76  ? 10.237  16.744 23.529 1.00 29.85 ? 76  ARG A C   1 
ATOM   565  O  O   . ARG A 1 76  ? 11.008  16.244 24.344 1.00 28.80 ? 76  ARG A O   1 
ATOM   566  C  CB  . ARG A 1 76  ? 9.940   15.278 21.566 1.00 27.22 ? 76  ARG A CB  1 
ATOM   567  C  CG  . ARG A 1 76  ? 9.373   13.931 21.109 1.00 26.58 ? 76  ARG A CG  1 
ATOM   568  C  CD  . ARG A 1 76  ? 9.997   13.527 19.778 1.00 27.83 ? 76  ARG A CD  1 
ATOM   569  N  NE  . ARG A 1 76  ? 9.769   14.486 18.678 1.00 24.00 ? 76  ARG A NE  1 
ATOM   570  C  CZ  . ARG A 1 76  ? 10.461  14.479 17.542 1.00 27.47 ? 76  ARG A CZ  1 
ATOM   571  N  NH1 . ARG A 1 76  ? 11.468  13.630 17.376 1.00 24.50 ? 76  ARG A NH1 1 
ATOM   572  N  NH2 . ARG A 1 76  ? 10.202  15.378 16.564 1.00 29.48 ? 76  ARG A NH2 1 
ATOM   573  N  N   . SER A 1 77  ? 10.244  18.038 23.233 1.00 24.44 ? 77  SER A N   1 
ATOM   574  C  CA  . SER A 1 77  ? 11.198  18.945 23.879 1.00 21.16 ? 77  SER A CA  1 
ATOM   575  C  C   . SER A 1 77  ? 10.464  20.133 24.461 1.00 25.29 ? 77  SER A C   1 
ATOM   576  O  O   . SER A 1 77  ? 9.981   21.043 23.706 1.00 21.54 ? 77  SER A O   1 
ATOM   577  C  CB  . SER A 1 77  ? 12.232  19.474 22.882 1.00 22.17 ? 77  SER A CB  1 
ATOM   578  O  OG  . SER A 1 77  ? 13.068  18.442 22.411 1.00 20.90 ? 77  SER A OG  1 
ATOM   579  N  N   . VAL A 1 78  ? 10.426  20.223 25.791 1.00 22.50 ? 78  VAL A N   1 
ATOM   580  C  CA  . VAL A 1 78  ? 9.549   21.237 26.374 1.00 22.96 ? 78  VAL A CA  1 
ATOM   581  C  C   . VAL A 1 78  ? 10.172  21.988 27.548 1.00 23.37 ? 78  VAL A C   1 
ATOM   582  O  O   . VAL A 1 78  ? 11.056  21.471 28.189 1.00 24.24 ? 78  VAL A O   1 
ATOM   583  C  CB  . VAL A 1 78  ? 8.176   20.652 26.754 1.00 26.93 ? 78  VAL A CB  1 
ATOM   584  C  CG1 . VAL A 1 78  ? 7.366   20.246 25.503 1.00 25.10 ? 78  VAL A CG1 1 
ATOM   585  C  CG2 . VAL A 1 78  ? 8.333   19.438 27.632 1.00 27.42 ? 78  VAL A CG2 1 
ATOM   586  N  N   . LEU A 1 79  ? 9.680   23.189 27.778 1.00 23.35 ? 79  LEU A N   1 
ATOM   587  C  CA  . LEU A 1 79  ? 9.912   23.985 29.027 1.00 23.06 ? 79  LEU A CA  1 
ATOM   588  C  C   . LEU A 1 79  ? 8.586   24.075 29.771 1.00 23.95 ? 79  LEU A C   1 
ATOM   589  O  O   . LEU A 1 79  ? 7.560   24.433 29.179 1.00 26.63 ? 79  LEU A O   1 
ATOM   590  C  CB  . LEU A 1 79  ? 10.297  25.405 28.619 1.00 23.99 ? 79  LEU A CB  1 
ATOM   591  C  CG  . LEU A 1 79  ? 10.334  26.575 29.581 1.00 24.84 ? 79  LEU A CG  1 
ATOM   592  C  CD1 . LEU A 1 79  ? 11.422  26.286 30.591 1.00 27.66 ? 79  LEU A CD1 1 
ATOM   593  C  CD2 . LEU A 1 79  ? 10.720  27.826 28.834 1.00 24.35 ? 79  LEU A CD2 1 
ATOM   594  N  N   . LYS A 1 80  ? 8.652   23.910 31.098 1.00 25.03 ? 80  LYS A N   1 
ATOM   595  C  CA  . LYS A 1 80  ? 7.516   24.057 32.029 1.00 29.45 ? 80  LYS A CA  1 
ATOM   596  C  C   . LYS A 1 80  ? 7.997   24.720 33.360 1.00 27.43 ? 80  LYS A C   1 
ATOM   597  O  O   . LYS A 1 80  ? 9.197   24.991 33.577 1.00 27.29 ? 80  LYS A O   1 
ATOM   598  C  CB  . LYS A 1 80  ? 6.916   22.678 32.370 1.00 33.81 ? 80  LYS A CB  1 
ATOM   599  C  CG  . LYS A 1 80  ? 5.968   22.068 31.341 1.00 44.12 ? 80  LYS A CG  1 
ATOM   600  C  CD  . LYS A 1 80  ? 5.287   20.825 31.897 1.00 53.60 ? 80  LYS A CD  1 
ATOM   601  C  CE  . LYS A 1 80  ? 5.972   19.539 31.436 1.00 60.48 ? 80  LYS A CE  1 
ATOM   602  N  NZ  . LYS A 1 80  ? 7.178   19.213 32.255 1.00 62.89 ? 80  LYS A NZ  1 
ATOM   603  N  N   . GLY A 1 81  ? 7.041   25.018 34.229 1.00 29.59 ? 81  GLY A N   1 
ATOM   604  C  CA  . GLY A 1 81  ? 7.314   25.614 35.544 1.00 28.37 ? 81  GLY A CA  1 
ATOM   605  C  C   . GLY A 1 81  ? 7.600   27.088 35.433 1.00 26.27 ? 81  GLY A C   1 
ATOM   606  O  O   . GLY A 1 81  ? 7.107   27.750 34.552 1.00 24.58 ? 81  GLY A O   1 
ATOM   607  N  N   . GLY A 1 82  ? 8.426   27.600 36.328 1.00 27.41 ? 82  GLY A N   1 
ATOM   608  C  CA  . GLY A 1 82  ? 8.613   29.037 36.432 1.00 26.15 ? 82  GLY A CA  1 
ATOM   609  C  C   . GLY A 1 82  ? 7.276   29.720 36.649 1.00 28.30 ? 82  GLY A C   1 
ATOM   610  O  O   . GLY A 1 82  ? 6.488   29.257 37.470 1.00 31.47 ? 82  GLY A O   1 
ATOM   611  N  N   . PRO A 1 83  ? 7.001   30.774 35.877 1.00 26.85 ? 83  PRO A N   1 
ATOM   612  C  CA  . PRO A 1 83  ? 5.778   31.608 35.841 1.00 26.65 ? 83  PRO A CA  1 
ATOM   613  C  C   . PRO A 1 83  ? 4.642   30.991 35.027 1.00 27.64 ? 83  PRO A C   1 
ATOM   614  O  O   . PRO A 1 83  ? 3.523   31.543 34.962 1.00 29.61 ? 83  PRO A O   1 
ATOM   615  C  CB  . PRO A 1 83  ? 6.269   32.893 35.212 1.00 28.75 ? 83  PRO A CB  1 
ATOM   616  C  CG  . PRO A 1 83  ? 7.404   32.472 34.313 1.00 27.53 ? 83  PRO A CG  1 
ATOM   617  C  CD  . PRO A 1 83  ? 7.977   31.188 34.852 1.00 27.49 ? 83  PRO A CD  1 
ATOM   618  N  N   . PHE A 1 84  ? 4.917   29.854 34.433 1.00 26.69 ? 84  PHE A N   1 
ATOM   619  C  CA  . PHE A 1 84  ? 4.061   29.298 33.383 1.00 28.32 ? 84  PHE A CA  1 
ATOM   620  C  C   . PHE A 1 84  ? 3.147   28.231 33.909 1.00 28.04 ? 84  PHE A C   1 
ATOM   621  O  O   . PHE A 1 84  ? 3.568   27.394 34.740 1.00 28.77 ? 84  PHE A O   1 
ATOM   622  C  CB  . PHE A 1 84  ? 4.909   28.605 32.313 1.00 26.87 ? 84  PHE A CB  1 
ATOM   623  C  CG  . PHE A 1 84  ? 5.876   29.520 31.655 1.00 27.54 ? 84  PHE A CG  1 
ATOM   624  C  CD1 . PHE A 1 84  ? 7.233   29.258 31.702 1.00 26.03 ? 84  PHE A CD1 1 
ATOM   625  C  CD2 . PHE A 1 84  ? 5.408   30.671 31.033 1.00 26.27 ? 84  PHE A CD2 1 
ATOM   626  C  CE1 . PHE A 1 84  ? 8.119   30.106 31.115 1.00 23.34 ? 84  PHE A CE1 1 
ATOM   627  C  CE2 . PHE A 1 84  ? 6.296   31.539 30.414 1.00 24.86 ? 84  PHE A CE2 1 
ATOM   628  C  CZ  . PHE A 1 84  ? 7.664   31.232 30.481 1.00 24.34 ? 84  PHE A CZ  1 
ATOM   629  N  N   . SER A 1 85  ? 1.909   28.243 33.419 1.00 31.84 ? 85  SER A N   1 
ATOM   630  C  CA  . SER A 1 85  ? 1.028   27.090 33.643 1.00 33.37 ? 85  SER A CA  1 
ATOM   631  C  C   . SER A 1 85  ? 0.892   26.181 32.402 1.00 33.19 ? 85  SER A C   1 
ATOM   632  O  O   . SER A 1 85  ? 0.480   25.019 32.507 1.00 32.69 ? 85  SER A O   1 
ATOM   633  C  CB  . SER A 1 85  ? -0.343  27.522 34.180 1.00 38.20 ? 85  SER A CB  1 
ATOM   634  O  OG  . SER A 1 85  ? -0.868  28.535 33.343 1.00 51.14 ? 85  SER A OG  1 
ATOM   635  N  N   . ASP A 1 86  ? 1.283   26.722 31.253 1.00 30.23 ? 86  ASP A N   1 
ATOM   636  C  CA  . ASP A 1 86  ? 1.287   26.033 29.976 1.00 30.65 ? 86  ASP A CA  1 
ATOM   637  C  C   . ASP A 1 86  ? 2.681   25.430 29.666 1.00 33.41 ? 86  ASP A C   1 
ATOM   638  O  O   . ASP A 1 86  ? 3.677   25.953 30.082 1.00 35.68 ? 86  ASP A O   1 
ATOM   639  C  CB  . ASP A 1 86  ? 0.947   27.072 28.903 1.00 34.94 ? 86  ASP A CB  1 
ATOM   640  C  CG  . ASP A 1 86  ? -0.505  27.626 29.026 1.00 33.38 ? 86  ASP A CG  1 
ATOM   641  O  OD1 . ASP A 1 86  ? -1.400  26.923 29.614 1.00 39.80 ? 86  ASP A OD1 1 
ATOM   642  O  OD2 . ASP A 1 86  ? -0.737  28.774 28.549 1.00 32.33 ? 86  ASP A OD2 1 
ATOM   643  N  N   . SER A 1 87  ? 2.735   24.352 28.909 1.00 34.57 ? 87  SER A N   1 
ATOM   644  C  CA  . SER A 1 87  ? 3.966   23.767 28.437 1.00 31.88 ? 87  SER A CA  1 
ATOM   645  C  C   . SER A 1 87  ? 4.429   24.490 27.154 1.00 27.99 ? 87  SER A C   1 
ATOM   646  O  O   . SER A 1 87  ? 3.597   24.779 26.263 1.00 23.84 ? 87  SER A O   1 
ATOM   647  C  CB  . SER A 1 87  ? 3.650   22.313 28.136 1.00 37.38 ? 87  SER A CB  1 
ATOM   648  O  OG  . SER A 1 87  ? 4.752   21.613 27.629 1.00 41.59 ? 87  SER A OG  1 
ATOM   649  N  N   . TYR A 1 88  ? 5.738   24.788 27.054 1.00 23.30 ? 88  TYR A N   1 
ATOM   650  C  CA  . TYR A 1 88  ? 6.252   25.518 25.859 1.00 21.33 ? 88  TYR A CA  1 
ATOM   651  C  C   . TYR A 1 88  ? 7.188   24.651 25.049 1.00 21.89 ? 88  TYR A C   1 
ATOM   652  O  O   . TYR A 1 88  ? 8.103   24.063 25.605 1.00 20.64 ? 88  TYR A O   1 
ATOM   653  C  CB  . TYR A 1 88  ? 6.964   26.821 26.260 1.00 22.25 ? 88  TYR A CB  1 
ATOM   654  C  CG  . TYR A 1 88  ? 6.010   27.904 26.703 1.00 21.13 ? 88  TYR A CG  1 
ATOM   655  C  CD1 . TYR A 1 88  ? 5.800   29.046 25.923 1.00 19.27 ? 88  TYR A CD1 1 
ATOM   656  C  CD2 . TYR A 1 88  ? 5.287   27.759 27.896 1.00 22.81 ? 88  TYR A CD2 1 
ATOM   657  C  CE1 . TYR A 1 88  ? 4.922   30.039 26.347 1.00 22.12 ? 88  TYR A CE1 1 
ATOM   658  C  CE2 . TYR A 1 88  ? 4.393   28.731 28.307 1.00 24.09 ? 88  TYR A CE2 1 
ATOM   659  C  CZ  . TYR A 1 88  ? 4.227   29.861 27.526 1.00 24.04 ? 88  TYR A CZ  1 
ATOM   660  O  OH  . TYR A 1 88  ? 3.330   30.786 27.943 1.00 24.97 ? 88  TYR A OH  1 
ATOM   661  N  N   . ARG A 1 89  ? 7.030   24.610 23.721 1.00 20.39 ? 89  ARG A N   1 
ATOM   662  C  CA  . ARG A 1 89  ? 7.796   23.679 22.942 1.00 18.27 ? 89  ARG A CA  1 
ATOM   663  C  C   . ARG A 1 89  ? 9.099   24.354 22.407 1.00 16.94 ? 89  ARG A C   1 
ATOM   664  O  O   . ARG A 1 89  ? 9.025   25.403 21.840 1.00 17.58 ? 89  ARG A O   1 
ATOM   665  C  CB  . ARG A 1 89  ? 6.864   23.317 21.736 1.00 22.27 ? 89  ARG A CB  1 
ATOM   666  C  CG  . ARG A 1 89  ? 7.247   22.090 20.988 1.00 23.24 ? 89  ARG A CG  1 
ATOM   667  C  CD  . ARG A 1 89  ? 6.154   21.803 19.963 1.00 25.13 ? 89  ARG A CD  1 
ATOM   668  N  NE  . ARG A 1 89  ? 5.020   21.124 20.584 1.00 26.54 ? 89  ARG A NE  1 
ATOM   669  C  CZ  . ARG A 1 89  ? 3.924   20.745 19.931 1.00 30.54 ? 89  ARG A CZ  1 
ATOM   670  N  NH1 . ARG A 1 89  ? 3.793   20.995 18.630 1.00 25.66 ? 89  ARG A NH1 1 
ATOM   671  N  NH2 . ARG A 1 89  ? 2.947   20.122 20.580 1.00 37.38 ? 89  ARG A NH2 1 
ATOM   672  N  N   . LEU A 1 90  ? 10.253  23.709 22.544 1.00 14.94 ? 90  LEU A N   1 
ATOM   673  C  CA  . LEU A 1 90  ? 11.523  24.244 21.996 1.00 14.74 ? 90  LEU A CA  1 
ATOM   674  C  C   . LEU A 1 90  ? 11.411  24.377 20.502 1.00 17.02 ? 90  LEU A C   1 
ATOM   675  O  O   . LEU A 1 90  ? 10.895  23.436 19.856 1.00 18.81 ? 90  LEU A O   1 
ATOM   676  C  CB  . LEU A 1 90  ? 12.643  23.253 22.346 1.00 16.77 ? 90  LEU A CB  1 
ATOM   677  C  CG  . LEU A 1 90  ? 14.021  23.489 21.757 1.00 17.10 ? 90  LEU A CG  1 
ATOM   678  C  CD1 . LEU A 1 90  ? 14.569  24.797 22.364 1.00 17.14 ? 90  LEU A CD1 1 
ATOM   679  C  CD2 . LEU A 1 90  ? 14.897  22.291 22.138 1.00 19.10 ? 90  LEU A CD2 1 
ATOM   680  N  N   . PHE A 1 91  ? 11.824  25.538 19.960 1.00 15.31 ? 91  PHE A N   1 
ATOM   681  C  CA  . PHE A 1 91  ? 12.014  25.651 18.493 1.00 17.34 ? 91  PHE A CA  1 
ATOM   682  C  C   . PHE A 1 91  ? 13.388  26.044 17.990 1.00 17.44 ? 91  PHE A C   1 
ATOM   683  O  O   . PHE A 1 91  ? 13.743  25.721 16.883 1.00 16.99 ? 91  PHE A O   1 
ATOM   684  C  CB  . PHE A 1 91  ? 10.880  26.482 17.852 1.00 17.09 ? 91  PHE A CB  1 
ATOM   685  C  CG  . PHE A 1 91  ? 10.914  27.958 18.120 1.00 14.64 ? 91  PHE A CG  1 
ATOM   686  C  CD1 . PHE A 1 91  ? 10.284  28.492 19.281 1.00 14.83 ? 91  PHE A CD1 1 
ATOM   687  C  CD2 . PHE A 1 91  ? 11.546  28.880 17.196 1.00 16.67 ? 91  PHE A CD2 1 
ATOM   688  C  CE1 . PHE A 1 91  ? 10.284  29.887 19.485 1.00 14.87 ? 91  PHE A CE1 1 
ATOM   689  C  CE2 . PHE A 1 91  ? 11.540  30.278 17.402 1.00 16.81 ? 91  PHE A CE2 1 
ATOM   690  C  CZ  . PHE A 1 91  ? 10.923  30.781 18.572 1.00 16.56 ? 91  PHE A CZ  1 
ATOM   691  N  N   . GLN A 1 92  ? 14.188  26.769 18.781 1.00 16.21 ? 92  GLN A N   1 
ATOM   692  C  CA  . GLN A 1 92  ? 15.451  27.260 18.257 1.00 19.29 ? 92  GLN A CA  1 
ATOM   693  C  C   . GLN A 1 92  ? 16.351  27.698 19.449 1.00 18.78 ? 92  GLN A C   1 
ATOM   694  O  O   . GLN A 1 92  ? 15.810  28.051 20.520 1.00 18.58 ? 92  GLN A O   1 
ATOM   695  C  CB  . GLN A 1 92  ? 15.128  28.483 17.353 1.00 22.13 ? 92  GLN A CB  1 
ATOM   696  C  CG  . GLN A 1 92  ? 16.256  29.398 17.116 1.00 28.97 ? 92  GLN A CG  1 
ATOM   697  C  CD  . GLN A 1 92  ? 15.826  30.576 16.320 1.00 31.66 ? 92  GLN A CD  1 
ATOM   698  O  OE1 . GLN A 1 92  ? 15.968  31.712 16.745 1.00 24.90 ? 92  GLN A OE1 1 
ATOM   699  N  NE2 . GLN A 1 92  ? 15.262  30.295 15.107 1.00 32.13 ? 92  GLN A NE2 1 
ATOM   700  N  N   . PHE A 1 93  ? 17.690  27.615 19.287 1.00 16.03 ? 93  PHE A N   1 
ATOM   701  C  CA  . PHE A 1 93  ? 18.551  28.428 20.092 1.00 15.32 ? 93  PHE A CA  1 
ATOM   702  C  C   . PHE A 1 93  ? 19.518  29.258 19.268 1.00 15.95 ? 93  PHE A C   1 
ATOM   703  O  O   . PHE A 1 93  ? 19.779  28.941 18.097 1.00 16.93 ? 93  PHE A O   1 
ATOM   704  C  CB  . PHE A 1 93  ? 19.259  27.603 21.189 1.00 14.33 ? 93  PHE A CB  1 
ATOM   705  C  CG  . PHE A 1 93  ? 20.388  26.721 20.743 1.00 14.80 ? 93  PHE A CG  1 
ATOM   706  C  CD1 . PHE A 1 93  ? 20.147  25.336 20.520 1.00 15.95 ? 93  PHE A CD1 1 
ATOM   707  C  CD2 . PHE A 1 93  ? 21.697  27.239 20.540 1.00 16.75 ? 93  PHE A CD2 1 
ATOM   708  C  CE1 . PHE A 1 93  ? 21.186  24.487 20.130 1.00 14.03 ? 93  PHE A CE1 1 
ATOM   709  C  CE2 . PHE A 1 93  ? 22.768  26.404 20.092 1.00 15.33 ? 93  PHE A CE2 1 
ATOM   710  C  CZ  . PHE A 1 93  ? 22.488  25.035 19.894 1.00 14.67 ? 93  PHE A CZ  1 
ATOM   711  N  N   . HIS A 1 94  ? 20.053  30.334 19.842 1.00 12.40 ? 94  HIS A N   1 
ATOM   712  C  CA  . HIS A 1 94  ? 21.057  31.153 19.149 1.00 14.86 ? 94  HIS A CA  1 
ATOM   713  C  C   . HIS A 1 94  ? 21.784  32.043 20.123 1.00 14.70 ? 94  HIS A C   1 
ATOM   714  O  O   . HIS A 1 94  ? 21.527  31.911 21.368 1.00 16.81 ? 94  HIS A O   1 
ATOM   715  C  CB  . HIS A 1 94  ? 20.410  32.067 18.106 1.00 13.87 ? 94  HIS A CB  1 
ATOM   716  C  CG  . HIS A 1 94  ? 19.362  33.011 18.724 1.00 14.84 ? 94  HIS A CG  1 
ATOM   717  N  ND1 . HIS A 1 94  ? 18.042  32.672 18.801 1.00 16.46 ? 94  HIS A ND1 1 
ATOM   718  C  CD2 . HIS A 1 94  ? 19.500  34.192 19.348 1.00 14.62 ? 94  HIS A CD2 1 
ATOM   719  C  CE1 . HIS A 1 94  ? 17.369  33.680 19.367 1.00 17.16 ? 94  HIS A CE1 1 
ATOM   720  N  NE2 . HIS A 1 94  ? 18.260  34.603 19.713 1.00 13.89 ? 94  HIS A NE2 1 
ATOM   721  N  N   . PHE A 1 95  ? 22.733  32.851 19.608 1.00 15.06 ? 95  PHE A N   1 
ATOM   722  C  CA  . PHE A 1 95  ? 23.591  33.661 20.522 1.00 14.89 ? 95  PHE A CA  1 
ATOM   723  C  C   . PHE A 1 95  ? 23.566  35.112 20.028 1.00 18.31 ? 95  PHE A C   1 
ATOM   724  O  O   . PHE A 1 95  ? 23.227  35.372 18.838 1.00 18.60 ? 95  PHE A O   1 
ATOM   725  C  CB  . PHE A 1 95  ? 25.036  33.150 20.541 1.00 15.36 ? 95  PHE A CB  1 
ATOM   726  C  CG  . PHE A 1 95  ? 25.173  31.770 20.925 1.00 14.73 ? 95  PHE A CG  1 
ATOM   727  C  CD1 . PHE A 1 95  ? 25.435  31.406 22.226 1.00 14.31 ? 95  PHE A CD1 1 
ATOM   728  C  CD2 . PHE A 1 95  ? 25.067  30.749 19.980 1.00 14.38 ? 95  PHE A CD2 1 
ATOM   729  C  CE1 . PHE A 1 95  ? 25.571  30.062 22.570 1.00 14.70 ? 95  PHE A CE1 1 
ATOM   730  C  CE2 . PHE A 1 95  ? 25.165  29.410 20.303 1.00 14.22 ? 95  PHE A CE2 1 
ATOM   731  C  CZ  . PHE A 1 95  ? 25.453  29.025 21.623 1.00 16.02 ? 95  PHE A CZ  1 
ATOM   732  N  N   . HIS A 1 96  ? 23.865  36.084 20.922 1.00 14.94 ? 96  HIS A N   1 
ATOM   733  C  CA  . HIS A 1 96  ? 24.180  37.436 20.512 1.00 15.23 ? 96  HIS A CA  1 
ATOM   734  C  C   . HIS A 1 96  ? 25.527  37.756 21.047 1.00 15.61 ? 96  HIS A C   1 
ATOM   735  O  O   . HIS A 1 96  ? 25.930  37.164 22.039 1.00 17.17 ? 96  HIS A O   1 
ATOM   736  C  CB  . HIS A 1 96  ? 23.235  38.449 21.140 1.00 15.57 ? 96  HIS A CB  1 
ATOM   737  C  CG  . HIS A 1 96  ? 21.821  38.219 20.746 1.00 14.49 ? 96  HIS A CG  1 
ATOM   738  N  ND1 . HIS A 1 96  ? 21.200  38.963 19.724 1.00 15.33 ? 96  HIS A ND1 1 
ATOM   739  C  CD2 . HIS A 1 96  ? 20.952  37.239 21.123 1.00 15.34 ? 96  HIS A CD2 1 
ATOM   740  C  CE1 . HIS A 1 96  ? 19.941  38.502 19.583 1.00 14.89 ? 96  HIS A CE1 1 
ATOM   741  N  NE2 . HIS A 1 96  ? 19.778  37.428 20.429 1.00 16.90 ? 96  HIS A NE2 1 
ATOM   742  N  N   . TRP A 1 97  ? 26.285  38.585 20.357 1.00 17.09 ? 97  TRP A N   1 
ATOM   743  C  CA  . TRP A 1 97  ? 27.630  38.898 20.764 1.00 19.23 ? 97  TRP A CA  1 
ATOM   744  C  C   . TRP A 1 97  ? 27.938  40.311 20.326 1.00 20.87 ? 97  TRP A C   1 
ATOM   745  O  O   . TRP A 1 97  ? 27.181  40.913 19.601 1.00 20.71 ? 97  TRP A O   1 
ATOM   746  C  CB  . TRP A 1 97  ? 28.683  37.927 20.257 1.00 18.14 ? 97  TRP A CB  1 
ATOM   747  C  CG  . TRP A 1 97  ? 28.683  37.810 18.768 1.00 18.08 ? 97  TRP A CG  1 
ATOM   748  C  CD1 . TRP A 1 97  ? 29.365  38.598 17.848 1.00 20.65 ? 97  TRP A CD1 1 
ATOM   749  C  CD2 . TRP A 1 97  ? 27.935  36.843 17.972 1.00 18.83 ? 97  TRP A CD2 1 
ATOM   750  N  NE1 . TRP A 1 97  ? 29.100  38.185 16.569 1.00 20.99 ? 97  TRP A NE1 1 
ATOM   751  C  CE2 . TRP A 1 97  ? 28.248  37.135 16.574 1.00 19.60 ? 97  TRP A CE2 1 
ATOM   752  C  CE3 . TRP A 1 97  ? 27.073  35.799 18.265 1.00 19.24 ? 97  TRP A CE3 1 
ATOM   753  C  CZ2 . TRP A 1 97  ? 27.709  36.401 15.536 1.00 19.54 ? 97  TRP A CZ2 1 
ATOM   754  C  CZ3 . TRP A 1 97  ? 26.535  35.065 17.210 1.00 21.32 ? 97  TRP A CZ3 1 
ATOM   755  C  CH2 . TRP A 1 97  ? 26.846  35.360 15.879 1.00 19.56 ? 97  TRP A CH2 1 
ATOM   756  N  N   . GLY A 1 98  ? 29.071  40.824 20.795 1.00 21.68 ? 98  GLY A N   1 
ATOM   757  C  CA  . GLY A 1 98  ? 29.597  42.147 20.446 1.00 23.26 ? 98  GLY A CA  1 
ATOM   758  C  C   . GLY A 1 98  ? 30.948  42.133 19.722 1.00 23.30 ? 98  GLY A C   1 
ATOM   759  O  O   . GLY A 1 98  ? 31.583  41.108 19.527 1.00 21.93 ? 98  GLY A O   1 
ATOM   760  N  N   . SER A 1 99  ? 31.398  43.317 19.341 1.00 27.18 ? 99  SER A N   1 
ATOM   761  C  CA  . SER A 1 99  ? 32.599  43.447 18.524 1.00 34.23 ? 99  SER A CA  1 
ATOM   762  C  C   . SER A 1 99  ? 33.876  43.177 19.354 1.00 35.33 ? 99  SER A C   1 
ATOM   763  O  O   . SER A 1 99  ? 34.891  42.681 18.831 1.00 36.82 ? 99  SER A O   1 
ATOM   764  C  CB  . SER A 1 99  ? 32.621  44.807 17.822 1.00 35.05 ? 99  SER A CB  1 
ATOM   765  O  OG  . SER A 1 99  ? 32.556  45.881 18.747 1.00 41.64 ? 99  SER A OG  1 
ATOM   766  N  N   . THR A 1 100 ? 33.798  43.432 20.658 1.00 32.27 ? 100 THR A N   1 
ATOM   767  C  CA  . THR A 1 100 ? 34.910  43.043 21.535 1.00 34.55 ? 100 THR A CA  1 
ATOM   768  C  C   . THR A 1 100 ? 34.340  42.299 22.742 1.00 28.67 ? 100 THR A C   1 
ATOM   769  O  O   . THR A 1 100 ? 33.113  42.272 22.959 1.00 24.56 ? 100 THR A O   1 
ATOM   770  C  CB  . THR A 1 100 ? 35.648  44.286 22.065 1.00 36.98 ? 100 THR A CB  1 
ATOM   771  O  OG1 . THR A 1 100 ? 34.776  44.958 22.968 1.00 32.17 ? 100 THR A OG1 1 
ATOM   772  C  CG2 . THR A 1 100 ? 36.015  45.252 20.929 1.00 39.55 ? 100 THR A CG2 1 
ATOM   773  N  N   . ASN A 1 101 ? 35.232  41.721 23.535 1.00 25.93 ? 101 ASN A N   1 
ATOM   774  C  CA  . ASN A 1 101 ? 34.822  41.029 24.751 1.00 26.74 ? 101 ASN A CA  1 
ATOM   775  C  C   . ASN A 1 101 ? 34.042  41.897 25.785 1.00 25.27 ? 101 ASN A C   1 
ATOM   776  O  O   . ASN A 1 101 ? 33.366  41.360 26.683 1.00 26.40 ? 101 ASN A O   1 
ATOM   777  C  CB  . ASN A 1 101 ? 36.050  40.433 25.420 1.00 26.53 ? 101 ASN A CB  1 
ATOM   778  C  CG  . ASN A 1 101 ? 36.679  39.287 24.642 1.00 31.34 ? 101 ASN A CG  1 
ATOM   779  O  OD1 . ASN A 1 101 ? 36.113  38.747 23.682 1.00 27.54 ? 101 ASN A OD1 1 
ATOM   780  N  ND2 . ASN A 1 101 ? 37.835  38.872 25.093 1.00 30.13 ? 101 ASN A ND2 1 
ATOM   781  N  N   . GLU A 1 102 ? 34.200  43.208 25.694 1.00 28.01 ? 102 GLU A N   1 
ATOM   782  C  CA  . GLU A 1 102 ? 33.627  44.116 26.705 1.00 28.09 ? 102 GLU A CA  1 
ATOM   783  C  C   . GLU A 1 102 ? 32.121  44.287 26.748 1.00 28.51 ? 102 GLU A C   1 
ATOM   784  O  O   . GLU A 1 102 ? 31.581  44.723 27.749 1.00 25.11 ? 102 GLU A O   1 
ATOM   785  C  CB  . GLU A 1 102 ? 34.352  45.490 26.781 1.00 36.18 ? 102 GLU A CB  1 
ATOM   786  C  CG  . GLU A 1 102 ? 33.749  46.649 25.970 1.00 48.16 ? 102 GLU A CG  1 
ATOM   787  C  CD  . GLU A 1 102 ? 32.763  47.527 26.737 1.00 54.57 ? 102 GLU A CD  1 
ATOM   788  O  OE1 . GLU A 1 102 ? 32.844  47.635 27.981 1.00 58.61 ? 102 GLU A OE1 1 
ATOM   789  O  OE2 . GLU A 1 102 ? 31.902  48.127 26.061 1.00 60.52 ? 102 GLU A OE2 1 
ATOM   790  N  N   . HIS A 1 103 ? 31.447  43.941 25.643 1.00 24.83 ? 103 HIS A N   1 
ATOM   791  C  CA  . HIS A 1 103 ? 29.991  43.975 25.580 1.00 25.44 ? 103 HIS A CA  1 
ATOM   792  C  C   . HIS A 1 103 ? 29.546  42.900 24.585 1.00 23.82 ? 103 HIS A C   1 
ATOM   793  O  O   . HIS A 1 103 ? 30.388  42.165 23.983 1.00 22.89 ? 103 HIS A O   1 
ATOM   794  C  CB  . HIS A 1 103 ? 29.576  45.352 25.108 1.00 27.23 ? 103 HIS A CB  1 
ATOM   795  C  CG  . HIS A 1 103 ? 30.246  45.726 23.835 1.00 34.39 ? 103 HIS A CG  1 
ATOM   796  N  ND1 . HIS A 1 103 ? 31.491  46.269 23.800 1.00 40.27 ? 103 HIS A ND1 1 
ATOM   797  C  CD2 . HIS A 1 103 ? 29.860  45.545 22.522 1.00 35.97 ? 103 HIS A CD2 1 
ATOM   798  C  CE1 . HIS A 1 103 ? 31.866  46.445 22.517 1.00 43.63 ? 103 HIS A CE1 1 
ATOM   799  N  NE2 . HIS A 1 103 ? 30.881  45.991 21.735 1.00 39.54 ? 103 HIS A NE2 1 
ATOM   800  N  N   . GLY A 1 104 ? 28.246  42.741 24.408 1.00 23.10 ? 104 GLY A N   1 
ATOM   801  C  CA  . GLY A 1 104 ? 27.790  41.732 23.499 1.00 24.50 ? 104 GLY A CA  1 
ATOM   802  C  C   . GLY A 1 104 ? 26.554  41.038 24.015 1.00 20.15 ? 104 GLY A C   1 
ATOM   803  O  O   . GLY A 1 104 ? 25.761  40.610 23.209 1.00 21.35 ? 104 GLY A O   1 
ATOM   804  N  N   . SER A 1 105 ? 26.372  40.926 25.345 1.00 19.20 ? 105 SER A N   1 
ATOM   805  C  CA  . SER A 1 105 ? 25.085  40.369 25.834 1.00 17.54 ? 105 SER A CA  1 
ATOM   806  C  C   . SER A 1 105 ? 23.979  41.417 25.514 1.00 16.23 ? 105 SER A C   1 
ATOM   807  O  O   . SER A 1 105 ? 24.241  42.612 25.298 1.00 17.42 ? 105 SER A O   1 
ATOM   808  C  CB  . SER A 1 105 ? 25.102  40.074 27.354 1.00 16.69 ? 105 SER A CB  1 
ATOM   809  O  OG  . SER A 1 105 ? 25.224  41.317 28.149 1.00 19.06 ? 105 SER A OG  1 
ATOM   810  N  N   . GLU A 1 106 ? 22.734  40.971 25.578 1.00 17.69 ? 106 GLU A N   1 
ATOM   811  C  CA  . GLU A 1 106 ? 21.569  41.852 25.362 1.00 16.28 ? 106 GLU A CA  1 
ATOM   812  C  C   . GLU A 1 106 ? 21.070  42.329 26.700 1.00 16.66 ? 106 GLU A C   1 
ATOM   813  O  O   . GLU A 1 106 ? 21.006  43.544 26.938 1.00 18.29 ? 106 GLU A O   1 
ATOM   814  C  CB  . GLU A 1 106 ? 20.453  41.089 24.648 1.00 17.19 ? 106 GLU A CB  1 
ATOM   815  C  CG  . GLU A 1 106 ? 20.963  40.651 23.240 1.00 18.41 ? 106 GLU A CG  1 
ATOM   816  C  CD  . GLU A 1 106 ? 19.861  40.706 22.167 1.00 17.33 ? 106 GLU A CD  1 
ATOM   817  O  OE1 . GLU A 1 106 ? 19.938  41.575 21.284 1.00 16.50 ? 106 GLU A OE1 1 
ATOM   818  O  OE2 . GLU A 1 106 ? 18.923  39.877 22.288 1.00 16.14 ? 106 GLU A OE2 1 
ATOM   819  N  N   . HIS A 1 107 ? 20.706  41.404 27.559 1.00 15.83 ? 107 HIS A N   1 
ATOM   820  C  CA  . HIS A 1 107 ? 20.371  41.804 28.935 1.00 17.31 ? 107 HIS A CA  1 
ATOM   821  C  C   . HIS A 1 107 ? 21.665  42.231 29.663 1.00 17.29 ? 107 HIS A C   1 
ATOM   822  O  O   . HIS A 1 107 ? 22.791  41.808 29.349 1.00 18.28 ? 107 HIS A O   1 
ATOM   823  C  CB  . HIS A 1 107 ? 19.649  40.669 29.656 1.00 17.92 ? 107 HIS A CB  1 
ATOM   824  C  CG  . HIS A 1 107 ? 18.271  40.412 29.094 1.00 18.10 ? 107 HIS A CG  1 
ATOM   825  N  ND1 . HIS A 1 107 ? 18.053  39.577 28.029 1.00 16.72 ? 107 HIS A ND1 1 
ATOM   826  C  CD2 . HIS A 1 107 ? 17.043  40.912 29.471 1.00 18.73 ? 107 HIS A CD2 1 
ATOM   827  C  CE1 . HIS A 1 107 ? 16.739  39.561 27.725 1.00 17.22 ? 107 HIS A CE1 1 
ATOM   828  N  NE2 . HIS A 1 107 ? 16.108  40.447 28.565 1.00 17.49 ? 107 HIS A NE2 1 
ATOM   829  N  N   . THR A 1 108 ? 21.519  43.158 30.618 1.00 18.70 ? 108 THR A N   1 
ATOM   830  C  CA  . THR A 1 108 ? 22.641  43.525 31.526 1.00 18.24 ? 108 THR A CA  1 
ATOM   831  C  C   . THR A 1 108 ? 22.096  43.394 32.939 1.00 19.14 ? 108 THR A C   1 
ATOM   832  O  O   . THR A 1 108 ? 20.864  43.341 33.163 1.00 20.64 ? 108 THR A O   1 
ATOM   833  C  CB  . THR A 1 108 ? 23.184  44.956 31.251 1.00 18.94 ? 108 THR A CB  1 
ATOM   834  O  OG1 . THR A 1 108 ? 22.123  45.882 31.391 1.00 22.72 ? 108 THR A OG1 1 
ATOM   835  C  CG2 . THR A 1 108 ? 23.706  45.048 29.784 1.00 20.72 ? 108 THR A CG2 1 
ATOM   836  N  N   . VAL A 1 109 ? 23.006  43.239 33.917 1.00 20.06 ? 109 VAL A N   1 
ATOM   837  C  CA  . VAL A 1 109 ? 22.572  43.085 35.302 1.00 20.68 ? 109 VAL A CA  1 
ATOM   838  C  C   . VAL A 1 109 ? 23.310  44.185 36.135 1.00 21.97 ? 109 VAL A C   1 
ATOM   839  O  O   . VAL A 1 109 ? 24.546  44.219 36.163 1.00 20.27 ? 109 VAL A O   1 
ATOM   840  C  CB  . VAL A 1 109 ? 22.899  41.673 35.877 1.00 23.39 ? 109 VAL A CB  1 
ATOM   841  C  CG1 . VAL A 1 109 ? 22.458  41.548 37.343 1.00 21.50 ? 109 VAL A CG1 1 
ATOM   842  C  CG2 . VAL A 1 109 ? 22.197  40.553 35.090 1.00 20.45 ? 109 VAL A CG2 1 
ATOM   843  N  N   . ASP A 1 110 ? 22.544  45.104 36.707 1.00 22.62 ? 110 ASP A N   1 
ATOM   844  C  CA  . ASP A 1 110 ? 23.131  46.296 37.402 1.00 25.37 ? 110 ASP A CA  1 
ATOM   845  C  C   . ASP A 1 110 ? 24.150  46.995 36.553 1.00 24.88 ? 110 ASP A C   1 
ATOM   846  O  O   . ASP A 1 110 ? 25.220  47.359 37.049 1.00 25.31 ? 110 ASP A O   1 
ATOM   847  C  CB  . ASP A 1 110 ? 23.706  45.898 38.807 1.00 26.46 ? 110 ASP A CB  1 
ATOM   848  C  CG  . ASP A 1 110 ? 22.646  45.420 39.754 1.00 23.49 ? 110 ASP A CG  1 
ATOM   849  O  OD1 . ASP A 1 110 ? 21.620  46.090 39.907 1.00 29.08 ? 110 ASP A OD1 1 
ATOM   850  O  OD2 . ASP A 1 110 ? 22.807  44.323 40.321 1.00 31.95 ? 110 ASP A OD2 1 
ATOM   851  N  N   . GLY A 1 111 ? 23.826  47.184 35.250 1.00 22.25 ? 111 GLY A N   1 
ATOM   852  C  CA  . GLY A 1 111 ? 24.676  47.918 34.331 1.00 24.61 ? 111 GLY A CA  1 
ATOM   853  C  C   . GLY A 1 111 ? 25.812  47.115 33.719 1.00 22.13 ? 111 GLY A C   1 
ATOM   854  O  O   . GLY A 1 111 ? 26.465  47.594 32.815 1.00 24.59 ? 111 GLY A O   1 
ATOM   855  N  N   . VAL A 1 112 ? 26.056  45.916 34.234 1.00 21.00 ? 112 VAL A N   1 
ATOM   856  C  CA  . VAL A 1 112 ? 27.175  45.101 33.824 1.00 21.42 ? 112 VAL A CA  1 
ATOM   857  C  C   . VAL A 1 112 ? 26.820  44.346 32.502 1.00 21.47 ? 112 VAL A C   1 
ATOM   858  O  O   . VAL A 1 112 ? 25.794  43.630 32.464 1.00 20.44 ? 112 VAL A O   1 
ATOM   859  C  CB  . VAL A 1 112 ? 27.619  44.118 34.907 1.00 25.66 ? 112 VAL A CB  1 
ATOM   860  C  CG1 . VAL A 1 112 ? 28.802  43.282 34.359 1.00 25.21 ? 112 VAL A CG1 1 
ATOM   861  C  CG2 . VAL A 1 112 ? 28.023  44.930 36.166 1.00 25.90 ? 112 VAL A CG2 1 
ATOM   862  N  N   . LYS A 1 113 ? 27.646  44.609 31.483 1.00 23.39 ? 113 LYS A N   1 
ATOM   863  C  CA  . LYS A 1 113 ? 27.517  43.968 30.123 1.00 22.54 ? 113 LYS A CA  1 
ATOM   864  C  C   . LYS A 1 113 ? 28.394  42.710 30.112 1.00 22.93 ? 113 LYS A C   1 
ATOM   865  O  O   . LYS A 1 113 ? 29.588  42.717 30.575 1.00 26.08 ? 113 LYS A O   1 
ATOM   866  C  CB  . LYS A 1 113 ? 28.003  44.949 29.034 1.00 25.84 ? 113 LYS A CB  1 
ATOM   867  C  CG  . LYS A 1 113 ? 27.279  46.311 29.012 1.00 25.16 ? 113 LYS A CG  1 
ATOM   868  C  CD  . LYS A 1 113 ? 27.763  47.207 27.874 1.00 30.49 ? 113 LYS A CD  1 
ATOM   869  C  CE  . LYS A 1 113 ? 29.149  47.814 28.109 1.00 34.56 ? 113 LYS A CE  1 
ATOM   870  N  NZ  . LYS A 1 113 ? 29.178  48.716 29.319 1.00 41.70 ? 113 LYS A NZ  1 
ATOM   871  N  N   . TYR A 1 114 ? 27.849  41.616 29.609 1.00 22.34 ? 114 TYR A N   1 
ATOM   872  C  CA  . TYR A 1 114 ? 28.624  40.365 29.427 1.00 19.34 ? 114 TYR A CA  1 
ATOM   873  C  C   . TYR A 1 114 ? 29.054  40.216 27.985 1.00 20.82 ? 114 TYR A C   1 
ATOM   874  O  O   . TYR A 1 114 ? 28.651  41.042 27.173 1.00 20.21 ? 114 TYR A O   1 
ATOM   875  C  CB  . TYR A 1 114 ? 27.784  39.218 29.943 1.00 17.63 ? 114 TYR A CB  1 
ATOM   876  C  CG  . TYR A 1 114 ? 27.760  39.247 31.458 1.00 18.76 ? 114 TYR A CG  1 
ATOM   877  C  CD1 . TYR A 1 114 ? 28.710  38.536 32.198 1.00 23.22 ? 114 TYR A CD1 1 
ATOM   878  C  CD2 . TYR A 1 114 ? 26.803  40.042 32.159 1.00 19.42 ? 114 TYR A CD2 1 
ATOM   879  C  CE1 . TYR A 1 114 ? 28.740  38.622 33.595 1.00 27.37 ? 114 TYR A CE1 1 
ATOM   880  C  CE2 . TYR A 1 114 ? 26.864  40.121 33.541 1.00 22.47 ? 114 TYR A CE2 1 
ATOM   881  C  CZ  . TYR A 1 114 ? 27.836  39.448 34.236 1.00 25.89 ? 114 TYR A CZ  1 
ATOM   882  O  OH  . TYR A 1 114 ? 27.850  39.550 35.630 1.00 26.18 ? 114 TYR A OH  1 
ATOM   883  N  N   . SER A 1 115 ? 29.918  39.232 27.662 1.00 19.06 ? 115 SER A N   1 
ATOM   884  C  CA  . SER A 1 115 ? 30.502  39.190 26.334 1.00 20.84 ? 115 SER A CA  1 
ATOM   885  C  C   . SER A 1 115 ? 29.492  38.684 25.262 1.00 22.56 ? 115 SER A C   1 
ATOM   886  O  O   . SER A 1 115 ? 29.691  38.917 24.058 1.00 19.76 ? 115 SER A O   1 
ATOM   887  C  CB  . SER A 1 115 ? 31.697  38.239 26.376 1.00 23.53 ? 115 SER A CB  1 
ATOM   888  O  OG  . SER A 1 115 ? 32.689  38.852 27.188 1.00 26.77 ? 115 SER A OG  1 
ATOM   889  N  N   . ALA A 1 116 ? 28.533  37.882 25.699 1.00 19.68 ? 116 ALA A N   1 
ATOM   890  C  CA  . ALA A 1 116 ? 27.565  37.256 24.773 1.00 19.00 ? 116 ALA A CA  1 
ATOM   891  C  C   . ALA A 1 116 ? 26.328  36.800 25.593 1.00 17.08 ? 116 ALA A C   1 
ATOM   892  O  O   . ALA A 1 116 ? 26.294  36.885 26.831 1.00 15.86 ? 116 ALA A O   1 
ATOM   893  C  CB  . ALA A 1 116 ? 28.191  36.084 24.044 1.00 19.97 ? 116 ALA A CB  1 
ATOM   894  N  N   . GLU A 1 117 ? 25.340  36.267 24.909 1.00 16.28 ? 117 GLU A N   1 
ATOM   895  C  CA  . GLU A 1 117 ? 24.134  35.759 25.574 1.00 15.26 ? 117 GLU A CA  1 
ATOM   896  C  C   . GLU A 1 117 ? 23.525  34.663 24.732 1.00 17.46 ? 117 GLU A C   1 
ATOM   897  O  O   . GLU A 1 117 ? 23.507  34.764 23.486 1.00 17.73 ? 117 GLU A O   1 
ATOM   898  C  CB  . GLU A 1 117 ? 23.168  36.911 25.793 1.00 14.60 ? 117 GLU A CB  1 
ATOM   899  C  CG  . GLU A 1 117 ? 21.883  36.535 26.586 1.00 14.92 ? 117 GLU A CG  1 
ATOM   900  C  CD  . GLU A 1 117 ? 21.079  37.803 26.952 1.00 14.32 ? 117 GLU A CD  1 
ATOM   901  O  OE1 . GLU A 1 117 ? 19.823  37.744 27.064 1.00 15.53 ? 117 GLU A OE1 1 
ATOM   902  O  OE2 . GLU A 1 117 ? 21.728  38.878 27.127 1.00 16.80 ? 117 GLU A OE2 1 
ATOM   903  N  N   . LEU A 1 118 ? 23.115  33.593 25.406 1.00 14.13 ? 118 LEU A N   1 
ATOM   904  C  CA  . LEU A 1 118 ? 22.492  32.452 24.758 1.00 13.52 ? 118 LEU A CA  1 
ATOM   905  C  C   . LEU A 1 118 ? 20.986  32.617 24.918 1.00 15.23 ? 118 LEU A C   1 
ATOM   906  O  O   . LEU A 1 118 ? 20.501  32.872 26.060 1.00 13.65 ? 118 LEU A O   1 
ATOM   907  C  CB  . LEU A 1 118 ? 23.013  31.170 25.408 1.00 13.57 ? 118 LEU A CB  1 
ATOM   908  C  CG  . LEU A 1 118 ? 22.175  29.884 25.251 1.00 14.49 ? 118 LEU A CG  1 
ATOM   909  C  CD1 . LEU A 1 118 ? 22.260  29.451 23.733 1.00 15.47 ? 118 LEU A CD1 1 
ATOM   910  C  CD2 . LEU A 1 118 ? 22.626  28.815 26.247 1.00 15.96 ? 118 LEU A CD2 1 
ATOM   911  N  N   . HIS A 1 119 ? 20.256  32.397 23.844 1.00 12.75 ? 119 HIS A N   1 
ATOM   912  C  CA  . HIS A 1 119 ? 18.738  32.405 23.938 1.00 13.18 ? 119 HIS A CA  1 
ATOM   913  C  C   . HIS A 1 119 ? 18.166  31.091 23.500 1.00 15.81 ? 119 HIS A C   1 
ATOM   914  O  O   . HIS A 1 119 ? 18.556  30.605 22.413 1.00 16.50 ? 119 HIS A O   1 
ATOM   915  C  CB  . HIS A 1 119 ? 18.180  33.502 23.011 1.00 14.54 ? 119 HIS A CB  1 
ATOM   916  C  CG  . HIS A 1 119 ? 18.432  34.904 23.511 1.00 14.57 ? 119 HIS A CG  1 
ATOM   917  N  ND1 . HIS A 1 119 ? 18.301  36.002 22.748 1.00 13.77 ? 119 HIS A ND1 1 
ATOM   918  C  CD2 . HIS A 1 119 ? 18.727  35.359 24.801 1.00 14.02 ? 119 HIS A CD2 1 
ATOM   919  C  CE1 . HIS A 1 119 ? 18.524  37.126 23.480 1.00 15.39 ? 119 HIS A CE1 1 
ATOM   920  N  NE2 . HIS A 1 119 ? 18.808  36.707 24.749 1.00 13.73 ? 119 HIS A NE2 1 
ATOM   921  N  N   . VAL A 1 120 ? 17.286  30.505 24.296 1.00 13.26 ? 120 VAL A N   1 
ATOM   922  C  CA  . VAL A 1 120 ? 16.688  29.203 23.979 1.00 14.04 ? 120 VAL A CA  1 
ATOM   923  C  C   . VAL A 1 120 ? 15.173  29.500 23.906 1.00 15.77 ? 120 VAL A C   1 
ATOM   924  O  O   . VAL A 1 120 ? 14.563  29.854 24.918 1.00 13.79 ? 120 VAL A O   1 
ATOM   925  C  CB  . VAL A 1 120 ? 17.079  28.144 25.041 1.00 14.25 ? 120 VAL A CB  1 
ATOM   926  C  CG1 . VAL A 1 120 ? 16.480  26.813 24.621 1.00 14.44 ? 120 VAL A CG1 1 
ATOM   927  C  CG2 . VAL A 1 120 ? 18.617  28.108 25.304 1.00 13.52 ? 120 VAL A CG2 1 
ATOM   928  N  N   . ALA A 1 121 ? 14.578  29.452 22.688 1.00 14.68 ? 121 ALA A N   1 
ATOM   929  C  CA  . ALA A 1 121 ? 13.244  30.011 22.463 1.00 13.40 ? 121 ALA A CA  1 
ATOM   930  C  C   . ALA A 1 121 ? 12.235  28.871 22.275 1.00 14.79 ? 121 ALA A C   1 
ATOM   931  O  O   . ALA A 1 121 ? 12.527  27.786 21.676 1.00 14.62 ? 121 ALA A O   1 
ATOM   932  C  CB  . ALA A 1 121 ? 13.243  30.892 21.209 1.00 13.20 ? 121 ALA A CB  1 
ATOM   933  N  N   . HIS A 1 122 ? 11.035  29.106 22.791 1.00 13.58 ? 122 HIS A N   1 
ATOM   934  C  CA  . HIS A 1 122 ? 9.963   28.103 22.827 1.00 14.77 ? 122 HIS A CA  1 
ATOM   935  C  C   . HIS A 1 122 ? 8.636   28.808 22.518 1.00 14.89 ? 122 HIS A C   1 
ATOM   936  O  O   . HIS A 1 122 ? 8.500   29.998 22.681 1.00 16.57 ? 122 HIS A O   1 
ATOM   937  C  CB  . HIS A 1 122 ? 9.828   27.542 24.272 1.00 15.36 ? 122 HIS A CB  1 
ATOM   938  C  CG  . HIS A 1 122 ? 11.139  27.105 24.937 1.00 14.55 ? 122 HIS A CG  1 
ATOM   939  N  ND1 . HIS A 1 122 ? 12.049  27.997 25.433 1.00 16.05 ? 122 HIS A ND1 1 
ATOM   940  C  CD2 . HIS A 1 122 ? 11.590  25.852 25.298 1.00 16.97 ? 122 HIS A CD2 1 
ATOM   941  C  CE1 . HIS A 1 122 ? 13.064  27.302 26.018 1.00 14.05 ? 122 HIS A CE1 1 
ATOM   942  N  NE2 . HIS A 1 122 ? 12.782  25.995 25.906 1.00 16.23 ? 122 HIS A NE2 1 
ATOM   943  N  N   . TRP A 1 123 ? 7.621   28.057 22.120 1.00 15.53 ? 123 TRP A N   1 
ATOM   944  C  CA  . TRP A 1 123 ? 6.311   28.606 21.842 1.00 16.34 ? 123 TRP A CA  1 
ATOM   945  C  C   . TRP A 1 123 ? 5.231   27.800 22.551 1.00 17.65 ? 123 TRP A C   1 
ATOM   946  O  O   . TRP A 1 123 ? 5.349   26.593 22.795 1.00 19.07 ? 123 TRP A O   1 
ATOM   947  C  CB  . TRP A 1 123 ? 6.041   28.767 20.318 1.00 17.84 ? 123 TRP A CB  1 
ATOM   948  C  CG  . TRP A 1 123 ? 6.020   27.503 19.511 1.00 18.11 ? 123 TRP A CG  1 
ATOM   949  C  CD1 . TRP A 1 123 ? 7.076   26.929 18.853 1.00 19.55 ? 123 TRP A CD1 1 
ATOM   950  C  CD2 . TRP A 1 123 ? 4.861   26.644 19.194 1.00 19.31 ? 123 TRP A CD2 1 
ATOM   951  N  NE1 . TRP A 1 123 ? 6.672   25.793 18.151 1.00 19.26 ? 123 TRP A NE1 1 
ATOM   952  C  CE2 . TRP A 1 123 ? 5.370   25.554 18.352 1.00 18.69 ? 123 TRP A CE2 1 
ATOM   953  C  CE3 . TRP A 1 123 ? 3.504   26.656 19.505 1.00 19.63 ? 123 TRP A CE3 1 
ATOM   954  C  CZ2 . TRP A 1 123 ? 4.538   24.532 17.860 1.00 20.52 ? 123 TRP A CZ2 1 
ATOM   955  C  CZ3 . TRP A 1 123 ? 2.680   25.610 19.014 1.00 18.93 ? 123 TRP A CZ3 1 
ATOM   956  C  CH2 . TRP A 1 123 ? 3.185   24.587 18.215 1.00 19.41 ? 123 TRP A CH2 1 
ATOM   957  N  N   . ASN A 1 124 ? 4.120   28.475 22.837 1.00 17.91 ? 124 ASN A N   1 
ATOM   958  C  CA  . ASN A 1 124 ? 3.047   27.906 23.708 1.00 18.59 ? 124 ASN A CA  1 
ATOM   959  C  C   . ASN A 1 124 ? 2.194   26.903 22.945 1.00 20.82 ? 124 ASN A C   1 
ATOM   960  O  O   . ASN A 1 124 ? 1.323   27.303 22.221 1.00 19.61 ? 124 ASN A O   1 
ATOM   961  C  CB  . ASN A 1 124 ? 2.194   29.045 24.235 1.00 20.20 ? 124 ASN A CB  1 
ATOM   962  C  CG  . ASN A 1 124 ? 1.191   28.605 25.310 1.00 22.45 ? 124 ASN A CG  1 
ATOM   963  O  OD1 . ASN A 1 124 ? 0.794   27.450 25.389 1.00 23.50 ? 124 ASN A OD1 1 
ATOM   964  N  ND2 . ASN A 1 124 ? 0.822   29.564 26.195 1.00 24.90 ? 124 ASN A ND2 1 
ATOM   965  N  N   . SER A 1 125 ? 2.469   25.634 23.126 1.00 19.67 ? 125 SER A N   1 
ATOM   966  C  CA  . SER A 1 125 ? 1.737   24.578 22.363 1.00 21.60 ? 125 SER A CA  1 
ATOM   967  C  C   . SER A 1 125 ? 0.429   24.204 23.101 1.00 25.13 ? 125 SER A C   1 
ATOM   968  O  O   . SER A 1 125 ? -0.348  23.382 22.617 1.00 23.04 ? 125 SER A O   1 
ATOM   969  C  CB  . SER A 1 125 ? 2.599   23.364 22.081 1.00 24.96 ? 125 SER A CB  1 
ATOM   970  O  OG  . SER A 1 125 ? 3.053   22.807 23.302 1.00 27.39 ? 125 SER A OG  1 
ATOM   971  N  N   . ALA A 1 126 ? 0.181   24.808 24.261 1.00 25.01 ? 126 ALA A N   1 
ATOM   972  C  CA  . ALA A 1 126 ? -1.056  24.528 24.998 1.00 27.81 ? 126 ALA A CA  1 
ATOM   973  C  C   . ALA A 1 126 ? -2.147  25.330 24.384 1.00 29.91 ? 126 ALA A C   1 
ATOM   974  O  O   . ALA A 1 126 ? -3.261  24.840 24.195 1.00 30.15 ? 126 ALA A O   1 
ATOM   975  C  CB  . ALA A 1 126 ? -0.949  24.864 26.490 1.00 32.20 ? 126 ALA A CB  1 
ATOM   976  N  N   . LYS A 1 127 ? -1.818  26.547 24.014 1.00 27.30 ? 127 LYS A N   1 
ATOM   977  C  CA  . LYS A 1 127 ? -2.807  27.460 23.520 1.00 27.12 ? 127 LYS A CA  1 
ATOM   978  C  C   . LYS A 1 127 ? -2.820  27.504 21.983 1.00 28.85 ? 127 LYS A C   1 
ATOM   979  O  O   . LYS A 1 127 ? -3.897  27.655 21.382 1.00 28.42 ? 127 LYS A O   1 
ATOM   980  C  CB  . LYS A 1 127 ? -2.574  28.843 24.128 1.00 32.59 ? 127 LYS A CB  1 
ATOM   981  C  CG  . LYS A 1 127 ? -2.879  28.901 25.627 1.00 33.11 ? 127 LYS A CG  1 
ATOM   982  C  CD  . LYS A 1 127 ? -3.065  30.353 26.057 1.00 35.03 ? 127 LYS A CD  1 
ATOM   983  C  CE  . LYS A 1 127 ? -4.207  31.077 25.338 1.00 36.54 ? 127 LYS A CE  1 
ATOM   984  N  NZ  . LYS A 1 127 ? -4.430  32.514 25.769 1.00 38.16 ? 127 LYS A NZ  1 
ATOM   985  N  N   . TYR A 1 128 ? -1.656  27.343 21.338 1.00 24.55 ? 128 TYR A N   1 
ATOM   986  C  CA  . TYR A 1 128 ? -1.545  27.534 19.892 1.00 20.99 ? 128 TYR A CA  1 
ATOM   987  C  C   . TYR A 1 128 ? -1.065  26.299 19.216 1.00 22.60 ? 128 TYR A C   1 
ATOM   988  O  O   . TYR A 1 128 ? -0.532  25.401 19.892 1.00 22.77 ? 128 TYR A O   1 
ATOM   989  C  CB  . TYR A 1 128 ? -0.633  28.736 19.615 1.00 21.22 ? 128 TYR A CB  1 
ATOM   990  C  CG  . TYR A 1 128 ? -1.113  29.903 20.435 1.00 22.46 ? 128 TYR A CG  1 
ATOM   991  C  CD1 . TYR A 1 128 ? -2.398  30.450 20.263 1.00 22.39 ? 128 TYR A CD1 1 
ATOM   992  C  CD2 . TYR A 1 128 ? -0.309  30.450 21.435 1.00 23.46 ? 128 TYR A CD2 1 
ATOM   993  C  CE1 . TYR A 1 128 ? -2.829  31.521 21.038 1.00 24.54 ? 128 TYR A CE1 1 
ATOM   994  C  CE2 . TYR A 1 128 ? -0.746  31.529 22.199 1.00 22.33 ? 128 TYR A CE2 1 
ATOM   995  C  CZ  . TYR A 1 128 ? -2.001  32.040 22.003 1.00 26.62 ? 128 TYR A CZ  1 
ATOM   996  O  OH  . TYR A 1 128 ? -2.401  33.082 22.817 1.00 25.98 ? 128 TYR A OH  1 
ATOM   997  N  N   A SER A 1 129 ? -1.244  26.198 17.895 0.50 22.77 ? 129 SER A N   1 
ATOM   998  N  N   B SER A 1 129 ? -1.307  26.215 17.892 0.50 22.33 ? 129 SER A N   1 
ATOM   999  C  CA  A SER A 1 129 ? -0.796  24.990 17.225 0.50 23.62 ? 129 SER A CA  1 
ATOM   1000 C  CA  B SER A 1 129 ? -0.932  25.041 17.104 0.50 23.35 ? 129 SER A CA  1 
ATOM   1001 C  C   A SER A 1 129 ? 0.321   25.180 16.205 0.50 23.87 ? 129 SER A C   1 
ATOM   1002 C  C   B SER A 1 129 ? 0.364   25.156 16.296 0.50 23.67 ? 129 SER A C   1 
ATOM   1003 O  O   A SER A 1 129 ? 0.675   24.243 15.457 0.50 24.74 ? 129 SER A O   1 
ATOM   1004 O  O   B SER A 1 129 ? 0.874   24.132 15.783 0.50 24.34 ? 129 SER A O   1 
ATOM   1005 C  CB  A SER A 1 129 ? -1.996  24.234 16.655 0.50 26.99 ? 129 SER A CB  1 
ATOM   1006 C  CB  B SER A 1 129 ? -2.107  24.553 16.209 0.50 25.21 ? 129 SER A CB  1 
ATOM   1007 O  OG  A SER A 1 129 ? -2.884  23.954 17.712 0.50 27.08 ? 129 SER A OG  1 
ATOM   1008 O  OG  B SER A 1 129 ? -2.486  25.488 15.211 0.50 25.37 ? 129 SER A OG  1 
ATOM   1009 N  N   . SER A 1 130 ? 0.951   26.362 16.206 1.00 22.35 ? 130 SER A N   1 
ATOM   1010 C  CA  . SER A 1 130 ? 2.185   26.514 15.419 1.00 21.66 ? 130 SER A CA  1 
ATOM   1011 C  C   . SER A 1 130 ? 2.935   27.696 15.984 1.00 18.70 ? 130 SER A C   1 
ATOM   1012 O  O   . SER A 1 130 ? 2.304   28.549 16.587 1.00 19.39 ? 130 SER A O   1 
ATOM   1013 C  CB  . SER A 1 130 ? 1.899   26.752 13.877 1.00 21.84 ? 130 SER A CB  1 
ATOM   1014 O  OG  . SER A 1 130 ? 1.234   28.004 13.698 1.00 22.78 ? 130 SER A OG  1 
ATOM   1015 N  N   . LEU A 1 131 ? 4.247   27.708 15.783 1.00 19.53 ? 131 LEU A N   1 
ATOM   1016 C  CA  . LEU A 1 131 ? 5.051   28.946 15.959 1.00 17.24 ? 131 LEU A CA  1 
ATOM   1017 C  C   . LEU A 1 131 ? 4.411   30.162 15.319 1.00 19.19 ? 131 LEU A C   1 
ATOM   1018 O  O   . LEU A 1 131 ? 4.403   31.243 15.899 1.00 19.03 ? 131 LEU A O   1 
ATOM   1019 C  CB  . LEU A 1 131 ? 6.507   28.762 15.494 1.00 17.10 ? 131 LEU A CB  1 
ATOM   1020 C  CG  . LEU A 1 131 ? 7.436   29.996 15.488 1.00 17.84 ? 131 LEU A CG  1 
ATOM   1021 C  CD1 . LEU A 1 131 ? 7.573   30.495 16.926 1.00 17.67 ? 131 LEU A CD1 1 
ATOM   1022 C  CD2 . LEU A 1 131 ? 8.843   29.683 14.905 1.00 20.02 ? 131 LEU A CD2 1 
ATOM   1023 N  N   . ALA A 1 132 ? 3.996   30.036 14.048 1.00 17.95 ? 132 ALA A N   1 
ATOM   1024 C  CA  . ALA A 1 132 ? 3.525   31.231 13.350 1.00 21.72 ? 132 ALA A CA  1 
ATOM   1025 C  C   . ALA A 1 132 ? 2.290   31.800 14.039 1.00 18.74 ? 132 ALA A C   1 
ATOM   1026 O  O   . ALA A 1 132 ? 2.093   33.024 14.081 1.00 21.88 ? 132 ALA A O   1 
ATOM   1027 C  CB  . ALA A 1 132 ? 3.195   30.854 11.908 1.00 22.75 ? 132 ALA A CB  1 
ATOM   1028 N  N   . GLU A 1 133 ? 1.416   30.932 14.533 1.00 18.90 ? 133 GLU A N   1 
ATOM   1029 C  CA  . GLU A 1 133 ? 0.267   31.391 15.296 1.00 20.29 ? 133 GLU A CA  1 
ATOM   1030 C  C   . GLU A 1 133 ? 0.664   32.039 16.658 1.00 19.83 ? 133 GLU A C   1 
ATOM   1031 O  O   . GLU A 1 133 ? 0.188   33.107 17.005 1.00 20.52 ? 133 GLU A O   1 
ATOM   1032 C  CB  . GLU A 1 133 ? -0.671  30.201 15.555 1.00 22.01 ? 133 GLU A CB  1 
ATOM   1033 C  CG  . GLU A 1 133 ? -1.956  30.597 16.289 1.00 20.69 ? 133 GLU A CG  1 
ATOM   1034 C  CD  . GLU A 1 133 ? -2.851  29.402 16.709 1.00 22.88 ? 133 GLU A CD  1 
ATOM   1035 O  OE1 . GLU A 1 133 ? -2.517  28.215 16.423 1.00 21.81 ? 133 GLU A OE1 1 
ATOM   1036 O  OE2 . GLU A 1 133 ? -3.851  29.701 17.415 1.00 26.16 ? 133 GLU A OE2 1 
ATOM   1037 N  N   . ALA A 1 134 ? 1.601   31.393 17.357 1.00 19.52 ? 134 ALA A N   1 
ATOM   1038 C  CA  . ALA A 1 134 ? 2.017   31.820 18.698 1.00 17.54 ? 134 ALA A CA  1 
ATOM   1039 C  C   . ALA A 1 134 ? 2.795   33.142 18.695 1.00 19.27 ? 134 ALA A C   1 
ATOM   1040 O  O   . ALA A 1 134 ? 2.779   33.857 19.704 1.00 20.34 ? 134 ALA A O   1 
ATOM   1041 C  CB  . ALA A 1 134 ? 2.908   30.734 19.300 1.00 18.49 ? 134 ALA A CB  1 
ATOM   1042 N  N   . ALA A 1 135 ? 3.510   33.434 17.625 1.00 19.49 ? 135 ALA A N   1 
ATOM   1043 C  CA  . ALA A 1 135 ? 4.629   34.368 17.748 1.00 21.47 ? 135 ALA A CA  1 
ATOM   1044 C  C   . ALA A 1 135 ? 4.199   35.772 18.101 1.00 22.33 ? 135 ALA A C   1 
ATOM   1045 O  O   . ALA A 1 135 ? 4.977   36.496 18.706 1.00 22.64 ? 135 ALA A O   1 
ATOM   1046 C  CB  . ALA A 1 135 ? 5.515   34.365 16.510 1.00 23.16 ? 135 ALA A CB  1 
ATOM   1047 N  N   . SER A 1 136 ? 2.993   36.165 17.693 1.00 23.09 ? 136 SER A N   1 
ATOM   1048 C  CA  . SER A 1 136 ? 2.562   37.572 17.913 1.00 22.58 ? 136 SER A CA  1 
ATOM   1049 C  C   . SER A 1 136 ? 1.618   37.709 19.143 1.00 24.93 ? 136 SER A C   1 
ATOM   1050 O  O   . SER A 1 136 ? 1.065   38.801 19.380 1.00 28.52 ? 136 SER A O   1 
ATOM   1051 C  CB  . SER A 1 136 ? 1.897   38.059 16.628 1.00 27.95 ? 136 SER A CB  1 
ATOM   1052 O  OG  . SER A 1 136 ? 0.644   37.440 16.513 1.00 30.24 ? 136 SER A OG  1 
ATOM   1053 N  N   . LYS A 1 137 ? 1.397   36.609 19.871 1.00 22.43 ? 137 LYS A N   1 
ATOM   1054 C  CA  . LYS A 1 137 ? 0.430   36.526 21.020 1.00 23.83 ? 137 LYS A CA  1 
ATOM   1055 C  C   . LYS A 1 137 ? 1.144   36.879 22.311 1.00 26.56 ? 137 LYS A C   1 
ATOM   1056 O  O   . LYS A 1 137 ? 2.290   36.548 22.450 1.00 20.80 ? 137 LYS A O   1 
ATOM   1057 C  CB  . LYS A 1 137 ? -0.145  35.137 21.234 1.00 25.01 ? 137 LYS A CB  1 
ATOM   1058 C  CG  . LYS A 1 137 ? -0.857  34.584 20.009 1.00 31.57 ? 137 LYS A CG  1 
ATOM   1059 C  CD  . LYS A 1 137 ? -2.082  35.398 19.688 1.00 32.58 ? 137 LYS A CD  1 
ATOM   1060 C  CE  . LYS A 1 137 ? -2.717  34.853 18.410 1.00 38.22 ? 137 LYS A CE  1 
ATOM   1061 N  NZ  . LYS A 1 137 ? -3.969  35.621 18.151 1.00 42.58 ? 137 LYS A NZ  1 
ATOM   1062 N  N   . ALA A 1 138 ? 0.448   37.518 23.252 1.00 24.15 ? 138 ALA A N   1 
ATOM   1063 C  CA  . ALA A 1 138 ? 1.179   38.027 24.450 1.00 26.43 ? 138 ALA A CA  1 
ATOM   1064 C  C   . ALA A 1 138 ? 1.741   36.898 25.258 1.00 25.30 ? 138 ALA A C   1 
ATOM   1065 O  O   . ALA A 1 138 ? 2.788   37.077 25.853 1.00 27.27 ? 138 ALA A O   1 
ATOM   1066 C  CB  . ALA A 1 138 ? 0.256   38.866 25.332 1.00 26.96 ? 138 ALA A CB  1 
ATOM   1067 N  N   . ASP A 1 139 ? 1.034   35.763 25.304 1.00 23.03 ? 139 ASP A N   1 
ATOM   1068 C  CA  . ASP A 1 139 ? 1.499   34.553 26.011 1.00 25.44 ? 139 ASP A CA  1 
ATOM   1069 C  C   . ASP A 1 139 ? 2.066   33.489 25.064 1.00 20.70 ? 139 ASP A C   1 
ATOM   1070 O  O   . ASP A 1 139 ? 2.083   32.306 25.355 1.00 21.54 ? 139 ASP A O   1 
ATOM   1071 C  CB  . ASP A 1 139 ? 0.351   33.945 26.805 1.00 27.63 ? 139 ASP A CB  1 
ATOM   1072 C  CG  . ASP A 1 139 ? -0.830  33.571 25.931 1.00 33.59 ? 139 ASP A CG  1 
ATOM   1073 O  OD1 . ASP A 1 139 ? -0.809  33.916 24.743 1.00 26.05 ? 139 ASP A OD1 1 
ATOM   1074 O  OD2 . ASP A 1 139 ? -1.771  32.897 26.428 1.00 35.76 ? 139 ASP A OD2 1 
ATOM   1075 N  N   . GLY A 1 140 ? 2.561   33.913 23.924 1.00 19.51 ? 140 GLY A N   1 
ATOM   1076 C  CA  . GLY A 1 140 ? 2.929   32.906 22.887 1.00 17.57 ? 140 GLY A CA  1 
ATOM   1077 C  C   . GLY A 1 140 ? 4.337   32.340 22.943 1.00 15.72 ? 140 GLY A C   1 
ATOM   1078 O  O   . GLY A 1 140 ? 4.528   31.214 22.504 1.00 16.89 ? 140 GLY A O   1 
ATOM   1079 N  N   . LEU A 1 141 ? 5.317   33.101 23.444 1.00 15.43 ? 141 LEU A N   1 
ATOM   1080 C  CA  . LEU A 1 141 ? 6.718   32.677 23.431 1.00 15.62 ? 141 LEU A CA  1 
ATOM   1081 C  C   . LEU A 1 141 ? 7.363   32.755 24.813 1.00 16.35 ? 141 LEU A C   1 
ATOM   1082 O  O   . LEU A 1 141 ? 6.933   33.609 25.665 1.00 17.10 ? 141 LEU A O   1 
ATOM   1083 C  CB  . LEU A 1 141 ? 7.553   33.565 22.480 1.00 15.92 ? 141 LEU A CB  1 
ATOM   1084 C  CG  . LEU A 1 141 ? 7.033   33.726 21.033 1.00 16.88 ? 141 LEU A CG  1 
ATOM   1085 C  CD1 . LEU A 1 141 ? 7.976   34.664 20.233 1.00 15.85 ? 141 LEU A CD1 1 
ATOM   1086 C  CD2 . LEU A 1 141 ? 6.912   32.350 20.350 1.00 16.71 ? 141 LEU A CD2 1 
ATOM   1087 N  N   . ALA A 1 142 ? 8.323   31.845 25.043 1.00 17.23 ? 142 ALA A N   1 
ATOM   1088 C  CA  . ALA A 1 142 ? 9.093   31.838 26.313 1.00 16.08 ? 142 ALA A CA  1 
ATOM   1089 C  C   . ALA A 1 142 ? 10.547  31.708 25.861 1.00 16.89 ? 142 ALA A C   1 
ATOM   1090 O  O   . ALA A 1 142 ? 10.884  30.795 25.057 1.00 15.89 ? 142 ALA A O   1 
ATOM   1091 C  CB  . ALA A 1 142 ? 8.704   30.690 27.206 1.00 16.62 ? 142 ALA A CB  1 
ATOM   1092 N  N   . VAL A 1 143 ? 11.384  32.628 26.302 1.00 14.98 ? 143 VAL A N   1 
ATOM   1093 C  CA  . VAL A 1 143 ? 12.862  32.531 25.912 1.00 14.58 ? 143 VAL A CA  1 
ATOM   1094 C  C   . VAL A 1 143 ? 13.709  32.532 27.191 1.00 15.98 ? 143 VAL A C   1 
ATOM   1095 O  O   . VAL A 1 143 ? 13.541  33.426 28.008 1.00 15.89 ? 143 VAL A O   1 
ATOM   1096 C  CB  . VAL A 1 143 ? 13.334  33.676 25.008 1.00 16.68 ? 143 VAL A CB  1 
ATOM   1097 C  CG1 . VAL A 1 143 ? 14.819  33.441 24.560 1.00 17.60 ? 143 VAL A CG1 1 
ATOM   1098 C  CG2 . VAL A 1 143 ? 12.457  33.787 23.766 1.00 17.51 ? 143 VAL A CG2 1 
ATOM   1099 N  N   . ILE A 1 144 ? 14.590  31.546 27.325 1.00 15.19 ? 144 ILE A N   1 
ATOM   1100 C  CA  . ILE A 1 144 ? 15.592  31.503 28.426 1.00 14.90 ? 144 ILE A CA  1 
ATOM   1101 C  C   . ILE A 1 144 ? 16.754  32.263 27.937 1.00 15.69 ? 144 ILE A C   1 
ATOM   1102 O  O   . ILE A 1 144 ? 17.267  31.959 26.835 1.00 16.51 ? 144 ILE A O   1 
ATOM   1103 C  CB  . ILE A 1 144 ? 15.999  30.072 28.712 1.00 15.16 ? 144 ILE A CB  1 
ATOM   1104 C  CG1 . ILE A 1 144 ? 14.746  29.222 29.198 1.00 16.29 ? 144 ILE A CG1 1 
ATOM   1105 C  CG2 . ILE A 1 144 ? 17.071  30.122 29.834 1.00 13.71 ? 144 ILE A CG2 1 
ATOM   1106 C  CD1 . ILE A 1 144 ? 14.999  27.717 29.210 1.00 16.82 ? 144 ILE A CD1 1 
ATOM   1107 N  N   . GLY A 1 145 ? 17.276  33.217 28.757 1.00 14.40 ? 145 GLY A N   1 
ATOM   1108 C  CA  . GLY A 1 145 ? 18.505  33.938 28.377 1.00 13.66 ? 145 GLY A CA  1 
ATOM   1109 C  C   . GLY A 1 145 ? 19.566  33.538 29.406 1.00 18.01 ? 145 GLY A C   1 
ATOM   1110 O  O   . GLY A 1 145 ? 19.286  33.417 30.634 1.00 20.13 ? 145 GLY A O   1 
ATOM   1111 N  N   . VAL A 1 146 ? 20.760  33.268 28.909 1.00 15.15 ? 146 VAL A N   1 
ATOM   1112 C  CA  . VAL A 1 146 ? 21.937  32.960 29.749 1.00 15.10 ? 146 VAL A CA  1 
ATOM   1113 C  C   . VAL A 1 146 ? 23.072  33.878 29.388 1.00 16.38 ? 146 VAL A C   1 
ATOM   1114 O  O   . VAL A 1 146 ? 23.530  33.940 28.207 1.00 15.61 ? 146 VAL A O   1 
ATOM   1115 C  CB  . VAL A 1 146 ? 22.447  31.555 29.539 1.00 14.90 ? 146 VAL A CB  1 
ATOM   1116 C  CG1 . VAL A 1 146 ? 23.616  31.311 30.523 1.00 14.66 ? 146 VAL A CG1 1 
ATOM   1117 C  CG2 . VAL A 1 146 ? 21.299  30.544 29.649 1.00 15.55 ? 146 VAL A CG2 1 
ATOM   1118 N  N   . LEU A 1 147 ? 23.577  34.629 30.370 1.00 16.76 ? 147 LEU A N   1 
ATOM   1119 C  CA  . LEU A 1 147 ? 24.652  35.577 30.148 1.00 16.53 ? 147 LEU A CA  1 
ATOM   1120 C  C   . LEU A 1 147 ? 25.924  34.741 30.025 1.00 16.35 ? 147 LEU A C   1 
ATOM   1121 O  O   . LEU A 1 147 ? 26.097  33.756 30.762 1.00 16.25 ? 147 LEU A O   1 
ATOM   1122 C  CB  . LEU A 1 147 ? 24.729  36.581 31.347 1.00 18.24 ? 147 LEU A CB  1 
ATOM   1123 C  CG  . LEU A 1 147 ? 23.489  37.455 31.363 1.00 21.32 ? 147 LEU A CG  1 
ATOM   1124 C  CD1 . LEU A 1 147 ? 23.261  38.076 32.698 1.00 24.03 ? 147 LEU A CD1 1 
ATOM   1125 C  CD2 . LEU A 1 147 ? 23.608  38.513 30.281 1.00 18.96 ? 147 LEU A CD2 1 
ATOM   1126 N  N   . MET A 1 148 ? 26.751  35.103 29.068 1.00 16.48 ? 148 MET A N   1 
ATOM   1127 C  CA  . MET A 1 148 ? 28.031  34.412 28.802 1.00 15.29 ? 148 MET A CA  1 
ATOM   1128 C  C   . MET A 1 148 ? 29.206  35.320 29.137 1.00 16.44 ? 148 MET A C   1 
ATOM   1129 O  O   . MET A 1 148 ? 29.337  36.400 28.601 1.00 17.03 ? 148 MET A O   1 
ATOM   1130 C  CB  . MET A 1 148 ? 28.130  33.964 27.325 1.00 17.38 ? 148 MET A CB  1 
ATOM   1131 C  CG  . MET A 1 148 ? 26.957  33.057 27.016 1.00 17.83 ? 148 MET A CG  1 
ATOM   1132 S  SD  . MET A 1 148 ? 26.793  32.512 25.276 1.00 18.55 ? 148 MET A SD  1 
ATOM   1133 C  CE  . MET A 1 148 ? 28.399  31.721 25.019 1.00 18.09 ? 148 MET A CE  1 
ATOM   1134 N  N   . LYS A 1 149 ? 30.060  34.829 30.020 1.00 17.33 ? 149 LYS A N   1 
ATOM   1135 C  CA  . LYS A 1 149 ? 31.100  35.667 30.580 1.00 18.06 ? 149 LYS A CA  1 
ATOM   1136 C  C   . LYS A 1 149 ? 32.470  35.172 30.038 1.00 16.38 ? 149 LYS A C   1 
ATOM   1137 O  O   . LYS A 1 149 ? 32.772  33.984 30.147 1.00 17.64 ? 149 LYS A O   1 
ATOM   1138 C  CB  . LYS A 1 149 ? 31.066  35.465 32.112 1.00 20.47 ? 149 LYS A CB  1 
ATOM   1139 C  CG  . LYS A 1 149 ? 32.083  36.327 32.864 1.00 22.05 ? 149 LYS A CG  1 
ATOM   1140 C  CD  . LYS A 1 149 ? 31.986  35.856 34.325 1.00 24.94 ? 149 LYS A CD  1 
ATOM   1141 C  CE  . LYS A 1 149 ? 32.702  36.828 35.224 1.00 29.98 ? 149 LYS A CE  1 
ATOM   1142 N  NZ  . LYS A 1 149 ? 34.150  36.890 34.854 1.00 27.05 ? 149 LYS A NZ  1 
ATOM   1143 N  N   . VAL A 1 150 ? 33.257  36.087 29.485 1.00 19.98 ? 150 VAL A N   1 
ATOM   1144 C  CA  . VAL A 1 150 ? 34.551  35.716 28.901 1.00 18.89 ? 150 VAL A CA  1 
ATOM   1145 C  C   . VAL A 1 150 ? 35.454  35.106 29.975 1.00 19.32 ? 150 VAL A C   1 
ATOM   1146 O  O   . VAL A 1 150 ? 35.533  35.627 31.107 1.00 17.32 ? 150 VAL A O   1 
ATOM   1147 C  CB  . VAL A 1 150 ? 35.184  36.878 28.121 1.00 20.84 ? 150 VAL A CB  1 
ATOM   1148 C  CG1 . VAL A 1 150 ? 35.668  37.981 29.063 1.00 23.83 ? 150 VAL A CG1 1 
ATOM   1149 C  CG2 . VAL A 1 150 ? 36.307  36.340 27.213 1.00 24.04 ? 150 VAL A CG2 1 
ATOM   1150 N  N   . GLY A 1 151 ? 36.077  33.983 29.670 1.00 19.73 ? 151 GLY A N   1 
ATOM   1151 C  CA  . GLY A 1 151 ? 36.939  33.290 30.657 1.00 18.62 ? 151 GLY A CA  1 
ATOM   1152 C  C   . GLY A 1 151 ? 37.392  32.012 30.041 1.00 19.32 ? 151 GLY A C   1 
ATOM   1153 O  O   . GLY A 1 151 ? 37.874  32.026 28.847 1.00 23.99 ? 151 GLY A O   1 
ATOM   1154 N  N   . GLU A 1 152 ? 37.234  30.896 30.747 1.00 23.72 ? 152 GLU A N   1 
ATOM   1155 C  CA  . GLU A 1 152 ? 37.745  29.615 30.288 1.00 23.54 ? 152 GLU A CA  1 
ATOM   1156 C  C   . GLU A 1 152 ? 36.920  29.073 29.123 1.00 23.99 ? 152 GLU A C   1 
ATOM   1157 O  O   . GLU A 1 152 ? 35.697  29.276 29.045 1.00 21.45 ? 152 GLU A O   1 
ATOM   1158 C  CB  . GLU A 1 152 ? 37.641  28.554 31.409 1.00 31.77 ? 152 GLU A CB  1 
ATOM   1159 C  CG  . GLU A 1 152 ? 38.545  28.782 32.609 1.00 44.46 ? 152 GLU A CG  1 
ATOM   1160 C  CD  . GLU A 1 152 ? 40.010  28.610 32.258 1.00 57.14 ? 152 GLU A CD  1 
ATOM   1161 O  OE1 . GLU A 1 152 ? 40.563  27.531 32.599 1.00 65.03 ? 152 GLU A OE1 1 
ATOM   1162 O  OE2 . GLU A 1 152 ? 40.594  29.535 31.623 1.00 61.10 ? 152 GLU A OE2 1 
ATOM   1163 N  N   . ALA A 1 153 ? 37.570  28.367 28.211 1.00 24.24 ? 153 ALA A N   1 
ATOM   1164 C  CA  . ALA A 1 153 ? 36.790  27.765 27.109 1.00 22.25 ? 153 ALA A CA  1 
ATOM   1165 C  C   . ALA A 1 153 ? 35.689  26.911 27.587 1.00 20.13 ? 153 ALA A C   1 
ATOM   1166 O  O   . ALA A 1 153 ? 35.797  26.183 28.561 1.00 22.11 ? 153 ALA A O   1 
ATOM   1167 C  CB  . ALA A 1 153 ? 37.704  26.990 26.120 1.00 23.37 ? 153 ALA A CB  1 
ATOM   1168 N  N   . ASN A 1 154 ? 34.541  26.956 26.902 1.00 18.75 ? 154 ASN A N   1 
ATOM   1169 C  CA  . ASN A 1 154 ? 33.379  26.178 27.362 1.00 20.20 ? 154 ASN A CA  1 
ATOM   1170 C  C   . ASN A 1 154 ? 33.248  24.930 26.495 1.00 21.86 ? 154 ASN A C   1 
ATOM   1171 O  O   . ASN A 1 154 ? 32.898  25.049 25.320 1.00 19.90 ? 154 ASN A O   1 
ATOM   1172 C  CB  . ASN A 1 154 ? 32.107  27.009 27.142 1.00 21.98 ? 154 ASN A CB  1 
ATOM   1173 C  CG  . ASN A 1 154 ? 30.906  26.388 27.796 1.00 22.30 ? 154 ASN A CG  1 
ATOM   1174 O  OD1 . ASN A 1 154 ? 30.810  25.173 27.922 1.00 23.42 ? 154 ASN A OD1 1 
ATOM   1175 N  ND2 . ASN A 1 154 ? 29.960  27.233 28.234 1.00 22.53 ? 154 ASN A ND2 1 
ATOM   1176 N  N   . PRO A 1 155 ? 33.565  23.764 27.018 1.00 22.84 ? 155 PRO A N   1 
ATOM   1177 C  CA  . PRO A 1 155 ? 33.595  22.680 26.031 1.00 25.33 ? 155 PRO A CA  1 
ATOM   1178 C  C   . PRO A 1 155 ? 32.165  22.250 25.594 1.00 26.11 ? 155 PRO A C   1 
ATOM   1179 O  O   . PRO A 1 155 ? 32.012  21.557 24.607 1.00 27.00 ? 155 PRO A O   1 
ATOM   1180 C  CB  . PRO A 1 155 ? 34.343  21.540 26.775 1.00 29.82 ? 155 PRO A CB  1 
ATOM   1181 C  CG  . PRO A 1 155 ? 34.233  21.880 28.251 1.00 26.48 ? 155 PRO A CG  1 
ATOM   1182 C  CD  . PRO A 1 155 ? 34.151  23.389 28.330 1.00 24.25 ? 155 PRO A CD  1 
ATOM   1183 N  N   . LYS A 1 156 ? 31.122  22.679 26.286 1.00 24.63 ? 156 LYS A N   1 
ATOM   1184 C  CA  . LYS A 1 156 ? 29.779  22.298 25.875 1.00 27.14 ? 156 LYS A CA  1 
ATOM   1185 C  C   . LYS A 1 156 ? 29.392  23.012 24.576 1.00 25.27 ? 156 LYS A C   1 
ATOM   1186 O  O   . LYS A 1 156 ? 28.427  22.597 23.937 1.00 23.46 ? 156 LYS A O   1 
ATOM   1187 C  CB  . LYS A 1 156 ? 28.707  22.625 26.919 1.00 26.19 ? 156 LYS A CB  1 
ATOM   1188 C  CG  . LYS A 1 156 ? 28.982  22.225 28.367 1.00 33.22 ? 156 LYS A CG  1 
ATOM   1189 C  CD  . LYS A 1 156 ? 28.512  20.829 28.744 1.00 31.92 ? 156 LYS A CD  1 
ATOM   1190 C  CE  . LYS A 1 156 ? 28.638  20.644 30.268 1.00 42.00 ? 156 LYS A CE  1 
ATOM   1191 N  NZ  . LYS A 1 156 ? 27.835  21.681 30.997 1.00 44.85 ? 156 LYS A NZ  1 
ATOM   1192 N  N   . LEU A 1 157 ? 30.093  24.086 24.227 1.00 22.43 ? 157 LEU A N   1 
ATOM   1193 C  CA  . LEU A 1 157 ? 29.840  24.761 22.950 1.00 26.12 ? 157 LEU A CA  1 
ATOM   1194 C  C   . LEU A 1 157 ? 30.388  24.051 21.707 1.00 29.10 ? 157 LEU A C   1 
ATOM   1195 O  O   . LEU A 1 157 ? 30.137  24.532 20.590 1.00 27.96 ? 157 LEU A O   1 
ATOM   1196 C  CB  . LEU A 1 157 ? 30.421  26.166 22.923 1.00 24.46 ? 157 LEU A CB  1 
ATOM   1197 C  CG  . LEU A 1 157 ? 29.781  27.132 23.901 1.00 24.71 ? 157 LEU A CG  1 
ATOM   1198 C  CD1 . LEU A 1 157 ? 30.539  28.450 23.864 1.00 24.12 ? 157 LEU A CD1 1 
ATOM   1199 C  CD2 . LEU A 1 157 ? 28.296  27.300 23.559 1.00 27.82 ? 157 LEU A CD2 1 
ATOM   1200 N  N   . GLN A 1 158 ? 31.163  22.984 21.912 1.00 27.88 ? 158 GLN A N   1 
ATOM   1201 C  CA  . GLN A 1 158 ? 31.918  22.313 20.830 1.00 29.24 ? 158 GLN A CA  1 
ATOM   1202 C  C   . GLN A 1 158 ? 31.213  21.967 19.554 1.00 28.50 ? 158 GLN A C   1 
ATOM   1203 O  O   . GLN A 1 158 ? 31.667  22.346 18.472 1.00 31.21 ? 158 GLN A O   1 
ATOM   1204 C  CB  . GLN A 1 158 ? 32.692  21.071 21.331 1.00 34.59 ? 158 GLN A CB  1 
ATOM   1205 C  CG  . GLN A 1 158 ? 33.892  20.749 20.453 1.00 38.50 ? 158 GLN A CG  1 
ATOM   1206 C  CD  . GLN A 1 158 ? 34.805  21.931 20.263 1.00 41.24 ? 158 GLN A CD  1 
ATOM   1207 O  OE1 . GLN A 1 158 ? 35.415  22.417 21.209 1.00 46.02 ? 158 GLN A OE1 1 
ATOM   1208 N  NE2 . GLN A 1 158 ? 34.905  22.401 19.057 1.00 40.62 ? 158 GLN A NE2 1 
ATOM   1209 N  N   . LYS A 1 159 ? 30.123  21.199 19.687 1.00 27.91 ? 159 LYS A N   1 
ATOM   1210 C  CA  . LYS A 1 159 ? 29.371  20.728 18.500 1.00 26.43 ? 159 LYS A CA  1 
ATOM   1211 C  C   . LYS A 1 159 ? 28.902  21.951 17.742 1.00 25.18 ? 159 LYS A C   1 
ATOM   1212 O  O   . LYS A 1 159 ? 29.026  22.006 16.507 1.00 25.14 ? 159 LYS A O   1 
ATOM   1213 C  CB  . LYS A 1 159 ? 28.184  19.896 18.897 1.00 28.58 ? 159 LYS A CB  1 
ATOM   1214 C  CG  . LYS A 1 159 ? 27.558  19.136 17.709 1.00 30.08 ? 159 LYS A CG  1 
ATOM   1215 C  CD  . LYS A 1 159 ? 26.204  18.575 18.079 1.00 28.81 ? 159 LYS A CD  1 
ATOM   1216 C  CE  . LYS A 1 159 ? 25.458  18.186 16.811 1.00 32.58 ? 159 LYS A CE  1 
ATOM   1217 N  NZ  . LYS A 1 159 ? 25.951  16.809 16.481 1.00 28.27 ? 159 LYS A NZ  1 
ATOM   1218 N  N   . VAL A 1 160 ? 28.435  22.987 18.461 1.00 26.55 ? 160 VAL A N   1 
ATOM   1219 C  CA  . VAL A 1 160 ? 27.965  24.231 17.756 1.00 23.49 ? 160 VAL A CA  1 
ATOM   1220 C  C   . VAL A 1 160 ? 29.072  24.922 17.011 1.00 22.91 ? 160 VAL A C   1 
ATOM   1221 O  O   . VAL A 1 160 ? 28.932  25.273 15.826 1.00 21.79 ? 160 VAL A O   1 
ATOM   1222 C  CB  . VAL A 1 160 ? 27.300  25.266 18.710 1.00 24.89 ? 160 VAL A CB  1 
ATOM   1223 C  CG1 . VAL A 1 160 ? 26.889  26.513 17.937 1.00 26.19 ? 160 VAL A CG1 1 
ATOM   1224 C  CG2 . VAL A 1 160 ? 26.116  24.627 19.378 1.00 26.35 ? 160 VAL A CG2 1 
ATOM   1225 N  N   . LEU A 1 161 ? 30.208  25.128 17.684 1.00 22.69 ? 161 LEU A N   1 
ATOM   1226 C  CA  . LEU A 1 161 ? 31.320  25.838 17.036 1.00 24.38 ? 161 LEU A CA  1 
ATOM   1227 C  C   . LEU A 1 161 ? 31.899  25.027 15.859 1.00 21.37 ? 161 LEU A C   1 
ATOM   1228 O  O   . LEU A 1 161 ? 32.238  25.660 14.834 1.00 26.50 ? 161 LEU A O   1 
ATOM   1229 C  CB  . LEU A 1 161 ? 32.470  26.043 18.031 1.00 24.59 ? 161 LEU A CB  1 
ATOM   1230 C  CG  . LEU A 1 161 ? 32.072  26.986 19.173 1.00 27.44 ? 161 LEU A CG  1 
ATOM   1231 C  CD1 . LEU A 1 161 ? 33.136  26.972 20.308 1.00 28.37 ? 161 LEU A CD1 1 
ATOM   1232 C  CD2 . LEU A 1 161 ? 31.712  28.375 18.705 1.00 27.46 ? 161 LEU A CD2 1 
ATOM   1233 N  N   . ASP A 1 162 ? 31.996  23.712 16.013 1.00 27.85 ? 162 ASP A N   1 
ATOM   1234 C  CA  . ASP A 1 162 ? 32.522  22.815 14.956 1.00 26.50 ? 162 ASP A CA  1 
ATOM   1235 C  C   . ASP A 1 162 ? 31.588  22.861 13.741 1.00 28.57 ? 162 ASP A C   1 
ATOM   1236 O  O   . ASP A 1 162 ? 32.056  22.555 12.628 1.00 29.40 ? 162 ASP A O   1 
ATOM   1237 C  CB  . ASP A 1 162 ? 32.585  21.357 15.424 1.00 31.15 ? 162 ASP A CB  1 
ATOM   1238 C  CG  . ASP A 1 162 ? 33.739  21.083 16.359 1.00 31.82 ? 162 ASP A CG  1 
ATOM   1239 O  OD1 . ASP A 1 162 ? 34.636  21.948 16.474 1.00 36.11 ? 162 ASP A OD1 1 
ATOM   1240 O  OD2 . ASP A 1 162 ? 33.719  20.035 16.995 1.00 37.20 ? 162 ASP A OD2 1 
ATOM   1241 N  N   . ALA A 1 163 ? 30.289  23.184 13.946 1.00 21.65 ? 163 ALA A N   1 
ATOM   1242 C  CA  . ALA A 1 163 ? 29.308  23.263 12.807 1.00 22.16 ? 163 ALA A CA  1 
ATOM   1243 C  C   . ALA A 1 163 ? 29.458  24.481 11.906 1.00 20.39 ? 163 ALA A C   1 
ATOM   1244 O  O   . ALA A 1 163 ? 28.937  24.505 10.779 1.00 24.23 ? 163 ALA A O   1 
ATOM   1245 C  CB  . ALA A 1 163 ? 27.850  23.160 13.311 1.00 21.95 ? 163 ALA A CB  1 
ATOM   1246 N  N   . LEU A 1 164 ? 30.048  25.556 12.411 1.00 19.01 ? 164 LEU A N   1 
ATOM   1247 C  CA  . LEU A 1 164 ? 30.000  26.843 11.768 1.00 20.09 ? 164 LEU A CA  1 
ATOM   1248 C  C   . LEU A 1 164 ? 30.783  26.844 10.415 1.00 20.50 ? 164 LEU A C   1 
ATOM   1249 O  O   . LEU A 1 164 ? 30.448  27.604 9.550  1.00 22.72 ? 164 LEU A O   1 
ATOM   1250 C  CB  . LEU A 1 164 ? 30.519  27.966 12.655 1.00 22.85 ? 164 LEU A CB  1 
ATOM   1251 C  CG  . LEU A 1 164 ? 29.831  28.170 14.009 1.00 21.57 ? 164 LEU A CG  1 
ATOM   1252 C  CD1 . LEU A 1 164 ? 30.483  29.367 14.711 1.00 22.72 ? 164 LEU A CD1 1 
ATOM   1253 C  CD2 . LEU A 1 164 ? 28.389  28.429 13.733 1.00 21.95 ? 164 LEU A CD2 1 
ATOM   1254 N  N   . GLN A 1 165 ? 31.795  25.979 10.320 1.00 23.78 ? 165 GLN A N   1 
ATOM   1255 C  CA  . GLN A 1 165 ? 32.588  25.914 9.077  1.00 24.14 ? 165 GLN A CA  1 
ATOM   1256 C  C   . GLN A 1 165 ? 31.730  25.502 7.892  1.00 26.05 ? 165 GLN A C   1 
ATOM   1257 O  O   . GLN A 1 165 ? 32.096  25.810 6.778  1.00 26.65 ? 165 GLN A O   1 
ATOM   1258 C  CB  . GLN A 1 165 ? 33.825  25.018 9.204  1.00 28.88 ? 165 GLN A CB  1 
ATOM   1259 C  CG  . GLN A 1 165 ? 33.634  23.648 9.827  1.00 35.50 ? 165 GLN A CG  1 
ATOM   1260 C  CD  . GLN A 1 165 ? 32.823  22.707 8.968  1.00 40.22 ? 165 GLN A CD  1 
ATOM   1261 O  OE1 . GLN A 1 165 ? 33.061  22.556 7.735  1.00 38.84 ? 165 GLN A OE1 1 
ATOM   1262 N  NE2 . GLN A 1 165 ? 31.837  22.044 9.611  1.00 43.66 ? 165 GLN A NE2 1 
ATOM   1263 N  N   . ALA A 1 166 ? 30.592  24.860 8.133  1.00 25.53 ? 166 ALA A N   1 
ATOM   1264 C  CA  . ALA A 1 166 ? 29.638  24.479 7.008  1.00 24.60 ? 166 ALA A CA  1 
ATOM   1265 C  C   . ALA A 1 166 ? 28.600  25.517 6.677  1.00 24.91 ? 166 ALA A C   1 
ATOM   1266 O  O   . ALA A 1 166 ? 27.870  25.358 5.696  1.00 27.80 ? 166 ALA A O   1 
ATOM   1267 C  CB  . ALA A 1 166 ? 28.956  23.168 7.344  1.00 28.08 ? 166 ALA A CB  1 
ATOM   1268 N  N   . ILE A 1 167 ? 28.515  26.587 7.461  1.00 19.50 ? 167 ILE A N   1 
ATOM   1269 C  CA  . ILE A 1 167 ? 27.536  27.612 7.234  1.00 21.47 ? 167 ILE A CA  1 
ATOM   1270 C  C   . ILE A 1 167 ? 28.165  28.994 7.285  1.00 21.70 ? 167 ILE A C   1 
ATOM   1271 O  O   . ILE A 1 167 ? 27.604  29.957 7.853  1.00 23.35 ? 167 ILE A O   1 
ATOM   1272 C  CB  . ILE A 1 167 ? 26.296  27.501 8.212  1.00 21.17 ? 167 ILE A CB  1 
ATOM   1273 C  CG1 . ILE A 1 167 ? 26.743  27.619 9.658  1.00 21.33 ? 167 ILE A CG1 1 
ATOM   1274 C  CG2 . ILE A 1 167 ? 25.474  26.200 8.002  1.00 21.72 ? 167 ILE A CG2 1 
ATOM   1275 C  CD1 . ILE A 1 167 ? 25.754  28.413 10.500 1.00 20.98 ? 167 ILE A CD1 1 
ATOM   1276 N  N   . LYS A 1 168 ? 29.340  29.152 6.650  1.00 22.06 ? 168 LYS A N   1 
ATOM   1277 C  CA  . LYS A 1 168 ? 30.101  30.370 6.810  1.00 22.22 ? 168 LYS A CA  1 
ATOM   1278 C  C   . LYS A 1 168 ? 29.469  31.597 6.276  1.00 23.53 ? 168 LYS A C   1 
ATOM   1279 O  O   . LYS A 1 168 ? 29.664  32.705 6.813  1.00 18.44 ? 168 LYS A O   1 
ATOM   1280 C  CB  . LYS A 1 168 ? 31.484  30.196 6.124  1.00 24.74 ? 168 LYS A CB  1 
ATOM   1281 C  CG  . LYS A 1 168 ? 32.589  29.714 7.024  1.00 35.50 ? 168 LYS A CG  1 
ATOM   1282 C  CD  . LYS A 1 168 ? 33.421  30.925 7.452  1.00 38.79 ? 168 LYS A CD  1 
ATOM   1283 C  CE  . LYS A 1 168 ? 33.012  31.430 8.802  1.00 30.69 ? 168 LYS A CE  1 
ATOM   1284 N  NZ  . LYS A 1 168 ? 34.095  31.206 9.815  1.00 31.18 ? 168 LYS A NZ  1 
ATOM   1285 N  N   . THR A 1 169 ? 28.647  31.435 5.221  1.00 22.44 ? 169 THR A N   1 
ATOM   1286 C  CA  . THR A 1 169 ? 28.064  32.587 4.547  1.00 20.34 ? 169 THR A CA  1 
ATOM   1287 C  C   . THR A 1 169 ? 26.533  32.533 4.550  1.00 19.01 ? 169 THR A C   1 
ATOM   1288 O  O   . THR A 1 169 ? 25.944  31.461 4.776  1.00 22.21 ? 169 THR A O   1 
ATOM   1289 C  CB  . THR A 1 169 ? 28.535  32.675 3.030  1.00 19.83 ? 169 THR A CB  1 
ATOM   1290 O  OG1 . THR A 1 169 ? 28.387  31.381 2.436  1.00 23.99 ? 169 THR A OG1 1 
ATOM   1291 C  CG2 . THR A 1 169 ? 30.073  33.064 2.965  1.00 22.05 ? 169 THR A CG2 1 
ATOM   1292 N  N   . LYS A 1 170 ? 25.988  33.710 4.347  1.00 20.26 ? 170 LYS A N   1 
ATOM   1293 C  CA  . LYS A 1 170 ? 24.544  33.954 4.490  1.00 24.05 ? 170 LYS A CA  1 
ATOM   1294 C  C   . LYS A 1 170 ? 23.691  33.014 3.689  1.00 27.95 ? 170 LYS A C   1 
ATOM   1295 O  O   . LYS A 1 170 ? 23.929  32.801 2.477  1.00 28.45 ? 170 LYS A O   1 
ATOM   1296 C  CB  . LYS A 1 170 ? 24.198  35.321 4.108  1.00 24.69 ? 170 LYS A CB  1 
ATOM   1297 C  CG  . LYS A 1 170 ? 22.683  35.539 4.238  1.00 26.37 ? 170 LYS A CG  1 
ATOM   1298 C  CD  . LYS A 1 170 ? 22.375  36.990 4.001  1.00 29.68 ? 170 LYS A CD  1 
ATOM   1299 C  CE  . LYS A 1 170 ? 20.848  37.175 4.011  1.00 36.80 ? 170 LYS A CE  1 
ATOM   1300 N  NZ  . LYS A 1 170 ? 20.435  38.531 4.485  1.00 42.89 ? 170 LYS A NZ  1 
ATOM   1301 N  N   . GLY A 1 171 ? 22.733  32.402 4.378  1.00 29.53 ? 171 GLY A N   1 
ATOM   1302 C  CA  . GLY A 1 171 ? 21.875  31.417 3.782  1.00 28.87 ? 171 GLY A CA  1 
ATOM   1303 C  C   . GLY A 1 171 ? 22.349  30.018 3.738  1.00 27.64 ? 171 GLY A C   1 
ATOM   1304 O  O   . GLY A 1 171 ? 21.536  29.179 3.440  1.00 29.83 ? 171 GLY A O   1 
ATOM   1305 N  N   . LYS A 1 172 ? 23.616  29.727 4.089  1.00 23.61 ? 172 LYS A N   1 
ATOM   1306 C  CA  . LYS A 1 172 ? 24.011  28.358 4.121  1.00 24.62 ? 172 LYS A CA  1 
ATOM   1307 C  C   . LYS A 1 172 ? 23.251  27.682 5.288  1.00 29.33 ? 172 LYS A C   1 
ATOM   1308 O  O   . LYS A 1 172 ? 22.975  28.359 6.308  1.00 30.61 ? 172 LYS A O   1 
ATOM   1309 C  CB  . LYS A 1 172 ? 25.503  28.244 4.221  1.00 25.46 ? 172 LYS A CB  1 
ATOM   1310 C  CG  . LYS A 1 172 ? 26.189  28.523 2.876  1.00 28.16 ? 172 LYS A CG  1 
ATOM   1311 C  CD  . LYS A 1 172 ? 27.615  27.925 2.803  1.00 31.77 ? 172 LYS A CD  1 
ATOM   1312 C  CE  . LYS A 1 172 ? 27.730  26.397 2.721  1.00 36.14 ? 172 LYS A CE  1 
ATOM   1313 N  NZ  . LYS A 1 172 ? 29.143  25.887 2.769  1.00 33.95 ? 172 LYS A NZ  1 
ATOM   1314 N  N   . ARG A 1 173 ? 22.963  26.400 5.135  1.00 28.75 ? 173 ARG A N   1 
ATOM   1315 C  CA  . ARG A 1 173 ? 22.308  25.603 6.179  1.00 29.16 ? 173 ARG A CA  1 
ATOM   1316 C  C   . ARG A 1 173 ? 22.805  24.209 6.103  1.00 30.25 ? 173 ARG A C   1 
ATOM   1317 O  O   . ARG A 1 173 ? 23.234  23.769 4.999  1.00 32.85 ? 173 ARG A O   1 
ATOM   1318 C  CB  . ARG A 1 173 ? 20.785  25.700 6.052  1.00 32.44 ? 173 ARG A CB  1 
ATOM   1319 C  CG  . ARG A 1 173 ? 20.167  25.334 4.728  1.00 39.33 ? 173 ARG A CG  1 
ATOM   1320 C  CD  . ARG A 1 173 ? 18.649  25.435 4.796  1.00 43.44 ? 173 ARG A CD  1 
ATOM   1321 N  NE  . ARG A 1 173 ? 18.184  26.812 4.736  1.00 48.47 ? 173 ARG A NE  1 
ATOM   1322 C  CZ  . ARG A 1 173 ? 17.086  27.278 5.348  1.00 42.56 ? 173 ARG A CZ  1 
ATOM   1323 N  NH1 . ARG A 1 173 ? 16.317  26.500 6.096  1.00 47.02 ? 173 ARG A NH1 1 
ATOM   1324 N  NH2 . ARG A 1 173 ? 16.773  28.548 5.231  1.00 41.04 ? 173 ARG A NH2 1 
ATOM   1325 N  N   . ALA A 1 174 ? 22.756  23.460 7.201  1.00 25.30 ? 174 ALA A N   1 
ATOM   1326 C  CA  . ALA A 1 174 ? 23.234  22.090 7.231  1.00 25.41 ? 174 ALA A CA  1 
ATOM   1327 C  C   . ALA A 1 174 ? 22.522  21.413 8.312  1.00 28.18 ? 174 ALA A C   1 
ATOM   1328 O  O   . ALA A 1 174 ? 22.064  22.132 9.260  1.00 26.26 ? 174 ALA A O   1 
ATOM   1329 C  CB  . ALA A 1 174 ? 24.745  22.087 7.515  1.00 30.28 ? 174 ALA A CB  1 
ATOM   1330 N  N   . PRO A 1 175 ? 22.384  20.079 8.237  1.00 26.47 ? 175 PRO A N   1 
ATOM   1331 C  CA  . PRO A 1 175 ? 21.817  19.324 9.320  1.00 27.72 ? 175 PRO A CA  1 
ATOM   1332 C  C   . PRO A 1 175 ? 22.610  19.509 10.598 1.00 25.93 ? 175 PRO A C   1 
ATOM   1333 O  O   . PRO A 1 175 ? 23.819  19.629 10.570 1.00 28.11 ? 175 PRO A O   1 
ATOM   1334 C  CB  . PRO A 1 175 ? 21.971  17.844 8.887  1.00 31.34 ? 175 PRO A CB  1 
ATOM   1335 C  CG  . PRO A 1 175 ? 22.212  17.892 7.458  1.00 30.38 ? 175 PRO A CG  1 
ATOM   1336 C  CD  . PRO A 1 175 ? 22.886  19.177 7.159  1.00 29.61 ? 175 PRO A CD  1 
ATOM   1337 N  N   . PHE A 1 176 ? 21.885  19.519 11.692 1.00 23.74 ? 176 PHE A N   1 
ATOM   1338 C  CA  . PHE A 1 176 ? 22.540  19.663 13.005 1.00 23.43 ? 176 PHE A CA  1 
ATOM   1339 C  C   . PHE A 1 176 ? 21.723  18.783 13.882 1.00 23.82 ? 176 PHE A C   1 
ATOM   1340 O  O   . PHE A 1 176 ? 20.597  19.148 14.283 1.00 22.32 ? 176 PHE A O   1 
ATOM   1341 C  CB  . PHE A 1 176 ? 22.557  21.175 13.422 1.00 23.29 ? 176 PHE A CB  1 
ATOM   1342 C  CG  . PHE A 1 176 ? 23.303  21.412 14.729 1.00 21.04 ? 176 PHE A CG  1 
ATOM   1343 C  CD1 . PHE A 1 176 ? 24.666  21.692 14.714 1.00 24.18 ? 176 PHE A CD1 1 
ATOM   1344 C  CD2 . PHE A 1 176 ? 22.645  21.286 15.929 1.00 24.44 ? 176 PHE A CD2 1 
ATOM   1345 C  CE1 . PHE A 1 176 ? 25.347  21.902 15.922 1.00 25.93 ? 176 PHE A CE1 1 
ATOM   1346 C  CE2 . PHE A 1 176 ? 23.320  21.502 17.158 1.00 24.35 ? 176 PHE A CE2 1 
ATOM   1347 C  CZ  . PHE A 1 176 ? 24.674  21.827 17.133 1.00 21.53 ? 176 PHE A CZ  1 
ATOM   1348 N  N   . THR A 1 177 ? 22.195  17.555 14.150 1.00 22.09 ? 177 THR A N   1 
ATOM   1349 C  CA  . THR A 1 177 ? 21.324  16.616 14.814 1.00 23.08 ? 177 THR A CA  1 
ATOM   1350 C  C   . THR A 1 177 ? 21.850  16.064 16.155 1.00 22.02 ? 177 THR A C   1 
ATOM   1351 O  O   . THR A 1 177 ? 22.976  16.289 16.494 1.00 24.77 ? 177 THR A O   1 
ATOM   1352 C  CB  . THR A 1 177 ? 20.935  15.415 13.891 1.00 26.91 ? 177 THR A CB  1 
ATOM   1353 O  OG1 . THR A 1 177 ? 22.117  14.699 13.590 1.00 28.62 ? 177 THR A OG1 1 
ATOM   1354 C  CG2 . THR A 1 177 ? 20.301  15.913 12.585 1.00 27.40 ? 177 THR A CG2 1 
ATOM   1355 N  N   . ASN A 1 178 ? 20.973  15.390 16.859 1.00 21.79 ? 178 ASN A N   1 
ATOM   1356 C  CA  . ASN A 1 178 ? 21.285  14.642 18.111 1.00 22.33 ? 178 ASN A CA  1 
ATOM   1357 C  C   . ASN A 1 178 ? 21.936  15.585 19.126 1.00 24.37 ? 178 ASN A C   1 
ATOM   1358 O  O   . ASN A 1 178 ? 23.101  15.403 19.479 1.00 23.85 ? 178 ASN A O   1 
ATOM   1359 C  CB  . ASN A 1 178 ? 22.297  13.531 17.778 1.00 22.60 ? 178 ASN A CB  1 
ATOM   1360 C  CG  . ASN A 1 178 ? 22.449  12.543 18.913 1.00 24.04 ? 178 ASN A CG  1 
ATOM   1361 O  OD1 . ASN A 1 178 ? 21.544  12.364 19.706 1.00 26.37 ? 178 ASN A OD1 1 
ATOM   1362 N  ND2 . ASN A 1 178 ? 23.569  11.852 18.944 1.00 29.28 ? 178 ASN A ND2 1 
ATOM   1363 N  N   . PHE A 1 179 ? 21.227  16.654 19.494 1.00 22.98 ? 179 PHE A N   1 
ATOM   1364 C  CA  . PHE A 1 179 ? 21.841  17.603 20.449 1.00 22.67 ? 179 PHE A CA  1 
ATOM   1365 C  C   . PHE A 1 179 ? 20.774  18.153 21.375 1.00 22.94 ? 179 PHE A C   1 
ATOM   1366 O  O   . PHE A 1 179 ? 19.699  18.641 20.950 1.00 22.30 ? 179 PHE A O   1 
ATOM   1367 C  CB  . PHE A 1 179 ? 22.438  18.737 19.726 1.00 20.86 ? 179 PHE A CB  1 
ATOM   1368 C  CG  . PHE A 1 179 ? 23.072  19.756 20.638 1.00 22.11 ? 179 PHE A CG  1 
ATOM   1369 C  CD1 . PHE A 1 179 ? 22.450  20.982 20.866 1.00 21.41 ? 179 PHE A CD1 1 
ATOM   1370 C  CD2 . PHE A 1 179 ? 24.335  19.499 21.186 1.00 22.73 ? 179 PHE A CD2 1 
ATOM   1371 C  CE1 . PHE A 1 179 ? 23.076  21.912 21.695 1.00 20.37 ? 179 PHE A CE1 1 
ATOM   1372 C  CE2 . PHE A 1 179 ? 24.972  20.431 22.015 1.00 24.54 ? 179 PHE A CE2 1 
ATOM   1373 C  CZ  . PHE A 1 179 ? 24.333  21.644 22.247 1.00 20.44 ? 179 PHE A CZ  1 
ATOM   1374 N  N   . ASP A 1 180 ? 21.098  18.048 22.662 1.00 24.06 ? 180 ASP A N   1 
ATOM   1375 C  CA  . ASP A 1 180 ? 20.217  18.546 23.719 1.00 21.07 ? 180 ASP A CA  1 
ATOM   1376 C  C   . ASP A 1 180 ? 20.762  19.875 24.302 1.00 19.54 ? 180 ASP A C   1 
ATOM   1377 O  O   . ASP A 1 180 ? 21.808  19.852 25.034 1.00 20.94 ? 180 ASP A O   1 
ATOM   1378 C  CB  . ASP A 1 180 ? 20.183  17.510 24.841 1.00 21.93 ? 180 ASP A CB  1 
ATOM   1379 C  CG  . ASP A 1 180 ? 19.338  17.938 26.003 1.00 24.33 ? 180 ASP A CG  1 
ATOM   1380 O  OD1 . ASP A 1 180 ? 18.910  19.102 26.070 1.00 22.90 ? 180 ASP A OD1 1 
ATOM   1381 O  OD2 . ASP A 1 180 ? 19.089  17.089 26.892 1.00 26.89 ? 180 ASP A OD2 1 
ATOM   1382 N  N   . PRO A 1 181 ? 20.089  21.030 23.989 1.00 18.84 ? 181 PRO A N   1 
ATOM   1383 C  CA  . PRO A 1 181 ? 20.692  22.270 24.410 1.00 17.85 ? 181 PRO A CA  1 
ATOM   1384 C  C   . PRO A 1 181 ? 20.536  22.576 25.889 1.00 17.98 ? 181 PRO A C   1 
ATOM   1385 O  O   . PRO A 1 181 ? 21.115  23.587 26.307 1.00 20.94 ? 181 PRO A O   1 
ATOM   1386 C  CB  . PRO A 1 181 ? 19.981  23.359 23.586 1.00 19.77 ? 181 PRO A CB  1 
ATOM   1387 C  CG  . PRO A 1 181 ? 18.671  22.750 23.198 1.00 16.24 ? 181 PRO A CG  1 
ATOM   1388 C  CD  . PRO A 1 181 ? 18.855  21.232 23.173 1.00 19.12 ? 181 PRO A CD  1 
ATOM   1389 N  N   . SER A 1 182 ? 19.812  21.765 26.617 1.00 20.71 ? 182 SER A N   1 
ATOM   1390 C  CA  . SER A 1 182 ? 19.922  21.964 28.098 1.00 21.27 ? 182 SER A CA  1 
ATOM   1391 C  C   . SER A 1 182 ? 21.366  21.735 28.601 1.00 20.09 ? 182 SER A C   1 
ATOM   1392 O  O   . SER A 1 182 ? 21.742  22.231 29.669 1.00 19.75 ? 182 SER A O   1 
ATOM   1393 C  CB  . SER A 1 182 ? 18.923  21.085 28.817 1.00 22.61 ? 182 SER A CB  1 
ATOM   1394 O  OG  . SER A 1 182 ? 19.332  19.727 28.787 1.00 25.12 ? 182 SER A OG  1 
ATOM   1395 N  N   . THR A 1 183 ? 22.190  21.031 27.855 1.00 19.56 ? 183 THR A N   1 
ATOM   1396 C  CA  . THR A 1 183 ? 23.645  20.908 28.216 1.00 20.54 ? 183 THR A CA  1 
ATOM   1397 C  C   . THR A 1 183 ? 24.403  22.244 28.254 1.00 20.74 ? 183 THR A C   1 
ATOM   1398 O  O   . THR A 1 183 ? 25.474  22.319 28.866 1.00 23.49 ? 183 THR A O   1 
ATOM   1399 C  CB  . THR A 1 183 ? 24.398  19.954 27.241 1.00 22.98 ? 183 THR A CB  1 
ATOM   1400 O  OG1 . THR A 1 183 ? 24.275  20.475 25.905 1.00 22.74 ? 183 THR A OG1 1 
ATOM   1401 C  CG2 . THR A 1 183 ? 23.799  18.539 27.333 1.00 20.70 ? 183 THR A CG2 1 
ATOM   1402 N  N   . LEU A 1 184 ? 23.846  23.286 27.611 1.00 18.54 ? 184 LEU A N   1 
ATOM   1403 C  CA  . LEU A 1 184 ? 24.434  24.627 27.589 1.00 16.57 ? 184 LEU A CA  1 
ATOM   1404 C  C   . LEU A 1 184 ? 24.032  25.520 28.781 1.00 17.69 ? 184 LEU A C   1 
ATOM   1405 O  O   . LEU A 1 184 ? 24.674  26.570 29.009 1.00 17.28 ? 184 LEU A O   1 
ATOM   1406 C  CB  . LEU A 1 184 ? 24.006  25.341 26.313 1.00 18.15 ? 184 LEU A CB  1 
ATOM   1407 C  CG  . LEU A 1 184 ? 24.406  24.725 24.935 1.00 21.00 ? 184 LEU A CG  1 
ATOM   1408 C  CD1 . LEU A 1 184 ? 23.840  25.567 23.761 1.00 22.72 ? 184 LEU A CD1 1 
ATOM   1409 C  CD2 . LEU A 1 184 ? 25.908  24.644 24.826 1.00 20.73 ? 184 LEU A CD2 1 
ATOM   1410 N  N   . LEU A 1 185 ? 22.957  25.127 29.454 1.00 19.25 ? 185 LEU A N   1 
ATOM   1411 C  CA  . LEU A 1 185 ? 22.394  25.943 30.569 1.00 18.61 ? 185 LEU A CA  1 
ATOM   1412 C  C   . LEU A 1 185 ? 23.316  25.825 31.784 1.00 19.94 ? 185 LEU A C   1 
ATOM   1413 O  O   . LEU A 1 185 ? 24.076  24.805 31.963 1.00 21.10 ? 185 LEU A O   1 
ATOM   1414 C  CB  . LEU A 1 185 ? 21.020  25.381 30.916 1.00 17.12 ? 185 LEU A CB  1 
ATOM   1415 C  CG  . LEU A 1 185 ? 19.975  25.525 29.766 1.00 17.21 ? 185 LEU A CG  1 
ATOM   1416 C  CD1 . LEU A 1 185 ? 18.639  25.041 30.303 1.00 18.34 ? 185 LEU A CD1 1 
ATOM   1417 C  CD2 . LEU A 1 185 ? 19.949  26.991 29.341 1.00 16.41 ? 185 LEU A CD2 1 
ATOM   1418 N  N   . PRO A 1 186 ? 23.311  26.861 32.634 1.00 19.56 ? 186 PRO A N   1 
ATOM   1419 C  CA  . PRO A 1 186 ? 24.192  26.782 33.837 1.00 20.27 ? 186 PRO A CA  1 
ATOM   1420 C  C   . PRO A 1 186 ? 23.656  25.742 34.836 1.00 22.23 ? 186 PRO A C   1 
ATOM   1421 O  O   . PRO A 1 186 ? 22.479  25.376 34.766 1.00 21.90 ? 186 PRO A O   1 
ATOM   1422 C  CB  . PRO A 1 186 ? 24.118  28.215 34.397 1.00 19.42 ? 186 PRO A CB  1 
ATOM   1423 C  CG  . PRO A 1 186 ? 22.729  28.677 34.008 1.00 19.51 ? 186 PRO A CG  1 
ATOM   1424 C  CD  . PRO A 1 186 ? 22.609  28.150 32.548 1.00 19.83 ? 186 PRO A CD  1 
ATOM   1425 N  N   . SER A 1 187 ? 24.469  25.278 35.816 1.00 22.79 ? 187 SER A N   1 
ATOM   1426 C  CA  . SER A 1 187 ? 23.987  24.168 36.655 1.00 24.46 ? 187 SER A CA  1 
ATOM   1427 C  C   . SER A 1 187 ? 22.806  24.602 37.572 1.00 25.73 ? 187 SER A C   1 
ATOM   1428 O  O   . SER A 1 187 ? 21.992  23.779 37.956 1.00 29.67 ? 187 SER A O   1 
ATOM   1429 C  CB  . SER A 1 187 ? 25.140  23.647 37.542 1.00 28.68 ? 187 SER A CB  1 
ATOM   1430 O  OG  . SER A 1 187 ? 25.622  24.765 38.292 1.00 28.25 ? 187 SER A OG  1 
ATOM   1431 N  N   . SER A 1 188 ? 22.748  25.881 37.948 1.00 22.91 ? 188 SER A N   1 
ATOM   1432 C  CA  . SER A 1 188 ? 21.609  26.409 38.698 1.00 25.69 ? 188 SER A CA  1 
ATOM   1433 C  C   . SER A 1 188 ? 20.687  27.112 37.727 1.00 25.66 ? 188 SER A C   1 
ATOM   1434 O  O   . SER A 1 188 ? 21.158  27.962 36.904 1.00 23.65 ? 188 SER A O   1 
ATOM   1435 C  CB  . SER A 1 188 ? 22.049  27.458 39.733 1.00 25.84 ? 188 SER A CB  1 
ATOM   1436 O  OG  . SER A 1 188 ? 20.896  28.191 40.220 1.00 28.01 ? 188 SER A OG  1 
ATOM   1437 N  N   . LEU A 1 189 ? 19.402  26.791 37.819 1.00 24.31 ? 189 LEU A N   1 
ATOM   1438 C  CA  . LEU A 1 189 ? 18.398  27.520 37.043 1.00 24.11 ? 189 LEU A CA  1 
ATOM   1439 C  C   . LEU A 1 189 ? 17.626  28.620 37.790 1.00 25.08 ? 189 LEU A C   1 
ATOM   1440 O  O   . LEU A 1 189 ? 16.566  29.076 37.328 1.00 24.38 ? 189 LEU A O   1 
ATOM   1441 C  CB  . LEU A 1 189 ? 17.474  26.573 36.218 1.00 25.05 ? 189 LEU A CB  1 
ATOM   1442 C  CG  . LEU A 1 189 ? 18.216  25.520 35.358 1.00 24.80 ? 189 LEU A CG  1 
ATOM   1443 C  CD1 . LEU A 1 189 ? 17.271  24.622 34.571 1.00 26.24 ? 189 LEU A CD1 1 
ATOM   1444 C  CD2 . LEU A 1 189 ? 19.126  26.254 34.407 1.00 22.55 ? 189 LEU A CD2 1 
ATOM   1445 N  N   . ASP A 1 190 ? 18.206  29.158 38.891 1.00 22.83 ? 190 ASP A N   1 
ATOM   1446 C  CA  . ASP A 1 190 ? 17.578  30.342 39.499 1.00 22.22 ? 190 ASP A CA  1 
ATOM   1447 C  C   . ASP A 1 190 ? 17.456  31.452 38.461 1.00 22.63 ? 190 ASP A C   1 
ATOM   1448 O  O   . ASP A 1 190 ? 18.408  31.671 37.680 1.00 19.26 ? 190 ASP A O   1 
ATOM   1449 C  CB  . ASP A 1 190 ? 18.455  30.866 40.680 1.00 23.73 ? 190 ASP A CB  1 
ATOM   1450 C  CG  . ASP A 1 190 ? 18.414  29.942 41.923 1.00 29.23 ? 190 ASP A CG  1 
ATOM   1451 O  OD1 . ASP A 1 190 ? 17.578  29.034 42.016 1.00 29.97 ? 190 ASP A OD1 1 
ATOM   1452 O  OD2 . ASP A 1 190 ? 19.246  30.155 42.818 1.00 31.44 ? 190 ASP A OD2 1 
ATOM   1453 N  N   . PHE A 1 191 ? 16.334  32.181 38.465 1.00 19.24 ? 191 PHE A N   1 
ATOM   1454 C  CA  . PHE A 1 191 ? 16.072  33.105 37.378 1.00 20.26 ? 191 PHE A CA  1 
ATOM   1455 C  C   . PHE A 1 191 ? 15.355  34.382 37.748 1.00 19.50 ? 191 PHE A C   1 
ATOM   1456 O  O   . PHE A 1 191 ? 14.726  34.473 38.871 1.00 23.66 ? 191 PHE A O   1 
ATOM   1457 C  CB  . PHE A 1 191 ? 15.232  32.403 36.295 1.00 21.18 ? 191 PHE A CB  1 
ATOM   1458 C  CG  . PHE A 1 191 ? 13.866  31.943 36.767 1.00 19.17 ? 191 PHE A CG  1 
ATOM   1459 C  CD1 . PHE A 1 191 ? 13.740  30.726 37.366 1.00 18.51 ? 191 PHE A CD1 1 
ATOM   1460 C  CD2 . PHE A 1 191 ? 12.719  32.763 36.564 1.00 20.09 ? 191 PHE A CD2 1 
ATOM   1461 C  CE1 . PHE A 1 191 ? 12.491  30.327 37.826 1.00 23.13 ? 191 PHE A CE1 1 
ATOM   1462 C  CE2 . PHE A 1 191 ? 11.464  32.324 36.996 1.00 19.39 ? 191 PHE A CE2 1 
ATOM   1463 C  CZ  . PHE A 1 191 ? 11.372  31.092 37.578 1.00 21.09 ? 191 PHE A CZ  1 
ATOM   1464 N  N   . TRP A 1 192 ? 15.408  35.340 36.846 1.00 18.30 ? 192 TRP A N   1 
ATOM   1465 C  CA  . TRP A 1 192 ? 14.537  36.487 36.823 1.00 16.85 ? 192 TRP A CA  1 
ATOM   1466 C  C   . TRP A 1 192 ? 13.568  36.308 35.696 1.00 22.70 ? 192 TRP A C   1 
ATOM   1467 O  O   . TRP A 1 192 ? 13.888  35.705 34.649 1.00 19.22 ? 192 TRP A O   1 
ATOM   1468 C  CB  . TRP A 1 192 ? 15.308  37.768 36.554 1.00 20.45 ? 192 TRP A CB  1 
ATOM   1469 C  CG  . TRP A 1 192 ? 16.308  38.181 37.603 1.00 19.29 ? 192 TRP A CG  1 
ATOM   1470 C  CD1 . TRP A 1 192 ? 16.049  38.748 38.848 1.00 22.72 ? 192 TRP A CD1 1 
ATOM   1471 C  CD2 . TRP A 1 192 ? 17.765  38.109 37.504 1.00 19.38 ? 192 TRP A CD2 1 
ATOM   1472 N  NE1 . TRP A 1 192 ? 17.221  39.009 39.510 1.00 22.92 ? 192 TRP A NE1 1 
ATOM   1473 C  CE2 . TRP A 1 192 ? 18.293  38.648 38.758 1.00 22.36 ? 192 TRP A CE2 1 
ATOM   1474 C  CE3 . TRP A 1 192 ? 18.659  37.656 36.536 1.00 20.16 ? 192 TRP A CE3 1 
ATOM   1475 C  CZ2 . TRP A 1 192 ? 19.653  38.721 39.007 1.00 18.13 ? 192 TRP A CZ2 1 
ATOM   1476 C  CZ3 . TRP A 1 192 ? 20.027  37.736 36.801 1.00 19.66 ? 192 TRP A CZ3 1 
ATOM   1477 C  CH2 . TRP A 1 192 ? 20.512  38.256 38.006 1.00 19.61 ? 192 TRP A CH2 1 
ATOM   1478 N  N   . THR A 1 193 ? 12.389  36.861 35.861 1.00 18.90 ? 193 THR A N   1 
ATOM   1479 C  CA  . THR A 1 193 ? 11.423  36.854 34.742 1.00 20.79 ? 193 THR A CA  1 
ATOM   1480 C  C   . THR A 1 193 ? 10.668  38.199 34.600 1.00 21.17 ? 193 THR A C   1 
ATOM   1481 O  O   . THR A 1 193 ? 10.378  38.937 35.610 1.00 20.85 ? 193 THR A O   1 
ATOM   1482 C  CB  . THR A 1 193 ? 10.500  35.638 34.874 1.00 21.73 ? 193 THR A CB  1 
ATOM   1483 O  OG1 . THR A 1 193 ? 9.559   35.576 33.792 1.00 22.35 ? 193 THR A OG1 1 
ATOM   1484 C  CG2 . THR A 1 193 ? 9.643   35.697 36.212 1.00 22.81 ? 193 THR A CG2 1 
ATOM   1485 N  N   . TYR A 1 194 ? 10.366  38.574 33.355 1.00 17.64 ? 194 TYR A N   1 
ATOM   1486 C  CA  . TYR A 1 194 ? 9.577   39.760 33.113 1.00 18.81 ? 194 TYR A CA  1 
ATOM   1487 C  C   . TYR A 1 194 ? 8.913   39.584 31.755 1.00 21.94 ? 194 TYR A C   1 
ATOM   1488 O  O   . TYR A 1 194 ? 9.401   38.770 30.894 1.00 19.77 ? 194 TYR A O   1 
ATOM   1489 C  CB  . TYR A 1 194 ? 10.493  40.979 33.147 1.00 19.71 ? 194 TYR A CB  1 
ATOM   1490 C  CG  . TYR A 1 194 ? 11.411  41.119 31.956 1.00 20.46 ? 194 TYR A CG  1 
ATOM   1491 C  CD1 . TYR A 1 194 ? 12.635  40.401 31.870 1.00 17.73 ? 194 TYR A CD1 1 
ATOM   1492 C  CD2 . TYR A 1 194 ? 11.069  41.947 30.893 1.00 18.33 ? 194 TYR A CD2 1 
ATOM   1493 C  CE1 . TYR A 1 194 ? 13.457  40.559 30.736 1.00 17.74 ? 194 TYR A CE1 1 
ATOM   1494 C  CE2 . TYR A 1 194 ? 11.877  42.116 29.806 1.00 18.77 ? 194 TYR A CE2 1 
ATOM   1495 C  CZ  . TYR A 1 194 ? 13.045  41.365 29.664 1.00 16.90 ? 194 TYR A CZ  1 
ATOM   1496 O  OH  . TYR A 1 194 ? 13.819  41.595 28.540 1.00 18.14 ? 194 TYR A OH  1 
ATOM   1497 N  N   . PRO A 1 195 ? 7.816   40.299 31.541 1.00 21.08 ? 195 PRO A N   1 
ATOM   1498 C  CA  . PRO A 1 195 ? 7.125   40.290 30.231 1.00 19.61 ? 195 PRO A CA  1 
ATOM   1499 C  C   . PRO A 1 195 ? 7.808   41.221 29.261 1.00 21.89 ? 195 PRO A C   1 
ATOM   1500 O  O   . PRO A 1 195 ? 8.046   42.394 29.560 1.00 22.82 ? 195 PRO A O   1 
ATOM   1501 C  CB  . PRO A 1 195 ? 5.697   40.769 30.644 1.00 19.27 ? 195 PRO A CB  1 
ATOM   1502 C  CG  . PRO A 1 195 ? 6.016   41.831 31.682 1.00 18.45 ? 195 PRO A CG  1 
ATOM   1503 C  CD  . PRO A 1 195 ? 7.204   41.280 32.464 1.00 20.94 ? 195 PRO A CD  1 
ATOM   1504 N  N   . GLY A 1 196 ? 8.180   40.695 28.060 1.00 20.89 ? 196 GLY A N   1 
ATOM   1505 C  CA  . GLY A 1 196 ? 8.930   41.483 27.117 1.00 19.86 ? 196 GLY A CA  1 
ATOM   1506 C  C   . GLY A 1 196 ? 8.673   41.082 25.671 1.00 17.99 ? 196 GLY A C   1 
ATOM   1507 O  O   . GLY A 1 196 ? 7.520   40.721 25.312 1.00 19.69 ? 196 GLY A O   1 
ATOM   1508 N  N   . SER A 1 197 ? 9.712   41.197 24.855 1.00 19.01 ? 197 SER A N   1 
ATOM   1509 C  CA  . SER A 1 197 ? 9.535   41.122 23.389 1.00 17.10 ? 197 SER A CA  1 
ATOM   1510 C  C   . SER A 1 197 ? 10.644  40.351 22.753 1.00 19.23 ? 197 SER A C   1 
ATOM   1511 O  O   . SER A 1 197 ? 11.663  40.053 23.396 1.00 16.61 ? 197 SER A O   1 
ATOM   1512 C  CB  . SER A 1 197 ? 9.594   42.537 22.848 1.00 18.49 ? 197 SER A CB  1 
ATOM   1513 O  OG  . SER A 1 197 ? 10.931  43.119 22.807 1.00 20.78 ? 197 SER A OG  1 
ATOM   1514 N  N   . LEU A 1 198 ? 10.469  40.073 21.458 1.00 16.60 ? 198 LEU A N   1 
ATOM   1515 C  CA  . LEU A 1 198 ? 11.612  39.655 20.635 1.00 17.01 ? 198 LEU A CA  1 
ATOM   1516 C  C   . LEU A 1 198 ? 12.574  40.790 20.594 1.00 16.98 ? 198 LEU A C   1 
ATOM   1517 O  O   . LEU A 1 198 ? 12.179  41.965 20.563 1.00 16.03 ? 198 LEU A O   1 
ATOM   1518 C  CB  . LEU A 1 198 ? 11.133  39.374 19.158 1.00 19.12 ? 198 LEU A CB  1 
ATOM   1519 C  CG  . LEU A 1 198 ? 10.004  38.373 19.053 1.00 19.76 ? 198 LEU A CG  1 
ATOM   1520 C  CD1 . LEU A 1 198 ? 9.540   38.274 17.601 1.00 19.44 ? 198 LEU A CD1 1 
ATOM   1521 C  CD2 . LEU A 1 198 ? 10.578  37.031 19.456 1.00 19.33 ? 198 LEU A CD2 1 
ATOM   1522 N  N   . THR A 1 199 ? 13.861  40.481 20.548 1.00 15.70 ? 199 THR A N   1 
ATOM   1523 C  CA  . THR A 1 199 ? 14.869  41.550 20.592 1.00 16.91 ? 199 THR A CA  1 
ATOM   1524 C  C   . THR A 1 199 ? 15.346  42.081 19.228 1.00 19.30 ? 199 THR A C   1 
ATOM   1525 O  O   . THR A 1 199 ? 16.246  42.924 19.136 1.00 19.83 ? 199 THR A O   1 
ATOM   1526 C  CB  . THR A 1 199 ? 16.151  41.166 21.418 1.00 14.87 ? 199 THR A CB  1 
ATOM   1527 O  OG1 . THR A 1 199 ? 16.834  40.079 20.782 1.00 15.85 ? 199 THR A OG1 1 
ATOM   1528 C  CG2 . THR A 1 199 ? 15.704  40.651 22.768 1.00 16.85 ? 199 THR A CG2 1 
ATOM   1529 N  N   . HIS A 1 200 ? 14.704  41.591 18.178 1.00 16.16 ? 200 HIS A N   1 
ATOM   1530 C  CA  . HIS A 1 200 ? 14.979  42.108 16.831 1.00 19.60 ? 200 HIS A CA  1 
ATOM   1531 C  C   . HIS A 1 200 ? 13.653  42.070 16.094 1.00 17.89 ? 200 HIS A C   1 
ATOM   1532 O  O   . HIS A 1 200 ? 12.683  41.443 16.564 1.00 16.56 ? 200 HIS A O   1 
ATOM   1533 C  CB  . HIS A 1 200 ? 16.179  41.440 16.076 1.00 18.63 ? 200 HIS A CB  1 
ATOM   1534 C  CG  . HIS A 1 200 ? 16.000  39.984 15.749 1.00 20.82 ? 200 HIS A CG  1 
ATOM   1535 N  ND1 . HIS A 1 200 ? 15.047  39.552 14.882 1.00 21.43 ? 200 HIS A ND1 1 
ATOM   1536 C  CD2 . HIS A 1 200 ? 16.726  38.873 16.129 1.00 22.95 ? 200 HIS A CD2 1 
ATOM   1537 C  CE1 . HIS A 1 200 ? 15.130  38.199 14.735 1.00 23.72 ? 200 HIS A CE1 1 
ATOM   1538 N  NE2 . HIS A 1 200 ? 16.142  37.766 15.494 1.00 23.34 ? 200 HIS A NE2 1 
ATOM   1539 N  N   . PRO A 1 201 ? 13.536  42.849 14.997 1.00 19.43 ? 201 PRO A N   1 
ATOM   1540 C  CA  . PRO A 1 201 ? 12.281  42.873 14.188 1.00 20.86 ? 201 PRO A CA  1 
ATOM   1541 C  C   . PRO A 1 201 ? 11.812  41.451 13.955 1.00 20.51 ? 201 PRO A C   1 
ATOM   1542 O  O   . PRO A 1 201 ? 12.630  40.568 13.670 1.00 20.83 ? 201 PRO A O   1 
ATOM   1543 C  CB  . PRO A 1 201 ? 12.766  43.497 12.850 1.00 20.16 ? 201 PRO A CB  1 
ATOM   1544 C  CG  . PRO A 1 201 ? 13.781  44.531 13.412 1.00 21.93 ? 201 PRO A CG  1 
ATOM   1545 C  CD  . PRO A 1 201 ? 14.587  43.666 14.351 1.00 19.87 ? 201 PRO A CD  1 
ATOM   1546 N  N   . PRO A 1 202 ? 10.510  41.233 14.093 1.00 20.96 ? 202 PRO A N   1 
ATOM   1547 C  CA  . PRO A 1 202 ? 9.448   42.242 14.196 1.00 22.23 ? 202 PRO A CA  1 
ATOM   1548 C  C   . PRO A 1 202 ? 9.138   42.712 15.630 1.00 23.21 ? 202 PRO A C   1 
ATOM   1549 O  O   . PRO A 1 202 ? 8.136   43.445 15.838 1.00 23.39 ? 202 PRO A O   1 
ATOM   1550 C  CB  . PRO A 1 202 ? 8.233   41.508 13.629 1.00 22.48 ? 202 PRO A CB  1 
ATOM   1551 C  CG  . PRO A 1 202 ? 8.504   40.106 14.041 1.00 20.22 ? 202 PRO A CG  1 
ATOM   1552 C  CD  . PRO A 1 202 ? 9.957   39.891 13.822 1.00 21.10 ? 202 PRO A CD  1 
ATOM   1553 N  N   . LEU A 1 203 ? 9.980   42.328 16.610 1.00 21.87 ? 203 LEU A N   1 
ATOM   1554 C  CA  . LEU A 1 203 ? 9.904   43.002 17.926 1.00 20.18 ? 203 LEU A CA  1 
ATOM   1555 C  C   . LEU A 1 203 ? 8.561   42.785 18.669 1.00 20.59 ? 203 LEU A C   1 
ATOM   1556 O  O   . LEU A 1 203 ? 8.199   43.572 19.570 1.00 18.90 ? 203 LEU A O   1 
ATOM   1557 C  CB  . LEU A 1 203 ? 10.217  44.502 17.735 1.00 17.49 ? 203 LEU A CB  1 
ATOM   1558 C  CG  . LEU A 1 203 ? 11.600  44.878 17.252 1.00 18.79 ? 203 LEU A CG  1 
ATOM   1559 C  CD1 . LEU A 1 203 ? 11.587  46.384 17.089 1.00 19.85 ? 203 LEU A CD1 1 
ATOM   1560 C  CD2 . LEU A 1 203 ? 12.668  44.608 18.317 1.00 19.21 ? 203 LEU A CD2 1 
ATOM   1561 N  N   . TYR A 1 204 ? 7.850   41.672 18.373 1.00 18.55 ? 204 TYR A N   1 
ATOM   1562 C  CA  . TYR A 1 204 ? 6.557   41.431 18.964 1.00 18.54 ? 204 TYR A CA  1 
ATOM   1563 C  C   . TYR A 1 204 ? 6.688   41.339 20.469 1.00 18.34 ? 204 TYR A C   1 
ATOM   1564 O  O   . TYR A 1 204 ? 7.614   40.690 20.970 1.00 17.90 ? 204 TYR A O   1 
ATOM   1565 C  CB  . TYR A 1 204 ? 6.049   40.017 18.581 1.00 18.12 ? 204 TYR A CB  1 
ATOM   1566 C  CG  . TYR A 1 204 ? 5.675   39.900 17.084 1.00 23.26 ? 204 TYR A CG  1 
ATOM   1567 C  CD1 . TYR A 1 204 ? 5.100   40.964 16.410 1.00 27.55 ? 204 TYR A CD1 1 
ATOM   1568 C  CD2 . TYR A 1 204 ? 5.848   38.709 16.404 1.00 25.45 ? 204 TYR A CD2 1 
ATOM   1569 C  CE1 . TYR A 1 204 ? 4.721   40.861 15.062 1.00 28.46 ? 204 TYR A CE1 1 
ATOM   1570 C  CE2 . TYR A 1 204 ? 5.457   38.585 15.062 1.00 26.31 ? 204 TYR A CE2 1 
ATOM   1571 C  CZ  . TYR A 1 204 ? 4.890   39.644 14.410 1.00 29.66 ? 204 TYR A CZ  1 
ATOM   1572 O  OH  . TYR A 1 204 ? 4.542   39.511 13.049 1.00 28.38 ? 204 TYR A OH  1 
ATOM   1573 N  N   . GLU A 1 205 ? 5.683   41.853 21.162 1.00 17.38 ? 205 GLU A N   1 
ATOM   1574 C  CA  . GLU A 1 205 ? 5.652   41.830 22.644 1.00 18.01 ? 205 GLU A CA  1 
ATOM   1575 C  C   . GLU A 1 205 ? 4.932   40.553 23.112 1.00 18.64 ? 205 GLU A C   1 
ATOM   1576 O  O   . GLU A 1 205 ? 3.873   40.560 23.799 1.00 19.56 ? 205 GLU A O   1 
ATOM   1577 C  CB  . GLU A 1 205 ? 5.019   43.172 23.117 1.00 20.27 ? 205 GLU A CB  1 
ATOM   1578 C  CG  . GLU A 1 205 ? 5.989   44.303 22.873 1.00 21.31 ? 205 GLU A CG  1 
ATOM   1579 C  CD  . GLU A 1 205 ? 5.519   45.655 23.402 1.00 23.33 ? 205 GLU A CD  1 
ATOM   1580 O  OE1 . GLU A 1 205 ? 6.385   46.558 23.502 1.00 23.56 ? 205 GLU A OE1 1 
ATOM   1581 O  OE2 . GLU A 1 205 ? 4.289   45.742 23.620 1.00 25.19 ? 205 GLU A OE2 1 
ATOM   1582 N  N   . SER A 1 206 ? 5.583   39.422 22.820 1.00 18.13 ? 206 SER A N   1 
ATOM   1583 C  CA  . SER A 1 206 ? 5.046   38.119 22.965 1.00 17.47 ? 206 SER A CA  1 
ATOM   1584 C  C   . SER A 1 206 ? 5.900   37.191 23.810 1.00 17.57 ? 206 SER A C   1 
ATOM   1585 O  O   . SER A 1 206 ? 5.578   36.018 23.940 1.00 17.33 ? 206 SER A O   1 
ATOM   1586 C  CB  . SER A 1 206 ? 4.920   37.511 21.546 1.00 19.25 ? 206 SER A CB  1 
ATOM   1587 O  OG  . SER A 1 206 ? 6.176   37.461 20.897 1.00 20.39 ? 206 SER A OG  1 
ATOM   1588 N  N   . VAL A 1 207 ? 6.952   37.731 24.431 1.00 17.68 ? 207 VAL A N   1 
ATOM   1589 C  CA  . VAL A 1 207 ? 7.955   36.889 25.103 1.00 15.91 ? 207 VAL A CA  1 
ATOM   1590 C  C   . VAL A 1 207 ? 7.876   37.079 26.639 1.00 17.10 ? 207 VAL A C   1 
ATOM   1591 O  O   . VAL A 1 207 ? 8.052   38.206 27.167 1.00 19.87 ? 207 VAL A O   1 
ATOM   1592 C  CB  . VAL A 1 207 ? 9.366   37.241 24.643 1.00 16.06 ? 207 VAL A CB  1 
ATOM   1593 C  CG1 . VAL A 1 207 ? 10.401  36.346 25.314 1.00 15.35 ? 207 VAL A CG1 1 
ATOM   1594 C  CG2 . VAL A 1 207 ? 9.476   37.017 23.132 1.00 14.52 ? 207 VAL A CG2 1 
ATOM   1595 N  N   . THR A 1 208 ? 7.729   35.957 27.291 1.00 17.63 ? 208 THR A N   1 
ATOM   1596 C  CA  . THR A 1 208 ? 8.015   35.897 28.747 1.00 17.45 ? 208 THR A CA  1 
ATOM   1597 C  C   . THR A 1 208 ? 9.503   35.477 28.866 1.00 17.73 ? 208 THR A C   1 
ATOM   1598 O  O   . THR A 1 208 ? 9.891   34.365 28.460 1.00 18.89 ? 208 THR A O   1 
ATOM   1599 C  CB  . THR A 1 208 ? 7.159   34.854 29.387 1.00 20.74 ? 208 THR A CB  1 
ATOM   1600 O  OG1 . THR A 1 208 ? 5.781   35.194 29.148 1.00 24.40 ? 208 THR A OG1 1 
ATOM   1601 C  CG2 . THR A 1 208 ? 7.372   34.860 30.952 1.00 23.12 ? 208 THR A CG2 1 
ATOM   1602 N  N   . TRP A 1 209 ? 10.282  36.363 29.449 1.00 15.68 ? 209 TRP A N   1 
ATOM   1603 C  CA  . TRP A 1 209 ? 11.728  36.122 29.575 1.00 15.62 ? 209 TRP A CA  1 
ATOM   1604 C  C   . TRP A 1 209 ? 12.061  35.376 30.862 1.00 16.29 ? 209 TRP A C   1 
ATOM   1605 O  O   . TRP A 1 209 ? 11.432  35.631 31.901 1.00 20.16 ? 209 TRP A O   1 
ATOM   1606 C  CB  . TRP A 1 209 ? 12.514  37.433 29.532 1.00 17.62 ? 209 TRP A CB  1 
ATOM   1607 C  CG  . TRP A 1 209 ? 12.680  37.911 28.105 1.00 16.92 ? 209 TRP A CG  1 
ATOM   1608 C  CD1 . TRP A 1 209 ? 11.891  38.823 27.376 1.00 16.25 ? 209 TRP A CD1 1 
ATOM   1609 C  CD2 . TRP A 1 209 ? 13.686  37.407 27.147 1.00 16.49 ? 209 TRP A CD2 1 
ATOM   1610 N  NE1 . TRP A 1 209 ? 12.363  38.924 26.062 1.00 18.51 ? 209 TRP A NE1 1 
ATOM   1611 C  CE2 . TRP A 1 209 ? 13.447  38.093 25.888 1.00 16.81 ? 209 TRP A CE2 1 
ATOM   1612 C  CE3 . TRP A 1 209 ? 14.702  36.475 27.231 1.00 17.38 ? 209 TRP A CE3 1 
ATOM   1613 C  CZ2 . TRP A 1 209 ? 14.245  37.862 24.761 1.00 18.42 ? 209 TRP A CZ2 1 
ATOM   1614 C  CZ3 . TRP A 1 209 ? 15.512  36.264 26.096 1.00 15.59 ? 209 TRP A CZ3 1 
ATOM   1615 C  CH2 . TRP A 1 209 ? 15.285  36.972 24.900 1.00 16.06 ? 209 TRP A CH2 1 
ATOM   1616 N  N   . ILE A 1 210 ? 13.012  34.443 30.766 1.00 17.13 ? 210 ILE A N   1 
ATOM   1617 C  CA  . ILE A 1 210 ? 13.582  33.693 31.897 1.00 16.59 ? 210 ILE A CA  1 
ATOM   1618 C  C   . ILE A 1 210 ? 15.067  33.938 31.811 1.00 18.04 ? 210 ILE A C   1 
ATOM   1619 O  O   . ILE A 1 210 ? 15.680  33.475 30.889 1.00 16.73 ? 210 ILE A O   1 
ATOM   1620 C  CB  . ILE A 1 210 ? 13.287  32.190 31.810 1.00 15.91 ? 210 ILE A CB  1 
ATOM   1621 C  CG1 . ILE A 1 210 ? 11.766  31.859 31.747 1.00 19.12 ? 210 ILE A CG1 1 
ATOM   1622 C  CG2 . ILE A 1 210 ? 13.956  31.389 32.970 1.00 17.37 ? 210 ILE A CG2 1 
ATOM   1623 C  CD1 . ILE A 1 210 ? 10.952  32.317 32.951 1.00 17.53 ? 210 ILE A CD1 1 
ATOM   1624 N  N   . ILE A 1 211 ? 15.644  34.766 32.689 1.00 16.99 ? 211 ILE A N   1 
ATOM   1625 C  CA  . ILE A 1 211 ? 17.037  35.124 32.565 1.00 16.86 ? 211 ILE A CA  1 
ATOM   1626 C  C   . ILE A 1 211 ? 17.706  34.403 33.747 1.00 16.33 ? 211 ILE A C   1 
ATOM   1627 O  O   . ILE A 1 211 ? 17.380  34.685 34.917 1.00 15.69 ? 211 ILE A O   1 
ATOM   1628 C  CB  . ILE A 1 211 ? 17.236  36.633 32.738 1.00 15.50 ? 211 ILE A CB  1 
ATOM   1629 C  CG1 . ILE A 1 211 ? 16.454  37.501 31.681 1.00 17.19 ? 211 ILE A CG1 1 
ATOM   1630 C  CG2 . ILE A 1 211 ? 18.721  36.977 32.655 1.00 14.36 ? 211 ILE A CG2 1 
ATOM   1631 C  CD1 . ILE A 1 211 ? 16.694  37.045 30.219 1.00 17.77 ? 211 ILE A CD1 1 
ATOM   1632 N  N   . CYS A 1 212 ? 18.588  33.465 33.465 1.00 17.20 ? 212 CYS A N   1 
ATOM   1633 C  CA  . CYS A 1 212 ? 19.409  32.799 34.506 1.00 17.41 ? 212 CYS A CA  1 
ATOM   1634 C  C   . CYS A 1 212 ? 20.272  33.738 35.295 1.00 16.31 ? 212 CYS A C   1 
ATOM   1635 O  O   . CYS A 1 212 ? 20.904  34.640 34.777 1.00 15.35 ? 212 CYS A O   1 
ATOM   1636 C  CB  . CYS A 1 212 ? 20.310  31.704 33.884 1.00 17.75 ? 212 CYS A CB  1 
ATOM   1637 S  SG  . CYS A 1 212 ? 19.210  30.382 33.244 1.00 20.89 ? 212 CYS A SG  1 
ATOM   1638 N  N   . LYS A 1 213 ? 20.291  33.563 36.634 1.00 18.36 ? 213 LYS A N   1 
ATOM   1639 C  CA  . LYS A 1 213 ? 21.216  34.435 37.342 1.00 17.75 ? 213 LYS A CA  1 
ATOM   1640 C  C   . LYS A 1 213 ? 22.675  34.048 37.275 1.00 15.96 ? 213 LYS A C   1 
ATOM   1641 O  O   . LYS A 1 213 ? 23.548  34.916 37.359 1.00 19.41 ? 213 LYS A O   1 
ATOM   1642 C  CB  . LYS A 1 213 ? 20.799  34.613 38.825 1.00 25.15 ? 213 LYS A CB  1 
ATOM   1643 C  CG  . LYS A 1 213 ? 21.233  33.531 39.783 1.00 26.46 ? 213 LYS A CG  1 
ATOM   1644 C  CD  . LYS A 1 213 ? 20.981  34.098 41.210 1.00 26.23 ? 213 LYS A CD  1 
ATOM   1645 C  CE  . LYS A 1 213 ? 21.551  33.285 42.352 1.00 32.83 ? 213 LYS A CE  1 
ATOM   1646 N  NZ  . LYS A 1 213 ? 22.056  31.945 41.975 1.00 35.30 ? 213 LYS A NZ  1 
ATOM   1647 N  N   . GLU A 1 214 ? 22.964  32.757 37.087 1.00 16.97 ? 214 GLU A N   1 
ATOM   1648 C  CA  . GLU A 1 214 ? 24.319  32.250 36.882 1.00 18.32 ? 214 GLU A CA  1 
ATOM   1649 C  C   . GLU A 1 214 ? 24.688  32.304 35.379 1.00 16.30 ? 214 GLU A C   1 
ATOM   1650 O  O   . GLU A 1 214 ? 23.854  31.948 34.520 1.00 17.27 ? 214 GLU A O   1 
ATOM   1651 C  CB  . GLU A 1 214 ? 24.323  30.809 37.340 1.00 21.72 ? 214 GLU A CB  1 
ATOM   1652 C  CG  . GLU A 1 214 ? 25.585  30.045 37.487 1.00 28.70 ? 214 GLU A CG  1 
ATOM   1653 C  CD  . GLU A 1 214 ? 25.336  28.816 38.410 1.00 34.55 ? 214 GLU A CD  1 
ATOM   1654 O  OE1 . GLU A 1 214 ? 25.355  27.696 37.852 1.00 32.43 ? 214 GLU A OE1 1 
ATOM   1655 O  OE2 . GLU A 1 214 ? 25.109  28.996 39.684 1.00 35.27 ? 214 GLU A OE2 1 
ATOM   1656 N  N   . SER A 1 215 ? 25.885  32.784 35.144 1.00 18.23 ? 215 SER A N   1 
ATOM   1657 C  CA  . SER A 1 215 ? 26.446  32.875 33.792 1.00 17.23 ? 215 SER A CA  1 
ATOM   1658 C  C   . SER A 1 215 ? 27.053  31.511 33.402 1.00 17.59 ? 215 SER A C   1 
ATOM   1659 O  O   . SER A 1 215 ? 27.215  30.577 34.235 1.00 17.39 ? 215 SER A O   1 
ATOM   1660 C  CB  . SER A 1 215 ? 27.477  33.970 33.717 1.00 17.58 ? 215 SER A CB  1 
ATOM   1661 O  OG  . SER A 1 215 ? 28.575  33.684 34.594 1.00 20.34 ? 215 SER A OG  1 
ATOM   1662 N  N   . ILE A 1 216 ? 27.388  31.367 32.112 1.00 17.25 ? 216 ILE A N   1 
ATOM   1663 C  CA  . ILE A 1 216 ? 28.209  30.240 31.674 1.00 16.83 ? 216 ILE A CA  1 
ATOM   1664 C  C   . ILE A 1 216 ? 29.423  30.919 31.030 1.00 15.05 ? 216 ILE A C   1 
ATOM   1665 O  O   . ILE A 1 216 ? 29.419  32.098 30.699 1.00 16.60 ? 216 ILE A O   1 
ATOM   1666 C  CB  . ILE A 1 216 ? 27.463  29.372 30.592 1.00 15.58 ? 216 ILE A CB  1 
ATOM   1667 C  CG1 . ILE A 1 216 ? 27.076  30.234 29.378 1.00 15.95 ? 216 ILE A CG1 1 
ATOM   1668 C  CG2 . ILE A 1 216 ? 26.307  28.648 31.239 1.00 17.32 ? 216 ILE A CG2 1 
ATOM   1669 C  CD1 . ILE A 1 216 ? 26.511  29.393 28.220 1.00 15.15 ? 216 ILE A CD1 1 
ATOM   1670 N  N   A SER A 1 217 ? 30.497  30.166 30.864 0.50 17.56 ? 217 SER A N   1 
ATOM   1671 N  N   B SER A 1 217 ? 30.476  30.141 30.849 0.50 17.16 ? 217 SER A N   1 
ATOM   1672 C  CA  A SER A 1 217 ? 31.710  30.753 30.320 0.50 17.72 ? 217 SER A CA  1 
ATOM   1673 C  CA  B SER A 1 217 ? 31.731  30.673 30.353 0.50 17.10 ? 217 SER A CA  1 
ATOM   1674 C  C   A SER A 1 217 ? 31.723  30.674 28.787 0.50 19.68 ? 217 SER A C   1 
ATOM   1675 C  C   B SER A 1 217 ? 31.819  30.558 28.816 0.50 19.30 ? 217 SER A C   1 
ATOM   1676 O  O   A SER A 1 217 ? 30.901  29.999 28.169 0.50 19.92 ? 217 SER A O   1 
ATOM   1677 O  O   B SER A 1 217 ? 31.092  29.769 28.219 0.50 19.42 ? 217 SER A O   1 
ATOM   1678 C  CB  A SER A 1 217 ? 32.956  30.040 30.887 0.50 18.72 ? 217 SER A CB  1 
ATOM   1679 C  CB  B SER A 1 217 ? 32.891  29.915 31.025 0.50 17.41 ? 217 SER A CB  1 
ATOM   1680 O  OG  A SER A 1 217 ? 32.999  28.716 30.387 0.50 21.75 ? 217 SER A OG  1 
ATOM   1681 O  OG  B SER A 1 217 ? 34.092  30.561 30.742 0.50 18.14 ? 217 SER A OG  1 
ATOM   1682 N  N   . VAL A 1 218 ? 32.683  31.375 28.230 1.00 19.27 ? 218 VAL A N   1 
ATOM   1683 C  CA  . VAL A 1 218 ? 33.015  31.303 26.800 1.00 18.23 ? 218 VAL A CA  1 
ATOM   1684 C  C   . VAL A 1 218 ? 34.440  31.891 26.787 1.00 21.47 ? 218 VAL A C   1 
ATOM   1685 O  O   . VAL A 1 218 ? 34.753  32.824 27.521 1.00 20.70 ? 218 VAL A O   1 
ATOM   1686 C  CB  . VAL A 1 218 ? 32.045  32.161 25.938 1.00 20.89 ? 218 VAL A CB  1 
ATOM   1687 C  CG1 . VAL A 1 218 ? 32.008  33.638 26.321 1.00 19.88 ? 218 VAL A CG1 1 
ATOM   1688 C  CG2 . VAL A 1 218 ? 32.360  31.990 24.435 1.00 17.57 ? 218 VAL A CG2 1 
ATOM   1689 N  N   . SER A 1 219 ? 35.324  31.308 25.959 1.00 22.27 ? 219 SER A N   1 
ATOM   1690 C  CA  . SER A 1 219 ? 36.623  31.966 25.706 1.00 23.22 ? 219 SER A CA  1 
ATOM   1691 C  C   . SER A 1 219 ? 36.643  33.072 24.621 1.00 24.51 ? 219 SER A C   1 
ATOM   1692 O  O   . SER A 1 219 ? 35.750  33.170 23.703 1.00 22.78 ? 219 SER A O   1 
ATOM   1693 C  CB  . SER A 1 219 ? 37.749  30.957 25.447 1.00 21.19 ? 219 SER A CB  1 
ATOM   1694 O  OG  . SER A 1 219 ? 37.572  30.382 24.147 1.00 20.95 ? 219 SER A OG  1 
ATOM   1695 N  N   A SER A 1 220 ? 37.671  33.920 24.721 0.50 22.30 ? 220 SER A N   1 
ATOM   1696 N  N   B SER A 1 220 ? 37.684  33.900 24.738 0.50 21.25 ? 220 SER A N   1 
ATOM   1697 C  CA  A SER A 1 220 ? 37.894  34.997 23.754 0.50 22.47 ? 220 SER A CA  1 
ATOM   1698 C  CA  B SER A 1 220 ? 38.025  34.941 23.773 0.50 21.21 ? 220 SER A CA  1 
ATOM   1699 C  C   A SER A 1 220 ? 38.030  34.371 22.334 0.50 20.74 ? 220 SER A C   1 
ATOM   1700 C  C   B SER A 1 220 ? 38.032  34.355 22.351 0.50 19.66 ? 220 SER A C   1 
ATOM   1701 O  O   A SER A 1 220 ? 37.585  34.987 21.366 0.50 23.34 ? 220 SER A O   1 
ATOM   1702 O  O   B SER A 1 220 ? 37.525  34.973 21.415 0.50 21.73 ? 220 SER A O   1 
ATOM   1703 C  CB  A SER A 1 220 ? 39.166  35.763 24.130 0.50 22.77 ? 220 SER A CB  1 
ATOM   1704 C  CB  B SER A 1 220 ? 39.439  35.403 24.094 0.50 18.99 ? 220 SER A CB  1 
ATOM   1705 O  OG  A SER A 1 220 ? 39.271  37.019 23.466 0.50 21.99 ? 220 SER A OG  1 
ATOM   1706 O  OG  B SER A 1 220 ? 39.391  36.211 25.246 0.50 18.35 ? 220 SER A OG  1 
ATOM   1707 N  N   . GLU A 1 221 ? 38.573  33.149 22.252 1.00 20.60 ? 221 GLU A N   1 
ATOM   1708 C  CA  . GLU A 1 221 ? 38.807  32.488 20.923 1.00 21.68 ? 221 GLU A CA  1 
ATOM   1709 C  C   . GLU A 1 221 ? 37.453  31.872 20.464 1.00 24.97 ? 221 GLU A C   1 
ATOM   1710 O  O   . GLU A 1 221 ? 37.143  31.798 19.246 1.00 23.15 ? 221 GLU A O   1 
ATOM   1711 C  CB  . GLU A 1 221 ? 39.851  31.366 21.016 1.00 23.67 ? 221 GLU A CB  1 
ATOM   1712 C  CG  . GLU A 1 221 ? 41.289  31.881 21.219 1.00 24.07 ? 221 GLU A CG  1 
ATOM   1713 C  CD  . GLU A 1 221 ? 41.496  32.374 22.645 1.00 28.52 ? 221 GLU A CD  1 
ATOM   1714 O  OE1 . GLU A 1 221 ? 41.030  31.687 23.577 1.00 27.17 ? 221 GLU A OE1 1 
ATOM   1715 O  OE2 . GLU A 1 221 ? 42.101  33.449 22.828 1.00 29.99 ? 221 GLU A OE2 1 
ATOM   1716 N  N   . GLN A 1 222 ? 36.671  31.389 21.434 1.00 20.52 ? 222 GLN A N   1 
ATOM   1717 C  CA  . GLN A 1 222 ? 35.348  30.930 21.083 1.00 21.61 ? 222 GLN A CA  1 
ATOM   1718 C  C   . GLN A 1 222 ? 34.491  32.078 20.550 1.00 20.83 ? 222 GLN A C   1 
ATOM   1719 O  O   . GLN A 1 222 ? 33.815  31.893 19.506 1.00 23.81 ? 222 GLN A O   1 
ATOM   1720 C  CB  . GLN A 1 222 ? 34.689  30.134 22.204 1.00 21.33 ? 222 GLN A CB  1 
ATOM   1721 C  CG  . GLN A 1 222 ? 35.324  28.763 22.492 1.00 21.62 ? 222 GLN A CG  1 
ATOM   1722 C  CD  . GLN A 1 222 ? 34.625  28.072 23.631 1.00 22.50 ? 222 GLN A CD  1 
ATOM   1723 O  OE1 . GLN A 1 222 ? 34.344  28.712 24.687 1.00 20.99 ? 222 GLN A OE1 1 
ATOM   1724 N  NE2 . GLN A 1 222 ? 34.316  26.830 23.461 1.00 23.24 ? 222 GLN A NE2 1 
ATOM   1725 N  N   . LEU A 1 223 ? 34.485  33.252 21.180 1.00 20.33 ? 223 LEU A N   1 
ATOM   1726 C  CA  . LEU A 1 223 ? 33.794  34.434 20.671 1.00 19.28 ? 223 LEU A CA  1 
ATOM   1727 C  C   . LEU A 1 223 ? 34.313  34.811 19.294 1.00 23.03 ? 223 LEU A C   1 
ATOM   1728 O  O   . LEU A 1 223 ? 33.556  35.319 18.445 1.00 23.78 ? 223 LEU A O   1 
ATOM   1729 C  CB  . LEU A 1 223 ? 33.997  35.657 21.556 1.00 22.79 ? 223 LEU A CB  1 
ATOM   1730 C  CG  . LEU A 1 223 ? 33.336  35.433 22.940 1.00 20.45 ? 223 LEU A CG  1 
ATOM   1731 C  CD1 . LEU A 1 223 ? 33.855  36.408 23.995 1.00 25.28 ? 223 LEU A CD1 1 
ATOM   1732 C  CD2 . LEU A 1 223 ? 31.861  35.669 22.747 1.00 21.35 ? 223 LEU A CD2 1 
ATOM   1733 N  N   . ALA A 1 224 ? 35.629  34.654 19.090 1.00 19.93 ? 224 ALA A N   1 
ATOM   1734 C  CA  . ALA A 1 224 ? 36.148  34.979 17.743 1.00 20.64 ? 224 ALA A CA  1 
ATOM   1735 C  C   . ALA A 1 224 ? 35.512  34.098 16.662 1.00 19.08 ? 224 ALA A C   1 
ATOM   1736 O  O   . ALA A 1 224 ? 35.388  34.567 15.539 1.00 22.36 ? 224 ALA A O   1 
ATOM   1737 C  CB  . ALA A 1 224 ? 37.668  34.803 17.718 1.00 21.16 ? 224 ALA A CB  1 
ATOM   1738 N  N   . GLN A 1 225 ? 35.192  32.821 16.952 1.00 21.38 ? 225 GLN A N   1 
ATOM   1739 C  CA  . GLN A 1 225 ? 34.521  31.977 15.995 1.00 21.13 ? 225 GLN A CA  1 
ATOM   1740 C  C   . GLN A 1 225 ? 33.192  32.556 15.604 1.00 23.78 ? 225 GLN A C   1 
ATOM   1741 O  O   . GLN A 1 225 ? 32.871  32.601 14.390 1.00 23.86 ? 225 GLN A O   1 
ATOM   1742 C  CB  . GLN A 1 225 ? 34.367  30.530 16.443 1.00 22.01 ? 225 GLN A CB  1 
ATOM   1743 C  CG  . GLN A 1 225 ? 35.733  29.842 16.692 1.00 22.19 ? 225 GLN A CG  1 
ATOM   1744 C  CD  . GLN A 1 225 ? 35.591  28.384 16.931 1.00 24.36 ? 225 GLN A CD  1 
ATOM   1745 O  OE1 . GLN A 1 225 ? 35.791  27.923 18.057 1.00 25.14 ? 225 GLN A OE1 1 
ATOM   1746 N  NE2 . GLN A 1 225 ? 35.251  27.590 15.836 1.00 25.30 ? 225 GLN A NE2 1 
ATOM   1747 N  N   . PHE A 1 226 ? 32.377  32.986 16.583 1.00 21.32 ? 226 PHE A N   1 
ATOM   1748 C  CA  . PHE A 1 226 ? 31.152  33.702 16.178 1.00 19.65 ? 226 PHE A CA  1 
ATOM   1749 C  C   . PHE A 1 226 ? 31.414  34.914 15.275 1.00 21.65 ? 226 PHE A C   1 
ATOM   1750 O  O   . PHE A 1 226 ? 30.706  35.171 14.299 1.00 21.67 ? 226 PHE A O   1 
ATOM   1751 C  CB  . PHE A 1 226 ? 30.305  34.216 17.392 1.00 22.47 ? 226 PHE A CB  1 
ATOM   1752 C  CG  . PHE A 1 226 ? 29.806  33.176 18.340 1.00 21.71 ? 226 PHE A CG  1 
ATOM   1753 C  CD1 . PHE A 1 226 ? 29.542  31.857 17.954 1.00 24.82 ? 226 PHE A CD1 1 
ATOM   1754 C  CD2 . PHE A 1 226 ? 29.581  33.520 19.718 1.00 23.36 ? 226 PHE A CD2 1 
ATOM   1755 C  CE1 . PHE A 1 226 ? 29.081  30.879 18.873 1.00 25.63 ? 226 PHE A CE1 1 
ATOM   1756 C  CE2 . PHE A 1 226 ? 29.118  32.560 20.607 1.00 21.60 ? 226 PHE A CE2 1 
ATOM   1757 C  CZ  . PHE A 1 226 ? 28.853  31.242 20.211 1.00 21.93 ? 226 PHE A CZ  1 
ATOM   1758 N  N   . ARG A 1 227 ? 32.425  35.717 15.589 1.00 20.13 ? 227 ARG A N   1 
ATOM   1759 C  CA  . ARG A 1 227 ? 32.613  36.947 14.883 1.00 20.59 ? 227 ARG A CA  1 
ATOM   1760 C  C   . ARG A 1 227 ? 33.190  36.709 13.487 1.00 22.03 ? 227 ARG A C   1 
ATOM   1761 O  O   . ARG A 1 227 ? 33.182  37.640 12.678 1.00 23.37 ? 227 ARG A O   1 
ATOM   1762 C  CB  . ARG A 1 227 ? 33.563  37.920 15.646 1.00 21.26 ? 227 ARG A CB  1 
ATOM   1763 C  CG  . ARG A 1 227 ? 33.010  38.348 17.031 1.00 21.95 ? 227 ARG A CG  1 
ATOM   1764 C  CD  . ARG A 1 227 ? 33.687  39.608 17.572 1.00 29.95 ? 227 ARG A CD  1 
ATOM   1765 N  NE  . ARG A 1 227 ? 33.627  39.678 19.038 1.00 28.71 ? 227 ARG A NE  1 
ATOM   1766 C  CZ  . ARG A 1 227 ? 34.530  39.172 19.869 1.00 29.41 ? 227 ARG A CZ  1 
ATOM   1767 N  NH1 . ARG A 1 227 ? 35.644  38.591 19.408 1.00 30.27 ? 227 ARG A NH1 1 
ATOM   1768 N  NH2 . ARG A 1 227 ? 34.341  39.255 21.206 1.00 28.71 ? 227 ARG A NH2 1 
ATOM   1769 N  N   . SER A 1 228 ? 33.663  35.497 13.222 1.00 21.30 ? 228 SER A N   1 
ATOM   1770 C  CA  . SER A 1 228 ? 34.268  35.216 11.922 1.00 22.94 ? 228 SER A CA  1 
ATOM   1771 C  C   . SER A 1 228 ? 33.204  34.606 10.995 1.00 26.25 ? 228 SER A C   1 
ATOM   1772 O  O   . SER A 1 228 ? 33.477  34.416 9.794  1.00 22.39 ? 228 SER A O   1 
ATOM   1773 C  CB  . SER A 1 228 ? 35.432  34.230 12.012 1.00 23.90 ? 228 SER A CB  1 
ATOM   1774 O  OG  . SER A 1 228 ? 35.018  32.975 12.450 1.00 28.56 ? 228 SER A OG  1 
ATOM   1775 N  N   . LEU A 1 229 ? 32.004  34.310 11.513 1.00 23.15 ? 229 LEU A N   1 
ATOM   1776 C  CA  . LEU A 1 229 ? 30.847  34.075 10.567 1.00 23.31 ? 229 LEU A CA  1 
ATOM   1777 C  C   . LEU A 1 229 ? 30.651  35.263 9.639  1.00 21.11 ? 229 LEU A C   1 
ATOM   1778 O  O   . LEU A 1 229 ? 30.927  36.444 9.987  1.00 21.21 ? 229 LEU A O   1 
ATOM   1779 C  CB  . LEU A 1 229 ? 29.529  33.914 11.363 1.00 23.27 ? 229 LEU A CB  1 
ATOM   1780 C  CG  . LEU A 1 229 ? 29.500  32.463 11.792 1.00 29.09 ? 229 LEU A CG  1 
ATOM   1781 C  CD1 . LEU A 1 229 ? 28.382  32.338 12.837 1.00 29.80 ? 229 LEU A CD1 1 
ATOM   1782 C  CD2 . LEU A 1 229 ? 29.296  31.455 10.646 1.00 25.84 ? 229 LEU A CD2 1 
ATOM   1783 N  N   . LEU A 1 230 ? 30.191  34.996 8.418  1.00 21.45 ? 230 LEU A N   1 
ATOM   1784 C  CA  . LEU A 1 230 ? 30.153  36.072 7.421  1.00 21.34 ? 230 LEU A CA  1 
ATOM   1785 C  C   . LEU A 1 230 ? 28.717  36.418 7.044  1.00 18.05 ? 230 LEU A C   1 
ATOM   1786 O  O   . LEU A 1 230 ? 27.904  35.503 6.937  1.00 21.45 ? 230 LEU A O   1 
ATOM   1787 C  CB  . LEU A 1 230 ? 30.903  35.589 6.152  1.00 21.88 ? 230 LEU A CB  1 
ATOM   1788 C  CG  . LEU A 1 230 ? 32.411  35.354 6.409  1.00 22.00 ? 230 LEU A CG  1 
ATOM   1789 C  CD1 . LEU A 1 230 ? 33.131  34.856 5.103  1.00 25.90 ? 230 LEU A CD1 1 
ATOM   1790 C  CD2 . LEU A 1 230 ? 33.061  36.661 6.875  1.00 22.60 ? 230 LEU A CD2 1 
ATOM   1791 N  N   . SER A 1 231 ? 28.388  37.692 7.042  1.00 19.94 ? 231 SER A N   1 
ATOM   1792 C  CA  . SER A 1 231 ? 27.032  38.155 6.686  1.00 23.21 ? 231 SER A CA  1 
ATOM   1793 C  C   . SER A 1 231 ? 26.706  38.281 5.130  1.00 28.89 ? 231 SER A C   1 
ATOM   1794 O  O   . SER A 1 231 ? 25.567  38.541 4.756  1.00 32.45 ? 231 SER A O   1 
ATOM   1795 C  CB  . SER A 1 231 ? 26.766  39.514 7.296  1.00 25.41 ? 231 SER A CB  1 
ATOM   1796 O  OG  . SER A 1 231 ? 27.570  40.529 6.654  1.00 31.05 ? 231 SER A OG  1 
ATOM   1797 N  N   . ASN A 1 232 ? 27.731  38.190 4.286  1.00 30.64 ? 232 ASN A N   1 
ATOM   1798 C  CA  . ASN A 1 232 ? 27.622  38.272 2.805  1.00 26.41 ? 232 ASN A CA  1 
ATOM   1799 C  C   . ASN A 1 232 ? 27.359  36.870 2.292  1.00 25.22 ? 232 ASN A C   1 
ATOM   1800 O  O   . ASN A 1 232 ? 27.622  35.895 2.989  1.00 24.38 ? 232 ASN A O   1 
ATOM   1801 C  CB  . ASN A 1 232 ? 28.958  38.766 2.219  1.00 26.54 ? 232 ASN A CB  1 
ATOM   1802 C  CG  . ASN A 1 232 ? 30.126  37.875 2.634  1.00 27.33 ? 232 ASN A CG  1 
ATOM   1803 O  OD1 . ASN A 1 232 ? 30.658  38.014 3.756  1.00 23.86 ? 232 ASN A OD1 1 
ATOM   1804 N  ND2 . ASN A 1 232 ? 30.553  36.964 1.748  1.00 24.21 ? 232 ASN A ND2 1 
ATOM   1805 N  N   . VAL A 1 233 ? 26.835  36.745 1.047  1.00 25.23 ? 233 VAL A N   1 
ATOM   1806 C  CA  . VAL A 1 233 ? 26.635  35.433 0.422  1.00 26.68 ? 233 VAL A CA  1 
ATOM   1807 C  C   . VAL A 1 233 ? 27.935  34.993 -0.240 1.00 23.08 ? 233 VAL A C   1 
ATOM   1808 O  O   . VAL A 1 233 ? 28.805  35.819 -0.485 1.00 26.02 ? 233 VAL A O   1 
ATOM   1809 C  CB  . VAL A 1 233 ? 25.564  35.473 -0.706 1.00 28.77 ? 233 VAL A CB  1 
ATOM   1810 C  CG1 . VAL A 1 233 ? 24.150  35.637 -0.120 1.00 31.45 ? 233 VAL A CG1 1 
ATOM   1811 C  CG2 . VAL A 1 233 ? 25.877  36.654 -1.631 1.00 28.64 ? 233 VAL A CG2 1 
ATOM   1812 N  N   . GLU A 1 234 ? 28.063  33.685 -0.446 1.00 23.44 ? 234 GLU A N   1 
ATOM   1813 C  CA  . GLU A 1 234 ? 29.249  33.074 -1.071 1.00 25.19 ? 234 GLU A CA  1 
ATOM   1814 C  C   . GLU A 1 234 ? 29.687  33.863 -2.332 1.00 30.83 ? 234 GLU A C   1 
ATOM   1815 O  O   . GLU A 1 234 ? 28.839  34.271 -3.153 1.00 27.08 ? 234 GLU A O   1 
ATOM   1816 C  CB  . GLU A 1 234 ? 28.927  31.619 -1.432 1.00 33.29 ? 234 GLU A CB  1 
ATOM   1817 C  CG  . GLU A 1 234 ? 30.154  30.856 -1.859 1.00 32.49 ? 234 GLU A CG  1 
ATOM   1818 C  CD  . GLU A 1 234 ? 29.888  29.389 -1.953 1.00 41.90 ? 234 GLU A CD  1 
ATOM   1819 O  OE1 . GLU A 1 234 ? 29.757  28.712 -0.892 1.00 36.86 ? 234 GLU A OE1 1 
ATOM   1820 O  OE2 . GLU A 1 234 ? 29.834  28.915 -3.116 1.00 42.74 ? 234 GLU A OE2 1 
ATOM   1821 N  N   . GLY A 1 235 ? 30.991  34.128 -2.417 1.00 26.39 ? 235 GLY A N   1 
ATOM   1822 C  CA  . GLY A 1 235 ? 31.570  34.715 -3.633 1.00 32.37 ? 235 GLY A CA  1 
ATOM   1823 C  C   . GLY A 1 235 ? 31.673  36.213 -3.494 1.00 31.97 ? 235 GLY A C   1 
ATOM   1824 O  O   . GLY A 1 235 ? 32.469  36.854 -4.184 1.00 34.28 ? 235 GLY A O   1 
ATOM   1825 N  N   . ASP A 1 236 ? 30.910  36.789 -2.557 1.00 30.58 ? 236 ASP A N   1 
ATOM   1826 C  CA  . ASP A 1 236 ? 31.042  38.202 -2.279 1.00 28.95 ? 236 ASP A CA  1 
ATOM   1827 C  C   . ASP A 1 236 ? 32.245  38.557 -1.364 1.00 35.35 ? 236 ASP A C   1 
ATOM   1828 O  O   . ASP A 1 236 ? 32.862  37.641 -0.789 1.00 33.77 ? 236 ASP A O   1 
ATOM   1829 C  CB  . ASP A 1 236 ? 29.732  38.759 -1.727 1.00 33.71 ? 236 ASP A CB  1 
ATOM   1830 C  CG  . ASP A 1 236 ? 28.776  39.191 -2.818 1.00 39.82 ? 236 ASP A CG  1 
ATOM   1831 O  OD1 . ASP A 1 236 ? 27.625  39.540 -2.462 1.00 32.94 ? 236 ASP A OD1 1 
ATOM   1832 O  OD2 . ASP A 1 236 ? 29.174  39.181 -4.026 1.00 45.01 ? 236 ASP A OD2 1 
ATOM   1833 N  N   . ASN A 1 237 ? 32.591  39.848 -1.251 1.00 31.40 ? 237 ASN A N   1 
ATOM   1834 C  CA  . ASN A 1 237 ? 33.668  40.246 -0.303 1.00 40.36 ? 237 ASN A CA  1 
ATOM   1835 C  C   . ASN A 1 237 ? 33.130  39.990 1.100  1.00 37.80 ? 237 ASN A C   1 
ATOM   1836 O  O   . ASN A 1 237 ? 31.951  40.230 1.384  1.00 35.05 ? 237 ASN A O   1 
ATOM   1837 C  CB  . ASN A 1 237 ? 34.204  41.694 -0.412 1.00 45.35 ? 237 ASN A CB  1 
ATOM   1838 C  CG  . ASN A 1 237 ? 35.777  41.783 -0.304 1.00 58.87 ? 237 ASN A CG  1 
ATOM   1839 O  OD1 . ASN A 1 237 ? 36.435  41.183 0.586  1.00 57.46 ? 237 ASN A OD1 1 
ATOM   1840 N  ND2 . ASN A 1 237 ? 36.372  42.546 -1.211 1.00 56.68 ? 237 ASN A ND2 1 
ATOM   1841 N  N   . ALA A 1 238 ? 34.031  39.513 1.943  1.00 38.15 ? 238 ALA A N   1 
ATOM   1842 C  CA  . ALA A 1 238 ? 33.701  39.103 3.323  1.00 38.03 ? 238 ALA A CA  1 
ATOM   1843 C  C   . ALA A 1 238 ? 33.249  40.315 4.141  1.00 33.49 ? 238 ALA A C   1 
ATOM   1844 O  O   . ALA A 1 238 ? 33.856  41.416 4.099  1.00 31.53 ? 238 ALA A O   1 
ATOM   1845 C  CB  . ALA A 1 238 ? 34.900  38.359 3.938  1.00 35.72 ? 238 ALA A CB  1 
ATOM   1846 N  N   . VAL A 1 239 ? 32.112  40.160 4.830  1.00 33.50 ? 239 VAL A N   1 
ATOM   1847 C  CA  . VAL A 1 239 ? 31.631  41.151 5.820  1.00 30.56 ? 239 VAL A CA  1 
ATOM   1848 C  C   . VAL A 1 239 ? 31.392  40.303 7.104  1.00 34.72 ? 239 VAL A C   1 
ATOM   1849 O  O   . VAL A 1 239 ? 30.389  39.625 7.201  1.00 30.85 ? 239 VAL A O   1 
ATOM   1850 C  CB  . VAL A 1 239 ? 30.367  41.915 5.371  1.00 32.95 ? 239 VAL A CB  1 
ATOM   1851 C  CG1 . VAL A 1 239 ? 29.867  42.885 6.441  1.00 29.08 ? 239 VAL A CG1 1 
ATOM   1852 C  CG2 . VAL A 1 239 ? 30.656  42.703 4.075  1.00 33.64 ? 239 VAL A CG2 1 
ATOM   1853 N  N   . PRO A 1 240 ? 32.376  40.289 8.029  1.00 29.63 ? 240 PRO A N   1 
ATOM   1854 C  CA  . PRO A 1 240 ? 32.223  39.472 9.268  1.00 28.74 ? 240 PRO A CA  1 
ATOM   1855 C  C   . PRO A 1 240 ? 31.014  39.942 10.081 1.00 24.23 ? 240 PRO A C   1 
ATOM   1856 O  O   . PRO A 1 240 ? 30.661  41.117 10.064 1.00 25.51 ? 240 PRO A O   1 
ATOM   1857 C  CB  . PRO A 1 240 ? 33.493  39.800 10.034 1.00 30.42 ? 240 PRO A CB  1 
ATOM   1858 C  CG  . PRO A 1 240 ? 34.500  40.148 8.903  1.00 34.32 ? 240 PRO A CG  1 
ATOM   1859 C  CD  . PRO A 1 240 ? 33.669  41.013 7.997  1.00 32.36 ? 240 PRO A CD  1 
ATOM   1860 N  N   . MET A 1 241 ? 30.403  39.009 10.798 1.00 24.92 ? 241 MET A N   1 
ATOM   1861 C  CA  . MET A 1 241 ? 29.316  39.308 11.744 1.00 25.01 ? 241 MET A CA  1 
ATOM   1862 C  C   . MET A 1 241 ? 29.895  39.807 13.095 1.00 25.98 ? 241 MET A C   1 
ATOM   1863 O  O   . MET A 1 241 ? 30.053  39.048 14.059 1.00 24.29 ? 241 MET A O   1 
ATOM   1864 C  CB  . MET A 1 241 ? 28.562  38.027 12.039 1.00 29.72 ? 241 MET A CB  1 
ATOM   1865 C  CG  . MET A 1 241 ? 27.331  37.723 11.237 1.00 30.79 ? 241 MET A CG  1 
ATOM   1866 S  SD  . MET A 1 241 ? 26.560  36.203 11.777 1.00 26.66 ? 241 MET A SD  1 
ATOM   1867 C  CE  . MET A 1 241 ? 26.165  35.490 10.138 1.00 24.61 ? 241 MET A CE  1 
ATOM   1868 N  N   . GLN A 1 242 ? 30.171  41.081 13.180 1.00 25.18 ? 242 GLN A N   1 
ATOM   1869 C  CA  . GLN A 1 242 ? 30.942  41.564 14.334 1.00 25.56 ? 242 GLN A CA  1 
ATOM   1870 C  C   . GLN A 1 242 ? 30.084  41.593 15.589 1.00 25.48 ? 242 GLN A C   1 
ATOM   1871 O  O   . GLN A 1 242 ? 30.617  41.396 16.695 1.00 22.84 ? 242 GLN A O   1 
ATOM   1872 C  CB  . GLN A 1 242 ? 31.544  42.923 14.072 1.00 29.13 ? 242 GLN A CB  1 
ATOM   1873 C  CG  . GLN A 1 242 ? 32.697  42.831 13.054 1.00 32.40 ? 242 GLN A CG  1 
ATOM   1874 C  CD  . GLN A 1 242 ? 33.627  44.056 13.061 1.00 40.40 ? 242 GLN A CD  1 
ATOM   1875 O  OE1 . GLN A 1 242 ? 33.347  45.085 12.433 1.00 47.71 ? 242 GLN A OE1 1 
ATOM   1876 N  NE2 . GLN A 1 242 ? 34.737  43.941 13.771 1.00 42.65 ? 242 GLN A NE2 1 
ATOM   1877 N  N   . HIS A 1 243 ? 28.788  41.926 15.408 1.00 25.70 ? 243 HIS A N   1 
ATOM   1878 C  CA  . HIS A 1 243 ? 27.892  42.124 16.566 1.00 21.14 ? 243 HIS A CA  1 
ATOM   1879 C  C   . HIS A 1 243 ? 26.418  42.071 16.224 1.00 21.12 ? 243 HIS A C   1 
ATOM   1880 O  O   . HIS A 1 243 ? 26.020  42.301 15.112 1.00 21.33 ? 243 HIS A O   1 
ATOM   1881 C  CB  . HIS A 1 243 ? 28.179  43.462 17.239 1.00 23.59 ? 243 HIS A CB  1 
ATOM   1882 C  CG  . HIS A 1 243 ? 27.872  44.653 16.378 1.00 26.53 ? 243 HIS A CG  1 
ATOM   1883 N  ND1 . HIS A 1 243 ? 26.725  45.390 16.507 1.00 28.37 ? 243 HIS A ND1 1 
ATOM   1884 C  CD2 . HIS A 1 243 ? 28.635  45.267 15.361 1.00 28.82 ? 243 HIS A CD2 1 
ATOM   1885 C  CE1 . HIS A 1 243 ? 26.753  46.406 15.593 1.00 32.98 ? 243 HIS A CE1 1 
ATOM   1886 N  NE2 . HIS A 1 243 ? 27.915  46.310 14.883 1.00 30.93 ? 243 HIS A NE2 1 
ATOM   1887 N  N   . ASN A 1 244 ? 25.583  41.735 17.214 1.00 19.59 ? 244 ASN A N   1 
ATOM   1888 C  CA  . ASN A 1 244 ? 24.177  41.627 16.941 1.00 17.35 ? 244 ASN A CA  1 
ATOM   1889 C  C   . ASN A 1 244 ? 23.332  41.731 18.180 1.00 19.32 ? 244 ASN A C   1 
ATOM   1890 O  O   . ASN A 1 244 ? 22.263  41.068 18.282 1.00 16.81 ? 244 ASN A O   1 
ATOM   1891 C  CB  . ASN A 1 244 ? 23.885  40.290 16.264 1.00 17.54 ? 244 ASN A CB  1 
ATOM   1892 C  CG  . ASN A 1 244 ? 24.476  39.076 16.995 1.00 19.86 ? 244 ASN A CG  1 
ATOM   1893 O  OD1 . ASN A 1 244 ? 24.803  39.115 18.191 1.00 19.51 ? 244 ASN A OD1 1 
ATOM   1894 N  ND2 . ASN A 1 244 ? 24.586  37.931 16.246 1.00 20.86 ? 244 ASN A ND2 1 
ATOM   1895 N  N   . ASN A 1 245 ? 23.829  42.518 19.147 1.00 19.60 ? 245 ASN A N   1 
ATOM   1896 C  CA  . ASN A 1 245 ? 22.994  42.807 20.324 1.00 19.12 ? 245 ASN A CA  1 
ATOM   1897 C  C   . ASN A 1 245 ? 22.258  44.112 20.269 1.00 19.51 ? 245 ASN A C   1 
ATOM   1898 O  O   . ASN A 1 245 ? 22.815  45.139 19.826 1.00 23.02 ? 245 ASN A O   1 
ATOM   1899 C  CB  . ASN A 1 245 ? 23.882  42.716 21.583 1.00 19.52 ? 245 ASN A CB  1 
ATOM   1900 C  CG  . ASN A 1 245 ? 24.968  43.758 21.619 1.00 21.80 ? 245 ASN A CG  1 
ATOM   1901 O  OD1 . ASN A 1 245 ? 25.699  43.983 20.668 1.00 24.91 ? 245 ASN A OD1 1 
ATOM   1902 N  ND2 . ASN A 1 245 ? 25.104  44.415 22.805 1.00 23.15 ? 245 ASN A ND2 1 
ATOM   1903 N  N   . ARG A 1 246 ? 21.027  44.106 20.760 1.00 17.50 ? 246 ARG A N   1 
ATOM   1904 C  CA  . ARG A 1 246 ? 20.234  45.299 20.831 1.00 18.43 ? 246 ARG A CA  1 
ATOM   1905 C  C   . ARG A 1 246 ? 20.515  45.956 22.193 1.00 20.36 ? 246 ARG A C   1 
ATOM   1906 O  O   . ARG A 1 246 ? 20.616  45.247 23.223 1.00 22.76 ? 246 ARG A O   1 
ATOM   1907 C  CB  . ARG A 1 246 ? 18.714  44.947 20.799 1.00 16.83 ? 246 ARG A CB  1 
ATOM   1908 C  CG  . ARG A 1 246 ? 17.805  46.169 20.757 1.00 17.84 ? 246 ARG A CG  1 
ATOM   1909 C  CD  . ARG A 1 246 ? 16.347  45.851 20.969 1.00 16.47 ? 246 ARG A CD  1 
ATOM   1910 N  NE  . ARG A 1 246 ? 15.493  47.003 20.537 1.00 18.26 ? 246 ARG A NE  1 
ATOM   1911 C  CZ  . ARG A 1 246 ? 14.185  47.074 20.799 1.00 17.66 ? 246 ARG A CZ  1 
ATOM   1912 N  NH1 . ARG A 1 246 ? 13.560  46.120 21.471 1.00 21.26 ? 246 ARG A NH1 1 
ATOM   1913 N  NH2 . ARG A 1 246 ? 13.491  48.121 20.331 1.00 21.02 ? 246 ARG A NH2 1 
ATOM   1914 N  N   . PRO A 1 247 ? 20.572  47.311 22.216 1.00 20.61 ? 247 PRO A N   1 
ATOM   1915 C  CA  . PRO A 1 247 ? 20.705  48.043 23.489 1.00 21.48 ? 247 PRO A CA  1 
ATOM   1916 C  C   . PRO A 1 247 ? 19.546  47.761 24.424 1.00 22.33 ? 247 PRO A C   1 
ATOM   1917 O  O   . PRO A 1 247 ? 18.389  47.426 23.983 1.00 24.23 ? 247 PRO A O   1 
ATOM   1918 C  CB  . PRO A 1 247 ? 20.715  49.545 23.068 1.00 25.46 ? 247 PRO A CB  1 
ATOM   1919 C  CG  . PRO A 1 247 ? 21.025  49.568 21.641 1.00 24.21 ? 247 PRO A CG  1 
ATOM   1920 C  CD  . PRO A 1 247 ? 20.548  48.213 21.053 1.00 21.13 ? 247 PRO A CD  1 
ATOM   1921 N  N   . THR A 1 248 ? 19.793  47.867 25.735 1.00 20.87 ? 248 THR A N   1 
ATOM   1922 C  CA  . THR A 1 248 ? 18.714  47.677 26.678 1.00 20.21 ? 248 THR A CA  1 
ATOM   1923 C  C   . THR A 1 248 ? 17.672  48.777 26.548 1.00 21.44 ? 248 THR A C   1 
ATOM   1924 O  O   . THR A 1 248 ? 18.001  49.912 26.109 1.00 24.53 ? 248 THR A O   1 
ATOM   1925 C  CB  . THR A 1 248 ? 19.218  47.599 28.142 1.00 22.70 ? 248 THR A CB  1 
ATOM   1926 O  OG1 . THR A 1 248 ? 20.030  48.759 28.352 1.00 20.15 ? 248 THR A OG1 1 
ATOM   1927 C  CG2 . THR A 1 248 ? 20.095  46.336 28.339 1.00 19.84 ? 248 THR A CG2 1 
ATOM   1928 N  N   . GLN A 1 249 ? 16.448  48.421 26.910 1.00 20.59 ? 249 GLN A N   1 
ATOM   1929 C  CA  . GLN A 1 249 ? 15.247  49.222 26.644 1.00 22.28 ? 249 GLN A CA  1 
ATOM   1930 C  C   . GLN A 1 249 ? 14.597  49.647 27.975 1.00 24.48 ? 249 GLN A C   1 
ATOM   1931 O  O   . GLN A 1 249 ? 14.715  48.969 28.974 1.00 26.42 ? 249 GLN A O   1 
ATOM   1932 C  CB  . GLN A 1 249 ? 14.235  48.410 25.788 1.00 22.13 ? 249 GLN A CB  1 
ATOM   1933 C  CG  . GLN A 1 249 ? 14.786  48.065 24.403 1.00 24.07 ? 249 GLN A CG  1 
ATOM   1934 C  CD  . GLN A 1 249 ? 15.212  49.303 23.624 1.00 24.19 ? 249 GLN A CD  1 
ATOM   1935 O  OE1 . GLN A 1 249 ? 14.433  50.240 23.481 1.00 27.88 ? 249 GLN A OE1 1 
ATOM   1936 N  NE2 . GLN A 1 249 ? 16.454  49.311 23.112 1.00 26.37 ? 249 GLN A NE2 1 
ATOM   1937 N  N   . PRO A 1 250 ? 13.840  50.744 27.969 1.00 25.66 ? 250 PRO A N   1 
ATOM   1938 C  CA  . PRO A 1 250 ? 13.237  51.158 29.254 1.00 28.74 ? 250 PRO A CA  1 
ATOM   1939 C  C   . PRO A 1 250 ? 12.193  50.198 29.836 1.00 27.59 ? 250 PRO A C   1 
ATOM   1940 O  O   . PRO A 1 250 ? 11.374  49.688 29.069 1.00 26.43 ? 250 PRO A O   1 
ATOM   1941 C  CB  . PRO A 1 250 ? 12.554  52.478 28.928 1.00 27.38 ? 250 PRO A CB  1 
ATOM   1942 C  CG  . PRO A 1 250 ? 12.713  52.718 27.468 1.00 28.37 ? 250 PRO A CG  1 
ATOM   1943 C  CD  . PRO A 1 250 ? 13.525  51.624 26.848 1.00 27.17 ? 250 PRO A CD  1 
ATOM   1944 N  N   . LEU A 1 251 ? 12.199  49.959 31.172 1.00 25.58 ? 251 LEU A N   1 
ATOM   1945 C  CA  . LEU A 1 251 ? 11.227  49.111 31.810 1.00 26.38 ? 251 LEU A CA  1 
ATOM   1946 C  C   . LEU A 1 251 ? 9.784   49.596 31.703 1.00 26.72 ? 251 LEU A C   1 
ATOM   1947 O  O   . LEU A 1 251 ? 8.895   48.779 31.699 1.00 27.89 ? 251 LEU A O   1 
ATOM   1948 C  CB  . LEU A 1 251 ? 11.554  48.857 33.299 1.00 36.00 ? 251 LEU A CB  1 
ATOM   1949 C  CG  . LEU A 1 251 ? 12.519  47.751 33.772 1.00 37.06 ? 251 LEU A CG  1 
ATOM   1950 C  CD1 . LEU A 1 251 ? 12.465  47.676 35.311 1.00 37.93 ? 251 LEU A CD1 1 
ATOM   1951 C  CD2 . LEU A 1 251 ? 12.181  46.402 33.171 1.00 32.86 ? 251 LEU A CD2 1 
ATOM   1952 N  N   . LYS A 1 252 ? 9.537   50.911 31.605 1.00 28.69 ? 252 LYS A N   1 
ATOM   1953 C  CA  . LYS A 1 252 ? 8.148   51.414 31.482 1.00 29.98 ? 252 LYS A CA  1 
ATOM   1954 C  C   . LYS A 1 252 ? 7.226   50.836 32.561 1.00 30.88 ? 252 LYS A C   1 
ATOM   1955 O  O   . LYS A 1 252 ? 6.064   50.449 32.330 1.00 34.87 ? 252 LYS A O   1 
ATOM   1956 C  CB  . LYS A 1 252 ? 7.561   51.169 30.069 1.00 30.78 ? 252 LYS A CB  1 
ATOM   1957 C  CG  . LYS A 1 252 ? 8.278   51.887 28.955 1.00 36.61 ? 252 LYS A CG  1 
ATOM   1958 C  CD  . LYS A 1 252 ? 7.940   53.373 28.909 1.00 42.91 ? 252 LYS A CD  1 
ATOM   1959 C  CE  . LYS A 1 252 ? 8.726   54.090 27.825 1.00 47.32 ? 252 LYS A CE  1 
ATOM   1960 N  NZ  . LYS A 1 252 ? 8.552   53.535 26.452 1.00 48.99 ? 252 LYS A NZ  1 
ATOM   1961 N  N   . GLY A 1 253 ? 7.768   50.739 33.759 1.00 32.99 ? 253 GLY A N   1 
ATOM   1962 C  CA  . GLY A 1 253 ? 6.953   50.327 34.868 1.00 31.02 ? 253 GLY A CA  1 
ATOM   1963 C  C   . GLY A 1 253 ? 6.730   48.879 35.044 1.00 31.17 ? 253 GLY A C   1 
ATOM   1964 O  O   . GLY A 1 253 ? 6.038   48.496 35.957 1.00 33.76 ? 253 GLY A O   1 
ATOM   1965 N  N   . ARG A 1 254 ? 7.361   48.037 34.208 1.00 31.41 ? 254 ARG A N   1 
ATOM   1966 C  CA  . ARG A 1 254 ? 7.315   46.608 34.437 1.00 26.97 ? 254 ARG A CA  1 
ATOM   1967 C  C   . ARG A 1 254 ? 8.123   46.206 35.688 1.00 27.89 ? 254 ARG A C   1 
ATOM   1968 O  O   . ARG A 1 254 ? 9.069   46.884 36.102 1.00 28.65 ? 254 ARG A O   1 
ATOM   1969 C  CB  . ARG A 1 254 ? 7.952   45.852 33.228 1.00 23.68 ? 254 ARG A CB  1 
ATOM   1970 C  CG  . ARG A 1 254 ? 7.114   45.959 31.980 1.00 23.92 ? 254 ARG A CG  1 
ATOM   1971 C  CD  . ARG A 1 254 ? 7.843   45.276 30.798 1.00 21.45 ? 254 ARG A CD  1 
ATOM   1972 N  NE  . ARG A 1 254 ? 8.803   46.208 30.243 1.00 23.84 ? 254 ARG A NE  1 
ATOM   1973 C  CZ  . ARG A 1 254 ? 9.703   45.860 29.343 1.00 22.94 ? 254 ARG A CZ  1 
ATOM   1974 N  NH1 . ARG A 1 254 ? 9.727   44.610 28.910 1.00 23.01 ? 254 ARG A NH1 1 
ATOM   1975 N  NH2 . ARG A 1 254 ? 10.562  46.751 28.876 1.00 18.61 ? 254 ARG A NH2 1 
ATOM   1976 N  N   . THR A 1 255 ? 7.739   45.071 36.235 1.00 28.95 ? 255 THR A N   1 
ATOM   1977 C  CA  . THR A 1 255 ? 8.385   44.515 37.399 1.00 32.38 ? 255 THR A CA  1 
ATOM   1978 C  C   . THR A 1 255 ? 9.157   43.282 36.984 1.00 31.02 ? 255 THR A C   1 
ATOM   1979 O  O   . THR A 1 255 ? 8.596   42.350 36.393 1.00 28.08 ? 255 THR A O   1 
ATOM   1980 C  CB  . THR A 1 255 ? 7.315   44.245 38.504 1.00 36.93 ? 255 THR A CB  1 
ATOM   1981 O  OG1 . THR A 1 255 ? 7.008   45.503 39.108 1.00 42.02 ? 255 THR A OG1 1 
ATOM   1982 C  CG2 . THR A 1 255 ? 7.783   43.303 39.619 1.00 39.22 ? 255 THR A CG2 1 
ATOM   1983 N  N   . VAL A 1 256 ? 10.443  43.292 37.283 1.00 26.20 ? 256 VAL A N   1 
ATOM   1984 C  CA  . VAL A 1 256 ? 11.217  42.061 37.157 1.00 24.85 ? 256 VAL A CA  1 
ATOM   1985 C  C   . VAL A 1 256 ? 11.088  41.218 38.413 1.00 25.38 ? 256 VAL A C   1 
ATOM   1986 O  O   . VAL A 1 256 ? 11.464  41.634 39.535 1.00 25.02 ? 256 VAL A O   1 
ATOM   1987 C  CB  . VAL A 1 256 ? 12.725  42.364 36.896 1.00 23.56 ? 256 VAL A CB  1 
ATOM   1988 C  CG1 . VAL A 1 256 ? 13.530  41.085 36.704 1.00 21.65 ? 256 VAL A CG1 1 
ATOM   1989 C  CG2 . VAL A 1 256 ? 12.898  43.347 35.719 1.00 23.44 ? 256 VAL A CG2 1 
ATOM   1990 N  N   . ARG A 1 257 ? 10.623  40.009 38.247 1.00 22.79 ? 257 ARG A N   1 
ATOM   1991 C  CA  . ARG A 1 257 ? 10.530  39.079 39.388 1.00 25.31 ? 257 ARG A CA  1 
ATOM   1992 C  C   . ARG A 1 257 ? 11.746  38.167 39.532 1.00 27.68 ? 257 ARG A C   1 
ATOM   1993 O  O   . ARG A 1 257 ? 12.422  37.844 38.522 1.00 23.76 ? 257 ARG A O   1 
ATOM   1994 C  CB  . ARG A 1 257 ? 9.298   38.273 39.267 1.00 25.29 ? 257 ARG A CB  1 
ATOM   1995 C  CG  . ARG A 1 257 ? 8.029   39.125 39.398 1.00 26.96 ? 257 ARG A CG  1 
ATOM   1996 C  CD  . ARG A 1 257 ? 6.802   38.201 39.399 1.00 33.12 ? 257 ARG A CD  1 
ATOM   1997 N  NE  . ARG A 1 257 ? 6.495   37.731 38.027 1.00 32.24 ? 257 ARG A NE  1 
ATOM   1998 C  CZ  . ARG A 1 257 ? 5.764   36.665 37.696 1.00 32.47 ? 257 ARG A CZ  1 
ATOM   1999 N  NH1 . ARG A 1 257 ? 5.232   35.874 38.603 1.00 36.46 ? 257 ARG A NH1 1 
ATOM   2000 N  NH2 . ARG A 1 257 ? 5.567   36.371 36.405 1.00 34.26 ? 257 ARG A NH2 1 
ATOM   2001 N  N   . ALA A 1 258 ? 12.093  37.830 40.781 1.00 23.40 ? 258 ALA A N   1 
ATOM   2002 C  CA  . ALA A 1 258 ? 13.242  36.937 41.058 1.00 24.38 ? 258 ALA A CA  1 
ATOM   2003 C  C   . ALA A 1 258 ? 12.750  35.700 41.685 1.00 24.33 ? 258 ALA A C   1 
ATOM   2004 O  O   . ALA A 1 258 ? 11.919  35.718 42.607 1.00 30.03 ? 258 ALA A O   1 
ATOM   2005 C  CB  . ALA A 1 258 ? 14.291  37.604 41.971 1.00 23.51 ? 258 ALA A CB  1 
ATOM   2006 N  N   . SER A 1 259 ? 13.266  34.597 41.223 1.00 24.22 ? 259 SER A N   1 
ATOM   2007 C  CA  . SER A 1 259 ? 12.881  33.298 41.704 1.00 23.50 ? 259 SER A CA  1 
ATOM   2008 C  C   . SER A 1 259 ? 13.659  32.966 42.977 1.00 25.95 ? 259 SER A C   1 
ATOM   2009 O  O   . SER A 1 259 ? 13.478  31.907 43.546 1.00 28.89 ? 259 SER A O   1 
ATOM   2010 C  CB  . SER A 1 259 ? 13.181  32.228 40.661 1.00 26.88 ? 259 SER A CB  1 
ATOM   2011 O  OG  . SER A 1 259 ? 14.561  31.902 40.670 1.00 27.42 ? 259 SER A OG  1 
ATOM   2012 N  N   . PHE A 1 260 ? 14.555  33.858 43.382 1.00 27.08 ? 260 PHE A N   1 
ATOM   2013 C  CA  . PHE A 1 260 ? 15.511  33.472 44.439 1.00 30.31 ? 260 PHE A CA  1 
ATOM   2014 C  C   . PHE A 1 260 ? 15.622  34.665 45.397 1.00 33.82 ? 260 PHE A C   1 
ATOM   2015 O  O   . PHE A 1 260 ? 16.268  34.494 46.451 1.00 34.29 ? 260 PHE A O   1 
ATOM   2016 C  CB  . PHE A 1 260 ? 16.871  33.129 43.789 1.00 28.61 ? 260 PHE A CB  1 
ATOM   2017 C  CG  . PHE A 1 260 ? 17.446  34.286 43.007 1.00 30.90 ? 260 PHE A CG  1 
ATOM   2018 C  CD1 . PHE A 1 260 ? 17.110  34.479 41.653 1.00 22.99 ? 260 PHE A CD1 1 
ATOM   2019 C  CD2 . PHE A 1 260 ? 18.306  35.222 43.614 1.00 30.00 ? 260 PHE A CD2 1 
ATOM   2020 C  CE1 . PHE A 1 260 ? 17.598  35.546 40.953 1.00 25.38 ? 260 PHE A CE1 1 
ATOM   2021 C  CE2 . PHE A 1 260 ? 18.779  36.332 42.889 1.00 31.64 ? 260 PHE A CE2 1 
ATOM   2022 C  CZ  . PHE A 1 260 ? 18.434  36.480 41.527 1.00 27.65 ? 260 PHE A CZ  1 
ATOM   2023 O  OXT . PHE A 1 260 ? 15.114  35.794 45.096 1.00 32.31 ? 260 PHE A OXT 1 
ATOM   2024 N  N   . ASP B 1 4   ? 3.183   82.041 42.685 1.00 54.59 ? 4   ASP B N   1 
ATOM   2025 C  CA  . ASP B 1 4   ? 4.591   81.651 43.063 1.00 49.97 ? 4   ASP B CA  1 
ATOM   2026 C  C   . ASP B 1 4   ? 5.164   82.253 44.397 1.00 45.96 ? 4   ASP B C   1 
ATOM   2027 O  O   . ASP B 1 4   ? 4.896   83.434 44.768 1.00 40.54 ? 4   ASP B O   1 
ATOM   2028 C  CB  . ASP B 1 4   ? 5.553   81.887 41.902 1.00 60.52 ? 4   ASP B CB  1 
ATOM   2029 C  CG  . ASP B 1 4   ? 6.823   81.068 42.042 1.00 61.56 ? 4   ASP B CG  1 
ATOM   2030 O  OD1 . ASP B 1 4   ? 7.898   81.672 42.283 1.00 55.84 ? 4   ASP B OD1 1 
ATOM   2031 O  OD2 . ASP B 1 4   ? 6.737   79.820 41.944 1.00 68.11 ? 4   ASP B OD2 1 
ATOM   2032 N  N   . TRP B 1 5   ? 5.950   81.425 45.107 1.00 34.65 ? 5   TRP B N   1 
ATOM   2033 C  CA  . TRP B 1 5   ? 6.386   81.719 46.481 1.00 26.66 ? 5   TRP B CA  1 
ATOM   2034 C  C   . TRP B 1 5   ? 7.633   80.938 46.843 1.00 23.14 ? 5   TRP B C   1 
ATOM   2035 O  O   . TRP B 1 5   ? 7.896   79.887 46.302 1.00 23.73 ? 5   TRP B O   1 
ATOM   2036 C  CB  . TRP B 1 5   ? 5.240   81.460 47.448 1.00 25.32 ? 5   TRP B CB  1 
ATOM   2037 C  CG  . TRP B 1 5   ? 4.988   79.982 47.655 1.00 24.93 ? 5   TRP B CG  1 
ATOM   2038 C  CD1 . TRP B 1 5   ? 4.045   79.171 47.013 1.00 27.79 ? 5   TRP B CD1 1 
ATOM   2039 C  CD2 . TRP B 1 5   ? 5.658   79.098 48.628 1.00 22.93 ? 5   TRP B CD2 1 
ATOM   2040 N  NE1 . TRP B 1 5   ? 4.122   77.866 47.468 1.00 25.44 ? 5   TRP B NE1 1 
ATOM   2041 C  CE2 . TRP B 1 5   ? 5.070   77.778 48.460 1.00 24.79 ? 5   TRP B CE2 1 
ATOM   2042 C  CE3 . TRP B 1 5   ? 6.687   79.263 49.545 1.00 24.93 ? 5   TRP B CE3 1 
ATOM   2043 C  CZ2 . TRP B 1 5   ? 5.474   76.676 49.245 1.00 22.46 ? 5   TRP B CZ2 1 
ATOM   2044 C  CZ3 . TRP B 1 5   ? 7.091   78.113 50.319 1.00 22.54 ? 5   TRP B CZ3 1 
ATOM   2045 C  CH2 . TRP B 1 5   ? 6.523   76.882 50.127 1.00 19.92 ? 5   TRP B CH2 1 
ATOM   2046 N  N   . GLY B 1 6   ? 8.457   81.495 47.713 1.00 24.90 ? 6   GLY B N   1 
ATOM   2047 C  CA  . GLY B 1 6   ? 9.673   80.841 48.203 1.00 23.21 ? 6   GLY B CA  1 
ATOM   2048 C  C   . GLY B 1 6   ? 10.148  81.437 49.515 1.00 21.57 ? 6   GLY B C   1 
ATOM   2049 O  O   . GLY B 1 6   ? 9.329   81.885 50.330 1.00 20.59 ? 6   GLY B O   1 
ATOM   2050 N  N   . TYR B 1 7   ? 11.466  81.436 49.720 1.00 22.58 ? 7   TYR B N   1 
ATOM   2051 C  CA  . TYR B 1 7   ? 12.044  81.932 50.971 1.00 23.72 ? 7   TYR B CA  1 
ATOM   2052 C  C   . TYR B 1 7   ? 13.050  83.050 50.746 1.00 27.90 ? 7   TYR B C   1 
ATOM   2053 O  O   . TYR B 1 7   ? 13.665  83.512 51.693 1.00 27.46 ? 7   TYR B O   1 
ATOM   2054 C  CB  . TYR B 1 7   ? 12.680  80.819 51.804 1.00 22.01 ? 7   TYR B CB  1 
ATOM   2055 C  CG  . TYR B 1 7   ? 11.597  79.884 52.382 1.00 18.59 ? 7   TYR B CG  1 
ATOM   2056 C  CD1 . TYR B 1 7   ? 11.230  78.712 51.704 1.00 18.67 ? 7   TYR B CD1 1 
ATOM   2057 C  CD2 . TYR B 1 7   ? 11.003  80.150 53.609 1.00 17.51 ? 7   TYR B CD2 1 
ATOM   2058 C  CE1 . TYR B 1 7   ? 10.219  77.871 52.224 1.00 17.17 ? 7   TYR B CE1 1 
ATOM   2059 C  CE2 . TYR B 1 7   ? 10.034  79.292 54.134 1.00 16.61 ? 7   TYR B CE2 1 
ATOM   2060 C  CZ  . TYR B 1 7   ? 9.680   78.136 53.446 1.00 20.07 ? 7   TYR B CZ  1 
ATOM   2061 O  OH  . TYR B 1 7   ? 8.686   77.293 53.957 1.00 19.51 ? 7   TYR B OH  1 
ATOM   2062 N  N   . ASP B 1 8   ? 13.197  83.462 49.483 1.00 31.66 ? 8   ASP B N   1 
ATOM   2063 C  CA  . ASP B 1 8   ? 14.192  84.505 49.122 1.00 35.63 ? 8   ASP B CA  1 
ATOM   2064 C  C   . ASP B 1 8   ? 13.564  85.869 49.272 1.00 33.03 ? 8   ASP B C   1 
ATOM   2065 O  O   . ASP B 1 8   ? 12.374  85.991 49.561 1.00 32.29 ? 8   ASP B O   1 
ATOM   2066 C  CB  . ASP B 1 8   ? 14.703  84.338 47.678 1.00 35.40 ? 8   ASP B CB  1 
ATOM   2067 C  CG  . ASP B 1 8   ? 15.468  83.050 47.470 1.00 41.47 ? 8   ASP B CG  1 
ATOM   2068 O  OD1 . ASP B 1 8   ? 15.096  82.291 46.530 1.00 43.58 ? 8   ASP B OD1 1 
ATOM   2069 O  OD2 . ASP B 1 8   ? 16.425  82.809 48.244 1.00 44.84 ? 8   ASP B OD2 1 
ATOM   2070 N  N   . ASP B 1 9   ? 14.326  86.921 49.057 1.00 33.84 ? 9   ASP B N   1 
ATOM   2071 C  CA  . ASP B 1 9   ? 13.796  88.248 49.252 1.00 40.47 ? 9   ASP B CA  1 
ATOM   2072 C  C   . ASP B 1 9   ? 12.598  88.519 48.387 1.00 36.00 ? 9   ASP B C   1 
ATOM   2073 O  O   . ASP B 1 9   ? 11.643  89.064 48.820 1.00 38.13 ? 9   ASP B O   1 
ATOM   2074 C  CB  . ASP B 1 9   ? 14.808  89.334 48.903 1.00 50.85 ? 9   ASP B CB  1 
ATOM   2075 C  CG  . ASP B 1 9   ? 16.029  89.326 49.757 1.00 64.68 ? 9   ASP B CG  1 
ATOM   2076 O  OD1 . ASP B 1 9   ? 15.930  88.932 50.921 1.00 59.79 ? 9   ASP B OD1 1 
ATOM   2077 O  OD2 . ASP B 1 9   ? 17.096  89.719 49.248 1.00 70.82 ? 9   ASP B OD2 1 
ATOM   2078 N  N   . LYS B 1 10  ? 12.689  88.191 47.125 1.00 38.19 ? 10  LYS B N   1 
ATOM   2079 C  CA  . LYS B 1 10  ? 11.604  88.587 46.195 1.00 38.33 ? 10  LYS B CA  1 
ATOM   2080 C  C   . LYS B 1 10  ? 10.257  87.854 46.390 1.00 36.94 ? 10  LYS B C   1 
ATOM   2081 O  O   . LYS B 1 10  ? 9.202   88.423 46.133 1.00 36.41 ? 10  LYS B O   1 
ATOM   2082 C  CB  . LYS B 1 10  ? 12.080  88.610 44.729 1.00 42.55 ? 10  LYS B CB  1 
ATOM   2083 C  CG  . LYS B 1 10  ? 12.757  87.345 44.241 1.00 51.52 ? 10  LYS B CG  1 
ATOM   2084 C  CD  . LYS B 1 10  ? 11.766  86.413 43.546 1.00 51.82 ? 10  LYS B CD  1 
ATOM   2085 C  CE  . LYS B 1 10  ? 12.512  85.316 42.808 1.00 53.78 ? 10  LYS B CE  1 
ATOM   2086 N  NZ  . LYS B 1 10  ? 13.684  84.844 43.598 1.00 55.75 ? 10  LYS B NZ  1 
ATOM   2087 N  N   . ASN B 1 11  ? 10.292  86.623 46.918 1.00 35.91 ? 11  ASN B N   1 
ATOM   2088 C  CA  . ASN B 1 11  ? 9.080   85.759 46.999 1.00 31.62 ? 11  ASN B CA  1 
ATOM   2089 C  C   . ASN B 1 11  ? 8.836   85.145 48.406 1.00 30.42 ? 11  ASN B C   1 
ATOM   2090 O  O   . ASN B 1 11  ? 8.007   84.221 48.530 1.00 24.92 ? 11  ASN B O   1 
ATOM   2091 C  CB  . ASN B 1 11  ? 9.194   84.582 46.015 1.00 33.17 ? 11  ASN B CB  1 
ATOM   2092 C  CG  . ASN B 1 11  ? 10.430  83.722 46.263 1.00 30.55 ? 11  ASN B CG  1 
ATOM   2093 O  OD1 . ASN B 1 11  ? 11.114  83.848 47.288 1.00 27.39 ? 11  ASN B OD1 1 
ATOM   2094 N  ND2 . ASN B 1 11  ? 10.738  82.851 45.316 1.00 35.48 ? 11  ASN B ND2 1 
ATOM   2095 N  N   . GLY B 1 12  ? 9.546   85.660 49.412 1.00 26.58 ? 12  GLY B N   1 
ATOM   2096 C  CA  . GLY B 1 12  ? 9.511   85.097 50.751 1.00 25.84 ? 12  GLY B CA  1 
ATOM   2097 C  C   . GLY B 1 12  ? 8.424   85.517 51.684 1.00 25.24 ? 12  GLY B C   1 
ATOM   2098 O  O   . GLY B 1 12  ? 7.474   86.204 51.313 1.00 26.64 ? 12  GLY B O   1 
ATOM   2099 N  N   . PRO B 1 13  ? 8.556   85.104 52.974 1.00 22.91 ? 13  PRO B N   1 
ATOM   2100 C  CA  . PRO B 1 13  ? 7.486   85.245 53.932 1.00 21.80 ? 13  PRO B CA  1 
ATOM   2101 C  C   . PRO B 1 13  ? 6.962   86.652 54.059 1.00 24.88 ? 13  PRO B C   1 
ATOM   2102 O  O   . PRO B 1 13  ? 5.793   86.803 54.330 1.00 23.06 ? 13  PRO B O   1 
ATOM   2103 C  CB  . PRO B 1 13  ? 8.147   84.821 55.262 1.00 23.75 ? 13  PRO B CB  1 
ATOM   2104 C  CG  . PRO B 1 13  ? 9.193   83.816 54.831 1.00 21.46 ? 13  PRO B CG  1 
ATOM   2105 C  CD  . PRO B 1 13  ? 9.650   84.219 53.445 1.00 23.36 ? 13  PRO B CD  1 
ATOM   2106 N  N   . GLU B 1 14  ? 7.824   87.649 53.890 1.00 25.32 ? 14  GLU B N   1 
ATOM   2107 C  CA  . GLU B 1 14  ? 7.368   89.042 53.978 1.00 32.22 ? 14  GLU B CA  1 
ATOM   2108 C  C   . GLU B 1 14  ? 6.431   89.482 52.849 1.00 31.34 ? 14  GLU B C   1 
ATOM   2109 O  O   . GLU B 1 14  ? 5.724   90.504 52.980 1.00 30.53 ? 14  GLU B O   1 
ATOM   2110 C  CB  . GLU B 1 14  ? 8.563   90.020 54.065 1.00 33.82 ? 14  GLU B CB  1 
ATOM   2111 C  CG  . GLU B 1 14  ? 9.414   89.813 55.315 1.00 46.32 ? 14  GLU B CG  1 
ATOM   2112 C  CD  . GLU B 1 14  ? 8.560   89.555 56.564 1.00 57.21 ? 14  GLU B CD  1 
ATOM   2113 O  OE1 . GLU B 1 14  ? 8.909   88.622 57.352 1.00 58.83 ? 14  GLU B OE1 1 
ATOM   2114 O  OE2 . GLU B 1 14  ? 7.529   90.267 56.755 1.00 57.36 ? 14  GLU B OE2 1 
ATOM   2115 N  N   A GLN B 1 15  ? 6.388   88.707 51.774 0.50 29.89 ? 15  GLN B N   1 
ATOM   2116 N  N   B GLN B 1 15  ? 6.430   88.715 51.756 0.50 30.87 ? 15  GLN B N   1 
ATOM   2117 C  CA  A GLN B 1 15  ? 5.546   89.059 50.638 0.50 30.44 ? 15  GLN B CA  1 
ATOM   2118 C  CA  B GLN B 1 15  ? 5.602   88.981 50.564 0.50 32.27 ? 15  GLN B CA  1 
ATOM   2119 C  C   A GLN B 1 15  ? 4.547   87.953 50.259 0.50 27.62 ? 15  GLN B C   1 
ATOM   2120 C  C   B GLN B 1 15  ? 4.339   88.117 50.507 0.50 29.63 ? 15  GLN B C   1 
ATOM   2121 O  O   A GLN B 1 15  ? 3.929   88.032 49.202 0.50 24.06 ? 15  GLN B O   1 
ATOM   2122 O  O   B GLN B 1 15  ? 3.345   88.500 49.909 0.50 27.67 ? 15  GLN B O   1 
ATOM   2123 C  CB  A GLN B 1 15  ? 6.432   89.397 49.433 0.50 31.10 ? 15  GLN B CB  1 
ATOM   2124 C  CB  B GLN B 1 15  ? 6.422   88.712 49.284 0.50 34.04 ? 15  GLN B CB  1 
ATOM   2125 C  CG  A GLN B 1 15  ? 6.599   88.219 48.482 0.50 32.36 ? 15  GLN B CG  1 
ATOM   2126 C  CG  B GLN B 1 15  ? 7.739   89.459 49.188 0.50 32.29 ? 15  GLN B CG  1 
ATOM   2127 C  CD  A GLN B 1 15  ? 6.188   88.569 47.067 0.50 31.62 ? 15  GLN B CD  1 
ATOM   2128 C  CD  B GLN B 1 15  ? 7.578   90.962 49.409 0.50 34.11 ? 15  GLN B CD  1 
ATOM   2129 O  OE1 A GLN B 1 15  ? 5.985   89.736 46.735 0.50 38.24 ? 15  GLN B OE1 1 
ATOM   2130 O  OE1 B GLN B 1 15  ? 6.695   91.586 48.834 0.50 33.98 ? 15  GLN B OE1 1 
ATOM   2131 N  NE2 A GLN B 1 15  ? 6.077   87.552 46.214 0.50 32.64 ? 15  GLN B NE2 1 
ATOM   2132 N  NE2 B GLN B 1 15  ? 8.422   91.540 50.263 0.50 36.53 ? 15  GLN B NE2 1 
ATOM   2133 N  N   . TRP B 1 16  ? 4.384   86.937 51.118 1.00 25.93 ? 16  TRP B N   1 
ATOM   2134 C  CA  . TRP B 1 16  ? 3.290   85.956 50.964 1.00 22.17 ? 16  TRP B CA  1 
ATOM   2135 C  C   . TRP B 1 16  ? 1.890   86.498 50.974 1.00 25.04 ? 16  TRP B C   1 
ATOM   2136 O  O   . TRP B 1 16  ? 1.038   85.985 50.240 1.00 24.09 ? 16  TRP B O   1 
ATOM   2137 C  CB  . TRP B 1 16  ? 3.420   84.816 51.993 1.00 22.42 ? 16  TRP B CB  1 
ATOM   2138 C  CG  . TRP B 1 16  ? 4.629   83.956 51.790 1.00 20.84 ? 16  TRP B CG  1 
ATOM   2139 C  CD1 . TRP B 1 16  ? 5.484   83.941 50.739 1.00 19.58 ? 16  TRP B CD1 1 
ATOM   2140 C  CD2 . TRP B 1 16  ? 5.107   82.895 52.710 1.00 18.72 ? 16  TRP B CD2 1 
ATOM   2141 N  NE1 . TRP B 1 16  ? 6.465   82.975 50.910 1.00 20.67 ? 16  TRP B NE1 1 
ATOM   2142 C  CE2 . TRP B 1 16  ? 6.288   82.317 52.091 1.00 20.39 ? 16  TRP B CE2 1 
ATOM   2143 C  CE3 . TRP B 1 16  ? 4.664   82.412 53.940 1.00 18.79 ? 16  TRP B CE3 1 
ATOM   2144 C  CZ2 . TRP B 1 16  ? 7.064   81.293 52.720 1.00 18.25 ? 16  TRP B CZ2 1 
ATOM   2145 C  CZ3 . TRP B 1 16  ? 5.424   81.397 54.549 1.00 16.47 ? 16  TRP B CZ3 1 
ATOM   2146 C  CH2 . TRP B 1 16  ? 6.580   80.843 53.939 1.00 17.97 ? 16  TRP B CH2 1 
ATOM   2147 N  N   . SER B 1 17  ? 1.579   87.479 51.837 1.00 22.90 ? 17  SER B N   1 
ATOM   2148 C  CA  . SER B 1 17  ? 0.182   87.971 51.984 1.00 24.37 ? 17  SER B CA  1 
ATOM   2149 C  C   . SER B 1 17  ? -0.423  88.486 50.665 1.00 23.91 ? 17  SER B C   1 
ATOM   2150 O  O   . SER B 1 17  ? -1.647  88.499 50.523 1.00 25.26 ? 17  SER B O   1 
ATOM   2151 C  CB  . SER B 1 17  ? 0.101   89.082 53.038 1.00 28.10 ? 17  SER B CB  1 
ATOM   2152 O  OG  . SER B 1 17  ? 0.910   90.136 52.548 1.00 25.72 ? 17  SER B OG  1 
ATOM   2153 N  N   . LYS B 1 18  ? 0.445   88.816 49.705 1.00 24.29 ? 18  LYS B N   1 
ATOM   2154 C  CA  . LYS B 1 18  ? -0.049  89.391 48.400 1.00 30.86 ? 18  LYS B CA  1 
ATOM   2155 C  C   . LYS B 1 18  ? -0.901  88.373 47.650 1.00 29.44 ? 18  LYS B C   1 
ATOM   2156 O  O   . LYS B 1 18  ? -2.022  88.667 47.219 1.00 31.81 ? 18  LYS B O   1 
ATOM   2157 C  CB  . LYS B 1 18  ? 1.122   89.822 47.530 1.00 29.09 ? 18  LYS B CB  1 
ATOM   2158 C  CG  . LYS B 1 18  ? 1.800   91.080 48.105 1.00 37.10 ? 18  LYS B CG  1 
ATOM   2159 C  CD  . LYS B 1 18  ? 2.773   91.691 47.112 1.00 39.12 ? 18  LYS B CD  1 
ATOM   2160 C  CE  . LYS B 1 18  ? 3.684   92.698 47.784 1.00 42.11 ? 18  LYS B CE  1 
ATOM   2161 N  NZ  . LYS B 1 18  ? 4.678   93.168 46.775 1.00 41.41 ? 18  LYS B NZ  1 
ATOM   2162 N  N   . LEU B 1 19  ? -0.342  87.164 47.514 1.00 28.68 ? 19  LEU B N   1 
ATOM   2163 C  CA  . LEU B 1 19  ? -1.020  86.047 46.836 1.00 27.18 ? 19  LEU B CA  1 
ATOM   2164 C  C   . LEU B 1 19  ? -1.862  85.219 47.890 1.00 26.60 ? 19  LEU B C   1 
ATOM   2165 O  O   . LEU B 1 19  ? -2.841  84.527 47.532 1.00 25.08 ? 19  LEU B O   1 
ATOM   2166 C  CB  . LEU B 1 19  ? 0.001   85.154 46.135 1.00 29.60 ? 19  LEU B CB  1 
ATOM   2167 C  CG  . LEU B 1 19  ? 0.669   85.871 44.961 1.00 36.19 ? 19  LEU B CG  1 
ATOM   2168 C  CD1 . LEU B 1 19  ? 1.608   84.981 44.159 1.00 37.97 ? 19  LEU B CD1 1 
ATOM   2169 C  CD2 . LEU B 1 19  ? -0.398  86.488 44.072 1.00 38.28 ? 19  LEU B CD2 1 
ATOM   2170 N  N   . TYR B 1 20  ? -1.475  85.283 49.171 1.00 22.91 ? 20  TYR B N   1 
ATOM   2171 C  CA  . TYR B 1 20  ? -2.144  84.494 50.199 1.00 22.95 ? 20  TYR B CA  1 
ATOM   2172 C  C   . TYR B 1 20  ? -2.528  85.371 51.402 1.00 26.78 ? 20  TYR B C   1 
ATOM   2173 O  O   . TYR B 1 20  ? -1.834  85.358 52.427 1.00 23.37 ? 20  TYR B O   1 
ATOM   2174 C  CB  . TYR B 1 20  ? -1.212  83.306 50.682 1.00 23.33 ? 20  TYR B CB  1 
ATOM   2175 C  CG  . TYR B 1 20  ? -0.684  82.481 49.512 1.00 22.80 ? 20  TYR B CG  1 
ATOM   2176 C  CD1 . TYR B 1 20  ? 0.526   82.787 48.900 1.00 23.82 ? 20  TYR B CD1 1 
ATOM   2177 C  CD2 . TYR B 1 20  ? -1.417  81.392 49.056 1.00 28.89 ? 20  TYR B CD2 1 
ATOM   2178 C  CE1 . TYR B 1 20  ? 0.987   82.039 47.789 1.00 23.83 ? 20  TYR B CE1 1 
ATOM   2179 C  CE2 . TYR B 1 20  ? -1.010  80.655 47.947 1.00 26.87 ? 20  TYR B CE2 1 
ATOM   2180 C  CZ  . TYR B 1 20  ? 0.171   80.981 47.338 1.00 26.32 ? 20  TYR B CZ  1 
ATOM   2181 O  OH  . TYR B 1 20  ? 0.565   80.220 46.284 1.00 28.81 ? 20  TYR B OH  1 
ATOM   2182 N  N   . PRO B 1 21  ? -3.648  86.132 51.297 1.00 23.68 ? 21  PRO B N   1 
ATOM   2183 C  CA  . PRO B 1 21  ? -4.007  87.097 52.336 1.00 23.28 ? 21  PRO B CA  1 
ATOM   2184 C  C   . PRO B 1 21  ? -4.171  86.549 53.771 1.00 23.91 ? 21  PRO B C   1 
ATOM   2185 O  O   . PRO B 1 21  ? -4.045  87.307 54.765 1.00 23.46 ? 21  PRO B O   1 
ATOM   2186 C  CB  . PRO B 1 21  ? -5.349  87.646 51.831 1.00 25.31 ? 21  PRO B CB  1 
ATOM   2187 C  CG  . PRO B 1 21  ? -5.194  87.566 50.355 1.00 23.10 ? 21  PRO B CG  1 
ATOM   2188 C  CD  . PRO B 1 21  ? -4.615  86.169 50.181 1.00 25.11 ? 21  PRO B CD  1 
ATOM   2189 N  N   . ILE B 1 22  ? -4.453  85.239 53.887 1.00 22.99 ? 22  ILE B N   1 
ATOM   2190 C  CA  . ILE B 1 22  ? -4.508  84.573 55.181 1.00 22.78 ? 22  ILE B CA  1 
ATOM   2191 C  C   . ILE B 1 22  ? -3.182  84.677 55.955 1.00 20.54 ? 22  ILE B C   1 
ATOM   2192 O  O   . ILE B 1 22  ? -3.220  84.455 57.167 1.00 22.97 ? 22  ILE B O   1 
ATOM   2193 C  CB  . ILE B 1 22  ? -4.963  83.093 55.007 1.00 21.28 ? 22  ILE B CB  1 
ATOM   2194 C  CG1 . ILE B 1 22  ? -5.607  82.531 56.263 1.00 23.16 ? 22  ILE B CG1 1 
ATOM   2195 C  CG2 . ILE B 1 22  ? -3.802  82.217 54.490 1.00 22.89 ? 22  ILE B CG2 1 
ATOM   2196 C  CD1 . ILE B 1 22  ? -6.592  83.466 56.913 1.00 31.36 ? 22  ILE B CD1 1 
ATOM   2197 N  N   . ALA B 1 23  ? -2.092  85.018 55.269 1.00 21.18 ? 23  ALA B N   1 
ATOM   2198 C  CA  . ALA B 1 23  ? -0.744  85.159 55.905 1.00 20.93 ? 23  ALA B CA  1 
ATOM   2199 C  C   . ALA B 1 23  ? -0.751  86.170 57.041 1.00 25.08 ? 23  ALA B C   1 
ATOM   2200 O  O   . ALA B 1 23  ? 0.094   86.091 57.945 1.00 23.37 ? 23  ALA B O   1 
ATOM   2201 C  CB  . ALA B 1 23  ? 0.342   85.532 54.899 1.00 21.88 ? 23  ALA B CB  1 
ATOM   2202 N  N   . ASN B 1 24  ? -1.723  87.101 56.979 1.00 27.84 ? 24  ASN B N   1 
ATOM   2203 C  CA  . ASN B 1 24  ? -1.909  88.136 57.996 1.00 27.98 ? 24  ASN B CA  1 
ATOM   2204 C  C   . ASN B 1 24  ? -3.057  87.724 58.924 1.00 28.20 ? 24  ASN B C   1 
ATOM   2205 O  O   . ASN B 1 24  ? -3.616  88.558 59.614 1.00 28.02 ? 24  ASN B O   1 
ATOM   2206 C  CB  . ASN B 1 24  ? -2.242  89.482 57.369 1.00 30.32 ? 24  ASN B CB  1 
ATOM   2207 C  CG  . ASN B 1 24  ? -1.059  90.105 56.672 1.00 31.53 ? 24  ASN B CG  1 
ATOM   2208 O  OD1 . ASN B 1 24  ? 0.079   89.980 57.122 1.00 32.48 ? 24  ASN B OD1 1 
ATOM   2209 N  ND2 . ASN B 1 24  ? -1.322  90.779 55.560 1.00 30.12 ? 24  ASN B ND2 1 
ATOM   2210 N  N   . GLY B 1 25  ? -3.436  86.453 58.953 1.00 22.26 ? 25  GLY B N   1 
ATOM   2211 C  CA  . GLY B 1 25  ? -4.580  85.967 59.727 1.00 22.47 ? 25  GLY B CA  1 
ATOM   2212 C  C   . GLY B 1 25  ? -4.400  85.951 61.232 1.00 23.56 ? 25  GLY B C   1 
ATOM   2213 O  O   . GLY B 1 25  ? -3.330  86.331 61.731 1.00 26.96 ? 25  GLY B O   1 
ATOM   2214 N  N   . ASN B 1 26  ? -5.409  85.442 61.941 1.00 23.51 ? 26  ASN B N   1 
ATOM   2215 C  CA  . ASN B 1 26  ? -5.359  85.422 63.408 1.00 26.07 ? 26  ASN B CA  1 
ATOM   2216 C  C   . ASN B 1 26  ? -4.860  84.133 64.028 1.00 24.15 ? 26  ASN B C   1 
ATOM   2217 O  O   . ASN B 1 26  ? -4.767  84.017 65.244 1.00 23.80 ? 26  ASN B O   1 
ATOM   2218 C  CB  . ASN B 1 26  ? -6.745  85.670 63.945 1.00 25.95 ? 26  ASN B CB  1 
ATOM   2219 C  CG  . ASN B 1 26  ? -7.172  87.100 63.734 1.00 31.70 ? 26  ASN B CG  1 
ATOM   2220 O  OD1 . ASN B 1 26  ? -6.342  87.991 63.557 1.00 31.37 ? 26  ASN B OD1 1 
ATOM   2221 N  ND2 . ASN B 1 26  ? -8.461  87.306 63.687 1.00 36.47 ? 26  ASN B ND2 1 
ATOM   2222 N  N   . ASN B 1 27  ? -4.613  83.140 63.180 1.00 21.86 ? 27  ASN B N   1 
ATOM   2223 C  CA  . ASN B 1 27  ? -4.192  81.810 63.631 1.00 21.17 ? 27  ASN B CA  1 
ATOM   2224 C  C   . ASN B 1 27  ? -2.978  81.322 62.834 1.00 20.42 ? 27  ASN B C   1 
ATOM   2225 O  O   . ASN B 1 27  ? -2.909  80.134 62.472 1.00 19.57 ? 27  ASN B O   1 
ATOM   2226 C  CB  . ASN B 1 27  ? -5.350  80.856 63.473 1.00 22.36 ? 27  ASN B CB  1 
ATOM   2227 C  CG  . ASN B 1 27  ? -6.481  81.115 64.504 1.00 27.45 ? 27  ASN B CG  1 
ATOM   2228 O  OD1 . ASN B 1 27  ? -7.439  81.834 64.220 1.00 33.00 ? 27  ASN B OD1 1 
ATOM   2229 N  ND2 . ASN B 1 27  ? -6.358  80.553 65.650 1.00 29.97 ? 27  ASN B ND2 1 
ATOM   2230 N  N   . GLN B 1 28  ? -2.022  82.225 62.605 1.00 21.98 ? 28  GLN B N   1 
ATOM   2231 C  CA  . GLN B 1 28  ? -0.827  81.867 61.787 1.00 18.60 ? 28  GLN B CA  1 
ATOM   2232 C  C   . GLN B 1 28  ? 0.290   81.248 62.593 1.00 18.39 ? 28  GLN B C   1 
ATOM   2233 O  O   . GLN B 1 28  ? 0.418   81.468 63.813 1.00 17.42 ? 28  GLN B O   1 
ATOM   2234 C  CB  . GLN B 1 28  ? -0.338  83.086 61.012 1.00 17.79 ? 28  GLN B CB  1 
ATOM   2235 C  CG  . GLN B 1 28  ? -1.328  83.468 59.927 1.00 20.69 ? 28  GLN B CG  1 
ATOM   2236 C  CD  . GLN B 1 28  ? -1.309  82.449 58.806 1.00 18.71 ? 28  GLN B CD  1 
ATOM   2237 O  OE1 . GLN B 1 28  ? -0.292  82.293 58.150 1.00 19.45 ? 28  GLN B OE1 1 
ATOM   2238 N  NE2 . GLN B 1 28  ? -2.401  81.791 58.580 1.00 18.91 ? 28  GLN B NE2 1 
ATOM   2239 N  N   . SER B 1 29  ? 1.027   80.354 61.927 1.00 16.29 ? 29  SER B N   1 
ATOM   2240 C  CA  . SER B 1 29  ? 2.190   79.651 62.538 1.00 15.96 ? 29  SER B CA  1 
ATOM   2241 C  C   . SER B 1 29  ? 3.442   79.912 61.752 1.00 16.62 ? 29  SER B C   1 
ATOM   2242 O  O   . SER B 1 29  ? 3.371   80.183 60.523 1.00 17.02 ? 29  SER B O   1 
ATOM   2243 C  CB  . SER B 1 29  ? 1.872   78.130 62.551 1.00 12.91 ? 29  SER B CB  1 
ATOM   2244 O  OG  . SER B 1 29  ? 0.774   77.856 63.408 1.00 16.29 ? 29  SER B OG  1 
ATOM   2245 N  N   . PRO B 1 30  ? 4.636   79.685 62.362 1.00 16.83 ? 30  PRO B N   1 
ATOM   2246 C  CA  . PRO B 1 30  ? 4.850   79.241 63.779 1.00 15.92 ? 30  PRO B CA  1 
ATOM   2247 C  C   . PRO B 1 30  ? 4.682   80.421 64.738 1.00 17.59 ? 30  PRO B C   1 
ATOM   2248 O  O   . PRO B 1 30  ? 4.425   81.550 64.302 1.00 17.24 ? 30  PRO B O   1 
ATOM   2249 C  CB  . PRO B 1 30  ? 6.338   78.769 63.761 1.00 13.64 ? 30  PRO B CB  1 
ATOM   2250 C  CG  . PRO B 1 30  ? 6.957   79.783 62.799 1.00 16.02 ? 30  PRO B CG  1 
ATOM   2251 C  CD  . PRO B 1 30  ? 5.930   79.914 61.678 1.00 16.59 ? 30  PRO B CD  1 
ATOM   2252 N  N   . VAL B 1 31  ? 4.845   80.122 66.012 1.00 15.76 ? 31  VAL B N   1 
ATOM   2253 C  CA  . VAL B 1 31  ? 4.716   81.100 67.105 1.00 19.15 ? 31  VAL B CA  1 
ATOM   2254 C  C   . VAL B 1 31  ? 5.884   80.920 68.074 1.00 18.00 ? 31  VAL B C   1 
ATOM   2255 O  O   . VAL B 1 31  ? 6.595   79.910 68.075 1.00 15.86 ? 31  VAL B O   1 
ATOM   2256 C  CB  . VAL B 1 31  ? 3.349   81.019 67.858 1.00 17.05 ? 31  VAL B CB  1 
ATOM   2257 C  CG1 . VAL B 1 31  ? 2.146   81.263 66.896 1.00 21.51 ? 31  VAL B CG1 1 
ATOM   2258 C  CG2 . VAL B 1 31  ? 3.202   79.709 68.624 1.00 17.37 ? 31  VAL B CG2 1 
ATOM   2259 N  N   . ASP B 1 32  ? 6.161   81.983 68.838 1.00 19.08 ? 32  ASP B N   1 
ATOM   2260 C  CA  . ASP B 1 32  ? 7.065   81.888 70.015 1.00 20.00 ? 32  ASP B CA  1 
ATOM   2261 C  C   . ASP B 1 32  ? 6.239   81.327 71.135 1.00 18.99 ? 32  ASP B C   1 
ATOM   2262 O  O   . ASP B 1 32  ? 5.078   81.762 71.370 1.00 23.23 ? 32  ASP B O   1 
ATOM   2263 C  CB  . ASP B 1 32  ? 7.558   83.246 70.479 1.00 21.06 ? 32  ASP B CB  1 
ATOM   2264 C  CG  . ASP B 1 32  ? 8.516   83.132 71.650 1.00 22.66 ? 32  ASP B CG  1 
ATOM   2265 O  OD1 . ASP B 1 32  ? 8.251   83.843 72.653 1.00 29.09 ? 32  ASP B OD1 1 
ATOM   2266 O  OD2 . ASP B 1 32  ? 9.503   82.332 71.587 1.00 19.45 ? 32  ASP B OD2 1 
ATOM   2267 N  N   . ILE B 1 33  ? 6.773   80.343 71.843 1.00 18.65 ? 33  ILE B N   1 
ATOM   2268 C  CA  . ILE B 1 33  ? 6.059   79.867 73.031 1.00 15.69 ? 33  ILE B CA  1 
ATOM   2269 C  C   . ILE B 1 33  ? 6.745   80.511 74.221 1.00 17.64 ? 33  ILE B C   1 
ATOM   2270 O  O   . ILE B 1 33  ? 7.889   80.149 74.542 1.00 18.38 ? 33  ILE B O   1 
ATOM   2271 C  CB  . ILE B 1 33  ? 6.220   78.328 73.139 1.00 18.29 ? 33  ILE B CB  1 
ATOM   2272 C  CG1 . ILE B 1 33  ? 5.497   77.763 71.920 1.00 17.35 ? 33  ILE B CG1 1 
ATOM   2273 C  CG2 . ILE B 1 33  ? 5.542   77.751 74.366 1.00 18.65 ? 33  ILE B CG2 1 
ATOM   2274 C  CD1 . ILE B 1 33  ? 5.644   76.262 71.795 1.00 17.13 ? 33  ILE B CD1 1 
ATOM   2275 N  N   . LYS B 1 34  ? 6.021   81.395 74.907 1.00 19.37 ? 34  LYS B N   1 
ATOM   2276 C  CA  . LYS B 1 34  ? 6.570   82.032 76.130 1.00 21.46 ? 34  LYS B CA  1 
ATOM   2277 C  C   . LYS B 1 34  ? 6.105   81.180 77.286 1.00 19.77 ? 34  LYS B C   1 
ATOM   2278 O  O   . LYS B 1 34  ? 4.897   81.177 77.587 1.00 21.46 ? 34  LYS B O   1 
ATOM   2279 C  CB  . LYS B 1 34  ? 6.031   83.456 76.200 1.00 23.14 ? 34  LYS B CB  1 
ATOM   2280 C  CG  . LYS B 1 34  ? 6.803   84.285 77.191 1.00 30.27 ? 34  LYS B CG  1 
ATOM   2281 N  N   . THR B 1 35  ? 7.028   80.468 77.911 1.00 20.27 ? 35  THR B N   1 
ATOM   2282 C  CA  . THR B 1 35  ? 6.639   79.391 78.845 1.00 24.64 ? 35  THR B CA  1 
ATOM   2283 C  C   . THR B 1 35  ? 5.948   79.970 80.090 1.00 25.87 ? 35  THR B C   1 
ATOM   2284 O  O   . THR B 1 35  ? 5.079   79.320 80.637 1.00 25.63 ? 35  THR B O   1 
ATOM   2285 C  CB  . THR B 1 35  ? 7.805   78.484 79.280 1.00 27.41 ? 35  THR B CB  1 
ATOM   2286 O  OG1 . THR B 1 35  ? 8.840   79.316 79.773 1.00 27.31 ? 35  THR B OG1 1 
ATOM   2287 C  CG2 . THR B 1 35  ? 8.394   77.685 78.118 1.00 23.83 ? 35  THR B CG2 1 
ATOM   2288 N  N   . SER B 1 36  ? 6.244   81.218 80.464 1.00 26.89 ? 36  SER B N   1 
ATOM   2289 C  CA  . SER B 1 36  ? 5.514   81.821 81.606 1.00 31.48 ? 36  SER B CA  1 
ATOM   2290 C  C   . SER B 1 36  ? 4.034   82.132 81.339 1.00 32.57 ? 36  SER B C   1 
ATOM   2291 O  O   . SER B 1 36  ? 3.271   82.364 82.284 1.00 31.28 ? 36  SER B O   1 
ATOM   2292 C  CB  . SER B 1 36  ? 6.266   83.054 82.096 1.00 30.45 ? 36  SER B CB  1 
ATOM   2293 O  OG  . SER B 1 36  ? 6.137   84.071 81.145 1.00 31.03 ? 36  SER B OG  1 
ATOM   2294 N  N   . GLU B 1 37  ? 3.624   82.157 80.067 1.00 26.07 ? 37  GLU B N   1 
ATOM   2295 C  CA  . GLU B 1 37  ? 2.225   82.443 79.667 1.00 25.70 ? 37  GLU B CA  1 
ATOM   2296 C  C   . GLU B 1 37  ? 1.435   81.193 79.254 1.00 22.84 ? 37  GLU B C   1 
ATOM   2297 O  O   . GLU B 1 37  ? 0.244   81.314 78.844 1.00 21.35 ? 37  GLU B O   1 
ATOM   2298 C  CB  . GLU B 1 37  ? 2.164   83.435 78.484 1.00 28.88 ? 37  GLU B CB  1 
ATOM   2299 C  CG  . GLU B 1 37  ? 2.957   84.719 78.613 1.00 35.18 ? 37  GLU B CG  1 
ATOM   2300 C  CD  . GLU B 1 37  ? 2.383   85.663 79.619 1.00 46.45 ? 37  GLU B CD  1 
ATOM   2301 O  OE1 . GLU B 1 37  ? 3.100   86.639 79.967 1.00 56.19 ? 37  GLU B OE1 1 
ATOM   2302 O  OE2 . GLU B 1 37  ? 1.231   85.411 80.069 1.00 47.94 ? 37  GLU B OE2 1 
ATOM   2303 N  N   . THR B 1 38  ? 2.102   80.025 79.286 1.00 19.38 ? 38  THR B N   1 
ATOM   2304 C  CA  . THR B 1 38  ? 1.376   78.758 78.940 1.00 21.75 ? 38  THR B CA  1 
ATOM   2305 C  C   . THR B 1 38  ? 0.386   78.398 80.048 1.00 22.70 ? 38  THR B C   1 
ATOM   2306 O  O   . THR B 1 38  ? 0.623   78.743 81.206 1.00 25.25 ? 38  THR B O   1 
ATOM   2307 C  CB  . THR B 1 38  ? 2.319   77.584 78.696 1.00 20.25 ? 38  THR B CB  1 
ATOM   2308 O  OG1 . THR B 1 38  ? 3.105   77.317 79.875 1.00 21.90 ? 38  THR B OG1 1 
ATOM   2309 C  CG2 . THR B 1 38  ? 3.220   77.853 77.500 1.00 17.43 ? 38  THR B CG2 1 
ATOM   2310 N  N   . LYS B 1 39  ? -0.685  77.714 79.700 1.00 19.57 ? 39  LYS B N   1 
ATOM   2311 C  CA  . LYS B 1 39  ? -1.719  77.285 80.672 1.00 22.82 ? 39  LYS B CA  1 
ATOM   2312 C  C   . LYS B 1 39  ? -1.742  75.767 80.714 1.00 23.10 ? 39  LYS B C   1 
ATOM   2313 O  O   . LYS B 1 39  ? -1.764  75.100 79.680 1.00 22.38 ? 39  LYS B O   1 
ATOM   2314 C  CB  . LYS B 1 39  ? -3.099  77.862 80.269 1.00 23.80 ? 39  LYS B CB  1 
ATOM   2315 C  CG  . LYS B 1 39  ? -3.177  79.378 80.197 1.00 26.69 ? 39  LYS B CG  1 
ATOM   2316 C  CD  . LYS B 1 39  ? -2.941  80.001 81.596 1.00 29.00 ? 39  LYS B CD  1 
ATOM   2317 C  CE  . LYS B 1 39  ? -2.803  81.527 81.530 1.00 34.52 ? 39  LYS B CE  1 
ATOM   2318 N  NZ  . LYS B 1 39  ? -2.669  81.992 82.956 1.00 37.54 ? 39  LYS B NZ  1 
ATOM   2319 N  N   . HIS B 1 40  ? -1.691  75.186 81.904 1.00 23.34 ? 40  HIS B N   1 
ATOM   2320 C  CA  . HIS B 1 40  ? -1.938  73.745 82.012 1.00 21.91 ? 40  HIS B CA  1 
ATOM   2321 C  C   . HIS B 1 40  ? -3.410  73.392 81.954 1.00 23.75 ? 40  HIS B C   1 
ATOM   2322 O  O   . HIS B 1 40  ? -4.252  73.817 82.775 1.00 21.39 ? 40  HIS B O   1 
ATOM   2323 C  CB  . HIS B 1 40  ? -1.302  73.175 83.253 1.00 25.44 ? 40  HIS B CB  1 
ATOM   2324 C  CG  . HIS B 1 40  ? -1.580  71.685 83.425 1.00 27.36 ? 40  HIS B CG  1 
ATOM   2325 N  ND1 . HIS B 1 40  ? -1.125  70.728 82.516 1.00 30.74 ? 40  HIS B ND1 1 
ATOM   2326 C  CD2 . HIS B 1 40  ? -2.355  71.004 84.334 1.00 26.44 ? 40  HIS B CD2 1 
ATOM   2327 C  CE1 . HIS B 1 40  ? -1.547  69.505 82.912 1.00 29.93 ? 40  HIS B CE1 1 
ATOM   2328 N  NE2 . HIS B 1 40  ? -2.321  69.676 84.009 1.00 31.90 ? 40  HIS B NE2 1 
ATOM   2329 N  N   . ASP B 1 41  ? -3.764  72.590 80.969 1.00 23.44 ? 41  ASP B N   1 
ATOM   2330 C  CA  . ASP B 1 41  ? -5.146  72.162 80.800 1.00 21.68 ? 41  ASP B CA  1 
ATOM   2331 C  C   . ASP B 1 41  ? -5.233  70.708 81.212 1.00 22.59 ? 41  ASP B C   1 
ATOM   2332 O  O   . ASP B 1 41  ? -4.614  69.816 80.616 1.00 22.30 ? 41  ASP B O   1 
ATOM   2333 C  CB  . ASP B 1 41  ? -5.532  72.448 79.337 1.00 22.97 ? 41  ASP B CB  1 
ATOM   2334 C  CG  . ASP B 1 41  ? -6.922  71.953 78.990 1.00 26.53 ? 41  ASP B CG  1 
ATOM   2335 O  OD1 . ASP B 1 41  ? -7.519  71.229 79.812 1.00 25.27 ? 41  ASP B OD1 1 
ATOM   2336 O  OD2 . ASP B 1 41  ? -7.411  72.288 77.893 1.00 29.76 ? 41  ASP B OD2 1 
ATOM   2337 N  N   . THR B 1 42  ? -6.022  70.430 82.274 1.00 19.32 ? 42  THR B N   1 
ATOM   2338 C  CA  . THR B 1 42  ? -6.101  69.089 82.787 1.00 18.12 ? 42  THR B CA  1 
ATOM   2339 C  C   . THR B 1 42  ? -6.781  68.137 81.791 1.00 19.46 ? 42  THR B C   1 
ATOM   2340 O  O   . THR B 1 42  ? -6.724  66.952 81.998 1.00 20.54 ? 42  THR B O   1 
ATOM   2341 C  CB  . THR B 1 42  ? -6.867  69.021 84.139 1.00 18.49 ? 42  THR B CB  1 
ATOM   2342 O  OG1 . THR B 1 42  ? -8.223  69.404 83.983 1.00 19.51 ? 42  THR B OG1 1 
ATOM   2343 C  CG2 . THR B 1 42  ? -6.149  70.008 85.140 1.00 17.25 ? 42  THR B CG2 1 
ATOM   2344 N  N   . SER B 1 43  ? -7.489  68.661 80.807 1.00 20.81 ? 43  SER B N   1 
ATOM   2345 C  CA  . SER B 1 43  ? -8.231  67.767 79.889 1.00 20.63 ? 43  SER B CA  1 
ATOM   2346 C  C   . SER B 1 43  ? -7.263  67.196 78.823 1.00 22.48 ? 43  SER B C   1 
ATOM   2347 O  O   . SER B 1 43  ? -7.627  66.283 78.081 1.00 23.51 ? 43  SER B O   1 
ATOM   2348 C  CB  . SER B 1 43  ? -9.380  68.530 79.222 1.00 21.36 ? 43  SER B CB  1 
ATOM   2349 O  OG  . SER B 1 43  ? -8.924  69.461 78.285 1.00 23.07 ? 43  SER B OG  1 
ATOM   2350 N  N   . LEU B 1 44  ? -6.037  67.678 78.775 1.00 21.60 ? 44  LEU B N   1 
ATOM   2351 C  CA  . LEU B 1 44  ? -5.066  67.092 77.767 1.00 20.44 ? 44  LEU B CA  1 
ATOM   2352 C  C   . LEU B 1 44  ? -4.544  65.716 78.122 1.00 24.41 ? 44  LEU B C   1 
ATOM   2353 O  O   . LEU B 1 44  ? -3.789  65.534 79.132 1.00 25.80 ? 44  LEU B O   1 
ATOM   2354 C  CB  . LEU B 1 44  ? -3.853  67.977 77.563 1.00 18.75 ? 44  LEU B CB  1 
ATOM   2355 C  CG  . LEU B 1 44  ? -4.087  69.373 77.088 1.00 18.81 ? 44  LEU B CG  1 
ATOM   2356 C  CD1 . LEU B 1 44  ? -2.753  70.123 77.140 1.00 20.43 ? 44  LEU B CD1 1 
ATOM   2357 C  CD2 . LEU B 1 44  ? -4.593  69.295 75.666 1.00 19.76 ? 44  LEU B CD2 1 
ATOM   2358 N  N   . LYS B 1 45  ? -4.833  64.730 77.273 1.00 21.77 ? 45  LYS B N   1 
ATOM   2359 C  CA  . LYS B 1 45  ? -4.281  63.400 77.499 1.00 21.66 ? 45  LYS B CA  1 
ATOM   2360 C  C   . LYS B 1 45  ? -2.863  63.325 76.953 1.00 19.39 ? 45  LYS B C   1 
ATOM   2361 O  O   . LYS B 1 45  ? -2.493  64.171 76.148 1.00 20.98 ? 45  LYS B O   1 
ATOM   2362 C  CB  . LYS B 1 45  ? -5.149  62.376 76.770 1.00 23.30 ? 45  LYS B CB  1 
ATOM   2363 C  CG  . LYS B 1 45  ? -6.519  62.256 77.400 1.00 26.14 ? 45  LYS B CG  1 
ATOM   2364 C  CD  . LYS B 1 45  ? -7.280  61.143 76.709 1.00 28.69 ? 45  LYS B CD  1 
ATOM   2365 C  CE  . LYS B 1 45  ? -8.577  60.902 77.435 1.00 32.89 ? 45  LYS B CE  1 
ATOM   2366 N  NZ  . LYS B 1 45  ? -9.359  59.818 76.771 1.00 33.38 ? 45  LYS B NZ  1 
ATOM   2367 N  N   . PRO B 1 46  ? -2.080  62.355 77.389 1.00 19.50 ? 46  PRO B N   1 
ATOM   2368 C  CA  . PRO B 1 46  ? -0.792  62.150 76.697 1.00 19.48 ? 46  PRO B CA  1 
ATOM   2369 C  C   . PRO B 1 46  ? -1.067  61.881 75.193 1.00 21.59 ? 46  PRO B C   1 
ATOM   2370 O  O   . PRO B 1 46  ? -2.124  61.382 74.854 1.00 20.69 ? 46  PRO B O   1 
ATOM   2371 C  CB  . PRO B 1 46  ? -0.312  60.846 77.260 1.00 22.33 ? 46  PRO B CB  1 
ATOM   2372 C  CG  . PRO B 1 46  ? -1.011  60.706 78.630 1.00 22.44 ? 46  PRO B CG  1 
ATOM   2373 C  CD  . PRO B 1 46  ? -2.375  61.226 78.291 1.00 20.71 ? 46  PRO B CD  1 
ATOM   2374 N  N   . ILE B 1 47  ? -0.116  62.219 74.331 1.00 21.57 ? 47  ILE B N   1 
ATOM   2375 C  CA  . ILE B 1 47  ? -0.235  61.879 72.925 1.00 24.59 ? 47  ILE B CA  1 
ATOM   2376 C  C   . ILE B 1 47  ? 0.254   60.476 72.711 1.00 24.21 ? 47  ILE B C   1 
ATOM   2377 O  O   . ILE B 1 47  ? 1.165   60.040 73.322 1.00 24.03 ? 47  ILE B O   1 
ATOM   2378 C  CB  . ILE B 1 47  ? 0.523   62.834 71.991 1.00 29.48 ? 47  ILE B CB  1 
ATOM   2379 C  CG1 . ILE B 1 47  ? 1.954   62.989 72.397 1.00 31.08 ? 47  ILE B CG1 1 
ATOM   2380 C  CG2 . ILE B 1 47  ? -0.183  64.158 71.779 1.00 29.04 ? 47  ILE B CG2 1 
ATOM   2381 C  CD1 . ILE B 1 47  ? 2.798   63.519 71.276 1.00 35.12 ? 47  ILE B CD1 1 
ATOM   2382 N  N   . SER B 1 48  ? -0.397  59.776 71.817 1.00 23.04 ? 48  SER B N   1 
ATOM   2383 C  CA  . SER B 1 48  ? -0.065  58.375 71.492 1.00 26.39 ? 48  SER B CA  1 
ATOM   2384 C  C   . SER B 1 48  ? 0.205   58.329 69.982 1.00 21.43 ? 48  SER B C   1 
ATOM   2385 O  O   . SER B 1 48  ? -0.614  58.748 69.221 1.00 20.85 ? 48  SER B O   1 
ATOM   2386 C  CB  . SER B 1 48  ? -1.278  57.491 71.829 1.00 30.03 ? 48  SER B CB  1 
ATOM   2387 O  OG  . SER B 1 48  ? -1.197  56.205 71.204 1.00 44.85 ? 48  SER B OG  1 
ATOM   2388 N  N   . VAL B 1 49  ? 1.376   57.867 69.574 1.00 21.46 ? 49  VAL B N   1 
ATOM   2389 C  CA  . VAL B 1 49  ? 1.579   57.662 68.146 1.00 23.59 ? 49  VAL B CA  1 
ATOM   2390 C  C   . VAL B 1 49  ? 1.882   56.202 67.873 1.00 22.43 ? 49  VAL B C   1 
ATOM   2391 O  O   . VAL B 1 49  ? 2.649   55.608 68.576 1.00 25.18 ? 49  VAL B O   1 
ATOM   2392 C  CB  . VAL B 1 49  ? 2.624   58.593 67.542 1.00 26.04 ? 49  VAL B CB  1 
ATOM   2393 C  CG1 . VAL B 1 49  ? 2.237   60.015 67.873 1.00 23.32 ? 49  VAL B CG1 1 
ATOM   2394 C  CG2 . VAL B 1 49  ? 4.034   58.322 68.033 1.00 23.54 ? 49  VAL B CG2 1 
ATOM   2395 N  N   . SER B 1 50  ? 1.272   55.647 66.852 1.00 24.83 ? 50  SER B N   1 
ATOM   2396 C  CA  . SER B 1 50  ? 1.661   54.321 66.434 1.00 25.64 ? 50  SER B CA  1 
ATOM   2397 C  C   . SER B 1 50  ? 1.708   54.289 64.913 1.00 21.70 ? 50  SER B C   1 
ATOM   2398 O  O   . SER B 1 50  ? 0.684   54.278 64.272 1.00 26.52 ? 50  SER B O   1 
ATOM   2399 C  CB  . SER B 1 50  ? 0.610   53.307 66.881 1.00 30.83 ? 50  SER B CB  1 
ATOM   2400 O  OG  . SER B 1 50  ? 1.211   52.008 66.789 1.00 41.17 ? 50  SER B OG  1 
ATOM   2401 N  N   . TYR B 1 51  ? 2.886   54.175 64.394 1.00 24.72 ? 51  TYR B N   1 
ATOM   2402 C  CA  . TYR B 1 51  ? 3.025   54.144 62.984 1.00 23.19 ? 51  TYR B CA  1 
ATOM   2403 C  C   . TYR B 1 51  ? 3.537   52.795 62.517 1.00 25.79 ? 51  TYR B C   1 
ATOM   2404 O  O   . TYR B 1 51  ? 4.550   52.245 63.046 1.00 31.13 ? 51  TYR B O   1 
ATOM   2405 C  CB  . TYR B 1 51  ? 4.045   55.165 62.616 1.00 21.09 ? 51  TYR B CB  1 
ATOM   2406 C  CG  . TYR B 1 51  ? 3.769   56.590 63.093 1.00 18.91 ? 51  TYR B CG  1 
ATOM   2407 C  CD1 . TYR B 1 51  ? 4.857   57.385 63.443 1.00 18.47 ? 51  TYR B CD1 1 
ATOM   2408 C  CD2 . TYR B 1 51  ? 2.495   57.127 63.124 1.00 18.03 ? 51  TYR B CD2 1 
ATOM   2409 C  CE1 . TYR B 1 51  ? 4.674   58.711 63.839 1.00 19.62 ? 51  TYR B CE1 1 
ATOM   2410 C  CE2 . TYR B 1 51  ? 2.273   58.500 63.513 1.00 17.12 ? 51  TYR B CE2 1 
ATOM   2411 C  CZ  . TYR B 1 51  ? 3.400   59.248 63.873 1.00 17.21 ? 51  TYR B CZ  1 
ATOM   2412 O  OH  . TYR B 1 51  ? 3.315   60.561 64.272 1.00 18.30 ? 51  TYR B OH  1 
ATOM   2413 N  N   . ASN B 1 52  ? 2.940   52.362 61.411 1.00 24.87 ? 52  ASN B N   1 
ATOM   2414 C  CA  . ASN B 1 52  ? 3.306   51.090 60.747 1.00 24.71 ? 52  ASN B CA  1 
ATOM   2415 C  C   . ASN B 1 52  ? 4.372   51.403 59.697 1.00 23.61 ? 52  ASN B C   1 
ATOM   2416 O  O   . ASN B 1 52  ? 4.110   52.205 58.785 1.00 22.36 ? 52  ASN B O   1 
ATOM   2417 C  CB  . ASN B 1 52  ? 2.019   50.509 60.149 1.00 25.46 ? 52  ASN B CB  1 
ATOM   2418 C  CG  . ASN B 1 52  ? 2.224   49.099 59.623 1.00 27.38 ? 52  ASN B CG  1 
ATOM   2419 O  OD1 . ASN B 1 52  ? 3.335   48.767 59.241 1.00 29.26 ? 52  ASN B OD1 1 
ATOM   2420 N  ND2 . ASN B 1 52  ? 1.142   48.246 59.681 1.00 29.23 ? 52  ASN B ND2 1 
ATOM   2421 N  N   . PRO B 1 53  ? 5.598   50.903 59.873 1.00 23.19 ? 53  PRO B N   1 
ATOM   2422 C  CA  . PRO B 1 53  ? 6.660   51.304 58.931 1.00 22.77 ? 53  PRO B CA  1 
ATOM   2423 C  C   . PRO B 1 53  ? 6.419   50.883 57.490 1.00 22.42 ? 53  PRO B C   1 
ATOM   2424 O  O   . PRO B 1 53  ? 7.078   51.454 56.606 1.00 21.21 ? 53  PRO B O   1 
ATOM   2425 C  CB  . PRO B 1 53  ? 7.912   50.639 59.456 1.00 25.80 ? 53  PRO B CB  1 
ATOM   2426 C  CG  . PRO B 1 53  ? 7.370   49.452 60.224 1.00 27.66 ? 53  PRO B CG  1 
ATOM   2427 C  CD  . PRO B 1 53  ? 6.105   49.920 60.862 1.00 25.69 ? 53  PRO B CD  1 
ATOM   2428 N  N   . ALA B 1 54  ? 5.489   49.970 57.249 1.00 25.63 ? 54  ALA B N   1 
ATOM   2429 C  CA  . ALA B 1 54  ? 5.133   49.545 55.884 1.00 26.39 ? 54  ALA B CA  1 
ATOM   2430 C  C   . ALA B 1 54  ? 4.301   50.639 55.178 1.00 26.73 ? 54  ALA B C   1 
ATOM   2431 O  O   . ALA B 1 54  ? 3.996   50.483 53.996 1.00 26.45 ? 54  ALA B O   1 
ATOM   2432 C  CB  . ALA B 1 54  ? 4.282   48.263 55.908 1.00 27.29 ? 54  ALA B CB  1 
ATOM   2433 N  N   . THR B 1 55  ? 3.872   51.695 55.896 1.00 23.40 ? 55  THR B N   1 
ATOM   2434 C  CA  . THR B 1 55  ? 3.140   52.761 55.226 1.00 20.00 ? 55  THR B CA  1 
ATOM   2435 C  C   . THR B 1 55  ? 4.126   53.808 54.628 1.00 18.97 ? 55  THR B C   1 
ATOM   2436 O  O   . THR B 1 55  ? 3.630   54.689 53.926 1.00 19.67 ? 55  THR B O   1 
ATOM   2437 C  CB  . THR B 1 55  ? 2.179   53.543 56.152 1.00 22.65 ? 55  THR B CB  1 
ATOM   2438 O  OG1 . THR B 1 55  ? 2.929   53.998 57.290 1.00 20.22 ? 55  THR B OG1 1 
ATOM   2439 C  CG2 . THR B 1 55  ? 0.896   52.712 56.503 1.00 24.28 ? 55  THR B CG2 1 
ATOM   2440 N  N   . ALA B 1 56  ? 5.438   53.740 54.882 1.00 20.07 ? 56  ALA B N   1 
ATOM   2441 C  CA  . ALA B 1 56  ? 6.382   54.664 54.283 1.00 19.78 ? 56  ALA B CA  1 
ATOM   2442 C  C   . ALA B 1 56  ? 6.371   54.426 52.769 1.00 22.87 ? 56  ALA B C   1 
ATOM   2443 O  O   . ALA B 1 56  ? 6.364   53.251 52.349 1.00 19.79 ? 56  ALA B O   1 
ATOM   2444 C  CB  . ALA B 1 56  ? 7.768   54.515 54.853 1.00 19.55 ? 56  ALA B CB  1 
ATOM   2445 N  N   . LYS B 1 57  ? 6.272   55.507 51.981 1.00 19.59 ? 57  LYS B N   1 
ATOM   2446 C  CA  . LYS B 1 57  ? 6.064   55.360 50.520 1.00 19.39 ? 57  LYS B CA  1 
ATOM   2447 C  C   . LYS B 1 57  ? 7.177   55.971 49.670 1.00 21.56 ? 57  LYS B C   1 
ATOM   2448 O  O   . LYS B 1 57  ? 7.789   55.261 48.818 1.00 19.31 ? 57  LYS B O   1 
ATOM   2449 C  CB  . LYS B 1 57  ? 4.640   55.792 50.122 1.00 20.56 ? 57  LYS B CB  1 
ATOM   2450 C  CG  . LYS B 1 57  ? 4.307   55.587 48.607 1.00 28.37 ? 57  LYS B CG  1 
ATOM   2451 C  CD  . LYS B 1 57  ? 2.980   56.223 48.122 1.00 34.59 ? 57  LYS B CD  1 
ATOM   2452 C  CE  . LYS B 1 57  ? 2.860   57.731 48.430 1.00 41.25 ? 57  LYS B CE  1 
ATOM   2453 N  NZ  . LYS B 1 57  ? 3.301   58.775 47.410 1.00 41.24 ? 57  LYS B NZ  1 
ATOM   2454 N  N   . GLU B 1 58  ? 7.412   57.284 49.816 1.00 19.53 ? 58  GLU B N   1 
ATOM   2455 C  CA  . GLU B 1 58  ? 8.150   58.014 48.763 1.00 18.96 ? 58  GLU B CA  1 
ATOM   2456 C  C   . GLU B 1 58  ? 8.843   59.193 49.399 1.00 18.45 ? 58  GLU B C   1 
ATOM   2457 O  O   . GLU B 1 58  ? 8.292   59.779 50.334 1.00 19.79 ? 58  GLU B O   1 
ATOM   2458 C  CB  . GLU B 1 58  ? 7.111   58.521 47.723 1.00 22.14 ? 58  GLU B CB  1 
ATOM   2459 C  CG  . GLU B 1 58  ? 7.707   59.294 46.571 1.00 29.98 ? 58  GLU B CG  1 
ATOM   2460 C  CD  . GLU B 1 58  ? 6.675   59.452 45.475 1.00 30.88 ? 58  GLU B CD  1 
ATOM   2461 O  OE1 . GLU B 1 58  ? 7.016   59.090 44.341 1.00 36.03 ? 58  GLU B OE1 1 
ATOM   2462 O  OE2 . GLU B 1 58  ? 5.541   59.918 45.785 1.00 34.19 ? 58  GLU B OE2 1 
ATOM   2463 N  N   . ILE B 1 59  ? 10.015  59.539 48.907 1.00 15.77 ? 59  ILE B N   1 
ATOM   2464 C  CA  . ILE B 1 59  ? 10.708  60.779 49.276 1.00 15.60 ? 59  ILE B CA  1 
ATOM   2465 C  C   . ILE B 1 59  ? 10.745  61.672 48.023 1.00 18.17 ? 59  ILE B C   1 
ATOM   2466 O  O   . ILE B 1 59  ? 10.946  61.187 46.886 1.00 19.82 ? 59  ILE B O   1 
ATOM   2467 C  CB  . ILE B 1 59  ? 12.098  60.514 49.923 1.00 16.34 ? 59  ILE B CB  1 
ATOM   2468 C  CG1 . ILE B 1 59  ? 12.730  61.751 50.563 1.00 15.87 ? 59  ILE B CG1 1 
ATOM   2469 C  CG2 . ILE B 1 59  ? 13.052  59.823 48.920 1.00 15.70 ? 59  ILE B CG2 1 
ATOM   2470 C  CD1 . ILE B 1 59  ? 13.968  61.366 51.389 1.00 17.60 ? 59  ILE B CD1 1 
ATOM   2471 N  N   . ILE B 1 60  ? 10.524  62.975 48.203 1.00 16.99 ? 60  ILE B N   1 
ATOM   2472 C  CA  . ILE B 1 60  ? 10.351  63.844 47.014 1.00 17.19 ? 60  ILE B CA  1 
ATOM   2473 C  C   . ILE B 1 60  ? 10.978  65.186 47.299 1.00 17.99 ? 60  ILE B C   1 
ATOM   2474 O  O   . ILE B 1 60  ? 10.827  65.729 48.430 1.00 15.52 ? 60  ILE B O   1 
ATOM   2475 C  CB  . ILE B 1 60  ? 8.875   63.992 46.598 1.00 18.85 ? 60  ILE B CB  1 
ATOM   2476 C  CG1 . ILE B 1 60  ? 8.739   64.889 45.330 1.00 18.33 ? 60  ILE B CG1 1 
ATOM   2477 C  CG2 . ILE B 1 60  ? 8.078   64.567 47.723 1.00 20.54 ? 60  ILE B CG2 1 
ATOM   2478 C  CD1 . ILE B 1 60  ? 7.379   64.924 44.702 1.00 25.11 ? 60  ILE B CD1 1 
ATOM   2479 N  N   . ASN B 1 61  ? 11.721  65.729 46.321 1.00 15.75 ? 61  ASN B N   1 
ATOM   2480 C  CA  . ASN B 1 61  ? 12.218  67.096 46.406 1.00 16.11 ? 61  ASN B CA  1 
ATOM   2481 C  C   . ASN B 1 61  ? 11.169  68.041 45.848 1.00 17.45 ? 61  ASN B C   1 
ATOM   2482 O  O   . ASN B 1 61  ? 10.767  67.879 44.688 1.00 18.16 ? 61  ASN B O   1 
ATOM   2483 C  CB  . ASN B 1 61  ? 13.508  67.188 45.517 1.00 17.29 ? 61  ASN B CB  1 
ATOM   2484 C  CG  . ASN B 1 61  ? 14.127  68.571 45.528 1.00 16.80 ? 61  ASN B CG  1 
ATOM   2485 O  OD1 . ASN B 1 61  ? 13.440  69.567 45.528 1.00 18.77 ? 61  ASN B OD1 1 
ATOM   2486 N  ND2 . ASN B 1 61  ? 15.472  68.640 45.492 1.00 19.22 ? 61  ASN B ND2 1 
ATOM   2487 N  N   . VAL B 1 62  ? 10.669  68.952 46.688 1.00 16.15 ? 62  VAL B N   1 
ATOM   2488 C  CA  . VAL B 1 62  ? 9.615   69.917 46.320 1.00 16.54 ? 62  VAL B CA  1 
ATOM   2489 C  C   . VAL B 1 62  ? 10.116  71.324 46.065 1.00 16.11 ? 62  VAL B C   1 
ATOM   2490 O  O   . VAL B 1 62  ? 9.354   72.278 46.096 1.00 18.88 ? 62  VAL B O   1 
ATOM   2491 C  CB  . VAL B 1 62  ? 8.427   69.880 47.335 1.00 17.06 ? 62  VAL B CB  1 
ATOM   2492 C  CG1 . VAL B 1 62  ? 7.881   68.482 47.329 1.00 17.66 ? 62  VAL B CG1 1 
ATOM   2493 C  CG2 . VAL B 1 62  ? 8.818   70.343 48.715 1.00 18.68 ? 62  VAL B CG2 1 
ATOM   2494 N  N   . GLY B 1 63  ? 11.419  71.464 45.855 1.00 16.49 ? 63  GLY B N   1 
ATOM   2495 C  CA  . GLY B 1 63  ? 11.950  72.815 45.488 1.00 17.11 ? 63  GLY B CA  1 
ATOM   2496 C  C   . GLY B 1 63  ? 12.435  73.642 46.622 1.00 18.46 ? 63  GLY B C   1 
ATOM   2497 O  O   . GLY B 1 63  ? 13.620  74.026 46.643 1.00 20.89 ? 63  GLY B O   1 
ATOM   2498 N  N   . HIS B 1 64  ? 11.549  73.899 47.610 1.00 15.18 ? 64  HIS B N   1 
ATOM   2499 C  CA  . HIS B 1 64  ? 11.925  74.632 48.795 1.00 16.28 ? 64  HIS B CA  1 
ATOM   2500 C  C   . HIS B 1 64  ? 12.269  73.691 49.947 1.00 15.87 ? 64  HIS B C   1 
ATOM   2501 O  O   . HIS B 1 64  ? 12.752  74.186 51.002 1.00 16.67 ? 64  HIS B O   1 
ATOM   2502 C  CB  . HIS B 1 64  ? 10.712  75.497 49.202 1.00 16.84 ? 64  HIS B CB  1 
ATOM   2503 C  CG  . HIS B 1 64  ? 9.463   74.695 49.446 1.00 17.72 ? 64  HIS B CG  1 
ATOM   2504 N  ND1 . HIS B 1 64  ? 9.095   74.254 50.722 1.00 20.16 ? 64  HIS B ND1 1 
ATOM   2505 C  CD2 . HIS B 1 64  ? 8.484   74.258 48.577 1.00 19.02 ? 64  HIS B CD2 1 
ATOM   2506 C  CE1 . HIS B 1 64  ? 7.925   73.579 50.617 1.00 21.69 ? 64  HIS B CE1 1 
ATOM   2507 N  NE2 . HIS B 1 64  ? 7.562   73.566 49.303 1.00 20.94 ? 64  HIS B NE2 1 
ATOM   2508 N  N   . SER B 1 65  ? 12.009  72.404 49.791 1.00 16.03 ? 65  SER B N   1 
ATOM   2509 C  CA  . SER B 1 65  ? 12.286  71.445 50.869 1.00 15.24 ? 65  SER B CA  1 
ATOM   2510 C  C   . SER B 1 65  ? 12.190  70.035 50.299 1.00 17.26 ? 65  SER B C   1 
ATOM   2511 O  O   . SER B 1 65  ? 12.116  69.843 49.072 1.00 15.51 ? 65  SER B O   1 
ATOM   2512 C  CB  . SER B 1 65  ? 11.216  71.673 51.968 1.00 18.68 ? 65  SER B CB  1 
ATOM   2513 O  OG  . SER B 1 65  ? 11.513  70.885 53.100 1.00 20.77 ? 65  SER B OG  1 
ATOM   2514 N  N   . PHE B 1 66  ? 12.123  69.016 51.170 1.00 14.75 ? 66  PHE B N   1 
ATOM   2515 C  CA  . PHE B 1 66  ? 11.843  67.689 50.696 1.00 14.61 ? 66  PHE B CA  1 
ATOM   2516 C  C   . PHE B 1 66  ? 10.864  67.078 51.694 1.00 15.95 ? 66  PHE B C   1 
ATOM   2517 O  O   . PHE B 1 66  ? 10.829  67.521 52.836 1.00 16.17 ? 66  PHE B O   1 
ATOM   2518 C  CB  . PHE B 1 66  ? 13.080  66.796 50.555 1.00 15.21 ? 66  PHE B CB  1 
ATOM   2519 C  CG  . PHE B 1 66  ? 13.696  66.398 51.884 1.00 14.91 ? 66  PHE B CG  1 
ATOM   2520 C  CD1 . PHE B 1 66  ? 13.309  65.159 52.468 1.00 17.08 ? 66  PHE B CD1 1 
ATOM   2521 C  CD2 . PHE B 1 66  ? 14.615  67.253 52.516 1.00 18.15 ? 66  PHE B CD2 1 
ATOM   2522 C  CE1 . PHE B 1 66  ? 13.846  64.774 53.702 1.00 16.94 ? 66  PHE B CE1 1 
ATOM   2523 C  CE2 . PHE B 1 66  ? 15.165  66.873 53.753 1.00 18.39 ? 66  PHE B CE2 1 
ATOM   2524 C  CZ  . PHE B 1 66  ? 14.751  65.646 54.335 1.00 15.99 ? 66  PHE B CZ  1 
ATOM   2525 N  N   A HIS B 1 67  ? 10.074  66.104 51.217 0.50 14.33 ? 67  HIS B N   1 
ATOM   2526 N  N   B HIS B 1 67  ? 10.088  66.093 51.282 0.50 14.79 ? 67  HIS B N   1 
ATOM   2527 C  CA  A HIS B 1 67  ? 8.992   65.445 51.976 0.50 15.25 ? 67  HIS B CA  1 
ATOM   2528 C  CA  B HIS B 1 67  ? 9.290   65.426 52.291 0.50 15.54 ? 67  HIS B CA  1 
ATOM   2529 C  C   A HIS B 1 67  ? 9.189   63.936 51.988 0.50 15.01 ? 67  HIS B C   1 
ATOM   2530 C  C   B HIS B 1 67  ? 9.142   63.971 52.024 0.50 15.23 ? 67  HIS B C   1 
ATOM   2531 O  O   A HIS B 1 67  ? 9.697   63.380 50.979 0.50 13.55 ? 67  HIS B O   1 
ATOM   2532 O  O   B HIS B 1 67  ? 9.345   63.488 50.883 0.50 13.45 ? 67  HIS B O   1 
ATOM   2533 C  CB  A HIS B 1 67  ? 7.630   65.805 51.332 0.50 14.68 ? 67  HIS B CB  1 
ATOM   2534 C  CB  B HIS B 1 67  ? 7.938   66.128 52.513 0.50 16.62 ? 67  HIS B CB  1 
ATOM   2535 C  CG  A HIS B 1 67  ? 7.245   67.274 51.515 0.50 15.70 ? 67  HIS B CG  1 
ATOM   2536 C  CG  B HIS B 1 67  ? 7.004   66.180 51.285 0.50 17.53 ? 67  HIS B CG  1 
ATOM   2537 N  ND1 A HIS B 1 67  ? 6.293   67.889 50.767 0.50 15.69 ? 67  HIS B ND1 1 
ATOM   2538 N  ND1 B HIS B 1 67  ? 6.459   67.339 50.860 0.50 19.16 ? 67  HIS B ND1 1 
ATOM   2539 C  CD2 A HIS B 1 67  ? 7.702   68.224 52.411 0.50 15.10 ? 67  HIS B CD2 1 
ATOM   2540 C  CD2 B HIS B 1 67  ? 6.468   65.199 50.481 0.50 18.28 ? 67  HIS B CD2 1 
ATOM   2541 C  CE1 A HIS B 1 67  ? 6.182   69.175 51.124 0.50 15.07 ? 67  HIS B CE1 1 
ATOM   2542 C  CE1 B HIS B 1 67  ? 5.626   67.119 49.816 0.50 19.34 ? 67  HIS B CE1 1 
ATOM   2543 N  NE2 A HIS B 1 67  ? 7.005   69.385 52.172 0.50 15.41 ? 67  HIS B NE2 1 
ATOM   2544 N  NE2 B HIS B 1 67  ? 5.612   65.833 49.566 0.50 18.17 ? 67  HIS B NE2 1 
ATOM   2545 N  N   . VAL B 1 68  ? 8.840   63.237 53.095 1.00 13.72 ? 68  VAL B N   1 
ATOM   2546 C  CA  . VAL B 1 68  ? 8.714   61.778 53.020 1.00 14.12 ? 68  VAL B CA  1 
ATOM   2547 C  C   . VAL B 1 68  ? 7.221   61.502 53.203 1.00 16.07 ? 68  VAL B C   1 
ATOM   2548 O  O   . VAL B 1 68  ? 6.619   61.920 54.219 1.00 15.45 ? 68  VAL B O   1 
ATOM   2549 C  CB  . VAL B 1 68  ? 9.495   61.019 54.096 1.00 15.63 ? 68  VAL B CB  1 
ATOM   2550 C  CG1 . VAL B 1 68  ? 9.107   59.560 54.080 1.00 15.98 ? 68  VAL B CG1 1 
ATOM   2551 C  CG2 . VAL B 1 68  ? 10.969  61.255 53.966 1.00 16.33 ? 68  VAL B CG2 1 
ATOM   2552 N  N   . ASN B 1 69  ? 6.584   60.929 52.181 1.00 16.40 ? 69  ASN B N   1 
ATOM   2553 C  CA  . ASN B 1 69  ? 5.153   60.710 52.200 1.00 15.77 ? 69  ASN B CA  1 
ATOM   2554 C  C   . ASN B 1 69  ? 4.800   59.271 52.574 1.00 15.56 ? 69  ASN B C   1 
ATOM   2555 O  O   . ASN B 1 69  ? 5.585   58.356 52.282 1.00 17.81 ? 69  ASN B O   1 
ATOM   2556 C  CB  . ASN B 1 69  ? 4.578   60.996 50.786 1.00 18.61 ? 69  ASN B CB  1 
ATOM   2557 C  CG  . ASN B 1 69  ? 4.486   62.469 50.530 1.00 20.50 ? 69  ASN B CG  1 
ATOM   2558 O  OD1 . ASN B 1 69  ? 4.419   63.264 51.487 1.00 25.67 ? 69  ASN B OD1 1 
ATOM   2559 N  ND2 . ASN B 1 69  ? 4.487   62.859 49.230 1.00 27.23 ? 69  ASN B ND2 1 
ATOM   2560 N  N   . PHE B 1 70  ? 3.646   59.104 53.220 1.00 15.67 ? 70  PHE B N   1 
ATOM   2561 C  CA  . PHE B 1 70  ? 3.165   57.774 53.658 1.00 17.00 ? 70  PHE B CA  1 
ATOM   2562 C  C   . PHE B 1 70  ? 1.879   57.408 52.986 1.00 19.76 ? 70  PHE B C   1 
ATOM   2563 O  O   . PHE B 1 70  ? 1.075   58.284 52.636 1.00 19.13 ? 70  PHE B O   1 
ATOM   2564 C  CB  . PHE B 1 70  ? 3.033   57.739 55.180 1.00 16.53 ? 70  PHE B CB  1 
ATOM   2565 C  CG  . PHE B 1 70  ? 4.347   57.882 55.895 1.00 16.54 ? 70  PHE B CG  1 
ATOM   2566 C  CD1 . PHE B 1 70  ? 4.919   56.801 56.537 1.00 16.08 ? 70  PHE B CD1 1 
ATOM   2567 C  CD2 . PHE B 1 70  ? 5.018   59.096 55.906 1.00 15.63 ? 70  PHE B CD2 1 
ATOM   2568 C  CE1 . PHE B 1 70  ? 6.133   56.926 57.187 1.00 16.93 ? 70  PHE B CE1 1 
ATOM   2569 C  CE2 . PHE B 1 70  ? 6.234   59.226 56.553 1.00 15.55 ? 70  PHE B CE2 1 
ATOM   2570 C  CZ  . PHE B 1 70  ? 6.794   58.140 57.192 1.00 17.39 ? 70  PHE B CZ  1 
ATOM   2571 N  N   . GLU B 1 71  ? 1.614   56.098 52.804 1.00 17.51 ? 71  GLU B N   1 
ATOM   2572 C  CA  . GLU B 1 71  ? 0.303   55.790 52.252 1.00 21.38 ? 71  GLU B CA  1 
ATOM   2573 C  C   . GLU B 1 71  ? -0.661  56.084 53.338 1.00 24.01 ? 71  GLU B C   1 
ATOM   2574 O  O   . GLU B 1 71  ? -0.370  55.772 54.495 1.00 26.21 ? 71  GLU B O   1 
ATOM   2575 C  CB  . GLU B 1 71  ? 0.199   54.299 51.900 1.00 26.97 ? 71  GLU B CB  1 
ATOM   2576 C  CG  . GLU B 1 71  ? 1.496   53.701 51.365 1.00 32.63 ? 71  GLU B CG  1 
ATOM   2577 C  CD  . GLU B 1 71  ? 1.329   52.282 50.819 1.00 43.25 ? 71  GLU B CD  1 
ATOM   2578 O  OE1 . GLU B 1 71  ? 0.525   51.493 51.382 1.00 48.97 ? 71  GLU B OE1 1 
ATOM   2579 O  OE2 . GLU B 1 71  ? 1.994   51.960 49.816 1.00 49.50 ? 71  GLU B OE2 1 
ATOM   2580 N  N   . ASP B 1 72  ? -1.792  56.621 52.969 1.00 26.06 ? 72  ASP B N   1 
ATOM   2581 C  CA  . ASP B 1 72  ? -2.748  57.144 53.926 1.00 27.42 ? 72  ASP B CA  1 
ATOM   2582 C  C   . ASP B 1 72  ? -4.184  56.729 53.565 1.00 31.19 ? 72  ASP B C   1 
ATOM   2583 O  O   . ASP B 1 72  ? -5.186  57.430 53.880 1.00 31.20 ? 72  ASP B O   1 
ATOM   2584 C  CB  . ASP B 1 72  ? -2.572  58.678 54.023 1.00 26.53 ? 72  ASP B CB  1 
ATOM   2585 C  CG  . ASP B 1 72  ? -3.017  59.399 52.765 1.00 32.88 ? 72  ASP B CG  1 
ATOM   2586 O  OD1 . ASP B 1 72  ? -3.381  60.577 52.815 1.00 33.45 ? 72  ASP B OD1 1 
ATOM   2587 O  OD2 . ASP B 1 72  ? -2.997  58.767 51.694 1.00 32.79 ? 72  ASP B OD2 1 
ATOM   2588 N  N   . ASN B 1 73  ? -4.266  55.531 52.970 1.00 27.41 ? 73  ASN B N   1 
ATOM   2589 C  CA  . ASN B 1 73  ? -5.522  54.940 52.482 1.00 33.50 ? 73  ASN B CA  1 
ATOM   2590 C  C   . ASN B 1 73  ? -6.307  54.273 53.622 1.00 33.48 ? 73  ASN B C   1 
ATOM   2591 O  O   . ASN B 1 73  ? -7.490  53.922 53.447 1.00 34.41 ? 73  ASN B O   1 
ATOM   2592 C  CB  . ASN B 1 73  ? -5.246  53.912 51.362 1.00 32.86 ? 73  ASN B CB  1 
ATOM   2593 C  CG  . ASN B 1 73  ? -4.117  52.945 51.709 1.00 40.19 ? 73  ASN B CG  1 
ATOM   2594 O  OD1 . ASN B 1 73  ? -2.931  53.326 51.765 1.00 49.20 ? 73  ASN B OD1 1 
ATOM   2595 N  ND2 . ASN B 1 73  ? -4.462  51.673 51.889 1.00 44.82 ? 73  ASN B ND2 1 
ATOM   2596 N  N   . ASP B 1 74  ? -5.648  54.111 54.774 1.00 29.82 ? 74  ASP B N   1 
ATOM   2597 C  CA  . ASP B 1 74  ? -6.257  53.502 55.949 1.00 34.21 ? 74  ASP B CA  1 
ATOM   2598 C  C   . ASP B 1 74  ? -5.576  54.005 57.282 1.00 32.46 ? 74  ASP B C   1 
ATOM   2599 O  O   . ASP B 1 74  ? -4.633  54.798 57.240 1.00 29.77 ? 74  ASP B O   1 
ATOM   2600 C  CB  . ASP B 1 74  ? -6.302  51.972 55.851 1.00 33.62 ? 74  ASP B CB  1 
ATOM   2601 C  CG  . ASP B 1 74  ? -4.947  51.326 56.047 1.00 39.39 ? 74  ASP B CG  1 
ATOM   2602 O  OD1 . ASP B 1 74  ? -4.010  52.016 56.499 1.00 32.17 ? 74  ASP B OD1 1 
ATOM   2603 O  OD2 . ASP B 1 74  ? -4.824  50.118 55.751 1.00 44.49 ? 74  ASP B OD2 1 
ATOM   2604 N  N   . ASN B 1 75  ? -6.051  53.542 58.425 1.00 31.88 ? 75  ASN B N   1 
ATOM   2605 C  CA  . ASN B 1 75  ? -5.454  53.938 59.720 1.00 32.78 ? 75  ASN B CA  1 
ATOM   2606 C  C   . ASN B 1 75  ? -4.396  53.000 60.291 1.00 35.96 ? 75  ASN B C   1 
ATOM   2607 O  O   . ASN B 1 75  ? -4.291  52.793 61.539 1.00 27.91 ? 75  ASN B O   1 
ATOM   2608 C  CB  . ASN B 1 75  ? -6.552  54.251 60.773 1.00 39.32 ? 75  ASN B CB  1 
ATOM   2609 C  CG  . ASN B 1 75  ? -7.517  55.298 60.303 1.00 36.94 ? 75  ASN B CG  1 
ATOM   2610 O  OD1 . ASN B 1 75  ? -7.132  56.396 59.958 1.00 43.37 ? 75  ASN B OD1 1 
ATOM   2611 N  ND2 . ASN B 1 75  ? -8.790  54.951 60.243 1.00 47.16 ? 75  ASN B ND2 1 
ATOM   2612 N  N   . ARG B 1 76  ? -3.479  52.537 59.427 1.00 24.44 ? 76  ARG B N   1 
ATOM   2613 C  CA  . ARG B 1 76  ? -2.349  51.840 59.965 1.00 24.25 ? 76  ARG B CA  1 
ATOM   2614 C  C   . ARG B 1 76  ? -1.459  52.712 60.830 1.00 26.29 ? 76  ARG B C   1 
ATOM   2615 O  O   . ARG B 1 76  ? -0.785  52.187 61.702 1.00 25.89 ? 76  ARG B O   1 
ATOM   2616 C  CB  . ARG B 1 76  ? -1.474  51.130 58.900 1.00 26.97 ? 76  ARG B CB  1 
ATOM   2617 C  CG  . ARG B 1 76  ? -2.180  49.830 58.380 1.00 29.59 ? 76  ARG B CG  1 
ATOM   2618 C  CD  . ARG B 1 76  ? -1.509  49.277 57.106 1.00 29.72 ? 76  ARG B CD  1 
ATOM   2619 N  NE  . ARG B 1 76  ? -1.692  50.168 55.954 1.00 29.17 ? 76  ARG B NE  1 
ATOM   2620 C  CZ  . ARG B 1 76  ? -0.905  50.164 54.861 1.00 29.63 ? 76  ARG B CZ  1 
ATOM   2621 N  NH1 . ARG B 1 76  ? 0.124   49.333 54.784 1.00 31.51 ? 76  ARG B NH1 1 
ATOM   2622 N  NH2 . ARG B 1 76  ? -1.134  51.015 53.871 1.00 30.91 ? 76  ARG B NH2 1 
ATOM   2623 N  N   . SER B 1 77  ? -1.433  54.039 60.553 1.00 26.62 ? 77  SER B N   1 
ATOM   2624 C  CA  . SER B 1 77  ? -0.375  54.879 61.123 1.00 21.17 ? 77  SER B CA  1 
ATOM   2625 C  C   . SER B 1 77  ? -1.128  56.137 61.637 1.00 20.34 ? 77  SER B C   1 
ATOM   2626 O  O   . SER B 1 77  ? -1.651  56.947 60.855 1.00 19.35 ? 77  SER B O   1 
ATOM   2627 C  CB  . SER B 1 77  ? 0.646   55.292 60.037 1.00 20.10 ? 77  SER B CB  1 
ATOM   2628 O  OG  . SER B 1 77  ? 1.504   54.191 59.745 1.00 20.09 ? 77  SER B OG  1 
ATOM   2629 N  N   . VAL B 1 78  ? -1.275  56.227 62.979 1.00 21.92 ? 78  VAL B N   1 
ATOM   2630 C  CA  . VAL B 1 78  ? -2.191  57.231 63.493 1.00 19.72 ? 78  VAL B CA  1 
ATOM   2631 C  C   . VAL B 1 78  ? -1.626  57.932 64.727 1.00 19.02 ? 78  VAL B C   1 
ATOM   2632 O  O   . VAL B 1 78  ? -0.827  57.346 65.447 1.00 20.02 ? 78  VAL B O   1 
ATOM   2633 C  CB  . VAL B 1 78  ? -3.625  56.757 63.843 1.00 22.07 ? 78  VAL B CB  1 
ATOM   2634 C  CG1 . VAL B 1 78  ? -4.484  56.469 62.591 1.00 25.13 ? 78  VAL B CG1 1 
ATOM   2635 C  CG2 . VAL B 1 78  ? -3.580  55.578 64.787 1.00 25.25 ? 78  VAL B CG2 1 
ATOM   2636 N  N   . LEU B 1 79  ? -2.037  59.209 64.893 1.00 17.40 ? 79  LEU B N   1 
ATOM   2637 C  CA  . LEU B 1 79  ? -1.827  59.984 66.134 1.00 17.28 ? 79  LEU B CA  1 
ATOM   2638 C  C   . LEU B 1 79  ? -3.151  60.078 66.915 1.00 17.83 ? 79  LEU B C   1 
ATOM   2639 O  O   . LEU B 1 79  ? -4.207  60.439 66.365 1.00 17.97 ? 79  LEU B O   1 
ATOM   2640 C  CB  . LEU B 1 79  ? -1.391  61.438 65.715 1.00 17.80 ? 79  LEU B CB  1 
ATOM   2641 C  CG  . LEU B 1 79  ? -1.431  62.515 66.809 1.00 17.48 ? 79  LEU B CG  1 
ATOM   2642 C  CD1 . LEU B 1 79  ? -0.481  62.171 67.939 1.00 20.72 ? 79  LEU B CD1 1 
ATOM   2643 C  CD2 . LEU B 1 79  ? -1.098  63.870 66.204 1.00 17.34 ? 79  LEU B CD2 1 
ATOM   2644 N  N   . LYS B 1 80  ? -3.115  59.794 68.213 1.00 19.05 ? 80  LYS B N   1 
ATOM   2645 C  CA  . LYS B 1 80  ? -4.371  59.987 69.002 1.00 21.15 ? 80  LYS B CA  1 
ATOM   2646 C  C   . LYS B 1 80  ? -3.975  60.677 70.296 1.00 19.62 ? 80  LYS B C   1 
ATOM   2647 O  O   . LYS B 1 80  ? -2.799  60.833 70.614 1.00 18.00 ? 80  LYS B O   1 
ATOM   2648 C  CB  . LYS B 1 80  ? -4.985  58.672 69.464 1.00 26.22 ? 80  LYS B CB  1 
ATOM   2649 C  CG  . LYS B 1 80  ? -4.911  57.526 68.489 1.00 35.03 ? 80  LYS B CG  1 
ATOM   2650 C  CD  . LYS B 1 80  ? -5.945  56.435 68.797 1.00 42.87 ? 80  LYS B CD  1 
ATOM   2651 C  CE  . LYS B 1 80  ? -5.858  55.881 70.218 1.00 45.74 ? 80  LYS B CE  1 
ATOM   2652 N  NZ  . LYS B 1 80  ? -4.553  55.206 70.453 1.00 53.56 ? 80  LYS B NZ  1 
ATOM   2653 N  N   . GLY B 1 81  ? -4.984  61.017 71.092 1.00 19.20 ? 81  GLY B N   1 
ATOM   2654 C  CA  . GLY B 1 81  ? -4.664  61.599 72.438 1.00 19.70 ? 81  GLY B CA  1 
ATOM   2655 C  C   . GLY B 1 81  ? -4.445  63.108 72.462 1.00 18.76 ? 81  GLY B C   1 
ATOM   2656 O  O   . GLY B 1 81  ? -4.881  63.815 71.574 1.00 18.19 ? 81  GLY B O   1 
ATOM   2657 N  N   . GLY B 1 82  ? -3.656  63.584 73.427 1.00 19.24 ? 82  GLY B N   1 
ATOM   2658 C  CA  . GLY B 1 82  ? -3.396  65.019 73.530 1.00 18.93 ? 82  GLY B CA  1 
ATOM   2659 C  C   . GLY B 1 82  ? -4.703  65.784 73.537 1.00 21.17 ? 82  GLY B C   1 
ATOM   2660 O  O   . GLY B 1 82  ? -5.639  65.439 74.320 1.00 22.87 ? 82  GLY B O   1 
ATOM   2661 N  N   . PRO B 1 83  ? -4.834  66.787 72.668 1.00 20.29 ? 83  PRO B N   1 
ATOM   2662 C  CA  . PRO B 1 83  ? -6.066  67.636 72.671 1.00 22.56 ? 83  PRO B CA  1 
ATOM   2663 C  C   . PRO B 1 83  ? -7.175  67.047 71.818 1.00 22.08 ? 83  PRO B C   1 
ATOM   2664 O  O   . PRO B 1 83  ? -8.224  67.649 71.716 1.00 23.63 ? 83  PRO B O   1 
ATOM   2665 C  CB  . PRO B 1 83  ? -5.637  68.953 72.032 1.00 25.07 ? 83  PRO B CB  1 
ATOM   2666 C  CG  . PRO B 1 83  ? -4.536  68.539 71.134 1.00 22.67 ? 83  PRO B CG  1 
ATOM   2667 C  CD  . PRO B 1 83  ? -3.838  67.301 71.719 1.00 23.11 ? 83  PRO B CD  1 
ATOM   2668 N  N   . PHE B 1 84  ? -6.952  65.878 71.215 1.00 21.50 ? 84  PHE B N   1 
ATOM   2669 C  CA  . PHE B 1 84  ? -7.903  65.345 70.212 1.00 21.90 ? 84  PHE B CA  1 
ATOM   2670 C  C   . PHE B 1 84  ? -8.855  64.293 70.768 1.00 25.04 ? 84  PHE B C   1 
ATOM   2671 O  O   . PHE B 1 84  ? -8.455  63.443 71.585 1.00 25.80 ? 84  PHE B O   1 
ATOM   2672 C  CB  . PHE B 1 84  ? -7.090  64.592 69.111 1.00 22.12 ? 84  PHE B CB  1 
ATOM   2673 C  CG  . PHE B 1 84  ? -6.061  65.487 68.436 1.00 21.68 ? 84  PHE B CG  1 
ATOM   2674 C  CD1 . PHE B 1 84  ? -4.693  65.198 68.514 1.00 22.94 ? 84  PHE B CD1 1 
ATOM   2675 C  CD2 . PHE B 1 84  ? -6.489  66.683 67.848 1.00 21.85 ? 84  PHE B CD2 1 
ATOM   2676 C  CE1 . PHE B 1 84  ? -3.775  66.093 67.942 1.00 22.13 ? 84  PHE B CE1 1 
ATOM   2677 C  CE2 . PHE B 1 84  ? -5.579  67.559 67.251 1.00 21.22 ? 84  PHE B CE2 1 
ATOM   2678 C  CZ  . PHE B 1 84  ? -4.224  67.249 67.318 1.00 20.76 ? 84  PHE B CZ  1 
ATOM   2679 N  N   . SER B 1 85  ? -10.076 64.257 70.252 1.00 26.00 ? 85  SER B N   1 
ATOM   2680 C  CA  . SER B 1 85  ? -10.844 63.007 70.477 1.00 32.47 ? 85  SER B CA  1 
ATOM   2681 C  C   . SER B 1 85  ? -10.931 62.042 69.272 1.00 35.20 ? 85  SER B C   1 
ATOM   2682 O  O   . SER B 1 85  ? -11.274 60.855 69.436 1.00 32.44 ? 85  SER B O   1 
ATOM   2683 C  CB  . SER B 1 85  ? -12.220 63.332 71.027 1.00 37.67 ? 85  SER B CB  1 
ATOM   2684 O  OG  . SER B 1 85  ? -12.739 64.360 70.238 1.00 40.65 ? 85  SER B OG  1 
ATOM   2685 N  N   . ASP B 1 86  ? -10.595 62.571 68.101 1.00 32.79 ? 86  ASP B N   1 
ATOM   2686 C  CA  . ASP B 1 86  ? -10.434 61.857 66.827 1.00 33.56 ? 86  ASP B CA  1 
ATOM   2687 C  C   . ASP B 1 86  ? -9.013  61.280 66.673 1.00 32.19 ? 86  ASP B C   1 
ATOM   2688 O  O   . ASP B 1 86  ? -8.029  61.813 67.238 1.00 26.78 ? 86  ASP B O   1 
ATOM   2689 C  CB  . ASP B 1 86  ? -10.672 62.877 65.660 1.00 35.36 ? 86  ASP B CB  1 
ATOM   2690 C  CG  . ASP B 1 86  ? -12.091 63.504 65.645 1.00 37.20 ? 86  ASP B CG  1 
ATOM   2691 O  OD1 . ASP B 1 86  ? -13.079 62.840 66.038 1.00 40.98 ? 86  ASP B OD1 1 
ATOM   2692 O  OD2 . ASP B 1 86  ? -12.237 64.663 65.195 1.00 33.25 ? 86  ASP B OD2 1 
ATOM   2693 N  N   . SER B 1 87  ? -8.877  60.176 65.940 1.00 28.04 ? 87  SER B N   1 
ATOM   2694 C  CA  . SER B 1 87  ? -7.555  59.790 65.458 1.00 25.57 ? 87  SER B CA  1 
ATOM   2695 C  C   . SER B 1 87  ? -7.202  60.560 64.181 1.00 25.14 ? 87  SER B C   1 
ATOM   2696 O  O   . SER B 1 87  ? -8.055  60.849 63.365 1.00 23.54 ? 87  SER B O   1 
ATOM   2697 C  CB  . SER B 1 87  ? -7.465  58.284 65.171 1.00 31.24 ? 87  SER B CB  1 
ATOM   2698 O  OG  . SER B 1 87  ? -7.601  57.567 66.395 1.00 37.34 ? 87  SER B OG  1 
ATOM   2699 N  N   . TYR B 1 88  ? -5.915  60.868 64.046 1.00 21.91 ? 88  TYR B N   1 
ATOM   2700 C  CA  . TYR B 1 88  ? -5.382  61.535 62.812 1.00 19.67 ? 88  TYR B CA  1 
ATOM   2701 C  C   . TYR B 1 88  ? -4.399  60.641 62.101 1.00 20.58 ? 88  TYR B C   1 
ATOM   2702 O  O   . TYR B 1 88  ? -3.554  60.019 62.707 1.00 22.45 ? 88  TYR B O   1 
ATOM   2703 C  CB  . TYR B 1 88  ? -4.651  62.886 63.194 1.00 19.36 ? 88  TYR B CB  1 
ATOM   2704 C  CG  . TYR B 1 88  ? -5.593  63.961 63.615 1.00 18.92 ? 88  TYR B CG  1 
ATOM   2705 C  CD1 . TYR B 1 88  ? -5.774  65.083 62.839 1.00 19.01 ? 88  TYR B CD1 1 
ATOM   2706 C  CD2 . TYR B 1 88  ? -6.364  63.841 64.810 1.00 22.15 ? 88  TYR B CD2 1 
ATOM   2707 C  CE1 . TYR B 1 88  ? -6.631  66.086 63.213 1.00 21.56 ? 88  TYR B CE1 1 
ATOM   2708 C  CE2 . TYR B 1 88  ? -7.266  64.828 65.151 1.00 21.71 ? 88  TYR B CE2 1 
ATOM   2709 C  CZ  . TYR B 1 88  ? -7.402  65.940 64.344 1.00 22.56 ? 88  TYR B CZ  1 
ATOM   2710 O  OH  . TYR B 1 88  ? -8.248  67.010 64.618 1.00 27.74 ? 88  TYR B OH  1 
ATOM   2711 N  N   . ARG B 1 89  ? -4.490  60.630 60.774 1.00 20.20 ? 89  ARG B N   1 
ATOM   2712 C  CA  . ARG B 1 89  ? -3.734  59.708 59.947 1.00 21.33 ? 89  ARG B CA  1 
ATOM   2713 C  C   . ARG B 1 89  ? -2.415  60.354 59.496 1.00 16.43 ? 89  ARG B C   1 
ATOM   2714 O  O   . ARG B 1 89  ? -2.469  61.429 58.935 1.00 18.61 ? 89  ARG B O   1 
ATOM   2715 C  CB  . ARG B 1 89  ? -4.542  59.419 58.660 1.00 23.30 ? 89  ARG B CB  1 
ATOM   2716 C  CG  . ARG B 1 89  ? -3.959  58.260 57.884 1.00 26.02 ? 89  ARG B CG  1 
ATOM   2717 C  CD  . ARG B 1 89  ? -4.950  57.917 56.739 1.00 26.80 ? 89  ARG B CD  1 
ATOM   2718 N  NE  . ARG B 1 89  ? -6.235  57.399 57.252 1.00 31.98 ? 89  ARG B NE  1 
ATOM   2719 C  CZ  . ARG B 1 89  ? -7.304  57.049 56.515 1.00 36.62 ? 89  ARG B CZ  1 
ATOM   2720 N  NH1 . ARG B 1 89  ? -7.303  57.174 55.205 1.00 33.98 ? 89  ARG B NH1 1 
ATOM   2721 N  NH2 . ARG B 1 89  ? -8.409  56.595 57.096 1.00 38.09 ? 89  ARG B NH2 1 
ATOM   2722 N  N   . LEU B 1 90  ? -1.285  59.699 59.745 1.00 15.84 ? 90  LEU B N   1 
ATOM   2723 C  CA  . LEU B 1 90  ? 0.029   60.159 59.268 1.00 15.20 ? 90  LEU B CA  1 
ATOM   2724 C  C   . LEU B 1 90  ? 0.035   60.287 57.762 1.00 15.36 ? 90  LEU B C   1 
ATOM   2725 O  O   . LEU B 1 90  ? -0.439  59.316 57.085 1.00 16.07 ? 90  LEU B O   1 
ATOM   2726 C  CB  . LEU B 1 90  ? 1.107   59.153 59.612 1.00 14.98 ? 90  LEU B CB  1 
ATOM   2727 C  CG  . LEU B 1 90  ? 2.536   59.326 59.114 1.00 13.21 ? 90  LEU B CG  1 
ATOM   2728 C  CD1 . LEU B 1 90  ? 3.168   60.625 59.714 1.00 13.66 ? 90  LEU B CD1 1 
ATOM   2729 C  CD2 . LEU B 1 90  ? 3.416   58.160 59.530 1.00 13.86 ? 90  LEU B CD2 1 
ATOM   2730 N  N   . PHE B 1 91  ? 0.524   61.423 57.225 1.00 13.93 ? 91  PHE B N   1 
ATOM   2731 C  CA  . PHE B 1 91  ? 0.731   61.524 55.759 1.00 16.17 ? 91  PHE B CA  1 
ATOM   2732 C  C   . PHE B 1 91  ? 2.121   61.898 55.312 1.00 15.81 ? 91  PHE B C   1 
ATOM   2733 O  O   . PHE B 1 91  ? 2.515   61.584 54.184 1.00 15.05 ? 91  PHE B O   1 
ATOM   2734 C  CB  . PHE B 1 91  ? -0.406  62.319 55.037 1.00 14.70 ? 91  PHE B CB  1 
ATOM   2735 C  CG  . PHE B 1 91  ? -0.372  63.850 55.269 1.00 14.79 ? 91  PHE B CG  1 
ATOM   2736 C  CD1 . PHE B 1 91  ? -1.052  64.413 56.397 1.00 15.53 ? 91  PHE B CD1 1 
ATOM   2737 C  CD2 . PHE B 1 91  ? 0.339   64.682 54.410 1.00 13.91 ? 91  PHE B CD2 1 
ATOM   2738 C  CE1 . PHE B 1 91  ? -1.047  65.792 56.604 1.00 14.06 ? 91  PHE B CE1 1 
ATOM   2739 C  CE2 . PHE B 1 91  ? 0.331   66.066 54.581 1.00 16.24 ? 91  PHE B CE2 1 
ATOM   2740 C  CZ  . PHE B 1 91  ? -0.327  66.627 55.692 1.00 16.69 ? 91  PHE B CZ  1 
ATOM   2741 N  N   . GLN B 1 92  ? 2.895   62.601 56.137 1.00 15.93 ? 92  GLN B N   1 
ATOM   2742 C  CA  . GLN B 1 92  ? 4.170   63.139 55.700 1.00 15.79 ? 92  GLN B CA  1 
ATOM   2743 C  C   . GLN B 1 92  ? 5.025   63.525 56.897 1.00 16.68 ? 92  GLN B C   1 
ATOM   2744 O  O   . GLN B 1 92  ? 4.470   63.848 57.980 1.00 15.35 ? 92  GLN B O   1 
ATOM   2745 C  CB  . GLN B 1 92  ? 3.874   64.447 54.881 1.00 20.68 ? 92  GLN B CB  1 
ATOM   2746 C  CG  . GLN B 1 92  ? 5.043   65.257 54.480 1.00 24.83 ? 92  GLN B CG  1 
ATOM   2747 C  CD  . GLN B 1 92  ? 4.627   66.443 53.711 1.00 26.99 ? 92  GLN B CD  1 
ATOM   2748 O  OE1 . GLN B 1 92  ? 4.814   67.540 54.141 1.00 19.02 ? 92  GLN B OE1 1 
ATOM   2749 N  NE2 . GLN B 1 92  ? 4.028   66.205 52.493 1.00 29.42 ? 92  GLN B NE2 1 
ATOM   2750 N  N   . PHE B 1 93  ? 6.339   63.401 56.773 1.00 13.89 ? 93  PHE B N   1 
ATOM   2751 C  CA  . PHE B 1 93  ? 7.202   64.270 57.639 1.00 14.09 ? 93  PHE B CA  1 
ATOM   2752 C  C   . PHE B 1 93  ? 8.235   65.013 56.816 1.00 13.77 ? 93  PHE B C   1 
ATOM   2753 O  O   . PHE B 1 93  ? 8.537   64.623 55.662 1.00 13.97 ? 93  PHE B O   1 
ATOM   2754 C  CB  . PHE B 1 93  ? 7.927   63.478 58.767 1.00 12.37 ? 93  PHE B CB  1 
ATOM   2755 C  CG  . PHE B 1 93  ? 9.044   62.528 58.279 1.00 11.63 ? 93  PHE B CG  1 
ATOM   2756 C  CD1 . PHE B 1 93  ? 8.745   61.199 58.037 1.00 14.05 ? 93  PHE B CD1 1 
ATOM   2757 C  CD2 . PHE B 1 93  ? 10.341  62.942 58.236 1.00 13.57 ? 93  PHE B CD2 1 
ATOM   2758 C  CE1 . PHE B 1 93  ? 9.752   60.321 57.626 1.00 12.77 ? 93  PHE B CE1 1 
ATOM   2759 C  CE2 . PHE B 1 93  ? 11.357  62.118 57.860 1.00 14.95 ? 93  PHE B CE2 1 
ATOM   2760 C  CZ  . PHE B 1 93  ? 11.062  60.781 57.576 1.00 13.53 ? 93  PHE B CZ  1 
ATOM   2761 N  N   . HIS B 1 94  ? 8.759   66.095 57.391 1.00 12.46 ? 94  HIS B N   1 
ATOM   2762 C  CA  . HIS B 1 94  ? 9.788   66.903 56.708 1.00 13.27 ? 94  HIS B CA  1 
ATOM   2763 C  C   . HIS B 1 94  ? 10.500  67.742 57.738 1.00 12.14 ? 94  HIS B C   1 
ATOM   2764 O  O   . HIS B 1 94  ? 10.207  67.645 58.997 1.00 12.32 ? 94  HIS B O   1 
ATOM   2765 C  CB  . HIS B 1 94  ? 9.134   67.826 55.607 1.00 13.20 ? 94  HIS B CB  1 
ATOM   2766 C  CG  . HIS B 1 94  ? 8.119   68.820 56.178 1.00 13.02 ? 94  HIS B CG  1 
ATOM   2767 N  ND1 . HIS B 1 94  ? 6.736   68.572 56.140 1.00 14.63 ? 94  HIS B ND1 1 
ATOM   2768 C  CD2 . HIS B 1 94  ? 8.287   70.002 56.870 1.00 14.02 ? 94  HIS B CD2 1 
ATOM   2769 C  CE1 . HIS B 1 94  ? 6.093   69.598 56.770 1.00 14.77 ? 94  HIS B CE1 1 
ATOM   2770 N  NE2 . HIS B 1 94  ? 6.996   70.449 57.226 1.00 12.96 ? 94  HIS B NE2 1 
ATOM   2771 N  N   . PHE B 1 95  ? 11.430  68.586 57.278 1.00 13.39 ? 95  PHE B N   1 
ATOM   2772 C  CA  . PHE B 1 95  ? 12.230  69.391 58.168 1.00 12.99 ? 95  PHE B CA  1 
ATOM   2773 C  C   . PHE B 1 95  ? 12.227  70.844 57.693 1.00 14.30 ? 95  PHE B C   1 
ATOM   2774 O  O   . PHE B 1 95  ? 11.931  71.100 56.530 1.00 15.22 ? 95  PHE B O   1 
ATOM   2775 C  CB  . PHE B 1 95  ? 13.715  68.918 58.232 1.00 13.45 ? 95  PHE B CB  1 
ATOM   2776 C  CG  . PHE B 1 95  ? 13.834  67.454 58.636 1.00 13.73 ? 95  PHE B CG  1 
ATOM   2777 C  CD1 . PHE B 1 95  ? 14.026  67.120 60.002 1.00 14.12 ? 95  PHE B CD1 1 
ATOM   2778 C  CD2 . PHE B 1 95  ? 13.727  66.428 57.675 1.00 14.42 ? 95  PHE B CD2 1 
ATOM   2779 C  CE1 . PHE B 1 95  ? 14.156  65.781 60.385 1.00 13.15 ? 95  PHE B CE1 1 
ATOM   2780 C  CE2 . PHE B 1 95  ? 13.787  65.078 58.051 1.00 13.24 ? 95  PHE B CE2 1 
ATOM   2781 C  CZ  . PHE B 1 95  ? 13.983  64.765 59.419 1.00 15.46 ? 95  PHE B CZ  1 
ATOM   2782 N  N   . HIS B 1 96  ? 12.577  71.740 58.582 1.00 13.02 ? 96  HIS B N   1 
ATOM   2783 C  CA  . HIS B 1 96  ? 12.951  73.164 58.219 1.00 13.16 ? 96  HIS B CA  1 
ATOM   2784 C  C   . HIS B 1 96  ? 14.287  73.420 58.788 1.00 13.79 ? 96  HIS B C   1 
ATOM   2785 O  O   . HIS B 1 96  ? 14.622  72.932 59.875 1.00 14.41 ? 96  HIS B O   1 
ATOM   2786 C  CB  . HIS B 1 96  ? 11.951  74.160 58.778 1.00 13.35 ? 96  HIS B CB  1 
ATOM   2787 C  CG  . HIS B 1 96  ? 10.578  73.928 58.269 1.00 12.00 ? 96  HIS B CG  1 
ATOM   2788 N  ND1 . HIS B 1 96  ? 10.023  74.679 57.277 1.00 14.51 ? 96  HIS B ND1 1 
ATOM   2789 C  CD2 . HIS B 1 96  ? 9.614   72.988 58.660 1.00 12.46 ? 96  HIS B CD2 1 
ATOM   2790 C  CE1 . HIS B 1 96  ? 8.742   74.266 57.045 1.00 13.31 ? 96  HIS B CE1 1 
ATOM   2791 N  NE2 . HIS B 1 96  ? 8.493   73.176 57.882 1.00 13.29 ? 96  HIS B NE2 1 
ATOM   2792 N  N   . TRP B 1 97  ? 15.082  74.209 58.093 1.00 14.33 ? 97  TRP B N   1 
ATOM   2793 C  CA  . TRP B 1 97  ? 16.414  74.610 58.543 1.00 15.95 ? 97  TRP B CA  1 
ATOM   2794 C  C   . TRP B 1 97  ? 16.696  76.039 58.127 1.00 15.92 ? 97  TRP B C   1 
ATOM   2795 O  O   . TRP B 1 97  ? 15.895  76.633 57.430 1.00 16.40 ? 97  TRP B O   1 
ATOM   2796 C  CB  . TRP B 1 97  ? 17.486  73.659 58.036 1.00 14.96 ? 97  TRP B CB  1 
ATOM   2797 C  CG  . TRP B 1 97  ? 17.490  73.526 56.540 1.00 17.23 ? 97  TRP B CG  1 
ATOM   2798 C  CD1 . TRP B 1 97  ? 18.189  74.307 55.625 1.00 17.03 ? 97  TRP B CD1 1 
ATOM   2799 C  CD2 . TRP B 1 97  ? 16.751  72.550 55.723 1.00 15.36 ? 97  TRP B CD2 1 
ATOM   2800 N  NE1 . TRP B 1 97  ? 17.943  73.891 54.342 1.00 17.80 ? 97  TRP B NE1 1 
ATOM   2801 C  CE2 . TRP B 1 97  ? 17.091  72.843 54.330 1.00 16.97 ? 97  TRP B CE2 1 
ATOM   2802 C  CE3 . TRP B 1 97  ? 15.880  71.501 55.997 1.00 14.84 ? 97  TRP B CE3 1 
ATOM   2803 C  CZ2 . TRP B 1 97  ? 16.572  72.107 53.278 1.00 16.39 ? 97  TRP B CZ2 1 
ATOM   2804 C  CZ3 . TRP B 1 97  ? 15.364  70.768 54.927 1.00 14.78 ? 97  TRP B CZ3 1 
ATOM   2805 C  CH2 . TRP B 1 97  ? 15.700  71.067 53.601 1.00 15.06 ? 97  TRP B CH2 1 
ATOM   2806 N  N   . GLY B 1 98  ? 17.847  76.566 58.564 1.00 15.58 ? 98  GLY B N   1 
ATOM   2807 C  CA  . GLY B 1 98  ? 18.199  77.944 58.325 1.00 17.33 ? 98  GLY B CA  1 
ATOM   2808 C  C   . GLY B 1 98  ? 19.577  77.963 57.645 1.00 16.90 ? 98  GLY B C   1 
ATOM   2809 O  O   . GLY B 1 98  ? 20.244  76.921 57.392 1.00 16.65 ? 98  GLY B O   1 
ATOM   2810 N  N   . SER B 1 99  ? 19.938  79.163 57.267 1.00 17.82 ? 99  SER B N   1 
ATOM   2811 C  CA  . SER B 1 99  ? 21.203  79.310 56.504 1.00 23.10 ? 99  SER B CA  1 
ATOM   2812 C  C   . SER B 1 99  ? 22.441  79.104 57.376 1.00 24.06 ? 99  SER B C   1 
ATOM   2813 O  O   . SER B 1 99  ? 23.489  78.705 56.851 1.00 26.92 ? 99  SER B O   1 
ATOM   2814 C  CB  . SER B 1 99  ? 21.247  80.669 55.788 1.00 24.22 ? 99  SER B CB  1 
ATOM   2815 O  OG  . SER B 1 99  ? 21.446  81.710 56.721 1.00 32.98 ? 99  SER B OG  1 
ATOM   2816 N  N   . THR B 1 100 ? 22.335  79.288 58.693 1.00 25.27 ? 100 THR B N   1 
ATOM   2817 C  CA  . THR B 1 100 ? 23.430  78.884 59.564 1.00 28.79 ? 100 THR B CA  1 
ATOM   2818 C  C   . THR B 1 100 ? 22.961  77.813 60.533 1.00 27.10 ? 100 THR B C   1 
ATOM   2819 O  O   . THR B 1 100 ? 21.755  77.583 60.645 1.00 22.63 ? 100 THR B O   1 
ATOM   2820 C  CB  . THR B 1 100 ? 23.943  80.070 60.400 1.00 31.55 ? 100 THR B CB  1 
ATOM   2821 O  OG1 . THR B 1 100 ? 22.905  80.461 61.297 1.00 30.92 ? 100 THR B OG1 1 
ATOM   2822 C  CG2 . THR B 1 100 ? 24.316  81.229 59.497 1.00 35.40 ? 100 THR B CG2 1 
ATOM   2823 N  N   . ASN B 1 101 ? 23.918  77.213 61.254 1.00 23.14 ? 101 ASN B N   1 
ATOM   2824 C  CA  . ASN B 1 101 ? 23.608  76.127 62.173 1.00 29.87 ? 101 ASN B CA  1 
ATOM   2825 C  C   . ASN B 1 101 ? 22.966  76.598 63.435 1.00 32.68 ? 101 ASN B C   1 
ATOM   2826 O  O   . ASN B 1 101 ? 22.457  75.780 64.175 1.00 37.19 ? 101 ASN B O   1 
ATOM   2827 C  CB  . ASN B 1 101 ? 24.834  75.241 62.496 1.00 30.68 ? 101 ASN B CB  1 
ATOM   2828 C  CG  . ASN B 1 101 ? 25.353  74.537 61.279 1.00 37.39 ? 101 ASN B CG  1 
ATOM   2829 O  OD1 . ASN B 1 101 ? 24.620  74.298 60.321 1.00 35.34 ? 101 ASN B OD1 1 
ATOM   2830 N  ND2 . ASN B 1 101 ? 26.658  74.234 61.273 1.00 37.76 ? 101 ASN B ND2 1 
ATOM   2831 N  N   . GLU B 1 102 ? 22.952  77.902 63.669 1.00 30.96 ? 102 GLU B N   1 
ATOM   2832 C  CA  . GLU B 1 102 ? 22.530  78.396 64.979 1.00 41.74 ? 102 GLU B CA  1 
ATOM   2833 C  C   . GLU B 1 102 ? 21.044  78.527 64.926 1.00 40.48 ? 102 GLU B C   1 
ATOM   2834 O  O   . GLU B 1 102 ? 20.373  78.147 65.916 1.00 37.79 ? 102 GLU B O   1 
ATOM   2835 C  CB  . GLU B 1 102 ? 23.137  79.764 65.408 1.00 42.74 ? 102 GLU B CB  1 
ATOM   2836 C  CG  . GLU B 1 102 ? 24.645  79.825 65.608 1.00 52.56 ? 102 GLU B CG  1 
ATOM   2837 C  CD  . GLU B 1 102 ? 25.390  79.885 64.277 1.00 57.99 ? 102 GLU B CD  1 
ATOM   2838 O  OE1 . GLU B 1 102 ? 25.813  78.802 63.798 1.00 59.07 ? 102 GLU B OE1 1 
ATOM   2839 O  OE2 . GLU B 1 102 ? 25.541  80.995 63.693 1.00 62.44 ? 102 GLU B OE2 1 
ATOM   2840 N  N   . HIS B 1 103 ? 20.551  79.033 63.779 1.00 30.83 ? 103 HIS B N   1 
ATOM   2841 C  CA  . HIS B 1 103 ? 19.183  79.518 63.668 1.00 32.08 ? 103 HIS B CA  1 
ATOM   2842 C  C   . HIS B 1 103 ? 18.395  79.051 62.471 1.00 30.90 ? 103 HIS B C   1 
ATOM   2843 O  O   . HIS B 1 103 ? 18.478  79.660 61.403 1.00 35.01 ? 103 HIS B O   1 
ATOM   2844 C  CB  . HIS B 1 103 ? 19.160  81.061 63.777 1.00 36.61 ? 103 HIS B CB  1 
ATOM   2845 C  CG  . HIS B 1 103 ? 19.879  81.587 65.036 1.00 41.31 ? 103 HIS B CG  1 
ATOM   2846 N  ND1 . HIS B 1 103 ? 19.627  81.091 66.300 1.00 48.24 ? 103 HIS B ND1 1 
ATOM   2847 C  CD2 . HIS B 1 103 ? 20.857  82.585 65.198 1.00 43.32 ? 103 HIS B CD2 1 
ATOM   2848 C  CE1 . HIS B 1 103 ? 20.414  81.736 67.218 1.00 41.23 ? 103 HIS B CE1 1 
ATOM   2849 N  NE2 . HIS B 1 103 ? 21.169  82.646 66.541 1.00 52.74 ? 103 HIS B NE2 1 
ATOM   2850 N  N   . GLY B 1 104 ? 17.509  78.074 62.679 1.00 22.55 ? 104 GLY B N   1 
ATOM   2851 C  CA  . GLY B 1 104 ? 16.683  77.570 61.569 1.00 20.33 ? 104 GLY B CA  1 
ATOM   2852 C  C   . GLY B 1 104 ? 15.400  76.813 61.901 1.00 18.05 ? 104 GLY B C   1 
ATOM   2853 O  O   . GLY B 1 104 ? 14.719  76.339 60.996 1.00 17.06 ? 104 GLY B O   1 
ATOM   2854 N  N   . SER B 1 105 ? 15.019  76.791 63.156 1.00 15.49 ? 105 SER B N   1 
ATOM   2855 C  CA  . SER B 1 105 ? 13.686  76.267 63.517 1.00 15.08 ? 105 SER B CA  1 
ATOM   2856 C  C   . SER B 1 105 ? 12.595  77.255 63.176 1.00 17.04 ? 105 SER B C   1 
ATOM   2857 O  O   . SER B 1 105 ? 12.883  78.397 62.877 1.00 17.65 ? 105 SER B O   1 
ATOM   2858 C  CB  . SER B 1 105 ? 13.582  75.867 65.030 1.00 16.72 ? 105 SER B CB  1 
ATOM   2859 O  OG  . SER B 1 105 ? 13.654  77.010 65.848 1.00 15.61 ? 105 SER B OG  1 
ATOM   2860 N  N   . GLU B 1 106 ? 11.331  76.808 63.225 1.00 14.85 ? 106 GLU B N   1 
ATOM   2861 C  CA  . GLU B 1 106 ? 10.199  77.664 62.959 1.00 13.71 ? 106 GLU B CA  1 
ATOM   2862 C  C   . GLU B 1 106 ? 9.671   78.127 64.293 1.00 14.58 ? 106 GLU B C   1 
ATOM   2863 O  O   . GLU B 1 106 ? 9.642   79.340 64.585 1.00 15.70 ? 106 GLU B O   1 
ATOM   2864 C  CB  . GLU B 1 106 ? 9.116   76.846 62.224 1.00 16.43 ? 106 GLU B CB  1 
ATOM   2865 C  CG  . GLU B 1 106 ? 9.656   76.466 60.840 1.00 17.95 ? 106 GLU B CG  1 
ATOM   2866 C  CD  . GLU B 1 106 ? 8.611   76.531 59.742 1.00 16.80 ? 106 GLU B CD  1 
ATOM   2867 O  OE1 . GLU B 1 106 ? 8.771   77.349 58.786 1.00 15.71 ? 106 GLU B OE1 1 
ATOM   2868 O  OE2 . GLU B 1 106 ? 7.629   75.746 59.820 1.00 15.15 ? 106 GLU B OE2 1 
ATOM   2869 N  N   . HIS B 1 107 ? 9.274   77.202 65.155 1.00 14.21 ? 107 HIS B N   1 
ATOM   2870 C  CA  . HIS B 1 107 ? 8.833   77.628 66.482 1.00 14.29 ? 107 HIS B CA  1 
ATOM   2871 C  C   . HIS B 1 107 ? 10.045  78.040 67.299 1.00 16.61 ? 107 HIS B C   1 
ATOM   2872 O  O   . HIS B 1 107 ? 11.169  77.581 67.033 1.00 16.70 ? 107 HIS B O   1 
ATOM   2873 C  CB  . HIS B 1 107 ? 8.098   76.521 67.183 1.00 14.77 ? 107 HIS B CB  1 
ATOM   2874 C  CG  . HIS B 1 107 ? 6.754   76.246 66.542 1.00 13.07 ? 107 HIS B CG  1 
ATOM   2875 N  ND1 . HIS B 1 107 ? 6.625   75.391 65.483 1.00 15.01 ? 107 HIS B ND1 1 
ATOM   2876 C  CD2 . HIS B 1 107 ? 5.481   76.757 66.822 1.00 13.13 ? 107 HIS B CD2 1 
ATOM   2877 C  CE1 . HIS B 1 107 ? 5.306   75.429 65.068 1.00 14.17 ? 107 HIS B CE1 1 
ATOM   2878 N  NE2 . HIS B 1 107 ? 4.620   76.254 65.895 1.00 16.11 ? 107 HIS B NE2 1 
ATOM   2879 N  N   . THR B 1 108 ? 9.813   78.961 68.239 1.00 16.73 ? 108 THR B N   1 
ATOM   2880 C  CA  . THR B 1 108 ? 10.869  79.344 69.202 1.00 15.45 ? 108 THR B CA  1 
ATOM   2881 C  C   . THR B 1 108 ? 10.312  79.152 70.579 1.00 15.50 ? 108 THR B C   1 
ATOM   2882 O  O   . THR B 1 108 ? 9.072   79.129 70.788 1.00 16.10 ? 108 THR B O   1 
ATOM   2883 C  CB  . THR B 1 108 ? 11.330  80.815 68.969 1.00 16.78 ? 108 THR B CB  1 
ATOM   2884 O  OG1 . THR B 1 108 ? 10.212  81.690 69.169 1.00 17.97 ? 108 THR B OG1 1 
ATOM   2885 C  CG2 . THR B 1 108 ? 11.936  80.951 67.573 1.00 18.25 ? 108 THR B CG2 1 
ATOM   2886 N  N   . VAL B 1 109 ? 11.205  79.005 71.563 1.00 16.26 ? 109 VAL B N   1 
ATOM   2887 C  CA  . VAL B 1 109 ? 10.722  78.878 72.977 1.00 18.37 ? 109 VAL B CA  1 
ATOM   2888 C  C   . VAL B 1 109 ? 11.385  80.008 73.790 1.00 18.38 ? 109 VAL B C   1 
ATOM   2889 O  O   . VAL B 1 109 ? 12.631  80.057 73.812 1.00 21.19 ? 109 VAL B O   1 
ATOM   2890 C  CB  . VAL B 1 109 ? 11.118  77.513 73.561 1.00 18.06 ? 109 VAL B CB  1 
ATOM   2891 C  CG1 . VAL B 1 109 ? 10.712  77.370 75.047 1.00 18.80 ? 109 VAL B CG1 1 
ATOM   2892 C  CG2 . VAL B 1 109 ? 10.377  76.378 72.839 1.00 18.34 ? 109 VAL B CG2 1 
ATOM   2893 N  N   . ASP B 1 110 ? 10.569  80.877 74.396 1.00 19.61 ? 110 ASP B N   1 
ATOM   2894 C  CA  . ASP B 1 110 ? 11.083  82.052 75.151 1.00 20.91 ? 110 ASP B CA  1 
ATOM   2895 C  C   . ASP B 1 110 ? 12.054  82.859 74.289 1.00 23.84 ? 110 ASP B C   1 
ATOM   2896 O  O   . ASP B 1 110 ? 13.088  83.350 74.808 1.00 24.79 ? 110 ASP B O   1 
ATOM   2897 C  CB  . ASP B 1 110 ? 11.764  81.561 76.469 1.00 21.25 ? 110 ASP B CB  1 
ATOM   2898 C  CG  . ASP B 1 110 ? 10.751  81.101 77.498 1.00 22.87 ? 110 ASP B CG  1 
ATOM   2899 O  OD1 . ASP B 1 110 ? 9.610   81.608 77.543 1.00 24.03 ? 110 ASP B OD1 1 
ATOM   2900 O  OD2 . ASP B 1 110 ? 11.082  80.175 78.246 1.00 28.65 ? 110 ASP B OD2 1 
ATOM   2901 N  N   . GLY B 1 111 ? 11.715  83.011 72.991 1.00 22.55 ? 111 GLY B N   1 
ATOM   2902 C  CA  . GLY B 1 111 ? 12.555  83.708 71.993 1.00 26.06 ? 111 GLY B CA  1 
ATOM   2903 C  C   . GLY B 1 111 ? 13.803  83.027 71.478 1.00 25.89 ? 111 GLY B C   1 
ATOM   2904 O  O   . GLY B 1 111 ? 14.507  83.591 70.607 1.00 27.89 ? 111 GLY B O   1 
ATOM   2905 N  N   . VAL B 1 112 ? 14.100  81.805 71.940 1.00 21.67 ? 112 VAL B N   1 
ATOM   2906 C  CA  . VAL B 1 112 ? 15.303  81.088 71.541 1.00 22.82 ? 112 VAL B CA  1 
ATOM   2907 C  C   . VAL B 1 112 ? 14.933  80.274 70.296 1.00 22.28 ? 112 VAL B C   1 
ATOM   2908 O  O   . VAL B 1 112 ? 13.921  79.521 70.294 1.00 19.56 ? 112 VAL B O   1 
ATOM   2909 C  CB  . VAL B 1 112 ? 15.847  80.203 72.644 1.00 25.38 ? 112 VAL B CB  1 
ATOM   2910 C  CG1 . VAL B 1 112 ? 17.034  79.373 72.120 1.00 28.62 ? 112 VAL B CG1 1 
ATOM   2911 C  CG2 . VAL B 1 112 ? 16.276  81.080 73.842 1.00 26.88 ? 112 VAL B CG2 1 
ATOM   2912 N  N   A LYS B 1 113 ? 15.729  80.489 69.260 0.50 20.89 ? 113 LYS B N   1 
ATOM   2913 N  N   B LYS B 1 113 ? 15.707  80.472 69.246 0.50 18.81 ? 113 LYS B N   1 
ATOM   2914 C  CA  A LYS B 1 113 ? 15.593  79.819 67.982 0.50 23.02 ? 113 LYS B CA  1 
ATOM   2915 C  CA  B LYS B 1 113 ? 15.480  79.784 67.985 0.50 19.33 ? 113 LYS B CA  1 
ATOM   2916 C  C   A LYS B 1 113 ? 16.548  78.651 68.039 0.50 22.82 ? 113 LYS B C   1 
ATOM   2917 C  C   B LYS B 1 113 ? 16.530  78.700 67.912 0.50 20.38 ? 113 LYS B C   1 
ATOM   2918 O  O   A LYS B 1 113 ? 17.710  78.813 68.481 0.50 25.35 ? 113 LYS B O   1 
ATOM   2919 O  O   B LYS B 1 113 ? 17.728  78.965 68.172 0.50 24.22 ? 113 LYS B O   1 
ATOM   2920 C  CB  A LYS B 1 113 ? 16.050  80.739 66.836 0.50 26.17 ? 113 LYS B CB  1 
ATOM   2921 C  CB  B LYS B 1 113 ? 15.632  80.744 66.793 0.50 19.11 ? 113 LYS B CB  1 
ATOM   2922 C  CG  A LYS B 1 113 ? 15.621  82.194 66.930 0.50 27.90 ? 113 LYS B CG  1 
ATOM   2923 C  CG  B LYS B 1 113 ? 15.421  80.072 65.432 0.50 15.96 ? 113 LYS B CG  1 
ATOM   2924 C  CD  B LYS B 1 113 ? 14.759  81.084 64.525 0.50 18.62 ? 113 LYS B CD  1 
ATOM   2925 C  CE  B LYS B 1 113 ? 14.914  80.671 63.107 0.50 18.55 ? 113 LYS B CE  1 
ATOM   2926 N  NZ  B LYS B 1 113 ? 13.685  81.216 62.452 0.50 19.81 ? 113 LYS B NZ  1 
ATOM   2927 N  N   . TYR B 1 114 ? 16.084  77.473 67.612 1.00 20.40 ? 114 TYR B N   1 
ATOM   2928 C  CA  . TYR B 1 114 ? 16.940  76.286 67.531 1.00 20.16 ? 114 TYR B CA  1 
ATOM   2929 C  C   . TYR B 1 114 ? 17.458  76.061 66.116 1.00 19.51 ? 114 TYR B C   1 
ATOM   2930 O  O   . TYR B 1 114 ? 17.159  76.834 65.195 1.00 20.39 ? 114 TYR B O   1 
ATOM   2931 C  CB  . TYR B 1 114 ? 16.103  75.070 67.959 1.00 22.30 ? 114 TYR B CB  1 
ATOM   2932 C  CG  . TYR B 1 114 ? 15.943  74.981 69.439 1.00 26.09 ? 114 TYR B CG  1 
ATOM   2933 C  CD1 . TYR B 1 114 ? 16.610  73.948 70.131 1.00 35.14 ? 114 TYR B CD1 1 
ATOM   2934 C  CD2 . TYR B 1 114 ? 15.130  75.890 70.173 1.00 27.14 ? 114 TYR B CD2 1 
ATOM   2935 C  CE1 . TYR B 1 114 ? 16.503  73.824 71.517 1.00 38.85 ? 114 TYR B CE1 1 
ATOM   2936 C  CE2 . TYR B 1 114 ? 15.011  75.805 71.571 1.00 33.36 ? 114 TYR B CE2 1 
ATOM   2937 C  CZ  . TYR B 1 114 ? 15.705  74.745 72.235 1.00 40.10 ? 114 TYR B CZ  1 
ATOM   2938 O  OH  . TYR B 1 114 ? 15.653  74.507 73.609 1.00 41.97 ? 114 TYR B OH  1 
ATOM   2939 N  N   . SER B 1 115 ? 18.293  75.058 65.937 1.00 18.94 ? 115 SER B N   1 
ATOM   2940 C  CA  . SER B 1 115 ? 18.949  74.888 64.643 1.00 18.51 ? 115 SER B CA  1 
ATOM   2941 C  C   . SER B 1 115 ? 18.013  74.454 63.506 1.00 19.79 ? 115 SER B C   1 
ATOM   2942 O  O   . SER B 1 115 ? 18.230  74.766 62.327 1.00 21.77 ? 115 SER B O   1 
ATOM   2943 C  CB  . SER B 1 115 ? 20.101  73.865 64.801 1.00 20.56 ? 115 SER B CB  1 
ATOM   2944 O  OG  . SER B 1 115 ? 20.962  74.302 65.866 1.00 22.22 ? 115 SER B OG  1 
ATOM   2945 N  N   . ALA B 1 116 ? 17.015  73.638 63.844 1.00 18.37 ? 116 ALA B N   1 
ATOM   2946 C  CA  . ALA B 1 116 ? 16.167  73.080 62.801 1.00 15.15 ? 116 ALA B CA  1 
ATOM   2947 C  C   . ALA B 1 116 ? 14.918  72.562 63.478 1.00 13.53 ? 116 ALA B C   1 
ATOM   2948 O  O   . ALA B 1 116 ? 14.790  72.619 64.682 1.00 14.23 ? 116 ALA B O   1 
ATOM   2949 C  CB  . ALA B 1 116 ? 16.896  71.934 62.063 1.00 16.27 ? 116 ALA B CB  1 
ATOM   2950 N  N   . GLU B 1 117 ? 13.997  72.029 62.686 1.00 13.63 ? 117 GLU B N   1 
ATOM   2951 C  CA  . GLU B 1 117 ? 12.697  71.556 63.212 1.00 14.09 ? 117 GLU B CA  1 
ATOM   2952 C  C   . GLU B 1 117 ? 12.162  70.410 62.362 1.00 13.44 ? 117 GLU B C   1 
ATOM   2953 O  O   . GLU B 1 117 ? 12.225  70.456 61.120 1.00 12.98 ? 117 GLU B O   1 
ATOM   2954 C  CB  . GLU B 1 117 ? 11.708  72.716 63.386 1.00 14.50 ? 117 GLU B CB  1 
ATOM   2955 C  CG  . GLU B 1 117 ? 10.426  72.379 64.161 1.00 14.29 ? 117 GLU B CG  1 
ATOM   2956 C  CD  . GLU B 1 117 ? 9.628   73.621 64.461 1.00 13.22 ? 117 GLU B CD  1 
ATOM   2957 O  OE1 . GLU B 1 117 ? 8.366   73.569 64.487 1.00 13.11 ? 117 GLU B OE1 1 
ATOM   2958 O  OE2 . GLU B 1 117 ? 10.288  74.646 64.716 1.00 14.52 ? 117 GLU B OE2 1 
ATOM   2959 N  N   . LEU B 1 118 ? 11.646  69.369 63.029 1.00 12.71 ? 118 LEU B N   1 
ATOM   2960 C  CA  . LEU B 1 118 ? 11.004  68.226 62.349 1.00 11.63 ? 118 LEU B CA  1 
ATOM   2961 C  C   . LEU B 1 118 ? 9.528   68.461 62.474 1.00 10.58 ? 118 LEU B C   1 
ATOM   2962 O  O   . LEU B 1 118 ? 9.070   68.788 63.546 1.00 12.12 ? 118 LEU B O   1 
ATOM   2963 C  CB  . LEU B 1 118 ? 11.474  66.905 63.051 1.00 11.55 ? 118 LEU B CB  1 
ATOM   2964 C  CG  . LEU B 1 118 ? 10.580  65.653 62.899 1.00 13.59 ? 118 LEU B CG  1 
ATOM   2965 C  CD1 . LEU B 1 118 ? 10.685  65.144 61.420 1.00 14.04 ? 118 LEU B CD1 1 
ATOM   2966 C  CD2 . LEU B 1 118 ? 10.949  64.539 63.887 1.00 13.99 ? 118 LEU B CD2 1 
ATOM   2967 N  N   . HIS B 1 119 ? 8.790   68.227 61.399 1.00 10.99 ? 119 HIS B N   1 
ATOM   2968 C  CA  . HIS B 1 119 ? 7.318   68.277 61.364 1.00 11.34 ? 119 HIS B CA  1 
ATOM   2969 C  C   . HIS B 1 119 ? 6.797   66.938 60.911 1.00 12.47 ? 119 HIS B C   1 
ATOM   2970 O  O   . HIS B 1 119 ? 7.223   66.428 59.839 1.00 13.87 ? 119 HIS B O   1 
ATOM   2971 C  CB  . HIS B 1 119 ? 6.910   69.362 60.391 1.00 12.87 ? 119 HIS B CB  1 
ATOM   2972 C  CG  . HIS B 1 119 ? 7.080   70.743 60.970 1.00 13.26 ? 119 HIS B CG  1 
ATOM   2973 N  ND1 . HIS B 1 119 ? 7.058   71.905 60.206 1.00 12.97 ? 119 HIS B ND1 1 
ATOM   2974 C  CD2 . HIS B 1 119 ? 7.288   71.109 62.289 1.00 14.54 ? 119 HIS B CD2 1 
ATOM   2975 C  CE1 . HIS B 1 119 ? 7.286   72.975 61.065 1.00 12.85 ? 119 HIS B CE1 1 
ATOM   2976 N  NE2 . HIS B 1 119 ? 7.475   72.451 62.324 1.00 14.41 ? 119 HIS B NE2 1 
ATOM   2977 N  N   . VAL B 1 120 ? 5.901   66.352 61.699 1.00 12.31 ? 120 VAL B N   1 
ATOM   2978 C  CA  . VAL B 1 120 ? 5.255   65.062 61.362 1.00 12.64 ? 120 VAL B CA  1 
ATOM   2979 C  C   . VAL B 1 120 ? 3.773   65.388 61.195 1.00 13.75 ? 120 VAL B C   1 
ATOM   2980 O  O   . VAL B 1 120 ? 3.089   65.779 62.161 1.00 13.20 ? 120 VAL B O   1 
ATOM   2981 C  CB  . VAL B 1 120 ? 5.570   63.990 62.440 1.00 13.23 ? 120 VAL B CB  1 
ATOM   2982 C  CG1 . VAL B 1 120 ? 4.990   62.634 62.003 1.00 13.46 ? 120 VAL B CG1 1 
ATOM   2983 C  CG2 . VAL B 1 120 ? 7.117   63.882 62.761 1.00 12.97 ? 120 VAL B CG2 1 
ATOM   2984 N  N   . ALA B 1 121 ? 3.236   65.276 59.973 1.00 13.04 ? 121 ALA B N   1 
ATOM   2985 C  CA  . ALA B 1 121 ? 1.900   65.835 59.674 1.00 15.10 ? 121 ALA B CA  1 
ATOM   2986 C  C   . ALA B 1 121 ? 0.858   64.719 59.501 1.00 14.42 ? 121 ALA B C   1 
ATOM   2987 O  O   . ALA B 1 121 ? 1.198   63.639 58.942 1.00 15.57 ? 121 ALA B O   1 
ATOM   2988 C  CB  . ALA B 1 121 ? 1.963   66.681 58.418 1.00 14.78 ? 121 ALA B CB  1 
ATOM   2989 N  N   . HIS B 1 122 ? -0.371  64.999 59.956 1.00 14.34 ? 122 HIS B N   1 
ATOM   2990 C  CA  . HIS B 1 122 ? -1.459  64.012 60.018 1.00 14.17 ? 122 HIS B CA  1 
ATOM   2991 C  C   . HIS B 1 122 ? -2.729  64.703 59.625 1.00 16.27 ? 122 HIS B C   1 
ATOM   2992 O  O   . HIS B 1 122 ? -2.873  65.949 59.797 1.00 15.65 ? 122 HIS B O   1 
ATOM   2993 C  CB  . HIS B 1 122 ? -1.633  63.506 61.478 1.00 14.06 ? 122 HIS B CB  1 
ATOM   2994 C  CG  . HIS B 1 122 ? -0.376  63.096 62.153 1.00 14.22 ? 122 HIS B CG  1 
ATOM   2995 N  ND1 . HIS B 1 122 ? 0.535   64.017 62.657 1.00 15.01 ? 122 HIS B ND1 1 
ATOM   2996 C  CD2 . HIS B 1 122 ? 0.067   61.854 62.546 1.00 13.95 ? 122 HIS B CD2 1 
ATOM   2997 C  CE1 . HIS B 1 122 ? 1.543   63.295 63.259 1.00 14.49 ? 122 HIS B CE1 1 
ATOM   2998 N  NE2 . HIS B 1 122 ? 1.240   61.993 63.178 1.00 14.93 ? 122 HIS B NE2 1 
ATOM   2999 N  N   . TRP B 1 123 ? -3.719  63.944 59.160 1.00 16.49 ? 123 TRP B N   1 
ATOM   3000 C  CA  . TRP B 1 123 ? -5.032  64.561 58.835 1.00 16.70 ? 123 TRP B CA  1 
ATOM   3001 C  C   . TRP B 1 123 ? -6.198  63.789 59.499 1.00 19.59 ? 123 TRP B C   1 
ATOM   3002 O  O   . TRP B 1 123 ? -6.102  62.612 59.754 1.00 17.33 ? 123 TRP B O   1 
ATOM   3003 C  CB  . TRP B 1 123 ? -5.229  64.758 57.329 1.00 18.67 ? 123 TRP B CB  1 
ATOM   3004 C  CG  . TRP B 1 123 ? -5.239  63.492 56.504 1.00 18.46 ? 123 TRP B CG  1 
ATOM   3005 C  CD1 . TRP B 1 123 ? -4.160  62.885 55.867 1.00 19.52 ? 123 TRP B CD1 1 
ATOM   3006 C  CD2 . TRP B 1 123 ? -6.398  62.645 56.177 1.00 25.05 ? 123 TRP B CD2 1 
ATOM   3007 N  NE1 . TRP B 1 123 ? -4.559  61.753 55.201 1.00 22.87 ? 123 TRP B NE1 1 
ATOM   3008 C  CE2 . TRP B 1 123 ? -5.884  61.552 55.349 1.00 24.22 ? 123 TRP B CE2 1 
ATOM   3009 C  CE3 . TRP B 1 123 ? -7.750  62.676 56.486 1.00 25.18 ? 123 TRP B CE3 1 
ATOM   3010 C  CZ2 . TRP B 1 123 ? -6.706  60.553 54.862 1.00 27.27 ? 123 TRP B CZ2 1 
ATOM   3011 C  CZ3 . TRP B 1 123 ? -8.569  61.660 55.988 1.00 28.60 ? 123 TRP B CZ3 1 
ATOM   3012 C  CH2 . TRP B 1 123 ? -8.058  60.626 55.197 1.00 24.99 ? 123 TRP B CH2 1 
ATOM   3013 N  N   . ASN B 1 124 ? -7.298  64.490 59.721 1.00 21.25 ? 124 ASN B N   1 
ATOM   3014 C  CA  . ASN B 1 124 ? -8.407  63.922 60.513 1.00 23.19 ? 124 ASN B CA  1 
ATOM   3015 C  C   . ASN B 1 124 ? -9.248  62.912 59.708 1.00 24.42 ? 124 ASN B C   1 
ATOM   3016 O  O   . ASN B 1 124 ? -10.130 63.316 58.949 1.00 28.91 ? 124 ASN B O   1 
ATOM   3017 C  CB  . ASN B 1 124 ? -9.307  65.077 60.967 1.00 22.58 ? 124 ASN B CB  1 
ATOM   3018 C  CG  . ASN B 1 124 ? -10.302 64.649 62.026 1.00 26.60 ? 124 ASN B CG  1 
ATOM   3019 O  OD1 . ASN B 1 124 ? -10.610 63.459 62.150 1.00 24.82 ? 124 ASN B OD1 1 
ATOM   3020 N  ND2 . ASN B 1 124 ? -10.780 65.625 62.842 1.00 26.34 ? 124 ASN B ND2 1 
ATOM   3021 N  N   . SER B 1 125 ? -8.974  61.635 59.925 1.00 26.35 ? 125 SER B N   1 
ATOM   3022 C  CA  . SER B 1 125 ? -9.672  60.599 59.146 1.00 31.09 ? 125 SER B CA  1 
ATOM   3023 C  C   . SER B 1 125 ? -10.952 60.141 59.852 1.00 30.74 ? 125 SER B C   1 
ATOM   3024 O  O   . SER B 1 125 ? -11.712 59.307 59.338 1.00 31.49 ? 125 SER B O   1 
ATOM   3025 C  CB  . SER B 1 125 ? -8.719  59.474 58.876 1.00 28.57 ? 125 SER B CB  1 
ATOM   3026 O  OG  . SER B 1 125 ? -8.318  58.815 60.071 1.00 29.17 ? 125 SER B OG  1 
ATOM   3027 N  N   . ALA B 1 126 ? -11.206 60.658 61.045 1.00 30.88 ? 126 ALA B N   1 
ATOM   3028 C  CA  . ALA B 1 126 ? -12.503 60.406 61.695 1.00 31.80 ? 126 ALA B CA  1 
ATOM   3029 C  C   . ALA B 1 126 ? -13.584 61.271 61.075 1.00 32.92 ? 126 ALA B C   1 
ATOM   3030 O  O   . ALA B 1 126 ? -14.716 60.809 60.869 1.00 34.28 ? 126 ALA B O   1 
ATOM   3031 C  CB  . ALA B 1 126 ? -12.413 60.608 63.210 1.00 31.36 ? 126 ALA B CB  1 
ATOM   3032 N  N   . LYS B 1 127 ? -13.250 62.512 60.746 1.00 29.25 ? 127 LYS B N   1 
ATOM   3033 C  CA  . LYS B 1 127 ? -14.208 63.456 60.194 1.00 35.37 ? 127 LYS B CA  1 
ATOM   3034 C  C   . LYS B 1 127 ? -14.162 63.526 58.683 1.00 38.93 ? 127 LYS B C   1 
ATOM   3035 O  O   . LYS B 1 127 ? -15.181 63.796 58.051 1.00 33.77 ? 127 LYS B O   1 
ATOM   3036 C  CB  . LYS B 1 127 ? -13.991 64.884 60.723 1.00 40.19 ? 127 LYS B CB  1 
ATOM   3037 C  CG  . LYS B 1 127 ? -14.260 65.043 62.208 1.00 43.70 ? 127 LYS B CG  1 
ATOM   3038 C  CD  . LYS B 1 127 ? -14.380 66.508 62.610 1.00 45.99 ? 127 LYS B CD  1 
ATOM   3039 C  CE  . LYS B 1 127 ? -15.767 67.066 62.354 1.00 50.65 ? 127 LYS B CE  1 
ATOM   3040 N  NZ  . LYS B 1 127 ? -15.776 68.543 62.099 1.00 51.08 ? 127 LYS B NZ  1 
ATOM   3041 N  N   . TYR B 1 128 ? -12.988 63.271 58.104 1.00 34.16 ? 128 TYR B N   1 
ATOM   3042 C  CA  . TYR B 1 128 ? -12.807 63.418 56.668 1.00 34.58 ? 128 TYR B CA  1 
ATOM   3043 C  C   . TYR B 1 128 ? -12.365 62.124 55.988 1.00 32.84 ? 128 TYR B C   1 
ATOM   3044 O  O   . TYR B 1 128 ? -12.012 61.133 56.691 1.00 35.97 ? 128 TYR B O   1 
ATOM   3045 C  CB  . TYR B 1 128 ? -11.867 64.621 56.389 1.00 34.64 ? 128 TYR B CB  1 
ATOM   3046 C  CG  . TYR B 1 128 ? -12.345 65.807 57.139 1.00 38.71 ? 128 TYR B CG  1 
ATOM   3047 C  CD1 . TYR B 1 128 ? -13.610 66.331 56.907 1.00 38.65 ? 128 TYR B CD1 1 
ATOM   3048 C  CD2 . TYR B 1 128 ? -11.572 66.369 58.178 1.00 39.72 ? 128 TYR B CD2 1 
ATOM   3049 C  CE1 . TYR B 1 128 ? -14.088 67.393 57.627 1.00 37.44 ? 128 TYR B CE1 1 
ATOM   3050 C  CE2 . TYR B 1 128 ? -12.054 67.438 58.906 1.00 33.87 ? 128 TYR B CE2 1 
ATOM   3051 C  CZ  . TYR B 1 128 ? -13.308 67.945 58.627 1.00 41.47 ? 128 TYR B CZ  1 
ATOM   3052 O  OH  . TYR B 1 128 ? -13.785 69.020 59.329 1.00 36.86 ? 128 TYR B OH  1 
ATOM   3053 N  N   . SER B 1 129 ? -12.355 62.168 54.644 1.00 39.20 ? 129 SER B N   1 
ATOM   3054 C  CA  . SER B 1 129 ? -12.127 61.049 53.708 1.00 39.97 ? 129 SER B CA  1 
ATOM   3055 C  C   . SER B 1 129 ? -10.772 61.087 53.073 1.00 38.06 ? 129 SER B C   1 
ATOM   3056 O  O   . SER B 1 129 ? -10.288 60.060 52.646 1.00 32.76 ? 129 SER B O   1 
ATOM   3057 C  CB  . SER B 1 129 ? -13.066 61.149 52.490 1.00 44.74 ? 129 SER B CB  1 
ATOM   3058 O  OG  . SER B 1 129 ? -14.396 61.337 52.859 1.00 50.67 ? 129 SER B OG  1 
ATOM   3059 N  N   . SER B 1 130 ? -10.191 62.289 52.945 1.00 36.68 ? 130 SER B N   1 
ATOM   3060 C  CA  . SER B 1 130 ? -8.926  62.467 52.239 1.00 30.87 ? 130 SER B CA  1 
ATOM   3061 C  C   . SER B 1 130 ? -8.216  63.687 52.788 1.00 24.18 ? 130 SER B C   1 
ATOM   3062 O  O   . SER B 1 130 ? -8.875  64.565 53.376 1.00 25.87 ? 130 SER B O   1 
ATOM   3063 C  CB  . SER B 1 130 ? -9.174  62.742 50.747 1.00 30.78 ? 130 SER B CB  1 
ATOM   3064 O  OG  . SER B 1 130 ? -9.863  63.960 50.588 1.00 35.86 ? 130 SER B OG  1 
ATOM   3065 N  N   . LEU B 1 131 ? -6.922  63.722 52.540 1.00 27.97 ? 131 LEU B N   1 
ATOM   3066 C  CA  . LEU B 1 131 ? -6.094  64.901 52.830 1.00 23.00 ? 131 LEU B CA  1 
ATOM   3067 C  C   . LEU B 1 131 ? -6.572  66.141 52.102 1.00 26.97 ? 131 LEU B C   1 
ATOM   3068 O  O   . LEU B 1 131 ? -6.677  67.222 52.673 1.00 26.25 ? 131 LEU B O   1 
ATOM   3069 C  CB  . LEU B 1 131 ? -4.624  64.608 52.509 1.00 23.18 ? 131 LEU B CB  1 
ATOM   3070 C  CG  . LEU B 1 131 ? -3.703  65.810 52.657 1.00 21.84 ? 131 LEU B CG  1 
ATOM   3071 C  CD1 . LEU B 1 131 ? -3.598  66.246 54.131 1.00 21.17 ? 131 LEU B CD1 1 
ATOM   3072 C  CD2 . LEU B 1 131 ? -2.297  65.554 52.080 1.00 21.38 ? 131 LEU B CD2 1 
ATOM   3073 N  N   . ALA B 1 132 ? -6.968  65.963 50.839 1.00 26.82 ? 132 ALA B N   1 
ATOM   3074 C  CA  . ALA B 1 132 ? -7.551  67.065 50.066 1.00 30.06 ? 132 ALA B CA  1 
ATOM   3075 C  C   . ALA B 1 132 ? -8.760  67.662 50.788 1.00 27.46 ? 132 ALA B C   1 
ATOM   3076 O  O   . ALA B 1 132 ? -8.872  68.886 50.868 1.00 32.08 ? 132 ALA B O   1 
ATOM   3077 C  CB  . ALA B 1 132 ? -7.899  66.588 48.643 1.00 26.28 ? 132 ALA B CB  1 
ATOM   3078 N  N   . GLU B 1 133 ? -9.644  66.821 51.329 1.00 29.90 ? 133 GLU B N   1 
ATOM   3079 C  CA  . GLU B 1 133 ? -10.832 67.300 52.040 1.00 27.59 ? 133 GLU B CA  1 
ATOM   3080 C  C   . GLU B 1 133 ? -10.443 67.926 53.433 1.00 30.65 ? 133 GLU B C   1 
ATOM   3081 O  O   . GLU B 1 133 ? -11.018 68.934 53.838 1.00 33.80 ? 133 GLU B O   1 
ATOM   3082 C  CB  . GLU B 1 133 ? -11.758 66.117 52.310 1.00 31.97 ? 133 GLU B CB  1 
ATOM   3083 C  CG  . GLU B 1 133 ? -12.951 66.461 53.178 1.00 31.72 ? 133 GLU B CG  1 
ATOM   3084 C  CD  . GLU B 1 133 ? -13.968 65.347 53.328 1.00 34.99 ? 133 GLU B CD  1 
ATOM   3085 O  OE1 . GLU B 1 133 ? -13.620 64.107 53.459 1.00 35.78 ? 133 GLU B OE1 1 
ATOM   3086 O  OE2 . GLU B 1 133 ? -15.131 65.781 53.385 1.00 43.50 ? 133 GLU B OE2 1 
ATOM   3087 N  N   . ALA B 1 134 ? -9.520  67.274 54.155 1.00 27.87 ? 134 ALA B N   1 
ATOM   3088 C  CA  . ALA B 1 134 ? -9.175  67.675 55.560 1.00 24.91 ? 134 ALA B CA  1 
ATOM   3089 C  C   . ALA B 1 134 ? -8.385  69.016 55.585 1.00 25.14 ? 134 ALA B C   1 
ATOM   3090 O  O   . ALA B 1 134 ? -8.509  69.773 56.556 1.00 27.54 ? 134 ALA B O   1 
ATOM   3091 C  CB  . ALA B 1 134 ? -8.385  66.587 56.269 1.00 22.32 ? 134 ALA B CB  1 
ATOM   3092 N  N   . ALA B 1 135 ? -7.605  69.350 54.552 1.00 25.26 ? 135 ALA B N   1 
ATOM   3093 C  CA  . ALA B 1 135 ? -6.508  70.345 54.696 1.00 26.43 ? 135 ALA B CA  1 
ATOM   3094 C  C   . ALA B 1 135 ? -6.939  71.760 54.963 1.00 27.18 ? 135 ALA B C   1 
ATOM   3095 O  O   . ALA B 1 135 ? -6.172  72.518 55.531 1.00 27.15 ? 135 ALA B O   1 
ATOM   3096 C  CB  . ALA B 1 135 ? -5.540  70.330 53.505 1.00 27.85 ? 135 ALA B CB  1 
ATOM   3097 N  N   . SER B 1 136 ? -8.114  72.151 54.482 1.00 30.13 ? 136 SER B N   1 
ATOM   3098 C  CA  . SER B 1 136 ? -8.603  73.507 54.727 1.00 31.86 ? 136 SER B CA  1 
ATOM   3099 C  C   . SER B 1 136 ? -9.539  73.587 55.929 1.00 29.13 ? 136 SER B C   1 
ATOM   3100 O  O   . SER B 1 136 ? -10.106 74.639 56.169 1.00 33.01 ? 136 SER B O   1 
ATOM   3101 C  CB  . SER B 1 136 ? -9.297  74.105 53.477 1.00 35.85 ? 136 SER B CB  1 
ATOM   3102 O  OG  . SER B 1 136 ? -10.352 73.271 53.084 1.00 35.92 ? 136 SER B OG  1 
ATOM   3103 N  N   . LYS B 1 137 ? -9.761  72.511 56.687 1.00 26.22 ? 137 LYS B N   1 
ATOM   3104 C  CA  . LYS B 1 137 ? -10.775 72.595 57.737 1.00 26.25 ? 137 LYS B CA  1 
ATOM   3105 C  C   . LYS B 1 137 ? -10.091 72.892 59.065 1.00 28.57 ? 137 LYS B C   1 
ATOM   3106 O  O   . LYS B 1 137 ? -9.006  72.372 59.291 1.00 22.92 ? 137 LYS B O   1 
ATOM   3107 C  CB  . LYS B 1 137 ? -11.474 71.263 57.887 1.00 24.44 ? 137 LYS B CB  1 
ATOM   3108 C  CG  . LYS B 1 137 ? -11.827 70.699 56.509 1.00 36.18 ? 137 LYS B CG  1 
ATOM   3109 C  CD  . LYS B 1 137 ? -12.982 71.464 55.909 1.00 41.54 ? 137 LYS B CD  1 
ATOM   3110 C  CE  . LYS B 1 137 ? -14.226 70.615 56.070 1.00 48.05 ? 137 LYS B CE  1 
ATOM   3111 N  NZ  . LYS B 1 137 ? -15.079 70.874 54.883 1.00 51.00 ? 137 LYS B NZ  1 
ATOM   3112 N  N   . ALA B 1 138 ? -10.738 73.670 59.937 1.00 28.33 ? 138 ALA B N   1 
ATOM   3113 C  CA  . ALA B 1 138 ? -10.072 74.091 61.186 1.00 28.19 ? 138 ALA B CA  1 
ATOM   3114 C  C   . ALA B 1 138 ? -9.569  72.924 62.015 1.00 27.59 ? 138 ALA B C   1 
ATOM   3115 O  O   . ALA B 1 138 ? -8.565  73.066 62.688 1.00 27.70 ? 138 ALA B O   1 
ATOM   3116 C  CB  . ALA B 1 138 ? -10.969 74.996 62.057 1.00 31.04 ? 138 ALA B CB  1 
ATOM   3117 N  N   . ASP B 1 139 ? -10.306 71.817 62.022 1.00 24.47 ? 139 ASP B N   1 
ATOM   3118 C  CA  . ASP B 1 139 ? -9.983  70.610 62.755 1.00 25.16 ? 139 ASP B CA  1 
ATOM   3119 C  C   . ASP B 1 139 ? -9.358  69.522 61.831 1.00 24.07 ? 139 ASP B C   1 
ATOM   3120 O  O   . ASP B 1 139 ? -9.372  68.328 62.150 1.00 25.72 ? 139 ASP B O   1 
ATOM   3121 C  CB  . ASP B 1 139 ? -11.219 70.081 63.507 1.00 31.28 ? 139 ASP B CB  1 
ATOM   3122 C  CG  . ASP B 1 139 ? -12.392 69.758 62.581 1.00 34.91 ? 139 ASP B CG  1 
ATOM   3123 O  OD1 . ASP B 1 139 ? -12.359 70.079 61.379 1.00 38.25 ? 139 ASP B OD1 1 
ATOM   3124 O  OD2 . ASP B 1 139 ? -13.388 69.206 63.105 1.00 37.25 ? 139 ASP B OD2 1 
ATOM   3125 N  N   . GLY B 1 140 ? -8.782  69.967 60.713 1.00 25.12 ? 140 GLY B N   1 
ATOM   3126 C  CA  . GLY B 1 140 ? -8.369  68.985 59.687 1.00 21.78 ? 140 GLY B CA  1 
ATOM   3127 C  C   . GLY B 1 140 ? -7.016  68.352 59.837 1.00 22.88 ? 140 GLY B C   1 
ATOM   3128 O  O   . GLY B 1 140 ? -6.836  67.148 59.499 1.00 19.73 ? 140 GLY B O   1 
ATOM   3129 N  N   . LEU B 1 141 ? -6.048  69.148 60.353 1.00 17.58 ? 141 LEU B N   1 
ATOM   3130 C  CA  . LEU B 1 141 ? -4.651  68.706 60.364 1.00 18.03 ? 141 LEU B CA  1 
ATOM   3131 C  C   . LEU B 1 141 ? -4.088  68.737 61.792 1.00 17.21 ? 141 LEU B C   1 
ATOM   3132 O  O   . LEU B 1 141 ? -4.562  69.508 62.634 1.00 18.15 ? 141 LEU B O   1 
ATOM   3133 C  CB  . LEU B 1 141 ? -3.829  69.534 59.383 1.00 15.73 ? 141 LEU B CB  1 
ATOM   3134 C  CG  . LEU B 1 141 ? -4.285  69.650 57.924 1.00 17.70 ? 141 LEU B CG  1 
ATOM   3135 C  CD1 . LEU B 1 141 ? -3.247  70.566 57.250 1.00 14.74 ? 141 LEU B CD1 1 
ATOM   3136 C  CD2 . LEU B 1 141 ? -4.265  68.191 57.392 1.00 16.58 ? 141 LEU B CD2 1 
ATOM   3137 N  N   . ALA B 1 142 ? -3.133  67.870 62.064 1.00 17.88 ? 142 ALA B N   1 
ATOM   3138 C  CA  . ALA B 1 142 ? -2.400  67.894 63.331 1.00 14.63 ? 142 ALA B CA  1 
ATOM   3139 C  C   . ALA B 1 142 ? -0.951  67.681 62.992 1.00 17.07 ? 142 ALA B C   1 
ATOM   3140 O  O   . ALA B 1 142 ? -0.596  66.732 62.257 1.00 15.50 ? 142 ALA B O   1 
ATOM   3141 C  CB  . ALA B 1 142 ? -2.868  66.723 64.176 1.00 15.71 ? 142 ALA B CB  1 
ATOM   3142 N  N   . VAL B 1 143 ? -0.088  68.562 63.454 1.00 14.02 ? 143 VAL B N   1 
ATOM   3143 C  CA  . VAL B 1 143 ? 1.309   68.419 63.116 1.00 14.55 ? 143 VAL B CA  1 
ATOM   3144 C  C   . VAL B 1 143 ? 2.103   68.396 64.440 1.00 14.06 ? 143 VAL B C   1 
ATOM   3145 O  O   . VAL B 1 143 ? 1.906   69.309 65.305 1.00 13.77 ? 143 VAL B O   1 
ATOM   3146 C  CB  . VAL B 1 143 ? 1.814   69.574 62.200 1.00 13.37 ? 143 VAL B CB  1 
ATOM   3147 C  CG1 . VAL B 1 143 ? 3.322   69.336 61.858 1.00 13.95 ? 143 VAL B CG1 1 
ATOM   3148 C  CG2 . VAL B 1 143 ? 1.020   69.614 60.901 1.00 14.55 ? 143 VAL B CG2 1 
ATOM   3149 N  N   . ILE B 1 144 ? 3.002   67.431 64.586 1.00 12.86 ? 144 ILE B N   1 
ATOM   3150 C  CA  . ILE B 1 144 ? 3.950   67.398 65.745 1.00 12.47 ? 144 ILE B CA  1 
ATOM   3151 C  C   . ILE B 1 144 ? 5.203   68.108 65.288 1.00 12.60 ? 144 ILE B C   1 
ATOM   3152 O  O   . ILE B 1 144 ? 5.729   67.772 64.268 1.00 12.09 ? 144 ILE B O   1 
ATOM   3153 C  CB  . ILE B 1 144 ? 4.361   65.968 66.093 1.00 14.30 ? 144 ILE B CB  1 
ATOM   3154 C  CG1 . ILE B 1 144 ? 3.094   65.180 66.510 1.00 15.77 ? 144 ILE B CG1 1 
ATOM   3155 C  CG2 . ILE B 1 144 ? 5.450   66.022 67.263 1.00 12.73 ? 144 ILE B CG2 1 
ATOM   3156 C  CD1 . ILE B 1 144 ? 3.324   63.685 66.703 1.00 15.61 ? 144 ILE B CD1 1 
ATOM   3157 N  N   . GLY B 1 145 ? 5.704   69.091 66.071 1.00 13.32 ? 145 GLY B N   1 
ATOM   3158 C  CA  . GLY B 1 145 ? 6.980   69.717 65.770 1.00 12.22 ? 145 GLY B CA  1 
ATOM   3159 C  C   . GLY B 1 145 ? 7.920   69.286 66.901 1.00 14.03 ? 145 GLY B C   1 
ATOM   3160 O  O   . GLY B 1 145 ? 7.550   69.269 68.118 1.00 14.57 ? 145 GLY B O   1 
ATOM   3161 N  N   . VAL B 1 146 ? 9.165   68.996 66.499 1.00 12.17 ? 146 VAL B N   1 
ATOM   3162 C  CA  . VAL B 1 146 ? 10.274  68.705 67.367 1.00 13.30 ? 146 VAL B CA  1 
ATOM   3163 C  C   . VAL B 1 146 ? 11.421  69.655 67.053 1.00 14.41 ? 146 VAL B C   1 
ATOM   3164 O  O   . VAL B 1 146 ? 11.935  69.665 65.918 1.00 14.83 ? 146 VAL B O   1 
ATOM   3165 C  CB  . VAL B 1 146 ? 10.773  67.243 67.141 1.00 12.73 ? 146 VAL B CB  1 
ATOM   3166 C  CG1 . VAL B 1 146 ? 11.849  66.928 68.194 1.00 13.50 ? 146 VAL B CG1 1 
ATOM   3167 C  CG2 . VAL B 1 146 ? 9.558   66.280 67.269 1.00 13.14 ? 146 VAL B CG2 1 
ATOM   3168 N  N   . LEU B 1 147 ? 11.859  70.438 68.031 1.00 14.06 ? 147 LEU B N   1 
ATOM   3169 C  CA  . LEU B 1 147 ? 13.002  71.303 67.873 1.00 13.83 ? 147 LEU B CA  1 
ATOM   3170 C  C   . LEU B 1 147 ? 14.282  70.492 67.811 1.00 15.11 ? 147 LEU B C   1 
ATOM   3171 O  O   . LEU B 1 147 ? 14.464  69.526 68.586 1.00 13.28 ? 147 LEU B O   1 
ATOM   3172 C  CB  . LEU B 1 147 ? 13.032  72.300 69.046 1.00 13.43 ? 147 LEU B CB  1 
ATOM   3173 C  CG  . LEU B 1 147 ? 11.745  73.154 69.111 1.00 16.09 ? 147 LEU B CG  1 
ATOM   3174 C  CD1 . LEU B 1 147 ? 11.540  73.629 70.550 1.00 20.57 ? 147 LEU B CD1 1 
ATOM   3175 C  CD2 . LEU B 1 147 ? 11.898  74.218 67.993 1.00 19.78 ? 147 LEU B CD2 1 
ATOM   3176 N  N   . MET B 1 148 ? 15.187  70.906 66.927 1.00 14.70 ? 148 MET B N   1 
ATOM   3177 C  CA  . MET B 1 148 ? 16.452  70.173 66.739 1.00 14.02 ? 148 MET B CA  1 
ATOM   3178 C  C   . MET B 1 148 ? 17.629  71.076 67.092 1.00 15.97 ? 148 MET B C   1 
ATOM   3179 O  O   . MET B 1 148 ? 17.686  72.218 66.639 1.00 17.15 ? 148 MET B O   1 
ATOM   3180 C  CB  . MET B 1 148 ? 16.572  69.745 65.253 1.00 15.44 ? 148 MET B CB  1 
ATOM   3181 C  CG  . MET B 1 148 ? 15.467  68.764 64.906 1.00 14.54 ? 148 MET B CG  1 
ATOM   3182 S  SD  . MET B 1 148 ? 15.337  68.386 63.103 1.00 17.07 ? 148 MET B SD  1 
ATOM   3183 C  CE  . MET B 1 148 ? 16.830  67.349 63.005 1.00 19.44 ? 148 MET B CE  1 
ATOM   3184 N  N   . LYS B 1 149 ? 18.502  70.605 67.963 1.00 15.35 ? 149 LYS B N   1 
ATOM   3185 C  CA  . LYS B 1 149 ? 19.562  71.439 68.488 1.00 17.62 ? 149 LYS B CA  1 
ATOM   3186 C  C   . LYS B 1 149 ? 20.933  70.913 67.961 1.00 17.67 ? 149 LYS B C   1 
ATOM   3187 O  O   . LYS B 1 149 ? 21.246  69.712 68.090 1.00 18.19 ? 149 LYS B O   1 
ATOM   3188 C  CB  . LYS B 1 149 ? 19.462  71.424 70.021 1.00 22.85 ? 149 LYS B CB  1 
ATOM   3189 C  CG  . LYS B 1 149 ? 20.649  71.989 70.778 1.00 29.20 ? 149 LYS B CG  1 
ATOM   3190 C  CD  . LYS B 1 149 ? 20.242  72.020 72.258 1.00 33.68 ? 149 LYS B CD  1 
ATOM   3191 C  CE  . LYS B 1 149 ? 20.813  73.261 72.967 1.00 45.93 ? 149 LYS B CE  1 
ATOM   3192 N  NZ  . LYS B 1 149 ? 22.290  73.102 73.110 1.00 41.44 ? 149 LYS B NZ  1 
ATOM   3193 N  N   . VAL B 1 150 ? 21.735  71.787 67.410 1.00 17.78 ? 150 VAL B N   1 
ATOM   3194 C  CA  . VAL B 1 150 ? 22.988  71.335 66.778 1.00 18.63 ? 150 VAL B CA  1 
ATOM   3195 C  C   . VAL B 1 150 ? 23.913  70.784 67.879 1.00 21.63 ? 150 VAL B C   1 
ATOM   3196 O  O   . VAL B 1 150 ? 23.994  71.389 68.972 1.00 20.87 ? 150 VAL B O   1 
ATOM   3197 C  CB  . VAL B 1 150 ? 23.669  72.446 65.927 1.00 20.17 ? 150 VAL B CB  1 
ATOM   3198 C  CG1 . VAL B 1 150 ? 24.209  73.617 66.802 1.00 23.69 ? 150 VAL B CG1 1 
ATOM   3199 C  CG2 . VAL B 1 150 ? 24.770  71.837 65.031 1.00 23.11 ? 150 VAL B CG2 1 
ATOM   3200 N  N   . GLY B 1 151 ? 24.543  69.650 67.626 1.00 19.99 ? 151 GLY B N   1 
ATOM   3201 C  CA  . GLY B 1 151 ? 25.432  69.033 68.588 1.00 20.53 ? 151 GLY B CA  1 
ATOM   3202 C  C   . GLY B 1 151 ? 25.914  67.746 68.019 1.00 21.47 ? 151 GLY B C   1 
ATOM   3203 O  O   . GLY B 1 151 ? 26.423  67.749 66.911 1.00 23.63 ? 151 GLY B O   1 
ATOM   3204 N  N   A GLU B 1 152 ? 25.708  66.638 68.747 0.50 21.06 ? 152 GLU B N   1 
ATOM   3205 N  N   B GLU B 1 152 ? 25.707  66.631 68.720 0.50 21.72 ? 152 GLU B N   1 
ATOM   3206 C  CA  A GLU B 1 152 ? 26.029  65.273 68.280 0.50 21.80 ? 152 GLU B CA  1 
ATOM   3207 C  CA  B GLU B 1 152 ? 26.158  65.327 68.222 0.50 22.51 ? 152 GLU B CA  1 
ATOM   3208 C  C   A GLU B 1 152 ? 25.314  64.967 66.966 0.50 21.83 ? 152 GLU B C   1 
ATOM   3209 C  C   B GLU B 1 152 ? 25.274  64.781 67.085 0.50 22.72 ? 152 GLU B C   1 
ATOM   3210 O  O   A GLU B 1 152 ? 24.172  65.408 66.760 0.50 18.01 ? 152 GLU B O   1 
ATOM   3211 O  O   B GLU B 1 152 ? 24.016  64.892 67.098 0.50 18.26 ? 152 GLU B O   1 
ATOM   3212 C  CB  A GLU B 1 152 ? 25.472  64.206 69.259 0.50 23.46 ? 152 GLU B CB  1 
ATOM   3213 C  CB  B GLU B 1 152 ? 26.179  64.278 69.347 0.50 26.15 ? 152 GLU B CB  1 
ATOM   3214 C  CG  A GLU B 1 152 ? 26.212  63.860 70.552 0.50 29.15 ? 152 GLU B CG  1 
ATOM   3215 C  CG  B GLU B 1 152 ? 26.878  64.681 70.655 0.50 31.34 ? 152 GLU B CG  1 
ATOM   3216 C  CD  A GLU B 1 152 ? 26.019  62.396 70.937 0.50 31.65 ? 152 GLU B CD  1 
ATOM   3217 C  CD  B GLU B 1 152 ? 28.374  64.902 70.532 0.50 34.41 ? 152 GLU B CD  1 
ATOM   3218 O  OE1 A GLU B 1 152 ? 24.896  61.992 71.322 0.50 36.09 ? 152 GLU B OE1 1 
ATOM   3219 O  OE1 B GLU B 1 152 ? 28.810  65.717 69.693 0.50 38.87 ? 152 GLU B OE1 1 
ATOM   3220 O  OE2 A GLU B 1 152 ? 26.992  61.625 70.830 0.50 34.36 ? 152 GLU B OE2 1 
ATOM   3221 O  OE2 B GLU B 1 152 ? 29.133  64.297 71.327 0.50 39.43 ? 152 GLU B OE2 1 
ATOM   3222 N  N   . ALA B 1 153 ? 25.924  64.138 66.114 1.00 19.98 ? 153 ALA B N   1 
ATOM   3223 C  CA  . ALA B 1 153 ? 25.160  63.501 65.014 1.00 21.14 ? 153 ALA B CA  1 
ATOM   3224 C  C   . ALA B 1 153 ? 24.041  62.645 65.471 1.00 20.71 ? 153 ALA B C   1 
ATOM   3225 O  O   . ALA B 1 153 ? 24.186  61.873 66.418 1.00 23.42 ? 153 ALA B O   1 
ATOM   3226 C  CB  . ALA B 1 153 ? 26.092  62.634 64.143 1.00 21.44 ? 153 ALA B CB  1 
ATOM   3227 N  N   . ASN B 1 154 ? 22.884  62.730 64.809 1.00 20.05 ? 154 ASN B N   1 
ATOM   3228 C  CA  . ASN B 1 154 ? 21.737  61.938 65.198 1.00 18.56 ? 154 ASN B CA  1 
ATOM   3229 C  C   . ASN B 1 154 ? 21.636  60.729 64.306 1.00 20.19 ? 154 ASN B C   1 
ATOM   3230 O  O   . ASN B 1 154 ? 21.282  60.861 63.131 1.00 18.37 ? 154 ASN B O   1 
ATOM   3231 C  CB  . ASN B 1 154 ? 20.456  62.813 65.065 1.00 20.08 ? 154 ASN B CB  1 
ATOM   3232 C  CG  . ASN B 1 154 ? 19.207  62.159 65.619 1.00 21.43 ? 154 ASN B CG  1 
ATOM   3233 O  OD1 . ASN B 1 154 ? 19.065  60.928 65.654 1.00 21.39 ? 154 ASN B OD1 1 
ATOM   3234 N  ND2 . ASN B 1 154 ? 18.200  63.026 66.010 1.00 18.79 ? 154 ASN B ND2 1 
ATOM   3235 N  N   . PRO B 1 155 ? 21.952  59.546 64.847 1.00 20.56 ? 155 PRO B N   1 
ATOM   3236 C  CA  . PRO B 1 155 ? 21.923  58.397 63.982 1.00 21.25 ? 155 PRO B CA  1 
ATOM   3237 C  C   . PRO B 1 155 ? 20.552  58.019 63.431 1.00 22.94 ? 155 PRO B C   1 
ATOM   3238 O  O   . PRO B 1 155 ? 20.506  57.324 62.388 1.00 23.30 ? 155 PRO B O   1 
ATOM   3239 C  CB  . PRO B 1 155 ? 22.490  57.254 64.872 1.00 26.65 ? 155 PRO B CB  1 
ATOM   3240 C  CG  . PRO B 1 155 ? 22.316  57.689 66.259 1.00 24.08 ? 155 PRO B CG  1 
ATOM   3241 C  CD  . PRO B 1 155 ? 22.147  59.195 66.266 1.00 23.12 ? 155 PRO B CD  1 
ATOM   3242 N  N   . LYS B 1 156 ? 19.444  58.420 64.088 1.00 21.14 ? 156 LYS B N   1 
ATOM   3243 C  CA  . LYS B 1 156 ? 18.085  58.107 63.598 1.00 21.43 ? 156 LYS B CA  1 
ATOM   3244 C  C   . LYS B 1 156 ? 17.747  58.749 62.260 1.00 19.81 ? 156 LYS B C   1 
ATOM   3245 O  O   . LYS B 1 156 ? 16.825  58.322 61.600 1.00 21.26 ? 156 LYS B O   1 
ATOM   3246 C  CB  . LYS B 1 156 ? 16.955  58.456 64.579 1.00 27.14 ? 156 LYS B CB  1 
ATOM   3247 C  CG  . LYS B 1 156 ? 17.192  58.019 66.030 1.00 32.62 ? 156 LYS B CG  1 
ATOM   3248 C  CD  . LYS B 1 156 ? 16.745  56.643 66.404 1.00 35.90 ? 156 LYS B CD  1 
ATOM   3249 C  CE  . LYS B 1 156 ? 16.823  56.595 67.939 1.00 37.80 ? 156 LYS B CE  1 
ATOM   3250 N  NZ  . LYS B 1 156 ? 15.601  57.179 68.603 1.00 39.92 ? 156 LYS B NZ  1 
ATOM   3251 N  N   . LEU B 1 157 ? 18.483  59.777 61.916 1.00 19.91 ? 157 LEU B N   1 
ATOM   3252 C  CA  . LEU B 1 157 ? 18.308  60.525 60.636 1.00 18.96 ? 157 LEU B CA  1 
ATOM   3253 C  C   . LEU B 1 157 ? 18.941  59.816 59.433 1.00 26.63 ? 157 LEU B C   1 
ATOM   3254 O  O   . LEU B 1 157 ? 18.805  60.268 58.294 1.00 22.98 ? 157 LEU B O   1 
ATOM   3255 C  CB  . LEU B 1 157 ? 18.975  61.876 60.749 1.00 22.33 ? 157 LEU B CB  1 
ATOM   3256 C  CG  . LEU B 1 157 ? 18.341  62.835 61.699 1.00 16.76 ? 157 LEU B CG  1 
ATOM   3257 C  CD1 . LEU B 1 157 ? 19.055  64.142 61.541 1.00 16.75 ? 157 LEU B CD1 1 
ATOM   3258 C  CD2 . LEU B 1 157 ? 16.892  63.037 61.282 1.00 19.33 ? 157 LEU B CD2 1 
ATOM   3259 N  N   . GLN B 1 158 ? 19.677  58.744 59.698 1.00 28.17 ? 158 GLN B N   1 
ATOM   3260 C  CA  . GLN B 1 158 ? 20.492  58.070 58.675 1.00 27.86 ? 158 GLN B CA  1 
ATOM   3261 C  C   . GLN B 1 158 ? 19.741  57.666 57.420 1.00 24.49 ? 158 GLN B C   1 
ATOM   3262 O  O   . GLN B 1 158 ? 20.251  57.995 56.346 1.00 25.59 ? 158 GLN B O   1 
ATOM   3263 C  CB  . GLN B 1 158 ? 21.211  56.824 59.253 1.00 31.28 ? 158 GLN B CB  1 
ATOM   3264 C  CG  . GLN B 1 158 ? 22.170  56.113 58.268 1.00 37.44 ? 158 GLN B CG  1 
ATOM   3265 C  CD  . GLN B 1 158 ? 23.410  56.957 57.930 1.00 43.02 ? 158 GLN B CD  1 
ATOM   3266 O  OE1 . GLN B 1 158 ? 23.642  58.029 58.505 1.00 47.50 ? 158 GLN B OE1 1 
ATOM   3267 N  NE2 . GLN B 1 158 ? 24.200  56.477 56.965 1.00 49.52 ? 158 GLN B NE2 1 
ATOM   3268 N  N   . LYS B 1 159 ? 18.590  56.986 57.522 1.00 21.80 ? 159 LYS B N   1 
ATOM   3269 C  CA  . LYS B 1 159 ? 17.908  56.465 56.299 1.00 25.63 ? 159 LYS B CA  1 
ATOM   3270 C  C   . LYS B 1 159 ? 17.453  57.652 55.455 1.00 25.37 ? 159 LYS B C   1 
ATOM   3271 O  O   . LYS B 1 159 ? 17.524  57.623 54.209 1.00 22.89 ? 159 LYS B O   1 
ATOM   3272 C  CB  . LYS B 1 159 ? 16.785  55.446 56.604 1.00 29.42 ? 159 LYS B CB  1 
ATOM   3273 C  CG  . LYS B 1 159 ? 15.960  54.973 55.364 1.00 26.83 ? 159 LYS B CG  1 
ATOM   3274 C  CD  . LYS B 1 159 ? 14.604  54.354 55.732 1.00 28.32 ? 159 LYS B CD  1 
ATOM   3275 C  CE  . LYS B 1 159 ? 13.867  53.911 54.477 1.00 30.87 ? 159 LYS B CE  1 
ATOM   3276 N  NZ  . LYS B 1 159 ? 14.511  52.645 53.991 1.00 31.12 ? 159 LYS B NZ  1 
ATOM   3277 N  N   . VAL B 1 160 ? 17.052  58.731 56.150 1.00 21.84 ? 160 VAL B N   1 
ATOM   3278 C  CA  . VAL B 1 160 ? 16.620  59.933 55.456 1.00 20.56 ? 160 VAL B CA  1 
ATOM   3279 C  C   . VAL B 1 160 ? 17.781  60.586 54.761 1.00 20.16 ? 160 VAL B C   1 
ATOM   3280 O  O   . VAL B 1 160 ? 17.683  60.915 53.601 1.00 20.92 ? 160 VAL B O   1 
ATOM   3281 C  CB  . VAL B 1 160 ? 16.007  60.981 56.439 1.00 20.08 ? 160 VAL B CB  1 
ATOM   3282 C  CG1 . VAL B 1 160 ? 15.591  62.215 55.654 1.00 22.60 ? 160 VAL B CG1 1 
ATOM   3283 C  CG2 . VAL B 1 160 ? 14.813  60.370 57.150 1.00 21.73 ? 160 VAL B CG2 1 
ATOM   3284 N  N   . LEU B 1 161 ? 18.912  60.769 55.426 1.00 16.95 ? 161 LEU B N   1 
ATOM   3285 C  CA  . LEU B 1 161 ? 20.002  61.526 54.826 1.00 21.26 ? 161 LEU B CA  1 
ATOM   3286 C  C   . LEU B 1 161 ? 20.636  60.705 53.644 1.00 21.40 ? 161 LEU B C   1 
ATOM   3287 O  O   . LEU B 1 161 ? 21.015  61.268 52.633 1.00 23.75 ? 161 LEU B O   1 
ATOM   3288 C  CB  . LEU B 1 161 ? 21.081  61.806 55.902 1.00 22.60 ? 161 LEU B CB  1 
ATOM   3289 C  CG  . LEU B 1 161 ? 20.654  62.836 56.984 1.00 22.33 ? 161 LEU B CG  1 
ATOM   3290 C  CD1 . LEU B 1 161 ? 21.674  62.872 58.134 1.00 23.39 ? 161 LEU B CD1 1 
ATOM   3291 C  CD2 . LEU B 1 161 ? 20.425  64.213 56.396 1.00 24.38 ? 161 LEU B CD2 1 
ATOM   3292 N  N   . ASP B 1 162 ? 20.666  59.395 53.797 1.00 21.44 ? 162 ASP B N   1 
ATOM   3293 C  CA  . ASP B 1 162 ? 21.187  58.461 52.760 1.00 23.40 ? 162 ASP B CA  1 
ATOM   3294 C  C   . ASP B 1 162 ? 20.294  58.505 51.506 1.00 20.86 ? 162 ASP B C   1 
ATOM   3295 O  O   . ASP B 1 162 ? 20.765  58.206 50.434 1.00 24.03 ? 162 ASP B O   1 
ATOM   3296 C  CB  . ASP B 1 162 ? 21.207  57.006 53.262 1.00 25.63 ? 162 ASP B CB  1 
ATOM   3297 C  CG  . ASP B 1 162 ? 22.382  56.695 54.235 1.00 28.40 ? 162 ASP B CG  1 
ATOM   3298 O  OD1 . ASP B 1 162 ? 23.284  57.553 54.394 1.00 29.12 ? 162 ASP B OD1 1 
ATOM   3299 O  OD2 . ASP B 1 162 ? 22.324  55.603 54.849 1.00 29.48 ? 162 ASP B OD2 1 
ATOM   3300 N  N   . ALA B 1 163 ? 19.011  58.877 51.657 1.00 19.13 ? 163 ALA B N   1 
ATOM   3301 C  CA  . ALA B 1 163 ? 18.058  58.918 50.536 1.00 20.43 ? 163 ALA B CA  1 
ATOM   3302 C  C   . ALA B 1 163 ? 18.223  60.150 49.702 1.00 17.86 ? 163 ALA B C   1 
ATOM   3303 O  O   . ALA B 1 163 ? 17.756  60.149 48.544 1.00 20.59 ? 163 ALA B O   1 
ATOM   3304 C  CB  . ALA B 1 163 ? 16.603  58.771 51.009 1.00 17.72 ? 163 ALA B CB  1 
ATOM   3305 N  N   . LEU B 1 164 ? 18.824  61.200 50.242 1.00 18.01 ? 164 LEU B N   1 
ATOM   3306 C  CA  . LEU B 1 164 ? 18.776  62.474 49.602 1.00 17.34 ? 164 LEU B CA  1 
ATOM   3307 C  C   . LEU B 1 164 ? 19.526  62.489 48.240 1.00 19.07 ? 164 LEU B C   1 
ATOM   3308 O  O   . LEU B 1 164 ? 19.155  63.283 47.356 1.00 19.09 ? 164 LEU B O   1 
ATOM   3309 C  CB  . LEU B 1 164 ? 19.283  63.611 50.457 1.00 20.23 ? 164 LEU B CB  1 
ATOM   3310 C  CG  . LEU B 1 164 ? 18.548  63.792 51.822 1.00 18.20 ? 164 LEU B CG  1 
ATOM   3311 C  CD1 . LEU B 1 164 ? 19.181  64.974 52.547 1.00 18.80 ? 164 LEU B CD1 1 
ATOM   3312 C  CD2 . LEU B 1 164 ? 17.105  64.108 51.514 1.00 19.41 ? 164 LEU B CD2 1 
ATOM   3313 N  N   . GLN B 1 165 ? 20.543  61.641 48.133 1.00 18.37 ? 165 GLN B N   1 
ATOM   3314 C  CA  . GLN B 1 165 ? 21.337  61.635 46.869 1.00 19.17 ? 165 GLN B CA  1 
ATOM   3315 C  C   . GLN B 1 165 ? 20.478  61.242 45.660 1.00 21.29 ? 165 GLN B C   1 
ATOM   3316 O  O   . GLN B 1 165 ? 20.893  61.531 44.535 1.00 22.34 ? 165 GLN B O   1 
ATOM   3317 C  CB  . GLN B 1 165 ? 22.602  60.730 47.026 1.00 23.18 ? 165 GLN B CB  1 
ATOM   3318 C  CG  . GLN B 1 165 ? 22.375  59.367 47.644 1.00 26.60 ? 165 GLN B CG  1 
ATOM   3319 C  CD  . GLN B 1 165 ? 21.552  58.395 46.817 1.00 31.44 ? 165 GLN B CD  1 
ATOM   3320 O  OE1 . GLN B 1 165 ? 21.752  58.246 45.577 1.00 29.85 ? 165 GLN B OE1 1 
ATOM   3321 N  NE2 . GLN B 1 165 ? 20.623  57.673 47.509 1.00 26.98 ? 165 GLN B NE2 1 
ATOM   3322 N  N   . ALA B 1 166 ? 19.348  60.562 45.850 1.00 19.72 ? 166 ALA B N   1 
ATOM   3323 C  CA  . ALA B 1 166 ? 18.474  60.158 44.734 1.00 20.39 ? 166 ALA B CA  1 
ATOM   3324 C  C   . ALA B 1 166 ? 17.436  61.221 44.388 1.00 20.74 ? 166 ALA B C   1 
ATOM   3325 O  O   . ALA B 1 166 ? 16.647  61.024 43.414 1.00 23.12 ? 166 ALA B O   1 
ATOM   3326 C  CB  . ALA B 1 166 ? 17.784  58.812 45.037 1.00 23.40 ? 166 ALA B CB  1 
ATOM   3327 N  N   . ILE B 1 167 ? 17.390  62.310 45.176 1.00 18.32 ? 167 ILE B N   1 
ATOM   3328 C  CA  . ILE B 1 167 ? 16.388  63.366 44.948 1.00 19.31 ? 167 ILE B CA  1 
ATOM   3329 C  C   . ILE B 1 167 ? 16.993  64.695 44.952 1.00 18.14 ? 167 ILE B C   1 
ATOM   3330 O  O   . ILE B 1 167 ? 16.475  65.607 45.516 1.00 16.48 ? 167 ILE B O   1 
ATOM   3331 C  CB  . ILE B 1 167 ? 15.143  63.247 45.940 1.00 18.52 ? 167 ILE B CB  1 
ATOM   3332 C  CG1 . ILE B 1 167 ? 15.574  63.382 47.384 1.00 19.77 ? 167 ILE B CG1 1 
ATOM   3333 C  CG2 . ILE B 1 167 ? 14.328  62.000 45.724 1.00 18.79 ? 167 ILE B CG2 1 
ATOM   3334 C  CD1 . ILE B 1 167 ? 14.428  64.026 48.159 1.00 21.29 ? 167 ILE B CD1 1 
ATOM   3335 N  N   . LYS B 1 168 ? 18.114  64.891 44.225 1.00 18.80 ? 168 LYS B N   1 
ATOM   3336 C  CA  . LYS B 1 168 ? 18.873  66.120 44.402 1.00 18.39 ? 168 LYS B CA  1 
ATOM   3337 C  C   . LYS B 1 168 ? 18.242  67.392 43.898 1.00 17.83 ? 168 LYS B C   1 
ATOM   3338 O  O   . LYS B 1 168 ? 18.448  68.482 44.482 1.00 15.64 ? 168 LYS B O   1 
ATOM   3339 C  CB  . LYS B 1 168 ? 20.314  65.916 43.824 1.00 20.95 ? 168 LYS B CB  1 
ATOM   3340 C  CG  . LYS B 1 168 ? 21.245  65.167 44.803 1.00 25.41 ? 168 LYS B CG  1 
ATOM   3341 C  CD  . LYS B 1 168 ? 21.653  66.044 45.980 1.00 28.91 ? 168 LYS B CD  1 
ATOM   3342 C  CE  . LYS B 1 168 ? 22.715  65.340 46.799 1.00 38.82 ? 168 LYS B CE  1 
ATOM   3343 N  NZ  . LYS B 1 168 ? 23.308  66.393 47.638 1.00 36.88 ? 168 LYS B NZ  1 
ATOM   3344 N  N   . THR B 1 169 ? 17.461  67.280 42.796 1.00 17.41 ? 169 THR B N   1 
ATOM   3345 C  CA  . THR B 1 169 ? 16.831  68.435 42.198 1.00 17.09 ? 169 THR B CA  1 
ATOM   3346 C  C   . THR B 1 169 ? 15.299  68.441 42.271 1.00 17.27 ? 169 THR B C   1 
ATOM   3347 O  O   . THR B 1 169 ? 14.694  67.379 42.474 1.00 18.06 ? 169 THR B O   1 
ATOM   3348 C  CB  . THR B 1 169 ? 17.223  68.480 40.670 1.00 16.63 ? 169 THR B CB  1 
ATOM   3349 O  OG1 . THR B 1 169 ? 17.099  67.189 40.064 1.00 18.45 ? 169 THR B OG1 1 
ATOM   3350 C  CG2 . THR B 1 169 ? 18.692  68.868 40.590 1.00 20.70 ? 169 THR B CG2 1 
ATOM   3351 N  N   . LYS B 1 170 ? 14.739  69.627 42.055 1.00 17.96 ? 170 LYS B N   1 
ATOM   3352 C  CA  . LYS B 1 170 ? 13.263  69.814 42.091 1.00 19.59 ? 170 LYS B CA  1 
ATOM   3353 C  C   . LYS B 1 170 ? 12.452  68.794 41.322 1.00 20.79 ? 170 LYS B C   1 
ATOM   3354 O  O   . LYS B 1 170 ? 12.703  68.542 40.108 1.00 19.50 ? 170 LYS B O   1 
ATOM   3355 C  CB  . LYS B 1 170 ? 12.901  71.194 41.680 1.00 19.90 ? 170 LYS B CB  1 
ATOM   3356 C  CG  . LYS B 1 170 ? 11.431  71.522 42.023 1.00 22.34 ? 170 LYS B CG  1 
ATOM   3357 C  CD  . LYS B 1 170 ? 11.111  72.951 41.597 1.00 24.15 ? 170 LYS B CD  1 
ATOM   3358 C  CE  . LYS B 1 170 ? 9.687   73.384 41.874 1.00 30.77 ? 170 LYS B CE  1 
ATOM   3359 N  NZ  . LYS B 1 170 ? 9.791   74.662 42.680 1.00 39.23 ? 170 LYS B NZ  1 
ATOM   3360 N  N   . GLY B 1 171 ? 11.448  68.182 41.996 1.00 18.41 ? 171 GLY B N   1 
ATOM   3361 C  CA  . GLY B 1 171 ? 10.611  67.184 41.352 1.00 17.54 ? 171 GLY B CA  1 
ATOM   3362 C  C   . GLY B 1 171 ? 11.088  65.739 41.341 1.00 19.72 ? 171 GLY B C   1 
ATOM   3363 O  O   . GLY B 1 171 ? 10.270  64.844 41.090 1.00 22.47 ? 171 GLY B O   1 
ATOM   3364 N  N   . LYS B 1 172 ? 12.396  65.466 41.640 1.00 16.77 ? 172 LYS B N   1 
ATOM   3365 C  CA  . LYS B 1 172 ? 12.797  64.079 41.690 1.00 16.45 ? 172 LYS B CA  1 
ATOM   3366 C  C   . LYS B 1 172 ? 12.168  63.399 42.929 1.00 17.75 ? 172 LYS B C   1 
ATOM   3367 O  O   . LYS B 1 172 ? 11.893  64.079 43.956 1.00 18.91 ? 172 LYS B O   1 
ATOM   3368 C  CB  . LYS B 1 172 ? 14.325  63.948 41.757 1.00 19.03 ? 172 LYS B CB  1 
ATOM   3369 C  CG  . LYS B 1 172 ? 15.022  64.412 40.460 1.00 25.12 ? 172 LYS B CG  1 
ATOM   3370 C  CD  . LYS B 1 172 ? 16.437  63.814 40.359 1.00 26.19 ? 172 LYS B CD  1 
ATOM   3371 C  CE  . LYS B 1 172 ? 16.451  62.285 40.400 1.00 28.86 ? 172 LYS B CE  1 
ATOM   3372 N  NZ  . LYS B 1 172 ? 17.828  61.738 40.340 1.00 31.99 ? 172 LYS B NZ  1 
ATOM   3373 N  N   . ARG B 1 173 ? 11.943  62.099 42.801 1.00 18.83 ? 173 ARG B N   1 
ATOM   3374 C  CA  . ARG B 1 173 ? 11.282  61.329 43.842 1.00 19.91 ? 173 ARG B CA  1 
ATOM   3375 C  C   . ARG B 1 173 ? 11.767  59.935 43.732 1.00 22.00 ? 173 ARG B C   1 
ATOM   3376 O  O   . ARG B 1 173 ? 12.223  59.468 42.630 1.00 22.44 ? 173 ARG B O   1 
ATOM   3377 C  CB  . ARG B 1 173 ? 9.765   61.368 43.680 1.00 20.10 ? 173 ARG B CB  1 
ATOM   3378 C  CG  . ARG B 1 173 ? 9.242   60.912 42.340 1.00 23.51 ? 173 ARG B CG  1 
ATOM   3379 C  CD  . ARG B 1 173 ? 7.962   61.689 41.932 1.00 27.05 ? 173 ARG B CD  1 
ATOM   3380 N  NE  . ARG B 1 173 ? 6.861   61.486 42.884 1.00 25.25 ? 173 ARG B NE  1 
ATOM   3381 C  CZ  . ARG B 1 173 ? 5.792   62.290 42.995 1.00 26.29 ? 173 ARG B CZ  1 
ATOM   3382 N  NH1 . ARG B 1 173 ? 5.672   63.364 42.237 1.00 27.69 ? 173 ARG B NH1 1 
ATOM   3383 N  NH2 . ARG B 1 173 ? 4.834   61.998 43.877 1.00 29.40 ? 173 ARG B NH2 1 
ATOM   3384 N  N   . ALA B 1 174 ? 11.737  59.247 44.859 1.00 19.26 ? 174 ALA B N   1 
ATOM   3385 C  CA  . ALA B 1 174 ? 12.158  57.845 44.903 1.00 19.32 ? 174 ALA B CA  1 
ATOM   3386 C  C   . ALA B 1 174 ? 11.341  57.112 45.922 1.00 20.76 ? 174 ALA B C   1 
ATOM   3387 O  O   . ALA B 1 174 ? 10.947  57.712 46.939 1.00 18.73 ? 174 ALA B O   1 
ATOM   3388 C  CB  . ALA B 1 174 ? 13.622  57.808 45.343 1.00 20.24 ? 174 ALA B CB  1 
ATOM   3389 N  N   . PRO B 1 175 ? 11.244  55.773 45.807 1.00 22.58 ? 175 PRO B N   1 
ATOM   3390 C  CA  . PRO B 1 175 ? 10.686  54.952 46.877 1.00 21.90 ? 175 PRO B CA  1 
ATOM   3391 C  C   . PRO B 1 175 ? 11.461  55.112 48.172 1.00 21.16 ? 175 PRO B C   1 
ATOM   3392 O  O   . PRO B 1 175 ? 12.697  55.246 48.156 1.00 21.30 ? 175 PRO B O   1 
ATOM   3393 C  CB  . PRO B 1 175 ? 10.874  53.495 46.339 1.00 21.91 ? 175 PRO B CB  1 
ATOM   3394 C  CG  . PRO B 1 175 ? 10.778  53.717 44.836 1.00 24.82 ? 175 PRO B CG  1 
ATOM   3395 C  CD  . PRO B 1 175 ? 11.599  54.939 44.621 1.00 21.11 ? 175 PRO B CD  1 
ATOM   3396 N  N   . PHE B 1 176 ? 10.710  55.130 49.284 1.00 21.17 ? 176 PHE B N   1 
ATOM   3397 C  CA  . PHE B 1 176 ? 11.299  55.239 50.616 1.00 20.41 ? 176 PHE B CA  1 
ATOM   3398 C  C   . PHE B 1 176 ? 10.349  54.409 51.479 1.00 21.63 ? 176 PHE B C   1 
ATOM   3399 O  O   . PHE B 1 176 ? 9.195   54.816 51.732 1.00 17.92 ? 176 PHE B O   1 
ATOM   3400 C  CB  . PHE B 1 176 ? 11.300  56.744 51.033 1.00 20.74 ? 176 PHE B CB  1 
ATOM   3401 C  CG  . PHE B 1 176 ? 11.959  57.005 52.351 1.00 18.43 ? 176 PHE B CG  1 
ATOM   3402 C  CD1 . PHE B 1 176 ? 13.288  57.410 52.399 1.00 20.34 ? 176 PHE B CD1 1 
ATOM   3403 C  CD2 . PHE B 1 176 ? 11.222  56.877 53.528 1.00 17.76 ? 176 PHE B CD2 1 
ATOM   3404 C  CE1 . PHE B 1 176 ? 13.967  57.626 53.601 1.00 23.04 ? 176 PHE B CE1 1 
ATOM   3405 C  CE2 . PHE B 1 176 ? 11.903  57.130 54.748 1.00 19.72 ? 176 PHE B CE2 1 
ATOM   3406 C  CZ  . PHE B 1 176 ? 13.238  57.489 54.770 1.00 19.48 ? 176 PHE B CZ  1 
ATOM   3407 N  N   . THR B 1 177 ? 10.819  53.232 51.896 1.00 22.96 ? 177 THR B N   1 
ATOM   3408 C  CA  . THR B 1 177 ? 9.943   52.269 52.487 1.00 21.20 ? 177 THR B CA  1 
ATOM   3409 C  C   . THR B 1 177 ? 10.494  51.783 53.831 1.00 21.32 ? 177 THR B C   1 
ATOM   3410 O  O   . THR B 1 177 ? 11.647  52.005 54.154 1.00 21.26 ? 177 THR B O   1 
ATOM   3411 C  CB  . THR B 1 177 ? 9.688   51.007 51.561 1.00 24.90 ? 177 THR B CB  1 
ATOM   3412 O  OG1 . THR B 1 177 ? 10.928  50.434 51.192 1.00 26.29 ? 177 THR B OG1 1 
ATOM   3413 C  CG2 . THR B 1 177 ? 8.907   51.419 50.258 1.00 26.43 ? 177 THR B CG2 1 
ATOM   3414 N  N   . ASN B 1 178 ? 9.616   51.072 54.531 1.00 21.63 ? 178 ASN B N   1 
ATOM   3415 C  CA  . ASN B 1 178 ? 9.947   50.383 55.809 1.00 23.85 ? 178 ASN B CA  1 
ATOM   3416 C  C   . ASN B 1 178 ? 10.578  51.404 56.809 1.00 23.14 ? 178 ASN B C   1 
ATOM   3417 O  O   . ASN B 1 178 ? 11.753  51.289 57.170 1.00 23.54 ? 178 ASN B O   1 
ATOM   3418 C  CB  . ASN B 1 178 ? 10.956  49.278 55.535 1.00 29.10 ? 178 ASN B CB  1 
ATOM   3419 C  CG  . ASN B 1 178 ? 11.128  48.364 56.725 1.00 34.62 ? 178 ASN B CG  1 
ATOM   3420 O  OD1 . ASN B 1 178 ? 10.208  48.210 57.520 1.00 41.16 ? 178 ASN B OD1 1 
ATOM   3421 N  ND2 . ASN B 1 178 ? 12.292  47.740 56.830 1.00 39.75 ? 178 ASN B ND2 1 
ATOM   3422 N  N   . PHE B 1 179 ? 9.828   52.460 57.133 1.00 21.80 ? 179 PHE B N   1 
ATOM   3423 C  CA  . PHE B 1 179 ? 10.366  53.462 58.046 1.00 22.79 ? 179 PHE B CA  1 
ATOM   3424 C  C   . PHE B 1 179 ? 9.259   53.925 58.986 1.00 20.92 ? 179 PHE B C   1 
ATOM   3425 O  O   . PHE B 1 179 ? 8.159   54.276 58.527 1.00 19.71 ? 179 PHE B O   1 
ATOM   3426 C  CB  . PHE B 1 179 ? 10.946  54.651 57.330 1.00 21.91 ? 179 PHE B CB  1 
ATOM   3427 C  CG  . PHE B 1 179 ? 11.647  55.597 58.241 1.00 21.35 ? 179 PHE B CG  1 
ATOM   3428 C  CD1 . PHE B 1 179 ? 11.070  56.837 58.545 1.00 23.46 ? 179 PHE B CD1 1 
ATOM   3429 C  CD2 . PHE B 1 179 ? 12.905  55.292 58.785 1.00 21.55 ? 179 PHE B CD2 1 
ATOM   3430 C  CE1 . PHE B 1 179 ? 11.754  57.726 59.405 1.00 18.70 ? 179 PHE B CE1 1 
ATOM   3431 C  CE2 . PHE B 1 179 ? 13.585  56.177 59.628 1.00 21.38 ? 179 PHE B CE2 1 
ATOM   3432 C  CZ  . PHE B 1 179 ? 12.976  57.409 59.937 1.00 18.93 ? 179 PHE B CZ  1 
ATOM   3433 N  N   . ASP B 1 180 ? 9.544   53.835 60.297 1.00 21.96 ? 180 ASP B N   1 
ATOM   3434 C  CA  . ASP B 1 180 ? 8.602   54.343 61.328 1.00 22.19 ? 180 ASP B CA  1 
ATOM   3435 C  C   . ASP B 1 180 ? 9.098   55.700 61.848 1.00 19.08 ? 180 ASP B C   1 
ATOM   3436 O  O   . ASP B 1 180 ? 10.097  55.708 62.565 1.00 18.94 ? 180 ASP B O   1 
ATOM   3437 C  CB  . ASP B 1 180 ? 8.674   53.355 62.540 1.00 23.81 ? 180 ASP B CB  1 
ATOM   3438 C  CG  . ASP B 1 180 ? 7.740   53.762 63.677 1.00 26.34 ? 180 ASP B CG  1 
ATOM   3439 O  OD1 . ASP B 1 180 ? 7.235   54.941 63.743 1.00 24.81 ? 180 ASP B OD1 1 
ATOM   3440 O  OD2 . ASP B 1 180 ? 7.492   52.875 64.524 1.00 26.46 ? 180 ASP B OD2 1 
ATOM   3441 N  N   . PRO B 1 181 ? 8.460   56.844 61.470 1.00 18.32 ? 181 PRO B N   1 
ATOM   3442 C  CA  . PRO B 1 181 ? 9.119   58.051 61.865 1.00 18.19 ? 181 PRO B CA  1 
ATOM   3443 C  C   . PRO B 1 181 ? 8.909   58.446 63.359 1.00 17.86 ? 181 PRO B C   1 
ATOM   3444 O  O   . PRO B 1 181 ? 9.528   59.448 63.787 1.00 18.58 ? 181 PRO B O   1 
ATOM   3445 C  CB  . PRO B 1 181 ? 8.406   59.148 61.000 1.00 19.12 ? 181 PRO B CB  1 
ATOM   3446 C  CG  . PRO B 1 181 ? 7.066   58.629 60.728 1.00 18.41 ? 181 PRO B CG  1 
ATOM   3447 C  CD  . PRO B 1 181 ? 7.182   57.091 60.742 1.00 19.23 ? 181 PRO B CD  1 
ATOM   3448 N  N   . SER B 1 182 ? 8.156   57.657 64.122 1.00 18.85 ? 182 SER B N   1 
ATOM   3449 C  CA  . SER B 1 182 ? 8.170   57.883 65.596 1.00 17.96 ? 182 SER B CA  1 
ATOM   3450 C  C   . SER B 1 182 ? 9.545   57.626 66.219 1.00 18.01 ? 182 SER B C   1 
ATOM   3451 O  O   . SER B 1 182 ? 9.850   58.078 67.352 1.00 19.83 ? 182 SER B O   1 
ATOM   3452 C  CB  . SER B 1 182 ? 7.055   57.131 66.296 1.00 19.23 ? 182 SER B CB  1 
ATOM   3453 O  OG  . SER B 1 182 ? 7.418   55.771 66.282 1.00 21.15 ? 182 SER B OG  1 
ATOM   3454 N  N   . THR B 1 183 ? 10.455  57.003 65.483 1.00 16.33 ? 183 THR B N   1 
ATOM   3455 C  CA  . THR B 1 183 ? 11.805  56.785 65.960 1.00 16.88 ? 183 THR B CA  1 
ATOM   3456 C  C   . THR B 1 183 ? 12.614  58.081 65.940 1.00 14.68 ? 183 THR B C   1 
ATOM   3457 O  O   . THR B 1 183 ? 13.646  58.192 66.585 1.00 16.84 ? 183 THR B O   1 
ATOM   3458 C  CB  . THR B 1 183 ? 12.586  55.764 65.127 1.00 21.68 ? 183 THR B CB  1 
ATOM   3459 O  OG1 . THR B 1 183 ? 12.693  56.272 63.793 1.00 20.40 ? 183 THR B OG1 1 
ATOM   3460 C  CG2 . THR B 1 183 ? 11.908  54.426 65.036 1.00 23.29 ? 183 THR B CG2 1 
ATOM   3461 N  N   . LEU B 1 184 ? 12.062  59.106 65.295 1.00 15.66 ? 184 LEU B N   1 
ATOM   3462 C  CA  . LEU B 1 184 ? 12.717  60.424 65.326 1.00 15.21 ? 184 LEU B CA  1 
ATOM   3463 C  C   . LEU B 1 184 ? 12.259  61.311 66.478 1.00 16.95 ? 184 LEU B C   1 
ATOM   3464 O  O   . LEU B 1 184 ? 12.908  62.332 66.709 1.00 16.80 ? 184 LEU B O   1 
ATOM   3465 C  CB  . LEU B 1 184 ? 12.360  61.187 64.044 1.00 17.16 ? 184 LEU B CB  1 
ATOM   3466 C  CG  . LEU B 1 184 ? 12.867  60.549 62.729 1.00 21.45 ? 184 LEU B CG  1 
ATOM   3467 C  CD1 . LEU B 1 184 ? 12.233  61.255 61.516 1.00 22.84 ? 184 LEU B CD1 1 
ATOM   3468 C  CD2 . LEU B 1 184 ? 14.390  60.620 62.724 1.00 22.80 ? 184 LEU B CD2 1 
ATOM   3469 N  N   . LEU B 1 185 ? 11.173  60.924 67.142 1.00 16.47 ? 185 LEU B N   1 
ATOM   3470 C  CA  . LEU B 1 185 ? 10.640  61.742 68.306 1.00 15.41 ? 185 LEU B CA  1 
ATOM   3471 C  C   . LEU B 1 185 ? 11.530  61.624 69.515 1.00 16.39 ? 185 LEU B C   1 
ATOM   3472 O  O   . LEU B 1 185 ? 12.234  60.573 69.729 1.00 18.03 ? 185 LEU B O   1 
ATOM   3473 C  CB  . LEU B 1 185 ? 9.231   61.302 68.601 1.00 16.05 ? 185 LEU B CB  1 
ATOM   3474 C  CG  . LEU B 1 185 ? 8.190   61.424 67.466 1.00 17.60 ? 185 LEU B CG  1 
ATOM   3475 C  CD1 . LEU B 1 185 ? 6.826   60.875 67.838 1.00 18.08 ? 185 LEU B CD1 1 
ATOM   3476 C  CD2 . LEU B 1 185 ? 8.080   62.874 66.976 1.00 18.12 ? 185 LEU B CD2 1 
ATOM   3477 N  N   . PRO B 1 186 ? 11.508  62.623 70.429 1.00 15.13 ? 186 PRO B N   1 
ATOM   3478 C  CA  . PRO B 1 186 ? 12.247  62.562 71.661 1.00 16.17 ? 186 PRO B CA  1 
ATOM   3479 C  C   . PRO B 1 186 ? 11.618  61.478 72.601 1.00 19.53 ? 186 PRO B C   1 
ATOM   3480 O  O   . PRO B 1 186 ? 10.500  61.034 72.364 1.00 19.96 ? 186 PRO B O   1 
ATOM   3481 C  CB  . PRO B 1 186 ? 12.111  63.980 72.244 1.00 16.64 ? 186 PRO B CB  1 
ATOM   3482 C  CG  . PRO B 1 186 ? 10.814  64.490 71.695 1.00 14.52 ? 186 PRO B CG  1 
ATOM   3483 C  CD  . PRO B 1 186 ? 10.716  63.869 70.296 1.00 15.50 ? 186 PRO B CD  1 
ATOM   3484 N  N   . SER B 1 187 ? 12.374  61.063 73.619 1.00 18.25 ? 187 SER B N   1 
ATOM   3485 C  CA  . SER B 1 187 ? 11.932  59.930 74.500 1.00 18.78 ? 187 SER B CA  1 
ATOM   3486 C  C   . SER B 1 187 ? 10.622  60.310 75.217 1.00 19.29 ? 187 SER B C   1 
ATOM   3487 O  O   . SER B 1 187 ? 9.665   59.532 75.310 1.00 21.35 ? 187 SER B O   1 
ATOM   3488 C  CB  . SER B 1 187 ? 13.078  59.694 75.495 1.00 21.81 ? 187 SER B CB  1 
ATOM   3489 O  OG  . SER B 1 187 ? 12.677  58.721 76.423 1.00 29.84 ? 187 SER B OG  1 
ATOM   3490 N  N   . SER B 1 188 ? 10.587  61.541 75.663 1.00 17.91 ? 188 SER B N   1 
ATOM   3491 C  CA  . SER B 1 188 ? 9.388   62.082 76.354 1.00 21.27 ? 188 SER B CA  1 
ATOM   3492 C  C   . SER B 1 188 ? 8.520   62.840 75.381 1.00 20.11 ? 188 SER B C   1 
ATOM   3493 O  O   . SER B 1 188 ? 9.075   63.646 74.591 1.00 18.16 ? 188 SER B O   1 
ATOM   3494 C  CB  . SER B 1 188 ? 9.814   63.015 77.475 1.00 25.24 ? 188 SER B CB  1 
ATOM   3495 O  OG  . SER B 1 188 ? 8.656   63.743 77.896 1.00 28.92 ? 188 SER B OG  1 
ATOM   3496 N  N   . LEU B 1 189 ? 7.202   62.596 75.411 1.00 18.38 ? 189 LEU B N   1 
ATOM   3497 C  CA  . LEU B 1 189 ? 6.257   63.311 74.526 1.00 18.44 ? 189 LEU B CA  1 
ATOM   3498 C  C   . LEU B 1 189 ? 5.456   64.392 75.264 1.00 17.22 ? 189 LEU B C   1 
ATOM   3499 O  O   . LEU B 1 189 ? 4.359   64.766 74.830 1.00 17.06 ? 189 LEU B O   1 
ATOM   3500 C  CB  . LEU B 1 189 ? 5.372   62.372 73.722 1.00 17.99 ? 189 LEU B CB  1 
ATOM   3501 C  CG  . LEU B 1 189 ? 6.137   61.332 72.831 1.00 20.87 ? 189 LEU B CG  1 
ATOM   3502 C  CD1 . LEU B 1 189 ? 5.064   60.521 72.122 1.00 21.31 ? 189 LEU B CD1 1 
ATOM   3503 C  CD2 . LEU B 1 189 ? 7.106   62.096 71.919 1.00 21.33 ? 189 LEU B CD2 1 
ATOM   3504 N  N   . ASP B 1 190 ? 6.049   64.950 76.319 1.00 18.13 ? 190 ASP B N   1 
ATOM   3505 C  CA  . ASP B 1 190 ? 5.439   66.190 76.899 1.00 18.78 ? 190 ASP B CA  1 
ATOM   3506 C  C   . ASP B 1 190 ? 5.318   67.247 75.839 1.00 16.59 ? 190 ASP B C   1 
ATOM   3507 O  O   . ASP B 1 190 ? 6.203   67.339 74.990 1.00 16.28 ? 190 ASP B O   1 
ATOM   3508 C  CB  . ASP B 1 190 ? 6.247   66.748 78.094 1.00 20.40 ? 190 ASP B CB  1 
ATOM   3509 C  CG  . ASP B 1 190 ? 6.316   65.799 79.302 1.00 29.13 ? 190 ASP B CG  1 
ATOM   3510 O  OD1 . ASP B 1 190 ? 5.439   64.933 79.438 1.00 26.11 ? 190 ASP B OD1 1 
ATOM   3511 O  OD2 . ASP B 1 190 ? 7.245   66.012 80.154 1.00 32.54 ? 190 ASP B OD2 1 
ATOM   3512 N  N   . PHE B 1 191 ? 4.228   68.002 75.821 1.00 15.60 ? 191 PHE B N   1 
ATOM   3513 C  CA  . PHE B 1 191 ? 4.014   68.917 74.703 1.00 15.59 ? 191 PHE B CA  1 
ATOM   3514 C  C   . PHE B 1 191 ? 3.297   70.217 75.083 1.00 15.45 ? 191 PHE B C   1 
ATOM   3515 O  O   . PHE B 1 191 ? 2.657   70.301 76.115 1.00 16.68 ? 191 PHE B O   1 
ATOM   3516 C  CB  . PHE B 1 191 ? 3.255   68.215 73.573 1.00 16.35 ? 191 PHE B CB  1 
ATOM   3517 C  CG  . PHE B 1 191 ? 1.824   67.835 73.960 1.00 16.56 ? 191 PHE B CG  1 
ATOM   3518 C  CD1 . PHE B 1 191 ? 1.552   66.608 74.594 1.00 17.98 ? 191 PHE B CD1 1 
ATOM   3519 C  CD2 . PHE B 1 191 ? 0.791   68.718 73.676 1.00 17.77 ? 191 PHE B CD2 1 
ATOM   3520 C  CE1 . PHE B 1 191 ? 0.218   66.278 74.973 1.00 16.36 ? 191 PHE B CE1 1 
ATOM   3521 C  CE2 . PHE B 1 191 ? -0.522  68.408 74.058 1.00 18.55 ? 191 PHE B CE2 1 
ATOM   3522 C  CZ  . PHE B 1 191 ? -0.789  67.224 74.691 1.00 17.54 ? 191 PHE B CZ  1 
ATOM   3523 N  N   . TRP B 1 192 ? 3.403   71.203 74.200 1.00 13.62 ? 192 TRP B N   1 
ATOM   3524 C  CA  . TRP B 1 192 ? 2.573   72.408 74.193 1.00 14.45 ? 192 TRP B CA  1 
ATOM   3525 C  C   . TRP B 1 192 ? 1.629   72.226 73.019 1.00 17.81 ? 192 TRP B C   1 
ATOM   3526 O  O   . TRP B 1 192 ? 2.000   71.583 71.986 1.00 16.57 ? 192 TRP B O   1 
ATOM   3527 C  CB  . TRP B 1 192 ? 3.407   73.608 73.872 1.00 15.66 ? 192 TRP B CB  1 
ATOM   3528 C  CG  . TRP B 1 192 ? 4.346   73.929 74.979 1.00 16.01 ? 192 TRP B CG  1 
ATOM   3529 C  CD1 . TRP B 1 192 ? 4.025   74.342 76.264 1.00 18.25 ? 192 TRP B CD1 1 
ATOM   3530 C  CD2 . TRP B 1 192 ? 5.806   73.842 74.954 1.00 16.19 ? 192 TRP B CD2 1 
ATOM   3531 N  NE1 . TRP B 1 192 ? 5.159   74.521 77.014 1.00 18.28 ? 192 TRP B NE1 1 
ATOM   3532 C  CE2 . TRP B 1 192 ? 6.264   74.240 76.287 1.00 17.47 ? 192 TRP B CE2 1 
ATOM   3533 C  CE3 . TRP B 1 192 ? 6.738   73.492 74.000 1.00 16.28 ? 192 TRP B CE3 1 
ATOM   3534 C  CZ2 . TRP B 1 192 ? 7.609   74.277 76.619 1.00 15.14 ? 192 TRP B CZ2 1 
ATOM   3535 C  CZ3 . TRP B 1 192 ? 8.086   73.526 74.342 1.00 16.44 ? 192 TRP B CZ3 1 
ATOM   3536 C  CH2 . TRP B 1 192 ? 8.512   73.916 75.616 1.00 18.87 ? 192 TRP B CH2 1 
ATOM   3537 N  N   . THR B 1 193 ? 0.442   72.798 73.100 1.00 14.32 ? 193 THR B N   1 
ATOM   3538 C  CA  . THR B 1 193 ? -0.385  72.790 71.866 1.00 15.30 ? 193 THR B CA  1 
ATOM   3539 C  C   . THR B 1 193 ? -1.080  74.142 71.648 1.00 17.50 ? 193 THR B C   1 
ATOM   3540 O  O   . THR B 1 193 ? -1.429  74.841 72.643 1.00 17.17 ? 193 THR B O   1 
ATOM   3541 C  CB  . THR B 1 193 ? -1.409  71.626 71.925 1.00 14.45 ? 193 THR B CB  1 
ATOM   3542 O  OG1 . THR B 1 193 ? -2.212  71.650 70.724 1.00 14.80 ? 193 THR B OG1 1 
ATOM   3543 C  CG2 . THR B 1 193 ? -2.355  71.763 73.195 1.00 15.09 ? 193 THR B CG2 1 
ATOM   3544 N  N   . TYR B 1 194 ? -1.333  74.513 70.402 1.00 14.76 ? 194 TYR B N   1 
ATOM   3545 C  CA  . TYR B 1 194 ? -2.093  75.746 70.117 1.00 16.06 ? 194 TYR B CA  1 
ATOM   3546 C  C   . TYR B 1 194 ? -2.698  75.619 68.713 1.00 17.94 ? 194 TYR B C   1 
ATOM   3547 O  O   . TYR B 1 194 ? -2.283  74.770 67.942 1.00 16.94 ? 194 TYR B O   1 
ATOM   3548 C  CB  . TYR B 1 194 ? -1.162  76.971 70.224 1.00 14.25 ? 194 TYR B CB  1 
ATOM   3549 C  CG  . TYR B 1 194 ? -0.223  77.127 69.037 1.00 14.38 ? 194 TYR B CG  1 
ATOM   3550 C  CD1 . TYR B 1 194 ? 1.002   76.409 69.009 1.00 15.19 ? 194 TYR B CD1 1 
ATOM   3551 C  CD2 . TYR B 1 194 ? -0.554  77.913 67.946 1.00 14.50 ? 194 TYR B CD2 1 
ATOM   3552 C  CE1 . TYR B 1 194 ? 1.860   76.540 67.896 1.00 15.99 ? 194 TYR B CE1 1 
ATOM   3553 C  CE2 . TYR B 1 194 ? 0.269   77.998 66.828 1.00 15.73 ? 194 TYR B CE2 1 
ATOM   3554 C  CZ  . TYR B 1 194 ? 1.489   77.305 66.819 1.00 13.99 ? 194 TYR B CZ  1 
ATOM   3555 O  OH  . TYR B 1 194 ? 2.307   77.357 65.730 1.00 14.45 ? 194 TYR B OH  1 
ATOM   3556 N  N   . PRO B 1 195 ? -3.744  76.388 68.411 1.00 17.14 ? 195 PRO B N   1 
ATOM   3557 C  CA  . PRO B 1 195 ? -4.401  76.294 67.123 1.00 17.26 ? 195 PRO B CA  1 
ATOM   3558 C  C   . PRO B 1 195 ? -3.659  77.214 66.175 1.00 17.40 ? 195 PRO B C   1 
ATOM   3559 O  O   . PRO B 1 195 ? -3.405  78.382 66.471 1.00 18.83 ? 195 PRO B O   1 
ATOM   3560 C  CB  . PRO B 1 195 ? -5.847  76.824 67.411 1.00 17.61 ? 195 PRO B CB  1 
ATOM   3561 C  CG  . PRO B 1 195 ? -5.612  77.798 68.545 1.00 17.57 ? 195 PRO B CG  1 
ATOM   3562 C  CD  . PRO B 1 195 ? -4.543  77.141 69.399 1.00 17.24 ? 195 PRO B CD  1 
ATOM   3563 N  N   . GLY B 1 196 ? -3.283  76.675 65.018 1.00 17.58 ? 196 GLY B N   1 
ATOM   3564 C  CA  . GLY B 1 196 ? -2.521  77.481 64.114 1.00 15.47 ? 196 GLY B CA  1 
ATOM   3565 C  C   . GLY B 1 196 ? -2.715  77.072 62.632 1.00 16.10 ? 196 GLY B C   1 
ATOM   3566 O  O   . GLY B 1 196 ? -3.787  76.670 62.235 1.00 16.15 ? 196 GLY B O   1 
ATOM   3567 N  N   . SER B 1 197 ? -1.635  77.159 61.859 1.00 15.40 ? 197 SER B N   1 
ATOM   3568 C  CA  . SER B 1 197 ? -1.746  77.117 60.385 1.00 15.95 ? 197 SER B CA  1 
ATOM   3569 C  C   . SER B 1 197 ? -0.594  76.282 59.802 1.00 14.76 ? 197 SER B C   1 
ATOM   3570 O  O   . SER B 1 197 ? 0.362   75.931 60.534 1.00 14.11 ? 197 SER B O   1 
ATOM   3571 C  CB  . SER B 1 197 ? -1.663  78.549 59.825 1.00 16.22 ? 197 SER B CB  1 
ATOM   3572 O  OG  . SER B 1 197 ? -0.332  79.046 59.738 1.00 17.57 ? 197 SER B OG  1 
ATOM   3573 N  N   . LEU B 1 198 ? -0.729  75.946 58.501 1.00 15.99 ? 198 LEU B N   1 
ATOM   3574 C  CA  . LEU B 1 198 ? 0.464   75.495 57.706 1.00 16.03 ? 198 LEU B CA  1 
ATOM   3575 C  C   . LEU B 1 198 ? 1.445   76.629 57.726 1.00 17.15 ? 198 LEU B C   1 
ATOM   3576 O  O   . LEU B 1 198 ? 1.050   77.836 57.697 1.00 15.71 ? 198 LEU B O   1 
ATOM   3577 C  CB  . LEU B 1 198 ? 0.046   75.229 56.254 1.00 17.09 ? 198 LEU B CB  1 
ATOM   3578 C  CG  . LEU B 1 198 ? -1.006  74.183 56.100 1.00 16.66 ? 198 LEU B CG  1 
ATOM   3579 C  CD1 . LEU B 1 198 ? -1.402  74.155 54.613 1.00 19.00 ? 198 LEU B CD1 1 
ATOM   3580 C  CD2 . LEU B 1 198 ? -0.457  72.826 56.540 1.00 16.76 ? 198 LEU B CD2 1 
ATOM   3581 N  N   . THR B 1 199 ? 2.728   76.328 57.863 1.00 14.24 ? 199 THR B N   1 
ATOM   3582 C  CA  . THR B 1 199 ? 3.745   77.412 57.920 1.00 14.91 ? 199 THR B CA  1 
ATOM   3583 C  C   . THR B 1 199 ? 4.276   77.956 56.581 1.00 16.25 ? 199 THR B C   1 
ATOM   3584 O  O   . THR B 1 199 ? 5.145   78.859 56.537 1.00 17.82 ? 199 THR B O   1 
ATOM   3585 C  CB  . THR B 1 199 ? 5.004   77.057 58.791 1.00 14.70 ? 199 THR B CB  1 
ATOM   3586 O  OG1 . THR B 1 199 ? 5.690   75.986 58.153 1.00 14.57 ? 199 THR B OG1 1 
ATOM   3587 C  CG2 . THR B 1 199 ? 4.539   76.591 60.148 1.00 14.12 ? 199 THR B CG2 1 
ATOM   3588 N  N   . HIS B 1 200 ? 3.773   77.402 55.475 1.00 17.47 ? 200 HIS B N   1 
ATOM   3589 C  CA  . HIS B 1 200 ? 4.067   77.966 54.175 1.00 17.76 ? 200 HIS B CA  1 
ATOM   3590 C  C   . HIS B 1 200 ? 2.756   77.922 53.383 1.00 16.11 ? 200 HIS B C   1 
ATOM   3591 O  O   . HIS B 1 200 ? 1.779   77.270 53.811 1.00 16.85 ? 200 HIS B O   1 
ATOM   3592 C  CB  . HIS B 1 200 ? 5.279   77.312 53.451 1.00 17.39 ? 200 HIS B CB  1 
ATOM   3593 C  CG  . HIS B 1 200 ? 5.118   75.853 53.153 1.00 18.22 ? 200 HIS B CG  1 
ATOM   3594 N  ND1 . HIS B 1 200 ? 4.169   75.393 52.285 1.00 19.23 ? 200 HIS B ND1 1 
ATOM   3595 C  CD2 . HIS B 1 200 ? 5.906   74.762 53.520 1.00 19.53 ? 200 HIS B CD2 1 
ATOM   3596 C  CE1 . HIS B 1 200 ? 4.329   74.032 52.178 1.00 20.96 ? 200 HIS B CE1 1 
ATOM   3597 N  NE2 . HIS B 1 200 ? 5.375   73.665 52.961 1.00 22.11 ? 200 HIS B NE2 1 
ATOM   3598 N  N   . PRO B 1 201 ? 2.722   78.587 52.238 1.00 18.08 ? 201 PRO B N   1 
ATOM   3599 C  CA  . PRO B 1 201 ? 1.508   78.649 51.446 1.00 18.93 ? 201 PRO B CA  1 
ATOM   3600 C  C   . PRO B 1 201 ? 1.035   77.257 51.119 1.00 18.86 ? 201 PRO B C   1 
ATOM   3601 O  O   . PRO B 1 201 ? 1.888   76.405 50.822 1.00 18.84 ? 201 PRO B O   1 
ATOM   3602 C  CB  . PRO B 1 201 ? 1.961   79.410 50.196 1.00 21.22 ? 201 PRO B CB  1 
ATOM   3603 C  CG  . PRO B 1 201 ? 2.915   80.382 50.769 1.00 19.47 ? 201 PRO B CG  1 
ATOM   3604 C  CD  . PRO B 1 201 ? 3.758   79.498 51.717 1.00 20.03 ? 201 PRO B CD  1 
ATOM   3605 N  N   . PRO B 1 202 ? -0.298  77.022 51.152 1.00 18.40 ? 202 PRO B N   1 
ATOM   3606 C  CA  . PRO B 1 202 ? -1.389  78.019 51.229 1.00 20.02 ? 202 PRO B CA  1 
ATOM   3607 C  C   . PRO B 1 202 ? -1.767  78.508 52.606 1.00 20.15 ? 202 PRO B C   1 
ATOM   3608 O  O   . PRO B 1 202 ? -2.825  79.174 52.746 1.00 19.91 ? 202 PRO B O   1 
ATOM   3609 C  CB  . PRO B 1 202 ? -2.603  77.253 50.676 1.00 20.10 ? 202 PRO B CB  1 
ATOM   3610 C  CG  . PRO B 1 202 ? -2.307  75.833 51.048 1.00 19.87 ? 202 PRO B CG  1 
ATOM   3611 C  CD  . PRO B 1 202 ? -0.819  75.672 50.831 1.00 20.48 ? 202 PRO B CD  1 
ATOM   3612 N  N   . LEU B 1 203 ? -0.945  78.175 53.618 1.00 19.66 ? 203 LEU B N   1 
ATOM   3613 C  CA  . LEU B 1 203 ? -1.079  78.845 54.945 1.00 19.14 ? 203 LEU B CA  1 
ATOM   3614 C  C   . LEU B 1 203 ? -2.444  78.662 55.627 1.00 19.83 ? 203 LEU B C   1 
ATOM   3615 O  O   . LEU B 1 203 ? -2.847  79.449 56.509 1.00 19.53 ? 203 LEU B O   1 
ATOM   3616 C  CB  . LEU B 1 203 ? -0.755  80.351 54.800 1.00 19.79 ? 203 LEU B CB  1 
ATOM   3617 C  CG  . LEU B 1 203 ? 0.639   80.705 54.337 1.00 20.76 ? 203 LEU B CG  1 
ATOM   3618 C  CD1 . LEU B 1 203 ? 0.782   82.182 54.052 1.00 23.19 ? 203 LEU B CD1 1 
ATOM   3619 C  CD2 . LEU B 1 203 ? 1.649   80.406 55.440 1.00 17.38 ? 203 LEU B CD2 1 
ATOM   3620 N  N   . TYR B 1 204 ? -3.129  77.575 55.292 1.00 19.63 ? 204 TYR B N   1 
ATOM   3621 C  CA  . TYR B 1 204 ? -4.457  77.326 55.787 1.00 19.19 ? 204 TYR B CA  1 
ATOM   3622 C  C   . TYR B 1 204 ? -4.433  77.295 57.290 1.00 19.45 ? 204 TYR B C   1 
ATOM   3623 O  O   . TYR B 1 204 ? -3.545  76.678 57.905 1.00 19.06 ? 204 TYR B O   1 
ATOM   3624 C  CB  . TYR B 1 204 ? -4.899  75.913 55.329 1.00 20.37 ? 204 TYR B CB  1 
ATOM   3625 C  CG  . TYR B 1 204 ? -5.307  75.813 53.838 1.00 22.87 ? 204 TYR B CG  1 
ATOM   3626 C  CD1 . TYR B 1 204 ? -5.953  76.858 53.191 1.00 26.47 ? 204 TYR B CD1 1 
ATOM   3627 C  CD2 . TYR B 1 204 ? -5.092  74.628 53.137 1.00 23.57 ? 204 TYR B CD2 1 
ATOM   3628 C  CE1 . TYR B 1 204 ? -6.328  76.740 51.845 1.00 27.70 ? 204 TYR B CE1 1 
ATOM   3629 C  CE2 . TYR B 1 204 ? -5.480  74.489 51.811 1.00 25.95 ? 204 TYR B CE2 1 
ATOM   3630 C  CZ  . TYR B 1 204 ? -6.067  75.541 51.168 1.00 29.22 ? 204 TYR B CZ  1 
ATOM   3631 O  OH  . TYR B 1 204 ? -6.447  75.329 49.846 1.00 31.25 ? 204 TYR B OH  1 
ATOM   3632 N  N   . GLU B 1 205 ? -5.470  77.823 57.906 1.00 19.60 ? 205 GLU B N   1 
ATOM   3633 C  CA  . GLU B 1 205 ? -5.506  77.786 59.383 1.00 17.30 ? 205 GLU B CA  1 
ATOM   3634 C  C   . GLU B 1 205 ? -6.208  76.525 59.892 1.00 18.19 ? 205 GLU B C   1 
ATOM   3635 O  O   . GLU B 1 205 ? -7.299  76.577 60.525 1.00 21.92 ? 205 GLU B O   1 
ATOM   3636 C  CB  . GLU B 1 205 ? -6.141  79.135 59.897 1.00 19.34 ? 205 GLU B CB  1 
ATOM   3637 C  CG  . GLU B 1 205 ? -5.216  80.309 59.568 1.00 18.47 ? 205 GLU B CG  1 
ATOM   3638 C  CD  . GLU B 1 205 ? -5.648  81.676 60.185 1.00 21.01 ? 205 GLU B CD  1 
ATOM   3639 O  OE1 . GLU B 1 205 ? -4.812  82.584 60.296 1.00 20.38 ? 205 GLU B OE1 1 
ATOM   3640 O  OE2 . GLU B 1 205 ? -6.855  81.804 60.449 1.00 21.88 ? 205 GLU B OE2 1 
ATOM   3641 N  N   . SER B 1 206 ? -5.599  75.346 59.619 1.00 16.72 ? 206 SER B N   1 
ATOM   3642 C  CA  . SER B 1 206 ? -6.269  74.046 59.830 1.00 17.43 ? 206 SER B CA  1 
ATOM   3643 C  C   . SER B 1 206 ? -5.477  73.137 60.716 1.00 16.37 ? 206 SER B C   1 
ATOM   3644 O  O   . SER B 1 206 ? -5.767  71.945 60.854 1.00 17.16 ? 206 SER B O   1 
ATOM   3645 C  CB  . SER B 1 206 ? -6.339  73.307 58.490 1.00 21.02 ? 206 SER B CB  1 
ATOM   3646 O  OG  . SER B 1 206 ? -5.085  73.440 57.824 1.00 19.41 ? 206 SER B OG  1 
ATOM   3647 N  N   . VAL B 1 207 ? -4.427  73.700 61.352 1.00 16.93 ? 207 VAL B N   1 
ATOM   3648 C  CA  . VAL B 1 207 ? -3.442  72.819 62.031 1.00 16.95 ? 207 VAL B CA  1 
ATOM   3649 C  C   . VAL B 1 207 ? -3.533  72.951 63.550 1.00 18.00 ? 207 VAL B C   1 
ATOM   3650 O  O   . VAL B 1 207 ? -3.396  74.057 64.104 1.00 19.99 ? 207 VAL B O   1 
ATOM   3651 C  CB  . VAL B 1 207 ? -1.980  73.142 61.646 1.00 16.32 ? 207 VAL B CB  1 
ATOM   3652 C  CG1 . VAL B 1 207 ? -1.014  72.236 62.425 1.00 16.22 ? 207 VAL B CG1 1 
ATOM   3653 C  CG2 . VAL B 1 207 ? -1.772  72.946 60.131 1.00 14.75 ? 207 VAL B CG2 1 
ATOM   3654 N  N   . THR B 1 208 ? -3.749  71.824 64.207 1.00 15.65 ? 208 THR B N   1 
ATOM   3655 C  CA  . THR B 1 208 ? -3.530  71.779 65.664 1.00 16.35 ? 208 THR B CA  1 
ATOM   3656 C  C   . THR B 1 208 ? -2.104  71.382 65.874 1.00 15.98 ? 208 THR B C   1 
ATOM   3657 O  O   . THR B 1 208 ? -1.685  70.286 65.501 1.00 17.19 ? 208 THR B O   1 
ATOM   3658 C  CB  . THR B 1 208 ? -4.469  70.802 66.376 1.00 16.59 ? 208 THR B CB  1 
ATOM   3659 O  OG1 . THR B 1 208 ? -5.834  71.213 66.092 1.00 18.76 ? 208 THR B OG1 1 
ATOM   3660 C  CG2 . THR B 1 208 ? -4.203  70.846 67.947 1.00 17.78 ? 208 THR B CG2 1 
ATOM   3661 N  N   . TRP B 1 209 ? -1.335  72.300 66.493 1.00 14.38 ? 209 TRP B N   1 
ATOM   3662 C  CA  . TRP B 1 209 ? 0.106   72.055 66.627 1.00 14.05 ? 209 TRP B CA  1 
ATOM   3663 C  C   . TRP B 1 209 ? 0.389   71.330 67.936 1.00 15.86 ? 209 TRP B C   1 
ATOM   3664 O  O   . TRP B 1 209 ? -0.222  71.633 68.980 1.00 18.15 ? 209 TRP B O   1 
ATOM   3665 C  CB  . TRP B 1 209 ? 0.866   73.399 66.634 1.00 15.51 ? 209 TRP B CB  1 
ATOM   3666 C  CG  . TRP B 1 209 ? 1.110   73.826 65.264 1.00 14.32 ? 209 TRP B CG  1 
ATOM   3667 C  CD1 . TRP B 1 209 ? 0.394   74.742 64.522 1.00 14.57 ? 209 TRP B CD1 1 
ATOM   3668 C  CD2 . TRP B 1 209 ? 2.186   73.325 64.363 1.00 14.08 ? 209 TRP B CD2 1 
ATOM   3669 N  NE1 . TRP B 1 209 ? 0.926   74.830 63.231 1.00 16.15 ? 209 TRP B NE1 1 
ATOM   3670 C  CE2 . TRP B 1 209 ? 2.005   74.013 63.096 1.00 13.47 ? 209 TRP B CE2 1 
ATOM   3671 C  CE3 . TRP B 1 209 ? 3.238   72.384 64.509 1.00 14.43 ? 209 TRP B CE3 1 
ATOM   3672 C  CZ2 . TRP B 1 209 ? 2.835   73.766 61.979 1.00 13.61 ? 209 TRP B CZ2 1 
ATOM   3673 C  CZ3 . TRP B 1 209 ? 4.070   72.170 63.390 1.00 13.01 ? 209 TRP B CZ3 1 
ATOM   3674 C  CH2 . TRP B 1 209 ? 3.864   72.841 62.166 1.00 12.85 ? 209 TRP B CH2 1 
ATOM   3675 N  N   . ILE B 1 210 ? 1.293   70.348 67.886 1.00 14.11 ? 210 ILE B N   1 
ATOM   3676 C  CA  . ILE B 1 210 ? 1.749   69.645 69.058 1.00 13.63 ? 210 ILE B CA  1 
ATOM   3677 C  C   . ILE B 1 210 ? 3.251   69.888 69.049 1.00 16.94 ? 210 ILE B C   1 
ATOM   3678 O  O   . ILE B 1 210 ? 3.981   69.280 68.244 1.00 15.11 ? 210 ILE B O   1 
ATOM   3679 C  CB  . ILE B 1 210 ? 1.475   68.116 68.944 1.00 12.71 ? 210 ILE B CB  1 
ATOM   3680 C  CG1 . ILE B 1 210 ? -0.031  67.791 68.794 1.00 16.22 ? 210 ILE B CG1 1 
ATOM   3681 C  CG2 . ILE B 1 210 ? 2.060   67.381 70.111 1.00 14.67 ? 210 ILE B CG2 1 
ATOM   3682 C  CD1 . ILE B 1 210 ? -0.952  68.249 69.914 1.00 18.43 ? 210 ILE B CD1 1 
ATOM   3683 N  N   . ILE B 1 211 ? 3.753   70.761 69.926 1.00 15.10 ? 211 ILE B N   1 
ATOM   3684 C  CA  . ILE B 1 211 ? 5.181   71.019 69.958 1.00 13.50 ? 211 ILE B CA  1 
ATOM   3685 C  C   . ILE B 1 211 ? 5.798   70.259 71.146 1.00 14.35 ? 211 ILE B C   1 
ATOM   3686 O  O   . ILE B 1 211 ? 5.396   70.492 72.303 1.00 13.24 ? 211 ILE B O   1 
ATOM   3687 C  CB  . ILE B 1 211 ? 5.421   72.545 70.161 1.00 14.40 ? 211 ILE B CB  1 
ATOM   3688 C  CG1 . ILE B 1 211 ? 4.677   73.362 69.100 1.00 14.89 ? 211 ILE B CG1 1 
ATOM   3689 C  CG2 . ILE B 1 211 ? 6.941   72.842 70.103 1.00 13.42 ? 211 ILE B CG2 1 
ATOM   3690 C  CD1 . ILE B 1 211 ? 5.066   73.030 67.655 1.00 15.31 ? 211 ILE B CD1 1 
ATOM   3691 N  N   . CYS B 1 212 ? 6.773   69.398 70.900 1.00 14.01 ? 212 CYS B N   1 
ATOM   3692 C  CA  . CYS B 1 212 ? 7.402   68.599 71.994 1.00 12.64 ? 212 CYS B CA  1 
ATOM   3693 C  C   . CYS B 1 212 ? 8.246   69.519 72.870 1.00 14.63 ? 212 CYS B C   1 
ATOM   3694 O  O   . CYS B 1 212 ? 8.953   70.440 72.379 1.00 13.70 ? 212 CYS B O   1 
ATOM   3695 C  CB  . CYS B 1 212 ? 8.351   67.556 71.371 1.00 14.34 ? 212 CYS B CB  1 
ATOM   3696 S  SG  . CYS B 1 212 ? 7.347   66.236 70.655 1.00 16.54 ? 212 CYS B SG  1 
ATOM   3697 N  N   . LYS B 1 213 ? 8.115   69.351 74.191 1.00 15.24 ? 213 LYS B N   1 
ATOM   3698 C  CA  . LYS B 1 213 ? 9.014   70.118 75.020 1.00 16.82 ? 213 LYS B CA  1 
ATOM   3699 C  C   . LYS B 1 213 ? 10.479  69.658 74.992 1.00 16.02 ? 213 LYS B C   1 
ATOM   3700 O  O   . LYS B 1 213 ? 11.361  70.521 75.240 1.00 19.28 ? 213 LYS B O   1 
ATOM   3701 C  CB  . LYS B 1 213 ? 8.442   70.177 76.441 1.00 22.87 ? 213 LYS B CB  1 
ATOM   3702 C  CG  . LYS B 1 213 ? 8.881   69.074 77.336 1.00 35.59 ? 213 LYS B CG  1 
ATOM   3703 C  CD  . LYS B 1 213 ? 8.989   69.614 78.785 1.00 37.56 ? 213 LYS B CD  1 
ATOM   3704 C  CE  . LYS B 1 213 ? 9.897   68.718 79.631 1.00 41.03 ? 213 LYS B CE  1 
ATOM   3705 N  NZ  . LYS B 1 213 ? 9.613   67.263 79.479 1.00 41.21 ? 213 LYS B NZ  1 
ATOM   3706 N  N   . GLU B 1 214 ? 10.755  68.382 74.680 1.00 15.17 ? 214 GLU B N   1 
ATOM   3707 C  CA  . GLU B 1 214 ? 12.173  67.900 74.581 1.00 16.55 ? 214 GLU B CA  1 
ATOM   3708 C  C   . GLU B 1 214 ? 12.632  68.025 73.138 1.00 16.27 ? 214 GLU B C   1 
ATOM   3709 O  O   . GLU B 1 214 ? 11.881  67.712 72.220 1.00 14.99 ? 214 GLU B O   1 
ATOM   3710 C  CB  . GLU B 1 214 ? 12.231  66.411 74.886 1.00 19.75 ? 214 GLU B CB  1 
ATOM   3711 C  CG  . GLU B 1 214 ? 13.536  65.905 75.513 1.00 31.71 ? 214 GLU B CG  1 
ATOM   3712 C  CD  . GLU B 1 214 ? 13.655  64.355 75.710 1.00 38.30 ? 214 GLU B CD  1 
ATOM   3713 O  OE1 . GLU B 1 214 ? 12.672  63.612 75.990 1.00 29.34 ? 214 GLU B OE1 1 
ATOM   3714 O  OE2 . GLU B 1 214 ? 14.817  63.868 75.621 1.00 45.08 ? 214 GLU B OE2 1 
ATOM   3715 N  N   . SER B 1 215 ? 13.858  68.461 72.960 1.00 14.37 ? 215 SER B N   1 
ATOM   3716 C  CA  . SER B 1 215 ? 14.469  68.539 71.610 1.00 15.40 ? 215 SER B CA  1 
ATOM   3717 C  C   . SER B 1 215 ? 15.216  67.252 71.213 1.00 15.01 ? 215 SER B C   1 
ATOM   3718 O  O   . SER B 1 215 ? 15.366  66.295 72.031 1.00 18.80 ? 215 SER B O   1 
ATOM   3719 C  CB  . SER B 1 215 ? 15.442  69.712 71.541 1.00 16.82 ? 215 SER B CB  1 
ATOM   3720 O  OG  . SER B 1 215 ? 16.475  69.556 72.522 1.00 19.18 ? 215 SER B OG  1 
ATOM   3721 N  N   . ILE B 1 216 ? 15.642  67.189 69.929 1.00 13.38 ? 216 ILE B N   1 
ATOM   3722 C  CA  . ILE B 1 216 ? 16.530  66.087 69.496 1.00 14.98 ? 216 ILE B CA  1 
ATOM   3723 C  C   . ILE B 1 216 ? 17.774  66.681 68.899 1.00 17.12 ? 216 ILE B C   1 
ATOM   3724 O  O   . ILE B 1 216 ? 17.783  67.899 68.593 1.00 15.91 ? 216 ILE B O   1 
ATOM   3725 C  CB  . ILE B 1 216 ? 15.822  65.160 68.459 1.00 15.57 ? 216 ILE B CB  1 
ATOM   3726 C  CG1 . ILE B 1 216 ? 15.395  65.953 67.201 1.00 14.30 ? 216 ILE B CG1 1 
ATOM   3727 C  CG2 . ILE B 1 216 ? 14.589  64.509 69.121 1.00 15.28 ? 216 ILE B CG2 1 
ATOM   3728 C  CD1 . ILE B 1 216 ? 14.916  65.001 66.058 1.00 15.52 ? 216 ILE B CD1 1 
ATOM   3729 N  N   . SER B 1 217 ? 18.842  65.893 68.754 1.00 18.16 ? 217 SER B N   1 
ATOM   3730 C  CA  . SER B 1 217 ? 20.073  66.525 68.189 1.00 18.22 ? 217 SER B CA  1 
ATOM   3731 C  C   . SER B 1 217 ? 20.162  66.412 66.652 1.00 17.52 ? 217 SER B C   1 
ATOM   3732 O  O   . SER B 1 217 ? 19.407  65.675 66.003 1.00 18.25 ? 217 SER B O   1 
ATOM   3733 C  CB  . SER B 1 217 ? 21.363  65.861 68.760 1.00 19.93 ? 217 SER B CB  1 
ATOM   3734 O  OG  . SER B 1 217 ? 21.421  64.545 68.189 1.00 26.39 ? 217 SER B OG  1 
ATOM   3735 N  N   . VAL B 1 218 ? 21.188  67.080 66.142 1.00 17.30 ? 218 VAL B N   1 
ATOM   3736 C  CA  . VAL B 1 218 ? 21.542  66.982 64.726 1.00 16.70 ? 218 VAL B CA  1 
ATOM   3737 C  C   . VAL B 1 218 ? 22.955  67.554 64.649 1.00 17.66 ? 218 VAL B C   1 
ATOM   3738 O  O   . VAL B 1 218 ? 23.253  68.533 65.377 1.00 16.95 ? 218 VAL B O   1 
ATOM   3739 C  CB  . VAL B 1 218 ? 20.560  67.829 63.847 1.00 16.41 ? 218 VAL B CB  1 
ATOM   3740 C  CG1 . VAL B 1 218 ? 20.573  69.303 64.124 1.00 15.67 ? 218 VAL B CG1 1 
ATOM   3741 C  CG2 . VAL B 1 218 ? 20.737  67.586 62.322 1.00 15.69 ? 218 VAL B CG2 1 
ATOM   3742 N  N   . SER B 1 219 ? 23.798  67.002 63.755 1.00 18.43 ? 219 SER B N   1 
ATOM   3743 C  CA  . SER B 1 219 ? 25.142  67.564 63.665 1.00 20.06 ? 219 SER B CA  1 
ATOM   3744 C  C   . SER B 1 219 ? 25.234  68.645 62.584 1.00 19.47 ? 219 SER B C   1 
ATOM   3745 O  O   . SER B 1 219 ? 24.337  68.744 61.702 1.00 18.28 ? 219 SER B O   1 
ATOM   3746 C  CB  . SER B 1 219 ? 26.246  66.494 63.402 1.00 20.11 ? 219 SER B CB  1 
ATOM   3747 O  OG  . SER B 1 219 ? 26.077  65.990 62.084 1.00 18.91 ? 219 SER B OG  1 
ATOM   3748 N  N   A SER B 1 220 ? 26.300  69.431 62.678 0.50 18.59 ? 220 SER B N   1 
ATOM   3749 N  N   B SER B 1 220 ? 26.287  69.473 62.660 0.50 18.58 ? 220 SER B N   1 
ATOM   3750 C  CA  A SER B 1 220 ? 26.596  70.473 61.724 0.50 18.83 ? 220 SER B CA  1 
ATOM   3751 C  CA  B SER B 1 220 ? 26.594  70.474 61.621 0.50 18.81 ? 220 SER B CA  1 
ATOM   3752 C  C   A SER B 1 220 ? 26.751  69.918 60.286 0.50 19.15 ? 220 SER B C   1 
ATOM   3753 C  C   B SER B 1 220 ? 26.590  69.807 60.235 0.50 18.90 ? 220 SER B C   1 
ATOM   3754 O  O   A SER B 1 220 ? 26.391  70.650 59.339 0.50 18.50 ? 220 SER B O   1 
ATOM   3755 O  O   B SER B 1 220 ? 25.980  70.303 59.288 0.50 18.73 ? 220 SER B O   1 
ATOM   3756 C  CB  A SER B 1 220 ? 27.835  71.247 62.197 0.50 18.98 ? 220 SER B CB  1 
ATOM   3757 C  CB  B SER B 1 220 ? 27.945  71.182 61.903 0.50 19.55 ? 220 SER B CB  1 
ATOM   3758 O  OG  A SER B 1 220 ? 28.895  70.336 62.284 0.50 19.27 ? 220 SER B OG  1 
ATOM   3759 O  OG  B SER B 1 220 ? 28.149  72.336 61.072 0.50 19.05 ? 220 SER B OG  1 
ATOM   3760 N  N   . GLU B 1 221 ? 27.238  68.660 60.144 1.00 18.84 ? 221 GLU B N   1 
ATOM   3761 C  CA  . GLU B 1 221 ? 27.382  67.997 58.822 1.00 18.57 ? 221 GLU B CA  1 
ATOM   3762 C  C   . GLU B 1 221 ? 26.043  67.478 58.313 1.00 17.92 ? 221 GLU B C   1 
ATOM   3763 O  O   . GLU B 1 221 ? 25.771  67.532 57.117 1.00 18.89 ? 221 GLU B O   1 
ATOM   3764 C  CB  . GLU B 1 221 ? 28.446  66.916 58.799 1.00 18.85 ? 221 GLU B CB  1 
ATOM   3765 C  CG  . GLU B 1 221 ? 29.849  67.533 58.954 1.00 21.45 ? 221 GLU B CG  1 
ATOM   3766 C  CD  . GLU B 1 221 ? 30.048  68.078 60.371 1.00 23.02 ? 221 GLU B CD  1 
ATOM   3767 O  OE1 . GLU B 1 221 ? 29.652  67.348 61.325 1.00 25.65 ? 221 GLU B OE1 1 
ATOM   3768 O  OE2 . GLU B 1 221 ? 30.497  69.211 60.527 1.00 23.76 ? 221 GLU B OE2 1 
ATOM   3769 N  N   . GLN B 1 222 ? 25.179  67.035 59.214 1.00 17.55 ? 222 GLN B N   1 
ATOM   3770 C  CA  . GLN B 1 222 ? 23.831  66.586 58.825 1.00 17.35 ? 222 GLN B CA  1 
ATOM   3771 C  C   . GLN B 1 222 ? 23.005  67.738 58.300 1.00 18.52 ? 222 GLN B C   1 
ATOM   3772 O  O   . GLN B 1 222 ? 22.276  67.591 57.260 1.00 19.70 ? 222 GLN B O   1 
ATOM   3773 C  CB  . GLN B 1 222 ? 23.141  65.855 59.984 1.00 17.16 ? 222 GLN B CB  1 
ATOM   3774 C  CG  . GLN B 1 222 ? 23.827  64.532 60.362 1.00 16.47 ? 222 GLN B CG  1 
ATOM   3775 C  CD  . GLN B 1 222 ? 23.164  63.826 61.525 1.00 16.79 ? 222 GLN B CD  1 
ATOM   3776 O  OE1 . GLN B 1 222 ? 22.787  64.458 62.542 1.00 19.37 ? 222 GLN B OE1 1 
ATOM   3777 N  NE2 . GLN B 1 222 ? 22.951  62.520 61.377 1.00 18.28 ? 222 GLN B NE2 1 
ATOM   3778 N  N   . LEU B 1 223 ? 23.103  68.884 58.966 1.00 16.23 ? 223 LEU B N   1 
ATOM   3779 C  CA  . LEU B 1 223 ? 22.456  70.089 58.481 1.00 17.83 ? 223 LEU B CA  1 
ATOM   3780 C  C   . LEU B 1 223 ? 22.971  70.489 57.090 1.00 20.75 ? 223 LEU B C   1 
ATOM   3781 O  O   . LEU B 1 223 ? 22.170  70.919 56.215 1.00 19.01 ? 223 LEU B O   1 
ATOM   3782 C  CB  . LEU B 1 223 ? 22.568  71.282 59.440 1.00 18.14 ? 223 LEU B CB  1 
ATOM   3783 C  CG  . LEU B 1 223 ? 21.858  71.085 60.791 1.00 19.17 ? 223 LEU B CG  1 
ATOM   3784 C  CD1 . LEU B 1 223 ? 22.274  72.159 61.793 1.00 18.95 ? 223 LEU B CD1 1 
ATOM   3785 C  CD2 . LEU B 1 223 ? 20.340  71.136 60.537 1.00 21.04 ? 223 LEU B CD2 1 
ATOM   3786 N  N   . ALA B 1 224 ? 24.298  70.365 56.894 1.00 17.95 ? 224 ALA B N   1 
ATOM   3787 C  CA  . ALA B 1 224 ? 24.827  70.712 55.586 1.00 19.46 ? 224 ALA B CA  1 
ATOM   3788 C  C   . ALA B 1 224 ? 24.233  69.796 54.527 1.00 16.75 ? 224 ALA B C   1 
ATOM   3789 O  O   . ALA B 1 224 ? 24.161  70.231 53.332 1.00 19.98 ? 224 ALA B O   1 
ATOM   3790 C  CB  . ALA B 1 224 ? 26.351  70.569 55.575 1.00 18.19 ? 224 ALA B CB  1 
ATOM   3791 N  N   . GLN B 1 225 ? 23.937  68.547 54.867 1.00 18.45 ? 225 GLN B N   1 
ATOM   3792 C  CA  . GLN B 1 225 ? 23.351  67.622 53.882 1.00 19.57 ? 225 GLN B CA  1 
ATOM   3793 C  C   . GLN B 1 225 ? 21.975  68.146 53.454 1.00 20.73 ? 225 GLN B C   1 
ATOM   3794 O  O   . GLN B 1 225 ? 21.640  68.124 52.267 1.00 21.10 ? 225 GLN B O   1 
ATOM   3795 C  CB  . GLN B 1 225 ? 23.189  66.212 54.414 1.00 21.67 ? 225 GLN B CB  1 
ATOM   3796 C  CG  . GLN B 1 225 ? 24.522  65.483 54.557 1.00 19.29 ? 225 GLN B CG  1 
ATOM   3797 C  CD  . GLN B 1 225 ? 24.324  64.012 54.731 1.00 23.15 ? 225 GLN B CD  1 
ATOM   3798 O  OE1 . GLN B 1 225 ? 24.443  63.510 55.855 1.00 27.48 ? 225 GLN B OE1 1 
ATOM   3799 N  NE2 . GLN B 1 225 ? 23.884  63.311 53.659 1.00 25.30 ? 225 GLN B NE2 1 
ATOM   3800 N  N   . PHE B 1 226 ? 21.163  68.648 54.399 1.00 17.39 ? 226 PHE B N   1 
ATOM   3801 C  CA  . PHE B 1 226 ? 19.902  69.250 53.974 1.00 16.27 ? 226 PHE B CA  1 
ATOM   3802 C  C   . PHE B 1 226 ? 20.185  70.411 53.051 1.00 18.04 ? 226 PHE B C   1 
ATOM   3803 O  O   . PHE B 1 226 ? 19.462  70.606 52.028 1.00 18.20 ? 226 PHE B O   1 
ATOM   3804 C  CB  . PHE B 1 226 ? 19.131  69.839 55.167 1.00 17.28 ? 226 PHE B CB  1 
ATOM   3805 C  CG  . PHE B 1 226 ? 18.555  68.817 56.127 1.00 18.37 ? 226 PHE B CG  1 
ATOM   3806 C  CD1 . PHE B 1 226 ? 18.289  67.504 55.782 1.00 23.22 ? 226 PHE B CD1 1 
ATOM   3807 C  CD2 . PHE B 1 226 ? 18.285  69.212 57.441 1.00 21.90 ? 226 PHE B CD2 1 
ATOM   3808 C  CE1 . PHE B 1 226 ? 17.777  66.585 56.717 1.00 23.78 ? 226 PHE B CE1 1 
ATOM   3809 C  CE2 . PHE B 1 226 ? 17.735  68.340 58.341 1.00 21.97 ? 226 PHE B CE2 1 
ATOM   3810 C  CZ  . PHE B 1 226 ? 17.479  67.033 57.991 1.00 23.31 ? 226 PHE B CZ  1 
ATOM   3811 N  N   . ARG B 1 227 ? 21.183  71.238 53.391 1.00 17.62 ? 227 ARG B N   1 
ATOM   3812 C  CA  . ARG B 1 227 ? 21.473  72.437 52.612 1.00 19.13 ? 227 ARG B CA  1 
ATOM   3813 C  C   . ARG B 1 227 ? 22.035  72.144 51.220 1.00 20.49 ? 227 ARG B C   1 
ATOM   3814 O  O   . ARG B 1 227 ? 22.106  73.044 50.379 1.00 22.74 ? 227 ARG B O   1 
ATOM   3815 C  CB  . ARG B 1 227 ? 22.418  73.360 53.387 1.00 23.26 ? 227 ARG B CB  1 
ATOM   3816 C  CG  . ARG B 1 227 ? 21.702  74.266 54.379 1.00 23.54 ? 227 ARG B CG  1 
ATOM   3817 C  CD  . ARG B 1 227 ? 22.636  75.295 54.993 1.00 25.69 ? 227 ARG B CD  1 
ATOM   3818 N  NE  . ARG B 1 227 ? 22.378  75.486 56.419 1.00 33.23 ? 227 ARG B NE  1 
ATOM   3819 C  CZ  . ARG B 1 227 ? 23.121  74.962 57.387 1.00 28.26 ? 227 ARG B CZ  1 
ATOM   3820 N  NH1 . ARG B 1 227 ? 24.172  74.213 57.082 1.00 24.98 ? 227 ARG B NH1 1 
ATOM   3821 N  NH2 . ARG B 1 227 ? 22.813  75.184 58.659 1.00 25.00 ? 227 ARG B NH2 1 
ATOM   3822 N  N   . SER B 1 228 ? 22.434  70.897 50.973 1.00 17.66 ? 228 SER B N   1 
ATOM   3823 C  CA  . SER B 1 228 ? 23.044  70.575 49.726 1.00 19.45 ? 228 SER B CA  1 
ATOM   3824 C  C   . SER B 1 228 ? 21.979  70.106 48.752 1.00 20.05 ? 228 SER B C   1 
ATOM   3825 O  O   . SER B 1 228 ? 22.299  69.790 47.573 1.00 18.26 ? 228 SER B O   1 
ATOM   3826 C  CB  . SER B 1 228 ? 24.157  69.544 49.873 1.00 20.65 ? 228 SER B CB  1 
ATOM   3827 O  OG  . SER B 1 228 ? 23.645  68.246 50.069 1.00 27.54 ? 228 SER B OG  1 
ATOM   3828 N  N   . LEU B 1 229 ? 20.722  69.962 49.235 1.00 16.87 ? 229 LEU B N   1 
ATOM   3829 C  CA  . LEU B 1 229 ? 19.673  69.672 48.283 1.00 18.44 ? 229 LEU B CA  1 
ATOM   3830 C  C   . LEU B 1 229 ? 19.543  70.881 47.341 1.00 18.64 ? 229 LEU B C   1 
ATOM   3831 O  O   . LEU B 1 229 ? 19.811  71.999 47.729 1.00 17.04 ? 229 LEU B O   1 
ATOM   3832 C  CB  . LEU B 1 229 ? 18.333  69.420 49.007 1.00 18.43 ? 229 LEU B CB  1 
ATOM   3833 C  CG  . LEU B 1 229 ? 18.201  68.000 49.522 1.00 23.00 ? 229 LEU B CG  1 
ATOM   3834 C  CD1 . LEU B 1 229 ? 16.895  67.939 50.343 1.00 21.23 ? 229 LEU B CD1 1 
ATOM   3835 C  CD2 . LEU B 1 229 ? 18.113  66.945 48.414 1.00 21.78 ? 229 LEU B CD2 1 
ATOM   3836 N  N   . LEU B 1 230 ? 19.032  70.632 46.127 1.00 20.45 ? 230 LEU B N   1 
ATOM   3837 C  CA  . LEU B 1 230 ? 18.943  71.728 45.160 1.00 19.50 ? 230 LEU B CA  1 
ATOM   3838 C  C   . LEU B 1 230 ? 17.502  72.147 44.838 1.00 18.79 ? 230 LEU B C   1 
ATOM   3839 O  O   . LEU B 1 230 ? 16.675  71.307 44.642 1.00 19.46 ? 230 LEU B O   1 
ATOM   3840 C  CB  . LEU B 1 230 ? 19.668  71.297 43.854 1.00 20.06 ? 230 LEU B CB  1 
ATOM   3841 C  CG  . LEU B 1 230 ? 21.151  70.892 44.059 1.00 18.72 ? 230 LEU B CG  1 
ATOM   3842 C  CD1 . LEU B 1 230 ? 21.804  70.390 42.717 1.00 21.02 ? 230 LEU B CD1 1 
ATOM   3843 C  CD2 . LEU B 1 230 ? 22.004  72.030 44.619 1.00 17.49 ? 230 LEU B CD2 1 
ATOM   3844 N  N   . SER B 1 231 ? 17.249  73.444 44.731 1.00 19.72 ? 231 SER B N   1 
ATOM   3845 C  CA  . SER B 1 231 ? 15.881  73.956 44.475 1.00 19.53 ? 231 SER B CA  1 
ATOM   3846 C  C   . SER B 1 231 ? 15.550  73.993 42.964 1.00 20.92 ? 231 SER B C   1 
ATOM   3847 O  O   . SER B 1 231 ? 14.410  74.239 42.593 1.00 23.00 ? 231 SER B O   1 
ATOM   3848 C  CB  . SER B 1 231 ? 15.710  75.338 45.108 1.00 22.84 ? 231 SER B CB  1 
ATOM   3849 O  OG  . SER B 1 231 ? 16.688  76.302 44.583 1.00 27.57 ? 231 SER B OG  1 
ATOM   3850 N  N   . ASN B 1 232 ? 16.573  73.813 42.112 1.00 20.32 ? 232 ASN B N   1 
ATOM   3851 C  CA  . ASN B 1 232 ? 16.462  73.952 40.631 1.00 19.75 ? 232 ASN B CA  1 
ATOM   3852 C  C   . ASN B 1 232 ? 16.115  72.629 40.075 1.00 19.49 ? 232 ASN B C   1 
ATOM   3853 O  O   . ASN B 1 232 ? 16.222  71.593 40.772 1.00 19.54 ? 232 ASN B O   1 
ATOM   3854 C  CB  . ASN B 1 232 ? 17.776  74.490 40.037 1.00 20.41 ? 232 ASN B CB  1 
ATOM   3855 C  CG  . ASN B 1 232 ? 18.964  73.588 40.365 1.00 21.08 ? 232 ASN B CG  1 
ATOM   3856 O  OD1 . ASN B 1 232 ? 19.501  73.638 41.488 1.00 22.75 ? 232 ASN B OD1 1 
ATOM   3857 N  ND2 . ASN B 1 232 ? 19.309  72.703 39.451 1.00 20.36 ? 232 ASN B ND2 1 
ATOM   3858 N  N   . VAL B 1 233 ? 15.544  72.632 38.846 1.00 19.78 ? 233 VAL B N   1 
ATOM   3859 C  CA  . VAL B 1 233 ? 15.285  71.385 38.125 1.00 22.23 ? 233 VAL B CA  1 
ATOM   3860 C  C   . VAL B 1 233 ? 16.617  70.901 37.482 1.00 20.13 ? 233 VAL B C   1 
ATOM   3861 O  O   . VAL B 1 233 ? 17.496  71.708 37.272 1.00 24.53 ? 233 VAL B O   1 
ATOM   3862 C  CB  . VAL B 1 233 ? 14.114  71.554 37.087 1.00 26.88 ? 233 VAL B CB  1 
ATOM   3863 C  CG1 . VAL B 1 233 ? 12.862  72.125 37.761 1.00 31.46 ? 233 VAL B CG1 1 
ATOM   3864 C  CG2 . VAL B 1 233 ? 14.503  72.582 36.021 1.00 27.62 ? 233 VAL B CG2 1 
ATOM   3865 N  N   . GLU B 1 234 ? 16.698  69.614 37.230 1.00 23.60 ? 234 GLU B N   1 
ATOM   3866 C  CA  . GLU B 1 234 ? 17.841  68.895 36.645 1.00 24.81 ? 234 GLU B CA  1 
ATOM   3867 C  C   . GLU B 1 234 ? 18.311  69.611 35.394 1.00 28.99 ? 234 GLU B C   1 
ATOM   3868 O  O   . GLU B 1 234 ? 17.473  69.934 34.533 1.00 27.43 ? 234 GLU B O   1 
ATOM   3869 C  CB  . GLU B 1 234 ? 17.466  67.508 36.252 1.00 26.88 ? 234 GLU B CB  1 
ATOM   3870 C  CG  . GLU B 1 234 ? 18.704  66.666 36.033 1.00 30.17 ? 234 GLU B CG  1 
ATOM   3871 C  CD  . GLU B 1 234 ? 18.378  65.217 35.873 1.00 33.36 ? 234 GLU B CD  1 
ATOM   3872 O  OE1 . GLU B 1 234 ? 18.171  64.507 36.897 1.00 34.56 ? 234 GLU B OE1 1 
ATOM   3873 O  OE2 . GLU B 1 234 ? 18.344  64.745 34.724 1.00 34.80 ? 234 GLU B OE2 1 
ATOM   3874 N  N   . GLY B 1 235 ? 19.608  69.902 35.345 1.00 28.86 ? 235 GLY B N   1 
ATOM   3875 C  CA  . GLY B 1 235 ? 20.206  70.578 34.177 1.00 32.15 ? 235 GLY B CA  1 
ATOM   3876 C  C   . GLY B 1 235 ? 20.467  72.063 34.360 1.00 30.71 ? 235 GLY B C   1 
ATOM   3877 O  O   . GLY B 1 235 ? 21.414  72.577 33.763 1.00 37.28 ? 235 GLY B O   1 
ATOM   3878 N  N   . ASP B 1 236 ? 19.665  72.769 35.168 1.00 25.02 ? 236 ASP B N   1 
ATOM   3879 C  CA  . ASP B 1 236 ? 19.855  74.148 35.435 1.00 24.75 ? 236 ASP B CA  1 
ATOM   3880 C  C   . ASP B 1 236 ? 21.063  74.304 36.360 1.00 26.46 ? 236 ASP B C   1 
ATOM   3881 O  O   . ASP B 1 236 ? 21.532  73.305 36.901 1.00 31.66 ? 236 ASP B O   1 
ATOM   3882 C  CB  . ASP B 1 236 ? 18.599  74.827 35.990 1.00 29.27 ? 236 ASP B CB  1 
ATOM   3883 C  CG  . ASP B 1 236 ? 17.573  75.119 34.914 1.00 36.18 ? 236 ASP B CG  1 
ATOM   3884 O  OD1 . ASP B 1 236 ? 16.505  75.668 35.247 1.00 30.04 ? 236 ASP B OD1 1 
ATOM   3885 O  OD2 . ASP B 1 236 ? 17.841  74.744 33.751 1.00 33.56 ? 236 ASP B OD2 1 
ATOM   3886 N  N   . ASN B 1 237 ? 21.584  75.514 36.482 1.00 30.60 ? 237 ASN B N   1 
ATOM   3887 C  CA  . ASN B 1 237 ? 22.718  75.738 37.406 1.00 29.03 ? 237 ASN B CA  1 
ATOM   3888 C  C   . ASN B 1 237 ? 22.251  75.424 38.850 1.00 30.91 ? 237 ASN B C   1 
ATOM   3889 O  O   . ASN B 1 237 ? 21.151  75.835 39.266 1.00 30.49 ? 237 ASN B O   1 
ATOM   3890 C  CB  . ASN B 1 237 ? 23.222  77.134 37.333 1.00 32.07 ? 237 ASN B CB  1 
ATOM   3891 C  CG  . ASN B 1 237 ? 24.407  77.349 38.237 1.00 39.10 ? 237 ASN B CG  1 
ATOM   3892 O  OD1 . ASN B 1 237 ? 25.428  76.645 38.135 1.00 34.86 ? 237 ASN B OD1 1 
ATOM   3893 N  ND2 . ASN B 1 237 ? 24.261  78.276 39.188 1.00 39.98 ? 237 ASN B ND2 1 
ATOM   3894 N  N   . ALA B 1 238 ? 23.075  74.663 39.553 1.00 27.34 ? 238 ALA B N   1 
ATOM   3895 C  CA  . ALA B 1 238 ? 22.752  74.213 40.929 1.00 28.97 ? 238 ALA B CA  1 
ATOM   3896 C  C   . ALA B 1 238 ? 22.637  75.282 41.981 1.00 31.56 ? 238 ALA B C   1 
ATOM   3897 O  O   . ALA B 1 238 ? 23.594  75.974 42.262 1.00 39.02 ? 238 ALA B O   1 
ATOM   3898 C  CB  . ALA B 1 238 ? 23.690  73.069 41.340 1.00 29.74 ? 238 ALA B CB  1 
ATOM   3899 N  N   . VAL B 1 239 ? 21.437  75.400 42.587 1.00 29.36 ? 239 VAL B N   1 
ATOM   3900 C  CA  . VAL B 1 239 ? 21.116  76.402 43.567 1.00 22.93 ? 239 VAL B CA  1 
ATOM   3901 C  C   . VAL B 1 239 ? 20.689  75.708 44.912 1.00 24.06 ? 239 VAL B C   1 
ATOM   3902 O  O   . VAL B 1 239 ? 19.611  75.061 44.995 1.00 24.06 ? 239 VAL B O   1 
ATOM   3903 C  CB  . VAL B 1 239 ? 19.976  77.293 43.154 1.00 24.58 ? 239 VAL B CB  1 
ATOM   3904 C  CG1 . VAL B 1 239 ? 19.704  78.328 44.226 1.00 23.72 ? 239 VAL B CG1 1 
ATOM   3905 C  CG2 . VAL B 1 239 ? 20.186  77.958 41.792 1.00 28.53 ? 239 VAL B CG2 1 
ATOM   3906 N  N   . PRO B 1 240 ? 21.537  75.802 45.911 1.00 22.76 ? 240 PRO B N   1 
ATOM   3907 C  CA  . PRO B 1 240 ? 21.256  74.972 47.141 1.00 20.98 ? 240 PRO B CA  1 
ATOM   3908 C  C   . PRO B 1 240 ? 20.053  75.499 47.892 1.00 21.28 ? 240 PRO B C   1 
ATOM   3909 O  O   . PRO B 1 240 ? 19.748  76.705 47.842 1.00 21.95 ? 240 PRO B O   1 
ATOM   3910 C  CB  . PRO B 1 240 ? 22.526  75.162 47.988 1.00 24.53 ? 240 PRO B CB  1 
ATOM   3911 C  CG  . PRO B 1 240 ? 23.614  75.444 46.934 1.00 26.76 ? 240 PRO B CG  1 
ATOM   3912 C  CD  . PRO B 1 240 ? 22.925  76.371 45.945 1.00 25.61 ? 240 PRO B CD  1 
ATOM   3913 N  N   . MET B 1 241 ? 19.377  74.613 48.620 1.00 21.53 ? 241 MET B N   1 
ATOM   3914 C  CA  . MET B 1 241 ? 18.212  75.029 49.474 1.00 21.68 ? 241 MET B CA  1 
ATOM   3915 C  C   . MET B 1 241 ? 18.823  75.479 50.828 1.00 22.23 ? 241 MET B C   1 
ATOM   3916 O  O   . MET B 1 241 ? 19.025  74.670 51.735 1.00 22.68 ? 241 MET B O   1 
ATOM   3917 C  CB  . MET B 1 241 ? 17.329  73.856 49.850 1.00 24.81 ? 241 MET B CB  1 
ATOM   3918 C  CG  . MET B 1 241 ? 16.291  73.461 48.831 1.00 26.65 ? 241 MET B CG  1 
ATOM   3919 S  SD  . MET B 1 241 ? 15.491  71.961 49.405 1.00 21.09 ? 241 MET B SD  1 
ATOM   3920 C  CE  . MET B 1 241 ? 15.169  71.236 47.808 1.00 21.38 ? 241 MET B CE  1 
ATOM   3921 N  N   . GLN B 1 242 ? 19.115  76.757 50.949 1.00 21.42 ? 242 GLN B N   1 
ATOM   3922 C  CA  . GLN B 1 242 ? 19.829  77.241 52.091 1.00 22.85 ? 242 GLN B CA  1 
ATOM   3923 C  C   . GLN B 1 242 ? 18.986  77.361 53.330 1.00 20.15 ? 242 GLN B C   1 
ATOM   3924 O  O   . GLN B 1 242 ? 19.505  77.159 54.450 1.00 22.78 ? 242 GLN B O   1 
ATOM   3925 C  CB  . GLN B 1 242 ? 20.501  78.540 51.765 1.00 26.99 ? 242 GLN B CB  1 
ATOM   3926 C  CG  . GLN B 1 242 ? 21.796  78.151 51.046 1.00 35.13 ? 242 GLN B CG  1 
ATOM   3927 C  CD  . GLN B 1 242 ? 22.643  79.337 50.661 1.00 42.33 ? 242 GLN B CD  1 
ATOM   3928 O  OE1 . GLN B 1 242 ? 22.435  80.443 51.164 1.00 45.27 ? 242 GLN B OE1 1 
ATOM   3929 N  NE2 . GLN B 1 242 ? 23.618  79.113 49.803 1.00 47.50 ? 242 GLN B NE2 1 
ATOM   3930 N  N   . HIS B 1 243 ? 17.703  77.641 53.140 1.00 20.16 ? 243 HIS B N   1 
ATOM   3931 C  CA  . HIS B 1 243 ? 16.800  77.872 54.272 1.00 18.44 ? 243 HIS B CA  1 
ATOM   3932 C  C   . HIS B 1 243 ? 15.355  77.787 53.902 1.00 18.26 ? 243 HIS B C   1 
ATOM   3933 O  O   . HIS B 1 243 ? 14.997  77.964 52.731 1.00 20.44 ? 243 HIS B O   1 
ATOM   3934 C  CB  . HIS B 1 243 ? 17.062  79.254 54.897 1.00 21.40 ? 243 HIS B CB  1 
ATOM   3935 C  CG  . HIS B 1 243 ? 16.950  80.410 53.916 1.00 25.77 ? 243 HIS B CG  1 
ATOM   3936 N  ND1 . HIS B 1 243 ? 15.853  81.159 53.841 1.00 34.70 ? 243 HIS B ND1 1 
ATOM   3937 C  CD2 . HIS B 1 243 ? 17.847  80.941 52.987 1.00 34.29 ? 243 HIS B CD2 1 
ATOM   3938 C  CE1 . HIS B 1 243 ? 16.022  82.127 52.903 1.00 34.91 ? 243 HIS B CE1 1 
ATOM   3939 N  NE2 . HIS B 1 243 ? 17.230  81.999 52.390 1.00 28.91 ? 243 HIS B NE2 1 
ATOM   3940 N  N   . ASN B 1 244 ? 14.511  77.444 54.893 1.00 16.40 ? 244 ASN B N   1 
ATOM   3941 C  CA  . ASN B 1 244 ? 13.114  77.303 54.582 1.00 15.84 ? 244 ASN B CA  1 
ATOM   3942 C  C   . ASN B 1 244 ? 12.244  77.416 55.872 1.00 16.21 ? 244 ASN B C   1 
ATOM   3943 O  O   . ASN B 1 244 ? 11.138  76.794 55.990 1.00 16.66 ? 244 ASN B O   1 
ATOM   3944 C  CB  . ASN B 1 244 ? 12.889  76.025 53.775 1.00 15.24 ? 244 ASN B CB  1 
ATOM   3945 C  CG  . ASN B 1 244 ? 13.303  74.804 54.533 1.00 16.23 ? 244 ASN B CG  1 
ATOM   3946 O  OD1 . ASN B 1 244 ? 13.555  74.915 55.750 1.00 17.00 ? 244 ASN B OD1 1 
ATOM   3947 N  ND2 . ASN B 1 244 ? 13.429  73.644 53.848 1.00 16.30 ? 244 ASN B ND2 1 
ATOM   3948 N  N   . ASN B 1 245 ? 12.663  78.334 56.758 1.00 16.19 ? 245 ASN B N   1 
ATOM   3949 C  CA  . ASN B 1 245 ? 11.876  78.610 57.953 1.00 15.77 ? 245 ASN B CA  1 
ATOM   3950 C  C   . ASN B 1 245 ? 11.130  79.935 57.920 1.00 18.20 ? 245 ASN B C   1 
ATOM   3951 O  O   . ASN B 1 245 ? 11.685  80.999 57.540 1.00 22.67 ? 245 ASN B O   1 
ATOM   3952 C  CB  . ASN B 1 245 ? 12.754  78.433 59.209 1.00 17.56 ? 245 ASN B CB  1 
ATOM   3953 C  CG  . ASN B 1 245 ? 13.896  79.446 59.301 1.00 22.16 ? 245 ASN B CG  1 
ATOM   3954 O  OD1 . ASN B 1 245 ? 13.793  80.478 60.016 1.00 26.61 ? 245 ASN B OD1 1 
ATOM   3955 N  ND2 . ASN B 1 245 ? 14.927  79.203 58.593 1.00 28.12 ? 245 ASN B ND2 1 
ATOM   3956 N  N   . ARG B 1 246 ? 9.875   79.895 58.328 1.00 16.62 ? 246 ARG B N   1 
ATOM   3957 C  CA  . ARG B 1 246 ? 9.086   81.100 58.387 1.00 16.20 ? 246 ARG B CA  1 
ATOM   3958 C  C   . ARG B 1 246 ? 9.304   81.798 59.737 1.00 18.33 ? 246 ARG B C   1 
ATOM   3959 O  O   . ARG B 1 246 ? 9.369   81.161 60.764 1.00 16.56 ? 246 ARG B O   1 
ATOM   3960 C  CB  . ARG B 1 246 ? 7.588   80.787 58.167 1.00 16.28 ? 246 ARG B CB  1 
ATOM   3961 C  CG  . ARG B 1 246 ? 6.737   82.052 58.152 1.00 14.78 ? 246 ARG B CG  1 
ATOM   3962 C  CD  . ARG B 1 246 ? 5.252   81.695 58.278 1.00 15.23 ? 246 ARG B CD  1 
ATOM   3963 N  NE  . ARG B 1 246 ? 4.412   82.859 57.808 1.00 17.78 ? 246 ARG B NE  1 
ATOM   3964 C  CZ  . ARG B 1 246 ? 3.090   82.895 57.944 1.00 18.44 ? 246 ARG B CZ  1 
ATOM   3965 N  NH1 . ARG B 1 246 ? 2.417   81.935 58.613 1.00 18.88 ? 246 ARG B NH1 1 
ATOM   3966 N  NH2 . ARG B 1 246 ? 2.400   83.958 57.454 1.00 21.28 ? 246 ARG B NH2 1 
ATOM   3967 N  N   . PRO B 1 247 ? 9.394   83.136 59.744 1.00 17.55 ? 247 PRO B N   1 
ATOM   3968 C  CA  . PRO B 1 247 ? 9.458   83.810 61.071 1.00 17.26 ? 247 PRO B CA  1 
ATOM   3969 C  C   . PRO B 1 247 ? 8.216   83.564 61.967 1.00 17.58 ? 247 PRO B C   1 
ATOM   3970 O  O   . PRO B 1 247 ? 7.131   83.266 61.478 1.00 19.19 ? 247 PRO B O   1 
ATOM   3971 C  CB  . PRO B 1 247 ? 9.506   85.332 60.697 1.00 17.65 ? 247 PRO B CB  1 
ATOM   3972 C  CG  . PRO B 1 247 ? 9.962   85.353 59.236 1.00 19.69 ? 247 PRO B CG  1 
ATOM   3973 C  CD  . PRO B 1 247 ? 9.411   84.098 58.617 1.00 20.37 ? 247 PRO B CD  1 
ATOM   3974 N  N   . THR B 1 248 ? 8.342   83.717 63.300 1.00 17.72 ? 248 THR B N   1 
ATOM   3975 C  CA  . THR B 1 248 ? 7.181   83.547 64.177 1.00 18.95 ? 248 THR B CA  1 
ATOM   3976 C  C   . THR B 1 248 ? 6.168   84.654 63.929 1.00 19.15 ? 248 THR B C   1 
ATOM   3977 O  O   . THR B 1 248 ? 6.582   85.804 63.613 1.00 22.09 ? 248 THR B O   1 
ATOM   3978 C  CB  . THR B 1 248 ? 7.574   83.453 65.692 1.00 19.19 ? 248 THR B CB  1 
ATOM   3979 O  OG1 . THR B 1 248 ? 8.374   84.618 66.015 1.00 21.16 ? 248 THR B OG1 1 
ATOM   3980 C  CG2 . THR B 1 248 ? 8.484   82.181 65.967 1.00 16.45 ? 248 THR B CG2 1 
ATOM   3981 N  N   . GLN B 1 249 ? 4.899   84.288 64.091 1.00 18.41 ? 249 GLN B N   1 
ATOM   3982 C  CA  . GLN B 1 249 ? 3.745   85.137 63.815 1.00 21.67 ? 249 GLN B CA  1 
ATOM   3983 C  C   . GLN B 1 249 ? 3.045   85.523 65.090 1.00 24.09 ? 249 GLN B C   1 
ATOM   3984 O  O   . GLN B 1 249 ? 3.123   84.825 66.119 1.00 23.15 ? 249 GLN B O   1 
ATOM   3985 C  CB  . GLN B 1 249 ? 2.783   84.419 62.853 1.00 22.91 ? 249 GLN B CB  1 
ATOM   3986 C  CG  . GLN B 1 249 ? 3.496   84.020 61.574 1.00 20.27 ? 249 GLN B CG  1 
ATOM   3987 C  CD  . GLN B 1 249 ? 4.061   85.202 60.802 1.00 21.77 ? 249 GLN B CD  1 
ATOM   3988 O  OE1 . GLN B 1 249 ? 3.387   86.222 60.661 1.00 25.02 ? 249 GLN B OE1 1 
ATOM   3989 N  NE2 . GLN B 1 249 ? 5.300   85.090 60.297 1.00 22.21 ? 249 GLN B NE2 1 
ATOM   3990 N  N   . PRO B 1 250 ? 2.330   86.657 65.035 1.00 22.87 ? 250 PRO B N   1 
ATOM   3991 C  CA  . PRO B 1 250 ? 1.695   87.087 66.295 1.00 25.60 ? 250 PRO B CA  1 
ATOM   3992 C  C   . PRO B 1 250 ? 0.689   86.121 66.842 1.00 23.90 ? 250 PRO B C   1 
ATOM   3993 O  O   . PRO B 1 250 ? -0.095  85.573 66.063 1.00 21.50 ? 250 PRO B O   1 
ATOM   3994 C  CB  . PRO B 1 250 ? 0.963   88.388 65.908 1.00 27.41 ? 250 PRO B CB  1 
ATOM   3995 C  CG  . PRO B 1 250 ? 1.251   88.662 64.488 1.00 30.15 ? 250 PRO B CG  1 
ATOM   3996 C  CD  . PRO B 1 250 ? 2.082   87.538 63.895 1.00 28.20 ? 250 PRO B CD  1 
ATOM   3997 N  N   . LEU B 1 251 ? 0.668   85.881 68.167 1.00 23.64 ? 251 LEU B N   1 
ATOM   3998 C  CA  . LEU B 1 251 ? -0.377  85.053 68.763 1.00 26.35 ? 251 LEU B CA  1 
ATOM   3999 C  C   . LEU B 1 251 ? -1.820  85.531 68.640 1.00 25.27 ? 251 LEU B C   1 
ATOM   4000 O  O   . LEU B 1 251 ? -2.713  84.750 68.593 1.00 22.24 ? 251 LEU B O   1 
ATOM   4001 C  CB  . LEU B 1 251 ? -0.112  84.806 70.262 1.00 31.80 ? 251 LEU B CB  1 
ATOM   4002 C  CG  . LEU B 1 251 ? 0.712   83.672 70.808 1.00 31.34 ? 251 LEU B CG  1 
ATOM   4003 C  CD1 . LEU B 1 251 ? 0.797   83.797 72.357 1.00 32.99 ? 251 LEU B CD1 1 
ATOM   4004 C  CD2 . LEU B 1 251 ? 0.283   82.299 70.307 1.00 25.34 ? 251 LEU B CD2 1 
ATOM   4005 N  N   . LYS B 1 252 ? -2.050  86.845 68.602 1.00 27.56 ? 252 LYS B N   1 
ATOM   4006 C  CA  . LYS B 1 252 ? -3.392  87.392 68.427 1.00 28.62 ? 252 LYS B CA  1 
ATOM   4007 C  C   . LYS B 1 252 ? -4.416  86.827 69.392 1.00 25.33 ? 252 LYS B C   1 
ATOM   4008 O  O   . LYS B 1 252 ? -5.552  86.514 69.030 1.00 30.05 ? 252 LYS B O   1 
ATOM   4009 C  CB  . LYS B 1 252 ? -3.847  87.381 66.960 1.00 27.19 ? 252 LYS B CB  1 
ATOM   4010 C  CG  . LYS B 1 252 ? -2.800  88.105 66.119 1.00 31.20 ? 252 LYS B CG  1 
ATOM   4011 C  CD  . LYS B 1 252 ? -3.254  88.451 64.725 1.00 39.07 ? 252 LYS B CD  1 
ATOM   4012 C  CE  . LYS B 1 252 ? -3.917  89.810 64.745 1.00 50.94 ? 252 LYS B CE  1 
ATOM   4013 N  NZ  . LYS B 1 252 ? -2.857  90.862 64.719 1.00 57.15 ? 252 LYS B NZ  1 
ATOM   4014 N  N   . GLY B 1 253 ? -3.946  86.682 70.615 1.00 26.07 ? 253 GLY B N   1 
ATOM   4015 C  CA  . GLY B 1 253 ? -4.821  86.319 71.717 1.00 31.17 ? 253 GLY B CA  1 
ATOM   4016 C  C   . GLY B 1 253 ? -4.955  84.833 71.936 1.00 30.15 ? 253 GLY B C   1 
ATOM   4017 O  O   . GLY B 1 253 ? -5.616  84.423 72.882 1.00 27.70 ? 253 GLY B O   1 
ATOM   4018 N  N   . ARG B 1 254 ? -4.300  83.992 71.095 1.00 25.52 ? 254 ARG B N   1 
ATOM   4019 C  CA  . ARG B 1 254 ? -4.412  82.535 71.350 1.00 22.38 ? 254 ARG B CA  1 
ATOM   4020 C  C   . ARG B 1 254 ? -3.690  82.165 72.640 1.00 22.32 ? 254 ARG B C   1 
ATOM   4021 O  O   . ARG B 1 254 ? -2.742  82.871 73.102 1.00 25.77 ? 254 ARG B O   1 
ATOM   4022 C  CB  . ARG B 1 254 ? -3.794  81.760 70.159 1.00 20.30 ? 254 ARG B CB  1 
ATOM   4023 C  CG  . ARG B 1 254 ? -4.621  81.794 68.885 1.00 21.28 ? 254 ARG B CG  1 
ATOM   4024 C  CD  . ARG B 1 254 ? -3.729  81.317 67.722 1.00 20.30 ? 254 ARG B CD  1 
ATOM   4025 N  NE  . ARG B 1 254 ? -2.659  82.209 67.300 1.00 19.43 ? 254 ARG B NE  1 
ATOM   4026 C  CZ  . ARG B 1 254 ? -1.809  81.906 66.312 1.00 19.75 ? 254 ARG B CZ  1 
ATOM   4027 N  NH1 . ARG B 1 254 ? -1.838  80.687 65.763 1.00 18.16 ? 254 ARG B NH1 1 
ATOM   4028 N  NH2 . ARG B 1 254 ? -0.911  82.742 65.935 1.00 17.92 ? 254 ARG B NH2 1 
ATOM   4029 N  N   . THR B 1 255 ? -4.051  81.000 73.152 1.00 21.93 ? 255 THR B N   1 
ATOM   4030 C  CA  . THR B 1 255 ? -3.440  80.424 74.336 1.00 19.62 ? 255 THR B CA  1 
ATOM   4031 C  C   . THR B 1 255 ? -2.635  79.221 73.956 1.00 18.73 ? 255 THR B C   1 
ATOM   4032 O  O   . THR B 1 255 ? -3.143  78.309 73.300 1.00 21.60 ? 255 THR B O   1 
ATOM   4033 C  CB  . THR B 1 255 ? -4.547  79.928 75.293 1.00 24.75 ? 255 THR B CB  1 
ATOM   4034 O  OG1 . THR B 1 255 ? -5.261  81.095 75.680 1.00 29.81 ? 255 THR B OG1 1 
ATOM   4035 C  CG2 . THR B 1 255 ? -3.999  79.289 76.565 1.00 26.89 ? 255 THR B CG2 1 
ATOM   4036 N  N   . VAL B 1 256 ? -1.406  79.202 74.403 1.00 17.73 ? 256 VAL B N   1 
ATOM   4037 C  CA  . VAL B 1 256 ? -0.618  77.949 74.310 1.00 16.08 ? 256 VAL B CA  1 
ATOM   4038 C  C   . VAL B 1 256 ? -0.849  77.098 75.539 1.00 17.36 ? 256 VAL B C   1 
ATOM   4039 O  O   . VAL B 1 256 ? -0.483  77.535 76.665 1.00 21.18 ? 256 VAL B O   1 
ATOM   4040 C  CB  . VAL B 1 256 ? 0.885   78.243 74.102 1.00 15.69 ? 256 VAL B CB  1 
ATOM   4041 C  CG1 . VAL B 1 256 ? 1.703   76.947 74.019 1.00 15.96 ? 256 VAL B CG1 1 
ATOM   4042 C  CG2 . VAL B 1 256 ? 1.071   79.100 72.861 1.00 17.85 ? 256 VAL B CG2 1 
ATOM   4043 N  N   . ARG B 1 257 ? -1.336  75.857 75.343 1.00 17.23 ? 257 ARG B N   1 
ATOM   4044 C  CA  . ARG B 1 257 ? -1.569  74.978 76.509 1.00 17.80 ? 257 ARG B CA  1 
ATOM   4045 C  C   . ARG B 1 257 ? -0.400  74.064 76.689 1.00 20.23 ? 257 ARG B C   1 
ATOM   4046 O  O   . ARG B 1 257 ? 0.215   73.646 75.670 1.00 17.03 ? 257 ARG B O   1 
ATOM   4047 C  CB  . ARG B 1 257 ? -2.864  74.215 76.342 1.00 16.71 ? 257 ARG B CB  1 
ATOM   4048 C  CG  . ARG B 1 257 ? -4.073  75.099 76.232 1.00 20.03 ? 257 ARG B CG  1 
ATOM   4049 C  CD  . ARG B 1 257 ? -5.328  74.234 76.036 1.00 23.08 ? 257 ARG B CD  1 
ATOM   4050 N  NE  . ARG B 1 257 ? -5.492  73.716 74.650 1.00 23.16 ? 257 ARG B NE  1 
ATOM   4051 C  CZ  . ARG B 1 257 ? -6.290  72.709 74.256 1.00 25.01 ? 257 ARG B CZ  1 
ATOM   4052 N  NH1 . ARG B 1 257 ? -7.056  72.040 75.101 1.00 28.52 ? 257 ARG B NH1 1 
ATOM   4053 N  NH2 . ARG B 1 257 ? -6.339  72.366 72.977 1.00 28.57 ? 257 ARG B NH2 1 
ATOM   4054 N  N   . ALA B 1 258 ? -0.127  73.709 77.952 1.00 16.50 ? 258 ALA B N   1 
ATOM   4055 C  CA  . ALA B 1 258 ? 0.951   72.742 78.321 1.00 17.71 ? 258 ALA B CA  1 
ATOM   4056 C  C   . ALA B 1 258 ? 0.360   71.445 78.833 1.00 20.43 ? 258 ALA B C   1 
ATOM   4057 O  O   . ALA B 1 258 ? -0.601  71.463 79.636 1.00 18.72 ? 258 ALA B O   1 
ATOM   4058 C  CB  . ALA B 1 258 ? 1.844   73.351 79.394 1.00 19.29 ? 258 ALA B CB  1 
ATOM   4059 N  N   A SER B 1 259 ? 0.886   70.298 78.384 0.50 16.90 ? 259 SER B N   1 
ATOM   4060 N  N   B SER B 1 259 ? 0.909   70.315 78.369 0.50 17.49 ? 259 SER B N   1 
ATOM   4061 C  CA  A SER B 1 259 ? 0.438   68.996 78.871 0.50 17.94 ? 259 SER B CA  1 
ATOM   4062 C  CA  B SER B 1 259 ? 0.669   69.017 78.977 0.50 19.16 ? 259 SER B CA  1 
ATOM   4063 C  C   A SER B 1 259 ? 1.017   68.608 80.247 0.50 18.74 ? 259 SER B C   1 
ATOM   4064 C  C   B SER B 1 259 ? 1.308   68.926 80.385 0.50 20.94 ? 259 SER B C   1 
ATOM   4065 O  O   A SER B 1 259 ? 0.508   67.678 80.871 0.50 18.93 ? 259 SER B O   1 
ATOM   4066 O  O   B SER B 1 259 ? 2.140   69.754 80.784 0.50 22.15 ? 259 SER B O   1 
ATOM   4067 C  CB  A SER B 1 259 ? 0.786   67.894 77.860 0.50 18.02 ? 259 SER B CB  1 
ATOM   4068 C  CB  B SER B 1 259 ? 1.189   67.875 78.075 0.50 18.57 ? 259 SER B CB  1 
ATOM   4069 O  OG  A SER B 1 259 ? 2.173   67.603 77.885 0.50 19.04 ? 259 SER B OG  1 
ATOM   4070 O  OG  B SER B 1 259 ? 2.600   67.693 78.228 0.50 17.64 ? 259 SER B OG  1 
ATOM   4071 N  N   A PHE B 1 260 ? 2.044   69.355 80.674 0.50 19.37 ? 260 PHE B N   1 
ATOM   4072 N  N   B PHE B 1 260 ? 0.893   67.904 81.116 0.50 24.42 ? 260 PHE B N   1 
ATOM   4073 C  CA  A PHE B 1 260 ? 3.004   69.028 81.747 0.50 19.19 ? 260 PHE B CA  1 
ATOM   4074 C  CA  B PHE B 1 260 ? 1.307   67.694 82.508 0.50 25.19 ? 260 PHE B CA  1 
ATOM   4075 C  C   A PHE B 1 260 ? 3.167   70.185 82.768 0.50 20.59 ? 260 PHE B C   1 
ATOM   4076 C  C   B PHE B 1 260 ? 2.825   67.695 82.729 0.50 26.98 ? 260 PHE B C   1 
ATOM   4077 O  O   A PHE B 1 260 ? 2.876   71.357 82.458 0.50 22.22 ? 260 PHE B O   1 
ATOM   4078 O  O   B PHE B 1 260 ? 3.310   68.288 83.721 0.50 27.60 ? 260 PHE B O   1 
ATOM   4079 C  CB  A PHE B 1 260 ? 4.371   68.721 81.119 0.50 20.04 ? 260 PHE B CB  1 
ATOM   4080 C  CB  B PHE B 1 260 ? 0.687   66.391 83.026 0.50 28.14 ? 260 PHE B CB  1 
ATOM   4081 C  CG  A PHE B 1 260 ? 4.971   69.908 80.404 0.50 19.93 ? 260 PHE B CG  1 
ATOM   4082 C  CG  B PHE B 1 260 ? 0.763   66.234 84.515 0.50 30.07 ? 260 PHE B CG  1 
ATOM   4083 C  CD1 A PHE B 1 260 ? 5.768   70.805 81.081 0.50 20.72 ? 260 PHE B CD1 1 
ATOM   4084 C  CD1 B PHE B 1 260 ? 1.879   65.680 85.104 0.50 31.97 ? 260 PHE B CD1 1 
ATOM   4085 C  CD2 A PHE B 1 260 ? 4.697   70.127 79.086 0.50 19.88 ? 260 PHE B CD2 1 
ATOM   4086 C  CD2 B PHE B 1 260 ? -0.283  66.641 85.319 0.50 29.12 ? 260 PHE B CD2 1 
ATOM   4087 C  CE1 A PHE B 1 260 ? 6.320   71.903 80.435 0.50 23.10 ? 260 PHE B CE1 1 
ATOM   4088 C  CE1 B PHE B 1 260 ? 1.953   65.536 86.476 0.50 30.06 ? 260 PHE B CE1 1 
ATOM   4089 C  CE2 A PHE B 1 260 ? 5.218   71.189 78.424 0.50 17.60 ? 260 PHE B CE2 1 
ATOM   4090 C  CE2 B PHE B 1 260 ? -0.221  66.491 86.681 0.50 28.50 ? 260 PHE B CE2 1 
ATOM   4091 C  CZ  A PHE B 1 260 ? 6.053   72.085 79.079 0.50 23.83 ? 260 PHE B CZ  1 
ATOM   4092 C  CZ  B PHE B 1 260 ? 0.897   65.944 87.265 0.50 30.56 ? 260 PHE B CZ  1 
HETATM 4093 ZN ZN  . ZN  C 2 .   ? 18.040  36.371 20.762 1.00 15.96 ? 301 ZN  A ZN  1 
HETATM 4094 C  C6  A 3UF D 3 .   ? 14.117  36.904 18.066 0.50 25.02 ? 302 3UF A C6  1 
HETATM 4095 C  C6  B 3UF D 3 .   ? 14.018  37.211 18.137 0.50 31.01 ? 302 3UF A C6  1 
HETATM 4096 C  C5  A 3UF D 3 .   ? 14.279  36.026 19.122 0.50 20.96 ? 302 3UF A C5  1 
HETATM 4097 C  C5  B 3UF D 3 .   ? 14.250  36.186 19.055 0.50 26.70 ? 302 3UF A C5  1 
HETATM 4098 O  O4  A 3UF D 3 .   ? 14.155  37.748 21.116 0.50 17.97 ? 302 3UF A O4  1 
HETATM 4099 O  O4  B 3UF D 3 .   ? 14.183  37.669 21.250 0.50 23.49 ? 302 3UF A O4  1 
HETATM 4100 S  S2  A 3UF D 3 .   ? 15.054  36.688 20.595 0.50 17.44 ? 302 3UF A S2  1 
HETATM 4101 S  S2  B 3UF D 3 .   ? 15.067  36.658 20.588 0.50 23.14 ? 302 3UF A S2  1 
HETATM 4102 O  O1  A 3UF D 3 .   ? 15.164  35.538 21.612 0.50 19.39 ? 302 3UF A O1  1 
HETATM 4103 O  O1  B 3UF D 3 .   ? 15.227  35.429 21.508 0.50 23.89 ? 302 3UF A O1  1 
HETATM 4104 N  N3  A 3UF D 3 .   ? 16.626  37.316 20.392 0.50 16.72 ? 302 3UF A N3  1 
HETATM 4105 N  N3  B 3UF D 3 .   ? 16.639  37.328 20.417 0.50 21.41 ? 302 3UF A N3  1 
HETATM 4106 C  C10 A 3UF D 3 .   ? 13.799  34.705 19.095 0.50 24.90 ? 302 3UF A C10 1 
HETATM 4107 C  C10 B 3UF D 3 .   ? 13.803  34.877 18.804 0.50 31.95 ? 302 3UF A C10 1 
HETATM 4108 C  C9  A 3UF D 3 .   ? 13.171  34.230 17.929 0.50 27.91 ? 302 3UF A C9  1 
HETATM 4109 C  C9  B 3UF D 3 .   ? 13.147  34.599 17.586 0.50 34.55 ? 302 3UF A C9  1 
HETATM 4110 C  C8  A 3UF D 3 .   ? 12.987  35.105 16.841 0.50 30.46 ? 302 3UF A C8  1 
HETATM 4111 C  C8  B 3UF D 3 .   ? 12.904  35.628 16.642 0.50 38.00 ? 302 3UF A C8  1 
HETATM 4112 C  C7  A 3UF D 3 .   ? 13.469  36.429 16.908 0.50 28.72 ? 302 3UF A C7  1 
HETATM 4113 C  C7  B 3UF D 3 .   ? 13.347  36.937 16.931 0.50 34.34 ? 302 3UF A C7  1 
HETATM 4114 S  S11 A 3UF D 3 .   ? 12.160  34.545 15.316 0.50 40.79 ? 302 3UF A S11 1 
HETATM 4115 S  S11 B 3UF D 3 .   ? 12.047  35.369 15.044 0.50 46.55 ? 302 3UF A S11 1 
HETATM 4116 C  C12 A 3UF D 3 .   ? 10.528  35.371 15.348 0.50 36.62 ? 302 3UF A C12 1 
HETATM 4117 C  C12 B 3UF D 3 .   ? 10.725  34.226 15.577 0.50 39.29 ? 302 3UF A C12 1 
HETATM 4118 C  C13 A 3UF D 3 .   ? 10.082  35.759 13.935 0.50 36.01 ? 302 3UF A C13 1 
HETATM 4119 C  C13 B 3UF D 3 .   ? 10.003  33.592 14.396 0.50 31.45 ? 302 3UF A C13 1 
HETATM 4120 O  O14 A 3UF D 3 .   ? 8.682   35.700 13.910 0.50 32.10 ? 302 3UF A O14 1 
HETATM 4121 O  O14 B 3UF D 3 .   ? 8.639   33.838 14.620 0.50 31.85 ? 302 3UF A O14 1 
HETATM 4122 C  C   . ACT E 4 .   ? 5.405   36.280 11.743 1.00 33.81 ? 303 ACT A C   1 
HETATM 4123 O  O   . ACT E 4 .   ? 6.278   36.864 11.057 1.00 34.59 ? 303 ACT A O   1 
HETATM 4124 O  OXT . ACT E 4 .   ? 4.546   36.932 12.379 1.00 35.27 ? 303 ACT A OXT 1 
HETATM 4125 C  CH3 . ACT E 4 .   ? 5.371   34.774 11.812 1.00 32.70 ? 303 ACT A CH3 1 
HETATM 4126 ZN ZN  . ZN  F 2 .   ? 6.785   72.177 58.197 1.00 13.84 ? 301 ZN  B ZN  1 
HETATM 4127 C  C6  . 3UF G 3 .   ? 2.651   70.526 56.414 1.00 28.60 ? 302 3UF B C6  1 
HETATM 4128 C  C5  . 3UF G 3 .   ? 3.112   71.845 56.469 1.00 22.22 ? 302 3UF B C5  1 
HETATM 4129 O  O4  . 3UF G 3 .   ? 2.860   73.562 58.556 1.00 17.92 ? 302 3UF B O4  1 
HETATM 4130 S  S2  . 3UF G 3 .   ? 3.781   72.527 57.921 1.00 16.44 ? 302 3UF B S2  1 
HETATM 4131 O  O1  . 3UF G 3 .   ? 3.954   71.357 58.891 1.00 15.65 ? 302 3UF B O1  1 
HETATM 4132 N  N3  . 3UF G 3 .   ? 5.275   73.252 57.655 1.00 15.84 ? 302 3UF B N3  1 
HETATM 4133 C  C10 . 3UF G 3 .   ? 3.110   72.730 55.374 1.00 27.80 ? 302 3UF B C10 1 
HETATM 4134 C  C9  . 3UF G 3 .   ? 2.578   72.282 54.150 1.00 36.78 ? 302 3UF B C9  1 
HETATM 4135 C  C8  . 3UF G 3 .   ? 2.098   70.952 54.035 1.00 39.29 ? 302 3UF B C8  1 
HETATM 4136 C  C7  . 3UF G 3 .   ? 2.153   70.118 55.168 1.00 35.19 ? 302 3UF B C7  1 
HETATM 4137 S  S11 . 3UF G 3 .   ? 1.434   70.256 52.435 1.00 66.63 ? 302 3UF B S11 1 
HETATM 4138 C  C12 . 3UF G 3 .   ? -0.187  70.985 52.011 1.00 54.60 ? 302 3UF B C12 1 
HETATM 4139 C  C13 . 3UF G 3 .   ? -1.070  69.930 51.330 1.00 57.04 ? 302 3UF B C13 1 
HETATM 4140 O  O14 . 3UF G 3 .   ? -2.294  70.525 50.964 1.00 55.87 ? 302 3UF B O14 1 
HETATM 4141 C  C1  . PEG H 5 .   ? 10.952  67.333 36.858 1.00 60.66 ? 303 PEG B C1  1 
HETATM 4142 O  O1  . PEG H 5 .   ? 11.135  68.483 37.727 1.00 47.67 ? 303 PEG B O1  1 
HETATM 4143 C  C2  . PEG H 5 .   ? 10.422  66.061 37.548 1.00 54.40 ? 303 PEG B C2  1 
HETATM 4144 O  O2  . PEG H 5 .   ? 11.487  65.127 37.864 1.00 58.54 ? 303 PEG B O2  1 
HETATM 4145 C  C3  . PEG H 5 .   ? 12.010  64.277 36.816 1.00 58.09 ? 303 PEG B C3  1 
HETATM 4146 C  C4  . PEG H 5 .   ? 13.517  64.514 36.541 1.00 60.21 ? 303 PEG B C4  1 
HETATM 4147 O  O4  . PEG H 5 .   ? 14.000  65.833 36.893 1.00 44.11 ? 303 PEG B O4  1 
HETATM 4148 O  O   . HOH I 6 .   ? 15.024  13.134 14.782 1.00 37.89 ? 401 HOH A O   1 
HETATM 4149 O  O   . HOH I 6 .   ? 15.494  29.810 10.175 1.00 47.45 ? 402 HOH A O   1 
HETATM 4150 O  O   . HOH I 6 .   ? 24.928  30.860 41.374 1.00 35.69 ? 403 HOH A O   1 
HETATM 4151 O  O   . HOH I 6 .   ? -1.365  27.298 13.745 1.00 36.92 ? 404 HOH A O   1 
HETATM 4152 O  O   . HOH I 6 .   ? 35.051  34.463 34.566 1.00 41.93 ? 405 HOH A O   1 
HETATM 4153 O  O   . HOH I 6 .   ? 40.504  29.140 23.759 1.00 35.74 ? 406 HOH A O   1 
HETATM 4154 O  O   . HOH I 6 .   ? 37.473  37.654 21.672 1.00 28.24 ? 407 HOH A O   1 
HETATM 4155 O  O   . HOH I 6 .   ? 41.466  35.495 21.295 1.00 25.52 ? 408 HOH A O   1 
HETATM 4156 O  O   . HOH I 6 .   ? 39.288  33.614 27.266 1.00 26.38 ? 409 HOH A O   1 
HETATM 4157 O  O   . HOH I 6 .   ? 34.556  36.145 -5.655 1.00 30.97 ? 410 HOH A O   1 
HETATM 4158 O  O   . HOH I 6 .   ? 15.963  16.046 12.981 1.00 33.72 ? 411 HOH A O   1 
HETATM 4159 O  O   . HOH I 6 .   ? 25.278  25.689 40.787 1.00 42.33 ? 412 HOH A O   1 
HETATM 4160 O  O   . HOH I 6 .   ? 9.355   26.144 14.209 1.00 35.51 ? 413 HOH A O   1 
HETATM 4161 O  O   . HOH I 6 .   ? 22.906  34.041 32.906 1.00 19.39 ? 414 HOH A O   1 
HETATM 4162 O  O   . HOH I 6 .   ? 35.752  34.551 8.349  1.00 28.74 ? 415 HOH A O   1 
HETATM 4163 O  O   . HOH I 6 .   ? 18.287  17.428 9.734  1.00 32.64 ? 416 HOH A O   1 
HETATM 4164 O  O   . HOH I 6 .   ? 41.287  32.084 26.244 1.00 25.08 ? 417 HOH A O   1 
HETATM 4165 O  O   . HOH I 6 .   ? 20.419  47.399 41.952 1.00 26.71 ? 418 HOH A O   1 
HETATM 4166 O  O   . HOH I 6 .   ? 5.693   44.517 15.282 1.00 25.15 ? 419 HOH A O   1 
HETATM 4167 O  O   . HOH I 6 .   ? 25.047  42.775 40.188 1.00 28.58 ? 420 HOH A O   1 
HETATM 4168 O  O   . HOH I 6 .   ? 19.064  11.733 18.740 1.00 34.62 ? 421 HOH A O   1 
HETATM 4169 O  O   . HOH I 6 .   ? 30.514  29.927 1.468  1.00 27.68 ? 422 HOH A O   1 
HETATM 4170 O  O   . HOH I 6 .   ? 30.600  31.921 33.870 1.00 29.06 ? 423 HOH A O   1 
HETATM 4171 O  O   . HOH I 6 .   ? 28.912  26.307 -3.505 1.00 35.72 ? 424 HOH A O   1 
HETATM 4172 O  O   . HOH I 6 .   ? 37.220  36.530 14.755 1.00 22.74 ? 425 HOH A O   1 
HETATM 4173 O  O   . HOH I 6 .   ? 34.762  38.096 32.273 1.00 31.45 ? 426 HOH A O   1 
HETATM 4174 O  O   . HOH I 6 .   ? 17.888  36.727 7.449  1.00 39.02 ? 427 HOH A O   1 
HETATM 4175 O  O   . HOH I 6 .   ? 39.151  31.300 17.251 1.00 29.93 ? 428 HOH A O   1 
HETATM 4176 O  O   . HOH I 6 .   ? 34.706  26.807 6.064  1.00 36.76 ? 429 HOH A O   1 
HETATM 4177 O  O   . HOH I 6 .   ? 27.382  22.195 10.004 1.00 39.50 ? 430 HOH A O   1 
HETATM 4178 O  O   . HOH I 6 .   ? 7.498   48.351 7.888  1.00 33.91 ? 431 HOH A O   1 
HETATM 4179 O  O   . HOH I 6 .   ? 26.150  23.550 4.120  1.00 34.06 ? 432 HOH A O   1 
HETATM 4180 O  O   . HOH I 6 .   ? 32.818  19.826 11.710 1.00 42.29 ? 433 HOH A O   1 
HETATM 4181 O  O   . HOH I 6 .   ? 27.078  46.528 39.246 1.00 28.92 ? 434 HOH A O   1 
HETATM 4182 O  O   . HOH I 6 .   ? 37.177  38.844 16.841 1.00 27.01 ? 435 HOH A O   1 
HETATM 4183 O  O   . HOH I 6 .   ? 40.564  28.028 28.321 1.00 28.46 ? 436 HOH A O   1 
HETATM 4184 O  O   . HOH I 6 .   ? 15.339  25.331 3.470  1.00 51.89 ? 437 HOH A O   1 
HETATM 4185 O  O   . HOH I 6 .   ? 5.776   47.296 14.925 1.00 26.97 ? 438 HOH A O   1 
HETATM 4186 O  O   . HOH I 6 .   ? 38.664  40.144 27.804 1.00 33.73 ? 439 HOH A O   1 
HETATM 4187 O  O   . HOH I 6 .   ? 19.736  20.519 6.346  1.00 32.99 ? 440 HOH A O   1 
HETATM 4188 O  O   . HOH I 6 .   ? 12.655  39.682 9.459  1.00 40.26 ? 441 HOH A O   1 
HETATM 4189 O  O   . HOH I 6 .   ? 21.381  43.562 45.427 1.00 51.93 ? 442 HOH A O   1 
HETATM 4190 O  O   . HOH I 6 .   ? 36.413  32.079 7.623  1.00 30.58 ? 443 HOH A O   1 
HETATM 4191 O  O   . HOH I 6 .   ? 5.231   27.961 11.773 1.00 30.75 ? 444 HOH A O   1 
HETATM 4192 O  O   . HOH I 6 .   ? 36.496  37.844 12.262 1.00 27.37 ? 445 HOH A O   1 
HETATM 4193 O  O   . HOH I 6 .   ? 3.338   50.291 18.058 1.00 32.78 ? 446 HOH A O   1 
HETATM 4194 O  O   . HOH I 6 .   ? 24.061  55.807 9.725  1.00 32.10 ? 447 HOH A O   1 
HETATM 4195 O  O   . HOH I 6 .   ? 32.279  28.344 2.998  1.00 29.76 ? 448 HOH A O   1 
HETATM 4196 O  O   . HOH I 6 .   ? 18.106  19.112 7.344  1.00 35.27 ? 449 HOH A O   1 
HETATM 4197 O  O   . HOH I 6 .   ? 39.984  28.810 18.456 1.00 23.93 ? 450 HOH A O   1 
HETATM 4198 O  O   . HOH I 6 .   ? 26.177  47.918 41.287 1.00 35.87 ? 451 HOH A O   1 
HETATM 4199 O  O   . HOH I 6 .   ? 29.333  47.493 38.797 1.00 33.26 ? 452 HOH A O   1 
HETATM 4200 O  O   . HOH I 6 .   ? 7.315   44.403 6.652  1.00 39.15 ? 453 HOH A O   1 
HETATM 4201 O  O   . HOH I 6 .   ? 4.193   44.097 13.173 1.00 41.01 ? 454 HOH A O   1 
HETATM 4202 O  O   . HOH I 6 .   ? 37.499  40.910 7.102  1.00 33.40 ? 455 HOH A O   1 
HETATM 4203 O  O   . HOH I 6 .   ? 3.633   44.427 17.177 1.00 33.05 ? 456 HOH A O   1 
HETATM 4204 O  O   . HOH I 6 .   ? 18.839  41.888 18.839 1.00 17.90 ? 457 HOH A O   1 
HETATM 4205 O  O   . HOH I 6 .   ? 23.739  32.919 17.091 1.00 17.12 ? 458 HOH A O   1 
HETATM 4206 O  O   . HOH I 6 .   ? 29.975  46.521 31.719 1.00 30.11 ? 459 HOH A O   1 
HETATM 4207 O  O   . HOH I 6 .   ? 4.794   34.808 26.804 1.00 18.96 ? 460 HOH A O   1 
HETATM 4208 O  O   . HOH I 6 .   ? 5.451   25.420 14.268 1.00 22.39 ? 461 HOH A O   1 
HETATM 4209 O  O   . HOH I 6 .   ? 16.886  17.635 28.589 1.00 26.16 ? 462 HOH A O   1 
HETATM 4210 O  O   . HOH I 6 .   ? 20.533  38.728 15.975 1.00 22.55 ? 463 HOH A O   1 
HETATM 4211 O  O   . HOH I 6 .   ? 22.220  48.303 30.129 1.00 23.58 ? 464 HOH A O   1 
HETATM 4212 O  O   . HOH I 6 .   ? 5.135   41.080 26.836 1.00 29.04 ? 465 HOH A O   1 
HETATM 4213 O  O   . HOH I 6 .   ? 33.983  26.612 31.627 1.00 41.98 ? 466 HOH A O   1 
HETATM 4214 O  O   . HOH I 6 .   ? 26.362  44.192 25.986 1.00 21.91 ? 467 HOH A O   1 
HETATM 4215 O  O   . HOH I 6 .   ? 3.595   48.478 23.969 1.00 29.85 ? 468 HOH A O   1 
HETATM 4216 O  O   . HOH I 6 .   ? 20.856  30.434 37.275 1.00 21.65 ? 469 HOH A O   1 
HETATM 4217 O  O   . HOH I 6 .   ? 35.884  25.286 21.458 1.00 31.66 ? 470 HOH A O   1 
HETATM 4218 O  O   . HOH I 6 .   ? 22.396  45.466 25.336 1.00 23.54 ? 471 HOH A O   1 
HETATM 4219 O  O   . HOH I 6 .   ? 16.079  49.516 19.344 1.00 31.15 ? 472 HOH A O   1 
HETATM 4220 O  O   . HOH I 6 .   ? 29.792  45.625 19.085 1.00 32.08 ? 473 HOH A O   1 
HETATM 4221 O  O   . HOH I 6 .   ? 7.287   37.607 34.107 1.00 23.33 ? 474 HOH A O   1 
HETATM 4222 O  O   . HOH I 6 .   ? 32.192  38.816 30.067 1.00 21.34 ? 475 HOH A O   1 
HETATM 4223 O  O   . HOH I 6 .   ? 24.709  46.561 26.161 1.00 25.46 ? 476 HOH A O   1 
HETATM 4224 O  O   . HOH I 6 .   ? 33.559  32.858 32.680 1.00 22.69 ? 477 HOH A O   1 
HETATM 4225 O  O   . HOH I 6 .   ? 8.862   17.843 17.998 1.00 23.52 ? 478 HOH A O   1 
HETATM 4226 O  O   . HOH I 6 .   ? 14.410  27.346 38.501 1.00 25.86 ? 479 HOH A O   1 
HETATM 4227 O  O   . HOH I 6 .   ? 4.293   25.062 32.919 1.00 36.56 ? 480 HOH A O   1 
HETATM 4228 O  O   . HOH I 6 .   ? 12.157  25.211 14.369 1.00 28.34 ? 481 HOH A O   1 
HETATM 4229 O  O   . HOH I 6 .   ? 9.431   18.925 20.676 1.00 24.29 ? 482 HOH A O   1 
HETATM 4230 O  O   . HOH I 6 .   ? 11.819  45.383 38.660 1.00 26.99 ? 483 HOH A O   1 
HETATM 4231 O  O   . HOH I 6 .   ? 19.870  22.170 32.144 1.00 32.01 ? 484 HOH A O   1 
HETATM 4232 O  O   . HOH I 6 .   ? 7.378   39.651 36.031 1.00 27.71 ? 485 HOH A O   1 
HETATM 4233 O  O   . HOH I 6 .   ? 26.069  32.009 0.902  1.00 26.82 ? 486 HOH A O   1 
HETATM 4234 O  O   . HOH I 6 .   ? 23.739  47.473 21.097 1.00 40.77 ? 487 HOH A O   1 
HETATM 4235 O  O   . HOH I 6 .   ? 4.681   27.316 37.104 1.00 36.21 ? 488 HOH A O   1 
HETATM 4236 O  O   . HOH I 6 .   ? 28.915  19.785 22.252 1.00 34.54 ? 489 HOH A O   1 
HETATM 4237 O  O   . HOH I 6 .   ? 27.398  26.033 29.043 1.00 23.71 ? 490 HOH A O   1 
HETATM 4238 O  O   . HOH I 6 .   ? 30.641  27.105 4.845  1.00 23.75 ? 491 HOH A O   1 
HETATM 4239 O  O   . HOH I 6 .   ? 3.527   43.176 19.707 1.00 26.45 ? 492 HOH A O   1 
HETATM 4240 O  O   . HOH I 6 .   ? 4.933   48.420 30.715 1.00 33.74 ? 493 HOH A O   1 
HETATM 4241 O  O   . HOH I 6 .   ? 30.398  27.497 32.046 1.00 26.32 ? 494 HOH A O   1 
HETATM 4242 O  O   . HOH I 6 .   ? 23.568  16.705 23.831 1.00 26.88 ? 495 HOH A O   1 
HETATM 4243 O  O   . HOH I 6 .   ? 22.388  49.173 26.017 1.00 31.11 ? 496 HOH A O   1 
HETATM 4244 O  O   . HOH I 6 .   ? 26.011  20.823 11.701 1.00 34.38 ? 497 HOH A O   1 
HETATM 4245 O  O   . HOH I 6 .   ? 33.538  25.731 12.576 1.00 29.31 ? 498 HOH A O   1 
HETATM 4246 O  O   . HOH I 6 .   ? 31.606  39.813 22.548 1.00 21.98 ? 499 HOH A O   1 
HETATM 4247 O  O   . HOH I 6 .   ? 26.976  41.588 4.337  1.00 38.23 ? 500 HOH A O   1 
HETATM 4248 O  O   . HOH I 6 .   ? 21.270  36.528 17.256 1.00 19.72 ? 501 HOH A O   1 
HETATM 4249 O  O   . HOH I 6 .   ? 9.741   49.027 26.720 1.00 25.10 ? 502 HOH A O   1 
HETATM 4250 O  O   . HOH I 6 .   ? 37.920  28.499 19.966 1.00 23.30 ? 503 HOH A O   1 
HETATM 4251 O  O   . HOH I 6 .   ? 29.350  19.842 14.721 1.00 29.45 ? 504 HOH A O   1 
HETATM 4252 O  O   . HOH I 6 .   ? 18.358  24.913 39.584 1.00 36.30 ? 505 HOH A O   1 
HETATM 4253 O  O   . HOH I 6 .   ? 14.429  52.420 16.777 1.00 29.03 ? 506 HOH A O   1 
HETATM 4254 O  O   . HOH I 6 .   ? 18.479  50.580 29.699 1.00 26.01 ? 507 HOH A O   1 
HETATM 4255 O  O   . HOH I 6 .   ? 16.460  48.740 30.949 1.00 26.44 ? 508 HOH A O   1 
HETATM 4256 O  O   . HOH I 6 .   ? 32.851  30.706 12.174 1.00 28.21 ? 509 HOH A O   1 
HETATM 4257 O  O   . HOH I 6 .   ? 3.942   39.053 27.566 1.00 30.98 ? 510 HOH A O   1 
HETATM 4258 O  O   . HOH I 6 .   ? 13.324  9.921  20.520 1.00 40.76 ? 511 HOH A O   1 
HETATM 4259 O  O   . HOH I 6 .   ? 21.970  49.567 36.572 1.00 30.38 ? 512 HOH A O   1 
HETATM 4260 O  O   . HOH I 6 .   ? 28.388  36.038 -4.941 1.00 43.49 ? 513 HOH A O   1 
HETATM 4261 O  O   . HOH I 6 .   ? 26.793  24.700 31.447 1.00 33.07 ? 514 HOH A O   1 
HETATM 4262 O  O   . HOH I 6 .   ? 18.270  35.651 16.351 1.00 33.21 ? 515 HOH A O   1 
HETATM 4263 O  O   . HOH I 6 .   ? 13.876  28.080 40.984 1.00 34.88 ? 516 HOH A O   1 
HETATM 4264 O  O   . HOH I 6 .   ? 24.629  45.564 17.797 1.00 31.28 ? 517 HOH A O   1 
HETATM 4265 O  O   . HOH I 6 .   ? 30.356  41.655 0.345  1.00 34.16 ? 518 HOH A O   1 
HETATM 4266 O  O   . HOH I 6 .   ? 17.375  39.918 42.286 1.00 30.13 ? 519 HOH A O   1 
HETATM 4267 O  O   . HOH I 6 .   ? 11.015  20.793 19.823 1.00 20.63 ? 520 HOH A O   1 
HETATM 4268 O  O   . HOH I 6 .   ? 16.069  38.351 44.827 1.00 40.33 ? 521 HOH A O   1 
HETATM 4269 O  O   . HOH I 6 .   ? 26.825  20.460 24.914 1.00 25.27 ? 522 HOH A O   1 
HETATM 4270 O  O   . HOH I 6 .   ? 28.395  43.700 12.211 1.00 41.50 ? 523 HOH A O   1 
HETATM 4271 O  O   . HOH I 6 .   ? 20.457  51.330 26.446 1.00 29.40 ? 524 HOH A O   1 
HETATM 4272 O  O   . HOH I 6 .   ? 35.698  30.968 33.170 1.00 31.00 ? 525 HOH A O   1 
HETATM 4273 O  O   . HOH I 6 .   ? 11.761  51.003 23.601 1.00 31.89 ? 526 HOH A O   1 
HETATM 4274 O  O   . HOH I 6 .   ? 4.707   46.640 37.151 1.00 41.75 ? 527 HOH A O   1 
HETATM 4275 O  O   . HOH I 6 .   ? 22.933  25.513 2.274  1.00 39.74 ? 528 HOH A O   1 
HETATM 4276 O  O   . HOH I 6 .   ? 20.805  23.046 34.429 1.00 33.54 ? 529 HOH A O   1 
HETATM 4277 O  O   . HOH I 6 .   ? 5.309   43.802 34.972 1.00 34.58 ? 530 HOH A O   1 
HETATM 4278 O  O   . HOH I 6 .   ? 9.877   20.007 30.729 1.00 35.84 ? 531 HOH A O   1 
HETATM 4279 O  O   . HOH I 6 .   ? 20.900  52.638 28.721 1.00 37.03 ? 532 HOH A O   1 
HETATM 4280 O  O   . HOH I 6 .   ? 5.062   41.135 35.663 1.00 27.86 ? 533 HOH A O   1 
HETATM 4281 O  O   . HOH I 6 .   ? 38.639  27.894 22.583 1.00 32.17 ? 534 HOH A O   1 
HETATM 4282 O  O   . HOH I 6 .   ? 15.421  21.306 34.285 1.00 34.32 ? 535 HOH A O   1 
HETATM 4283 O  O   . HOH I 6 .   ? 14.726  45.339 38.143 1.00 31.95 ? 536 HOH A O   1 
HETATM 4284 O  O   . HOH I 6 .   ? 35.197  24.253 16.437 1.00 31.66 ? 537 HOH A O   1 
HETATM 4285 O  O   . HOH I 6 .   ? 9.246   20.596 12.682 1.00 35.26 ? 538 HOH A O   1 
HETATM 4286 O  O   . HOH I 6 .   ? 4.988   37.524 30.019 1.00 29.37 ? 539 HOH A O   1 
HETATM 4287 O  O   . HOH I 6 .   ? 27.717  48.478 12.792 1.00 43.08 ? 540 HOH A O   1 
HETATM 4288 O  O   . HOH I 6 .   ? 24.017  48.476 28.136 1.00 32.79 ? 541 HOH A O   1 
HETATM 4289 O  O   . HOH I 6 .   ? 38.065  25.138 23.233 1.00 31.48 ? 542 HOH A O   1 
HETATM 4290 O  O   . HOH I 6 .   ? 31.927  43.464 9.579  1.00 32.43 ? 543 HOH A O   1 
HETATM 4291 O  O   . HOH I 6 .   ? 1.786   29.758 30.535 1.00 30.88 ? 544 HOH A O   1 
HETATM 4292 O  O   . HOH I 6 .   ? 3.982   31.910 39.189 1.00 42.13 ? 545 HOH A O   1 
HETATM 4293 O  O   . HOH I 6 .   ? 21.101  18.465 30.644 1.00 37.88 ? 546 HOH A O   1 
HETATM 4294 O  O   . HOH I 6 .   ? -1.956  38.760 22.749 1.00 35.23 ? 547 HOH A O   1 
HETATM 4295 O  O   . HOH I 6 .   ? 34.972  28.275 33.588 1.00 39.62 ? 548 HOH A O   1 
HETATM 4296 O  O   . HOH I 6 .   ? 23.812  22.028 32.282 1.00 37.52 ? 549 HOH A O   1 
HETATM 4297 O  O   . HOH I 6 .   ? -1.615  24.114 29.593 1.00 41.99 ? 550 HOH A O   1 
HETATM 4298 O  O   . HOH I 6 .   ? 4.986   37.673 32.589 1.00 33.34 ? 551 HOH A O   1 
HETATM 4299 O  O   . HOH I 6 .   ? 25.503  40.348 12.660 1.00 37.96 ? 552 HOH A O   1 
HETATM 4300 O  O   . HOH I 6 .   ? 34.798  42.968 16.090 1.00 30.46 ? 553 HOH A O   1 
HETATM 4301 O  O   . HOH I 6 .   ? 31.918  41.449 29.401 1.00 31.90 ? 554 HOH A O   1 
HETATM 4302 O  O   . HOH I 6 .   ? 34.589  28.550 13.483 1.00 35.49 ? 555 HOH A O   1 
HETATM 4303 O  O   . HOH I 6 .   ? 27.721  41.712 1.374  1.00 35.72 ? 556 HOH A O   1 
HETATM 4304 O  O   . HOH I 6 .   ? 21.936  50.152 32.266 1.00 38.52 ? 557 HOH A O   1 
HETATM 4305 O  O   . HOH I 6 .   ? 22.777  49.628 18.554 1.00 38.30 ? 558 HOH A O   1 
HETATM 4306 O  O   . HOH I 6 .   ? 12.895  45.749 7.593  1.00 37.17 ? 559 HOH A O   1 
HETATM 4307 O  O   . HOH I 6 .   ? 23.678  44.167 10.058 1.00 42.06 ? 560 HOH A O   1 
HETATM 4308 O  O   . HOH I 6 .   ? 7.109   54.104 17.656 1.00 38.53 ? 561 HOH A O   1 
HETATM 4309 O  O   . HOH I 6 .   ? 17.081  18.398 30.936 1.00 37.29 ? 562 HOH A O   1 
HETATM 4310 O  O   . HOH I 6 .   ? 15.903  10.639 21.724 1.00 36.10 ? 563 HOH A O   1 
HETATM 4311 O  O   . HOH I 6 .   ? 11.981  10.884 18.556 1.00 32.45 ? 564 HOH A O   1 
HETATM 4312 O  O   . HOH I 6 .   ? 3.514   35.199 33.218 1.00 38.63 ? 565 HOH A O   1 
HETATM 4313 O  O   . HOH I 6 .   ? -1.755  34.371 15.456 1.00 32.44 ? 566 HOH A O   1 
HETATM 4314 O  O   . HOH I 6 .   ? 23.404  19.490 31.635 1.00 40.72 ? 567 HOH A O   1 
HETATM 4315 O  O   . HOH I 6 .   ? 3.673   44.481 33.299 1.00 34.67 ? 568 HOH A O   1 
HETATM 4316 O  O   . HOH I 6 .   ? 38.065  24.819 29.353 1.00 39.76 ? 569 HOH A O   1 
HETATM 4317 O  O   . HOH I 6 .   ? 24.814  17.141 13.504 1.00 34.53 ? 570 HOH A O   1 
HETATM 4318 O  O   . HOH I 6 .   ? 2.308   41.622 31.426 1.00 35.14 ? 571 HOH A O   1 
HETATM 4319 O  O   . HOH I 6 .   ? 25.493  29.804 -0.617 1.00 36.92 ? 572 HOH A O   1 
HETATM 4320 O  O   . HOH J 6 .   ? -7.618  64.139 74.170 1.00 35.35 ? 401 HOH B O   1 
HETATM 4321 O  O   . HOH J 6 .   ? -9.542  65.365 76.832 1.00 40.81 ? 402 HOH B O   1 
HETATM 4322 O  O   . HOH J 6 .   ? 7.137   72.992 45.198 1.00 35.06 ? 403 HOH B O   1 
HETATM 4323 O  O   . HOH J 6 .   ? 13.284  56.258 75.894 1.00 27.96 ? 404 HOH B O   1 
HETATM 4324 O  O   . HOH J 6 .   ? -4.593  82.600 47.790 1.00 32.31 ? 405 HOH B O   1 
HETATM 4325 O  O   . HOH J 6 .   ? -5.154  80.097 51.974 1.00 33.45 ? 406 HOH B O   1 
HETATM 4326 O  O   . HOH J 6 .   ? 30.061  71.312 59.014 1.00 27.37 ? 407 HOH B O   1 
HETATM 4327 O  O   . HOH J 6 .   ? 26.111  60.342 67.375 1.00 33.38 ? 408 HOH B O   1 
HETATM 4328 O  O   . HOH J 6 .   ? 19.172  65.765 39.259 1.00 22.29 ? 409 HOH B O   1 
HETATM 4329 O  O   . HOH J 6 .   ? 27.818  69.121 65.109 1.00 22.47 ? 410 HOH B O   1 
HETATM 4330 O  O   . HOH J 6 .   ? 10.375  84.024 67.885 1.00 23.88 ? 411 HOH B O   1 
HETATM 4331 O  O   . HOH J 6 .   ? 8.724   50.533 64.086 1.00 37.66 ? 412 HOH B O   1 
HETATM 4332 O  O   . HOH J 6 .   ? 5.543   62.265 79.727 1.00 39.32 ? 413 HOH B O   1 
HETATM 4333 O  O   . HOH J 6 .   ? 29.915  67.710 63.989 1.00 22.70 ? 414 HOH B O   1 
HETATM 4334 O  O   . HOH J 6 .   ? 7.574   64.935 40.898 1.00 32.37 ? 415 HOH B O   1 
HETATM 4335 O  O   . HOH J 6 .   ? 24.662  70.113 46.290 1.00 27.51 ? 416 HOH B O   1 
HETATM 4336 O  O   . HOH J 6 .   ? 20.654  77.055 34.458 1.00 38.95 ? 417 HOH B O   1 
HETATM 4337 O  O   . HOH J 6 .   ? 24.150  58.414 44.323 1.00 33.95 ? 418 HOH B O   1 
HETATM 4338 O  O   . HOH J 6 .   ? 15.071  83.639 76.642 1.00 32.80 ? 419 HOH B O   1 
HETATM 4339 O  O   . HOH J 6 .   ? 28.603  63.701 66.406 1.00 31.32 ? 420 HOH B O   1 
HETATM 4340 O  O   . HOH J 6 .   ? 9.073   58.755 71.858 1.00 23.54 ? 421 HOH B O   1 
HETATM 4341 O  O   . HOH J 6 .   ? 4.686   50.001 64.616 1.00 41.50 ? 422 HOH B O   1 
HETATM 4342 O  O   . HOH J 6 .   ? 6.758   86.264 67.501 1.00 30.49 ? 423 HOH B O   1 
HETATM 4343 O  O   . HOH J 6 .   ? 27.668  67.086 55.181 1.00 23.21 ? 424 HOH B O   1 
HETATM 4344 O  O   . HOH J 6 .   ? 23.006  71.355 31.877 1.00 37.63 ? 425 HOH B O   1 
HETATM 4345 O  O   . HOH J 6 .   ? 23.397  62.571 43.930 1.00 30.40 ? 426 HOH B O   1 
HETATM 4346 O  O   . HOH J 6 .   ? -3.139  67.249 81.225 1.00 29.22 ? 427 HOH B O   1 
HETATM 4347 O  O   . HOH J 6 .   ? 12.633  58.285 71.282 1.00 38.57 ? 428 HOH B O   1 
HETATM 4348 O  O   . HOH J 6 .   ? 9.809   85.195 74.544 1.00 35.34 ? 429 HOH B O   1 
HETATM 4349 O  O   . HOH J 6 .   ? 28.739  64.731 61.751 1.00 41.38 ? 430 HOH B O   1 
HETATM 4350 O  O   . HOH J 6 .   ? 3.932   51.321 66.720 1.00 35.79 ? 431 HOH B O   1 
HETATM 4351 O  O   . HOH J 6 .   ? 25.831  72.293 52.364 1.00 25.37 ? 432 HOH B O   1 
HETATM 4352 O  O   . HOH J 6 .   ? -5.280  65.230 83.750 1.00 26.96 ? 433 HOH B O   1 
HETATM 4353 O  O   . HOH J 6 .   ? 5.123   53.647 66.094 1.00 29.23 ? 434 HOH B O   1 
HETATM 4354 O  O   . HOH J 6 .   ? 2.315   75.803 46.657 1.00 36.23 ? 435 HOH B O   1 
HETATM 4355 O  O   . HOH J 6 .   ? 4.173   65.664 47.094 1.00 36.12 ? 436 HOH B O   1 
HETATM 4356 O  O   . HOH J 6 .   ? 17.933  82.368 69.386 1.00 27.41 ? 437 HOH B O   1 
HETATM 4357 O  O   . HOH J 6 .   ? 4.957   46.354 59.402 1.00 42.41 ? 438 HOH B O   1 
HETATM 4358 O  O   . HOH J 6 .   ? 25.545  66.153 50.833 1.00 38.67 ? 439 HOH B O   1 
HETATM 4359 O  O   . HOH J 6 .   ? 24.979  73.540 50.067 1.00 23.56 ? 440 HOH B O   1 
HETATM 4360 O  O   . HOH J 6 .   ? 25.153  67.578 45.682 1.00 33.38 ? 441 HOH B O   1 
HETATM 4361 O  O   . HOH J 6 .   ? 1.890   73.969 83.378 1.00 35.54 ? 442 HOH B O   1 
HETATM 4362 O  O   . HOH J 6 .   ? -2.126  76.854 84.302 1.00 35.28 ? 443 HOH B O   1 
HETATM 4363 O  O   . HOH J 6 .   ? -5.710  78.037 48.915 1.00 36.76 ? 444 HOH B O   1 
HETATM 4364 O  O   . HOH J 6 .   ? -7.850  51.251 58.939 1.00 41.39 ? 445 HOH B O   1 
HETATM 4365 O  O   . HOH J 6 .   ? 11.094  84.518 64.079 1.00 28.60 ? 446 HOH B O   1 
HETATM 4366 O  O   . HOH J 6 .   ? 5.686   54.734 68.470 1.00 30.85 ? 447 HOH B O   1 
HETATM 4367 O  O   . HOH J 6 .   ? -3.271  84.045 44.614 1.00 24.92 ? 448 HOH B O   1 
HETATM 4368 O  O   . HOH J 6 .   ? 8.009   68.154 43.437 1.00 33.37 ? 449 HOH B O   1 
HETATM 4369 O  O   . HOH J 6 .   ? 25.805  74.226 54.510 1.00 22.12 ? 450 HOH B O   1 
HETATM 4370 O  O   . HOH J 6 .   ? -9.331  76.529 50.072 1.00 39.13 ? 451 HOH B O   1 
HETATM 4371 O  O   . HOH J 6 .   ? -5.170  83.168 51.582 1.00 32.93 ? 452 HOH B O   1 
HETATM 4372 O  O   . HOH J 6 .   ? 11.521  56.368 69.541 1.00 41.16 ? 453 HOH B O   1 
HETATM 4373 O  O   . HOH J 6 .   ? 10.249  85.169 76.958 1.00 34.50 ? 454 HOH B O   1 
HETATM 4374 O  O   . HOH J 6 .   ? -4.197  62.707 81.060 1.00 28.55 ? 455 HOH B O   1 
HETATM 4375 O  O   . HOH J 6 .   ? 2.913   88.456 69.316 1.00 35.14 ? 456 HOH B O   1 
HETATM 4376 O  O   . HOH J 6 .   ? 5.140   88.130 66.772 1.00 36.71 ? 457 HOH B O   1 
HETATM 4377 O  O   . HOH J 6 .   ? 20.862  64.019 40.633 1.00 25.85 ? 458 HOH B O   1 
HETATM 4378 O  O   . HOH J 6 .   ? 27.227  63.558 51.833 1.00 40.85 ? 459 HOH B O   1 
HETATM 4379 O  O   . HOH J 6 .   ? 13.082  84.941 61.863 1.00 46.11 ? 460 HOH B O   1 
HETATM 4380 O  O   . HOH J 6 .   ? -1.759  82.087 43.552 1.00 34.89 ? 461 HOH B O   1 
HETATM 4381 O  O   . HOH J 6 .   ? 14.384  57.654 72.702 1.00 35.64 ? 462 HOH B O   1 
HETATM 4382 O  O   . HOH J 6 .   ? 28.531  64.503 56.121 1.00 24.20 ? 463 HOH B O   1 
HETATM 4383 O  O   . HOH J 6 .   ? -12.379 67.430 76.755 1.00 34.21 ? 464 HOH B O   1 
HETATM 4384 O  O   . HOH J 6 .   ? 24.984  76.295 50.820 1.00 35.33 ? 465 HOH B O   1 
HETATM 4385 O  O   . HOH J 6 .   ? 15.653  61.767 66.886 1.00 20.28 ? 466 HOH B O   1 
HETATM 4386 O  O   . HOH J 6 .   ? -6.736  70.700 63.610 1.00 20.45 ? 467 HOH B O   1 
HETATM 4387 O  O   . HOH J 6 .   ? 7.181   71.439 53.701 1.00 24.77 ? 468 HOH B O   1 
HETATM 4388 O  O   . HOH J 6 .   ? 4.711   84.467 68.269 1.00 21.77 ? 469 HOH B O   1 
HETATM 4389 O  O   . HOH J 6 .   ? -7.655  61.009 69.868 1.00 27.40 ? 470 HOH B O   1 
HETATM 4390 O  O   . HOH J 6 .   ? -4.503  73.644 70.931 1.00 20.33 ? 471 HOH B O   1 
HETATM 4391 O  O   . HOH J 6 .   ? 9.978   72.279 54.837 1.00 17.16 ? 472 HOH B O   1 
HETATM 4392 O  O   . HOH J 6 .   ? 12.531  68.636 54.700 1.00 16.15 ? 473 HOH B O   1 
HETATM 4393 O  O   . HOH J 6 .   ? 10.936  69.933 70.619 1.00 16.23 ? 474 HOH B O   1 
HETATM 4394 O  O   . HOH J 6 .   ? 13.596  52.747 51.040 1.00 26.38 ? 475 HOH B O   1 
HETATM 4395 O  O   . HOH J 6 .   ? -2.286  53.579 55.010 1.00 28.01 ? 476 HOH B O   1 
HETATM 4396 O  O   . HOH J 6 .   ? 7.750   77.677 56.343 1.00 17.30 ? 477 HOH B O   1 
HETATM 4397 O  O   . HOH J 6 .   ? 14.843  67.815 38.646 1.00 22.98 ? 478 HOH B O   1 
HETATM 4398 O  O   . HOH J 6 .   ? 9.522   74.554 53.533 1.00 16.23 ? 479 HOH B O   1 
HETATM 4399 O  O   . HOH J 6 .   ? 6.964   50.710 53.210 1.00 23.88 ? 480 HOH B O   1 
HETATM 4400 O  O   . HOH J 6 .   ? -6.107  79.637 71.573 1.00 26.72 ? 481 HOH B O   1 
HETATM 4401 O  O   . HOH J 6 .   ? 12.316  61.321 39.911 1.00 23.56 ? 482 HOH B O   1 
HETATM 4402 O  O   . HOH J 6 .   ? 19.491  77.553 38.204 1.00 29.84 ? 483 HOH B O   1 
HETATM 4403 O  O   . HOH J 6 .   ? 2.750   80.895 75.558 1.00 26.77 ? 484 HOH B O   1 
HETATM 4404 O  O   . HOH J 6 .   ? 8.914   57.033 43.989 1.00 26.84 ? 485 HOH B O   1 
HETATM 4405 O  O   . HOH J 6 .   ? 20.259  81.091 60.165 1.00 32.05 ? 486 HOH B O   1 
HETATM 4406 O  O   . HOH J 6 .   ? -6.556  73.789 69.158 1.00 26.95 ? 487 HOH B O   1 
HETATM 4407 O  O   . HOH J 6 .   ? 8.803   66.195 74.642 1.00 18.54 ? 488 HOH B O   1 
HETATM 4408 O  O   . HOH J 6 .   ? 2.190   63.189 75.853 1.00 22.28 ? 489 HOH B O   1 
HETATM 4409 O  O   . HOH J 6 .   ? 4.947   85.420 56.685 1.00 24.02 ? 490 HOH B O   1 
HETATM 4410 O  O   . HOH J 6 .   ? 19.382  62.846 42.537 1.00 22.61 ? 491 HOH B O   1 
HETATM 4411 O  O   . HOH J 6 .   ? 15.172  56.281 62.659 1.00 29.49 ? 492 HOH B O   1 
HETATM 4412 O  O   . HOH J 6 .   ? 13.895  49.908 52.809 1.00 38.12 ? 493 HOH B O   1 
HETATM 4413 O  O   . HOH J 6 .   ? -1.668  84.914 63.614 1.00 22.75 ? 494 HOH B O   1 
HETATM 4414 O  O   . HOH J 6 .   ? 14.527  76.291 50.395 1.00 26.32 ? 495 HOH B O   1 
HETATM 4415 O  O   . HOH J 6 .   ? 14.208  78.403 75.392 1.00 30.32 ? 496 HOH B O   1 
HETATM 4416 O  O   . HOH J 6 .   ? 3.038   65.756 79.655 1.00 24.93 ? 497 HOH B O   1 
HETATM 4417 O  O   . HOH J 6 .   ? -6.171  84.778 67.291 1.00 28.62 ? 498 HOH B O   1 
HETATM 4418 O  O   . HOH J 6 .   ? 3.690   82.429 73.685 1.00 25.85 ? 499 HOH B O   1 
HETATM 4419 O  O   . HOH J 6 .   ? -2.202  54.904 57.738 1.00 25.54 ? 500 HOH B O   1 
HETATM 4420 O  O   . HOH J 6 .   ? 10.927  81.253 63.108 1.00 19.26 ? 501 HOH B O   1 
HETATM 4421 O  O   . HOH J 6 .   ? 23.362  73.550 70.227 1.00 31.79 ? 502 HOH B O   1 
HETATM 4422 O  O   . HOH J 6 .   ? 8.564   82.659 79.887 1.00 31.04 ? 503 HOH B O   1 
HETATM 4423 O  O   . HOH J 6 .   ? 3.338   88.383 53.954 1.00 26.01 ? 504 HOH B O   1 
HETATM 4424 O  O   . HOH J 6 .   ? -4.507  75.909 72.844 1.00 27.77 ? 505 HOH B O   1 
HETATM 4425 O  O   . HOH J 6 .   ? -11.089 66.178 68.282 1.00 36.14 ? 506 HOH B O   1 
HETATM 4426 O  O   . HOH J 6 .   ? 19.991  74.869 68.730 1.00 27.35 ? 507 HOH B O   1 
HETATM 4427 O  O   . HOH J 6 .   ? 15.209  87.383 45.964 1.00 41.05 ? 508 HOH B O   1 
HETATM 4428 O  O   . HOH J 6 .   ? 14.740  56.445 49.469 1.00 28.75 ? 509 HOH B O   1 
HETATM 4429 O  O   . HOH J 6 .   ? 17.301  71.898 32.511 1.00 35.80 ? 510 HOH B O   1 
HETATM 4430 O  O   . HOH J 6 .   ? 24.134  60.209 54.207 1.00 31.53 ? 511 HOH B O   1 
HETATM 4431 O  O   . HOH J 6 .   ? 26.581  64.187 57.617 1.00 24.43 ? 512 HOH B O   1 
HETATM 4432 O  O   . HOH J 6 .   ? 4.848   51.883 50.567 1.00 40.51 ? 513 HOH B O   1 
HETATM 4433 O  O   . HOH J 6 .   ? 21.191  78.982 47.353 1.00 29.13 ? 514 HOH B O   1 
HETATM 4434 O  O   . HOH J 6 .   ? 1.563   63.925 78.427 1.00 25.49 ? 515 HOH B O   1 
HETATM 4435 O  O   . HOH J 6 .   ? 16.133  63.934 72.742 1.00 30.58 ? 516 HOH B O   1 
HETATM 4436 O  O   . HOH J 6 .   ? 18.785  63.369 69.803 1.00 24.13 ? 517 HOH B O   1 
HETATM 4437 O  O   . HOH J 6 .   ? -0.121  81.248 76.091 1.00 26.15 ? 518 HOH B O   1 
HETATM 4438 O  O   . HOH J 6 .   ? 19.904  75.497 60.297 1.00 18.18 ? 519 HOH B O   1 
HETATM 4439 O  O   . HOH J 6 .   ? -5.780  61.452 51.322 1.00 31.75 ? 520 HOH B O   1 
HETATM 4440 O  O   . HOH J 6 .   ? 13.991  81.119 55.746 1.00 21.99 ? 521 HOH B O   1 
HETATM 4441 O  O   . HOH J 6 .   ? 7.176   53.313 47.085 1.00 30.09 ? 522 HOH B O   1 
HETATM 4442 O  O   . HOH J 6 .   ? -8.152  68.785 75.749 1.00 32.07 ? 523 HOH B O   1 
HETATM 4443 O  O   . HOH J 6 .   ? 7.176   54.918 44.625 1.00 36.66 ? 524 HOH B O   1 
HETATM 4444 O  O   . HOH J 6 .   ? -0.276  56.698 56.937 1.00 21.75 ? 525 HOH B O   1 
HETATM 4445 O  O   . HOH J 6 .   ? -6.256  77.183 63.569 1.00 23.14 ? 526 HOH B O   1 
HETATM 4446 O  O   . HOH J 6 .   ? -6.700  77.125 72.327 1.00 24.83 ? 527 HOH B O   1 
HETATM 4447 O  O   . HOH J 6 .   ? 16.099  77.493 42.005 1.00 35.22 ? 528 HOH B O   1 
HETATM 4448 O  O   . HOH J 6 .   ? 2.956   86.777 47.550 1.00 29.37 ? 529 HOH B O   1 
HETATM 4449 O  O   . HOH J 6 .   ? 24.436  61.051 59.303 1.00 30.93 ? 530 HOH B O   1 
HETATM 4450 O  O   . HOH J 6 .   ? -3.238  58.952 75.077 1.00 31.17 ? 531 HOH B O   1 
HETATM 4451 O  O   . HOH J 6 .   ? 3.292   57.033 71.794 1.00 31.48 ? 532 HOH B O   1 
HETATM 4452 O  O   . HOH J 6 .   ? 10.492  87.601 52.664 1.00 35.26 ? 533 HOH B O   1 
HETATM 4453 O  O   . HOH J 6 .   ? -0.195  89.246 69.083 1.00 33.86 ? 534 HOH B O   1 
HETATM 4454 O  O   . HOH J 6 .   ? 17.383  55.769 59.728 1.00 35.02 ? 535 HOH B O   1 
HETATM 4455 O  O   . HOH J 6 .   ? -8.224  75.767 70.346 1.00 27.99 ? 536 HOH B O   1 
HETATM 4456 O  O   . HOH J 6 .   ? -0.960  64.943 79.405 1.00 32.47 ? 537 HOH B O   1 
HETATM 4457 O  O   . HOH J 6 .   ? 22.457  61.373 50.430 1.00 23.31 ? 538 HOH B O   1 
HETATM 4458 O  O   . HOH J 6 .   ? 22.074  68.701 70.584 1.00 29.39 ? 539 HOH B O   1 
HETATM 4459 O  O   . HOH J 6 .   ? 15.172  59.275 41.988 1.00 34.80 ? 540 HOH B O   1 
HETATM 4460 O  O   . HOH J 6 .   ? -9.357  77.139 68.377 1.00 36.90 ? 541 HOH B O   1 
HETATM 4461 O  O   . HOH J 6 .   ? 21.591  66.140 50.018 1.00 31.84 ? 542 HOH B O   1 
HETATM 4462 O  O   . HOH J 6 .   ? -11.114 58.458 65.695 1.00 33.06 ? 543 HOH B O   1 
HETATM 4463 O  O   . HOH J 6 .   ? 17.191  77.888 46.798 1.00 31.66 ? 544 HOH B O   1 
HETATM 4464 O  O   . HOH J 6 .   ? 2.791   59.958 75.291 1.00 34.35 ? 545 HOH B O   1 
HETATM 4465 O  O   . HOH J 6 .   ? -7.835  84.192 60.777 1.00 26.79 ? 546 HOH B O   1 
HETATM 4466 O  O   . HOH J 6 .   ? -7.172  82.178 73.976 1.00 33.54 ? 547 HOH B O   1 
HETATM 4467 O  O   . HOH J 6 .   ? 15.458  75.294 37.870 1.00 29.86 ? 548 HOH B O   1 
HETATM 4468 O  O   . HOH J 6 .   ? -1.842  55.947 68.068 1.00 27.97 ? 549 HOH B O   1 
HETATM 4469 O  O   . HOH J 6 .   ? -7.943  71.260 69.990 1.00 37.16 ? 550 HOH B O   1 
HETATM 4470 O  O   . HOH J 6 .   ? 17.486  81.837 57.750 1.00 34.33 ? 551 HOH B O   1 
HETATM 4471 O  O   . HOH J 6 .   ? -7.731  78.943 56.482 1.00 23.50 ? 552 HOH B O   1 
HETATM 4472 O  O   . HOH J 6 .   ? 11.942  52.545 61.230 1.00 29.00 ? 553 HOH B O   1 
HETATM 4473 O  O   . HOH J 6 .   ? -7.459  74.946 64.464 1.00 28.49 ? 554 HOH B O   1 
HETATM 4474 O  O   . HOH J 6 .   ? 18.862  67.728 71.981 1.00 30.88 ? 555 HOH B O   1 
HETATM 4475 O  O   . HOH J 6 .   ? 16.588  77.671 39.324 1.00 33.27 ? 556 HOH B O   1 
HETATM 4476 O  O   . HOH J 6 .   ? 15.241  68.899 75.410 1.00 32.70 ? 557 HOH B O   1 
HETATM 4477 O  O   . HOH J 6 .   ? -9.498  85.384 56.361 1.00 35.69 ? 558 HOH B O   1 
HETATM 4478 O  O   . HOH J 6 .   ? 16.361  57.851 47.617 1.00 33.43 ? 559 HOH B O   1 
HETATM 4479 O  O   . HOH J 6 .   ? 18.023  55.520 52.362 1.00 29.75 ? 560 HOH B O   1 
HETATM 4480 O  O   . HOH J 6 .   ? 7.851   47.546 56.737 1.00 34.11 ? 561 HOH B O   1 
HETATM 4481 O  O   . HOH J 6 .   ? 5.200   75.508 79.862 1.00 30.46 ? 562 HOH B O   1 
HETATM 4482 O  O   . HOH J 6 .   ? -6.590  73.646 66.599 1.00 30.38 ? 563 HOH B O   1 
HETATM 4483 O  O   . HOH J 6 .   ? 10.222  89.798 50.962 1.00 43.02 ? 564 HOH B O   1 
HETATM 4484 O  O   . HOH J 6 .   ? 15.072  60.378 69.123 1.00 30.66 ? 565 HOH B O   1 
HETATM 4485 O  O   . HOH J 6 .   ? 0.693   86.968 60.412 1.00 31.00 ? 566 HOH B O   1 
HETATM 4486 O  O   . HOH J 6 .   ? -1.069  88.144 61.950 1.00 31.55 ? 567 HOH B O   1 
HETATM 4487 O  O   . HOH J 6 .   ? -6.378  87.611 57.105 1.00 39.67 ? 568 HOH B O   1 
HETATM 4488 O  O   . HOH J 6 .   ? 14.317  75.519 33.553 1.00 45.40 ? 569 HOH B O   1 
HETATM 4489 O  O   . HOH J 6 .   ? 12.757  81.027 45.436 1.00 40.43 ? 570 HOH B O   1 
HETATM 4490 O  O   . HOH J 6 .   ? 0.600   81.076 82.689 1.00 37.22 ? 571 HOH B O   1 
HETATM 4491 O  O   . HOH J 6 .   ? -4.366  57.783 73.088 1.00 34.06 ? 572 HOH B O   1 
HETATM 4492 O  O   . HOH J 6 .   ? 23.624  78.556 53.873 1.00 33.36 ? 573 HOH B O   1 
HETATM 4493 O  O   . HOH J 6 .   ? 4.986   84.848 47.216 1.00 35.93 ? 574 HOH B O   1 
HETATM 4494 O  O   . HOH J 6 .   ? 17.664  79.127 49.546 1.00 34.16 ? 575 HOH B O   1 
HETATM 4495 O  O   . HOH J 6 .   ? 14.818  77.185 48.082 1.00 34.25 ? 576 HOH B O   1 
HETATM 4496 O  O   . HOH J 6 .   ? 6.725   87.309 58.633 1.00 38.18 ? 577 HOH B O   1 
HETATM 4497 O  O   . HOH J 6 .   ? -3.244  90.726 51.271 1.00 32.92 ? 578 HOH B O   1 
HETATM 4498 O  O   . HOH J 6 .   ? -3.796  89.925 54.218 1.00 33.85 ? 579 HOH B O   1 
HETATM 4499 O  O   . HOH J 6 .   ? -8.155  86.008 58.531 1.00 37.61 ? 580 HOH B O   1 
HETATM 4500 O  O   . HOH J 6 .   ? -10.002 84.476 63.205 1.00 38.25 ? 581 HOH B O   1 
HETATM 4501 O  O   . HOH J 6 .   ? -1.257  49.609 61.657 1.00 31.24 ? 582 HOH B O   1 
HETATM 4502 O  O   . HOH J 6 .   ? -13.388 60.396 66.579 1.00 40.80 ? 583 HOH B O   1 
HETATM 4503 O  O   . HOH J 6 .   ? -13.235 74.569 59.393 1.00 36.92 ? 584 HOH B O   1 
HETATM 4504 O  O   . HOH J 6 .   ? 14.043  71.698 74.248 1.00 42.47 ? 585 HOH B O   1 
HETATM 4505 O  O   . HOH J 6 .   ? 24.217  66.770 71.009 1.00 35.29 ? 586 HOH B O   1 
HETATM 4506 O  O   . HOH J 6 .   ? 20.546  61.880 68.739 1.00 33.47 ? 587 HOH B O   1 
HETATM 4507 O  O   . HOH J 6 .   ? 19.064  59.988 68.319 1.00 35.98 ? 588 HOH B O   1 
HETATM 4508 O  O   . HOH J 6 .   ? 15.510  54.676 51.155 1.00 36.80 ? 589 HOH B O   1 
HETATM 4509 O  O   . HOH J 6 .   ? 14.660  54.228 46.574 1.00 30.42 ? 590 HOH B O   1 
HETATM 4510 O  O   . HOH J 6 .   ? 16.417  55.720 45.960 1.00 40.27 ? 591 HOH B O   1 
HETATM 4511 O  O   . HOH J 6 .   ? 12.671  51.055 48.980 1.00 37.17 ? 592 HOH B O   1 
HETATM 4512 O  O   . HOH J 6 .   ? 2.193   88.223 56.416 1.00 39.92 ? 593 HOH B O   1 
HETATM 4513 O  O   . HOH J 6 .   ? -4.448  58.021 77.480 1.00 32.51 ? 594 HOH B O   1 
HETATM 4514 O  O   . HOH J 6 .   ? 1.024   61.079 51.566 1.00 40.05 ? 595 HOH B O   1 
HETATM 4515 O  O   . HOH J 6 .   ? 5.004   72.319 48.847 1.00 32.30 ? 596 HOH B O   1 
HETATM 4516 O  O   . HOH J 6 .   ? -7.811  51.349 51.830 1.00 42.16 ? 597 HOH B O   1 
HETATM 4517 O  O   . HOH J 6 .   ? 2.317   74.017 49.409 1.00 35.16 ? 598 HOH B O   1 
# 
