data_9C50
# 
_entry.id   9C50 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9C50         pdb_00009c50 10.2210/pdb9c50/pdb 
WWPDB D_1000284542 ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-22 ? 
2 'Structure model' 1 1 2025-04-16 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
4 2 'Structure model' '_citation_author.name'    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9C50 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              enrico.dicera@health.slu.edu 
_pdbx_contact_author.name_first         Enrico 
_pdbx_contact_author.name_last          'Di Cera' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2300-4891 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dei Rossi, A.'  1 0009-0006-4883-8744 
'Deavila, S.'    2 ?                   
'Mohammed, B.M.' 3 0000-0001-7227-3663 
'Korolev, S.'    4 0000-0001-9313-7126 
'Di Cera, E.'    5 0000-0003-2300-4891 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Thromb.Haemost. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1538-7836 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            23 
_citation.language                  ? 
_citation.page_first                1241 
_citation.page_last                 1246 
_citation.title                     'Replacement of a single residue changes the primary specificity of thrombin.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jtha.2024.12.024 
_citation.pdbx_database_id_PubMed   39756655 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dei Rossi, A.'  1 ? 
primary 'Deavila, S.'    2 ? 
primary 'Mohammed, B.M.' 3 ? 
primary 'Korolev, S.'    4 ? 
primary 'Di Cera, E.'    5 ? 
# 
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 'Thrombin A-chain' 4096.534  2   ? ? ? ?                                                         
2 polymer     man 'Thrombin B-chain' 31425.033 2   ? ? ? 'Thrombin B-Chain + C-terminus HPC4 tag (YLEDQVDPRLIDGK)' 
3 polymer     syn FPF                441.950   2   ? ? ? ?                                                         
4 non-polymer syn 'SODIUM ION'       22.990    2   ? ? ? ?                                                         
5 water       nat water              18.015    121 ? ? ? ?                                                         
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Coagulation factor II' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  TFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR TFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR A,C ? 
2 'polypeptide(L)' no no  
;IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISM
LEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVL
QVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFY
THVFRLKKWIQKVIDQFGEYLEDQVDPRLIDGK
;
;IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISM
LEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVL
QVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFY
THVFRLKKWIQKVIDQFGEYLEDQVDPRLIDGK
;
B,D ? 
3 'polypeptide(L)' no yes 'FP(PCS)' FPF E,F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'SODIUM ION' NA  
5 water        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   PHE n 
1 3   GLY n 
1 4   SER n 
1 5   GLY n 
1 6   GLU n 
1 7   ALA n 
1 8   ASP n 
1 9   CYS n 
1 10  GLY n 
1 11  LEU n 
1 12  ARG n 
1 13  PRO n 
1 14  LEU n 
1 15  PHE n 
1 16  GLU n 
1 17  LYS n 
1 18  LYS n 
1 19  SER n 
1 20  LEU n 
1 21  GLU n 
1 22  ASP n 
1 23  LYS n 
1 24  THR n 
1 25  GLU n 
1 26  ARG n 
1 27  GLU n 
1 28  LEU n 
1 29  LEU n 
1 30  GLU n 
1 31  SER n 
1 32  TYR n 
1 33  ILE n 
1 34  ASP n 
1 35  GLY n 
1 36  ARG n 
2 1   ILE n 
2 2   VAL n 
2 3   GLU n 
2 4   GLY n 
2 5   SER n 
2 6   ASP n 
2 7   ALA n 
2 8   GLU n 
2 9   ILE n 
2 10  GLY n 
2 11  MET n 
2 12  SER n 
2 13  PRO n 
2 14  TRP n 
2 15  GLN n 
2 16  VAL n 
2 17  MET n 
2 18  LEU n 
2 19  PHE n 
2 20  ARG n 
2 21  LYS n 
2 22  SER n 
2 23  PRO n 
2 24  GLN n 
2 25  GLU n 
2 26  LEU n 
2 27  LEU n 
2 28  CYS n 
2 29  GLY n 
2 30  ALA n 
2 31  SER n 
2 32  LEU n 
2 33  ILE n 
2 34  SER n 
2 35  ASP n 
2 36  ARG n 
2 37  TRP n 
2 38  VAL n 
2 39  LEU n 
2 40  THR n 
2 41  ALA n 
2 42  ALA n 
2 43  HIS n 
2 44  CYS n 
2 45  LEU n 
2 46  LEU n 
2 47  TYR n 
2 48  PRO n 
2 49  PRO n 
2 50  TRP n 
2 51  ASP n 
2 52  LYS n 
2 53  ASN n 
2 54  PHE n 
2 55  THR n 
2 56  GLU n 
2 57  ASN n 
2 58  ASP n 
2 59  LEU n 
2 60  LEU n 
2 61  VAL n 
2 62  ARG n 
2 63  ILE n 
2 64  GLY n 
2 65  LYS n 
2 66  HIS n 
2 67  SER n 
2 68  ARG n 
2 69  THR n 
2 70  ARG n 
2 71  TYR n 
2 72  GLU n 
2 73  ARG n 
2 74  ASN n 
2 75  ILE n 
2 76  GLU n 
2 77  LYS n 
2 78  ILE n 
2 79  SER n 
2 80  MET n 
2 81  LEU n 
2 82  GLU n 
2 83  LYS n 
2 84  ILE n 
2 85  TYR n 
2 86  ILE n 
2 87  HIS n 
2 88  PRO n 
2 89  ARG n 
2 90  TYR n 
2 91  ASN n 
2 92  TRP n 
2 93  ARG n 
2 94  GLU n 
2 95  ASN n 
2 96  LEU n 
2 97  ASP n 
2 98  ARG n 
2 99  ASP n 
2 100 ILE n 
2 101 ALA n 
2 102 LEU n 
2 103 MET n 
2 104 LYS n 
2 105 LEU n 
2 106 LYS n 
2 107 LYS n 
2 108 PRO n 
2 109 VAL n 
2 110 ALA n 
2 111 PHE n 
2 112 SER n 
2 113 ASP n 
2 114 TYR n 
2 115 ILE n 
2 116 HIS n 
2 117 PRO n 
2 118 VAL n 
2 119 CYS n 
2 120 LEU n 
2 121 PRO n 
2 122 ASP n 
2 123 ARG n 
2 124 GLU n 
2 125 THR n 
2 126 ALA n 
2 127 ALA n 
2 128 SER n 
2 129 LEU n 
2 130 LEU n 
2 131 GLN n 
2 132 ALA n 
2 133 GLY n 
2 134 TYR n 
2 135 LYS n 
2 136 GLY n 
2 137 ARG n 
2 138 VAL n 
2 139 THR n 
2 140 GLY n 
2 141 TRP n 
2 142 GLY n 
2 143 ASN n 
2 144 LEU n 
2 145 LYS n 
2 146 GLU n 
2 147 THR n 
2 148 TRP n 
2 149 THR n 
2 150 ALA n 
2 151 ASN n 
2 152 VAL n 
2 153 GLY n 
2 154 LYS n 
2 155 GLY n 
2 156 GLN n 
2 157 PRO n 
2 158 SER n 
2 159 VAL n 
2 160 LEU n 
2 161 GLN n 
2 162 VAL n 
2 163 VAL n 
2 164 ASN n 
2 165 LEU n 
2 166 PRO n 
2 167 ILE n 
2 168 VAL n 
2 169 GLU n 
2 170 ARG n 
2 171 PRO n 
2 172 VAL n 
2 173 CYS n 
2 174 LYS n 
2 175 ASP n 
2 176 SER n 
2 177 THR n 
2 178 ARG n 
2 179 ILE n 
2 180 ARG n 
2 181 ILE n 
2 182 THR n 
2 183 ASP n 
2 184 ASN n 
2 185 MET n 
2 186 PHE n 
2 187 CYS n 
2 188 ALA n 
2 189 GLY n 
2 190 TYR n 
2 191 LYS n 
2 192 PRO n 
2 193 ASP n 
2 194 GLU n 
2 195 GLY n 
2 196 LYS n 
2 197 ARG n 
2 198 GLY n 
2 199 ASP n 
2 200 ALA n 
2 201 CYS n 
2 202 GLU n 
2 203 GLY n 
2 204 ASP n 
2 205 SER n 
2 206 GLY n 
2 207 GLY n 
2 208 PRO n 
2 209 PHE n 
2 210 VAL n 
2 211 MET n 
2 212 LYS n 
2 213 SER n 
2 214 PRO n 
2 215 PHE n 
2 216 ASN n 
2 217 ASN n 
2 218 ARG n 
2 219 TRP n 
2 220 TYR n 
2 221 GLN n 
2 222 MET n 
2 223 GLY n 
2 224 ILE n 
2 225 VAL n 
2 226 SER n 
2 227 TRP n 
2 228 GLY n 
2 229 GLU n 
2 230 GLY n 
2 231 CYS n 
2 232 ASP n 
2 233 ARG n 
2 234 ASP n 
2 235 GLY n 
2 236 LYS n 
2 237 TYR n 
2 238 GLY n 
2 239 PHE n 
2 240 TYR n 
2 241 THR n 
2 242 HIS n 
2 243 VAL n 
2 244 PHE n 
2 245 ARG n 
2 246 LEU n 
2 247 LYS n 
2 248 LYS n 
2 249 TRP n 
2 250 ILE n 
2 251 GLN n 
2 252 LYS n 
2 253 VAL n 
2 254 ILE n 
2 255 ASP n 
2 256 GLN n 
2 257 PHE n 
2 258 GLY n 
2 259 GLU n 
2 260 TYR n 
2 261 LEU n 
2 262 GLU n 
2 263 ASP n 
2 264 GLN n 
2 265 VAL n 
2 266 ASP n 
2 267 PRO n 
2 268 ARG n 
2 269 LEU n 
2 270 ILE n 
2 271 ASP n 
2 272 GLY n 
2 273 LYS n 
3 1   PHE n 
3 2   PRO n 
3 3   PCS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 36  human ? F2 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'golden hamster' 
'Mesocricetus auratus' 10036 ? ? ? ? ? ? ? ? BHK ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 273 human ? F2 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'golden hamster' 
'Mesocricetus auratus' 10036 ? ? ? ? ? ? ? ? BHK ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_src_syn.entity_id              3 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       ? 
_pdbx_entity_src_syn.pdbx_end_seq_num       ? 
_pdbx_entity_src_syn.organism_scientific    'synthetic construct' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       32630 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                    ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                   ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                 ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'            ? 'C4 H7 N O4'     133.103 
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 
NA  non-polymer         . 'SODIUM ION'               ? 'Na 1'           22.990  
PCS 'L-peptide linking' n PHENYLALANYLMETHYLCHLORIDE ? 'C10 H12 Cl N O' 197.661 
PHE 'L-peptide linking' y PHENYLALANINE              ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                    ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                     ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                  ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                 ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                   ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                     ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   THR 1   -5  ?   ?   ?   A . n 
A 1 2   PHE 2   -4  ?   ?   ?   A . n 
A 1 3   GLY 3   -3  ?   ?   ?   A . n 
A 1 4   SER 4   -2  ?   ?   ?   A . n 
A 1 5   GLY 5   -1  ?   ?   ?   A . n 
A 1 6   GLU 6   0   ?   ?   ?   A . n 
A 1 7   ALA 7   1   1   ALA ALA A B n 
A 1 8   ASP 8   1   1   ASP ASP A A n 
A 1 9   CYS 9   1   1   CYS CYS A . n 
A 1 10  GLY 10  2   2   GLY GLY A . n 
A 1 11  LEU 11  3   3   LEU LEU A . n 
A 1 12  ARG 12  4   4   ARG ARG A . n 
A 1 13  PRO 13  5   5   PRO PRO A . n 
A 1 14  LEU 14  6   6   LEU LEU A . n 
A 1 15  PHE 15  7   7   PHE PHE A . n 
A 1 16  GLU 16  8   8   GLU GLU A . n 
A 1 17  LYS 17  9   9   LYS LYS A . n 
A 1 18  LYS 18  10  10  LYS LYS A . n 
A 1 19  SER 19  11  11  SER SER A . n 
A 1 20  LEU 20  12  12  LEU LEU A . n 
A 1 21  GLU 21  13  13  GLU GLU A . n 
A 1 22  ASP 22  14  14  ASP ASP A . n 
A 1 23  LYS 23  14  14  LYS LYS A A n 
A 1 24  THR 24  14  14  THR THR A B n 
A 1 25  GLU 25  14  14  GLU GLU A C n 
A 1 26  ARG 26  14  14  ARG ARG A D n 
A 1 27  GLU 27  14  14  GLU GLU A E n 
A 1 28  LEU 28  14  14  LEU LEU A F n 
A 1 29  LEU 29  14  14  LEU LEU A G n 
A 1 30  GLU 30  14  14  GLU GLU A H n 
A 1 31  SER 31  14  14  SER SER A I n 
A 1 32  TYR 32  14  14  TYR TYR A J n 
A 1 33  ILE 33  14  14  ILE ILE A K n 
A 1 34  ASP 34  15  ?   ?   ?   A . n 
A 1 35  GLY 35  16  ?   ?   ?   A . n 
A 1 36  ARG 36  17  ?   ?   ?   A . n 
B 2 1   ILE 1   16  16  ILE ILE B . n 
B 2 2   VAL 2   17  17  VAL VAL B . n 
B 2 3   GLU 3   18  18  GLU GLU B . n 
B 2 4   GLY 4   19  19  GLY GLY B . n 
B 2 5   SER 5   20  20  SER SER B . n 
B 2 6   ASP 6   21  21  ASP ASP B . n 
B 2 7   ALA 7   22  22  ALA ALA B . n 
B 2 8   GLU 8   23  23  GLU GLU B . n 
B 2 9   ILE 9   24  24  ILE ILE B . n 
B 2 10  GLY 10  25  25  GLY GLY B . n 
B 2 11  MET 11  26  26  MET MET B . n 
B 2 12  SER 12  27  27  SER SER B . n 
B 2 13  PRO 13  28  28  PRO PRO B . n 
B 2 14  TRP 14  29  29  TRP TRP B . n 
B 2 15  GLN 15  30  30  GLN GLN B . n 
B 2 16  VAL 16  31  31  VAL VAL B . n 
B 2 17  MET 17  32  32  MET MET B . n 
B 2 18  LEU 18  33  33  LEU LEU B . n 
B 2 19  PHE 19  34  34  PHE PHE B . n 
B 2 20  ARG 20  35  35  ARG ARG B . n 
B 2 21  LYS 21  36  36  LYS LYS B . n 
B 2 22  SER 22  36  36  SER SER B A n 
B 2 23  PRO 23  37  37  PRO PRO B . n 
B 2 24  GLN 24  38  38  GLN GLN B . n 
B 2 25  GLU 25  39  39  GLU GLU B . n 
B 2 26  LEU 26  40  40  LEU LEU B . n 
B 2 27  LEU 27  41  41  LEU LEU B . n 
B 2 28  CYS 28  42  42  CYS CYS B . n 
B 2 29  GLY 29  43  43  GLY GLY B . n 
B 2 30  ALA 30  44  44  ALA ALA B . n 
B 2 31  SER 31  45  45  SER SER B . n 
B 2 32  LEU 32  46  46  LEU LEU B . n 
B 2 33  ILE 33  47  47  ILE ILE B . n 
B 2 34  SER 34  48  48  SER SER B . n 
B 2 35  ASP 35  49  49  ASP ASP B . n 
B 2 36  ARG 36  50  50  ARG ARG B . n 
B 2 37  TRP 37  51  51  TRP TRP B . n 
B 2 38  VAL 38  52  52  VAL VAL B . n 
B 2 39  LEU 39  53  53  LEU LEU B . n 
B 2 40  THR 40  54  54  THR THR B . n 
B 2 41  ALA 41  55  55  ALA ALA B . n 
B 2 42  ALA 42  56  56  ALA ALA B . n 
B 2 43  HIS 43  57  57  HIS HIS B . n 
B 2 44  CYS 44  58  58  CYS CYS B . n 
B 2 45  LEU 45  59  59  LEU LEU B . n 
B 2 46  LEU 46  60  60  LEU LEU B . n 
B 2 47  TYR 47  60  60  TYR TYR B A n 
B 2 48  PRO 48  60  60  PRO PRO B B n 
B 2 49  PRO 49  60  60  PRO PRO B C n 
B 2 50  TRP 50  60  60  TRP TRP B D n 
B 2 51  ASP 51  60  60  ASP ASP B E n 
B 2 52  LYS 52  60  60  LYS LYS B F n 
B 2 53  ASN 53  60  60  ASN ASN B G n 
B 2 54  PHE 54  60  60  PHE PHE B H n 
B 2 55  THR 55  60  60  THR THR B I n 
B 2 56  GLU 56  61  61  GLU GLU B . n 
B 2 57  ASN 57  62  62  ASN ASN B . n 
B 2 58  ASP 58  63  63  ASP ASP B . n 
B 2 59  LEU 59  64  64  LEU LEU B . n 
B 2 60  LEU 60  65  65  LEU LEU B . n 
B 2 61  VAL 61  66  66  VAL VAL B . n 
B 2 62  ARG 62  67  67  ARG ARG B . n 
B 2 63  ILE 63  68  68  ILE ILE B . n 
B 2 64  GLY 64  69  69  GLY GLY B . n 
B 2 65  LYS 65  70  70  LYS LYS B . n 
B 2 66  HIS 66  71  71  HIS HIS B . n 
B 2 67  SER 67  72  72  SER SER B . n 
B 2 68  ARG 68  73  73  ARG ARG B . n 
B 2 69  THR 69  74  74  THR THR B . n 
B 2 70  ARG 70  75  75  ARG ARG B . n 
B 2 71  TYR 71  76  76  TYR TYR B . n 
B 2 72  GLU 72  77  77  GLU GLU B . n 
B 2 73  ARG 73  77  77  ARG ARG B A n 
B 2 74  ASN 74  78  78  ASN ASN B . n 
B 2 75  ILE 75  79  79  ILE ILE B . n 
B 2 76  GLU 76  80  80  GLU GLU B . n 
B 2 77  LYS 77  81  81  LYS LYS B . n 
B 2 78  ILE 78  82  82  ILE ILE B . n 
B 2 79  SER 79  83  83  SER SER B . n 
B 2 80  MET 80  84  84  MET MET B . n 
B 2 81  LEU 81  85  85  LEU LEU B . n 
B 2 82  GLU 82  86  86  GLU GLU B . n 
B 2 83  LYS 83  87  87  LYS LYS B . n 
B 2 84  ILE 84  88  88  ILE ILE B . n 
B 2 85  TYR 85  89  89  TYR TYR B . n 
B 2 86  ILE 86  90  90  ILE ILE B . n 
B 2 87  HIS 87  91  91  HIS HIS B . n 
B 2 88  PRO 88  92  92  PRO PRO B . n 
B 2 89  ARG 89  93  93  ARG ARG B . n 
B 2 90  TYR 90  94  94  TYR TYR B . n 
B 2 91  ASN 91  95  95  ASN ASN B . n 
B 2 92  TRP 92  96  96  TRP TRP B . n 
B 2 93  ARG 93  97  97  ARG ARG B . n 
B 2 94  GLU 94  97  97  GLU GLU B A n 
B 2 95  ASN 95  98  98  ASN ASN B . n 
B 2 96  LEU 96  99  99  LEU LEU B . n 
B 2 97  ASP 97  100 100 ASP ASP B . n 
B 2 98  ARG 98  101 101 ARG ARG B . n 
B 2 99  ASP 99  102 102 ASP ASP B . n 
B 2 100 ILE 100 103 103 ILE ILE B . n 
B 2 101 ALA 101 104 104 ALA ALA B . n 
B 2 102 LEU 102 105 105 LEU LEU B . n 
B 2 103 MET 103 106 106 MET MET B . n 
B 2 104 LYS 104 107 107 LYS LYS B . n 
B 2 105 LEU 105 108 108 LEU LEU B . n 
B 2 106 LYS 106 109 109 LYS LYS B . n 
B 2 107 LYS 107 110 110 LYS LYS B . n 
B 2 108 PRO 108 111 111 PRO PRO B . n 
B 2 109 VAL 109 112 112 VAL VAL B . n 
B 2 110 ALA 110 113 113 ALA ALA B . n 
B 2 111 PHE 111 114 114 PHE PHE B . n 
B 2 112 SER 112 115 115 SER SER B . n 
B 2 113 ASP 113 116 116 ASP ASP B . n 
B 2 114 TYR 114 117 117 TYR TYR B . n 
B 2 115 ILE 115 118 118 ILE ILE B . n 
B 2 116 HIS 116 119 119 HIS HIS B . n 
B 2 117 PRO 117 120 120 PRO PRO B . n 
B 2 118 VAL 118 121 121 VAL VAL B . n 
B 2 119 CYS 119 122 122 CYS CYS B . n 
B 2 120 LEU 120 123 123 LEU LEU B . n 
B 2 121 PRO 121 124 124 PRO PRO B . n 
B 2 122 ASP 122 125 125 ASP ASP B . n 
B 2 123 ARG 123 126 126 ARG ARG B . n 
B 2 124 GLU 124 127 127 GLU GLU B . n 
B 2 125 THR 125 128 128 THR THR B . n 
B 2 126 ALA 126 129 129 ALA ALA B . n 
B 2 127 ALA 127 129 129 ALA ALA B A n 
B 2 128 SER 128 129 129 SER SER B B n 
B 2 129 LEU 129 129 129 LEU LEU B C n 
B 2 130 LEU 130 130 130 LEU LEU B . n 
B 2 131 GLN 131 131 131 GLN GLN B . n 
B 2 132 ALA 132 132 132 ALA ALA B . n 
B 2 133 GLY 133 133 133 GLY GLY B . n 
B 2 134 TYR 134 134 134 TYR TYR B . n 
B 2 135 LYS 135 135 135 LYS LYS B . n 
B 2 136 GLY 136 136 136 GLY GLY B . n 
B 2 137 ARG 137 137 137 ARG ARG B . n 
B 2 138 VAL 138 138 138 VAL VAL B . n 
B 2 139 THR 139 139 139 THR THR B . n 
B 2 140 GLY 140 140 140 GLY GLY B . n 
B 2 141 TRP 141 141 141 TRP TRP B . n 
B 2 142 GLY 142 142 142 GLY GLY B . n 
B 2 143 ASN 143 143 143 ASN ASN B . n 
B 2 144 LEU 144 144 144 LEU LEU B . n 
B 2 145 LYS 145 145 145 LYS LYS B . n 
B 2 146 GLU 146 146 146 GLU GLU B . n 
B 2 147 THR 147 147 147 THR THR B . n 
B 2 148 TRP 148 147 ?   ?   ?   B A n 
B 2 149 THR 149 147 ?   ?   ?   B B n 
B 2 150 ALA 150 147 ?   ?   ?   B C n 
B 2 151 ASN 151 147 ?   ?   ?   B D n 
B 2 152 VAL 152 147 ?   ?   ?   B E n 
B 2 153 GLY 153 147 ?   ?   ?   B F n 
B 2 154 LYS 154 147 ?   ?   ?   B G n 
B 2 155 GLY 155 150 150 GLY GLY B . n 
B 2 156 GLN 156 151 151 GLN GLN B . n 
B 2 157 PRO 157 152 152 PRO PRO B . n 
B 2 158 SER 158 153 153 SER SER B . n 
B 2 159 VAL 159 154 154 VAL VAL B . n 
B 2 160 LEU 160 155 155 LEU LEU B . n 
B 2 161 GLN 161 156 156 GLN GLN B . n 
B 2 162 VAL 162 157 157 VAL VAL B . n 
B 2 163 VAL 163 158 158 VAL VAL B . n 
B 2 164 ASN 164 159 159 ASN ASN B . n 
B 2 165 LEU 165 160 160 LEU LEU B . n 
B 2 166 PRO 166 161 161 PRO PRO B . n 
B 2 167 ILE 167 162 162 ILE ILE B . n 
B 2 168 VAL 168 163 163 VAL VAL B . n 
B 2 169 GLU 169 164 164 GLU GLU B . n 
B 2 170 ARG 170 165 165 ARG ARG B . n 
B 2 171 PRO 171 166 166 PRO PRO B . n 
B 2 172 VAL 172 167 167 VAL VAL B . n 
B 2 173 CYS 173 168 168 CYS CYS B . n 
B 2 174 LYS 174 169 169 LYS LYS B . n 
B 2 175 ASP 175 170 170 ASP ASP B . n 
B 2 176 SER 176 171 171 SER SER B . n 
B 2 177 THR 177 172 172 THR THR B . n 
B 2 178 ARG 178 173 173 ARG ARG B . n 
B 2 179 ILE 179 174 174 ILE ILE B . n 
B 2 180 ARG 180 175 175 ARG ARG B . n 
B 2 181 ILE 181 176 176 ILE ILE B . n 
B 2 182 THR 182 177 177 THR THR B . n 
B 2 183 ASP 183 178 178 ASP ASP B . n 
B 2 184 ASN 184 179 179 ASN ASN B . n 
B 2 185 MET 185 180 180 MET MET B . n 
B 2 186 PHE 186 181 181 PHE PHE B . n 
B 2 187 CYS 187 182 182 CYS CYS B . n 
B 2 188 ALA 188 183 183 ALA ALA B . n 
B 2 189 GLY 189 184 184 GLY GLY B . n 
B 2 190 TYR 190 184 184 TYR TYR B A n 
B 2 191 LYS 191 185 185 LYS LYS B . n 
B 2 192 PRO 192 186 186 PRO PRO B . n 
B 2 193 ASP 193 186 186 ASP ASP B A n 
B 2 194 GLU 194 186 186 GLU GLU B B n 
B 2 195 GLY 195 186 186 GLY GLY B C n 
B 2 196 LYS 196 186 186 LYS LYS B D n 
B 2 197 ARG 197 187 187 ARG ARG B . n 
B 2 198 GLY 198 188 188 GLY GLY B . n 
B 2 199 ASP 199 189 189 ASP ASP B . n 
B 2 200 ALA 200 190 190 ALA ALA B . n 
B 2 201 CYS 201 191 191 CYS CYS B . n 
B 2 202 GLU 202 192 192 GLU GLU B . n 
B 2 203 GLY 203 193 193 GLY GLY B . n 
B 2 204 ASP 204 194 194 ASP ASP B . n 
B 2 205 SER 205 195 195 SER SER B . n 
B 2 206 GLY 206 196 196 GLY GLY B . n 
B 2 207 GLY 207 197 197 GLY GLY B . n 
B 2 208 PRO 208 198 198 PRO PRO B . n 
B 2 209 PHE 209 199 199 PHE PHE B . n 
B 2 210 VAL 210 200 200 VAL VAL B . n 
B 2 211 MET 211 201 201 MET MET B . n 
B 2 212 LYS 212 202 202 LYS LYS B . n 
B 2 213 SER 213 203 203 SER SER B . n 
B 2 214 PRO 214 204 204 PRO PRO B . n 
B 2 215 PHE 215 204 204 PHE PHE B A n 
B 2 216 ASN 216 204 204 ASN ASN B B n 
B 2 217 ASN 217 205 205 ASN ASN B . n 
B 2 218 ARG 218 206 206 ARG ARG B . n 
B 2 219 TRP 219 207 207 TRP TRP B . n 
B 2 220 TYR 220 208 208 TYR TYR B . n 
B 2 221 GLN 221 209 209 GLN GLN B . n 
B 2 222 MET 222 210 210 MET MET B . n 
B 2 223 GLY 223 211 211 GLY GLY B . n 
B 2 224 ILE 224 212 212 ILE ILE B . n 
B 2 225 VAL 225 213 213 VAL VAL B . n 
B 2 226 SER 226 214 214 SER SER B . n 
B 2 227 TRP 227 215 215 TRP TRP B . n 
B 2 228 GLY 228 216 216 GLY GLY B . n 
B 2 229 GLU 229 217 217 GLU GLU B . n 
B 2 230 GLY 230 219 219 GLY GLY B . n 
B 2 231 CYS 231 220 220 CYS CYS B . n 
B 2 232 ASP 232 221 221 ASP ASP B . n 
B 2 233 ARG 233 221 221 ARG ARG B A n 
B 2 234 ASP 234 222 222 ASP ASP B . n 
B 2 235 GLY 235 223 223 GLY GLY B . n 
B 2 236 LYS 236 224 224 LYS LYS B . n 
B 2 237 TYR 237 225 225 TYR TYR B . n 
B 2 238 GLY 238 226 226 GLY GLY B . n 
B 2 239 PHE 239 227 227 PHE PHE B . n 
B 2 240 TYR 240 228 228 TYR TYR B . n 
B 2 241 THR 241 229 229 THR THR B . n 
B 2 242 HIS 242 230 230 HIS HIS B . n 
B 2 243 VAL 243 231 231 VAL VAL B . n 
B 2 244 PHE 244 232 232 PHE PHE B . n 
B 2 245 ARG 245 233 233 ARG ARG B . n 
B 2 246 LEU 246 234 234 LEU LEU B . n 
B 2 247 LYS 247 235 235 LYS LYS B . n 
B 2 248 LYS 248 236 236 LYS LYS B . n 
B 2 249 TRP 249 237 237 TRP TRP B . n 
B 2 250 ILE 250 238 238 ILE ILE B . n 
B 2 251 GLN 251 239 239 GLN GLN B . n 
B 2 252 LYS 252 240 240 LYS LYS B . n 
B 2 253 VAL 253 241 241 VAL VAL B . n 
B 2 254 ILE 254 242 242 ILE ILE B . n 
B 2 255 ASP 255 243 243 ASP ASP B . n 
B 2 256 GLN 256 244 244 GLN GLN B . n 
B 2 257 PHE 257 245 245 PHE PHE B . n 
B 2 258 GLY 258 246 ?   ?   ?   B . n 
B 2 259 GLU 259 247 ?   ?   ?   B . n 
B 2 260 TYR 260 248 ?   ?   ?   B . n 
B 2 261 LEU 261 249 ?   ?   ?   B . n 
B 2 262 GLU 262 250 ?   ?   ?   B . n 
B 2 263 ASP 263 251 ?   ?   ?   B . n 
B 2 264 GLN 264 252 ?   ?   ?   B . n 
B 2 265 VAL 265 253 ?   ?   ?   B . n 
B 2 266 ASP 266 254 ?   ?   ?   B . n 
B 2 267 PRO 267 255 ?   ?   ?   B . n 
B 2 268 ARG 268 256 ?   ?   ?   B . n 
B 2 269 LEU 269 257 ?   ?   ?   B . n 
B 2 270 ILE 270 258 ?   ?   ?   B . n 
B 2 271 ASP 271 259 ?   ?   ?   B . n 
B 2 272 GLY 272 260 ?   ?   ?   B . n 
B 2 273 LYS 273 261 ?   ?   ?   B . n 
C 1 1   THR 1   -5  ?   ?   ?   C . n 
C 1 2   PHE 2   -4  ?   ?   ?   C . n 
C 1 3   GLY 3   -3  ?   ?   ?   C . n 
C 1 4   SER 4   -2  ?   ?   ?   C . n 
C 1 5   GLY 5   -1  ?   ?   ?   C . n 
C 1 6   GLU 6   0   ?   ?   ?   C . n 
C 1 7   ALA 7   1   1   ALA ALA C B n 
C 1 8   ASP 8   1   1   ASP ASP C A n 
C 1 9   CYS 9   1   1   CYS CYS C . n 
C 1 10  GLY 10  2   2   GLY GLY C . n 
C 1 11  LEU 11  3   3   LEU LEU C . n 
C 1 12  ARG 12  4   4   ARG ARG C . n 
C 1 13  PRO 13  5   5   PRO PRO C . n 
C 1 14  LEU 14  6   6   LEU LEU C . n 
C 1 15  PHE 15  7   7   PHE PHE C . n 
C 1 16  GLU 16  8   8   GLU GLU C . n 
C 1 17  LYS 17  9   9   LYS LYS C . n 
C 1 18  LYS 18  10  10  LYS LYS C . n 
C 1 19  SER 19  11  11  SER SER C . n 
C 1 20  LEU 20  12  12  LEU LEU C . n 
C 1 21  GLU 21  13  13  GLU GLU C . n 
C 1 22  ASP 22  14  14  ASP ASP C . n 
C 1 23  LYS 23  14  14  LYS LYS C A n 
C 1 24  THR 24  14  14  THR THR C B n 
C 1 25  GLU 25  14  14  GLU GLU C C n 
C 1 26  ARG 26  14  14  ARG ARG C D n 
C 1 27  GLU 27  14  14  GLU GLU C E n 
C 1 28  LEU 28  14  14  LEU LEU C F n 
C 1 29  LEU 29  14  14  LEU LEU C G n 
C 1 30  GLU 30  14  14  GLU GLU C H n 
C 1 31  SER 31  14  14  SER SER C I n 
C 1 32  TYR 32  14  14  TYR TYR C J n 
C 1 33  ILE 33  14  14  ILE ILE C K n 
C 1 34  ASP 34  15  ?   ?   ?   C . n 
C 1 35  GLY 35  16  ?   ?   ?   C . n 
C 1 36  ARG 36  17  ?   ?   ?   C . n 
D 2 1   ILE 1   16  16  ILE ILE D . n 
D 2 2   VAL 2   17  17  VAL VAL D . n 
D 2 3   GLU 3   18  18  GLU GLU D . n 
D 2 4   GLY 4   19  19  GLY GLY D . n 
D 2 5   SER 5   20  20  SER SER D . n 
D 2 6   ASP 6   21  21  ASP ASP D . n 
D 2 7   ALA 7   22  22  ALA ALA D . n 
D 2 8   GLU 8   23  23  GLU GLU D . n 
D 2 9   ILE 9   24  24  ILE ILE D . n 
D 2 10  GLY 10  25  25  GLY GLY D . n 
D 2 11  MET 11  26  26  MET MET D . n 
D 2 12  SER 12  27  27  SER SER D . n 
D 2 13  PRO 13  28  28  PRO PRO D . n 
D 2 14  TRP 14  29  29  TRP TRP D . n 
D 2 15  GLN 15  30  30  GLN GLN D . n 
D 2 16  VAL 16  31  31  VAL VAL D . n 
D 2 17  MET 17  32  32  MET MET D . n 
D 2 18  LEU 18  33  33  LEU LEU D . n 
D 2 19  PHE 19  34  34  PHE PHE D . n 
D 2 20  ARG 20  35  35  ARG ARG D . n 
D 2 21  LYS 21  36  36  LYS LYS D . n 
D 2 22  SER 22  36  36  SER SER D A n 
D 2 23  PRO 23  37  37  PRO PRO D . n 
D 2 24  GLN 24  38  38  GLN GLN D . n 
D 2 25  GLU 25  39  39  GLU GLU D . n 
D 2 26  LEU 26  40  40  LEU LEU D . n 
D 2 27  LEU 27  41  41  LEU LEU D . n 
D 2 28  CYS 28  42  42  CYS CYS D . n 
D 2 29  GLY 29  43  43  GLY GLY D . n 
D 2 30  ALA 30  44  44  ALA ALA D . n 
D 2 31  SER 31  45  45  SER SER D . n 
D 2 32  LEU 32  46  46  LEU LEU D . n 
D 2 33  ILE 33  47  47  ILE ILE D . n 
D 2 34  SER 34  48  48  SER SER D . n 
D 2 35  ASP 35  49  49  ASP ASP D . n 
D 2 36  ARG 36  50  50  ARG ARG D . n 
D 2 37  TRP 37  51  51  TRP TRP D . n 
D 2 38  VAL 38  52  52  VAL VAL D . n 
D 2 39  LEU 39  53  53  LEU LEU D . n 
D 2 40  THR 40  54  54  THR THR D . n 
D 2 41  ALA 41  55  55  ALA ALA D . n 
D 2 42  ALA 42  56  56  ALA ALA D . n 
D 2 43  HIS 43  57  57  HIS HIS D . n 
D 2 44  CYS 44  58  58  CYS CYS D . n 
D 2 45  LEU 45  59  59  LEU LEU D . n 
D 2 46  LEU 46  60  60  LEU LEU D . n 
D 2 47  TYR 47  60  60  TYR TYR D A n 
D 2 48  PRO 48  60  60  PRO PRO D B n 
D 2 49  PRO 49  60  60  PRO PRO D C n 
D 2 50  TRP 50  60  60  TRP TRP D D n 
D 2 51  ASP 51  60  60  ASP ASP D E n 
D 2 52  LYS 52  60  60  LYS LYS D F n 
D 2 53  ASN 53  60  60  ASN ASN D G n 
D 2 54  PHE 54  60  60  PHE PHE D H n 
D 2 55  THR 55  60  60  THR THR D I n 
D 2 56  GLU 56  61  61  GLU GLU D . n 
D 2 57  ASN 57  62  62  ASN ASN D . n 
D 2 58  ASP 58  63  63  ASP ASP D . n 
D 2 59  LEU 59  64  64  LEU LEU D . n 
D 2 60  LEU 60  65  65  LEU LEU D . n 
D 2 61  VAL 61  66  66  VAL VAL D . n 
D 2 62  ARG 62  67  67  ARG ARG D . n 
D 2 63  ILE 63  68  68  ILE ILE D . n 
D 2 64  GLY 64  69  69  GLY GLY D . n 
D 2 65  LYS 65  70  70  LYS LYS D . n 
D 2 66  HIS 66  71  71  HIS HIS D . n 
D 2 67  SER 67  72  72  SER SER D . n 
D 2 68  ARG 68  73  73  ARG ARG D . n 
D 2 69  THR 69  74  74  THR THR D . n 
D 2 70  ARG 70  75  75  ARG ARG D . n 
D 2 71  TYR 71  76  76  TYR TYR D . n 
D 2 72  GLU 72  77  77  GLU GLU D . n 
D 2 73  ARG 73  77  77  ARG ARG D A n 
D 2 74  ASN 74  78  78  ASN ASN D . n 
D 2 75  ILE 75  79  79  ILE ILE D . n 
D 2 76  GLU 76  80  80  GLU GLU D . n 
D 2 77  LYS 77  81  81  LYS LYS D . n 
D 2 78  ILE 78  82  82  ILE ILE D . n 
D 2 79  SER 79  83  83  SER SER D . n 
D 2 80  MET 80  84  84  MET MET D . n 
D 2 81  LEU 81  85  85  LEU LEU D . n 
D 2 82  GLU 82  86  86  GLU GLU D . n 
D 2 83  LYS 83  87  87  LYS LYS D . n 
D 2 84  ILE 84  88  88  ILE ILE D . n 
D 2 85  TYR 85  89  89  TYR TYR D . n 
D 2 86  ILE 86  90  90  ILE ILE D . n 
D 2 87  HIS 87  91  91  HIS HIS D . n 
D 2 88  PRO 88  92  92  PRO PRO D . n 
D 2 89  ARG 89  93  93  ARG ARG D . n 
D 2 90  TYR 90  94  94  TYR TYR D . n 
D 2 91  ASN 91  95  95  ASN ASN D . n 
D 2 92  TRP 92  96  96  TRP TRP D . n 
D 2 93  ARG 93  97  97  ARG ARG D . n 
D 2 94  GLU 94  97  97  GLU GLU D A n 
D 2 95  ASN 95  98  98  ASN ASN D . n 
D 2 96  LEU 96  99  99  LEU LEU D . n 
D 2 97  ASP 97  100 100 ASP ASP D . n 
D 2 98  ARG 98  101 101 ARG ARG D . n 
D 2 99  ASP 99  102 102 ASP ASP D . n 
D 2 100 ILE 100 103 103 ILE ILE D . n 
D 2 101 ALA 101 104 104 ALA ALA D . n 
D 2 102 LEU 102 105 105 LEU LEU D . n 
D 2 103 MET 103 106 106 MET MET D . n 
D 2 104 LYS 104 107 107 LYS LYS D . n 
D 2 105 LEU 105 108 108 LEU LEU D . n 
D 2 106 LYS 106 109 109 LYS LYS D . n 
D 2 107 LYS 107 110 110 LYS LYS D . n 
D 2 108 PRO 108 111 111 PRO PRO D . n 
D 2 109 VAL 109 112 112 VAL VAL D . n 
D 2 110 ALA 110 113 113 ALA ALA D . n 
D 2 111 PHE 111 114 114 PHE PHE D . n 
D 2 112 SER 112 115 115 SER SER D . n 
D 2 113 ASP 113 116 116 ASP ASP D . n 
D 2 114 TYR 114 117 117 TYR TYR D . n 
D 2 115 ILE 115 118 118 ILE ILE D . n 
D 2 116 HIS 116 119 119 HIS HIS D . n 
D 2 117 PRO 117 120 120 PRO PRO D . n 
D 2 118 VAL 118 121 121 VAL VAL D . n 
D 2 119 CYS 119 122 122 CYS CYS D . n 
D 2 120 LEU 120 123 123 LEU LEU D . n 
D 2 121 PRO 121 124 124 PRO PRO D . n 
D 2 122 ASP 122 125 125 ASP ASP D . n 
D 2 123 ARG 123 126 126 ARG ARG D . n 
D 2 124 GLU 124 127 127 GLU GLU D . n 
D 2 125 THR 125 128 128 THR THR D . n 
D 2 126 ALA 126 129 129 ALA ALA D . n 
D 2 127 ALA 127 129 129 ALA ALA D A n 
D 2 128 SER 128 129 129 SER SER D B n 
D 2 129 LEU 129 129 129 LEU LEU D C n 
D 2 130 LEU 130 130 130 LEU LEU D . n 
D 2 131 GLN 131 131 131 GLN GLN D . n 
D 2 132 ALA 132 132 132 ALA ALA D . n 
D 2 133 GLY 133 133 133 GLY GLY D . n 
D 2 134 TYR 134 134 134 TYR TYR D . n 
D 2 135 LYS 135 135 135 LYS LYS D . n 
D 2 136 GLY 136 136 136 GLY GLY D . n 
D 2 137 ARG 137 137 137 ARG ARG D . n 
D 2 138 VAL 138 138 138 VAL VAL D . n 
D 2 139 THR 139 139 139 THR THR D . n 
D 2 140 GLY 140 140 140 GLY GLY D . n 
D 2 141 TRP 141 141 141 TRP TRP D . n 
D 2 142 GLY 142 142 142 GLY GLY D . n 
D 2 143 ASN 143 143 143 ASN ASN D . n 
D 2 144 LEU 144 144 144 LEU LEU D . n 
D 2 145 LYS 145 145 145 LYS LYS D . n 
D 2 146 GLU 146 146 146 GLU GLU D . n 
D 2 147 THR 147 147 147 THR THR D . n 
D 2 148 TRP 148 147 ?   ?   ?   D A n 
D 2 149 THR 149 147 ?   ?   ?   D B n 
D 2 150 ALA 150 147 ?   ?   ?   D C n 
D 2 151 ASN 151 147 ?   ?   ?   D D n 
D 2 152 VAL 152 147 ?   ?   ?   D E n 
D 2 153 GLY 153 147 ?   ?   ?   D F n 
D 2 154 LYS 154 147 ?   ?   ?   D G n 
D 2 155 GLY 155 150 150 GLY GLY D . n 
D 2 156 GLN 156 151 151 GLN GLN D . n 
D 2 157 PRO 157 152 152 PRO PRO D . n 
D 2 158 SER 158 153 153 SER SER D . n 
D 2 159 VAL 159 154 154 VAL VAL D . n 
D 2 160 LEU 160 155 155 LEU LEU D . n 
D 2 161 GLN 161 156 156 GLN GLN D . n 
D 2 162 VAL 162 157 157 VAL VAL D . n 
D 2 163 VAL 163 158 158 VAL VAL D . n 
D 2 164 ASN 164 159 159 ASN ASN D . n 
D 2 165 LEU 165 160 160 LEU LEU D . n 
D 2 166 PRO 166 161 161 PRO PRO D . n 
D 2 167 ILE 167 162 162 ILE ILE D . n 
D 2 168 VAL 168 163 163 VAL VAL D . n 
D 2 169 GLU 169 164 164 GLU GLU D . n 
D 2 170 ARG 170 165 165 ARG ARG D . n 
D 2 171 PRO 171 166 166 PRO PRO D . n 
D 2 172 VAL 172 167 167 VAL VAL D . n 
D 2 173 CYS 173 168 168 CYS CYS D . n 
D 2 174 LYS 174 169 169 LYS LYS D . n 
D 2 175 ASP 175 170 170 ASP ASP D . n 
D 2 176 SER 176 171 171 SER SER D . n 
D 2 177 THR 177 172 172 THR THR D . n 
D 2 178 ARG 178 173 173 ARG ARG D . n 
D 2 179 ILE 179 174 174 ILE ILE D . n 
D 2 180 ARG 180 175 175 ARG ARG D . n 
D 2 181 ILE 181 176 176 ILE ILE D . n 
D 2 182 THR 182 177 177 THR THR D . n 
D 2 183 ASP 183 178 178 ASP ASP D . n 
D 2 184 ASN 184 179 179 ASN ASN D . n 
D 2 185 MET 185 180 180 MET MET D . n 
D 2 186 PHE 186 181 181 PHE PHE D . n 
D 2 187 CYS 187 182 182 CYS CYS D . n 
D 2 188 ALA 188 183 183 ALA ALA D . n 
D 2 189 GLY 189 184 184 GLY GLY D . n 
D 2 190 TYR 190 184 184 TYR TYR D A n 
D 2 191 LYS 191 185 185 LYS LYS D . n 
D 2 192 PRO 192 186 186 PRO PRO D . n 
D 2 193 ASP 193 186 186 ASP ASP D A n 
D 2 194 GLU 194 186 186 GLU GLU D B n 
D 2 195 GLY 195 186 186 GLY GLY D C n 
D 2 196 LYS 196 186 186 LYS LYS D D n 
D 2 197 ARG 197 187 187 ARG ARG D . n 
D 2 198 GLY 198 188 188 GLY GLY D . n 
D 2 199 ASP 199 189 189 ASP ASP D . n 
D 2 200 ALA 200 190 190 ALA ALA D . n 
D 2 201 CYS 201 191 191 CYS CYS D . n 
D 2 202 GLU 202 192 192 GLU GLU D . n 
D 2 203 GLY 203 193 193 GLY GLY D . n 
D 2 204 ASP 204 194 194 ASP ASP D . n 
D 2 205 SER 205 195 195 SER SER D . n 
D 2 206 GLY 206 196 196 GLY GLY D . n 
D 2 207 GLY 207 197 197 GLY GLY D . n 
D 2 208 PRO 208 198 198 PRO PRO D . n 
D 2 209 PHE 209 199 199 PHE PHE D . n 
D 2 210 VAL 210 200 200 VAL VAL D . n 
D 2 211 MET 211 201 201 MET MET D . n 
D 2 212 LYS 212 202 202 LYS LYS D . n 
D 2 213 SER 213 203 203 SER SER D . n 
D 2 214 PRO 214 204 204 PRO PRO D . n 
D 2 215 PHE 215 204 204 PHE PHE D A n 
D 2 216 ASN 216 204 204 ASN ASN D B n 
D 2 217 ASN 217 205 205 ASN ASN D . n 
D 2 218 ARG 218 206 206 ARG ARG D . n 
D 2 219 TRP 219 207 207 TRP TRP D . n 
D 2 220 TYR 220 208 208 TYR TYR D . n 
D 2 221 GLN 221 209 209 GLN GLN D . n 
D 2 222 MET 222 210 210 MET MET D . n 
D 2 223 GLY 223 211 211 GLY GLY D . n 
D 2 224 ILE 224 212 212 ILE ILE D . n 
D 2 225 VAL 225 213 213 VAL VAL D . n 
D 2 226 SER 226 214 214 SER SER D . n 
D 2 227 TRP 227 215 215 TRP TRP D . n 
D 2 228 GLY 228 216 216 GLY GLY D . n 
D 2 229 GLU 229 217 217 GLU GLU D . n 
D 2 230 GLY 230 219 219 GLY GLY D . n 
D 2 231 CYS 231 220 220 CYS CYS D . n 
D 2 232 ASP 232 221 221 ASP ASP D . n 
D 2 233 ARG 233 221 221 ARG ARG D A n 
D 2 234 ASP 234 222 222 ASP ASP D . n 
D 2 235 GLY 235 223 223 GLY GLY D . n 
D 2 236 LYS 236 224 224 LYS LYS D . n 
D 2 237 TYR 237 225 225 TYR TYR D . n 
D 2 238 GLY 238 226 226 GLY GLY D . n 
D 2 239 PHE 239 227 227 PHE PHE D . n 
D 2 240 TYR 240 228 228 TYR TYR D . n 
D 2 241 THR 241 229 229 THR THR D . n 
D 2 242 HIS 242 230 230 HIS HIS D . n 
D 2 243 VAL 243 231 231 VAL VAL D . n 
D 2 244 PHE 244 232 232 PHE PHE D . n 
D 2 245 ARG 245 233 233 ARG ARG D . n 
D 2 246 LEU 246 234 234 LEU LEU D . n 
D 2 247 LYS 247 235 235 LYS LYS D . n 
D 2 248 LYS 248 236 236 LYS LYS D . n 
D 2 249 TRP 249 237 237 TRP TRP D . n 
D 2 250 ILE 250 238 238 ILE ILE D . n 
D 2 251 GLN 251 239 239 GLN GLN D . n 
D 2 252 LYS 252 240 240 LYS LYS D . n 
D 2 253 VAL 253 241 241 VAL VAL D . n 
D 2 254 ILE 254 242 242 ILE ILE D . n 
D 2 255 ASP 255 243 243 ASP ASP D . n 
D 2 256 GLN 256 244 244 GLN GLN D . n 
D 2 257 PHE 257 245 245 PHE PHE D . n 
D 2 258 GLY 258 246 246 GLY GLY D . n 
D 2 259 GLU 259 247 247 GLU GLU D . n 
D 2 260 TYR 260 248 248 TYR TYR D . n 
D 2 261 LEU 261 249 249 LEU LEU D . n 
D 2 262 GLU 262 250 250 GLU GLU D . n 
D 2 263 ASP 263 251 251 ASP ASP D . n 
D 2 264 GLN 264 252 252 GLN GLN D . n 
D 2 265 VAL 265 253 253 VAL VAL D . n 
D 2 266 ASP 266 254 ?   ?   ?   D . n 
D 2 267 PRO 267 255 ?   ?   ?   D . n 
D 2 268 ARG 268 256 ?   ?   ?   D . n 
D 2 269 LEU 269 257 ?   ?   ?   D . n 
D 2 270 ILE 270 258 ?   ?   ?   D . n 
D 2 271 ASP 271 259 ?   ?   ?   D . n 
D 2 272 GLY 272 260 ?   ?   ?   D . n 
D 2 273 LYS 273 261 ?   ?   ?   D . n 
E 3 1   PHE 1   1   301 PHE FPF E . n 
E 3 2   PRO 2   2   301 PRO FPF E . n 
E 3 3   PCS 3   3   301 PCS FPF E . n 
F 3 1   PHE 1   1   301 PHE FPF F . n 
F 3 2   PRO 2   2   301 PRO FPF F . n 
F 3 3   PCS 3   3   301 PCS FPF F . 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 
G 4 NA  1  301 302 NA  NA  B . 
H 4 NA  1  301 303 NA  NA  D . 
I 5 HOH 1  101 59  HOH HOH A . 
J 5 HOH 1  401 18  HOH HOH B . 
J 5 HOH 2  402 56  HOH HOH B . 
J 5 HOH 3  403 9   HOH HOH B . 
J 5 HOH 4  404 31  HOH HOH B . 
J 5 HOH 5  405 85  HOH HOH B . 
J 5 HOH 6  406 122 HOH HOH B . 
J 5 HOH 7  407 72  HOH HOH B . 
J 5 HOH 8  408 12  HOH HOH B . 
J 5 HOH 9  409 30  HOH HOH B . 
J 5 HOH 10 410 34  HOH HOH B . 
J 5 HOH 11 411 33  HOH HOH B . 
J 5 HOH 12 412 37  HOH HOH B . 
J 5 HOH 13 413 44  HOH HOH B . 
J 5 HOH 14 414 54  HOH HOH B . 
J 5 HOH 15 415 112 HOH HOH B . 
J 5 HOH 16 416 2   HOH HOH B . 
J 5 HOH 17 417 88  HOH HOH B . 
J 5 HOH 18 418 15  HOH HOH B . 
J 5 HOH 19 419 49  HOH HOH B . 
J 5 HOH 20 420 95  HOH HOH B . 
J 5 HOH 21 421 64  HOH HOH B . 
J 5 HOH 22 422 84  HOH HOH B . 
J 5 HOH 23 423 74  HOH HOH B . 
J 5 HOH 24 424 106 HOH HOH B . 
J 5 HOH 25 425 73  HOH HOH B . 
J 5 HOH 26 426 87  HOH HOH B . 
J 5 HOH 27 427 120 HOH HOH B . 
J 5 HOH 28 428 113 HOH HOH B . 
J 5 HOH 29 429 29  HOH HOH B . 
J 5 HOH 30 430 63  HOH HOH B . 
J 5 HOH 31 431 69  HOH HOH B . 
J 5 HOH 32 432 109 HOH HOH B . 
J 5 HOH 33 433 19  HOH HOH B . 
J 5 HOH 34 434 41  HOH HOH B . 
J 5 HOH 35 435 46  HOH HOH B . 
J 5 HOH 36 436 77  HOH HOH B . 
J 5 HOH 37 437 67  HOH HOH B . 
J 5 HOH 38 438 100 HOH HOH B . 
J 5 HOH 39 439 108 HOH HOH B . 
J 5 HOH 40 440 91  HOH HOH B . 
J 5 HOH 41 441 47  HOH HOH B . 
J 5 HOH 42 442 117 HOH HOH B . 
J 5 HOH 43 443 81  HOH HOH B . 
K 5 HOH 1  101 14  HOH HOH C . 
K 5 HOH 2  102 42  HOH HOH C . 
K 5 HOH 3  103 3   HOH HOH C . 
K 5 HOH 4  104 17  HOH HOH C . 
K 5 HOH 5  105 21  HOH HOH C . 
K 5 HOH 6  106 71  HOH HOH C . 
L 5 HOH 1  401 99  HOH HOH D . 
L 5 HOH 2  402 76  HOH HOH D . 
L 5 HOH 3  403 5   HOH HOH D . 
L 5 HOH 4  404 96  HOH HOH D . 
L 5 HOH 5  405 45  HOH HOH D . 
L 5 HOH 6  406 121 HOH HOH D . 
L 5 HOH 7  407 27  HOH HOH D . 
L 5 HOH 8  408 48  HOH HOH D . 
L 5 HOH 9  409 60  HOH HOH D . 
L 5 HOH 10 410 28  HOH HOH D . 
L 5 HOH 11 411 55  HOH HOH D . 
L 5 HOH 12 412 43  HOH HOH D . 
L 5 HOH 13 413 1   HOH HOH D . 
L 5 HOH 14 414 10  HOH HOH D . 
L 5 HOH 15 415 50  HOH HOH D . 
L 5 HOH 16 416 57  HOH HOH D . 
L 5 HOH 17 417 25  HOH HOH D . 
L 5 HOH 18 418 118 HOH HOH D . 
L 5 HOH 19 419 24  HOH HOH D . 
L 5 HOH 20 420 40  HOH HOH D . 
L 5 HOH 21 421 13  HOH HOH D . 
L 5 HOH 22 422 116 HOH HOH D . 
L 5 HOH 23 423 70  HOH HOH D . 
L 5 HOH 24 424 23  HOH HOH D . 
L 5 HOH 25 425 78  HOH HOH D . 
L 5 HOH 26 426 8   HOH HOH D . 
L 5 HOH 27 427 11  HOH HOH D . 
L 5 HOH 28 428 32  HOH HOH D . 
L 5 HOH 29 429 35  HOH HOH D . 
L 5 HOH 30 430 79  HOH HOH D . 
L 5 HOH 31 431 62  HOH HOH D . 
L 5 HOH 32 432 20  HOH HOH D . 
L 5 HOH 33 433 114 HOH HOH D . 
L 5 HOH 34 434 16  HOH HOH D . 
L 5 HOH 35 435 38  HOH HOH D . 
L 5 HOH 36 436 4   HOH HOH D . 
L 5 HOH 37 437 22  HOH HOH D . 
L 5 HOH 38 438 83  HOH HOH D . 
L 5 HOH 39 439 7   HOH HOH D . 
L 5 HOH 40 440 119 HOH HOH D . 
L 5 HOH 41 441 65  HOH HOH D . 
L 5 HOH 42 442 53  HOH HOH D . 
L 5 HOH 43 443 75  HOH HOH D . 
L 5 HOH 44 444 82  HOH HOH D . 
L 5 HOH 45 445 61  HOH HOH D . 
L 5 HOH 46 446 36  HOH HOH D . 
L 5 HOH 47 447 80  HOH HOH D . 
L 5 HOH 48 448 105 HOH HOH D . 
L 5 HOH 49 449 94  HOH HOH D . 
L 5 HOH 50 450 68  HOH HOH D . 
L 5 HOH 51 451 51  HOH HOH D . 
L 5 HOH 52 452 86  HOH HOH D . 
L 5 HOH 53 453 93  HOH HOH D . 
L 5 HOH 54 454 101 HOH HOH D . 
L 5 HOH 55 455 89  HOH HOH D . 
L 5 HOH 56 456 107 HOH HOH D . 
L 5 HOH 57 457 58  HOH HOH D . 
L 5 HOH 58 458 39  HOH HOH D . 
L 5 HOH 59 459 66  HOH HOH D . 
L 5 HOH 60 460 102 HOH HOH D . 
L 5 HOH 61 461 115 HOH HOH D . 
L 5 HOH 62 462 26  HOH HOH D . 
L 5 HOH 63 463 92  HOH HOH D . 
L 5 HOH 64 464 103 HOH HOH D . 
L 5 HOH 65 465 97  HOH HOH D . 
L 5 HOH 66 466 104 HOH HOH D . 
L 5 HOH 67 467 90  HOH HOH D . 
L 5 HOH 68 468 6   HOH HOH D . 
L 5 HOH 69 469 110 HOH HOH D . 
L 5 HOH 70 470 98  HOH HOH D . 
L 5 HOH 71 471 111 HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21rc1_5127 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .            2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .            4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   113.77 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9C50 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     131.150 
_cell.length_a_esd                 ? 
_cell.length_b                     76.732 
_cell.length_b_esd                 ? 
_cell.length_c                     89.588 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9C50 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9C50 
_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             2.90 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.64 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M succinic acid, 15% PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     'IMAGE PLATE' 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RIGAKU RAXIS IV++' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-05-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    M 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9C50 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.49 
_reflns.d_resolution_low                               50.00 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     27672 
_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                           96.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.900 
_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                                0.122 
_reflns.pdbx_Rpim_I_all                                0.068 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       75189 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.101 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.49 2.53  ? ? ? ? ? ? 1366 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.793 ? ? 0.822 0.462 ? 1  1 0.713 0.912 ? 95.6 ? 0.677 ? ? ? ? ? ? ? ? ? 
2.53 2.58  ? ? ? ? ? ? 1337 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.782 ? ? 0.713 0.401 ? 2  1 0.765 0.931 ? 94.3 ? 0.586 ? ? ? ? ? ? ? ? ? 
2.58 2.63  ? ? ? ? ? ? 1377 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.801 ? ? 0.708 0.397 ? 3  1 0.775 0.935 ? 95.6 ? 0.583 ? ? ? ? ? ? ? ? ? 
2.63 2.68  ? ? ? ? ? ? 1348 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.977 ? ? 0.597 0.334 ? 4  1 0.812 0.947 ? 95.4 ? 0.492 ? ? ? ? ? ? ? ? ? 
2.68 2.74  ? ? ? ? ? ? 1370 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.869 ? ? 0.561 0.316 ? 5  1 0.846 0.957 ? 95.3 ? 0.462 ? ? ? ? ? ? ? ? ? 
2.74 2.80  ? ? ? ? ? ? 1354 ? ? ? ? ? ? ? ? ? ? ? 2.8 0.824 ? ? 0.444 0.247 ? 6  1 0.884 0.969 ? 95.6 ? 0.368 ? ? ? ? ? ? ? ? ? 
2.80 2.87  ? ? ? ? ? ? 1373 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.865 ? ? 0.418 0.233 ? 7  1 0.902 0.974 ? 95.9 ? 0.345 ? ? ? ? ? ? ? ? ? 
2.87 2.95  ? ? ? ? ? ? 1375 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.858 ? ? 0.347 0.194 ? 8  1 0.923 0.980 ? 96.5 ? 0.286 ? ? ? ? ? ? ? ? ? 
2.95 3.04  ? ? ? ? ? ? 1375 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.854 ? ? 0.299 0.166 ? 9  1 0.946 0.986 ? 96.2 ? 0.247 ? ? ? ? ? ? ? ? ? 
3.04 3.14  ? ? ? ? ? ? 1363 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.856 ? ? 0.263 0.146 ? 10 1 0.964 0.991 ? 96.3 ? 0.218 ? ? ? ? ? ? ? ? ? 
3.14 3.25  ? ? ? ? ? ? 1386 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.953 ? ? 0.215 0.119 ? 11 1 0.971 0.993 ? 96.8 ? 0.178 ? ? ? ? ? ? ? ? ? 
3.25 3.38  ? ? ? ? ? ? 1385 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.942 ? ? 0.166 0.092 ? 12 1 0.975 0.994 ? 96.9 ? 0.137 ? ? ? ? ? ? ? ? ? 
3.38 3.53  ? ? ? ? ? ? 1388 ? ? ? ? ? ? ? ? ? ? ? 2.7 1.219 ? ? 0.141 0.078 ? 13 1 0.980 0.995 ? 96.9 ? 0.117 ? ? ? ? ? ? ? ? ? 
3.53 3.72  ? ? ? ? ? ? 1380 ? ? ? ? ? ? ? ? ? ? ? 2.7 1.400 ? ? 0.114 0.063 ? 14 1 0.982 0.995 ? 97.0 ? 0.094 ? ? ? ? ? ? ? ? ? 
3.72 3.95  ? ? ? ? ? ? 1428 ? ? ? ? ? ? ? ? ? ? ? 2.7 1.273 ? ? 0.093 0.052 ? 15 1 0.990 0.997 ? 98.0 ? 0.077 ? ? ? ? ? ? ? ? ? 
3.95 4.26  ? ? ? ? ? ? 1411 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.955 ? ? 0.066 0.037 ? 16 1 0.996 0.999 ? 97.7 ? 0.055 ? ? ? ? ? ? ? ? ? 
4.26 4.69  ? ? ? ? ? ? 1420 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.805 ? ? 0.049 0.028 ? 17 1 0.996 0.999 ? 98.3 ? 0.041 ? ? ? ? ? ? ? ? ? 
4.69 5.36  ? ? ? ? ? ? 1409 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.744 ? ? 0.046 0.026 ? 18 1 0.997 0.999 ? 98.0 ? 0.038 ? ? ? ? ? ? ? ? ? 
5.36 6.75  ? ? ? ? ? ? 1422 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.681 ? ? 0.051 0.029 ? 19 1 0.995 0.999 ? 97.7 ? 0.042 ? ? ? ? ? ? ? ? ? 
6.75 50.00 ? ? ? ? ? ? 1405 ? ? ? ? ? ? ? ? ? ? ? 2.7 0.548 ? ? 0.032 0.018 ? 20 1 0.998 1.000 ? 94.0 ? 0.026 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9C50 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.50 
_refine.ls_d_res_low                             30.85 
_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                     25437 
_refine.ls_number_reflns_R_free                  1292 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    89.85 
_refine.ls_percent_reflns_R_free                 5.08 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1929 
_refine.ls_R_factor_R_free                       0.2454 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1901 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.72 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.35 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.50 
_refine_hist.d_res_low                        30.85 
_refine_hist.number_atoms_solvent             122 
_refine_hist.number_atoms_total               4744 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4560 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         62 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  ? 4733 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.183  ? 6387 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.030 ? 645  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.064  ? 664  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.013  ? 820  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.50 2.60  . . 86  1650 56.00 . . . . 0.2494 . . . . . . . . . . . 0.3806 
'X-RAY DIFFRACTION' 2.60 2.72  . . 137 2368 79.00 . . . . 0.2464 . . . . . . . . . . . 0.2933 
'X-RAY DIFFRACTION' 2.72 2.86  . . 151 2686 92.00 . . . . 0.2447 . . . . . . . . . . . 0.3138 
'X-RAY DIFFRACTION' 2.86 3.04  . . 158 2847 96.00 . . . . 0.2503 . . . . . . . . . . . 0.3056 
'X-RAY DIFFRACTION' 3.04 3.28  . . 156 2881 96.00 . . . . 0.2340 . . . . . . . . . . . 0.3196 
'X-RAY DIFFRACTION' 3.28 3.60  . . 141 2900 97.00 . . . . 0.2010 . . . . . . . . . . . 0.2545 
'X-RAY DIFFRACTION' 3.60 4.12  . . 172 2902 98.00 . . . . 0.1754 . . . . . . . . . . . 0.2210 
'X-RAY DIFFRACTION' 4.13 5.19  . . 160 2929 98.00 . . . . 0.1370 . . . . . . . . . . . 0.1803 
'X-RAY DIFFRACTION' 5.19 30.85 . . 131 2982 96.00 . . . . 0.1688 . . . . . . . . . . . 0.2151 
# 
_struct.entry_id                     9C50 
_struct.title                        'Replacement of a single residue changes the primary specificity of thrombin' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9C50 
_struct_keywords.text            'coagulation, Thrombin, BLOOD CLOTTING' 
_struct_keywords.pdbx_keywords   'BLOOD CLOTTING' 
# 
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 2 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
K N N 5 ? 
L N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP THRB_HUMAN P00734 ? 1 TFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR 328 
2 UNP THRB_HUMAN P00734 ? 2 
;IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISM
LEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVL
QVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFY
THVFRLKKWIQKVIDQFGE
;
364 
3 PDB 9C50       9C50   ? 3 ? 1   
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9C50 A 1 ? 36  ? P00734 328 ? 363 ? -5 17  
2 2 9C50 B 1 ? 259 ? P00734 364 ? 622 ? 16 247 
3 1 9C50 C 1 ? 36  ? P00734 328 ? 363 ? -5 17  
4 2 9C50 D 1 ? 259 ? P00734 364 ? 622 ? 16 247 
5 3 9C50 E 1 ? 3   ? 9C50   1   ? 3   ? 1  3   
6 3 9C50 F 1 ? 3   ? 9C50   1   ? 3   ? 1  3   
# 
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 
2 9C50 TYR B 260 ? UNP P00734 ? ? 'expression tag' 248 1  
2 9C50 LEU B 261 ? UNP P00734 ? ? 'expression tag' 249 2  
2 9C50 GLU B 262 ? UNP P00734 ? ? 'expression tag' 250 3  
2 9C50 ASP B 263 ? UNP P00734 ? ? 'expression tag' 251 4  
2 9C50 GLN B 264 ? UNP P00734 ? ? 'expression tag' 252 5  
2 9C50 VAL B 265 ? UNP P00734 ? ? 'expression tag' 253 6  
2 9C50 ASP B 266 ? UNP P00734 ? ? 'expression tag' 254 7  
2 9C50 PRO B 267 ? UNP P00734 ? ? 'expression tag' 255 8  
2 9C50 ARG B 268 ? UNP P00734 ? ? 'expression tag' 256 9  
2 9C50 LEU B 269 ? UNP P00734 ? ? 'expression tag' 257 10 
2 9C50 ILE B 270 ? UNP P00734 ? ? 'expression tag' 258 11 
2 9C50 ASP B 271 ? UNP P00734 ? ? 'expression tag' 259 12 
2 9C50 GLY B 272 ? UNP P00734 ? ? 'expression tag' 260 13 
2 9C50 LYS B 273 ? UNP P00734 ? ? 'expression tag' 261 14 
4 9C50 TYR D 260 ? UNP P00734 ? ? 'expression tag' 248 15 
4 9C50 LEU D 261 ? UNP P00734 ? ? 'expression tag' 249 16 
4 9C50 GLU D 262 ? UNP P00734 ? ? 'expression tag' 250 17 
4 9C50 ASP D 263 ? UNP P00734 ? ? 'expression tag' 251 18 
4 9C50 GLN D 264 ? UNP P00734 ? ? 'expression tag' 252 19 
4 9C50 VAL D 265 ? UNP P00734 ? ? 'expression tag' 253 20 
4 9C50 ASP D 266 ? UNP P00734 ? ? 'expression tag' 254 21 
4 9C50 PRO D 267 ? UNP P00734 ? ? 'expression tag' 255 22 
4 9C50 ARG D 268 ? UNP P00734 ? ? 'expression tag' 256 23 
4 9C50 LEU D 269 ? UNP P00734 ? ? 'expression tag' 257 24 
4 9C50 ILE D 270 ? UNP P00734 ? ? 'expression tag' 258 25 
4 9C50 ASP D 271 ? UNP P00734 ? ? 'expression tag' 259 26 
4 9C50 GLY D 272 ? UNP P00734 ? ? 'expression tag' 260 27 
4 9C50 LYS D 273 ? UNP P00734 ? ? 'expression tag' 261 28 
# 
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 ? trimeric 3 
2 author_defined_assembly ? trimeric 3 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,G,I,J 
2 1 C,D,F,H,K,L 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PHE A 15  ? SER A 19  ? PHE A 7   SER A 11  5 ? 5  
HELX_P HELX_P2  AA2 THR A 24  B TYR A 32  J THR A 14  TYR A 14  1 ? 9  
HELX_P HELX_P3  AA3 ALA B 41  ? CYS B 44  ? ALA B 55  CYS B 58  5 ? 4  
HELX_P HELX_P4  AA4 PRO B 48  B ASP B 51  E PRO B 60  ASP B 60  5 ? 4  
HELX_P HELX_P5  AA5 THR B 55  I ASN B 57  ? THR B 60  ASN B 62  5 ? 3  
HELX_P HELX_P6  AA6 ASP B 122 ? LEU B 130 ? ASP B 125 LEU B 130 1 ? 9  
HELX_P HELX_P7  AA7 GLU B 169 ? THR B 177 ? GLU B 164 THR B 172 1 ? 9  
HELX_P HELX_P8  AA8 LYS B 191 ? GLY B 195 C LYS B 185 GLY B 186 5 ? 5  
HELX_P HELX_P9  AA9 LEU B 246 ? PHE B 257 ? LEU B 234 PHE B 245 1 ? 12 
HELX_P HELX_P10 AB1 PHE C 15  ? SER C 19  ? PHE C 7   SER C 11  5 ? 5  
HELX_P HELX_P11 AB2 THR C 24  B TYR C 32  J THR C 14  TYR C 14  1 ? 9  
HELX_P HELX_P12 AB3 ALA D 41  ? CYS D 44  ? ALA D 55  CYS D 58  5 ? 4  
HELX_P HELX_P13 AB4 PRO D 48  B ASP D 51  E PRO D 60  ASP D 60  5 ? 4  
HELX_P HELX_P14 AB5 THR D 55  I ASN D 57  ? THR D 60  ASN D 62  5 ? 3  
HELX_P HELX_P15 AB6 ASP D 122 ? LEU D 130 ? ASP D 125 LEU D 130 1 ? 9  
HELX_P HELX_P16 AB7 GLU D 169 ? SER D 176 ? GLU D 164 SER D 171 1 ? 8  
HELX_P HELX_P17 AB8 LYS D 191 ? GLY D 195 C LYS D 185 GLY D 186 5 ? 5  
HELX_P HELX_P18 AB9 LEU D 246 ? GLY D 258 ? LEU D 234 GLY D 246 1 ? 13 
HELX_P HELX_P19 AC1 TYR D 260 ? GLN D 264 ? TYR D 248 GLN D 252 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 9   SG  ? ? ? 1_555 B CYS 119 SG ? ? A CYS 1   B CYS 122 1_555 ? ? ? ? ? ? ? 2.059 ? ? 
disulf2  disulf ?    ? B CYS 28  SG  ? ? ? 1_555 B CYS 44  SG ? ? B CYS 42  B CYS 58  1_555 ? ? ? ? ? ? ? 2.047 ? ? 
disulf3  disulf ?    ? B CYS 173 SG  ? ? ? 1_555 B CYS 187 SG ? ? B CYS 168 B CYS 182 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf4  disulf ?    ? B CYS 201 SG  ? ? ? 1_555 B CYS 231 SG ? ? B CYS 191 B CYS 220 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
disulf5  disulf ?    ? C CYS 9   SG  ? ? ? 1_555 D CYS 119 SG ? ? C CYS 1   D CYS 122 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
disulf6  disulf ?    ? D CYS 28  SG  ? ? ? 1_555 D CYS 44  SG ? ? D CYS 42  D CYS 58  1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf7  disulf ?    ? D CYS 173 SG  ? ? ? 1_555 D CYS 187 SG ? ? D CYS 168 D CYS 182 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
disulf8  disulf ?    ? D CYS 201 SG  ? ? ? 1_555 D CYS 231 SG ? ? D CYS 191 D CYS 220 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
covale1  covale one  ? B HIS 43  NE2 ? ? ? 1_555 E PCS 3   CT ? ? B HIS 57  E PCS 3   1_555 ? ? ? ? ? ? ? 1.308 ? ? 
covale2  covale one  ? D HIS 43  NE2 ? ? ? 1_555 F PCS 3   CT ? ? D HIS 57  F PCS 3   1_555 ? ? ? ? ? ? ? 1.438 ? ? 
covale3  covale both ? E PRO 2   C   ? ? ? 1_555 E PCS 3   N  ? ? E PRO 2   E PCS 3   1_555 ? ? ? ? ? ? ? 1.464 ? ? 
covale4  covale both ? F PRO 2   C   ? ? ? 1_555 F PCS 3   N  ? ? F PRO 2   F PCS 3   1_555 ? ? ? ? ? ? ? 1.464 ? ? 
metalc1  metalc ?    ? B ARG 233 O   ? A ? 1_555 G NA  .   NA ? ? B ARG 221 B NA  301 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc2  metalc ?    ? B LYS 236 O   ? ? ? 1_555 G NA  .   NA ? ? B LYS 224 B NA  301 1_555 ? ? ? ? ? ? ? 2.269 ? ? 
metalc3  metalc ?    ? G NA  .   NA  ? ? ? 1_555 J HOH .   O  ? ? B NA  301 B HOH 413 1_555 ? ? ? ? ? ? ? 3.125 ? ? 
metalc4  metalc ?    ? G NA  .   NA  ? ? ? 1_555 J HOH .   O  ? ? B NA  301 B HOH 421 1_555 ? ? ? ? ? ? ? 2.598 ? ? 
metalc5  metalc ?    ? G NA  .   NA  ? ? ? 1_555 J HOH .   O  ? ? B NA  301 B HOH 423 1_555 ? ? ? ? ? ? ? 2.558 ? ? 
metalc6  metalc ?    ? G NA  .   NA  ? ? ? 1_555 J HOH .   O  ? ? B NA  301 B HOH 427 1_555 ? ? ? ? ? ? ? 2.437 ? ? 
metalc7  metalc ?    ? D ARG 233 O   ? A ? 1_555 H NA  .   NA ? ? D ARG 221 D NA  301 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc8  metalc ?    ? D LYS 236 O   ? ? ? 1_555 H NA  .   NA ? ? D LYS 224 D NA  301 1_555 ? ? ? ? ? ? ? 2.282 ? ? 
metalc9  metalc ?    ? H NA  .   NA  ? ? ? 1_555 L HOH .   O  ? ? D NA  301 D HOH 406 1_555 ? ? ? ? ? ? ? 2.285 ? ? 
metalc10 metalc ?    ? H NA  .   NA  ? ? ? 1_555 L HOH .   O  ? ? D NA  301 D HOH 416 1_555 ? ? ? ? ? ? ? 2.840 ? ? 
metalc11 metalc ?    ? H NA  .   NA  ? ? ? 1_555 L HOH .   O  ? ? D NA  301 D HOH 451 1_555 ? ? ? ? ? ? ? 2.266 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O ? B ARG 233 ? B ARG 221 A 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? B LYS 236 ? B LYS 224 ? 1_555 97.8  ? 
2  O ? B ARG 233 ? B ARG 221 A 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? J HOH .   ? B HOH 413 ? 1_555 89.2  ? 
3  O ? B LYS 236 ? B LYS 224 ? 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? J HOH .   ? B HOH 413 ? 1_555 103.9 ? 
4  O ? B ARG 233 ? B ARG 221 A 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? J HOH .   ? B HOH 421 ? 1_555 158.6 ? 
5  O ? B LYS 236 ? B LYS 224 ? 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? J HOH .   ? B HOH 421 ? 1_555 67.3  ? 
6  O ? J HOH .   ? B HOH 413 ? 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? J HOH .   ? B HOH 421 ? 1_555 80.2  ? 
7  O ? B ARG 233 ? B ARG 221 A 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? J HOH .   ? B HOH 423 ? 1_555 111.8 ? 
8  O ? B LYS 236 ? B LYS 224 ? 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? J HOH .   ? B HOH 423 ? 1_555 149.6 ? 
9  O ? J HOH .   ? B HOH 413 ? 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? J HOH .   ? B HOH 423 ? 1_555 70.6  ? 
10 O ? J HOH .   ? B HOH 421 ? 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? J HOH .   ? B HOH 423 ? 1_555 82.3  ? 
11 O ? B ARG 233 ? B ARG 221 A 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? J HOH .   ? B HOH 427 ? 1_555 100.7 ? 
12 O ? B LYS 236 ? B LYS 224 ? 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? J HOH .   ? B HOH 427 ? 1_555 90.2  ? 
13 O ? J HOH .   ? B HOH 413 ? 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? J HOH .   ? B HOH 427 ? 1_555 161.6 ? 
14 O ? J HOH .   ? B HOH 421 ? 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? J HOH .   ? B HOH 427 ? 1_555 94.8  ? 
15 O ? J HOH .   ? B HOH 423 ? 1_555 NA ? G NA . ? B NA 301 ? 1_555 O ? J HOH .   ? B HOH 427 ? 1_555 91.2  ? 
16 O ? D ARG 233 ? D ARG 221 A 1_555 NA ? H NA . ? D NA 301 ? 1_555 O ? D LYS 236 ? D LYS 224 ? 1_555 95.6  ? 
17 O ? D ARG 233 ? D ARG 221 A 1_555 NA ? H NA . ? D NA 301 ? 1_555 O ? L HOH .   ? D HOH 406 ? 1_555 100.1 ? 
18 O ? D LYS 236 ? D LYS 224 ? 1_555 NA ? H NA . ? D NA 301 ? 1_555 O ? L HOH .   ? D HOH 406 ? 1_555 113.2 ? 
19 O ? D ARG 233 ? D ARG 221 A 1_555 NA ? H NA . ? D NA 301 ? 1_555 O ? L HOH .   ? D HOH 416 ? 1_555 92.8  ? 
20 O ? D LYS 236 ? D LYS 224 ? 1_555 NA ? H NA . ? D NA 301 ? 1_555 O ? L HOH .   ? D HOH 416 ? 1_555 145.3 ? 
21 O ? L HOH .   ? D HOH 406 ? 1_555 NA ? H NA . ? D NA 301 ? 1_555 O ? L HOH .   ? D HOH 416 ? 1_555 98.2  ? 
22 O ? D ARG 233 ? D ARG 221 A 1_555 NA ? H NA . ? D NA 301 ? 1_555 O ? L HOH .   ? D HOH 451 ? 1_555 143.0 ? 
23 O ? D LYS 236 ? D LYS 224 ? 1_555 NA ? H NA . ? D NA 301 ? 1_555 O ? L HOH .   ? D HOH 451 ? 1_555 80.9  ? 
24 O ? L HOH .   ? D HOH 406 ? 1_555 NA ? H NA . ? D NA 301 ? 1_555 O ? L HOH .   ? D HOH 451 ? 1_555 115.2 ? 
25 O ? L HOH .   ? D HOH 416 ? 1_555 NA ? H NA . ? D NA 301 ? 1_555 O ? L HOH .   ? D HOH 451 ? 1_555 72.4  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  PCS E 3   ? .   . .   . PCS E 3   ? 1_555 .   . .   . .     .   .  PHE 2 PCS None 'Non-standard residue' 
2  PCS F 3   ? .   . .   . PCS F 3   ? 1_555 .   . .   . .     .   .  PHE 2 PCS None 'Non-standard residue' 
3  CYS A 9   ? CYS B 119 ? CYS A 1   ? 1_555 CYS B 122 ? 1_555 SG  SG .   . .   None 'Disulfide bridge'     
4  CYS B 28  ? CYS B 44  ? CYS B 42  ? 1_555 CYS B 58  ? 1_555 SG  SG .   . .   None 'Disulfide bridge'     
5  CYS B 173 ? CYS B 187 ? CYS B 168 ? 1_555 CYS B 182 ? 1_555 SG  SG .   . .   None 'Disulfide bridge'     
6  CYS B 201 ? CYS B 231 ? CYS B 191 ? 1_555 CYS B 220 ? 1_555 SG  SG .   . .   None 'Disulfide bridge'     
7  CYS C 9   ? CYS D 119 ? CYS C 1   ? 1_555 CYS D 122 ? 1_555 SG  SG .   . .   None 'Disulfide bridge'     
8  CYS D 28  ? CYS D 44  ? CYS D 42  ? 1_555 CYS D 58  ? 1_555 SG  SG .   . .   None 'Disulfide bridge'     
9  CYS D 173 ? CYS D 187 ? CYS D 168 ? 1_555 CYS D 182 ? 1_555 SG  SG .   . .   None 'Disulfide bridge'     
10 CYS D 201 ? CYS D 231 ? CYS D 191 ? 1_555 CYS D 220 ? 1_555 SG  SG .   . .   None 'Disulfide bridge'     
11 HIS B 43  ? PCS E 3   ? HIS B 57  ? 1_555 PCS E 3   ? 1_555 NE2 CT .   . .   None 'Non-standard linkage' 
12 HIS D 43  ? PCS F 3   ? HIS D 57  ? 1_555 PCS F 3   ? 1_555 NE2 CT .   . .   None 'Non-standard linkage' 
13 PRO E 2   ? PCS E 3   ? PRO E 2   ? 1_555 PCS E 3   ? 1_555 C   N  .   . .   None 'Non-standard linkage' 
14 PRO F 2   ? PCS F 3   ? PRO F 2   ? 1_555 PCS F 3   ? 1_555 C   N  .   . .   None 'Non-standard linkage' 
# 
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 22 B . A SER 36 B PRO 23 B ? PRO 37 B 1 -10.45 
2 SER 22 D . A SER 36 D PRO 23 D ? PRO 37 D 1 -5.30  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 7 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER B 5   ? ASP B 6   ? SER B 20  ASP B 21  
AA1 2 GLN B 161 ? PRO B 166 ? GLN B 156 PRO B 161 
AA1 3 LYS B 135 ? GLY B 140 ? LYS B 135 GLY B 140 
AA1 4 PRO B 208 ? LYS B 212 ? PRO B 198 LYS B 202 
AA1 5 TRP B 219 ? TRP B 227 ? TRP B 207 TRP B 215 
AA1 6 GLY B 238 ? HIS B 242 ? GLY B 226 HIS B 230 
AA1 7 MET B 185 ? ALA B 188 ? MET B 180 ALA B 183 
AA2 1 GLN B 15  ? ARG B 20  ? GLN B 30  ARG B 35  
AA2 2 GLU B 25  ? LEU B 32  ? GLU B 39  LEU B 46  
AA2 3 TRP B 37  ? THR B 40  ? TRP B 51  THR B 54  
AA2 4 ALA B 101 ? LEU B 105 ? ALA B 104 LEU B 108 
AA2 5 LYS B 77  ? ILE B 86  ? LYS B 81  ILE B 90  
AA2 6 LEU B 59  ? ILE B 63  ? LEU B 64  ILE B 68  
AA2 7 GLN B 15  ? ARG B 20  ? GLN B 30  ARG B 35  
AA3 1 LEU B 46  ? TYR B 47  A LEU B 60  TYR B 60  
AA3 2 LYS B 52  F ASN B 53  G LYS B 60  ASN B 60  
AA4 1 SER D 5   ? ASP D 6   ? SER D 20  ASP D 21  
AA4 2 GLN D 161 ? PRO D 166 ? GLN D 156 PRO D 161 
AA4 3 LYS D 135 ? GLY D 140 ? LYS D 135 GLY D 140 
AA4 4 PRO D 208 ? LYS D 212 ? PRO D 198 LYS D 202 
AA4 5 TRP D 219 ? TRP D 227 ? TRP D 207 TRP D 215 
AA4 6 GLY D 238 ? HIS D 242 ? GLY D 226 HIS D 230 
AA4 7 MET D 185 ? ALA D 188 ? MET D 180 ALA D 183 
AA5 1 LYS D 77  ? SER D 79  ? LYS D 81  SER D 83  
AA5 2 LEU D 59  ? ILE D 63  ? LEU D 64  ILE D 68  
AA5 3 GLN D 15  ? ARG D 20  ? GLN D 30  ARG D 35  
AA5 4 GLU D 25  ? LEU D 32  ? GLU D 39  LEU D 46  
AA5 5 TRP D 37  ? THR D 40  ? TRP D 51  THR D 54  
AA5 6 ALA D 101 ? LEU D 105 ? ALA D 104 LEU D 108 
AA5 7 LEU D 81  ? ILE D 86  ? LEU D 85  ILE D 90  
AA6 1 LEU D 46  ? TYR D 47  A LEU D 60  TYR D 60  
AA6 2 LYS D 52  F ASN D 53  G LYS D 60  ASN D 60  
# 
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 SER B 5   ? N SER B 20  O VAL B 162 ? O VAL B 157 
AA1 2 3 O LEU B 165 ? O LEU B 160 N GLY B 136 ? N GLY B 136 
AA1 3 4 N ARG B 137 ? N ARG B 137 O VAL B 210 ? O VAL B 200 
AA1 4 5 N MET B 211 ? N MET B 201 O TYR B 220 ? O TYR B 208 
AA1 5 6 N ILE B 224 ? N ILE B 212 O THR B 241 ? O THR B 229 
AA1 6 7 O TYR B 240 ? O TYR B 228 N PHE B 186 ? N PHE B 181 
AA2 1 2 N LEU B 18  ? N LEU B 33  O LEU B 27  ? O LEU B 41  
AA2 2 3 N SER B 31  ? N SER B 45  O LEU B 39  ? O LEU B 53  
AA2 3 4 N VAL B 38  ? N VAL B 52  O MET B 103 ? O MET B 106 
AA2 4 5 O LYS B 104 ? O LYS B 107 N GLU B 82  ? N GLU B 86  
AA2 5 6 O LYS B 77  ? O LYS B 81  N ILE B 63  ? N ILE B 68  
AA2 6 7 O LEU B 60  ? O LEU B 65  N PHE B 19  ? N PHE B 34  
AA3 1 2 N TYR B 47  A N TYR B 60  O LYS B 52  F O LYS B 60  
AA4 1 2 N SER D 5   ? N SER D 20  O VAL D 162 ? O VAL D 157 
AA4 2 3 O VAL D 163 ? O VAL D 158 N VAL D 138 ? N VAL D 138 
AA4 3 4 N ARG D 137 ? N ARG D 137 O VAL D 210 ? O VAL D 200 
AA4 4 5 N MET D 211 ? N MET D 201 O TYR D 220 ? O TYR D 208 
AA4 5 6 N ILE D 224 ? N ILE D 212 O THR D 241 ? O THR D 229 
AA4 6 7 O TYR D 240 ? O TYR D 228 N PHE D 186 ? N PHE D 181 
AA5 1 2 O SER D 79  ? O SER D 83  N VAL D 61  ? N VAL D 66  
AA5 2 3 O LEU D 60  ? O LEU D 65  N PHE D 19  ? N PHE D 34  
AA5 3 4 N LEU D 18  ? N LEU D 33  O LEU D 27  ? O LEU D 41  
AA5 4 5 N SER D 31  ? N SER D 45  O LEU D 39  ? O LEU D 53  
AA5 5 6 N VAL D 38  ? N VAL D 52  O MET D 103 ? O MET D 106 
AA5 6 7 O LYS D 104 ? O LYS D 107 N GLU D 82  ? N GLU D 86  
AA6 1 2 N TYR D 47  A N TYR D 60  O LYS D 52  F O LYS D 60  
# 
_pdbx_entry_details.entry_id                   9C50 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OG  D SER 195 ? ? C  F PCS 3   ? ? 1.38 
2  1 OG  B SER 195 ? ? C  E PCS 3   ? ? 1.48 
3  1 OG  D SER 195 ? ? O  F PCS 3   ? ? 1.88 
4  1 OG  D SER 195 ? ? CT F PCS 3   ? ? 1.98 
5  1 NZ  D LYS 185 ? ? O  D HOH 401 ? ? 1.99 
6  1 OG  B SER 195 ? ? O  E PCS 3   ? ? 2.00 
7  1 OG  B SER 195 ? ? CT E PCS 3   ? ? 2.11 
8  1 O   B HOH 406 ? ? O  B HOH 413 ? ? 2.13 
9  1 OG  B SER 195 ? ? CA E PCS 3   ? ? 2.16 
10 1 OE1 B GLU 80  ? ? O  B HOH 401 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NZ 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    LYS 
_pdbx_validate_symm_contact.auth_seq_id_1     14 
_pdbx_validate_symm_contact.PDB_ins_code_1    A 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    GLU 
_pdbx_validate_symm_contact.auth_seq_id_2     97 
_pdbx_validate_symm_contact.PDB_ins_code_2    A 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_555 
_pdbx_validate_symm_contact.dist              1.93 
# 
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 C  E PHE 1 ? ? N  E PRO 2 ? ? 1.513 1.338 0.175  0.019 Y 
2 1 N  E PRO 2 ? ? CA E PRO 2 ? ? 1.629 1.468 0.161  0.017 N 
3 1 CA E PRO 2 ? ? CB E PRO 2 ? ? 1.362 1.531 -0.169 0.020 N 
4 1 CD E PRO 2 ? ? N  E PRO 2 ? ? 1.341 1.474 -0.133 0.014 N 
5 1 C  F PHE 1 ? ? N  F PRO 2 ? ? 1.513 1.338 0.175  0.019 Y 
6 1 N  F PRO 2 ? ? CA F PRO 2 ? ? 1.629 1.468 0.161  0.017 N 
7 1 CA F PRO 2 ? ? CB F PRO 2 ? ? 1.361 1.531 -0.170 0.020 N 
8 1 CD F PRO 2 ? ? N  F PRO 2 ? ? 1.341 1.474 -0.133 0.014 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PHE A 7   ? ? -131.12 -74.65 
2  1 TYR B 60  A ? -153.27 82.83  
3  1 ASN B 60  G ? -154.62 73.90  
4  1 HIS B 71  ? ? -120.04 -57.56 
5  1 THR B 74  ? ? -100.92 -64.95 
6  1 ILE B 79  ? ? -103.55 -60.95 
7  1 GLU B 97  A ? -111.38 -71.93 
8  1 ASN B 98  ? ? -148.28 18.12  
9  1 SER B 214 ? ? -123.12 -56.68 
10 1 PHE C 7   ? ? -132.73 -75.53 
11 1 ASN D 60  G ? -151.27 75.98  
12 1 THR D 74  ? ? -99.57  -63.26 
13 1 ILE D 79  ? ? -101.81 -64.46 
14 1 GLU D 97  A ? -96.70  -75.52 
15 1 ASN D 98  ? ? -145.00 18.45  
16 1 SER D 214 ? ? -124.51 -57.47 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     50 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.154 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 THR -5  ? A THR 1   
2  1 Y 1 A PHE -4  ? A PHE 2   
3  1 Y 1 A GLY -3  ? A GLY 3   
4  1 Y 1 A SER -2  ? A SER 4   
5  1 Y 1 A GLY -1  ? A GLY 5   
6  1 Y 1 A GLU 0   ? A GLU 6   
7  1 Y 1 A ASP 15  ? A ASP 34  
8  1 Y 1 A GLY 16  ? A GLY 35  
9  1 Y 1 A ARG 17  ? A ARG 36  
10 1 Y 1 B TRP 147 A B TRP 148 
11 1 Y 1 B THR 147 B B THR 149 
12 1 Y 1 B ALA 147 C B ALA 150 
13 1 Y 1 B ASN 147 D B ASN 151 
14 1 Y 1 B VAL 147 E B VAL 152 
15 1 Y 1 B GLY 147 F B GLY 153 
16 1 Y 1 B LYS 147 G B LYS 154 
17 1 Y 1 B GLY 246 ? B GLY 258 
18 1 Y 1 B GLU 247 ? B GLU 259 
19 1 Y 1 B TYR 248 ? B TYR 260 
20 1 Y 1 B LEU 249 ? B LEU 261 
21 1 Y 1 B GLU 250 ? B GLU 262 
22 1 Y 1 B ASP 251 ? B ASP 263 
23 1 Y 1 B GLN 252 ? B GLN 264 
24 1 Y 1 B VAL 253 ? B VAL 265 
25 1 Y 1 B ASP 254 ? B ASP 266 
26 1 Y 1 B PRO 255 ? B PRO 267 
27 1 Y 1 B ARG 256 ? B ARG 268 
28 1 Y 1 B LEU 257 ? B LEU 269 
29 1 Y 1 B ILE 258 ? B ILE 270 
30 1 Y 1 B ASP 259 ? B ASP 271 
31 1 Y 1 B GLY 260 ? B GLY 272 
32 1 Y 1 B LYS 261 ? B LYS 273 
33 1 Y 1 C THR -5  ? C THR 1   
34 1 Y 1 C PHE -4  ? C PHE 2   
35 1 Y 1 C GLY -3  ? C GLY 3   
36 1 Y 1 C SER -2  ? C SER 4   
37 1 Y 1 C GLY -1  ? C GLY 5   
38 1 Y 1 C GLU 0   ? C GLU 6   
39 1 Y 1 C ASP 15  ? C ASP 34  
40 1 Y 1 C GLY 16  ? C GLY 35  
41 1 Y 1 C ARG 17  ? C ARG 36  
42 1 Y 1 D TRP 147 A D TRP 148 
43 1 Y 1 D THR 147 B D THR 149 
44 1 Y 1 D ALA 147 C D ALA 150 
45 1 Y 1 D ASN 147 D D ASN 151 
46 1 Y 1 D VAL 147 E D VAL 152 
47 1 Y 1 D GLY 147 F D GLY 153 
48 1 Y 1 D LYS 147 G D LYS 154 
49 1 Y 1 D ASP 254 ? D ASP 266 
50 1 Y 1 D PRO 255 ? D PRO 267 
51 1 Y 1 D ARG 256 ? D ARG 268 
52 1 Y 1 D LEU 257 ? D LEU 269 
53 1 Y 1 D ILE 258 ? D ILE 270 
54 1 Y 1 D ASP 259 ? D ASP 271 
55 1 Y 1 D GLY 260 ? D GLY 272 
56 1 Y 1 D LYS 261 ? D LYS 273 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
NA  NA   NA N N 250 
PCS N    N  N N 251 
PCS CA   C  N S 252 
PCS C    C  N N 253 
PCS CB   C  N N 254 
PCS O    O  N N 255 
PCS CD1  C  Y N 256 
PCS CG   C  Y N 257 
PCS CD2  C  Y N 258 
PCS CE2  C  Y N 259 
PCS CZ   C  Y N 260 
PCS CE1  C  Y N 261 
PCS CT   C  N N 262 
PCS CL1  CL N N 263 
PCS H    H  N N 264 
PCS H2   H  N N 265 
PCS HA   H  N N 266 
PCS HB2  H  N N 267 
PCS HB3  H  N N 268 
PCS HD1  H  N N 269 
PCS HD2  H  N N 270 
PCS HE2  H  N N 271 
PCS HZ   H  N N 272 
PCS HE1  H  N N 273 
PCS HT1  H  N N 274 
PCS HT2  H  N N 275 
PHE N    N  N N 276 
PHE CA   C  N S 277 
PHE C    C  N N 278 
PHE O    O  N N 279 
PHE CB   C  N N 280 
PHE CG   C  Y N 281 
PHE CD1  C  Y N 282 
PHE CD2  C  Y N 283 
PHE CE1  C  Y N 284 
PHE CE2  C  Y N 285 
PHE CZ   C  Y N 286 
PHE OXT  O  N N 287 
PHE H    H  N N 288 
PHE H2   H  N N 289 
PHE HA   H  N N 290 
PHE HB2  H  N N 291 
PHE HB3  H  N N 292 
PHE HD1  H  N N 293 
PHE HD2  H  N N 294 
PHE HE1  H  N N 295 
PHE HE2  H  N N 296 
PHE HZ   H  N N 297 
PHE HXT  H  N N 298 
PRO N    N  N N 299 
PRO CA   C  N S 300 
PRO C    C  N N 301 
PRO O    O  N N 302 
PRO CB   C  N N 303 
PRO CG   C  N N 304 
PRO CD   C  N N 305 
PRO OXT  O  N N 306 
PRO H    H  N N 307 
PRO HA   H  N N 308 
PRO HB2  H  N N 309 
PRO HB3  H  N N 310 
PRO HG2  H  N N 311 
PRO HG3  H  N N 312 
PRO HD2  H  N N 313 
PRO HD3  H  N N 314 
PRO HXT  H  N N 315 
SER N    N  N N 316 
SER CA   C  N S 317 
SER C    C  N N 318 
SER O    O  N N 319 
SER CB   C  N N 320 
SER OG   O  N N 321 
SER OXT  O  N N 322 
SER H    H  N N 323 
SER H2   H  N N 324 
SER HA   H  N N 325 
SER HB2  H  N N 326 
SER HB3  H  N N 327 
SER HG   H  N N 328 
SER HXT  H  N N 329 
THR N    N  N N 330 
THR CA   C  N S 331 
THR C    C  N N 332 
THR O    O  N N 333 
THR CB   C  N R 334 
THR OG1  O  N N 335 
THR CG2  C  N N 336 
THR OXT  O  N N 337 
THR H    H  N N 338 
THR H2   H  N N 339 
THR HA   H  N N 340 
THR HB   H  N N 341 
THR HG1  H  N N 342 
THR HG21 H  N N 343 
THR HG22 H  N N 344 
THR HG23 H  N N 345 
THR HXT  H  N N 346 
TRP N    N  N N 347 
TRP CA   C  N S 348 
TRP C    C  N N 349 
TRP O    O  N N 350 
TRP CB   C  N N 351 
TRP CG   C  Y N 352 
TRP CD1  C  Y N 353 
TRP CD2  C  Y N 354 
TRP NE1  N  Y N 355 
TRP CE2  C  Y N 356 
TRP CE3  C  Y N 357 
TRP CZ2  C  Y N 358 
TRP CZ3  C  Y N 359 
TRP CH2  C  Y N 360 
TRP OXT  O  N N 361 
TRP H    H  N N 362 
TRP H2   H  N N 363 
TRP HA   H  N N 364 
TRP HB2  H  N N 365 
TRP HB3  H  N N 366 
TRP HD1  H  N N 367 
TRP HE1  H  N N 368 
TRP HE3  H  N N 369 
TRP HZ2  H  N N 370 
TRP HZ3  H  N N 371 
TRP HH2  H  N N 372 
TRP HXT  H  N N 373 
TYR N    N  N N 374 
TYR CA   C  N S 375 
TYR C    C  N N 376 
TYR O    O  N N 377 
TYR CB   C  N N 378 
TYR CG   C  Y N 379 
TYR CD1  C  Y N 380 
TYR CD2  C  Y N 381 
TYR CE1  C  Y N 382 
TYR CE2  C  Y N 383 
TYR CZ   C  Y N 384 
TYR OH   O  N N 385 
TYR OXT  O  N N 386 
TYR H    H  N N 387 
TYR H2   H  N N 388 
TYR HA   H  N N 389 
TYR HB2  H  N N 390 
TYR HB3  H  N N 391 
TYR HD1  H  N N 392 
TYR HD2  H  N N 393 
TYR HE1  H  N N 394 
TYR HE2  H  N N 395 
TYR HH   H  N N 396 
TYR HXT  H  N N 397 
VAL N    N  N N 398 
VAL CA   C  N S 399 
VAL C    C  N N 400 
VAL O    O  N N 401 
VAL CB   C  N N 402 
VAL CG1  C  N N 403 
VAL CG2  C  N N 404 
VAL OXT  O  N N 405 
VAL H    H  N N 406 
VAL H2   H  N N 407 
VAL HA   H  N N 408 
VAL HB   H  N N 409 
VAL HG11 H  N N 410 
VAL HG12 H  N N 411 
VAL HG13 H  N N 412 
VAL HG21 H  N N 413 
VAL HG22 H  N N 414 
VAL HG23 H  N N 415 
VAL HXT  H  N N 416 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PCS N   CA   sing N N 237 
PCS N   H    sing N N 238 
PCS N   H2   sing N N 239 
PCS CA  C    sing N N 240 
PCS CA  CB   sing N N 241 
PCS CA  HA   sing N N 242 
PCS C   O    doub N N 243 
PCS C   CT   sing N N 244 
PCS CB  CG   sing N N 245 
PCS CB  HB2  sing N N 246 
PCS CB  HB3  sing N N 247 
PCS CD1 CG   doub Y N 248 
PCS CD1 CE1  sing Y N 249 
PCS CD1 HD1  sing N N 250 
PCS CG  CD2  sing Y N 251 
PCS CD2 CE2  doub Y N 252 
PCS CD2 HD2  sing N N 253 
PCS CE2 CZ   sing Y N 254 
PCS CE2 HE2  sing N N 255 
PCS CZ  CE1  doub Y N 256 
PCS CZ  HZ   sing N N 257 
PCS CE1 HE1  sing N N 258 
PCS CT  CL1  sing N N 259 
PCS CT  HT1  sing N N 260 
PCS CT  HT2  sing N N 261 
PHE N   CA   sing N N 262 
PHE N   H    sing N N 263 
PHE N   H2   sing N N 264 
PHE CA  C    sing N N 265 
PHE CA  CB   sing N N 266 
PHE CA  HA   sing N N 267 
PHE C   O    doub N N 268 
PHE C   OXT  sing N N 269 
PHE CB  CG   sing N N 270 
PHE CB  HB2  sing N N 271 
PHE CB  HB3  sing N N 272 
PHE CG  CD1  doub Y N 273 
PHE CG  CD2  sing Y N 274 
PHE CD1 CE1  sing Y N 275 
PHE CD1 HD1  sing N N 276 
PHE CD2 CE2  doub Y N 277 
PHE CD2 HD2  sing N N 278 
PHE CE1 CZ   doub Y N 279 
PHE CE1 HE1  sing N N 280 
PHE CE2 CZ   sing Y N 281 
PHE CE2 HE2  sing N N 282 
PHE CZ  HZ   sing N N 283 
PHE OXT HXT  sing N N 284 
PRO N   CA   sing N N 285 
PRO N   CD   sing N N 286 
PRO N   H    sing N N 287 
PRO CA  C    sing N N 288 
PRO CA  CB   sing N N 289 
PRO CA  HA   sing N N 290 
PRO C   O    doub N N 291 
PRO C   OXT  sing N N 292 
PRO CB  CG   sing N N 293 
PRO CB  HB2  sing N N 294 
PRO CB  HB3  sing N N 295 
PRO CG  CD   sing N N 296 
PRO CG  HG2  sing N N 297 
PRO CG  HG3  sing N N 298 
PRO CD  HD2  sing N N 299 
PRO CD  HD3  sing N N 300 
PRO OXT HXT  sing N N 301 
SER N   CA   sing N N 302 
SER N   H    sing N N 303 
SER N   H2   sing N N 304 
SER CA  C    sing N N 305 
SER CA  CB   sing N N 306 
SER CA  HA   sing N N 307 
SER C   O    doub N N 308 
SER C   OXT  sing N N 309 
SER CB  OG   sing N N 310 
SER CB  HB2  sing N N 311 
SER CB  HB3  sing N N 312 
SER OG  HG   sing N N 313 
SER OXT HXT  sing N N 314 
THR N   CA   sing N N 315 
THR N   H    sing N N 316 
THR N   H2   sing N N 317 
THR CA  C    sing N N 318 
THR CA  CB   sing N N 319 
THR CA  HA   sing N N 320 
THR C   O    doub N N 321 
THR C   OXT  sing N N 322 
THR CB  OG1  sing N N 323 
THR CB  CG2  sing N N 324 
THR CB  HB   sing N N 325 
THR OG1 HG1  sing N N 326 
THR CG2 HG21 sing N N 327 
THR CG2 HG22 sing N N 328 
THR CG2 HG23 sing N N 329 
THR OXT HXT  sing N N 330 
TRP N   CA   sing N N 331 
TRP N   H    sing N N 332 
TRP N   H2   sing N N 333 
TRP CA  C    sing N N 334 
TRP CA  CB   sing N N 335 
TRP CA  HA   sing N N 336 
TRP C   O    doub N N 337 
TRP C   OXT  sing N N 338 
TRP CB  CG   sing N N 339 
TRP CB  HB2  sing N N 340 
TRP CB  HB3  sing N N 341 
TRP CG  CD1  doub Y N 342 
TRP CG  CD2  sing Y N 343 
TRP CD1 NE1  sing Y N 344 
TRP CD1 HD1  sing N N 345 
TRP CD2 CE2  doub Y N 346 
TRP CD2 CE3  sing Y N 347 
TRP NE1 CE2  sing Y N 348 
TRP NE1 HE1  sing N N 349 
TRP CE2 CZ2  sing Y N 350 
TRP CE3 CZ3  doub Y N 351 
TRP CE3 HE3  sing N N 352 
TRP CZ2 CH2  doub Y N 353 
TRP CZ2 HZ2  sing N N 354 
TRP CZ3 CH2  sing Y N 355 
TRP CZ3 HZ3  sing N N 356 
TRP CH2 HH2  sing N N 357 
TRP OXT HXT  sing N N 358 
TYR N   CA   sing N N 359 
TYR N   H    sing N N 360 
TYR N   H2   sing N N 361 
TYR CA  C    sing N N 362 
TYR CA  CB   sing N N 363 
TYR CA  HA   sing N N 364 
TYR C   O    doub N N 365 
TYR C   OXT  sing N N 366 
TYR CB  CG   sing N N 367 
TYR CB  HB2  sing N N 368 
TYR CB  HB3  sing N N 369 
TYR CG  CD1  doub Y N 370 
TYR CG  CD2  sing Y N 371 
TYR CD1 CE1  sing Y N 372 
TYR CD1 HD1  sing N N 373 
TYR CD2 CE2  doub Y N 374 
TYR CD2 HD2  sing N N 375 
TYR CE1 CZ   doub Y N 376 
TYR CE1 HE1  sing N N 377 
TYR CE2 CZ   sing Y N 378 
TYR CE2 HE2  sing N N 379 
TYR CZ  OH   sing N N 380 
TYR OH  HH   sing N N 381 
TYR OXT HXT  sing N N 382 
VAL N   CA   sing N N 383 
VAL N   H    sing N N 384 
VAL N   H2   sing N N 385 
VAL CA  C    sing N N 386 
VAL CA  CB   sing N N 387 
VAL CA  HA   sing N N 388 
VAL C   O    doub N N 389 
VAL C   OXT  sing N N 390 
VAL CB  CG1  sing N N 391 
VAL CB  CG2  sing N N 392 
VAL CB  HB   sing N N 393 
VAL CG1 HG11 sing N N 394 
VAL CG1 HG12 sing N N 395 
VAL CG1 HG13 sing N N 396 
VAL CG2 HG21 sing N N 397 
VAL CG2 HG22 sing N N 398 
VAL CG2 HG23 sing N N 399 
VAL OXT HXT  sing N N 400 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)' 'United States' HL049413 1 
'National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)' 'United States' HL139554 2 
'National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)' 'United States' HL147821 3 
# 
_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   1SHH 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9C50 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.007625 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003358 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013032 
_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]   0.012196 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
NA 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 7   B 11.795  23.430  -13.146 1.00 55.52 ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 7   B 10.853  24.436  -12.677 1.00 57.54 ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 7   B 11.525  25.816  -12.543 1.00 58.13 ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 7   B 12.006  26.402  -13.517 1.00 55.05 ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 7   B 10.245  23.994  -11.342 1.00 53.11 ? 1   ALA A CB  1 
ATOM   6    N  N   . ASP A 1 8   A 11.533  26.322  -11.310 1.00 61.67 ? 1   ASP A N   1 
ATOM   7    C  CA  . ASP A 1 8   A 12.285  27.501  -10.897 1.00 58.48 ? 1   ASP A CA  1 
ATOM   8    C  C   . ASP A 1 8   A 13.690  27.125  -10.374 1.00 59.33 ? 1   ASP A C   1 
ATOM   9    O  O   . ASP A 1 8   A 14.373  27.945  -9.740  1.00 52.56 ? 1   ASP A O   1 
ATOM   10   C  CB  . ASP A 1 8   A 11.460  28.240  -9.836  1.00 66.29 ? 1   ASP A CB  1 
ATOM   11   C  CG  . ASP A 1 8   A 12.033  29.581  -9.454  1.00 74.00 ? 1   ASP A CG  1 
ATOM   12   O  OD1 . ASP A 1 8   A 12.878  30.106  -10.216 1.00 72.78 ? 1   ASP A OD1 1 
ATOM   13   O  OD2 . ASP A 1 8   A 11.627  30.107  -8.390  1.00 76.53 ? 1   ASP A OD2 1 
ATOM   14   N  N   . CYS A 1 9   ? 14.138  25.912  -10.689 1.00 54.79 ? 1   CYS A N   1 
ATOM   15   C  CA  . CYS A 1 9   ? 15.205  25.213  -9.991  1.00 42.44 ? 1   CYS A CA  1 
ATOM   16   C  C   . CYS A 1 9   ? 16.557  25.910  -10.105 1.00 43.07 ? 1   CYS A C   1 
ATOM   17   O  O   . CYS A 1 9   ? 16.811  26.731  -10.990 1.00 43.88 ? 1   CYS A O   1 
ATOM   18   C  CB  . CYS A 1 9   ? 15.331  23.796  -10.546 1.00 43.98 ? 1   CYS A CB  1 
ATOM   19   S  SG  . CYS A 1 9   ? 15.785  23.772  -12.315 1.00 50.62 ? 1   CYS A SG  1 
ATOM   20   N  N   . GLY A 1 10  ? 17.447  25.537  -9.188  1.00 45.98 ? 2   GLY A N   1 
ATOM   21   C  CA  . GLY A 1 10  ? 18.851  25.886  -9.264  1.00 43.65 ? 2   GLY A CA  1 
ATOM   22   C  C   . GLY A 1 10  ? 19.174  27.340  -9.022  1.00 41.41 ? 2   GLY A C   1 
ATOM   23   O  O   . GLY A 1 10  ? 20.347  27.712  -9.109  1.00 39.69 ? 2   GLY A O   1 
ATOM   24   N  N   . LEU A 1 11  ? 18.178  28.171  -8.726  1.00 42.94 ? 3   LEU A N   1 
ATOM   25   C  CA  . LEU A 1 11  ? 18.368  29.587  -8.436  1.00 46.51 ? 3   LEU A CA  1 
ATOM   26   C  C   . LEU A 1 11  ? 18.083  29.812  -6.953  1.00 47.71 ? 3   LEU A C   1 
ATOM   27   O  O   . LEU A 1 11  ? 16.968  29.556  -6.487  1.00 50.14 ? 3   LEU A O   1 
ATOM   28   C  CB  . LEU A 1 11  ? 17.455  30.451  -9.313  1.00 46.26 ? 3   LEU A CB  1 
ATOM   29   C  CG  . LEU A 1 11  ? 17.598  30.362  -10.840 1.00 49.74 ? 3   LEU A CG  1 
ATOM   30   C  CD1 . LEU A 1 11  ? 16.491  31.145  -11.540 1.00 49.69 ? 3   LEU A CD1 1 
ATOM   31   C  CD2 . LEU A 1 11  ? 18.963  30.843  -11.316 1.00 41.99 ? 3   LEU A CD2 1 
ATOM   32   N  N   . ARG A 1 12  ? 19.099  30.287  -6.205  1.00 47.70 ? 4   ARG A N   1 
ATOM   33   C  CA  . ARG A 1 12  ? 19.012  30.307  -4.742  1.00 42.71 ? 4   ARG A CA  1 
ATOM   34   C  C   . ARG A 1 12  ? 18.369  31.603  -4.258  1.00 46.93 ? 4   ARG A C   1 
ATOM   35   O  O   . ARG A 1 12  ? 18.742  32.686  -4.736  1.00 44.31 ? 4   ARG A O   1 
ATOM   36   C  CB  . ARG A 1 12  ? 20.389  30.148  -4.118  1.00 38.95 ? 4   ARG A CB  1 
ATOM   37   C  CG  . ARG A 1 12  ? 20.991  28.778  -4.355  1.00 40.14 ? 4   ARG A CG  1 
ATOM   38   C  CD  . ARG A 1 12  ? 22.452  28.720  -3.967  1.00 40.73 ? 4   ARG A CD  1 
ATOM   39   N  NE  . ARG A 1 12  ? 23.281  29.679  -4.690  1.00 38.49 ? 4   ARG A NE  1 
ATOM   40   C  CZ  . ARG A 1 12  ? 24.572  29.860  -4.451  1.00 41.71 ? 4   ARG A CZ  1 
ATOM   41   N  NH1 . ARG A 1 12  ? 25.198  29.187  -3.493  1.00 42.47 ? 4   ARG A NH1 1 
ATOM   42   N  NH2 . ARG A 1 12  ? 25.256  30.729  -5.195  1.00 42.43 ? 4   ARG A NH2 1 
ATOM   43   N  N   . PRO A 1 13  ? 17.369  31.513  -3.361  1.00 43.32 ? 5   PRO A N   1 
ATOM   44   C  CA  . PRO A 1 13  ? 16.799  32.732  -2.758  1.00 40.46 ? 5   PRO A CA  1 
ATOM   45   C  C   . PRO A 1 13  ? 17.820  33.733  -2.243  1.00 44.13 ? 5   PRO A C   1 
ATOM   46   O  O   . PRO A 1 13  ? 17.767  34.913  -2.611  1.00 46.05 ? 5   PRO A O   1 
ATOM   47   C  CB  . PRO A 1 13  ? 15.954  32.163  -1.616  1.00 40.57 ? 5   PRO A CB  1 
ATOM   48   C  CG  . PRO A 1 13  ? 15.488  30.836  -2.131  1.00 42.05 ? 5   PRO A CG  1 
ATOM   49   C  CD  . PRO A 1 13  ? 16.550  30.320  -3.077  1.00 38.46 ? 5   PRO A CD  1 
ATOM   50   N  N   . LEU A 1 14  ? 18.772  33.295  -1.429  1.00 44.77 ? 6   LEU A N   1 
ATOM   51   C  CA  . LEU A 1 14  ? 19.701  34.213  -0.784  1.00 44.20 ? 6   LEU A CA  1 
ATOM   52   C  C   . LEU A 1 14  ? 20.919  34.577  -1.638  1.00 48.05 ? 6   LEU A C   1 
ATOM   53   O  O   . LEU A 1 14  ? 21.772  35.338  -1.170  1.00 48.48 ? 6   LEU A O   1 
ATOM   54   C  CB  . LEU A 1 14  ? 20.149  33.625  0.556   1.00 40.65 ? 6   LEU A CB  1 
ATOM   55   C  CG  . LEU A 1 14  ? 18.979  33.374  1.516   1.00 44.66 ? 6   LEU A CG  1 
ATOM   56   C  CD1 . LEU A 1 14  ? 19.461  32.813  2.842   1.00 41.04 ? 6   LEU A CD1 1 
ATOM   57   C  CD2 . LEU A 1 14  ? 18.146  34.647  1.746   1.00 43.52 ? 6   LEU A CD2 1 
ATOM   58   N  N   . PHE A 1 15  ? 21.037  34.072  -2.869  1.00 48.84 ? 7   PHE A N   1 
ATOM   59   C  CA  . PHE A 1 15  ? 22.210  34.419  -3.668  1.00 45.66 ? 7   PHE A CA  1 
ATOM   60   C  C   . PHE A 1 15  ? 21.824  34.873  -5.076  1.00 46.06 ? 7   PHE A C   1 
ATOM   61   O  O   . PHE A 1 15  ? 21.894  36.071  -5.377  1.00 44.37 ? 7   PHE A O   1 
ATOM   62   C  CB  . PHE A 1 15  ? 23.198  33.238  -3.682  1.00 39.67 ? 7   PHE A CB  1 
ATOM   63   C  CG  . PHE A 1 15  ? 23.885  33.032  -2.354  1.00 46.45 ? 7   PHE A CG  1 
ATOM   64   C  CD1 . PHE A 1 15  ? 25.026  33.761  -2.022  1.00 46.01 ? 7   PHE A CD1 1 
ATOM   65   C  CD2 . PHE A 1 15  ? 23.349  32.166  -1.402  1.00 42.27 ? 7   PHE A CD2 1 
ATOM   66   C  CE1 . PHE A 1 15  ? 25.647  33.594  -0.781  1.00 44.14 ? 7   PHE A CE1 1 
ATOM   67   C  CE2 . PHE A 1 15  ? 23.961  31.996  -0.163  1.00 36.81 ? 7   PHE A CE2 1 
ATOM   68   C  CZ  . PHE A 1 15  ? 25.108  32.704  0.146   1.00 39.94 ? 7   PHE A CZ  1 
ATOM   69   N  N   . GLU A 1 16  ? 21.433  33.938  -5.949  1.00 43.87 ? 8   GLU A N   1 
ATOM   70   C  CA  . GLU A 1 16  ? 21.050  34.312  -7.309  1.00 41.26 ? 8   GLU A CA  1 
ATOM   71   C  C   . GLU A 1 16  ? 19.863  35.271  -7.295  1.00 39.69 ? 8   GLU A C   1 
ATOM   72   O  O   . GLU A 1 16  ? 19.868  36.289  -7.985  1.00 36.85 ? 8   GLU A O   1 
ATOM   73   C  CB  . GLU A 1 16  ? 20.734  33.058  -8.131  1.00 41.20 ? 8   GLU A CB  1 
ATOM   74   C  CG  . GLU A 1 16  ? 21.958  32.323  -8.656  1.00 41.39 ? 8   GLU A CG  1 
ATOM   75   C  CD  . GLU A 1 16  ? 22.571  31.389  -7.628  1.00 43.08 ? 8   GLU A CD  1 
ATOM   76   O  OE1 . GLU A 1 16  ? 21.882  31.073  -6.628  1.00 38.37 ? 8   GLU A OE1 1 
ATOM   77   O  OE2 . GLU A 1 16  ? 23.741  30.971  -7.826  1.00 38.43 ? 8   GLU A OE2 1 
ATOM   78   N  N   . LYS A 1 17  ? 18.838  34.969  -6.498  1.00 40.79 ? 9   LYS A N   1 
ATOM   79   C  CA  . LYS A 1 17  ? 17.681  35.854  -6.434  1.00 44.64 ? 9   LYS A CA  1 
ATOM   80   C  C   . LYS A 1 17  ? 17.982  37.183  -5.739  1.00 45.04 ? 9   LYS A C   1 
ATOM   81   O  O   . LYS A 1 17  ? 17.174  38.110  -5.842  1.00 46.22 ? 9   LYS A O   1 
ATOM   82   C  CB  . LYS A 1 17  ? 16.505  35.135  -5.764  1.00 41.62 ? 9   LYS A CB  1 
ATOM   83   C  CG  . LYS A 1 17  ? 15.957  33.990  -6.625  1.00 50.08 ? 9   LYS A CG  1 
ATOM   84   C  CD  . LYS A 1 17  ? 15.238  32.908  -5.812  1.00 52.39 ? 9   LYS A CD  1 
ATOM   85   C  CE  . LYS A 1 17  ? 14.218  32.118  -6.638  1.00 53.93 ? 9   LYS A CE  1 
ATOM   86   N  NZ  . LYS A 1 17  ? 12.970  31.829  -5.867  1.00 56.15 ? 9   LYS A NZ  1 
ATOM   87   N  N   . LYS A 1 18  ? 19.120  37.318  -5.057  1.00 44.96 ? 10  LYS A N   1 
ATOM   88   C  CA  . LYS A 1 18  ? 19.497  38.592  -4.457  1.00 47.90 ? 10  LYS A CA  1 
ATOM   89   C  C   . LYS A 1 18  ? 20.728  39.204  -5.117  1.00 49.80 ? 10  LYS A C   1 
ATOM   90   O  O   . LYS A 1 18  ? 21.337  40.117  -4.543  1.00 50.65 ? 10  LYS A O   1 
ATOM   91   C  CB  . LYS A 1 18  ? 19.781  38.424  -2.959  1.00 43.53 ? 10  LYS A CB  1 
ATOM   92   C  CG  . LYS A 1 18  ? 18.596  38.008  -2.094  1.00 48.71 ? 10  LYS A CG  1 
ATOM   93   C  CD  . LYS A 1 18  ? 18.964  37.952  -0.609  1.00 39.18 ? 10  LYS A CD  1 
ATOM   94   C  CE  . LYS A 1 18  ? 18.016  38.808  0.214   1.00 42.13 ? 10  LYS A CE  1 
ATOM   95   N  NZ  . LYS A 1 18  ? 16.973  38.025  0.963   1.00 53.63 ? 10  LYS A NZ  1 
ATOM   96   N  N   . SER A 1 19  ? 21.093  38.734  -6.312  1.00 43.25 ? 11  SER A N   1 
ATOM   97   C  CA  . SER A 1 19  ? 22.268  39.231  -7.037  1.00 43.32 ? 11  SER A CA  1 
ATOM   98   C  C   . SER A 1 19  ? 23.495  39.289  -6.122  1.00 45.28 ? 11  SER A C   1 
ATOM   99   O  O   . SER A 1 19  ? 24.171  40.309  -6.004  1.00 51.68 ? 11  SER A O   1 
ATOM   100  C  CB  . SER A 1 19  ? 21.978  40.591  -7.674  1.00 48.56 ? 11  SER A CB  1 
ATOM   101  O  OG  . SER A 1 19  ? 20.704  40.584  -8.315  1.00 52.73 ? 11  SER A OG  1 
ATOM   102  N  N   . LEU A 1 20  ? 23.770  38.172  -5.454  1.00 47.38 ? 12  LEU A N   1 
ATOM   103  C  CA  . LEU A 1 20  ? 24.894  38.067  -4.537  1.00 46.46 ? 12  LEU A CA  1 
ATOM   104  C  C   . LEU A 1 20  ? 25.684  36.797  -4.821  1.00 48.04 ? 12  LEU A C   1 
ATOM   105  O  O   . LEU A 1 20  ? 25.105  35.720  -5.011  1.00 48.42 ? 12  LEU A O   1 
ATOM   106  C  CB  . LEU A 1 20  ? 24.413  38.065  -3.085  1.00 43.98 ? 12  LEU A CB  1 
ATOM   107  C  CG  . LEU A 1 20  ? 23.827  39.358  -2.524  1.00 45.17 ? 12  LEU A CG  1 
ATOM   108  C  CD1 . LEU A 1 20  ? 23.475  39.115  -1.078  1.00 42.39 ? 12  LEU A CD1 1 
ATOM   109  C  CD2 . LEU A 1 20  ? 24.774  40.550  -2.647  1.00 41.23 ? 12  LEU A CD2 1 
ATOM   110  N  N   . GLU A 1 21  ? 27.011  36.940  -4.883  1.00 49.26 ? 13  GLU A N   1 
ATOM   111  C  CA  . GLU A 1 21  ? 27.881  35.790  -5.233  1.00 44.34 ? 13  GLU A CA  1 
ATOM   112  C  C   . GLU A 1 21  ? 28.247  34.993  -3.977  1.00 45.04 ? 13  GLU A C   1 
ATOM   113  O  O   . GLU A 1 21  ? 28.668  35.622  -2.981  1.00 49.04 ? 13  GLU A O   1 
ATOM   114  C  CB  . GLU A 1 21  ? 29.156  36.331  -5.881  1.00 42.14 ? 13  GLU A CB  1 
ATOM   115  C  CG  . GLU A 1 21  ? 29.842  35.345  -6.820  1.00 49.70 ? 13  GLU A CG  1 
ATOM   116  C  CD  . GLU A 1 21  ? 31.360  35.348  -6.760  1.00 57.22 ? 13  GLU A CD  1 
ATOM   117  O  OE1 . GLU A 1 21  ? 31.941  34.336  -6.317  1.00 50.48 ? 13  GLU A OE1 1 
ATOM   118  O  OE2 . GLU A 1 21  ? 31.963  36.365  -7.162  1.00 68.32 ? 13  GLU A OE2 1 
ATOM   119  N  N   . ASP A 1 22  ? 28.100  33.666  -4.020  1.00 39.96 ? 14  ASP A N   1 
ATOM   120  C  CA  . ASP A 1 22  ? 28.558  32.832  -2.873  1.00 43.71 ? 14  ASP A CA  1 
ATOM   121  C  C   . ASP A 1 22  ? 30.086  32.939  -2.834  1.00 44.47 ? 14  ASP A C   1 
ATOM   122  O  O   . ASP A 1 22  ? 30.683  33.080  -3.924  1.00 47.31 ? 14  ASP A O   1 
ATOM   123  C  CB  . ASP A 1 22  ? 27.942  31.439  -2.888  1.00 39.88 ? 14  ASP A CB  1 
ATOM   124  C  CG  . ASP A 1 22  ? 28.595  30.409  -3.796  1.00 40.73 ? 14  ASP A CG  1 
ATOM   125  O  OD1 . ASP A 1 22  ? 29.811  30.170  -3.641  1.00 39.33 ? 14  ASP A OD1 1 
ATOM   126  O  OD2 . ASP A 1 22  ? 27.873  29.831  -4.633  1.00 37.21 ? 14  ASP A OD2 1 
ATOM   127  N  N   . LYS A 1 23  A 30.684  32.848  -1.636  1.00 41.05 ? 14  LYS A N   1 
ATOM   128  C  CA  . LYS A 1 23  A 32.145  33.043  -1.402  1.00 43.53 ? 14  LYS A CA  1 
ATOM   129  C  C   . LYS A 1 23  A 33.089  32.351  -2.393  1.00 38.52 ? 14  LYS A C   1 
ATOM   130  O  O   . LYS A 1 23  A 34.158  32.971  -2.633  1.00 43.50 ? 14  LYS A O   1 
ATOM   131  C  CB  . LYS A 1 23  A 32.504  32.472  -0.027  1.00 41.78 ? 14  LYS A CB  1 
ATOM   132  C  CG  . LYS A 1 23  A 32.388  33.414  1.157   1.00 44.17 ? 14  LYS A CG  1 
ATOM   133  C  CD  . LYS A 1 23  A 32.600  32.677  2.473   1.00 46.78 ? 14  LYS A CD  1 
ATOM   134  C  CE  . LYS A 1 23  A 31.937  33.353  3.629   1.00 51.95 ? 14  LYS A CE  1 
ATOM   135  N  NZ  . LYS A 1 23  A 32.568  32.991  4.901   1.00 51.35 ? 14  LYS A NZ  1 
ATOM   136  N  N   . THR A 1 24  B 32.740  31.170  -2.937  1.00 40.87 ? 14  THR A N   1 
ATOM   137  C  CA  . THR A 1 24  B 33.685  30.404  -3.742  1.00 41.93 ? 14  THR A CA  1 
ATOM   138  C  C   . THR A 1 24  B 33.188  29.964  -5.115  1.00 41.77 ? 14  THR A C   1 
ATOM   139  O  O   . THR A 1 24  B 33.917  29.228  -5.788  1.00 44.40 ? 14  THR A O   1 
ATOM   140  C  CB  . THR A 1 24  B 34.123  29.133  -3.003  1.00 38.29 ? 14  THR A CB  1 
ATOM   141  O  OG1 . THR A 1 24  B 32.995  28.261  -2.907  1.00 43.29 ? 14  THR A OG1 1 
ATOM   142  C  CG2 . THR A 1 24  B 34.623  29.457  -1.604  1.00 36.01 ? 14  THR A CG2 1 
ATOM   143  N  N   . GLU A 1 25  C 31.972  30.338  -5.537  1.00 38.13 ? 14  GLU A N   1 
ATOM   144  C  CA  . GLU A 1 25  C 31.479  29.879  -6.837  1.00 41.41 ? 14  GLU A CA  1 
ATOM   145  C  C   . GLU A 1 25  C 32.375  30.355  -7.985  1.00 40.02 ? 14  GLU A C   1 
ATOM   146  O  O   . GLU A 1 25  C 32.502  29.671  -9.020  1.00 43.51 ? 14  GLU A O   1 
ATOM   147  C  CB  . GLU A 1 25  C 30.030  30.334  -7.035  1.00 37.85 ? 14  GLU A CB  1 
ATOM   148  C  CG  . GLU A 1 25  C 29.792  31.815  -6.808  1.00 37.70 ? 14  GLU A CG  1 
ATOM   149  C  CD  . GLU A 1 25  C 28.367  32.231  -7.155  1.00 40.04 ? 14  GLU A CD  1 
ATOM   150  O  OE1 . GLU A 1 25  C 27.998  32.140  -8.340  1.00 37.19 ? 14  GLU A OE1 1 
ATOM   151  O  OE2 . GLU A 1 25  C 27.608  32.646  -6.251  1.00 47.84 ? 14  GLU A OE2 1 
ATOM   152  N  N   . ARG A 1 26  D 33.042  31.492  -7.803  1.00 39.40 ? 14  ARG A N   1 
ATOM   153  C  CA  . ARG A 1 26  D 33.964  31.973  -8.824  1.00 45.74 ? 14  ARG A CA  1 
ATOM   154  C  C   . ARG A 1 26  D 35.044  30.945  -9.132  1.00 47.06 ? 14  ARG A C   1 
ATOM   155  O  O   . ARG A 1 26  D 35.565  30.914  -10.250 1.00 48.99 ? 14  ARG A O   1 
ATOM   156  C  CB  . ARG A 1 26  D 34.587  33.288  -8.377  1.00 46.17 ? 14  ARG A CB  1 
ATOM   157  C  CG  . ARG A 1 26  D 35.092  34.117  -9.507  1.00 48.24 ? 14  ARG A CG  1 
ATOM   158  C  CD  . ARG A 1 26  D 35.943  35.215  -8.967  1.00 48.97 ? 14  ARG A CD  1 
ATOM   159  N  NE  . ARG A 1 26  D 35.113  36.302  -8.474  1.00 54.92 ? 14  ARG A NE  1 
ATOM   160  C  CZ  . ARG A 1 26  D 35.516  37.561  -8.415  1.00 53.49 ? 14  ARG A CZ  1 
ATOM   161  N  NH1 . ARG A 1 26  D 36.718  37.920  -8.847  1.00 45.64 ? 14  ARG A NH1 1 
ATOM   162  N  NH2 . ARG A 1 26  D 34.689  38.483  -7.927  1.00 46.64 ? 14  ARG A NH2 1 
ATOM   163  N  N   . GLU A 1 27  E 35.400  30.106  -8.156  1.00 42.68 ? 14  GLU A N   1 
ATOM   164  C  CA  . GLU A 1 27  E 36.350  29.031  -8.411  1.00 43.54 ? 14  GLU A CA  1 
ATOM   165  C  C   . GLU A 1 27  E 35.817  28.088  -9.485  1.00 44.03 ? 14  GLU A C   1 
ATOM   166  O  O   . GLU A 1 27  E 36.549  27.694  -10.404 1.00 46.42 ? 14  GLU A O   1 
ATOM   167  C  CB  . GLU A 1 27  E 36.634  28.286  -7.106  1.00 35.90 ? 14  GLU A CB  1 
ATOM   168  C  CG  . GLU A 1 27  E 37.702  27.222  -7.184  1.00 39.66 ? 14  GLU A CG  1 
ATOM   169  C  CD  . GLU A 1 27  E 37.998  26.566  -5.821  1.00 43.39 ? 14  GLU A CD  1 
ATOM   170  O  OE1 . GLU A 1 27  E 37.357  26.925  -4.809  1.00 39.51 ? 14  GLU A OE1 1 
ATOM   171  O  OE2 . GLU A 1 27  E 38.880  25.683  -5.761  1.00 44.42 ? 14  GLU A OE2 1 
ATOM   172  N  N   . LEU A 1 28  F 34.526  27.760  -9.409  1.00 38.34 ? 14  LEU A N   1 
ATOM   173  C  CA  . LEU A 1 28  F 33.892  26.920  -10.422 1.00 40.91 ? 14  LEU A CA  1 
ATOM   174  C  C   . LEU A 1 28  F 33.888  27.597  -11.792 1.00 45.84 ? 14  LEU A C   1 
ATOM   175  O  O   . LEU A 1 28  F 34.285  27.001  -12.812 1.00 42.65 ? 14  LEU A O   1 
ATOM   176  C  CB  . LEU A 1 28  F 32.471  26.608  -9.974  1.00 36.77 ? 14  LEU A CB  1 
ATOM   177  C  CG  . LEU A 1 28  F 32.369  26.140  -8.526  1.00 41.35 ? 14  LEU A CG  1 
ATOM   178  C  CD1 . LEU A 1 28  F 30.913  26.169  -8.065  1.00 38.52 ? 14  LEU A CD1 1 
ATOM   179  C  CD2 . LEU A 1 28  F 32.973  24.727  -8.363  1.00 32.25 ? 14  LEU A CD2 1 
ATOM   180  N  N   . LEU A 1 29  G 33.388  28.836  -11.833 1.00 45.51 ? 14  LEU A N   1 
ATOM   181  C  CA  . LEU A 1 29  G 33.362  29.592  -13.082 1.00 44.36 ? 14  LEU A CA  1 
ATOM   182  C  C   . LEU A 1 29  G 34.743  29.632  -13.738 1.00 50.15 ? 14  LEU A C   1 
ATOM   183  O  O   . LEU A 1 29  G 34.904  29.316  -14.928 1.00 51.74 ? 14  LEU A O   1 
ATOM   184  C  CB  . LEU A 1 29  G 32.824  30.991  -12.794 1.00 43.72 ? 14  LEU A CB  1 
ATOM   185  C  CG  . LEU A 1 29  G 32.948  32.184  -13.730 1.00 48.81 ? 14  LEU A CG  1 
ATOM   186  C  CD1 . LEU A 1 29  G 31.659  32.975  -13.672 1.00 52.89 ? 14  LEU A CD1 1 
ATOM   187  C  CD2 . LEU A 1 29  G 34.085  33.079  -13.290 1.00 56.65 ? 14  LEU A CD2 1 
ATOM   188  N  N   . GLU A 1 30  H 35.769  29.957  -12.956 1.00 47.64 ? 14  GLU A N   1 
ATOM   189  C  CA  . GLU A 1 30  H 37.098  30.080  -13.525 1.00 56.14 ? 14  GLU A CA  1 
ATOM   190  C  C   . GLU A 1 30  H 37.684  28.725  -13.912 1.00 55.21 ? 14  GLU A C   1 
ATOM   191  O  O   . GLU A 1 30  H 38.518  28.660  -14.824 1.00 58.89 ? 14  GLU A O   1 
ATOM   192  C  CB  . GLU A 1 30  H 37.997  30.857  -12.549 1.00 54.66 ? 14  GLU A CB  1 
ATOM   193  C  CG  . GLU A 1 30  H 38.153  32.345  -12.951 1.00 62.01 ? 14  GLU A CG  1 
ATOM   194  C  CD  . GLU A 1 30  H 38.138  33.362  -11.796 1.00 65.44 ? 14  GLU A CD  1 
ATOM   195  O  OE1 . GLU A 1 30  H 38.751  33.113  -10.726 1.00 59.06 ? 14  GLU A OE1 1 
ATOM   196  O  OE2 . GLU A 1 30  H 37.534  34.445  -11.992 1.00 62.99 ? 14  GLU A OE2 1 
ATOM   197  N  N   . SER A 1 31  I 37.238  27.639  -13.281 1.00 52.22 ? 14  SER A N   1 
ATOM   198  C  CA  . SER A 1 31  I 37.620  26.326  -13.777 1.00 48.80 ? 14  SER A CA  1 
ATOM   199  C  C   . SER A 1 31  I 37.037  26.059  -15.161 1.00 58.20 ? 14  SER A C   1 
ATOM   200  O  O   . SER A 1 31  I 37.652  25.350  -15.968 1.00 56.81 ? 14  SER A O   1 
ATOM   201  C  CB  . SER A 1 31  I 37.182  25.252  -12.784 1.00 44.22 ? 14  SER A CB  1 
ATOM   202  O  OG  . SER A 1 31  I 35.799  24.978  -12.910 1.00 44.17 ? 14  SER A OG  1 
ATOM   203  N  N   . TYR A 1 32  J 35.836  26.601  -15.442 1.00 63.24 ? 14  TYR A N   1 
ATOM   204  C  CA  . TYR A 1 32  J 35.131  26.377  -16.744 1.00 56.70 ? 14  TYR A CA  1 
ATOM   205  C  C   . TYR A 1 32  J 35.819  27.199  -17.822 1.00 66.52 ? 14  TYR A C   1 
ATOM   206  O  O   . TYR A 1 32  J 35.265  28.233  -18.237 1.00 64.77 ? 14  TYR A O   1 
ATOM   207  C  CB  . TYR A 1 32  J 33.645  26.744  -16.724 1.00 50.45 ? 14  TYR A CB  1 
ATOM   208  C  CG  . TYR A 1 32  J 32.838  26.177  -15.567 1.00 49.25 ? 14  TYR A CG  1 
ATOM   209  C  CD1 . TYR A 1 32  J 33.092  24.908  -15.066 1.00 45.81 ? 14  TYR A CD1 1 
ATOM   210  C  CD2 . TYR A 1 32  J 31.817  26.915  -14.986 1.00 52.31 ? 14  TYR A CD2 1 
ATOM   211  C  CE1 . TYR A 1 32  J 32.363  24.398  -14.007 1.00 51.26 ? 14  TYR A CE1 1 
ATOM   212  C  CE2 . TYR A 1 32  J 31.078  26.412  -13.930 1.00 50.74 ? 14  TYR A CE2 1 
ATOM   213  C  CZ  . TYR A 1 32  J 31.348  25.148  -13.441 1.00 50.27 ? 14  TYR A CZ  1 
ATOM   214  O  OH  . TYR A 1 32  J 30.619  24.651  -12.400 1.00 53.93 ? 14  TYR A OH  1 
ATOM   215  N  N   . ILE A 1 33  K 36.987  26.748  -18.277 1.00 76.96 ? 14  ILE A N   1 
ATOM   216  C  CA  . ILE A 1 33  K 37.771  27.536  -19.272 1.00 81.82 ? 14  ILE A CA  1 
ATOM   217  C  C   . ILE A 1 33  K 38.503  26.558  -20.208 1.00 83.05 ? 14  ILE A C   1 
ATOM   218  O  O   . ILE A 1 33  K 37.798  25.811  -20.919 1.00 88.68 ? 14  ILE A O   1 
ATOM   219  C  CB  . ILE A 1 33  K 38.747  28.480  -18.544 1.00 79.42 ? 14  ILE A CB  1 
ATOM   220  C  CG1 . ILE A 1 33  K 38.395  29.948  -18.781 1.00 80.36 ? 14  ILE A CG1 1 
ATOM   221  C  CG2 . ILE A 1 33  K 40.195  28.173  -18.923 1.00 77.39 ? 14  ILE A CG2 1 
ATOM   222  C  CD1 . ILE A 1 33  K 37.682  30.609  -17.615 1.00 79.41 ? 14  ILE A CD1 1 
ATOM   223  N  N   . ILE B 2 1   ? 32.878  15.491  4.721   1.00 38.73 ? 16  ILE B N   1 
ATOM   224  C  CA  . ILE B 2 1   ? 33.715  16.332  3.880   1.00 34.75 ? 16  ILE B CA  1 
ATOM   225  C  C   . ILE B 2 1   ? 35.051  16.559  4.573   1.00 40.08 ? 16  ILE B C   1 
ATOM   226  O  O   . ILE B 2 1   ? 35.099  17.036  5.719   1.00 41.97 ? 16  ILE B O   1 
ATOM   227  C  CB  . ILE B 2 1   ? 33.038  17.688  3.570   1.00 37.86 ? 16  ILE B CB  1 
ATOM   228  C  CG1 . ILE B 2 1   ? 31.594  17.507  3.061   1.00 36.76 ? 16  ILE B CG1 1 
ATOM   229  C  CG2 . ILE B 2 1   ? 33.908  18.526  2.630   1.00 32.99 ? 16  ILE B CG2 1 
ATOM   230  C  CD1 . ILE B 2 1   ? 31.456  16.988  1.667   1.00 29.43 ? 16  ILE B CD1 1 
ATOM   231  N  N   . VAL B 2 2   ? 36.138  16.189  3.901   1.00 41.14 ? 17  VAL B N   1 
ATOM   232  C  CA  . VAL B 2 2   ? 37.495  16.417  4.397   1.00 43.37 ? 17  VAL B CA  1 
ATOM   233  C  C   . VAL B 2 2   ? 38.078  17.637  3.691   1.00 41.46 ? 17  VAL B C   1 
ATOM   234  O  O   . VAL B 2 2   ? 37.939  17.770  2.470   1.00 41.12 ? 17  VAL B O   1 
ATOM   235  C  CB  . VAL B 2 2   ? 38.387  15.185  4.176   1.00 41.81 ? 17  VAL B CB  1 
ATOM   236  C  CG1 . VAL B 2 2   ? 39.782  15.449  4.721   1.00 44.33 ? 17  VAL B CG1 1 
ATOM   237  C  CG2 . VAL B 2 2   ? 37.768  13.957  4.820   1.00 40.79 ? 17  VAL B CG2 1 
ATOM   238  N  N   . GLU B 2 3   ? 38.727  18.525  4.460   1.00 39.99 ? 18  GLU B N   1 
ATOM   239  C  CA  . GLU B 2 3   ? 39.428  19.714  3.947   1.00 38.80 ? 18  GLU B CA  1 
ATOM   240  C  C   . GLU B 2 3   ? 38.498  20.719  3.287   1.00 37.84 ? 18  GLU B C   1 
ATOM   241  O  O   . GLU B 2 3   ? 38.919  21.482  2.411   1.00 43.61 ? 18  GLU B O   1 
ATOM   242  C  CB  . GLU B 2 3   ? 40.556  19.335  2.983   1.00 39.90 ? 18  GLU B CB  1 
ATOM   243  C  CG  . GLU B 2 3   ? 41.741  18.638  3.691   1.00 46.76 ? 18  GLU B CG  1 
ATOM   244  C  CD  . GLU B 2 3   ? 42.511  19.578  4.626   1.00 48.14 ? 18  GLU B CD  1 
ATOM   245  O  OE1 . GLU B 2 3   ? 42.751  20.751  4.237   1.00 50.27 ? 18  GLU B OE1 1 
ATOM   246  O  OE2 . GLU B 2 3   ? 42.864  19.152  5.751   1.00 46.12 ? 18  GLU B OE2 1 
ATOM   247  N  N   . GLY B 2 4   ? 37.243  20.743  3.713   1.00 35.58 ? 19  GLY B N   1 
ATOM   248  C  CA  . GLY B 2 4   ? 36.284  21.734  3.279   1.00 35.17 ? 19  GLY B CA  1 
ATOM   249  C  C   . GLY B 2 4   ? 36.180  22.888  4.261   1.00 35.92 ? 19  GLY B C   1 
ATOM   250  O  O   . GLY B 2 4   ? 37.058  23.118  5.100   1.00 36.76 ? 19  GLY B O   1 
ATOM   251  N  N   . SER B 2 5   ? 35.067  23.606  4.169   1.00 35.16 ? 20  SER B N   1 
ATOM   252  C  CA  . SER B 2 5   ? 34.801  24.711  5.077   1.00 34.25 ? 20  SER B CA  1 
ATOM   253  C  C   . SER B 2 5   ? 33.297  24.793  5.350   1.00 33.81 ? 20  SER B C   1 
ATOM   254  O  O   . SER B 2 5   ? 32.506  24.011  4.821   1.00 37.61 ? 20  SER B O   1 
ATOM   255  C  CB  . SER B 2 5   ? 35.353  25.997  4.487   1.00 32.17 ? 20  SER B CB  1 
ATOM   256  O  OG  . SER B 2 5   ? 34.718  26.245  3.253   1.00 43.90 ? 20  SER B OG  1 
ATOM   257  N  N   . ASP B 2 6   ? 32.906  25.743  6.201   1.00 32.46 ? 21  ASP B N   1 
ATOM   258  C  CA  . ASP B 2 6   ? 31.503  25.907  6.563   1.00 34.65 ? 21  ASP B CA  1 
ATOM   259  C  C   . ASP B 2 6   ? 30.716  26.532  5.406   1.00 40.76 ? 21  ASP B C   1 
ATOM   260  O  O   . ASP B 2 6   ? 31.099  27.569  4.861   1.00 45.36 ? 21  ASP B O   1 
ATOM   261  C  CB  . ASP B 2 6   ? 31.359  26.791  7.807   1.00 30.05 ? 21  ASP B CB  1 
ATOM   262  C  CG  . ASP B 2 6   ? 31.965  26.171  9.077   1.00 37.70 ? 21  ASP B CG  1 
ATOM   263  O  OD1 . ASP B 2 6   ? 32.401  24.993  9.063   1.00 36.92 ? 21  ASP B OD1 1 
ATOM   264  O  OD2 . ASP B 2 6   ? 32.007  26.889  10.109  1.00 34.56 ? 21  ASP B OD2 1 
ATOM   265  N  N   . ALA B 2 7   ? 29.605  25.910  5.037   1.00 35.91 ? 22  ALA B N   1 
ATOM   266  C  CA  . ALA B 2 7   ? 28.727  26.523  4.054   1.00 43.09 ? 22  ALA B CA  1 
ATOM   267  C  C   . ALA B 2 7   ? 28.147  27.813  4.606   1.00 38.77 ? 22  ALA B C   1 
ATOM   268  O  O   . ALA B 2 7   ? 27.926  27.953  5.812   1.00 38.71 ? 22  ALA B O   1 
ATOM   269  C  CB  . ALA B 2 7   ? 27.587  25.573  3.675   1.00 44.09 ? 22  ALA B CB  1 
ATOM   270  N  N   . GLU B 2 8   ? 27.906  28.767  3.717   1.00 39.26 ? 23  GLU B N   1 
ATOM   271  C  CA  . GLU B 2 8   ? 27.112  29.904  4.146   1.00 42.00 ? 23  GLU B CA  1 
ATOM   272  C  C   . GLU B 2 8   ? 25.660  29.475  4.294   1.00 42.05 ? 23  GLU B C   1 
ATOM   273  O  O   . GLU B 2 8   ? 25.234  28.424  3.805   1.00 41.11 ? 23  GLU B O   1 
ATOM   274  C  CB  . GLU B 2 8   ? 27.240  31.077  3.166   1.00 39.18 ? 23  GLU B CB  1 
ATOM   275  C  CG  . GLU B 2 8   ? 28.677  31.565  2.973   1.00 40.79 ? 23  GLU B CG  1 
ATOM   276  C  CD  . GLU B 2 8   ? 28.904  32.249  1.624   1.00 47.29 ? 23  GLU B CD  1 
ATOM   277  O  OE1 . GLU B 2 8   ? 28.505  33.435  1.438   1.00 41.34 ? 23  GLU B OE1 1 
ATOM   278  O  OE2 . GLU B 2 8   ? 29.495  31.585  0.742   1.00 47.99 ? 23  GLU B OE2 1 
ATOM   279  N  N   . ILE B 2 9   ? 24.908  30.272  5.040   1.00 47.65 ? 24  ILE B N   1 
ATOM   280  C  CA  . ILE B 2 9   ? 23.491  29.997  5.193   1.00 45.71 ? 24  ILE B CA  1 
ATOM   281  C  C   . ILE B 2 9   ? 22.805  30.208  3.852   1.00 37.56 ? 24  ILE B C   1 
ATOM   282  O  O   . ILE B 2 9   ? 22.952  31.262  3.220   1.00 39.55 ? 24  ILE B O   1 
ATOM   283  C  CB  . ILE B 2 9   ? 22.889  30.888  6.286   1.00 38.74 ? 24  ILE B CB  1 
ATOM   284  C  CG1 . ILE B 2 9   ? 23.195  30.285  7.649   1.00 38.83 ? 24  ILE B CG1 1 
ATOM   285  C  CG2 . ILE B 2 9   ? 21.419  31.039  6.080   1.00 31.04 ? 24  ILE B CG2 1 
ATOM   286  C  CD1 . ILE B 2 9   ? 22.931  31.212  8.777   1.00 43.01 ? 24  ILE B CD1 1 
ATOM   287  N  N   . GLY B 2 10  ? 22.025  29.219  3.431   1.00 37.88 ? 25  GLY B N   1 
ATOM   288  C  CA  . GLY B 2 10  ? 21.306  29.278  2.174   1.00 35.79 ? 25  GLY B CA  1 
ATOM   289  C  C   . GLY B 2 10  ? 22.131  28.954  0.958   1.00 39.09 ? 25  GLY B C   1 
ATOM   290  O  O   . GLY B 2 10  ? 21.610  29.030  -0.162  1.00 40.92 ? 25  GLY B O   1 
ATOM   291  N  N   . MET B 2 11  ? 23.394  28.569  1.149   1.00 41.89 ? 26  MET B N   1 
ATOM   292  C  CA  . MET B 2 11  ? 24.288  28.248  0.041   1.00 38.31 ? 26  MET B CA  1 
ATOM   293  C  C   . MET B 2 11  ? 23.827  27.020  -0.739  1.00 39.92 ? 26  MET B C   1 
ATOM   294  O  O   . MET B 2 11  ? 24.076  26.925  -1.948  1.00 38.99 ? 26  MET B O   1 
ATOM   295  C  CB  . MET B 2 11  ? 25.689  28.015  0.592   1.00 33.53 ? 26  MET B CB  1 
ATOM   296  C  CG  . MET B 2 11  ? 26.795  28.221  -0.387  1.00 38.69 ? 26  MET B CG  1 
ATOM   297  S  SD  . MET B 2 11  ? 28.333  27.564  0.255   1.00 43.18 ? 26  MET B SD  1 
ATOM   298  C  CE  . MET B 2 11  ? 29.493  28.611  -0.597  1.00 35.81 ? 26  MET B CE  1 
ATOM   299  N  N   . SER B 2 12  ? 23.179  26.067  -0.065  1.00 39.84 ? 27  SER B N   1 
ATOM   300  C  CA  . SER B 2 12  ? 22.835  24.772  -0.652  1.00 34.12 ? 27  SER B CA  1 
ATOM   301  C  C   . SER B 2 12  ? 21.410  24.394  -0.245  1.00 35.85 ? 27  SER B C   1 
ATOM   302  O  O   . SER B 2 12  ? 21.176  23.381  0.419   1.00 34.30 ? 27  SER B O   1 
ATOM   303  C  CB  . SER B 2 12  ? 23.852  23.723  -0.205  1.00 27.01 ? 27  SER B CB  1 
ATOM   304  O  OG  . SER B 2 12  ? 23.634  22.461  -0.797  1.00 34.77 ? 27  SER B OG  1 
ATOM   305  N  N   . PRO B 2 13  ? 20.419  25.196  -0.652  1.00 36.04 ? 28  PRO B N   1 
ATOM   306  C  CA  . PRO B 2 13  ? 19.048  25.000  -0.119  1.00 35.80 ? 28  PRO B CA  1 
ATOM   307  C  C   . PRO B 2 13  ? 18.390  23.685  -0.527  1.00 39.61 ? 28  PRO B C   1 
ATOM   308  O  O   . PRO B 2 13  ? 17.287  23.394  -0.036  1.00 42.62 ? 28  PRO B O   1 
ATOM   309  C  CB  . PRO B 2 13  ? 18.273  26.197  -0.685  1.00 32.99 ? 28  PRO B CB  1 
ATOM   310  C  CG  . PRO B 2 13  ? 19.061  26.612  -1.922  1.00 38.86 ? 28  PRO B CG  1 
ATOM   311  C  CD  . PRO B 2 13  ? 20.507  26.294  -1.632  1.00 32.02 ? 28  PRO B CD  1 
ATOM   312  N  N   . TRP B 2 14  ? 19.018  22.886  -1.391  1.00 35.51 ? 29  TRP B N   1 
ATOM   313  C  CA  . TRP B 2 14  ? 18.494  21.589  -1.778  1.00 31.00 ? 29  TRP B CA  1 
ATOM   314  C  C   . TRP B 2 14  ? 19.035  20.482  -0.894  1.00 34.53 ? 29  TRP B C   1 
ATOM   315  O  O   . TRP B 2 14  ? 18.660  19.319  -1.070  1.00 39.88 ? 29  TRP B O   1 
ATOM   316  C  CB  . TRP B 2 14  ? 18.829  21.303  -3.251  1.00 33.63 ? 29  TRP B CB  1 
ATOM   317  C  CG  . TRP B 2 14  ? 20.147  21.906  -3.657  1.00 36.85 ? 29  TRP B CG  1 
ATOM   318  C  CD1 . TRP B 2 14  ? 21.394  21.393  -3.414  1.00 34.54 ? 29  TRP B CD1 1 
ATOM   319  C  CD2 . TRP B 2 14  ? 20.357  23.157  -4.331  1.00 34.64 ? 29  TRP B CD2 1 
ATOM   320  N  NE1 . TRP B 2 14  ? 22.362  22.241  -3.908  1.00 36.81 ? 29  TRP B NE1 1 
ATOM   321  C  CE2 . TRP B 2 14  ? 21.751  23.331  -4.471  1.00 34.87 ? 29  TRP B CE2 1 
ATOM   322  C  CE3 . TRP B 2 14  ? 19.504  24.143  -4.829  1.00 34.73 ? 29  TRP B CE3 1 
ATOM   323  C  CZ2 . TRP B 2 14  ? 22.307  24.446  -5.095  1.00 33.64 ? 29  TRP B CZ2 1 
ATOM   324  C  CZ3 . TRP B 2 14  ? 20.061  25.256  -5.442  1.00 37.66 ? 29  TRP B CZ3 1 
ATOM   325  C  CH2 . TRP B 2 14  ? 21.449  25.397  -5.566  1.00 35.56 ? 29  TRP B CH2 1 
ATOM   326  N  N   . GLN B 2 15  ? 19.872  20.819  0.080   1.00 34.49 ? 30  GLN B N   1 
ATOM   327  C  CA  . GLN B 2 15  ? 20.469  19.800  0.931   1.00 33.76 ? 30  GLN B CA  1 
ATOM   328  C  C   . GLN B 2 15  ? 19.406  19.164  1.829   1.00 36.42 ? 30  GLN B C   1 
ATOM   329  O  O   . GLN B 2 15  ? 18.591  19.864  2.447   1.00 35.43 ? 30  GLN B O   1 
ATOM   330  C  CB  . GLN B 2 15  ? 21.588  20.414  1.767   1.00 30.25 ? 30  GLN B CB  1 
ATOM   331  C  CG  . GLN B 2 15  ? 22.571  19.394  2.289   1.00 37.20 ? 30  GLN B CG  1 
ATOM   332  C  CD  . GLN B 2 15  ? 23.664  19.084  1.292   1.00 33.27 ? 30  GLN B CD  1 
ATOM   333  O  OE1 . GLN B 2 15  ? 23.926  19.873  0.378   1.00 31.70 ? 30  GLN B OE1 1 
ATOM   334  N  NE2 . GLN B 2 15  ? 24.304  17.934  1.458   1.00 29.16 ? 30  GLN B NE2 1 
ATOM   335  N  N   . VAL B 2 16  ? 19.415  17.834  1.906   1.00 36.10 ? 31  VAL B N   1 
ATOM   336  C  CA  . VAL B 2 16  ? 18.480  17.080  2.727   1.00 34.93 ? 31  VAL B CA  1 
ATOM   337  C  C   . VAL B 2 16  ? 19.284  16.122  3.592   1.00 38.33 ? 31  VAL B C   1 
ATOM   338  O  O   . VAL B 2 16  ? 20.281  15.547  3.138   1.00 40.42 ? 31  VAL B O   1 
ATOM   339  C  CB  . VAL B 2 16  ? 17.452  16.319  1.854   1.00 42.02 ? 31  VAL B CB  1 
ATOM   340  C  CG1 . VAL B 2 16  ? 16.504  15.483  2.706   1.00 42.00 ? 31  VAL B CG1 1 
ATOM   341  C  CG2 . VAL B 2 16  ? 16.657  17.291  0.977   1.00 38.50 ? 31  VAL B CG2 1 
ATOM   342  N  N   . MET B 2 17  ? 18.860  15.961  4.843   1.00 44.92 ? 32  MET B N   1 
ATOM   343  C  CA  . MET B 2 17  ? 19.400  14.946  5.734   1.00 40.26 ? 32  MET B CA  1 
ATOM   344  C  C   . MET B 2 17  ? 18.464  13.753  5.739   1.00 41.63 ? 32  MET B C   1 
ATOM   345  O  O   . MET B 2 17  ? 17.242  13.921  5.776   1.00 42.44 ? 32  MET B O   1 
ATOM   346  C  CB  . MET B 2 17  ? 19.530  15.460  7.162   1.00 38.50 ? 32  MET B CB  1 
ATOM   347  C  CG  . MET B 2 17  ? 20.340  16.710  7.345   1.00 40.08 ? 32  MET B CG  1 
ATOM   348  S  SD  . MET B 2 17  ? 20.337  17.076  9.099   1.00 42.17 ? 32  MET B SD  1 
ATOM   349  C  CE  . MET B 2 17  ? 21.102  18.669  9.126   1.00 46.81 ? 32  MET B CE  1 
ATOM   350  N  N   . LEU B 2 18  ? 19.041  12.553  5.728   1.00 41.83 ? 33  LEU B N   1 
ATOM   351  C  CA  . LEU B 2 18  ? 18.284  11.314  5.771   1.00 39.25 ? 33  LEU B CA  1 
ATOM   352  C  C   . LEU B 2 18  ? 18.634  10.581  7.050   1.00 39.11 ? 33  LEU B C   1 
ATOM   353  O  O   . LEU B 2 18  ? 19.803  10.207  7.259   1.00 36.47 ? 33  LEU B O   1 
ATOM   354  C  CB  . LEU B 2 18  ? 18.583  10.433  4.561   1.00 40.30 ? 33  LEU B CB  1 
ATOM   355  C  CG  . LEU B 2 18  ? 18.003  9.028   4.655   1.00 39.27 ? 33  LEU B CG  1 
ATOM   356  C  CD1 . LEU B 2 18  ? 16.500  9.099   4.488   1.00 42.32 ? 33  LEU B CD1 1 
ATOM   357  C  CD2 . LEU B 2 18  ? 18.643  8.126   3.610   1.00 36.58 ? 33  LEU B CD2 1 
ATOM   358  N  N   . PHE B 2 19  ? 17.611  10.355  7.870   1.00 39.45 ? 34  PHE B N   1 
ATOM   359  C  CA  . PHE B 2 19  ? 17.708  9.732   9.176   1.00 41.07 ? 34  PHE B CA  1 
ATOM   360  C  C   . PHE B 2 19  ? 17.030  8.372   9.166   1.00 42.95 ? 34  PHE B C   1 
ATOM   361  O  O   . PHE B 2 19  ? 15.984  8.180   8.526   1.00 45.72 ? 34  PHE B O   1 
ATOM   362  C  CB  . PHE B 2 19  ? 17.005  10.559  10.257  1.00 35.42 ? 34  PHE B CB  1 
ATOM   363  C  CG  . PHE B 2 19  ? 17.649  11.855  10.559  1.00 41.25 ? 34  PHE B CG  1 
ATOM   364  C  CD1 . PHE B 2 19  ? 17.413  12.967  9.756   1.00 37.62 ? 34  PHE B CD1 1 
ATOM   365  C  CD2 . PHE B 2 19  ? 18.458  11.989  11.684  1.00 41.93 ? 34  PHE B CD2 1 
ATOM   366  C  CE1 . PHE B 2 19  ? 17.984  14.190  10.060  1.00 34.85 ? 34  PHE B CE1 1 
ATOM   367  C  CE2 . PHE B 2 19  ? 19.040  13.209  11.995  1.00 33.60 ? 34  PHE B CE2 1 
ATOM   368  C  CZ  . PHE B 2 19  ? 18.797  14.313  11.182  1.00 35.09 ? 34  PHE B CZ  1 
ATOM   369  N  N   . ARG B 2 20  ? 17.624  7.447   9.893   1.00 38.01 ? 35  ARG B N   1 
ATOM   370  C  CA  . ARG B 2 20  ? 16.858  6.348   10.436  1.00 42.71 ? 35  ARG B CA  1 
ATOM   371  C  C   . ARG B 2 20  ? 15.968  6.900   11.542  1.00 44.13 ? 35  ARG B C   1 
ATOM   372  O  O   . ARG B 2 20  ? 16.393  7.754   12.323  1.00 43.54 ? 35  ARG B O   1 
ATOM   373  C  CB  . ARG B 2 20  ? 17.813  5.290   10.972  1.00 42.34 ? 35  ARG B CB  1 
ATOM   374  C  CG  . ARG B 2 20  ? 17.206  4.230   11.795  1.00 46.99 ? 35  ARG B CG  1 
ATOM   375  C  CD  . ARG B 2 20  ? 18.273  3.196   12.028  1.00 53.63 ? 35  ARG B CD  1 
ATOM   376  N  NE  . ARG B 2 20  ? 17.727  1.941   12.529  1.00 60.82 ? 35  ARG B NE  1 
ATOM   377  C  CZ  . ARG B 2 20  ? 18.439  0.833   12.689  1.00 66.99 ? 35  ARG B CZ  1 
ATOM   378  N  NH1 . ARG B 2 20  ? 19.731  0.792   12.388  1.00 64.22 ? 35  ARG B NH1 1 
ATOM   379  N  NH2 . ARG B 2 20  ? 17.843  -0.259  13.169  1.00 68.61 ? 35  ARG B NH2 1 
ATOM   380  N  N   . LYS B 2 21  ? 14.723  6.416   11.598  1.00 50.42 ? 36  LYS B N   1 
ATOM   381  C  CA  . LYS B 2 21  ? 13.752  6.875   12.596  1.00 49.07 ? 36  LYS B CA  1 
ATOM   382  C  C   . LYS B 2 21  ? 14.046  6.305   13.975  1.00 47.74 ? 36  LYS B C   1 
ATOM   383  O  O   . LYS B 2 21  ? 14.060  7.041   14.966  1.00 52.88 ? 36  LYS B O   1 
ATOM   384  C  CB  . LYS B 2 21  ? 12.327  6.499   12.189  1.00 47.60 ? 36  LYS B CB  1 
ATOM   385  C  CG  . LYS B 2 21  ? 11.771  7.323   11.065  1.00 52.21 ? 36  LYS B CG  1 
ATOM   386  C  CD  . LYS B 2 21  ? 10.499  6.715   10.515  1.00 56.28 ? 36  LYS B CD  1 
ATOM   387  C  CE  . LYS B 2 21  ? 9.265   7.225   11.244  1.00 56.86 ? 36  LYS B CE  1 
ATOM   388  N  NZ  . LYS B 2 21  ? 8.032   7.111   10.400  1.00 52.49 ? 36  LYS B NZ  1 
ATOM   389  N  N   . SER B 2 22  A 14.241  4.989   14.061  1.00 47.47 ? 36  SER B N   1 
ATOM   390  C  CA  . SER B 2 22  A 14.353  4.319   15.345  1.00 45.78 ? 36  SER B CA  1 
ATOM   391  C  C   . SER B 2 22  A 15.507  3.324   15.359  1.00 49.70 ? 36  SER B C   1 
ATOM   392  O  O   . SER B 2 22  A 15.475  2.319   14.633  1.00 46.29 ? 36  SER B O   1 
ATOM   393  C  CB  . SER B 2 22  A 13.038  3.610   15.679  1.00 49.03 ? 36  SER B CB  1 
ATOM   394  O  OG  . SER B 2 22  A 13.071  3.022   16.972  1.00 52.67 ? 36  SER B OG  1 
ATOM   395  N  N   . PRO B 2 23  ? 16.573  3.596   16.131  1.00 54.18 ? 37  PRO B N   1 
ATOM   396  C  CA  . PRO B 2 23  ? 16.890  4.856   16.835  1.00 46.79 ? 37  PRO B CA  1 
ATOM   397  C  C   . PRO B 2 23  ? 17.268  5.945   15.829  1.00 47.78 ? 37  PRO B C   1 
ATOM   398  O  O   . PRO B 2 23  ? 17.907  5.668   14.794  1.00 47.03 ? 37  PRO B O   1 
ATOM   399  C  CB  . PRO B 2 23  ? 18.069  4.475   17.748  1.00 41.44 ? 37  PRO B CB  1 
ATOM   400  C  CG  . PRO B 2 23  ? 18.044  2.979   17.839  1.00 48.11 ? 37  PRO B CG  1 
ATOM   401  C  CD  . PRO B 2 23  ? 17.504  2.519   16.510  1.00 54.81 ? 37  PRO B CD  1 
ATOM   402  N  N   . GLN B 2 24  ? 16.851  7.179   16.100  1.00 43.98 ? 38  GLN B N   1 
ATOM   403  C  CA  . GLN B 2 24  ? 17.197  8.310   15.253  1.00 47.58 ? 38  GLN B CA  1 
ATOM   404  C  C   . GLN B 2 24  ? 18.701  8.421   15.044  1.00 45.63 ? 38  GLN B C   1 
ATOM   405  O  O   . GLN B 2 24  ? 19.468  8.534   16.005  1.00 40.93 ? 38  GLN B O   1 
ATOM   406  C  CB  . GLN B 2 24  ? 16.650  9.604   15.861  1.00 44.17 ? 38  GLN B CB  1 
ATOM   407  C  CG  . GLN B 2 24  ? 15.999  10.509  14.823  1.00 49.39 ? 38  GLN B CG  1 
ATOM   408  C  CD  . GLN B 2 24  ? 15.257  11.682  15.429  1.00 54.43 ? 38  GLN B CD  1 
ATOM   409  O  OE1 . GLN B 2 24  ? 14.022  11.712  15.442  1.00 56.62 ? 38  GLN B OE1 1 
ATOM   410  N  NE2 . GLN B 2 24  ? 16.005  12.666  15.917  1.00 55.16 ? 38  GLN B NE2 1 
ATOM   411  N  N   . GLU B 2 25  ? 19.128  8.358   13.784  1.00 44.83 ? 39  GLU B N   1 
ATOM   412  C  CA  . GLU B 2 25  ? 20.504  8.704   13.462  1.00 44.86 ? 39  GLU B CA  1 
ATOM   413  C  C   . GLU B 2 25  ? 20.592  9.227   12.034  1.00 41.83 ? 39  GLU B C   1 
ATOM   414  O  O   . GLU B 2 25  ? 19.919  8.723   11.128  1.00 39.96 ? 39  GLU B O   1 
ATOM   415  C  CB  . GLU B 2 25  ? 21.472  7.528   13.656  1.00 37.62 ? 39  GLU B CB  1 
ATOM   416  C  CG  . GLU B 2 25  ? 21.053  6.216   13.036  1.00 48.74 ? 39  GLU B CG  1 
ATOM   417  C  CD  . GLU B 2 25  ? 22.231  5.250   12.846  1.00 51.87 ? 39  GLU B CD  1 
ATOM   418  O  OE1 . GLU B 2 25  ? 23.398  5.709   12.829  1.00 50.03 ? 39  GLU B OE1 1 
ATOM   419  O  OE2 . GLU B 2 25  ? 21.986  4.025   12.729  1.00 59.40 ? 39  GLU B OE2 1 
ATOM   420  N  N   . LEU B 2 26  ? 21.410  10.267  11.861  1.00 37.93 ? 40  LEU B N   1 
ATOM   421  C  CA  . LEU B 2 26  ? 21.818  10.731  10.545  1.00 38.62 ? 40  LEU B CA  1 
ATOM   422  C  C   . LEU B 2 26  ? 22.533  9.610   9.817   1.00 39.66 ? 40  LEU B C   1 
ATOM   423  O  O   . LEU B 2 26  ? 23.609  9.174   10.245  1.00 37.65 ? 40  LEU B O   1 
ATOM   424  C  CB  . LEU B 2 26  ? 22.743  11.936  10.652  1.00 36.28 ? 40  LEU B CB  1 
ATOM   425  C  CG  . LEU B 2 26  ? 22.876  12.736  9.373   1.00 31.63 ? 40  LEU B CG  1 
ATOM   426  C  CD1 . LEU B 2 26  ? 21.510  13.158  8.884   1.00 33.03 ? 40  LEU B CD1 1 
ATOM   427  C  CD2 . LEU B 2 26  ? 23.714  13.943  9.686   1.00 30.74 ? 40  LEU B CD2 1 
ATOM   428  N  N   . LEU B 2 27  ? 21.921  9.109   8.748   1.00 39.71 ? 41  LEU B N   1 
ATOM   429  C  CA  . LEU B 2 27  ? 22.524  8.079   7.917   1.00 34.17 ? 41  LEU B CA  1 
ATOM   430  C  C   . LEU B 2 27  ? 23.235  8.684   6.720   1.00 36.55 ? 41  LEU B C   1 
ATOM   431  O  O   . LEU B 2 27  ? 24.387  8.328   6.444   1.00 31.53 ? 41  LEU B O   1 
ATOM   432  C  CB  . LEU B 2 27  ? 21.464  7.083   7.423   1.00 35.90 ? 41  LEU B CB  1 
ATOM   433  C  CG  . LEU B 2 27  ? 20.582  6.276   8.381   1.00 36.13 ? 41  LEU B CG  1 
ATOM   434  C  CD1 . LEU B 2 27  ? 19.473  5.595   7.574   1.00 33.77 ? 41  LEU B CD1 1 
ATOM   435  C  CD2 . LEU B 2 27  ? 21.381  5.256   9.197   1.00 34.39 ? 41  LEU B CD2 1 
ATOM   436  N  N   . CYS B 2 28  ? 22.579  9.623   6.021   1.00 39.61 ? 42  CYS B N   1 
ATOM   437  C  CA  . CYS B 2 28  ? 23.101  10.054  4.729   1.00 34.32 ? 42  CYS B CA  1 
ATOM   438  C  C   . CYS B 2 28  ? 22.679  11.474  4.395   1.00 34.59 ? 42  CYS B C   1 
ATOM   439  O  O   . CYS B 2 28  ? 21.848  12.086  5.073   1.00 35.14 ? 42  CYS B O   1 
ATOM   440  C  CB  . CYS B 2 28  ? 22.628  9.126   3.612   1.00 29.90 ? 42  CYS B CB  1 
ATOM   441  S  SG  . CYS B 2 28  ? 23.635  7.691   3.518   0.82 37.20 ? 42  CYS B SG  1 
ATOM   442  N  N   . GLY B 2 29  ? 23.267  11.984  3.305   1.00 38.07 ? 43  GLY B N   1 
ATOM   443  C  CA  . GLY B 2 29  ? 22.767  13.170  2.638   1.00 34.71 ? 43  GLY B CA  1 
ATOM   444  C  C   . GLY B 2 29  ? 21.829  12.822  1.487   1.00 35.14 ? 43  GLY B C   1 
ATOM   445  O  O   . GLY B 2 29  ? 21.615  11.662  1.133   1.00 33.84 ? 43  GLY B O   1 
ATOM   446  N  N   . ALA B 2 30  ? 21.279  13.868  0.887   1.00 31.39 ? 44  ALA B N   1 
ATOM   447  C  CA  . ALA B 2 30  ? 20.293  13.726  -0.176  1.00 34.36 ? 44  ALA B CA  1 
ATOM   448  C  C   . ALA B 2 30  ? 20.034  15.119  -0.732  1.00 36.42 ? 44  ALA B C   1 
ATOM   449  O  O   . ALA B 2 30  ? 20.467  16.120  -0.155  1.00 35.55 ? 44  ALA B O   1 
ATOM   450  C  CB  . ALA B 2 30  ? 19.001  13.093  0.358   1.00 39.19 ? 44  ALA B CB  1 
ATOM   451  N  N   . SER B 2 31  ? 19.276  15.193  -1.823  1.00 33.02 ? 45  SER B N   1 
ATOM   452  C  CA  . SER B 2 31  ? 19.007  16.497  -2.420  1.00 36.69 ? 45  SER B CA  1 
ATOM   453  C  C   . SER B 2 31  ? 17.537  16.625  -2.797  1.00 40.99 ? 45  SER B C   1 
ATOM   454  O  O   . SER B 2 31  ? 16.832  15.633  -2.997  1.00 40.28 ? 45  SER B O   1 
ATOM   455  C  CB  . SER B 2 31  ? 19.880  16.765  -3.655  1.00 33.65 ? 45  SER B CB  1 
ATOM   456  O  OG  . SER B 2 31  ? 19.817  15.681  -4.570  1.00 34.66 ? 45  SER B OG  1 
ATOM   457  N  N   . LEU B 2 32  ? 17.073  17.867  -2.842  1.00 39.33 ? 46  LEU B N   1 
ATOM   458  C  CA  . LEU B 2 32  ? 15.693  18.175  -3.182  1.00 43.91 ? 46  LEU B CA  1 
ATOM   459  C  C   . LEU B 2 32  ? 15.626  18.544  -4.656  1.00 47.01 ? 46  LEU B C   1 
ATOM   460  O  O   . LEU B 2 32  ? 16.295  19.488  -5.095  1.00 45.85 ? 46  LEU B O   1 
ATOM   461  C  CB  . LEU B 2 32  ? 15.153  19.320  -2.326  1.00 39.55 ? 46  LEU B CB  1 
ATOM   462  C  CG  . LEU B 2 32  ? 13.630  19.398  -2.351  1.00 38.37 ? 46  LEU B CG  1 
ATOM   463  C  CD1 . LEU B 2 32  ? 13.055  18.540  -1.240  1.00 36.10 ? 46  LEU B CD1 1 
ATOM   464  C  CD2 . LEU B 2 32  ? 13.143  20.828  -2.262  1.00 41.16 ? 46  LEU B CD2 1 
ATOM   465  N  N   . ILE B 2 33  ? 14.798  17.827  -5.408  1.00 49.40 ? 47  ILE B N   1 
ATOM   466  C  CA  . ILE B 2 33  ? 14.643  18.095  -6.833  1.00 47.07 ? 47  ILE B CA  1 
ATOM   467  C  C   . ILE B 2 33  ? 13.265  18.637  -7.179  1.00 45.67 ? 47  ILE B C   1 
ATOM   468  O  O   . ILE B 2 33  ? 13.091  19.169  -8.288  1.00 42.23 ? 47  ILE B O   1 
ATOM   469  C  CB  . ILE B 2 33  ? 14.952  16.839  -7.673  1.00 47.45 ? 47  ILE B CB  1 
ATOM   470  C  CG1 . ILE B 2 33  ? 14.006  15.696  -7.307  1.00 42.04 ? 47  ILE B CG1 1 
ATOM   471  C  CG2 . ILE B 2 33  ? 16.387  16.407  -7.443  1.00 42.38 ? 47  ILE B CG2 1 
ATOM   472  C  CD1 . ILE B 2 33  ? 14.303  14.416  -8.069  1.00 39.60 ? 47  ILE B CD1 1 
ATOM   473  N  N   . SER B 2 34  ? 12.299  18.549  -6.267  1.00 47.93 ? 48  SER B N   1 
ATOM   474  C  CA  . SER B 2 34  ? 10.990  19.187  -6.384  1.00 46.23 ? 48  SER B CA  1 
ATOM   475  C  C   . SER B 2 34  ? 10.435  19.326  -4.973  1.00 54.93 ? 48  SER B C   1 
ATOM   476  O  O   . SER B 2 34  ? 11.112  18.996  -3.989  1.00 53.43 ? 48  SER B O   1 
ATOM   477  C  CB  . SER B 2 34  ? 10.068  18.392  -7.323  1.00 42.65 ? 48  SER B CB  1 
ATOM   478  O  OG  . SER B 2 34  ? 9.493   17.286  -6.666  1.00 46.39 ? 48  SER B OG  1 
ATOM   479  N  N   . ASP B 2 35  ? 9.178   19.759  -4.870  1.00 55.58 ? 49  ASP B N   1 
ATOM   480  C  CA  . ASP B 2 35  ? 8.585   19.942  -3.547  1.00 55.67 ? 49  ASP B CA  1 
ATOM   481  C  C   . ASP B 2 35  ? 8.328   18.568  -2.951  1.00 54.95 ? 49  ASP B C   1 
ATOM   482  O  O   . ASP B 2 35  ? 8.103   18.443  -1.764  1.00 54.48 ? 49  ASP B O   1 
ATOM   483  C  CB  . ASP B 2 35  ? 7.234   20.673  -3.650  1.00 57.50 ? 49  ASP B CB  1 
ATOM   484  C  CG  . ASP B 2 35  ? 6.255   19.967  -4.564  1.00 59.98 ? 49  ASP B CG  1 
ATOM   485  O  OD1 . ASP B 2 35  ? 6.688   19.285  -5.503  1.00 67.21 ? 49  ASP B OD1 1 
ATOM   486  O  OD2 . ASP B 2 35  ? 5.038   20.128  -4.361  1.00 60.37 ? 49  ASP B OD2 1 
ATOM   487  N  N   . ARG B 2 36  ? 8.325   17.485  -3.747  1.00 53.23 ? 50  ARG B N   1 
ATOM   488  C  CA  . ARG B 2 36  ? 7.917   16.157  -3.184  1.00 53.87 ? 50  ARG B CA  1 
ATOM   489  C  C   . ARG B 2 36  ? 8.939   15.030  -3.400  1.00 51.60 ? 50  ARG B C   1 
ATOM   490  O  O   . ARG B 2 36  ? 8.762   13.965  -2.782  1.00 53.98 ? 50  ARG B O   1 
ATOM   491  C  CB  . ARG B 2 36  ? 6.636   15.638  -3.841  1.00 62.62 ? 50  ARG B CB  1 
ATOM   492  C  CG  . ARG B 2 36  ? 5.407   16.523  -3.723  1.00 63.97 ? 50  ARG B CG  1 
ATOM   493  C  CD  . ARG B 2 36  ? 4.539   16.365  -4.957  1.00 71.21 ? 50  ARG B CD  1 
ATOM   494  N  NE  . ARG B 2 36  ? 3.712   17.549  -5.205  1.00 87.93 ? 50  ARG B NE  1 
ATOM   495  C  CZ  . ARG B 2 36  ? 2.690   17.912  -4.445  1.00 83.26 ? 50  ARG B CZ  1 
ATOM   496  N  NH1 . ARG B 2 36  ? 2.401   19.192  -4.298  1.00 73.81 ? 50  ARG B NH1 1 
ATOM   497  N  NH2 . ARG B 2 36  ? 1.964   16.994  -3.832  1.00 84.31 ? 50  ARG B NH2 1 
ATOM   498  N  N   . TRP B 2 37  ? 9.903   15.206  -4.291  1.00 48.44 ? 51  TRP B N   1 
ATOM   499  C  CA  . TRP B 2 37  ? 10.947  14.246  -4.581  1.00 48.48 ? 51  TRP B CA  1 
ATOM   500  C  C   . TRP B 2 37  ? 12.362  14.532  -4.106  1.00 47.22 ? 51  TRP B C   1 
ATOM   501  O  O   . TRP B 2 37  ? 12.835  15.668  -4.195  1.00 44.81 ? 51  TRP B O   1 
ATOM   502  C  CB  . TRP B 2 37  ? 10.930  14.094  -6.125  1.00 48.09 ? 51  TRP B CB  1 
ATOM   503  C  CG  . TRP B 2 37  ? 9.730   13.332  -6.599  1.00 51.13 ? 51  TRP B CG  1 
ATOM   504  C  CD1 . TRP B 2 37  ? 8.604   13.855  -7.171  1.00 53.56 ? 51  TRP B CD1 1 
ATOM   505  C  CD2 . TRP B 2 37  ? 9.522   11.906  -6.532  1.00 53.74 ? 51  TRP B CD2 1 
ATOM   506  N  NE1 . TRP B 2 37  ? 7.724   12.845  -7.486  1.00 59.65 ? 51  TRP B NE1 1 
ATOM   507  C  CE2 . TRP B 2 37  ? 8.260   11.642  -7.102  1.00 56.88 ? 51  TRP B CE2 1 
ATOM   508  C  CE3 . TRP B 2 37  ? 10.284  10.830  -6.061  1.00 52.18 ? 51  TRP B CE3 1 
ATOM   509  C  CZ2 . TRP B 2 37  ? 7.739   10.345  -7.210  1.00 54.09 ? 51  TRP B CZ2 1 
ATOM   510  C  CZ3 . TRP B 2 37  ? 9.758   9.537   -6.169  1.00 50.90 ? 51  TRP B CZ3 1 
ATOM   511  C  CH2 . TRP B 2 37  ? 8.500   9.312   -6.739  1.00 51.73 ? 51  TRP B CH2 1 
ATOM   512  N  N   . VAL B 2 38  ? 12.985  13.538  -3.493  1.00 44.91 ? 52  VAL B N   1 
ATOM   513  C  CA  . VAL B 2 38  ? 14.313  13.675  -2.931  1.00 46.94 ? 52  VAL B CA  1 
ATOM   514  C  C   . VAL B 2 38  ? 15.189  12.582  -3.527  1.00 45.40 ? 52  VAL B C   1 
ATOM   515  O  O   . VAL B 2 38  ? 14.766  11.424  -3.659  1.00 44.17 ? 52  VAL B O   1 
ATOM   516  C  CB  . VAL B 2 38  ? 14.261  13.616  -1.388  1.00 40.45 ? 52  VAL B CB  1 
ATOM   517  C  CG1 . VAL B 2 38  ? 15.632  13.373  -0.832  1.00 39.17 ? 52  VAL B CG1 1 
ATOM   518  C  CG2 . VAL B 2 38  ? 13.706  14.913  -0.863  1.00 38.45 ? 52  VAL B CG2 1 
ATOM   519  N  N   . LEU B 2 39  ? 16.395  12.971  -3.920  1.00 40.53 ? 53  LEU B N   1 
ATOM   520  C  CA  . LEU B 2 39  ? 17.397  12.091  -4.495  1.00 40.41 ? 53  LEU B CA  1 
ATOM   521  C  C   . LEU B 2 39  ? 18.411  11.678  -3.427  1.00 37.08 ? 53  LEU B C   1 
ATOM   522  O  O   . LEU B 2 39  ? 18.711  12.449  -2.516  1.00 36.54 ? 53  LEU B O   1 
ATOM   523  C  CB  . LEU B 2 39  ? 18.081  12.816  -5.655  1.00 43.00 ? 53  LEU B CB  1 
ATOM   524  C  CG  . LEU B 2 39  ? 18.694  12.117  -6.859  1.00 41.86 ? 53  LEU B CG  1 
ATOM   525  C  CD1 . LEU B 2 39  ? 17.796  11.044  -7.428  1.00 43.16 ? 53  LEU B CD1 1 
ATOM   526  C  CD2 . LEU B 2 39  ? 18.957  13.188  -7.901  1.00 44.75 ? 53  LEU B CD2 1 
ATOM   527  N  N   . THR B 2 40  ? 18.933  10.452  -3.533  1.00 39.94 ? 54  THR B N   1 
ATOM   528  C  CA  . THR B 2 40  ? 19.977  9.993   -2.614  1.00 39.62 ? 54  THR B CA  1 
ATOM   529  C  C   . THR B 2 40  ? 20.683  8.790   -3.230  1.00 40.60 ? 54  THR B C   1 
ATOM   530  O  O   . THR B 2 40  ? 20.408  8.390   -4.365  1.00 40.65 ? 54  THR B O   1 
ATOM   531  C  CB  . THR B 2 40  ? 19.409  9.635   -1.223  1.00 42.58 ? 54  THR B CB  1 
ATOM   532  O  OG1 . THR B 2 40  ? 20.461  9.187   -0.344  1.00 30.19 ? 54  THR B OG1 1 
ATOM   533  C  CG2 . THR B 2 40  ? 18.356  8.527   -1.342  1.00 44.74 ? 54  THR B CG2 1 
ATOM   534  N  N   . ALA B 2 41  ? 21.621  8.234   -2.472  1.00 38.41 ? 55  ALA B N   1 
ATOM   535  C  CA  . ALA B 2 41  ? 22.367  7.058   -2.887  1.00 41.43 ? 55  ALA B CA  1 
ATOM   536  C  C   . ALA B 2 41  ? 21.627  5.801   -2.454  1.00 44.63 ? 55  ALA B C   1 
ATOM   537  O  O   . ALA B 2 41  ? 21.040  5.756   -1.367  1.00 41.57 ? 55  ALA B O   1 
ATOM   538  C  CB  . ALA B 2 41  ? 23.775  7.062   -2.285  1.00 38.11 ? 55  ALA B CB  1 
ATOM   539  N  N   . ALA B 2 42  ? 21.675  4.774   -3.309  1.00 44.42 ? 56  ALA B N   1 
ATOM   540  C  CA  . ALA B 2 42  ? 20.946  3.536   -3.039  1.00 41.39 ? 56  ALA B CA  1 
ATOM   541  C  C   . ALA B 2 42  ? 21.495  2.787   -1.827  1.00 42.42 ? 56  ALA B C   1 
ATOM   542  O  O   . ALA B 2 42  ? 20.719  2.226   -1.045  1.00 43.39 ? 56  ALA B O   1 
ATOM   543  C  CB  . ALA B 2 42  ? 20.967  2.638   -4.276  1.00 45.74 ? 56  ALA B CB  1 
ATOM   544  N  N   . HIS B 2 43  ? 22.823  2.737   -1.657  1.00 41.36 ? 57  HIS B N   1 
ATOM   545  C  CA  . HIS B 2 43  ? 23.378  1.974   -0.539  1.00 40.72 ? 57  HIS B CA  1 
ATOM   546  C  C   . HIS B 2 43  ? 23.061  2.623   0.805   1.00 40.01 ? 57  HIS B C   1 
ATOM   547  O  O   . HIS B 2 43  ? 23.163  1.967   1.848   1.00 36.03 ? 57  HIS B O   1 
ATOM   548  C  CB  . HIS B 2 43  ? 24.890  1.809   -0.695  1.00 39.20 ? 57  HIS B CB  1 
ATOM   549  C  CG  . HIS B 2 43  ? 25.677  2.991   -0.227  1.00 38.73 ? 57  HIS B CG  1 
ATOM   550  N  ND1 . HIS B 2 43  ? 26.183  3.934   -1.094  1.00 40.70 ? 57  HIS B ND1 1 
ATOM   551  C  CD2 . HIS B 2 43  ? 26.045  3.385   1.015   1.00 38.55 ? 57  HIS B CD2 1 
ATOM   552  C  CE1 . HIS B 2 43  ? 26.822  4.861   -0.404  1.00 43.01 ? 57  HIS B CE1 1 
ATOM   553  N  NE2 . HIS B 2 43  ? 26.753  4.552   0.879   1.00 40.33 ? 57  HIS B NE2 1 
ATOM   554  N  N   . CYS B 2 44  ? 22.683  3.898   0.802   1.00 40.98 ? 58  CYS B N   1 
ATOM   555  C  CA  . CYS B 2 44  ? 22.180  4.509   2.020   1.00 42.42 ? 58  CYS B CA  1 
ATOM   556  C  C   . CYS B 2 44  ? 20.928  3.794   2.514   1.00 47.10 ? 58  CYS B C   1 
ATOM   557  O  O   . CYS B 2 44  ? 20.673  3.744   3.725   1.00 50.75 ? 58  CYS B O   1 
ATOM   558  C  CB  . CYS B 2 44  ? 21.895  5.987   1.762   1.00 42.35 ? 58  CYS B CB  1 
ATOM   559  S  SG  . CYS B 2 44  ? 23.385  7.011   1.603   1.00 38.37 ? 58  CYS B SG  1 
ATOM   560  N  N   . LEU B 2 45  ? 20.138  3.279   1.570   1.00 47.57 ? 59  LEU B N   1 
ATOM   561  C  CA  . LEU B 2 45  ? 18.876  2.589   1.938   1.00 46.70 ? 59  LEU B CA  1 
ATOM   562  C  C   . LEU B 2 45  ? 19.143  1.080   2.002   1.00 48.69 ? 59  LEU B C   1 
ATOM   563  O  O   . LEU B 2 45  ? 18.861  0.470   3.057   1.00 50.60 ? 59  LEU B O   1 
ATOM   564  C  CB  . LEU B 2 45  ? 17.792  2.930   0.917   1.00 41.71 ? 59  LEU B CB  1 
ATOM   565  C  CG  . LEU B 2 45  ? 17.616  4.419   0.605   1.00 50.64 ? 59  LEU B CG  1 
ATOM   566  C  CD1 . LEU B 2 45  ? 16.462  4.646   -0.355  1.00 50.91 ? 59  LEU B CD1 1 
ATOM   567  C  CD2 . LEU B 2 45  ? 17.394  5.203   1.883   1.00 48.73 ? 59  LEU B CD2 1 
ATOM   568  N  N   . LEU B 2 46  ? 19.682  0.497   0.925   1.00 45.78 ? 60  LEU B N   1 
ATOM   569  C  CA  . LEU B 2 46  ? 19.866  -0.976  0.848   1.00 46.07 ? 60  LEU B CA  1 
ATOM   570  C  C   . LEU B 2 46  ? 21.345  -1.345  0.681   1.00 44.45 ? 60  LEU B C   1 
ATOM   571  O  O   . LEU B 2 46  ? 21.913  -0.915  -0.353  1.00 45.57 ? 60  LEU B O   1 
ATOM   572  C  CB  . LEU B 2 46  ? 19.063  -1.391  -0.381  1.00 45.90 ? 60  LEU B CB  1 
ATOM   573  C  CG  . LEU B 2 46  ? 18.480  -2.807  -0.435  1.00 47.77 ? 60  LEU B CG  1 
ATOM   574  C  CD1 . LEU B 2 46  ? 18.511  -3.296  -1.871  1.00 43.20 ? 60  LEU B CD1 1 
ATOM   575  C  CD2 . LEU B 2 46  ? 19.117  -3.832  0.479   1.00 50.15 ? 60  LEU B CD2 1 
ATOM   576  N  N   . TYR B 2 47  A 21.911  -2.128  1.619   1.00 40.45 ? 60  TYR B N   1 
ATOM   577  C  CA  . TYR B 2 47  A 23.321  -2.597  1.513   1.00 45.67 ? 60  TYR B CA  1 
ATOM   578  C  C   . TYR B 2 47  A 23.352  -3.911  2.306   1.00 48.51 ? 60  TYR B C   1 
ATOM   579  O  O   . TYR B 2 47  A 23.743  -3.783  3.502   1.00 50.83 ? 60  TYR B O   1 
ATOM   580  C  CB  . TYR B 2 47  A 24.393  -1.618  2.000   1.00 44.13 ? 60  TYR B CB  1 
ATOM   581  C  CG  . TYR B 2 47  A 25.772  -2.033  1.508   1.00 41.24 ? 60  TYR B CG  1 
ATOM   582  C  CD1 . TYR B 2 47  A 26.093  -1.980  0.158   1.00 44.88 ? 60  TYR B CD1 1 
ATOM   583  C  CD2 . TYR B 2 47  A 26.734  -2.516  2.386   1.00 46.79 ? 60  TYR B CD2 1 
ATOM   584  C  CE1 . TYR B 2 47  A 27.340  -2.371  -0.302  1.00 45.18 ? 60  TYR B CE1 1 
ATOM   585  C  CE2 . TYR B 2 47  A 27.984  -2.910  1.939   1.00 50.62 ? 60  TYR B CE2 1 
ATOM   586  C  CZ  . TYR B 2 47  A 28.287  -2.838  0.591   1.00 52.55 ? 60  TYR B CZ  1 
ATOM   587  O  OH  . TYR B 2 47  A 29.517  -3.221  0.143   1.00 49.61 ? 60  TYR B OH  1 
ATOM   588  N  N   . PRO B 2 48  B 22.958  -5.098  1.748   1.00 50.58 ? 60  PRO B N   1 
ATOM   589  C  CA  . PRO B 2 48  B 22.828  -6.334  2.558   1.00 50.50 ? 60  PRO B CA  1 
ATOM   590  C  C   . PRO B 2 48  B 24.082  -6.697  3.341   1.00 54.59 ? 60  PRO B C   1 
ATOM   591  O  O   . PRO B 2 48  B 23.980  -7.002  4.541   1.00 51.26 ? 60  PRO B O   1 
ATOM   592  C  CB  . PRO B 2 48  B 22.498  -7.403  1.505   1.00 46.92 ? 60  PRO B CB  1 
ATOM   593  C  CG  . PRO B 2 48  B 21.836  -6.645  0.398   1.00 46.01 ? 60  PRO B CG  1 
ATOM   594  C  CD  . PRO B 2 48  B 22.521  -5.301  0.353   1.00 51.20 ? 60  PRO B CD  1 
ATOM   595  N  N   . PRO B 2 49  C 25.305  -6.665  2.731   1.00 49.58 ? 60  PRO B N   1 
ATOM   596  C  CA  . PRO B 2 49  C 26.482  -7.118  3.489   1.00 47.09 ? 60  PRO B CA  1 
ATOM   597  C  C   . PRO B 2 49  C 26.642  -6.443  4.845   1.00 55.31 ? 60  PRO B C   1 
ATOM   598  O  O   . PRO B 2 49  C 27.279  -7.010  5.741   1.00 56.09 ? 60  PRO B O   1 
ATOM   599  C  CB  . PRO B 2 49  C 27.651  -6.781  2.557   1.00 49.31 ? 60  PRO B CB  1 
ATOM   600  C  CG  . PRO B 2 49  C 27.066  -6.789  1.206   1.00 48.38 ? 60  PRO B CG  1 
ATOM   601  C  CD  . PRO B 2 49  C 25.685  -6.263  1.360   1.00 48.38 ? 60  PRO B CD  1 
ATOM   602  N  N   . TRP B 2 50  D 26.051  -5.258  5.026   1.00 51.43 ? 60  TRP B N   1 
ATOM   603  C  CA  . TRP B 2 50  D 26.087  -4.553  6.303   1.00 52.84 ? 60  TRP B CA  1 
ATOM   604  C  C   . TRP B 2 50  D 24.753  -4.616  7.051   1.00 61.88 ? 60  TRP B C   1 
ATOM   605  O  O   . TRP B 2 50  D 24.587  -3.924  8.066   1.00 56.17 ? 60  TRP B O   1 
ATOM   606  C  CB  . TRP B 2 50  D 26.471  -3.092  6.085   1.00 50.01 ? 60  TRP B CB  1 
ATOM   607  C  CG  . TRP B 2 50  D 27.867  -2.869  5.679   1.00 51.28 ? 60  TRP B CG  1 
ATOM   608  C  CD1 . TRP B 2 50  D 28.845  -3.805  5.533   1.00 48.56 ? 60  TRP B CD1 1 
ATOM   609  C  CD2 . TRP B 2 50  D 28.459  -1.612  5.355   1.00 51.07 ? 60  TRP B CD2 1 
ATOM   610  N  NE1 . TRP B 2 50  D 30.010  -3.207  5.143   1.00 47.06 ? 60  TRP B NE1 1 
ATOM   611  C  CE2 . TRP B 2 50  D 29.800  -1.859  5.021   1.00 46.42 ? 60  TRP B CE2 1 
ATOM   612  C  CE3 . TRP B 2 50  D 27.980  -0.298  5.306   1.00 46.84 ? 60  TRP B CE3 1 
ATOM   613  C  CZ2 . TRP B 2 50  D 30.670  -0.844  4.646   1.00 41.09 ? 60  TRP B CZ2 1 
ATOM   614  C  CZ3 . TRP B 2 50  D 28.844  0.705   4.935   1.00 41.97 ? 60  TRP B CZ3 1 
ATOM   615  C  CH2 . TRP B 2 50  D 30.174  0.431   4.611   1.00 41.15 ? 60  TRP B CH2 1 
ATOM   616  N  N   . ASP B 2 51  E 23.812  -5.442  6.576   1.00 60.10 ? 60  ASP B N   1 
ATOM   617  C  CA  . ASP B 2 51  E 22.483  -5.593  7.172   1.00 57.97 ? 60  ASP B CA  1 
ATOM   618  C  C   . ASP B 2 51  E 21.653  -4.320  7.043   1.00 56.52 ? 60  ASP B C   1 
ATOM   619  O  O   . ASP B 2 51  E 21.049  -3.868  8.016   1.00 53.32 ? 60  ASP B O   1 
ATOM   620  C  CB  . ASP B 2 51  E 22.563  -6.037  8.632   1.00 60.89 ? 60  ASP B CB  1 
ATOM   621  C  CG  . ASP B 2 51  E 22.148  -7.479  8.813   1.00 70.20 ? 60  ASP B CG  1 
ATOM   622  O  OD1 . ASP B 2 51  E 21.373  -7.982  7.963   1.00 68.69 ? 60  ASP B OD1 1 
ATOM   623  O  OD2 . ASP B 2 51  E 22.620  -8.113  9.787   1.00 77.03 ? 60  ASP B OD2 1 
ATOM   624  N  N   . LYS B 2 52  F 21.657  -3.718  5.850   1.00 56.14 ? 60  LYS B N   1 
ATOM   625  C  CA  . LYS B 2 52  F 20.864  -2.527  5.557   1.00 56.70 ? 60  LYS B CA  1 
ATOM   626  C  C   . LYS B 2 52  F 19.784  -2.861  4.529   1.00 54.45 ? 60  LYS B C   1 
ATOM   627  O  O   . LYS B 2 52  F 20.095  -3.230  3.391   1.00 52.35 ? 60  LYS B O   1 
ATOM   628  C  CB  . LYS B 2 52  F 21.751  -1.385  5.049   1.00 54.73 ? 60  LYS B CB  1 
ATOM   629  C  CG  . LYS B 2 52  F 22.421  -0.558  6.146   1.00 59.29 ? 60  LYS B CG  1 
ATOM   630  C  CD  . LYS B 2 52  F 23.141  0.675   5.565   1.00 65.15 ? 60  LYS B CD  1 
ATOM   631  C  CE  . LYS B 2 52  F 24.278  1.138   6.491   1.00 62.94 ? 60  LYS B CE  1 
ATOM   632  N  NZ  . LYS B 2 52  F 23.819  2.124   7.515   1.00 54.12 ? 60  LYS B NZ  1 
ATOM   633  N  N   . ASN B 2 53  G 18.514  -2.709  4.926   1.00 52.06 ? 60  ASN B N   1 
ATOM   634  C  CA  . ASN B 2 53  G 17.374  -2.837  4.020   1.00 54.83 ? 60  ASN B CA  1 
ATOM   635  C  C   . ASN B 2 53  G 16.234  -2.008  4.617   1.00 53.05 ? 60  ASN B C   1 
ATOM   636  O  O   . ASN B 2 53  G 15.272  -2.538  5.157   1.00 55.06 ? 60  ASN B O   1 
ATOM   637  C  CB  . ASN B 2 53  G 16.976  -4.301  3.803   1.00 53.19 ? 60  ASN B CB  1 
ATOM   638  C  CG  . ASN B 2 53  G 15.918  -4.474  2.724   1.00 54.86 ? 60  ASN B CG  1 
ATOM   639  O  OD1 . ASN B 2 53  G 15.759  -3.612  1.862   1.00 50.72 ? 60  ASN B OD1 1 
ATOM   640  N  ND2 . ASN B 2 53  G 15.222  -5.619  2.736   1.00 64.95 ? 60  ASN B ND2 1 
ATOM   641  N  N   . PHE B 2 54  H 16.357  -0.683  4.513   1.00 55.44 ? 60  PHE B N   1 
ATOM   642  C  CA  . PHE B 2 54  H 15.341  0.243   5.007   1.00 56.49 ? 60  PHE B CA  1 
ATOM   643  C  C   . PHE B 2 54  H 14.202  0.372   4.010   1.00 55.39 ? 60  PHE B C   1 
ATOM   644  O  O   . PHE B 2 54  H 14.405  0.291   2.796   1.00 60.81 ? 60  PHE B O   1 
ATOM   645  C  CB  . PHE B 2 54  H 15.936  1.635   5.277   1.00 49.12 ? 60  PHE B CB  1 
ATOM   646  C  CG  . PHE B 2 54  H 17.006  1.632   6.316   1.00 48.74 ? 60  PHE B CG  1 
ATOM   647  C  CD1 . PHE B 2 54  H 16.740  1.178   7.591   1.00 47.55 ? 60  PHE B CD1 1 
ATOM   648  C  CD2 . PHE B 2 54  H 18.289  2.055   6.014   1.00 53.83 ? 60  PHE B CD2 1 
ATOM   649  C  CE1 . PHE B 2 54  H 17.728  1.145   8.548   1.00 48.89 ? 60  PHE B CE1 1 
ATOM   650  C  CE2 . PHE B 2 54  H 19.288  2.029   6.978   1.00 48.52 ? 60  PHE B CE2 1 
ATOM   651  C  CZ  . PHE B 2 54  H 19.006  1.575   8.242   1.00 46.32 ? 60  PHE B CZ  1 
ATOM   652  N  N   . THR B 2 55  I 12.995  0.571   4.533   1.00 53.20 ? 60  THR B N   1 
ATOM   653  C  CA  . THR B 2 55  I 11.854  0.944   3.704   1.00 62.95 ? 60  THR B CA  1 
ATOM   654  C  C   . THR B 2 55  I 11.308  2.296   4.171   1.00 56.91 ? 60  THR B C   1 
ATOM   655  O  O   . THR B 2 55  I 11.898  2.968   5.019   1.00 54.29 ? 60  THR B O   1 
ATOM   656  C  CB  . THR B 2 55  I 10.771  -0.136  3.728   1.00 60.64 ? 60  THR B CB  1 
ATOM   657  O  OG1 . THR B 2 55  I 10.621  -0.634  5.061   1.00 59.62 ? 60  THR B OG1 1 
ATOM   658  C  CG2 . THR B 2 55  I 11.137  -1.278  2.773   1.00 54.87 ? 60  THR B CG2 1 
ATOM   659  N  N   . GLU B 2 56  ? 10.169  2.688   3.593   1.00 56.38 ? 61  GLU B N   1 
ATOM   660  C  CA  . GLU B 2 56  ? 9.567   3.988   3.885   1.00 58.55 ? 61  GLU B CA  1 
ATOM   661  C  C   . GLU B 2 56  ? 9.418   4.223   5.385   1.00 56.60 ? 61  GLU B C   1 
ATOM   662  O  O   . GLU B 2 56  ? 9.731   5.307   5.885   1.00 55.38 ? 61  GLU B O   1 
ATOM   663  C  CB  . GLU B 2 56  ? 8.199   4.100   3.201   1.00 56.60 ? 61  GLU B CB  1 
ATOM   664  C  CG  . GLU B 2 56  ? 8.207   3.955   1.672   1.00 60.10 ? 61  GLU B CG  1 
ATOM   665  C  CD  . GLU B 2 56  ? 8.500   2.539   1.163   1.00 62.81 ? 61  GLU B CD  1 
ATOM   666  O  OE1 . GLU B 2 56  ? 8.498   2.342   -0.074  1.00 60.06 ? 61  GLU B OE1 1 
ATOM   667  O  OE2 . GLU B 2 56  ? 8.693   1.616   1.989   1.00 68.24 ? 61  GLU B OE2 1 
ATOM   668  N  N   . ASN B 2 57  ? 8.980   3.206   6.123   1.00 54.89 ? 62  ASN B N   1 
ATOM   669  C  CA  . ASN B 2 57  ? 8.648   3.395   7.528   1.00 55.75 ? 62  ASN B CA  1 
ATOM   670  C  C   . ASN B 2 57  ? 9.864   3.518   8.422   1.00 55.10 ? 62  ASN B C   1 
ATOM   671  O  O   . ASN B 2 57  ? 9.711   3.902   9.582   1.00 58.24 ? 62  ASN B O   1 
ATOM   672  C  CB  . ASN B 2 57  ? 7.804   2.221   8.035   1.00 65.11 ? 62  ASN B CB  1 
ATOM   673  C  CG  . ASN B 2 57  ? 6.315   2.430   7.824   1.00 69.71 ? 62  ASN B CG  1 
ATOM   674  O  OD1 . ASN B 2 57  ? 5.885   3.455   7.285   1.00 66.18 ? 62  ASN B OD1 1 
ATOM   675  N  ND2 . ASN B 2 57  ? 5.519   1.450   8.244   1.00 70.79 ? 62  ASN B ND2 1 
ATOM   676  N  N   . ASP B 2 58  ? 11.049  3.178   7.938   1.00 53.92 ? 63  ASP B N   1 
ATOM   677  C  CA  . ASP B 2 58  ? 12.235  3.201   8.780   1.00 51.22 ? 63  ASP B CA  1 
ATOM   678  C  C   . ASP B 2 58  ? 12.978  4.521   8.752   1.00 46.85 ? 63  ASP B C   1 
ATOM   679  O  O   . ASP B 2 58  ? 13.961  4.667   9.479   1.00 49.23 ? 63  ASP B O   1 
ATOM   680  C  CB  . ASP B 2 58  ? 13.190  2.090   8.361   1.00 54.01 ? 63  ASP B CB  1 
ATOM   681  C  CG  . ASP B 2 58  ? 12.509  0.761   8.286   1.00 53.33 ? 63  ASP B CG  1 
ATOM   682  O  OD1 . ASP B 2 58  ? 12.034  0.316   9.347   1.00 52.84 ? 63  ASP B OD1 1 
ATOM   683  O  OD2 . ASP B 2 58  ? 12.437  0.178   7.178   1.00 52.46 ? 63  ASP B OD2 1 
ATOM   684  N  N   . LEU B 2 59  ? 12.553  5.472   7.936   1.00 49.45 ? 64  LEU B N   1 
ATOM   685  C  CA  . LEU B 2 59  ? 13.371  6.632   7.634   1.00 49.59 ? 64  LEU B CA  1 
ATOM   686  C  C   . LEU B 2 59  ? 12.534  7.897   7.707   1.00 50.49 ? 64  LEU B C   1 
ATOM   687  O  O   . LEU B 2 59  ? 11.310  7.871   7.557   1.00 49.03 ? 64  LEU B O   1 
ATOM   688  C  CB  . LEU B 2 59  ? 13.996  6.525   6.243   1.00 47.35 ? 64  LEU B CB  1 
ATOM   689  C  CG  . LEU B 2 59  ? 14.615  5.194   5.852   1.00 45.85 ? 64  LEU B CG  1 
ATOM   690  C  CD1 . LEU B 2 59  ? 14.631  5.095   4.356   1.00 48.83 ? 64  LEU B CD1 1 
ATOM   691  C  CD2 . LEU B 2 59  ? 16.018  5.124   6.396   1.00 48.71 ? 64  LEU B CD2 1 
ATOM   692  N  N   . LEU B 2 60  ? 13.230  9.014   7.905   1.00 47.26 ? 65  LEU B N   1 
ATOM   693  C  CA  . LEU B 2 60  ? 12.644  10.335  7.743   1.00 44.20 ? 65  LEU B CA  1 
ATOM   694  C  C   . LEU B 2 60  ? 13.696  11.252  7.145   1.00 41.09 ? 65  LEU B C   1 
ATOM   695  O  O   . LEU B 2 60  ? 14.881  10.916  7.103   1.00 41.05 ? 65  LEU B O   1 
ATOM   696  C  CB  . LEU B 2 60  ? 12.134  10.896  9.071   1.00 44.92 ? 65  LEU B CB  1 
ATOM   697  C  CG  . LEU B 2 60  ? 13.162  10.960  10.205  1.00 43.93 ? 65  LEU B CG  1 
ATOM   698  C  CD1 . LEU B 2 60  ? 13.931  12.282  10.210  1.00 41.20 ? 65  LEU B CD1 1 
ATOM   699  C  CD2 . LEU B 2 60  ? 12.470  10.767  11.518  1.00 42.91 ? 65  LEU B CD2 1 
ATOM   700  N  N   . VAL B 2 61  ? 13.256  12.410  6.653   1.00 41.51 ? 66  VAL B N   1 
ATOM   701  C  CA  . VAL B 2 61  ? 14.181  13.394  6.108   1.00 41.67 ? 66  VAL B CA  1 
ATOM   702  C  C   . VAL B 2 61  ? 13.964  14.745  6.774   1.00 41.72 ? 66  VAL B C   1 
ATOM   703  O  O   . VAL B 2 61  ? 12.872  15.065  7.260   1.00 42.54 ? 66  VAL B O   1 
ATOM   704  C  CB  . VAL B 2 61  ? 14.057  13.533  4.579   1.00 36.49 ? 66  VAL B CB  1 
ATOM   705  C  CG1 . VAL B 2 61  ? 14.312  12.188  3.918   1.00 42.91 ? 66  VAL B CG1 1 
ATOM   706  C  CG2 . VAL B 2 61  ? 12.705  14.106  4.192   1.00 38.39 ? 66  VAL B CG2 1 
ATOM   707  N  N   . ARG B 2 62  ? 15.024  15.545  6.779   1.00 40.23 ? 67  ARG B N   1 
ATOM   708  C  CA  . ARG B 2 62  ? 14.977  16.917  7.264   1.00 42.77 ? 67  ARG B CA  1 
ATOM   709  C  C   . ARG B 2 62  ? 15.506  17.824  6.171   1.00 42.45 ? 67  ARG B C   1 
ATOM   710  O  O   . ARG B 2 62  ? 16.468  17.487  5.475   1.00 46.74 ? 67  ARG B O   1 
ATOM   711  C  CB  . ARG B 2 62  ? 15.779  17.104  8.570   1.00 41.69 ? 67  ARG B CB  1 
ATOM   712  C  CG  . ARG B 2 62  ? 15.061  16.516  9.761   1.00 39.56 ? 67  ARG B CG  1 
ATOM   713  C  CD  . ARG B 2 62  ? 15.698  16.895  11.069  1.00 45.95 ? 67  ARG B CD  1 
ATOM   714  N  NE  . ARG B 2 62  ? 14.729  16.788  12.155  1.00 43.06 ? 67  ARG B NE  1 
ATOM   715  C  CZ  . ARG B 2 62  ? 14.644  15.754  12.982  1.00 47.80 ? 67  ARG B CZ  1 
ATOM   716  N  NH1 . ARG B 2 62  ? 15.456  14.710  12.874  1.00 40.38 ? 67  ARG B NH1 1 
ATOM   717  N  NH2 . ARG B 2 62  ? 13.728  15.770  13.948  1.00 45.65 ? 67  ARG B NH2 1 
ATOM   718  N  N   . ILE B 2 63  ? 14.834  18.944  5.984   1.00 39.51 ? 68  ILE B N   1 
ATOM   719  C  CA  . ILE B 2 63  ? 15.086  19.833  4.870   1.00 41.59 ? 68  ILE B CA  1 
ATOM   720  C  C   . ILE B 2 63  ? 15.345  21.217  5.437   1.00 43.12 ? 68  ILE B C   1 
ATOM   721  O  O   . ILE B 2 63  ? 14.758  21.588  6.455   1.00 40.77 ? 68  ILE B O   1 
ATOM   722  C  CB  . ILE B 2 63  ? 13.895  19.837  3.890   1.00 42.50 ? 68  ILE B CB  1 
ATOM   723  C  CG1 . ILE B 2 63  ? 13.474  18.404  3.588   1.00 39.47 ? 68  ILE B CG1 1 
ATOM   724  C  CG2 . ILE B 2 63  ? 14.248  20.583  2.601   1.00 41.67 ? 68  ILE B CG2 1 
ATOM   725  C  CD1 . ILE B 2 63  ? 12.303  18.315  2.657   1.00 41.87 ? 68  ILE B CD1 1 
ATOM   726  N  N   . GLY B 2 64  ? 16.301  21.929  4.845   1.00 43.84 ? 69  GLY B N   1 
ATOM   727  C  CA  . GLY B 2 64  ? 16.496  23.334  5.141   1.00 39.07 ? 69  GLY B CA  1 
ATOM   728  C  C   . GLY B 2 64  ? 17.427  23.617  6.295   1.00 42.21 ? 69  GLY B C   1 
ATOM   729  O  O   . GLY B 2 64  ? 17.453  24.753  6.784   1.00 39.67 ? 69  GLY B O   1 
ATOM   730  N  N   . LYS B 2 65  ? 18.199  22.628  6.741   1.00 40.47 ? 70  LYS B N   1 
ATOM   731  C  CA  . LYS B 2 65  ? 19.019  22.770  7.933   1.00 42.67 ? 70  LYS B CA  1 
ATOM   732  C  C   . LYS B 2 65  ? 20.404  23.315  7.588   1.00 45.99 ? 70  LYS B C   1 
ATOM   733  O  O   . LYS B 2 65  ? 20.881  23.219  6.451   1.00 41.21 ? 70  LYS B O   1 
ATOM   734  C  CB  . LYS B 2 65  ? 19.155  21.435  8.671   1.00 39.58 ? 70  LYS B CB  1 
ATOM   735  C  CG  . LYS B 2 65  ? 17.993  21.158  9.598   1.00 41.57 ? 70  LYS B CG  1 
ATOM   736  C  CD  . LYS B 2 65  ? 18.242  20.029  10.597  1.00 46.17 ? 70  LYS B CD  1 
ATOM   737  C  CE  . LYS B 2 65  ? 19.229  20.411  11.686  1.00 46.04 ? 70  LYS B CE  1 
ATOM   738  N  NZ  . LYS B 2 65  ? 18.809  21.588  12.483  1.00 45.32 ? 70  LYS B NZ  1 
ATOM   739  N  N   . HIS B 2 66  ? 21.027  23.935  8.592   1.00 41.35 ? 71  HIS B N   1 
ATOM   740  C  CA  . HIS B 2 66  ? 22.394  24.429  8.494   1.00 40.88 ? 71  HIS B CA  1 
ATOM   741  C  C   . HIS B 2 66  ? 23.287  23.770  9.533   1.00 38.65 ? 71  HIS B C   1 
ATOM   742  O  O   . HIS B 2 66  ? 24.292  23.156  9.170   1.00 41.22 ? 71  HIS B O   1 
ATOM   743  C  CB  . HIS B 2 66  ? 22.435  25.955  8.641   1.00 44.45 ? 71  HIS B CB  1 
ATOM   744  C  CG  . HIS B 2 66  ? 23.798  26.543  8.430   1.00 45.19 ? 71  HIS B CG  1 
ATOM   745  N  ND1 . HIS B 2 66  ? 24.515  27.141  9.442   1.00 47.81 ? 71  HIS B ND1 1 
ATOM   746  C  CD2 . HIS B 2 66  ? 24.572  26.624  7.323   1.00 45.56 ? 71  HIS B CD2 1 
ATOM   747  C  CE1 . HIS B 2 66  ? 25.673  27.564  8.969   1.00 44.54 ? 71  HIS B CE1 1 
ATOM   748  N  NE2 . HIS B 2 66  ? 25.732  27.265  7.685   1.00 44.29 ? 71  HIS B NE2 1 
ATOM   749  N  N   . SER B 2 67  ? 22.945  23.890  10.815  1.00 46.63 ? 72  SER B N   1 
ATOM   750  C  CA  . SER B 2 67  ? 23.666  23.229  11.896  1.00 43.78 ? 72  SER B CA  1 
ATOM   751  C  C   . SER B 2 67  ? 23.231  21.777  12.020  1.00 45.80 ? 72  SER B C   1 
ATOM   752  O  O   . SER B 2 67  ? 22.038  21.472  11.954  1.00 51.90 ? 72  SER B O   1 
ATOM   753  C  CB  . SER B 2 67  ? 23.397  23.932  13.221  1.00 44.02 ? 72  SER B CB  1 
ATOM   754  O  OG  . SER B 2 67  ? 23.458  23.003  14.293  1.00 51.49 ? 72  SER B OG  1 
ATOM   755  N  N   . ARG B 2 68  ? 24.208  20.877  12.185  1.00 48.31 ? 73  ARG B N   1 
ATOM   756  C  CA  . ARG B 2 68  ? 23.887  19.456  12.347  1.00 51.60 ? 73  ARG B CA  1 
ATOM   757  C  C   . ARG B 2 68  ? 22.979  19.209  13.547  1.00 50.74 ? 73  ARG B C   1 
ATOM   758  O  O   . ARG B 2 68  ? 22.041  18.410  13.465  1.00 52.07 ? 73  ARG B O   1 
ATOM   759  C  CB  . ARG B 2 68  ? 25.164  18.624  12.501  1.00 51.79 ? 73  ARG B CB  1 
ATOM   760  C  CG  . ARG B 2 68  ? 24.886  17.135  12.696  1.00 52.49 ? 73  ARG B CG  1 
ATOM   761  C  CD  . ARG B 2 68  ? 26.121  16.267  12.466  1.00 55.45 ? 73  ARG B CD  1 
ATOM   762  N  NE  . ARG B 2 68  ? 27.155  16.479  13.474  1.00 66.63 ? 73  ARG B NE  1 
ATOM   763  C  CZ  . ARG B 2 68  ? 27.153  15.929  14.685  1.00 69.53 ? 73  ARG B CZ  1 
ATOM   764  N  NH1 . ARG B 2 68  ? 26.169  15.137  15.087  1.00 64.30 ? 73  ARG B NH1 1 
ATOM   765  N  NH2 . ARG B 2 68  ? 28.169  16.171  15.511  1.00 65.46 ? 73  ARG B NH2 1 
ATOM   766  N  N   . THR B 2 69  ? 23.234  19.883  14.672  1.00 53.28 ? 74  THR B N   1 
ATOM   767  C  CA  . THR B 2 69  ? 22.550  19.560  15.924  1.00 54.07 ? 74  THR B CA  1 
ATOM   768  C  C   . THR B 2 69  ? 21.417  20.531  16.223  1.00 55.48 ? 74  THR B C   1 
ATOM   769  O  O   . THR B 2 69  ? 20.243  20.150  16.183  1.00 57.68 ? 74  THR B O   1 
ATOM   770  C  CB  . THR B 2 69  ? 23.527  19.562  17.105  1.00 53.64 ? 74  THR B CB  1 
ATOM   771  O  OG1 . THR B 2 69  ? 24.488  20.611  16.925  1.00 64.87 ? 74  THR B OG1 1 
ATOM   772  C  CG2 . THR B 2 69  ? 24.241  18.230  17.209  1.00 58.57 ? 74  THR B CG2 1 
ATOM   773  N  N   . ARG B 2 70  ? 21.756  21.798  16.454  1.00 52.67 ? 75  ARG B N   1 
ATOM   774  C  CA  . ARG B 2 70  ? 20.801  22.773  16.962  1.00 45.82 ? 75  ARG B CA  1 
ATOM   775  C  C   . ARG B 2 70  ? 19.568  22.921  16.067  1.00 52.99 ? 75  ARG B C   1 
ATOM   776  O  O   . ARG B 2 70  ? 19.658  22.943  14.832  1.00 47.38 ? 75  ARG B O   1 
ATOM   777  C  CB  . ARG B 2 70  ? 21.501  24.108  17.113  1.00 45.58 ? 75  ARG B CB  1 
ATOM   778  C  CG  . ARG B 2 70  ? 21.269  24.738  18.440  1.00 57.30 ? 75  ARG B CG  1 
ATOM   779  C  CD  . ARG B 2 70  ? 21.682  23.811  19.578  1.00 52.57 ? 75  ARG B CD  1 
ATOM   780  N  NE  . ARG B 2 70  ? 21.237  24.389  20.843  1.00 51.29 ? 75  ARG B NE  1 
ATOM   781  C  CZ  . ARG B 2 70  ? 21.442  23.851  22.038  1.00 46.52 ? 75  ARG B CZ  1 
ATOM   782  N  NH1 . ARG B 2 70  ? 22.076  22.701  22.183  1.00 38.76 ? 75  ARG B NH1 1 
ATOM   783  N  NH2 . ARG B 2 70  ? 21.051  24.517  23.122  1.00 50.34 ? 75  ARG B NH2 1 
ATOM   784  N  N   . TYR B 2 71  ? 18.406  23.015  16.717  1.00 46.15 ? 76  TYR B N   1 
ATOM   785  C  CA  . TYR B 2 71  ? 17.141  23.213  16.029  1.00 42.71 ? 76  TYR B CA  1 
ATOM   786  C  C   . TYR B 2 71  ? 17.027  24.645  15.523  1.00 45.17 ? 76  TYR B C   1 
ATOM   787  O  O   . TYR B 2 71  ? 17.461  25.591  16.185  1.00 51.45 ? 76  TYR B O   1 
ATOM   788  C  CB  . TYR B 2 71  ? 15.970  22.901  16.967  1.00 37.55 ? 76  TYR B CB  1 
ATOM   789  C  CG  . TYR B 2 71  ? 14.621  23.032  16.282  1.00 41.80 ? 76  TYR B CG  1 
ATOM   790  C  CD1 . TYR B 2 71  ? 14.191  22.081  15.361  1.00 38.91 ? 76  TYR B CD1 1 
ATOM   791  C  CD2 . TYR B 2 71  ? 13.786  24.118  16.535  1.00 39.95 ? 76  TYR B CD2 1 
ATOM   792  C  CE1 . TYR B 2 71  ? 12.974  22.200  14.724  1.00 35.34 ? 76  TYR B CE1 1 
ATOM   793  C  CE2 . TYR B 2 71  ? 12.568  24.238  15.899  1.00 38.54 ? 76  TYR B CE2 1 
ATOM   794  C  CZ  . TYR B 2 71  ? 12.174  23.278  14.993  1.00 39.02 ? 76  TYR B CZ  1 
ATOM   795  O  OH  . TYR B 2 71  ? 10.965  23.392  14.356  1.00 46.77 ? 76  TYR B OH  1 
ATOM   796  N  N   . GLU B 2 72  ? 16.470  24.805  14.324  1.00 44.87 ? 77  GLU B N   1 
ATOM   797  C  CA  . GLU B 2 72  ? 16.426  26.102  13.645  1.00 44.67 ? 77  GLU B CA  1 
ATOM   798  C  C   . GLU B 2 72  ? 14.960  26.471  13.442  1.00 44.16 ? 77  GLU B C   1 
ATOM   799  O  O   . GLU B 2 72  ? 14.377  26.151  12.404  1.00 45.65 ? 77  GLU B O   1 
ATOM   800  C  CB  . GLU B 2 72  ? 17.221  26.039  12.331  1.00 41.45 ? 77  GLU B CB  1 
ATOM   801  C  CG  . GLU B 2 72  ? 18.696  25.716  12.594  1.00 40.64 ? 77  GLU B CG  1 
ATOM   802  C  CD  . GLU B 2 72  ? 19.426  25.099  11.416  1.00 41.96 ? 77  GLU B CD  1 
ATOM   803  O  OE1 . GLU B 2 72  ? 18.772  24.462  10.581  1.00 51.26 ? 77  GLU B OE1 1 
ATOM   804  O  OE2 . GLU B 2 72  ? 20.663  25.212  11.342  1.00 41.54 ? 77  GLU B OE2 1 
ATOM   805  N  N   . ARG B 2 73  A 14.398  27.151  14.456  1.00 43.24 ? 77  ARG B N   1 
ATOM   806  C  CA  . ARG B 2 73  A 12.948  27.493  14.499  1.00 43.02 ? 77  ARG B CA  1 
ATOM   807  C  C   . ARG B 2 73  A 12.443  28.143  13.210  1.00 45.20 ? 77  ARG B C   1 
ATOM   808  O  O   . ARG B 2 73  A 13.096  29.088  12.729  1.00 46.43 ? 77  ARG B O   1 
ATOM   809  C  CB  . ARG B 2 73  A 12.651  28.368  15.724  1.00 50.00 ? 77  ARG B CB  1 
ATOM   810  C  CG  . ARG B 2 73  A 11.175  28.679  15.916  1.00 50.00 ? 77  ARG B CG  1 
ATOM   811  C  CD  . ARG B 2 73  A 10.878  29.173  17.320  1.00 50.00 ? 77  ARG B CD  1 
ATOM   812  N  NE  . ARG B 2 73  A 10.300  28.115  18.154  1.00 50.00 ? 77  ARG B NE  1 
ATOM   813  C  CZ  . ARG B 2 73  A 9.024   28.052  18.505  1.00 50.00 ? 77  ARG B CZ  1 
ATOM   814  N  NH1 . ARG B 2 73  A 8.534   26.937  19.016  1.00 50.00 ? 77  ARG B NH1 1 
ATOM   815  N  NH2 . ARG B 2 73  A 8.245   29.107  18.349  1.00 50.00 ? 77  ARG B NH2 1 
ATOM   816  N  N   . ASN B 2 74  ? 11.329  27.631  12.693  1.00 46.09 ? 78  ASN B N   1 
ATOM   817  C  CA  . ASN B 2 74  ? 10.675  28.158  11.501  1.00 46.55 ? 78  ASN B CA  1 
ATOM   818  C  C   . ASN B 2 74  ? 11.521  28.027  10.240  1.00 50.73 ? 78  ASN B C   1 
ATOM   819  O  O   . ASN B 2 74  ? 11.095  28.513  9.178   1.00 52.99 ? 78  ASN B O   1 
ATOM   820  C  CB  . ASN B 2 74  ? 10.274  29.634  11.648  1.00 50.08 ? 78  ASN B CB  1 
ATOM   821  C  CG  . ASN B 2 74  ? 9.281   29.866  12.773  1.00 56.87 ? 78  ASN B CG  1 
ATOM   822  O  OD1 . ASN B 2 74  ? 8.503   28.978  13.142  1.00 54.11 ? 78  ASN B OD1 1 
ATOM   823  N  ND2 . ASN B 2 74  ? 9.310   31.072  13.330  1.00 52.45 ? 78  ASN B ND2 1 
ATOM   824  N  N   . ILE B 2 75  ? 12.703  27.407  10.307  1.00 45.72 ? 79  ILE B N   1 
ATOM   825  C  CA  . ILE B 2 75  ? 13.538  27.212  9.125   1.00 41.60 ? 79  ILE B CA  1 
ATOM   826  C  C   . ILE B 2 75  ? 13.436  25.766  8.655   1.00 41.43 ? 79  ILE B C   1 
ATOM   827  O  O   . ILE B 2 75  ? 13.019  25.495  7.523   1.00 42.54 ? 79  ILE B O   1 
ATOM   828  C  CB  . ILE B 2 75  ? 15.003  27.598  9.395   1.00 44.51 ? 79  ILE B CB  1 
ATOM   829  C  CG1 . ILE B 2 75  ? 15.090  28.999  10.014  1.00 46.42 ? 79  ILE B CG1 1 
ATOM   830  C  CG2 . ILE B 2 75  ? 15.847  27.472  8.122   1.00 38.52 ? 79  ILE B CG2 1 
ATOM   831  C  CD1 . ILE B 2 75  ? 14.224  30.034  9.344   1.00 45.77 ? 79  ILE B CD1 1 
ATOM   832  N  N   . GLU B 2 76  ? 13.832  24.828  9.507   1.00 37.89 ? 80  GLU B N   1 
ATOM   833  C  CA  . GLU B 2 76  ? 13.923  23.447  9.073   1.00 38.41 ? 80  GLU B CA  1 
ATOM   834  C  C   . GLU B 2 76  ? 12.553  22.806  9.063   1.00 42.42 ? 80  GLU B C   1 
ATOM   835  O  O   . GLU B 2 76  ? 11.685  23.123  9.878   1.00 49.04 ? 80  GLU B O   1 
ATOM   836  C  CB  . GLU B 2 76  ? 14.864  22.639  9.972   1.00 43.62 ? 80  GLU B CB  1 
ATOM   837  C  CG  . GLU B 2 76  ? 14.434  22.458  11.416  1.00 35.15 ? 80  GLU B CG  1 
ATOM   838  C  CD  . GLU B 2 76  ? 15.421  21.606  12.207  1.00 37.61 ? 80  GLU B CD  1 
ATOM   839  O  OE1 . GLU B 2 76  ? 15.336  20.362  12.170  1.00 36.98 ? 80  GLU B OE1 1 
ATOM   840  O  OE2 . GLU B 2 76  ? 16.311  22.176  12.867  1.00 46.83 ? 80  GLU B OE2 1 
ATOM   841  N  N   . LYS B 2 77  ? 12.378  21.868  8.144   1.00 46.08 ? 81  LYS B N   1 
ATOM   842  C  CA  . LYS B 2 77  ? 11.132  21.141  7.998   1.00 44.50 ? 81  LYS B CA  1 
ATOM   843  C  C   . LYS B 2 77  ? 11.429  19.653  8.042   1.00 42.20 ? 81  LYS B C   1 
ATOM   844  O  O   . LYS B 2 77  ? 12.496  19.201  7.622   1.00 47.20 ? 81  LYS B O   1 
ATOM   845  C  CB  . LYS B 2 77  ? 10.418  21.528  6.696   1.00 41.17 ? 81  LYS B CB  1 
ATOM   846  C  CG  . LYS B 2 77  ? 10.134  23.034  6.560   1.00 44.58 ? 81  LYS B CG  1 
ATOM   847  C  CD  . LYS B 2 77  ? 9.214   23.565  7.666   1.00 45.14 ? 81  LYS B CD  1 
ATOM   848  C  CE  . LYS B 2 77  ? 8.884   25.041  7.436   1.00 50.61 ? 81  LYS B CE  1 
ATOM   849  N  NZ  . LYS B 2 77  ? 8.662   25.814  8.709   1.00 50.54 ? 81  LYS B NZ  1 
ATOM   850  N  N   . ILE B 2 78  ? 10.507  18.904  8.610   1.00 39.58 ? 82  ILE B N   1 
ATOM   851  C  CA  . ILE B 2 78  ? 10.646  17.461  8.718   1.00 42.46 ? 82  ILE B CA  1 
ATOM   852  C  C   . ILE B 2 78  ? 9.623   16.826  7.789   1.00 42.29 ? 82  ILE B C   1 
ATOM   853  O  O   . ILE B 2 78  ? 8.567   17.410  7.521   1.00 40.50 ? 82  ILE B O   1 
ATOM   854  C  CB  . ILE B 2 78  ? 10.497  16.979  10.178  1.00 41.27 ? 82  ILE B CB  1 
ATOM   855  C  CG1 . ILE B 2 78  ? 11.571  17.615  11.084  1.00 54.17 ? 82  ILE B CG1 1 
ATOM   856  C  CG2 . ILE B 2 78  ? 10.677  15.485  10.273  1.00 37.71 ? 82  ILE B CG2 1 
ATOM   857  C  CD1 . ILE B 2 78  ? 11.416  19.128  11.454  1.00 52.64 ? 82  ILE B CD1 1 
ATOM   858  N  N   . SER B 2 79  ? 9.981   15.676  7.212   1.00 42.82 ? 83  SER B N   1 
ATOM   859  C  CA  . SER B 2 79  ? 9.024   14.934  6.400   1.00 41.27 ? 83  SER B CA  1 
ATOM   860  C  C   . SER B 2 79  ? 9.250   13.435  6.511   1.00 46.23 ? 83  SER B C   1 
ATOM   861  O  O   . SER B 2 79  ? 10.366  12.953  6.752   1.00 48.31 ? 83  SER B O   1 
ATOM   862  C  CB  . SER B 2 79  ? 9.033   15.307  4.919   1.00 49.26 ? 83  SER B CB  1 
ATOM   863  O  OG  . SER B 2 79  ? 8.113   14.460  4.230   1.00 52.33 ? 83  SER B OG  1 
ATOM   864  N  N   . MET B 2 80  ? 8.145   12.715  6.375   1.00 47.42 ? 84  MET B N   1 
ATOM   865  C  CA  . MET B 2 80  ? 8.121   11.271  6.292   1.00 48.01 ? 84  MET B CA  1 
ATOM   866  C  C   . MET B 2 80  ? 8.172   10.865  4.823   1.00 47.11 ? 84  MET B C   1 
ATOM   867  O  O   . MET B 2 80  ? 8.021   11.697  3.919   1.00 44.90 ? 84  MET B O   1 
ATOM   868  C  CB  . MET B 2 80  ? 6.860   10.751  6.985   1.00 44.18 ? 84  MET B CB  1 
ATOM   869  C  CG  . MET B 2 80  ? 6.877   10.965  8.488   1.00 37.53 ? 84  MET B CG  1 
ATOM   870  S  SD  . MET B 2 80  ? 8.229   10.076  9.267   1.00 54.53 ? 84  MET B SD  1 
ATOM   871  C  CE  . MET B 2 80  ? 8.417   10.935  10.822  1.00 47.93 ? 84  MET B CE  1 
ATOM   872  N  N   . LEU B 2 81  ? 8.361   9.573   4.580   1.00 45.56 ? 85  LEU B N   1 
ATOM   873  C  CA  . LEU B 2 81  ? 8.513   9.076   3.220   1.00 51.53 ? 85  LEU B CA  1 
ATOM   874  C  C   . LEU B 2 81  ? 7.291   8.264   2.822   1.00 51.95 ? 85  LEU B C   1 
ATOM   875  O  O   . LEU B 2 81  ? 6.920   7.312   3.514   1.00 49.96 ? 85  LEU B O   1 
ATOM   876  C  CB  . LEU B 2 81  ? 9.781   8.231   3.072   1.00 50.96 ? 85  LEU B CB  1 
ATOM   877  C  CG  . LEU B 2 81  ? 11.100  9.012   3.065   1.00 52.35 ? 85  LEU B CG  1 
ATOM   878  C  CD1 . LEU B 2 81  ? 10.947  10.322  2.311   1.00 40.87 ? 85  LEU B CD1 1 
ATOM   879  C  CD2 . LEU B 2 81  ? 11.612  9.250   4.473   1.00 52.65 ? 85  LEU B CD2 1 
ATOM   880  N  N   . GLU B 2 82  ? 6.683   8.635   1.692   1.00 58.07 ? 86  GLU B N   1 
ATOM   881  C  CA  . GLU B 2 82  ? 5.606   7.841   1.114   1.00 53.92 ? 86  GLU B CA  1 
ATOM   882  C  C   . GLU B 2 82  ? 6.143   6.643   0.350   1.00 54.75 ? 86  GLU B C   1 
ATOM   883  O  O   . GLU B 2 82  ? 5.646   5.525   0.522   1.00 58.45 ? 86  GLU B O   1 
ATOM   884  C  CB  . GLU B 2 82  ? 4.741   8.700   0.198   1.00 59.51 ? 86  GLU B CB  1 
ATOM   885  C  CG  . GLU B 2 82  ? 3.556   7.953   -0.391  1.00 61.80 ? 86  GLU B CG  1 
ATOM   886  C  CD  . GLU B 2 82  ? 2.823   8.762   -1.445  1.00 68.30 ? 86  GLU B CD  1 
ATOM   887  O  OE1 . GLU B 2 82  ? 2.511   9.955   -1.186  1.00 64.43 ? 86  GLU B OE1 1 
ATOM   888  O  OE2 . GLU B 2 82  ? 2.571   8.201   -2.536  1.00 71.35 ? 86  GLU B OE2 1 
ATOM   889  N  N   . LYS B 2 83  ? 7.170   6.837   -0.480  1.00 56.13 ? 87  LYS B N   1 
ATOM   890  C  CA  . LYS B 2 83  ? 7.650   5.688   -1.250  1.00 58.35 ? 87  LYS B CA  1 
ATOM   891  C  C   . LYS B 2 83  ? 9.155   5.766   -1.482  1.00 51.94 ? 87  LYS B C   1 
ATOM   892  O  O   . LYS B 2 83  ? 9.715   6.850   -1.632  1.00 52.89 ? 87  LYS B O   1 
ATOM   893  C  CB  . LYS B 2 83  ? 6.916   5.570   -2.602  1.00 58.03 ? 87  LYS B CB  1 
ATOM   894  C  CG  . LYS B 2 83  ? 6.467   4.144   -2.970  1.00 59.33 ? 87  LYS B CG  1 
ATOM   895  C  CD  . LYS B 2 83  ? 5.574   3.541   -1.883  1.00 70.59 ? 87  LYS B CD  1 
ATOM   896  C  CE  . LYS B 2 83  ? 5.669   2.015   -1.813  1.00 73.26 ? 87  LYS B CE  1 
ATOM   897  N  NZ  . LYS B 2 83  ? 4.902   1.481   -0.636  1.00 66.45 ? 87  LYS B NZ  1 
ATOM   898  N  N   . ILE B 2 84  ? 9.797   4.589   -1.527  1.00 55.77 ? 88  ILE B N   1 
ATOM   899  C  CA  . ILE B 2 84  ? 11.227  4.424   -1.815  1.00 54.30 ? 88  ILE B CA  1 
ATOM   900  C  C   . ILE B 2 84  ? 11.368  3.683   -3.143  1.00 50.25 ? 88  ILE B C   1 
ATOM   901  O  O   . ILE B 2 84  ? 10.694  2.675   -3.366  1.00 54.31 ? 88  ILE B O   1 
ATOM   902  C  CB  . ILE B 2 84  ? 11.940  3.644   -0.683  1.00 50.75 ? 88  ILE B CB  1 
ATOM   903  C  CG1 . ILE B 2 84  ? 12.586  4.557   0.357   1.00 53.82 ? 88  ILE B CG1 1 
ATOM   904  C  CG2 . ILE B 2 84  ? 13.013  2.720   -1.225  1.00 54.63 ? 88  ILE B CG2 1 
ATOM   905  C  CD1 . ILE B 2 84  ? 11.669  5.542   1.012   1.00 57.51 ? 88  ILE B CD1 1 
ATOM   906  N  N   . TYR B 2 85  ? 12.265  4.147   -4.012  1.00 49.28 ? 89  TYR B N   1 
ATOM   907  C  CA  . TYR B 2 85  ? 12.509  3.501   -5.303  1.00 48.91 ? 89  TYR B CA  1 
ATOM   908  C  C   . TYR B 2 85  ? 14.005  3.326   -5.532  1.00 46.88 ? 89  TYR B C   1 
ATOM   909  O  O   . TYR B 2 85  ? 14.715  4.310   -5.773  1.00 51.81 ? 89  TYR B O   1 
ATOM   910  C  CB  . TYR B 2 85  ? 11.906  4.315   -6.447  1.00 54.26 ? 89  TYR B CB  1 
ATOM   911  C  CG  . TYR B 2 85  ? 10.445  4.661   -6.281  1.00 62.31 ? 89  TYR B CG  1 
ATOM   912  C  CD1 . TYR B 2 85  ? 10.056  5.784   -5.556  1.00 58.31 ? 89  TYR B CD1 1 
ATOM   913  C  CD2 . TYR B 2 85  ? 9.451   3.875   -6.865  1.00 62.12 ? 89  TYR B CD2 1 
ATOM   914  C  CE1 . TYR B 2 85  ? 8.721   6.111   -5.409  1.00 59.52 ? 89  TYR B CE1 1 
ATOM   915  C  CE2 . TYR B 2 85  ? 8.110   4.192   -6.722  1.00 61.35 ? 89  TYR B CE2 1 
ATOM   916  C  CZ  . TYR B 2 85  ? 7.750   5.311   -5.992  1.00 63.37 ? 89  TYR B CZ  1 
ATOM   917  O  OH  . TYR B 2 85  ? 6.419   5.638   -5.838  1.00 67.35 ? 89  TYR B OH  1 
ATOM   918  N  N   . ILE B 2 86  ? 14.483  2.088   -5.471  1.00 44.59 ? 90  ILE B N   1 
ATOM   919  C  CA  . ILE B 2 86  ? 15.867  1.766   -5.811  1.00 45.05 ? 90  ILE B CA  1 
ATOM   920  C  C   . ILE B 2 86  ? 15.946  1.456   -7.297  1.00 50.83 ? 90  ILE B C   1 
ATOM   921  O  O   . ILE B 2 86  ? 15.008  0.900   -7.872  1.00 57.70 ? 90  ILE B O   1 
ATOM   922  C  CB  . ILE B 2 86  ? 16.389  0.574   -4.985  1.00 42.77 ? 90  ILE B CB  1 
ATOM   923  C  CG1 . ILE B 2 86  ? 15.984  0.711   -3.516  1.00 48.07 ? 90  ILE B CG1 1 
ATOM   924  C  CG2 . ILE B 2 86  ? 17.895  0.397   -5.174  1.00 44.09 ? 90  ILE B CG2 1 
ATOM   925  C  CD1 . ILE B 2 86  ? 16.646  1.830   -2.806  1.00 50.12 ? 90  ILE B CD1 1 
ATOM   926  N  N   . HIS B 2 87  ? 17.051  1.824   -7.939  1.00 50.56 ? 91  HIS B N   1 
ATOM   927  C  CA  . HIS B 2 87  ? 17.258  1.395   -9.314  1.00 50.10 ? 91  HIS B CA  1 
ATOM   928  C  C   . HIS B 2 87  ? 17.275  -0.132  -9.342  1.00 53.65 ? 91  HIS B C   1 
ATOM   929  O  O   . HIS B 2 87  ? 17.933  -0.752  -8.493  1.00 47.08 ? 91  HIS B O   1 
ATOM   930  C  CB  . HIS B 2 87  ? 18.560  1.958   -9.878  1.00 53.45 ? 91  HIS B CB  1 
ATOM   931  C  CG  . HIS B 2 87  ? 18.630  1.961   -11.376 1.00 52.14 ? 91  HIS B CG  1 
ATOM   932  N  ND1 . HIS B 2 87  ? 19.005  0.853   -12.106 1.00 57.21 ? 91  HIS B ND1 1 
ATOM   933  C  CD2 . HIS B 2 87  ? 18.390  2.943   -12.279 1.00 51.21 ? 91  HIS B CD2 1 
ATOM   934  C  CE1 . HIS B 2 87  ? 18.981  1.150   -13.394 1.00 56.48 ? 91  HIS B CE1 1 
ATOM   935  N  NE2 . HIS B 2 87  ? 18.609  2.411   -13.526 1.00 50.47 ? 91  HIS B NE2 1 
ATOM   936  N  N   . PRO B 2 88  ? 16.512  -0.771  -10.241 1.00 56.87 ? 92  PRO B N   1 
ATOM   937  C  CA  . PRO B 2 88  ? 16.465  -2.244  -10.255 1.00 51.43 ? 92  PRO B CA  1 
ATOM   938  C  C   . PRO B 2 88  ? 17.783  -2.892  -10.639 1.00 60.63 ? 92  PRO B C   1 
ATOM   939  O  O   . PRO B 2 88  ? 17.997  -4.067  -10.308 1.00 59.10 ? 92  PRO B O   1 
ATOM   940  C  CB  . PRO B 2 88  ? 15.364  -2.549  -11.278 1.00 48.65 ? 92  PRO B CB  1 
ATOM   941  C  CG  . PRO B 2 88  ? 15.309  -1.347  -12.144 1.00 51.43 ? 92  PRO B CG  1 
ATOM   942  C  CD  . PRO B 2 88  ? 15.622  -0.180  -11.255 1.00 53.23 ? 92  PRO B CD  1 
ATOM   943  N  N   . ARG B 2 89  ? 18.677  -2.173  -11.319 1.00 57.39 ? 93  ARG B N   1 
ATOM   944  C  CA  . ARG B 2 89  ? 19.967  -2.720  -11.707 1.00 57.27 ? 93  ARG B CA  1 
ATOM   945  C  C   . ARG B 2 89  ? 21.107  -2.215  -10.814 1.00 56.38 ? 93  ARG B C   1 
ATOM   946  O  O   . ARG B 2 89  ? 22.275  -2.256  -11.220 1.00 53.40 ? 93  ARG B O   1 
ATOM   947  C  CB  . ARG B 2 89  ? 20.224  -2.412  -13.185 1.00 61.01 ? 93  ARG B CB  1 
ATOM   948  C  CG  . ARG B 2 89  ? 19.289  -3.201  -14.116 1.00 60.97 ? 93  ARG B CG  1 
ATOM   949  C  CD  . ARG B 2 89  ? 19.769  -3.310  -15.566 1.00 51.68 ? 93  ARG B CD  1 
ATOM   950  N  NE  . ARG B 2 89  ? 20.085  -2.036  -16.218 1.00 65.07 ? 93  ARG B NE  1 
ATOM   951  C  CZ  . ARG B 2 89  ? 19.244  -1.019  -16.418 1.00 71.78 ? 93  ARG B CZ  1 
ATOM   952  N  NH1 . ARG B 2 89  ? 19.629  0.081   -17.053 1.00 70.03 ? 93  ARG B NH1 1 
ATOM   953  N  NH2 . ARG B 2 89  ? 17.986  -1.105  -15.978 1.00 65.53 ? 93  ARG B NH2 1 
ATOM   954  N  N   . TYR B 2 90  ? 20.781  -1.707  -9.622  1.00 54.89 ? 94  TYR B N   1 
ATOM   955  C  CA  . TYR B 2 90  ? 21.783  -1.381  -8.607  1.00 52.41 ? 94  TYR B CA  1 
ATOM   956  C  C   . TYR B 2 90  ? 22.565  -2.619  -8.185  1.00 48.23 ? 94  TYR B C   1 
ATOM   957  O  O   . TYR B 2 90  ? 21.982  -3.620  -7.762  1.00 51.06 ? 94  TYR B O   1 
ATOM   958  C  CB  . TYR B 2 90  ? 21.090  -0.743  -7.404  1.00 48.29 ? 94  TYR B CB  1 
ATOM   959  C  CG  . TYR B 2 90  ? 21.866  -0.707  -6.102  1.00 48.16 ? 94  TYR B CG  1 
ATOM   960  C  CD1 . TYR B 2 90  ? 23.096  -0.048  -6.001  1.00 49.39 ? 94  TYR B CD1 1 
ATOM   961  C  CD2 . TYR B 2 90  ? 21.342  -1.285  -4.955  1.00 46.09 ? 94  TYR B CD2 1 
ATOM   962  C  CE1 . TYR B 2 90  ? 23.784  0.002   -4.798  1.00 45.32 ? 94  TYR B CE1 1 
ATOM   963  C  CE2 . TYR B 2 90  ? 22.015  -1.231  -3.759  1.00 45.20 ? 94  TYR B CE2 1 
ATOM   964  C  CZ  . TYR B 2 90  ? 23.231  -0.587  -3.685  1.00 45.21 ? 94  TYR B CZ  1 
ATOM   965  O  OH  . TYR B 2 90  ? 23.886  -0.545  -2.482  1.00 45.46 ? 94  TYR B OH  1 
ATOM   966  N  N   . ASN B 2 91  ? 23.890  -2.529  -8.270  1.00 45.23 ? 95  ASN B N   1 
ATOM   967  C  CA  . ASN B 2 91  ? 24.805  -3.656  -8.086  1.00 48.35 ? 95  ASN B CA  1 
ATOM   968  C  C   . ASN B 2 91  ? 25.634  -3.458  -6.812  1.00 50.27 ? 95  ASN B C   1 
ATOM   969  O  O   . ASN B 2 91  ? 26.751  -2.943  -6.864  1.00 49.03 ? 95  ASN B O   1 
ATOM   970  C  CB  . ASN B 2 91  ? 25.700  -3.781  -9.325  1.00 50.73 ? 95  ASN B CB  1 
ATOM   971  C  CG  . ASN B 2 91  ? 26.636  -4.980  -9.275  1.00 52.88 ? 95  ASN B CG  1 
ATOM   972  O  OD1 . ASN B 2 91  ? 26.822  -5.620  -8.233  1.00 53.58 ? 95  ASN B OD1 1 
ATOM   973  N  ND2 . ASN B 2 91  ? 27.261  -5.269  -10.413 1.00 53.28 ? 95  ASN B ND2 1 
ATOM   974  N  N   . TRP B 2 92  ? 25.098  -3.899  -5.673  1.00 47.49 ? 96  TRP B N   1 
ATOM   975  C  CA  . TRP B 2 92  ? 25.800  -3.792  -4.403  1.00 44.32 ? 96  TRP B CA  1 
ATOM   976  C  C   . TRP B 2 92  ? 26.758  -4.952  -4.146  1.00 51.22 ? 96  TRP B C   1 
ATOM   977  O  O   . TRP B 2 92  ? 27.556  -4.888  -3.200  1.00 49.44 ? 96  TRP B O   1 
ATOM   978  C  CB  . TRP B 2 92  ? 24.808  -3.711  -3.261  1.00 43.71 ? 96  TRP B CB  1 
ATOM   979  C  CG  . TRP B 2 92  ? 23.766  -4.774  -3.348  1.00 51.44 ? 96  TRP B CG  1 
ATOM   980  C  CD1 . TRP B 2 92  ? 22.556  -4.676  -3.966  1.00 52.28 ? 96  TRP B CD1 1 
ATOM   981  C  CD2 . TRP B 2 92  ? 23.858  -6.120  -2.847  1.00 52.91 ? 96  TRP B CD2 1 
ATOM   982  N  NE1 . TRP B 2 92  ? 21.871  -5.867  -3.853  1.00 55.90 ? 96  TRP B NE1 1 
ATOM   983  C  CE2 . TRP B 2 92  ? 22.650  -6.771  -3.176  1.00 53.88 ? 96  TRP B CE2 1 
ATOM   984  C  CE3 . TRP B 2 92  ? 24.841  -6.834  -2.143  1.00 56.15 ? 96  TRP B CE3 1 
ATOM   985  C  CZ2 . TRP B 2 92  ? 22.394  -8.099  -2.829  1.00 52.98 ? 96  TRP B CZ2 1 
ATOM   986  C  CZ3 . TRP B 2 92  ? 24.577  -8.167  -1.791  1.00 53.26 ? 96  TRP B CZ3 1 
ATOM   987  C  CH2 . TRP B 2 92  ? 23.365  -8.774  -2.137  1.00 55.65 ? 96  TRP B CH2 1 
ATOM   988  N  N   . ARG B 2 93  ? 26.688  -5.984  -4.977  1.00 51.62 ? 97  ARG B N   1 
ATOM   989  C  CA  . ARG B 2 93  ? 27.553  -7.163  -4.754  1.00 52.84 ? 97  ARG B CA  1 
ATOM   990  C  C   . ARG B 2 93  ? 28.914  -6.928  -5.410  1.00 51.17 ? 97  ARG B C   1 
ATOM   991  O  O   . ARG B 2 93  ? 29.872  -7.608  -4.960  1.00 53.53 ? 97  ARG B O   1 
ATOM   992  C  CB  . ARG B 2 93  ? 26.891  -8.402  -5.359  1.00 60.97 ? 97  ARG B CB  1 
ATOM   993  C  CG  . ARG B 2 93  ? 26.783  -9.577  -4.400  1.00 70.16 ? 97  ARG B CG  1 
ATOM   994  C  CD  . ARG B 2 93  ? 25.548  -10.410 -4.694  1.00 64.83 ? 97  ARG B CD  1 
ATOM   995  N  NE  . ARG B 2 93  ? 25.865  -11.838 -4.792  1.00 79.02 ? 97  ARG B NE  1 
ATOM   996  C  CZ  . ARG B 2 93  ? 25.728  -12.709 -3.800  1.00 81.45 ? 97  ARG B CZ  1 
ATOM   997  N  NH1 . ARG B 2 93  ? 25.301  -12.304 -2.617  1.00 81.93 ? 97  ARG B NH1 1 
ATOM   998  N  NH2 . ARG B 2 93  ? 26.015  -13.983 -3.996  1.00 78.12 ? 97  ARG B NH2 1 
ATOM   999  N  N   . GLU B 2 94  A 28.998  -5.997  -6.375  1.00 49.78 ? 97  GLU B N   1 
ATOM   1000 C  CA  . GLU B 2 94  A 30.213  -5.801  -7.144  1.00 51.42 ? 97  GLU B CA  1 
ATOM   1001 C  C   . GLU B 2 94  A 30.840  -4.463  -6.796  1.00 50.89 ? 97  GLU B C   1 
ATOM   1002 O  O   . GLU B 2 94  A 31.883  -4.423  -6.146  1.00 48.23 ? 97  GLU B O   1 
ATOM   1003 C  CB  . GLU B 2 94  A 29.907  -5.927  -8.642  1.00 54.15 ? 97  GLU B CB  1 
ATOM   1004 C  CG  . GLU B 2 94  A 31.038  -5.492  -9.577  1.00 54.90 ? 97  GLU B CG  1 
ATOM   1005 C  CD  . GLU B 2 94  A 30.781  -5.861  -11.042 1.00 60.87 ? 97  GLU B CD  1 
ATOM   1006 O  OE1 . GLU B 2 94  A 29.733  -6.491  -11.332 1.00 67.12 ? 97  GLU B OE1 1 
ATOM   1007 O  OE2 . GLU B 2 94  A 31.643  -5.552  -11.894 1.00 57.88 ? 97  GLU B OE2 1 
ATOM   1008 N  N   . ASN B 2 95  ? 30.217  -3.362  -7.240  1.00 46.86 ? 98  ASN B N   1 
ATOM   1009 C  CA  . ASN B 2 95  ? 30.908  -2.078  -7.266  1.00 42.54 ? 98  ASN B CA  1 
ATOM   1010 C  C   . ASN B 2 95  ? 29.983  -0.888  -7.040  1.00 45.32 ? 98  ASN B C   1 
ATOM   1011 O  O   . ASN B 2 95  ? 30.339  0.228   -7.442  1.00 45.40 ? 98  ASN B O   1 
ATOM   1012 C  CB  . ASN B 2 95  ? 31.578  -1.885  -8.608  1.00 46.40 ? 98  ASN B CB  1 
ATOM   1013 C  CG  . ASN B 2 95  ? 30.589  -2.009  -9.760  1.00 49.77 ? 98  ASN B CG  1 
ATOM   1014 O  OD1 . ASN B 2 95  ? 29.428  -2.372  -9.555  1.00 48.25 ? 98  ASN B OD1 1 
ATOM   1015 N  ND2 . ASN B 2 95  ? 31.035  -1.689  -10.967 1.00 48.73 ? 98  ASN B ND2 1 
ATOM   1016 N  N   . LEU B 2 96  ? 28.785  -1.098  -6.494  1.00 44.90 ? 99  LEU B N   1 
ATOM   1017 C  CA  . LEU B 2 96  ? 27.796  -0.032  -6.300  1.00 45.91 ? 99  LEU B CA  1 
ATOM   1018 C  C   . LEU B 2 96  ? 27.410  0.643   -7.615  1.00 46.59 ? 99  LEU B C   1 
ATOM   1019 O  O   . LEU B 2 96  ? 27.059  1.831   -7.628  1.00 43.00 ? 99  LEU B O   1 
ATOM   1020 C  CB  . LEU B 2 96  ? 28.294  1.012   -5.303  1.00 43.11 ? 99  LEU B CB  1 
ATOM   1021 C  CG  . LEU B 2 96  ? 28.605  0.445   -3.931  1.00 42.22 ? 99  LEU B CG  1 
ATOM   1022 C  CD1 . LEU B 2 96  ? 29.274  1.528   -3.086  1.00 39.61 ? 99  LEU B CD1 1 
ATOM   1023 C  CD2 . LEU B 2 96  ? 27.297  -0.029  -3.318  1.00 39.10 ? 99  LEU B CD2 1 
ATOM   1024 N  N   . ASP B 2 97  ? 27.437  -0.106  -8.723  1.00 43.82 ? 100 ASP B N   1 
ATOM   1025 C  CA  . ASP B 2 97  ? 27.010  0.461   -9.997  1.00 45.31 ? 100 ASP B CA  1 
ATOM   1026 C  C   . ASP B 2 97  ? 25.547  0.872   -9.905  1.00 44.81 ? 100 ASP B C   1 
ATOM   1027 O  O   . ASP B 2 97  ? 24.714  0.139   -9.362  1.00 43.21 ? 100 ASP B O   1 
ATOM   1028 C  CB  . ASP B 2 97  ? 27.213  -0.544  -11.137 1.00 46.41 ? 100 ASP B CB  1 
ATOM   1029 C  CG  . ASP B 2 97  ? 27.029  0.074   -12.528 1.00 43.31 ? 100 ASP B CG  1 
ATOM   1030 O  OD1 . ASP B 2 97  ? 27.094  1.311   -12.685 1.00 40.37 ? 100 ASP B OD1 1 
ATOM   1031 O  OD2 . ASP B 2 97  ? 26.826  -0.700  -13.484 1.00 48.61 ? 100 ASP B OD2 1 
ATOM   1032 N  N   . ARG B 2 98  ? 25.253  2.071   -10.418 1.00 42.65 ? 101 ARG B N   1 
ATOM   1033 C  CA  . ARG B 2 98  ? 23.912  2.654   -10.381 1.00 45.30 ? 101 ARG B CA  1 
ATOM   1034 C  C   . ARG B 2 98  ? 23.471  2.883   -8.934  1.00 46.52 ? 101 ARG B C   1 
ATOM   1035 O  O   . ARG B 2 98  ? 22.370  2.505   -8.525  1.00 48.43 ? 101 ARG B O   1 
ATOM   1036 C  CB  . ARG B 2 98  ? 22.902  1.786   -11.148 1.00 44.31 ? 101 ARG B CB  1 
ATOM   1037 C  CG  . ARG B 2 98  ? 23.335  1.417   -12.571 1.00 50.22 ? 101 ARG B CG  1 
ATOM   1038 C  CD  . ARG B 2 98  ? 22.458  0.329   -13.229 1.00 54.21 ? 101 ARG B CD  1 
ATOM   1039 N  NE  . ARG B 2 98  ? 23.176  -0.340  -14.312 1.00 57.19 ? 101 ARG B NE  1 
ATOM   1040 C  CZ  . ARG B 2 98  ? 23.132  0.016   -15.591 1.00 60.23 ? 101 ARG B CZ  1 
ATOM   1041 N  NH1 . ARG B 2 98  ? 22.343  0.998   -16.015 1.00 55.35 ? 101 ARG B NH1 1 
ATOM   1042 N  NH2 . ARG B 2 98  ? 23.931  -0.601  -16.459 1.00 58.19 ? 101 ARG B NH2 1 
ATOM   1043 N  N   . ASP B 2 99  ? 24.355  3.507   -8.150  1.00 42.31 ? 102 ASP B N   1 
ATOM   1044 C  CA  . ASP B 2 99  ? 24.093  3.767   -6.733  1.00 42.71 ? 102 ASP B CA  1 
ATOM   1045 C  C   . ASP B 2 99  ? 23.188  4.992   -6.627  1.00 40.86 ? 102 ASP B C   1 
ATOM   1046 O  O   . ASP B 2 99  ? 23.620  6.104   -6.313  1.00 40.66 ? 102 ASP B O   1 
ATOM   1047 C  CB  . ASP B 2 99  ? 25.397  3.962   -5.964  1.00 42.48 ? 102 ASP B CB  1 
ATOM   1048 C  CG  . ASP B 2 99  ? 25.204  3.894   -4.452  1.00 42.24 ? 102 ASP B CG  1 
ATOM   1049 O  OD1 . ASP B 2 99  ? 24.065  3.625   -4.001  1.00 38.65 ? 102 ASP B OD1 1 
ATOM   1050 O  OD2 . ASP B 2 99  ? 26.195  4.103   -3.715  1.00 38.87 ? 102 ASP B OD2 1 
ATOM   1051 N  N   . ILE B 2 100 ? 21.894  4.773   -6.860  1.00 39.85 ? 103 ILE B N   1 
ATOM   1052 C  CA  . ILE B 2 100 ? 20.924  5.858   -6.940  1.00 41.19 ? 103 ILE B CA  1 
ATOM   1053 C  C   . ILE B 2 100 ? 19.587  5.424   -6.349  1.00 45.39 ? 103 ILE B C   1 
ATOM   1054 O  O   . ILE B 2 100 ? 19.212  4.245   -6.389  1.00 47.85 ? 103 ILE B O   1 
ATOM   1055 C  CB  . ILE B 2 100 ? 20.735  6.328   -8.395  1.00 40.42 ? 103 ILE B CB  1 
ATOM   1056 C  CG1 . ILE B 2 100 ? 20.006  7.669   -8.430  1.00 39.01 ? 103 ILE B CG1 1 
ATOM   1057 C  CG2 . ILE B 2 100 ? 19.979  5.276   -9.201  1.00 41.92 ? 103 ILE B CG2 1 
ATOM   1058 C  CD1 . ILE B 2 100 ? 20.122  8.385   -9.737  1.00 37.23 ? 103 ILE B CD1 1 
ATOM   1059 N  N   . ALA B 2 101 ? 18.860  6.391   -5.795  1.00 42.52 ? 104 ALA B N   1 
ATOM   1060 C  CA  . ALA B 2 101 ? 17.578  6.077   -5.183  1.00 43.06 ? 104 ALA B CA  1 
ATOM   1061 C  C   . ALA B 2 101 ? 16.721  7.328   -5.119  1.00 44.56 ? 104 ALA B C   1 
ATOM   1062 O  O   . ALA B 2 101 ? 17.229  8.445   -4.939  1.00 44.07 ? 104 ALA B O   1 
ATOM   1063 C  CB  . ALA B 2 101 ? 17.755  5.488   -3.779  1.00 41.66 ? 104 ALA B CB  1 
ATOM   1064 N  N   . LEU B 2 102 ? 15.409  7.119   -5.235  1.00 47.88 ? 105 LEU B N   1 
ATOM   1065 C  CA  . LEU B 2 102 ? 14.430  8.193   -5.164  1.00 49.09 ? 105 LEU B CA  1 
ATOM   1066 C  C   . LEU B 2 102 ? 13.495  7.984   -3.978  1.00 48.19 ? 105 LEU B C   1 
ATOM   1067 O  O   . LEU B 2 102 ? 13.061  6.864   -3.705  1.00 49.57 ? 105 LEU B O   1 
ATOM   1068 C  CB  . LEU B 2 102 ? 13.635  8.256   -6.459  1.00 47.27 ? 105 LEU B CB  1 
ATOM   1069 C  CG  . LEU B 2 102 ? 14.182  9.211   -7.512  1.00 47.49 ? 105 LEU B CG  1 
ATOM   1070 C  CD1 . LEU B 2 102 ? 13.302  9.176   -8.750  1.00 59.57 ? 105 LEU B CD1 1 
ATOM   1071 C  CD2 . LEU B 2 102 ? 14.233  10.621  -6.963  1.00 47.78 ? 105 LEU B CD2 1 
ATOM   1072 N  N   . MET B 2 103 ? 13.169  9.061   -3.275  1.00 47.71 ? 106 MET B N   1 
ATOM   1073 C  CA  . MET B 2 103 ? 12.230  8.988   -2.166  1.00 46.27 ? 106 MET B CA  1 
ATOM   1074 C  C   . MET B 2 103 ? 11.159  10.046  -2.372  1.00 52.34 ? 106 MET B C   1 
ATOM   1075 O  O   . MET B 2 103 ? 11.476  11.227  -2.576  1.00 48.92 ? 106 MET B O   1 
ATOM   1076 C  CB  . MET B 2 103 ? 12.931  9.175   -0.821  1.00 41.97 ? 106 MET B CB  1 
ATOM   1077 C  CG  . MET B 2 103 ? 14.294  8.512   -0.750  1.00 42.53 ? 106 MET B CG  1 
ATOM   1078 S  SD  . MET B 2 103 ? 14.987  8.461   0.919   1.00 46.02 ? 106 MET B SD  1 
ATOM   1079 C  CE  . MET B 2 103 ? 15.920  9.998   0.943   1.00 40.30 ? 106 MET B CE  1 
ATOM   1080 N  N   . LYS B 2 104 ? 9.897   9.603   -2.360  1.00 53.52 ? 107 LYS B N   1 
ATOM   1081 C  CA  . LYS B 2 104 ? 8.728   10.469  -2.474  1.00 53.81 ? 107 LYS B CA  1 
ATOM   1082 C  C   . LYS B 2 104 ? 8.217   10.748  -1.070  1.00 49.17 ? 107 LYS B C   1 
ATOM   1083 O  O   . LYS B 2 104 ? 7.909   9.808   -0.321  1.00 51.49 ? 107 LYS B O   1 
ATOM   1084 C  CB  . LYS B 2 104 ? 7.639   9.811   -3.320  1.00 54.04 ? 107 LYS B CB  1 
ATOM   1085 C  CG  . LYS B 2 104 ? 6.246   10.429  -3.212  1.00 55.91 ? 107 LYS B CG  1 
ATOM   1086 C  CD  . LYS B 2 104 ? 5.535   10.381  -4.568  1.00 57.51 ? 107 LYS B CD  1 
ATOM   1087 C  CE  . LYS B 2 104 ? 4.016   10.575  -4.483  1.00 67.93 ? 107 LYS B CE  1 
ATOM   1088 N  NZ  . LYS B 2 104 ? 3.548   11.311  -3.260  1.00 71.23 ? 107 LYS B NZ  1 
ATOM   1089 N  N   . LEU B 2 105 ? 8.139   12.033  -0.730  1.00 46.42 ? 108 LEU B N   1 
ATOM   1090 C  CA  . LEU B 2 105 ? 7.713   12.499  0.585   1.00 56.06 ? 108 LEU B CA  1 
ATOM   1091 C  C   . LEU B 2 105 ? 6.201   12.395  0.786   1.00 59.55 ? 108 LEU B C   1 
ATOM   1092 O  O   . LEU B 2 105 ? 5.420   12.660  -0.135  1.00 63.21 ? 108 LEU B O   1 
ATOM   1093 C  CB  . LEU B 2 105 ? 8.148   13.952  0.764   1.00 53.37 ? 108 LEU B CB  1 
ATOM   1094 C  CG  . LEU B 2 105 ? 9.539   14.310  0.242   1.00 49.97 ? 108 LEU B CG  1 
ATOM   1095 C  CD1 . LEU B 2 105 ? 9.718   15.828  0.215   1.00 54.40 ? 108 LEU B CD1 1 
ATOM   1096 C  CD2 . LEU B 2 105 ? 10.592  13.661  1.099   1.00 41.14 ? 108 LEU B CD2 1 
ATOM   1097 N  N   . LYS B 2 106 ? 5.792   12.082  2.025   1.00 57.54 ? 109 LYS B N   1 
ATOM   1098 C  CA  . LYS B 2 106 ? 4.365   12.022  2.353   1.00 60.45 ? 109 LYS B CA  1 
ATOM   1099 C  C   . LYS B 2 106 ? 3.679   13.353  2.085   1.00 64.54 ? 109 LYS B C   1 
ATOM   1100 O  O   . LYS B 2 106 ? 2.576   13.392  1.520   1.00 65.22 ? 109 LYS B O   1 
ATOM   1101 C  CB  . LYS B 2 106 ? 4.159   11.630  3.819   1.00 48.26 ? 109 LYS B CB  1 
ATOM   1102 C  CG  . LYS B 2 106 ? 4.077   10.133  4.043   1.00 60.21 ? 109 LYS B CG  1 
ATOM   1103 C  CD  . LYS B 2 106 ? 2.727   9.687   4.585   1.00 60.15 ? 109 LYS B CD  1 
ATOM   1104 C  CE  . LYS B 2 106 ? 2.770   8.219   5.008   1.00 57.80 ? 109 LYS B CE  1 
ATOM   1105 N  NZ  . LYS B 2 106 ? 3.305   8.012   6.383   1.00 57.46 ? 109 LYS B NZ  1 
ATOM   1106 N  N   . LYS B 2 107 ? 4.337   14.458  2.442   1.00 62.98 ? 110 LYS B N   1 
ATOM   1107 C  CA  . LYS B 2 107 ? 3.746   15.770  2.283   1.00 63.49 ? 110 LYS B CA  1 
ATOM   1108 C  C   . LYS B 2 107 ? 4.745   16.677  1.568   1.00 63.28 ? 110 LYS B C   1 
ATOM   1109 O  O   . LYS B 2 107 ? 5.892   16.831  2.034   1.00 57.07 ? 110 LYS B O   1 
ATOM   1110 C  CB  . LYS B 2 107 ? 3.387   16.390  3.645   1.00 70.24 ? 110 LYS B CB  1 
ATOM   1111 C  CG  . LYS B 2 107 ? 1.972   16.136  4.154   1.00 74.80 ? 110 LYS B CG  1 
ATOM   1112 C  CD  . LYS B 2 107 ? 1.965   16.159  5.677   1.00 69.03 ? 110 LYS B CD  1 
ATOM   1113 C  CE  . LYS B 2 107 ? 0.614   16.576  6.213   1.00 72.96 ? 110 LYS B CE  1 
ATOM   1114 N  NZ  . LYS B 2 107 ? 0.500   18.065  6.272   1.00 76.79 ? 110 LYS B NZ  1 
ATOM   1115 N  N   . PRO B 2 108 ? 4.317   17.344  0.504   1.00 57.06 ? 111 PRO B N   1 
ATOM   1116 C  CA  . PRO B 2 108 ? 5.186   18.321  -0.151  1.00 56.17 ? 111 PRO B CA  1 
ATOM   1117 C  C   . PRO B 2 108 ? 5.678   19.362  0.841   1.00 59.01 ? 111 PRO B C   1 
ATOM   1118 O  O   . PRO B 2 108 ? 4.945   19.793  1.734   1.00 63.12 ? 111 PRO B O   1 
ATOM   1119 C  CB  . PRO B 2 108 ? 4.276   18.939  -1.215  1.00 56.78 ? 111 PRO B CB  1 
ATOM   1120 C  CG  . PRO B 2 108 ? 2.872   18.512  -0.826  1.00 59.33 ? 111 PRO B CG  1 
ATOM   1121 C  CD  . PRO B 2 108 ? 3.045   17.177  -0.207  1.00 56.67 ? 111 PRO B CD  1 
ATOM   1122 N  N   . VAL B 2 109 ? 6.948   19.736  0.699   1.00 51.85 ? 112 VAL B N   1 
ATOM   1123 C  CA  . VAL B 2 109 ? 7.532   20.759  1.550   1.00 47.66 ? 112 VAL B CA  1 
ATOM   1124 C  C   . VAL B 2 109 ? 7.357   22.103  0.867   1.00 49.55 ? 112 VAL B C   1 
ATOM   1125 O  O   . VAL B 2 109 ? 7.337   22.202  -0.369  1.00 50.20 ? 112 VAL B O   1 
ATOM   1126 C  CB  . VAL B 2 109 ? 9.015   20.466  1.849   1.00 44.70 ? 112 VAL B CB  1 
ATOM   1127 C  CG1 . VAL B 2 109 ? 9.844   20.545  0.568   1.00 44.05 ? 112 VAL B CG1 1 
ATOM   1128 C  CG2 . VAL B 2 109 ? 9.534   21.426  2.910   1.00 44.58 ? 112 VAL B CG2 1 
ATOM   1129 N  N   . ALA B 2 110 ? 7.216   23.151  1.677   1.00 43.14 ? 113 ALA B N   1 
ATOM   1130 C  CA  . ALA B 2 110 ? 7.081   24.499  1.156   1.00 41.60 ? 113 ALA B CA  1 
ATOM   1131 C  C   . ALA B 2 110 ? 8.468   25.088  0.973   1.00 44.07 ? 113 ALA B C   1 
ATOM   1132 O  O   . ALA B 2 110 ? 9.325   24.978  1.860   1.00 43.69 ? 113 ALA B O   1 
ATOM   1133 C  CB  . ALA B 2 110 ? 6.248   25.380  2.086   1.00 32.38 ? 113 ALA B CB  1 
ATOM   1134 N  N   . PHE B 2 111 ? 8.678   25.721  -0.172  1.00 43.54 ? 114 PHE B N   1 
ATOM   1135 C  CA  . PHE B 2 111 ? 9.948   26.366  -0.415  1.00 42.45 ? 114 PHE B CA  1 
ATOM   1136 C  C   . PHE B 2 111 ? 10.037  27.628  0.434   1.00 42.94 ? 114 PHE B C   1 
ATOM   1137 O  O   . PHE B 2 111 ? 9.036   28.163  0.920   1.00 48.84 ? 114 PHE B O   1 
ATOM   1138 C  CB  . PHE B 2 111 ? 10.120  26.688  -1.900  1.00 39.53 ? 114 PHE B CB  1 
ATOM   1139 C  CG  . PHE B 2 111 ? 10.078  25.471  -2.801  1.00 40.33 ? 114 PHE B CG  1 
ATOM   1140 C  CD1 . PHE B 2 111 ? 10.432  24.218  -2.326  1.00 42.42 ? 114 PHE B CD1 1 
ATOM   1141 C  CD2 . PHE B 2 111 ? 9.680   25.583  -4.127  1.00 41.58 ? 114 PHE B CD2 1 
ATOM   1142 C  CE1 . PHE B 2 111 ? 10.389  23.094  -3.165  1.00 43.36 ? 114 PHE B CE1 1 
ATOM   1143 C  CE2 . PHE B 2 111 ? 9.638   24.470  -4.963  1.00 37.14 ? 114 PHE B CE2 1 
ATOM   1144 C  CZ  . PHE B 2 111 ? 9.994   23.225  -4.476  1.00 36.76 ? 114 PHE B CZ  1 
ATOM   1145 N  N   . SER B 2 112 ? 11.264  28.061  0.664   1.00 44.81 ? 115 SER B N   1 
ATOM   1146 C  CA  . SER B 2 112 ? 11.542  29.217  1.498   1.00 44.28 ? 115 SER B CA  1 
ATOM   1147 C  C   . SER B 2 112 ? 12.911  29.732  1.087   1.00 46.07 ? 115 SER B C   1 
ATOM   1148 O  O   . SER B 2 112 ? 13.527  29.210  0.151   1.00 48.30 ? 115 SER B O   1 
ATOM   1149 C  CB  . SER B 2 112 ? 11.498  28.843  2.982   1.00 40.65 ? 115 SER B CB  1 
ATOM   1150 O  OG  . SER B 2 112 ? 12.627  28.049  3.310   1.00 40.60 ? 115 SER B OG  1 
ATOM   1151 N  N   . ASP B 2 113 ? 13.420  30.717  1.823   1.00 42.99 ? 116 ASP B N   1 
ATOM   1152 C  CA  . ASP B 2 113 ? 14.779  31.160  1.571   1.00 40.54 ? 116 ASP B CA  1 
ATOM   1153 C  C   . ASP B 2 113 ? 15.780  30.037  1.793   1.00 43.81 ? 116 ASP B C   1 
ATOM   1154 O  O   . ASP B 2 113 ? 16.896  30.108  1.265   1.00 45.80 ? 116 ASP B O   1 
ATOM   1155 C  CB  . ASP B 2 113 ? 15.124  32.350  2.469   1.00 39.08 ? 116 ASP B CB  1 
ATOM   1156 C  CG  . ASP B 2 113 ? 14.544  33.652  1.965   1.00 45.90 ? 116 ASP B CG  1 
ATOM   1157 O  OD1 . ASP B 2 113 ? 13.777  33.628  0.969   1.00 50.26 ? 116 ASP B OD1 1 
ATOM   1158 O  OD2 . ASP B 2 113 ? 14.856  34.705  2.566   1.00 46.51 ? 116 ASP B OD2 1 
ATOM   1159 N  N   . TYR B 2 114 ? 15.399  28.990  2.536   1.00 37.56 ? 117 TYR B N   1 
ATOM   1160 C  CA  . TYR B 2 114 ? 16.312  27.924  2.923   1.00 35.21 ? 117 TYR B CA  1 
ATOM   1161 C  C   . TYR B 2 114 ? 16.000  26.583  2.279   1.00 36.74 ? 117 TYR B C   1 
ATOM   1162 O  O   . TYR B 2 114 ? 16.765  25.629  2.461   1.00 43.30 ? 117 TYR B O   1 
ATOM   1163 C  CB  . TYR B 2 114 ? 16.308  27.766  4.454   1.00 39.08 ? 117 TYR B CB  1 
ATOM   1164 C  CG  . TYR B 2 114 ? 16.363  29.088  5.160   1.00 41.32 ? 117 TYR B CG  1 
ATOM   1165 C  CD1 . TYR B 2 114 ? 17.577  29.730  5.375   1.00 44.86 ? 117 TYR B CD1 1 
ATOM   1166 C  CD2 . TYR B 2 114 ? 15.202  29.723  5.583   1.00 42.77 ? 117 TYR B CD2 1 
ATOM   1167 C  CE1 . TYR B 2 114 ? 17.636  30.965  6.021   1.00 41.45 ? 117 TYR B CE1 1 
ATOM   1168 C  CE2 . TYR B 2 114 ? 15.255  30.958  6.218   1.00 42.78 ? 117 TYR B CE2 1 
ATOM   1169 C  CZ  . TYR B 2 114 ? 16.474  31.570  6.430   1.00 41.20 ? 117 TYR B CZ  1 
ATOM   1170 O  OH  . TYR B 2 114 ? 16.532  32.791  7.052   1.00 48.19 ? 117 TYR B OH  1 
ATOM   1171 N  N   . ILE B 2 115 ? 14.903  26.476  1.543   1.00 41.89 ? 118 ILE B N   1 
ATOM   1172 C  CA  . ILE B 2 115 ? 14.444  25.215  0.987   1.00 43.54 ? 118 ILE B CA  1 
ATOM   1173 C  C   . ILE B 2 115 ? 14.076  25.480  -0.465  1.00 45.12 ? 118 ILE B C   1 
ATOM   1174 O  O   . ILE B 2 115 ? 13.132  26.232  -0.747  1.00 44.46 ? 118 ILE B O   1 
ATOM   1175 C  CB  . ILE B 2 115 ? 13.257  24.638  1.768   1.00 42.76 ? 118 ILE B CB  1 
ATOM   1176 C  CG1 . ILE B 2 115 ? 13.720  24.245  3.174   1.00 38.67 ? 118 ILE B CG1 1 
ATOM   1177 C  CG2 . ILE B 2 115 ? 12.668  23.450  1.022   1.00 39.01 ? 118 ILE B CG2 1 
ATOM   1178 C  CD1 . ILE B 2 115 ? 12.629  23.712  4.069   1.00 43.93 ? 118 ILE B CD1 1 
ATOM   1179 N  N   . HIS B 2 116 ? 14.850  24.902  -1.387  1.00 41.02 ? 119 HIS B N   1 
ATOM   1180 C  CA  . HIS B 2 116 ? 14.680  25.189  -2.803  1.00 40.98 ? 119 HIS B CA  1 
ATOM   1181 C  C   . HIS B 2 116 ? 15.328  24.102  -3.650  1.00 43.34 ? 119 HIS B C   1 
ATOM   1182 O  O   . HIS B 2 116 ? 16.455  23.683  -3.340  1.00 36.78 ? 119 HIS B O   1 
ATOM   1183 C  CB  . HIS B 2 116 ? 15.275  26.550  -3.146  1.00 38.70 ? 119 HIS B CB  1 
ATOM   1184 C  CG  . HIS B 2 116 ? 14.938  27.017  -4.523  1.00 48.81 ? 119 HIS B CG  1 
ATOM   1185 N  ND1 . HIS B 2 116 ? 13.835  27.797  -4.796  1.00 50.13 ? 119 HIS B ND1 1 
ATOM   1186 C  CD2 . HIS B 2 116 ? 15.554  26.804  -5.710  1.00 48.72 ? 119 HIS B CD2 1 
ATOM   1187 C  CE1 . HIS B 2 116 ? 13.791  28.053  -6.091  1.00 50.83 ? 119 HIS B CE1 1 
ATOM   1188 N  NE2 . HIS B 2 116 ? 14.824  27.463  -6.668  1.00 53.98 ? 119 HIS B NE2 1 
ATOM   1189 N  N   . PRO B 2 117 ? 14.656  23.634  -4.707  1.00 42.33 ? 120 PRO B N   1 
ATOM   1190 C  CA  . PRO B 2 117 ? 15.144  22.475  -5.470  1.00 43.03 ? 120 PRO B CA  1 
ATOM   1191 C  C   . PRO B 2 117 ? 16.267  22.804  -6.450  1.00 42.29 ? 120 PRO B C   1 
ATOM   1192 O  O   . PRO B 2 117 ? 16.390  23.924  -6.961  1.00 39.09 ? 120 PRO B O   1 
ATOM   1193 C  CB  . PRO B 2 117 ? 13.893  22.016  -6.227  1.00 38.76 ? 120 PRO B CB  1 
ATOM   1194 C  CG  . PRO B 2 117 ? 13.163  23.264  -6.461  1.00 37.24 ? 120 PRO B CG  1 
ATOM   1195 C  CD  . PRO B 2 117 ? 13.382  24.131  -5.241  1.00 42.10 ? 120 PRO B CD  1 
ATOM   1196 N  N   . VAL B 2 118 ? 17.107  21.778  -6.704  1.00 37.95 ? 121 VAL B N   1 
ATOM   1197 C  CA  . VAL B 2 118 ? 18.207  21.863  -7.657  1.00 38.62 ? 121 VAL B CA  1 
ATOM   1198 C  C   . VAL B 2 118 ? 17.722  21.329  -9.000  1.00 42.71 ? 121 VAL B C   1 
ATOM   1199 O  O   . VAL B 2 118 ? 16.813  20.495  -9.060  1.00 44.66 ? 121 VAL B O   1 
ATOM   1200 C  CB  . VAL B 2 118 ? 19.440  21.090  -7.130  1.00 37.17 ? 121 VAL B CB  1 
ATOM   1201 C  CG1 . VAL B 2 118 ? 19.224  19.581  -7.232  1.00 35.36 ? 121 VAL B CG1 1 
ATOM   1202 C  CG2 . VAL B 2 118 ? 20.717  21.517  -7.846  1.00 34.55 ? 121 VAL B CG2 1 
ATOM   1203 N  N   . CYS B 2 119 ? 18.324  21.808  -10.091 1.00 42.33 ? 122 CYS B N   1 
ATOM   1204 C  CA  . CYS B 2 119 ? 17.977  21.331  -11.422 1.00 38.05 ? 122 CYS B CA  1 
ATOM   1205 C  C   . CYS B 2 119 ? 18.637  19.993  -11.700 1.00 44.88 ? 122 CYS B C   1 
ATOM   1206 O  O   . CYS B 2 119 ? 19.775  19.745  -11.284 1.00 43.75 ? 122 CYS B O   1 
ATOM   1207 C  CB  . CYS B 2 119 ? 18.436  22.313  -12.497 1.00 38.69 ? 122 CYS B CB  1 
ATOM   1208 S  SG  . CYS B 2 119 ? 17.834  23.974  -12.361 1.00 45.86 ? 122 CYS B SG  1 
ATOM   1209 N  N   . LEU B 2 120 ? 17.917  19.132  -12.445 1.00 44.43 ? 123 LEU B N   1 
ATOM   1210 C  CA  . LEU B 2 120 ? 18.595  18.003  -13.061 1.00 42.86 ? 123 LEU B CA  1 
ATOM   1211 C  C   . LEU B 2 120 ? 19.100  18.395  -14.444 1.00 44.11 ? 123 LEU B C   1 
ATOM   1212 O  O   . LEU B 2 120 ? 18.488  19.225  -15.122 1.00 43.82 ? 123 LEU B O   1 
ATOM   1213 C  CB  . LEU B 2 120 ? 17.661  16.811  -13.167 1.00 41.41 ? 123 LEU B CB  1 
ATOM   1214 C  CG  . LEU B 2 120 ? 17.326  16.249  -11.783 1.00 46.29 ? 123 LEU B CG  1 
ATOM   1215 C  CD1 . LEU B 2 120 ? 16.665  14.875  -11.869 1.00 43.59 ? 123 LEU B CD1 1 
ATOM   1216 C  CD2 . LEU B 2 120 ? 18.611  16.191  -10.934 1.00 47.35 ? 123 LEU B CD2 1 
ATOM   1217 N  N   . PRO B 2 121 ? 20.238  17.865  -14.881 1.00 44.28 ? 124 PRO B N   1 
ATOM   1218 C  CA  . PRO B 2 121 ? 20.803  18.320  -16.154 1.00 43.80 ? 124 PRO B CA  1 
ATOM   1219 C  C   . PRO B 2 121 ? 20.121  17.673  -17.350 1.00 46.77 ? 124 PRO B C   1 
ATOM   1220 O  O   . PRO B 2 121 ? 19.805  16.477  -17.351 1.00 40.48 ? 124 PRO B O   1 
ATOM   1221 C  CB  . PRO B 2 121 ? 22.269  17.884  -16.060 1.00 45.44 ? 124 PRO B CB  1 
ATOM   1222 C  CG  . PRO B 2 121 ? 22.221  16.658  -15.167 1.00 45.72 ? 124 PRO B CG  1 
ATOM   1223 C  CD  . PRO B 2 121 ? 21.094  16.873  -14.198 1.00 41.12 ? 124 PRO B CD  1 
ATOM   1224 N  N   . ASP B 2 122 ? 19.927  18.488  -18.384 1.00 46.42 ? 125 ASP B N   1 
ATOM   1225 C  CA  . ASP B 2 122 ? 19.574  18.021  -19.714 1.00 49.08 ? 125 ASP B CA  1 
ATOM   1226 C  C   . ASP B 2 122 ? 20.838  17.535  -20.419 1.00 47.61 ? 125 ASP B C   1 
ATOM   1227 O  O   . ASP B 2 122 ? 21.947  17.592  -19.880 1.00 48.65 ? 125 ASP B O   1 
ATOM   1228 C  CB  . ASP B 2 122 ? 18.899  19.138  -20.514 1.00 43.71 ? 125 ASP B CB  1 
ATOM   1229 C  CG  . ASP B 2 122 ? 19.778  20.377  -20.639 1.00 51.57 ? 125 ASP B CG  1 
ATOM   1230 O  OD1 . ASP B 2 122 ? 20.130  20.967  -19.592 1.00 57.82 ? 125 ASP B OD1 1 
ATOM   1231 O  OD2 . ASP B 2 122 ? 20.136  20.762  -21.772 1.00 52.42 ? 125 ASP B OD2 1 
ATOM   1232 N  N   . ARG B 2 123 ? 20.683  17.072  -21.653 1.00 48.46 ? 126 ARG B N   1 
ATOM   1233 C  CA  . ARG B 2 123 ? 21.822  16.486  -22.349 1.00 48.25 ? 126 ARG B CA  1 
ATOM   1234 C  C   . ARG B 2 123 ? 22.897  17.523  -22.628 1.00 47.25 ? 126 ARG B C   1 
ATOM   1235 O  O   . ARG B 2 123 ? 24.076  17.297  -22.340 1.00 48.07 ? 126 ARG B O   1 
ATOM   1236 C  CB  . ARG B 2 123 ? 21.360  15.841  -23.642 1.00 45.10 ? 126 ARG B CB  1 
ATOM   1237 C  CG  . ARG B 2 123 ? 22.474  15.245  -24.407 1.00 46.01 ? 126 ARG B CG  1 
ATOM   1238 C  CD  . ARG B 2 123 ? 21.922  14.296  -25.415 1.00 48.91 ? 126 ARG B CD  1 
ATOM   1239 N  NE  . ARG B 2 123 ? 21.445  13.044  -24.837 1.00 46.43 ? 126 ARG B NE  1 
ATOM   1240 C  CZ  . ARG B 2 123 ? 22.237  12.061  -24.430 1.00 49.36 ? 126 ARG B CZ  1 
ATOM   1241 N  NH1 . ARG B 2 123 ? 23.559  12.166  -24.494 1.00 51.22 ? 126 ARG B NH1 1 
ATOM   1242 N  NH2 . ARG B 2 123 ? 21.691  10.936  -23.970 1.00 43.69 ? 126 ARG B NH2 1 
ATOM   1243 N  N   . GLU B 2 124 ? 22.507  18.668  -23.187 1.00 51.49 ? 127 GLU B N   1 
ATOM   1244 C  CA  . GLU B 2 124 ? 23.483  19.697  -23.525 1.00 53.33 ? 127 GLU B CA  1 
ATOM   1245 C  C   . GLU B 2 124 ? 24.252  20.147  -22.293 1.00 49.26 ? 127 GLU B C   1 
ATOM   1246 O  O   . GLU B 2 124 ? 25.481  20.278  -22.333 1.00 48.87 ? 127 GLU B O   1 
ATOM   1247 C  CB  . GLU B 2 124 ? 22.787  20.894  -24.172 1.00 55.74 ? 127 GLU B CB  1 
ATOM   1248 C  CG  . GLU B 2 124 ? 22.634  20.798  -25.677 1.00 62.66 ? 127 GLU B CG  1 
ATOM   1249 C  CD  . GLU B 2 124 ? 23.947  20.554  -26.386 1.00 73.52 ? 127 GLU B CD  1 
ATOM   1250 O  OE1 . GLU B 2 124 ? 24.181  19.395  -26.801 1.00 74.99 ? 127 GLU B OE1 1 
ATOM   1251 O  OE2 . GLU B 2 124 ? 24.739  21.521  -26.534 1.00 70.49 ? 127 GLU B OE2 1 
ATOM   1252 N  N   . THR B 2 125 ? 23.542  20.392  -21.190 1.00 48.94 ? 128 THR B N   1 
ATOM   1253 C  CA  . THR B 2 125 ? 24.199  20.818  -19.958 1.00 47.90 ? 128 THR B CA  1 
ATOM   1254 C  C   . THR B 2 125 ? 25.222  19.784  -19.495 1.00 46.62 ? 128 THR B C   1 
ATOM   1255 O  O   . THR B 2 125 ? 26.347  20.136  -19.122 1.00 46.60 ? 128 THR B O   1 
ATOM   1256 C  CB  . THR B 2 125 ? 23.154  21.077  -18.866 1.00 49.01 ? 128 THR B CB  1 
ATOM   1257 O  OG1 . THR B 2 125 ? 22.271  22.135  -19.277 1.00 49.84 ? 128 THR B OG1 1 
ATOM   1258 C  CG2 . THR B 2 125 ? 23.818  21.449  -17.548 1.00 40.67 ? 128 THR B CG2 1 
ATOM   1259 N  N   . ALA B 2 126 ? 24.844  18.498  -19.508 1.00 44.12 ? 129 ALA B N   1 
ATOM   1260 C  CA  . ALA B 2 126 ? 25.763  17.445  -19.076 1.00 44.27 ? 129 ALA B CA  1 
ATOM   1261 C  C   . ALA B 2 126 ? 26.978  17.339  -19.997 1.00 45.11 ? 129 ALA B C   1 
ATOM   1262 O  O   . ALA B 2 126 ? 28.107  17.128  -19.535 1.00 42.69 ? 129 ALA B O   1 
ATOM   1263 C  CB  . ALA B 2 126 ? 25.032  16.108  -18.991 1.00 48.69 ? 129 ALA B CB  1 
ATOM   1264 N  N   . ALA B 2 127 A 26.769  17.469  -21.307 1.00 48.81 ? 129 ALA B N   1 
ATOM   1265 C  CA  . ALA B 2 127 A 27.900  17.400  -22.222 1.00 45.59 ? 129 ALA B CA  1 
ATOM   1266 C  C   . ALA B 2 127 A 28.838  18.574  -22.002 1.00 43.51 ? 129 ALA B C   1 
ATOM   1267 O  O   . ALA B 2 127 A 30.059  18.417  -22.064 1.00 43.79 ? 129 ALA B O   1 
ATOM   1268 C  CB  . ALA B 2 127 A 27.409  17.378  -23.667 1.00 48.28 ? 129 ALA B CB  1 
ATOM   1269 N  N   . SER B 2 128 B 28.276  19.749  -21.704 1.00 42.73 ? 129 SER B N   1 
ATOM   1270 C  CA  . SER B 2 128 B 29.076  20.953  -21.513 1.00 42.84 ? 129 SER B CA  1 
ATOM   1271 C  C   . SER B 2 128 B 29.840  20.948  -20.188 1.00 49.18 ? 129 SER B C   1 
ATOM   1272 O  O   . SER B 2 128 B 30.990  21.406  -20.136 1.00 47.75 ? 129 SER B O   1 
ATOM   1273 C  CB  . SER B 2 128 B 28.171  22.180  -21.596 1.00 50.10 ? 129 SER B CB  1 
ATOM   1274 O  OG  . SER B 2 128 B 27.736  22.398  -22.933 1.00 54.89 ? 129 SER B OG  1 
ATOM   1275 N  N   . LEU B 2 129 C 29.226  20.456  -19.103 1.00 47.96 ? 129 LEU B N   1 
ATOM   1276 C  CA  . LEU B 2 129 C 29.805  20.641  -17.771 1.00 46.91 ? 129 LEU B CA  1 
ATOM   1277 C  C   . LEU B 2 129 C 30.605  19.450  -17.243 1.00 42.67 ? 129 LEU B C   1 
ATOM   1278 O  O   . LEU B 2 129 C 31.580  19.664  -16.521 1.00 40.34 ? 129 LEU B O   1 
ATOM   1279 C  CB  . LEU B 2 129 C 28.705  21.018  -16.769 1.00 44.29 ? 129 LEU B CB  1 
ATOM   1280 C  CG  . LEU B 2 129 C 27.990  22.311  -17.193 1.00 45.12 ? 129 LEU B CG  1 
ATOM   1281 C  CD1 . LEU B 2 129 C 26.923  22.749  -16.193 1.00 40.01 ? 129 LEU B CD1 1 
ATOM   1282 C  CD2 . LEU B 2 129 C 29.012  23.417  -17.434 1.00 41.84 ? 129 LEU B CD2 1 
ATOM   1283 N  N   . LEU B 2 130 ? 30.258  18.206  -17.582 1.00 44.13 ? 130 LEU B N   1 
ATOM   1284 C  CA  . LEU B 2 130 ? 31.000  17.049  -17.069 1.00 44.63 ? 130 LEU B CA  1 
ATOM   1285 C  C   . LEU B 2 130 ? 32.278  16.835  -17.871 1.00 42.56 ? 130 LEU B C   1 
ATOM   1286 O  O   . LEU B 2 130 ? 32.480  15.796  -18.505 1.00 44.50 ? 130 LEU B O   1 
ATOM   1287 C  CB  . LEU B 2 130 ? 30.142  15.787  -17.087 1.00 44.73 ? 130 LEU B CB  1 
ATOM   1288 C  CG  . LEU B 2 130 ? 29.418  15.314  -15.829 1.00 48.55 ? 130 LEU B CG  1 
ATOM   1289 C  CD1 . LEU B 2 130 ? 29.230  13.831  -15.948 1.00 48.73 ? 130 LEU B CD1 1 
ATOM   1290 C  CD2 . LEU B 2 130 ? 30.152  15.657  -14.557 1.00 45.46 ? 130 LEU B CD2 1 
ATOM   1291 N  N   . GLN B 2 131 ? 33.197  17.778  -17.716 1.00 45.90 ? 131 GLN B N   1 
ATOM   1292 C  CA  . GLN B 2 131 ? 34.421  17.783  -18.488 1.00 48.10 ? 131 GLN B CA  1 
ATOM   1293 C  C   . GLN B 2 131 ? 35.567  17.704  -17.478 1.00 46.83 ? 131 GLN B C   1 
ATOM   1294 O  O   . GLN B 2 131 ? 35.535  18.401  -16.453 1.00 45.59 ? 131 GLN B O   1 
ATOM   1295 C  CB  . GLN B 2 131 ? 34.629  19.117  -19.244 1.00 46.56 ? 131 GLN B CB  1 
ATOM   1296 C  CG  . GLN B 2 131 ? 35.160  19.033  -20.737 1.00 63.54 ? 131 GLN B CG  1 
ATOM   1297 C  CD  . GLN B 2 131 ? 34.490  20.160  -21.607 1.00 69.87 ? 131 GLN B CD  1 
ATOM   1298 O  OE1 . GLN B 2 131 ? 34.614  21.340  -21.248 1.00 90.10 ? 131 GLN B OE1 1 
ATOM   1299 N  NE2 . GLN B 2 131 ? 33.603  19.759  -22.629 1.00 57.06 ? 131 GLN B NE2 1 
ATOM   1300 N  N   . ALA B 2 132 ? 36.570  16.859  -17.734 1.00 40.17 ? 132 ALA B N   1 
ATOM   1301 C  CA  . ALA B 2 132 ? 37.749  16.798  -16.858 1.00 45.19 ? 132 ALA B CA  1 
ATOM   1302 C  C   . ALA B 2 132 ? 38.350  18.184  -16.609 1.00 45.58 ? 132 ALA B C   1 
ATOM   1303 O  O   . ALA B 2 132 ? 38.385  19.034  -17.504 1.00 46.92 ? 132 ALA B O   1 
ATOM   1304 C  CB  . ALA B 2 132 ? 38.828  15.889  -17.466 1.00 44.39 ? 132 ALA B CB  1 
ATOM   1305 N  N   . GLY B 2 133 ? 38.814  18.424  -15.380 1.00 40.91 ? 133 GLY B N   1 
ATOM   1306 C  CA  . GLY B 2 133 ? 39.346  19.724  -15.002 1.00 34.29 ? 133 GLY B CA  1 
ATOM   1307 C  C   . GLY B 2 133 ? 38.300  20.719  -14.558 1.00 41.37 ? 133 GLY B C   1 
ATOM   1308 O  O   . GLY B 2 133 ? 38.612  21.650  -13.807 1.00 43.17 ? 133 GLY B O   1 
ATOM   1309 N  N   . TYR B 2 134 ? 37.072  20.572  -15.042 1.00 47.11 ? 134 TYR B N   1 
ATOM   1310 C  CA  . TYR B 2 134 ? 35.991  21.431  -14.580 1.00 46.27 ? 134 TYR B CA  1 
ATOM   1311 C  C   . TYR B 2 134 ? 35.634  21.074  -13.144 1.00 44.86 ? 134 TYR B C   1 
ATOM   1312 O  O   . TYR B 2 134 ? 35.647  19.903  -12.752 1.00 44.22 ? 134 TYR B O   1 
ATOM   1313 C  CB  . TYR B 2 134 ? 34.763  21.291  -15.474 1.00 45.99 ? 134 TYR B CB  1 
ATOM   1314 C  CG  . TYR B 2 134 ? 34.888  21.934  -16.847 1.00 51.61 ? 134 TYR B CG  1 
ATOM   1315 C  CD1 . TYR B 2 134 ? 36.094  22.475  -17.285 1.00 54.01 ? 134 TYR B CD1 1 
ATOM   1316 C  CD2 . TYR B 2 134 ? 33.781  22.027  -17.696 1.00 52.21 ? 134 TYR B CD2 1 
ATOM   1317 C  CE1 . TYR B 2 134 ? 36.201  23.065  -18.542 1.00 56.32 ? 134 TYR B CE1 1 
ATOM   1318 C  CE2 . TYR B 2 134 ? 33.882  22.605  -18.949 1.00 51.77 ? 134 TYR B CE2 1 
ATOM   1319 C  CZ  . TYR B 2 134 ? 35.090  23.126  -19.365 1.00 55.25 ? 134 TYR B CZ  1 
ATOM   1320 O  OH  . TYR B 2 134 ? 35.184  23.718  -20.603 1.00 64.38 ? 134 TYR B OH  1 
ATOM   1321 N  N   . LYS B 2 135 ? 35.328  22.089  -12.350 1.00 45.57 ? 135 LYS B N   1 
ATOM   1322 C  CA  . LYS B 2 135 ? 35.112  21.899  -10.924 1.00 43.72 ? 135 LYS B CA  1 
ATOM   1323 C  C   . LYS B 2 135 ? 33.625  21.904  -10.591 1.00 43.44 ? 135 LYS B C   1 
ATOM   1324 O  O   . LYS B 2 135 ? 32.844  22.685  -11.154 1.00 42.87 ? 135 LYS B O   1 
ATOM   1325 C  CB  . LYS B 2 135 ? 35.848  22.969  -10.111 1.00 38.64 ? 135 LYS B CB  1 
ATOM   1326 C  CG  . LYS B 2 135 ? 37.376  22.798  -10.078 1.00 39.50 ? 135 LYS B CG  1 
ATOM   1327 C  CD  . LYS B 2 135 ? 38.016  23.966  -9.338  1.00 41.33 ? 135 LYS B CD  1 
ATOM   1328 C  CE  . LYS B 2 135 ? 39.501  23.769  -9.129  1.00 38.45 ? 135 LYS B CE  1 
ATOM   1329 N  NZ  . LYS B 2 135 ? 40.128  24.972  -8.502  1.00 38.81 ? 135 LYS B NZ  1 
ATOM   1330 N  N   . GLY B 2 136 ? 33.244  20.990  -9.695  1.00 35.62 ? 136 GLY B N   1 
ATOM   1331 C  CA  . GLY B 2 136 ? 31.945  20.983  -9.070  1.00 36.04 ? 136 GLY B CA  1 
ATOM   1332 C  C   . GLY B 2 136 ? 32.076  21.146  -7.563  1.00 36.12 ? 136 GLY B C   1 
ATOM   1333 O  O   . GLY B 2 136 ? 33.171  21.351  -7.028  1.00 34.60 ? 136 GLY B O   1 
ATOM   1334 N  N   . ARG B 2 137 ? 30.923  21.079  -6.886  1.00 37.53 ? 137 ARG B N   1 
ATOM   1335 C  CA  . ARG B 2 137 ? 30.849  21.343  -5.450  1.00 36.60 ? 137 ARG B CA  1 
ATOM   1336 C  C   . ARG B 2 137 ? 30.131  20.199  -4.738  1.00 36.15 ? 137 ARG B C   1 
ATOM   1337 O  O   . ARG B 2 137 ? 29.124  19.682  -5.232  1.00 35.58 ? 137 ARG B O   1 
ATOM   1338 C  CB  . ARG B 2 137 ? 30.158  22.692  -5.196  1.00 36.75 ? 137 ARG B CB  1 
ATOM   1339 C  CG  . ARG B 2 137 ? 29.935  23.071  -3.754  1.00 33.81 ? 137 ARG B CG  1 
ATOM   1340 C  CD  . ARG B 2 137 ? 29.097  24.339  -3.666  1.00 35.23 ? 137 ARG B CD  1 
ATOM   1341 N  NE  . ARG B 2 137 ? 29.891  25.545  -3.873  1.00 37.27 ? 137 ARG B NE  1 
ATOM   1342 C  CZ  . ARG B 2 137 ? 29.390  26.766  -4.021  1.00 36.49 ? 137 ARG B CZ  1 
ATOM   1343 N  NH1 . ARG B 2 137 ? 28.085  26.992  -4.000  1.00 37.58 ? 137 ARG B NH1 1 
ATOM   1344 N  NH2 . ARG B 2 137 ? 30.220  27.788  -4.208  1.00 38.05 ? 137 ARG B NH2 1 
ATOM   1345 N  N   . VAL B 2 138 ? 30.686  19.782  -3.595  1.00 34.76 ? 138 VAL B N   1 
ATOM   1346 C  CA  . VAL B 2 138 ? 30.177  18.680  -2.784  1.00 35.37 ? 138 VAL B CA  1 
ATOM   1347 C  C   . VAL B 2 138 ? 29.899  19.198  -1.377  1.00 37.64 ? 138 VAL B C   1 
ATOM   1348 O  O   . VAL B 2 138 ? 30.716  19.932  -0.801  1.00 31.39 ? 138 VAL B O   1 
ATOM   1349 C  CB  . VAL B 2 138 ? 31.167  17.498  -2.717  1.00 31.84 ? 138 VAL B CB  1 
ATOM   1350 C  CG1 . VAL B 2 138 ? 30.466  16.218  -2.266  1.00 26.05 ? 138 VAL B CG1 1 
ATOM   1351 C  CG2 . VAL B 2 138 ? 31.844  17.306  -4.040  1.00 37.47 ? 138 VAL B CG2 1 
ATOM   1352 N  N   . THR B 2 139 ? 28.766  18.759  -0.811  1.00 35.33 ? 139 THR B N   1 
ATOM   1353 C  CA  . THR B 2 139 ? 28.259  19.231  0.469   1.00 34.63 ? 139 THR B CA  1 
ATOM   1354 C  C   . THR B 2 139 ? 27.789  18.066  1.322   1.00 37.31 ? 139 THR B C   1 
ATOM   1355 O  O   . THR B 2 139 ? 27.156  17.134  0.816   1.00 34.91 ? 139 THR B O   1 
ATOM   1356 C  CB  . THR B 2 139 ? 27.082  20.143  0.270   1.00 34.12 ? 139 THR B CB  1 
ATOM   1357 O  OG1 . THR B 2 139 ? 26.178  19.480  -0.619  1.00 33.77 ? 139 THR B OG1 1 
ATOM   1358 C  CG2 . THR B 2 139 ? 27.529  21.470  -0.307  1.00 33.08 ? 139 THR B CG2 1 
ATOM   1359 N  N   . GLY B 2 140 ? 28.036  18.154  2.622   1.00 37.30 ? 140 GLY B N   1 
ATOM   1360 C  CA  . GLY B 2 140 ? 27.535  17.111  3.504   1.00 35.95 ? 140 GLY B CA  1 
ATOM   1361 C  C   . GLY B 2 140 ? 27.878  17.360  4.960   1.00 41.08 ? 140 GLY B C   1 
ATOM   1362 O  O   . GLY B 2 140 ? 28.730  18.195  5.303   1.00 37.20 ? 140 GLY B O   1 
ATOM   1363 N  N   . TRP B 2 141 ? 27.186  16.597  5.815   1.00 41.62 ? 141 TRP B N   1 
ATOM   1364 C  CA  . TRP B 2 141 ? 27.438  16.513  7.246   1.00 33.49 ? 141 TRP B CA  1 
ATOM   1365 C  C   . TRP B 2 141 ? 28.257  15.288  7.626   1.00 33.57 ? 141 TRP B C   1 
ATOM   1366 O  O   . TRP B 2 141 ? 28.347  14.959  8.811   1.00 36.82 ? 141 TRP B O   1 
ATOM   1367 C  CB  . TRP B 2 141 ? 26.108  16.505  8.005   1.00 31.44 ? 141 TRP B CB  1 
ATOM   1368 C  CG  . TRP B 2 141 ? 25.462  17.868  8.125   1.00 37.39 ? 141 TRP B CG  1 
ATOM   1369 C  CD1 . TRP B 2 141 ? 25.788  18.853  9.020   1.00 37.83 ? 141 TRP B CD1 1 
ATOM   1370 C  CD2 . TRP B 2 141 ? 24.378  18.388  7.340   1.00 36.23 ? 141 TRP B CD2 1 
ATOM   1371 N  NE1 . TRP B 2 141 ? 24.989  19.952  8.830   1.00 37.77 ? 141 TRP B NE1 1 
ATOM   1372 C  CE2 . TRP B 2 141 ? 24.112  19.699  7.811   1.00 36.43 ? 141 TRP B CE2 1 
ATOM   1373 C  CE3 . TRP B 2 141 ? 23.609  17.879  6.289   1.00 33.91 ? 141 TRP B CE3 1 
ATOM   1374 C  CZ2 . TRP B 2 141 ? 23.114  20.509  7.262   1.00 38.13 ? 141 TRP B CZ2 1 
ATOM   1375 C  CZ3 . TRP B 2 141 ? 22.614  18.685  5.736   1.00 35.29 ? 141 TRP B CZ3 1 
ATOM   1376 C  CH2 . TRP B 2 141 ? 22.371  19.984  6.231   1.00 40.35 ? 141 TRP B CH2 1 
ATOM   1377 N  N   . GLY B 2 142 ? 28.870  14.618  6.658   1.00 36.74 ? 142 GLY B N   1 
ATOM   1378 C  CA  . GLY B 2 142 ? 29.695  13.460  6.930   1.00 34.47 ? 142 GLY B CA  1 
ATOM   1379 C  C   . GLY B 2 142 ? 31.000  13.800  7.652   1.00 39.04 ? 142 GLY B C   1 
ATOM   1380 O  O   . GLY B 2 142 ? 31.303  14.946  7.991   1.00 33.89 ? 142 GLY B O   1 
ATOM   1381 N  N   . ASN B 2 143 ? 31.795  12.747  7.867   1.00 42.19 ? 143 ASN B N   1 
ATOM   1382 C  CA  . ASN B 2 143 ? 33.030  12.827  8.645   1.00 40.70 ? 143 ASN B CA  1 
ATOM   1383 C  C   . ASN B 2 143 ? 34.013  13.847  8.079   1.00 42.73 ? 143 ASN B C   1 
ATOM   1384 O  O   . ASN B 2 143 ? 34.146  14.006  6.861   1.00 42.92 ? 143 ASN B O   1 
ATOM   1385 C  CB  . ASN B 2 143 ? 33.722  11.464  8.676   1.00 41.31 ? 143 ASN B CB  1 
ATOM   1386 C  CG  . ASN B 2 143 ? 32.930  10.405  9.426   1.00 48.13 ? 143 ASN B CG  1 
ATOM   1387 O  OD1 . ASN B 2 143 ? 31.862  10.671  9.991   1.00 43.88 ? 143 ASN B OD1 1 
ATOM   1388 N  ND2 . ASN B 2 143 ? 33.470  9.182   9.441   1.00 49.40 ? 143 ASN B ND2 1 
ATOM   1389 N  N   . LEU B 2 144 ? 34.715  14.535  8.984   1.00 45.58 ? 144 LEU B N   1 
ATOM   1390 C  CA  . LEU B 2 144 ? 35.761  15.483  8.611   1.00 42.52 ? 144 LEU B CA  1 
ATOM   1391 C  C   . LEU B 2 144 ? 37.104  14.808  8.372   1.00 41.90 ? 144 LEU B C   1 
ATOM   1392 O  O   . LEU B 2 144 ? 37.960  15.381  7.691   1.00 48.38 ? 144 LEU B O   1 
ATOM   1393 C  CB  . LEU B 2 144 ? 35.918  16.548  9.701   1.00 44.17 ? 144 LEU B CB  1 
ATOM   1394 C  CG  . LEU B 2 144 ? 34.662  17.337  10.077  1.00 42.29 ? 144 LEU B CG  1 
ATOM   1395 C  CD1 . LEU B 2 144 ? 34.886  18.154  11.340  1.00 37.61 ? 144 LEU B CD1 1 
ATOM   1396 C  CD2 . LEU B 2 144 ? 34.220  18.219  8.908   1.00 34.83 ? 144 LEU B CD2 1 
ATOM   1397 N  N   . LYS B 2 145 ? 37.303  13.607  8.905   1.00 41.77 ? 145 LYS B N   1 
ATOM   1398 C  CA  . LYS B 2 145 ? 38.541  12.863  8.725   1.00 47.44 ? 145 LYS B CA  1 
ATOM   1399 C  C   . LYS B 2 145 ? 38.204  11.388  8.538   1.00 49.82 ? 145 LYS B C   1 
ATOM   1400 O  O   . LYS B 2 145 ? 37.113  10.924  8.876   1.00 40.27 ? 145 LYS B O   1 
ATOM   1401 C  CB  . LYS B 2 145 ? 39.503  13.023  9.920   1.00 42.40 ? 145 LYS B CB  1 
ATOM   1402 C  CG  . LYS B 2 145 ? 40.073  14.415  10.141  1.00 47.66 ? 145 LYS B CG  1 
ATOM   1403 C  CD  . LYS B 2 145 ? 41.385  14.340  10.933  1.00 58.87 ? 145 LYS B CD  1 
ATOM   1404 C  CE  . LYS B 2 145 ? 41.742  15.659  11.612  1.00 66.41 ? 145 LYS B CE  1 
ATOM   1405 N  NZ  . LYS B 2 145 ? 42.470  16.590  10.706  1.00 63.11 ? 145 LYS B NZ  1 
ATOM   1406 N  N   . GLU B 2 146 ? 39.145  10.664  7.958   1.00 47.38 ? 146 GLU B N   1 
ATOM   1407 C  CA  . GLU B 2 146 ? 39.056  9.215   7.899   1.00 51.55 ? 146 GLU B CA  1 
ATOM   1408 C  C   . GLU B 2 146 ? 39.100  8.604   9.305   1.00 62.75 ? 146 GLU B C   1 
ATOM   1409 O  O   . GLU B 2 146 ? 40.025  8.877   10.081  1.00 63.51 ? 146 GLU B O   1 
ATOM   1410 C  CB  . GLU B 2 146 ? 40.213  8.725   7.045   1.00 49.86 ? 146 GLU B CB  1 
ATOM   1411 C  CG  . GLU B 2 146 ? 40.160  7.323   6.581   1.00 46.42 ? 146 GLU B CG  1 
ATOM   1412 C  CD  . GLU B 2 146 ? 41.331  7.064   5.679   1.00 50.77 ? 146 GLU B CD  1 
ATOM   1413 O  OE1 . GLU B 2 146 ? 41.448  7.791   4.672   1.00 47.06 ? 146 GLU B OE1 1 
ATOM   1414 O  OE2 . GLU B 2 146 ? 42.158  6.178   5.996   1.00 55.69 ? 146 GLU B OE2 1 
ATOM   1415 N  N   . THR B 2 147 ? 38.078  7.808   9.640   1.00 66.55 ? 147 THR B N   1 
ATOM   1416 C  CA  . THR B 2 147 ? 37.896  7.228   10.993  1.00 78.41 ? 147 THR B CA  1 
ATOM   1417 C  C   . THR B 2 147 ? 39.195  6.731   11.655  1.00 83.42 ? 147 THR B C   1 
ATOM   1418 O  O   . THR B 2 147 ? 39.748  5.685   11.292  1.00 85.15 ? 147 THR B O   1 
ATOM   1419 C  CB  . THR B 2 147 ? 36.864  6.062   10.976  1.00 84.38 ? 147 THR B CB  1 
ATOM   1420 O  OG1 . THR B 2 147 ? 35.543  6.602   10.850  1.00 82.66 ? 147 THR B OG1 1 
ATOM   1421 C  CG2 . THR B 2 147 ? 36.931  5.239   12.271  1.00 85.57 ? 147 THR B CG2 1 
ATOM   1422 N  N   . GLY B 2 155 ? 35.090  14.625  15.164  1.00 65.53 ? 150 GLY B N   1 
ATOM   1423 C  CA  . GLY B 2 155 ? 35.012  14.130  13.800  1.00 58.18 ? 150 GLY B CA  1 
ATOM   1424 C  C   . GLY B 2 155 ? 33.767  14.490  12.984  1.00 58.62 ? 150 GLY B C   1 
ATOM   1425 O  O   . GLY B 2 155 ? 33.783  14.413  11.753  1.00 53.59 ? 150 GLY B O   1 
ATOM   1426 N  N   . GLN B 2 156 ? 32.694  14.915  13.653  1.00 60.39 ? 151 GLN B N   1 
ATOM   1427 C  CA  . GLN B 2 156 ? 31.452  15.248  12.973  1.00 54.40 ? 151 GLN B CA  1 
ATOM   1428 C  C   . GLN B 2 156 ? 31.236  16.744  12.996  1.00 56.19 ? 151 GLN B C   1 
ATOM   1429 O  O   . GLN B 2 156 ? 31.316  17.354  14.068  1.00 61.61 ? 151 GLN B O   1 
ATOM   1430 C  CB  . GLN B 2 156 ? 30.267  14.537  13.636  1.00 57.80 ? 151 GLN B CB  1 
ATOM   1431 C  CG  . GLN B 2 156 ? 30.339  13.025  13.479  1.00 65.83 ? 151 GLN B CG  1 
ATOM   1432 C  CD  . GLN B 2 156 ? 29.576  12.535  12.261  1.00 73.68 ? 151 GLN B CD  1 
ATOM   1433 O  OE1 . GLN B 2 156 ? 30.154  12.335  11.190  1.00 74.15 ? 151 GLN B OE1 1 
ATOM   1434 N  NE2 . GLN B 2 156 ? 28.269  12.299  12.433  1.00 77.54 ? 151 GLN B NE2 1 
ATOM   1435 N  N   . PRO B 2 157 ? 30.990  17.376  11.854  1.00 51.82 ? 152 PRO B N   1 
ATOM   1436 C  CA  . PRO B 2 157 ? 30.923  18.835  11.826  1.00 46.65 ? 152 PRO B CA  1 
ATOM   1437 C  C   . PRO B 2 157 ? 29.688  19.347  12.543  1.00 50.45 ? 152 PRO B C   1 
ATOM   1438 O  O   . PRO B 2 157 ? 28.692  18.645  12.723  1.00 54.72 ? 152 PRO B O   1 
ATOM   1439 C  CB  . PRO B 2 157 ? 30.867  19.163  10.329  1.00 40.56 ? 152 PRO B CB  1 
ATOM   1440 C  CG  . PRO B 2 157 ? 30.224  18.005  9.740   1.00 44.37 ? 152 PRO B CG  1 
ATOM   1441 C  CD  . PRO B 2 157 ? 30.673  16.797  10.541  1.00 49.27 ? 152 PRO B CD  1 
ATOM   1442 N  N   . SER B 2 158 ? 29.786  20.595  12.985  1.00 49.21 ? 153 SER B N   1 
ATOM   1443 C  CA  . SER B 2 158 ? 28.642  21.266  13.578  1.00 49.21 ? 153 SER B CA  1 
ATOM   1444 C  C   . SER B 2 158 ? 27.727  21.850  12.509  1.00 49.53 ? 153 SER B C   1 
ATOM   1445 O  O   . SER B 2 158 ? 26.502  21.877  12.686  1.00 52.65 ? 153 SER B O   1 
ATOM   1446 C  CB  . SER B 2 158 ? 29.126  22.357  14.518  1.00 52.79 ? 153 SER B CB  1 
ATOM   1447 O  OG  . SER B 2 158 ? 30.210  23.037  13.920  1.00 61.24 ? 153 SER B OG  1 
ATOM   1448 N  N   . VAL B 2 159 ? 28.301  22.370  11.421  1.00 45.60 ? 154 VAL B N   1 
ATOM   1449 C  CA  . VAL B 2 159 ? 27.521  22.912  10.316  1.00 42.11 ? 154 VAL B CA  1 
ATOM   1450 C  C   . VAL B 2 159 ? 27.916  22.225  9.017   1.00 38.99 ? 154 VAL B C   1 
ATOM   1451 O  O   . VAL B 2 159 ? 28.993  21.632  8.887   1.00 38.95 ? 154 VAL B O   1 
ATOM   1452 C  CB  . VAL B 2 159 ? 27.676  24.433  10.174  1.00 42.33 ? 154 VAL B CB  1 
ATOM   1453 C  CG1 . VAL B 2 159 ? 27.502  25.095  11.520  1.00 44.45 ? 154 VAL B CG1 1 
ATOM   1454 C  CG2 . VAL B 2 159 ? 29.006  24.750  9.590   1.00 34.69 ? 154 VAL B CG2 1 
ATOM   1455 N  N   . LEU B 2 160 ? 27.000  22.302  8.053   1.00 42.83 ? 155 LEU B N   1 
ATOM   1456 C  CA  . LEU B 2 160 ? 27.188  21.702  6.737   1.00 38.87 ? 155 LEU B CA  1 
ATOM   1457 C  C   . LEU B 2 160 ? 28.542  22.082  6.141   1.00 37.75 ? 155 LEU B C   1 
ATOM   1458 O  O   . LEU B 2 160 ? 28.941  23.247  6.173   1.00 34.64 ? 155 LEU B O   1 
ATOM   1459 C  CB  . LEU B 2 160 ? 26.053  22.159  5.818   1.00 36.63 ? 155 LEU B CB  1 
ATOM   1460 C  CG  . LEU B 2 160 ? 26.063  21.659  4.372   1.00 36.98 ? 155 LEU B CG  1 
ATOM   1461 C  CD1 . LEU B 2 160 ? 25.902  20.138  4.312   1.00 37.24 ? 155 LEU B CD1 1 
ATOM   1462 C  CD2 . LEU B 2 160 ? 24.973  22.366  3.590   1.00 36.09 ? 155 LEU B CD2 1 
ATOM   1463 N  N   . GLN B 2 161 ? 29.245  21.097  5.592   1.00 34.86 ? 156 GLN B N   1 
ATOM   1464 C  CA  . GLN B 2 161 ? 30.539  21.341  4.979   1.00 34.83 ? 156 GLN B CA  1 
ATOM   1465 C  C   . GLN B 2 161 ? 30.419  21.342  3.460   1.00 38.73 ? 156 GLN B C   1 
ATOM   1466 O  O   . GLN B 2 161 ? 29.542  20.682  2.886   1.00 38.95 ? 156 GLN B O   1 
ATOM   1467 C  CB  . GLN B 2 161 ? 31.559  20.302  5.432   1.00 36.75 ? 156 GLN B CB  1 
ATOM   1468 C  CG  . GLN B 2 161 ? 31.746  20.293  6.937   1.00 34.88 ? 156 GLN B CG  1 
ATOM   1469 C  CD  . GLN B 2 161 ? 32.415  21.567  7.449   1.00 36.42 ? 156 GLN B CD  1 
ATOM   1470 O  OE1 . GLN B 2 161 ? 33.609  21.787  7.230   1.00 34.02 ? 156 GLN B OE1 1 
ATOM   1471 N  NE2 . GLN B 2 161 ? 31.639  22.421  8.116   1.00 33.65 ? 156 GLN B NE2 1 
ATOM   1472 N  N   . VAL B 2 162 ? 31.318  22.101  2.819   1.00 38.67 ? 157 VAL B N   1 
ATOM   1473 C  CA  . VAL B 2 162 ? 31.305  22.343  1.379   1.00 35.30 ? 157 VAL B CA  1 
ATOM   1474 C  C   . VAL B 2 162 ? 32.741  22.332  0.858   1.00 36.09 ? 157 VAL B C   1 
ATOM   1475 O  O   . VAL B 2 162 ? 33.669  22.747  1.560   1.00 39.87 ? 157 VAL B O   1 
ATOM   1476 C  CB  . VAL B 2 162 ? 30.594  23.676  1.038   1.00 30.35 ? 157 VAL B CB  1 
ATOM   1477 C  CG1 . VAL B 2 162 ? 31.375  24.864  1.537   1.00 32.19 ? 157 VAL B CG1 1 
ATOM   1478 C  CG2 . VAL B 2 162 ? 30.367  23.788  -0.442  1.00 31.41 ? 157 VAL B CG2 1 
ATOM   1479 N  N   . VAL B 2 163 ? 32.931  21.818  -0.358  1.00 36.78 ? 158 VAL B N   1 
ATOM   1480 C  CA  . VAL B 2 163 ? 34.256  21.794  -0.978  1.00 33.91 ? 158 VAL B CA  1 
ATOM   1481 C  C   . VAL B 2 163 ? 34.096  21.722  -2.493  1.00 35.56 ? 158 VAL B C   1 
ATOM   1482 O  O   . VAL B 2 163 ? 33.216  21.034  -3.010  1.00 32.19 ? 158 VAL B O   1 
ATOM   1483 C  CB  . VAL B 2 163 ? 35.124  20.628  -0.445  1.00 34.65 ? 158 VAL B CB  1 
ATOM   1484 C  CG1 . VAL B 2 163 ? 34.543  19.285  -0.844  1.00 32.90 ? 158 VAL B CG1 1 
ATOM   1485 C  CG2 . VAL B 2 163 ? 36.563  20.755  -0.950  1.00 32.70 ? 158 VAL B CG2 1 
ATOM   1486 N  N   . ASN B 2 164 ? 34.971  22.435  -3.199  1.00 41.52 ? 159 ASN B N   1 
ATOM   1487 C  CA  . ASN B 2 164 ? 35.022  22.426  -4.654  1.00 37.07 ? 159 ASN B CA  1 
ATOM   1488 C  C   . ASN B 2 164 ? 36.117  21.474  -5.106  1.00 37.02 ? 159 ASN B C   1 
ATOM   1489 O  O   . ASN B 2 164 ? 37.225  21.494  -4.564  1.00 34.39 ? 159 ASN B O   1 
ATOM   1490 C  CB  . ASN B 2 164 ? 35.280  23.830  -5.200  1.00 36.29 ? 159 ASN B CB  1 
ATOM   1491 C  CG  . ASN B 2 164 ? 34.179  24.799  -4.840  1.00 38.37 ? 159 ASN B CG  1 
ATOM   1492 O  OD1 . ASN B 2 164 ? 33.024  24.400  -4.617  1.00 34.46 ? 159 ASN B OD1 1 
ATOM   1493 N  ND2 . ASN B 2 164 ? 34.522  26.085  -4.786  1.00 35.57 ? 159 ASN B ND2 1 
ATOM   1494 N  N   . LEU B 2 165 ? 35.801  20.648  -6.100  1.00 39.43 ? 160 LEU B N   1 
ATOM   1495 C  CA  . LEU B 2 165 ? 36.697  19.611  -6.573  1.00 41.27 ? 160 LEU B CA  1 
ATOM   1496 C  C   . LEU B 2 165 ? 36.624  19.474  -8.094  1.00 42.34 ? 160 LEU B C   1 
ATOM   1497 O  O   . LEU B 2 165 ? 35.534  19.550  -8.680  1.00 37.74 ? 160 LEU B O   1 
ATOM   1498 C  CB  . LEU B 2 165 ? 36.356  18.262  -5.907  1.00 37.48 ? 160 LEU B CB  1 
ATOM   1499 C  CG  . LEU B 2 165 ? 36.382  18.195  -4.365  1.00 36.48 ? 160 LEU B CG  1 
ATOM   1500 C  CD1 . LEU B 2 165 ? 35.890  16.856  -3.857  1.00 29.64 ? 160 LEU B CD1 1 
ATOM   1501 C  CD2 . LEU B 2 165 ? 37.763  18.491  -3.793  1.00 34.92 ? 160 LEU B CD2 1 
ATOM   1502 N  N   . PRO B 2 166 ? 37.763  19.276  -8.751  1.00 41.94 ? 161 PRO B N   1 
ATOM   1503 C  CA  . PRO B 2 166 ? 37.762  19.092  -10.204 1.00 44.36 ? 161 PRO B CA  1 
ATOM   1504 C  C   . PRO B 2 166 ? 37.375  17.674  -10.596 1.00 44.65 ? 161 PRO B C   1 
ATOM   1505 O  O   . PRO B 2 166 ? 37.748  16.699  -9.935  1.00 43.18 ? 161 PRO B O   1 
ATOM   1506 C  CB  . PRO B 2 166 ? 39.219  19.379  -10.586 1.00 36.79 ? 161 PRO B CB  1 
ATOM   1507 C  CG  . PRO B 2 166 ? 39.981  18.875  -9.422  1.00 35.74 ? 161 PRO B CG  1 
ATOM   1508 C  CD  . PRO B 2 166 ? 39.133  19.257  -8.205  1.00 44.24 ? 161 PRO B CD  1 
ATOM   1509 N  N   . ILE B 2 167 ? 36.602  17.582  -11.683 1.00 40.89 ? 162 ILE B N   1 
ATOM   1510 C  CA  . ILE B 2 167 ? 36.357  16.308  -12.346 1.00 40.26 ? 162 ILE B CA  1 
ATOM   1511 C  C   . ILE B 2 167 ? 37.654  15.755  -12.924 1.00 42.80 ? 162 ILE B C   1 
ATOM   1512 O  O   . ILE B 2 167 ? 38.491  16.501  -13.447 1.00 47.38 ? 162 ILE B O   1 
ATOM   1513 C  CB  . ILE B 2 167 ? 35.293  16.505  -13.435 1.00 35.03 ? 162 ILE B CB  1 
ATOM   1514 C  CG1 . ILE B 2 167 ? 33.995  16.984  -12.795 1.00 42.12 ? 162 ILE B CG1 1 
ATOM   1515 C  CG2 . ILE B 2 167 ? 35.034  15.234  -14.175 1.00 37.32 ? 162 ILE B CG2 1 
ATOM   1516 C  CD1 . ILE B 2 167 ? 33.018  17.570  -13.785 1.00 43.87 ? 162 ILE B CD1 1 
ATOM   1517 N  N   . VAL B 2 168 ? 37.817  14.435  -12.857 1.00 41.24 ? 163 VAL B N   1 
ATOM   1518 C  CA  . VAL B 2 168 ? 39.055  13.776  -13.255 1.00 44.58 ? 163 VAL B CA  1 
ATOM   1519 C  C   . VAL B 2 168 ? 38.827  12.979  -14.533 1.00 46.49 ? 163 VAL B C   1 
ATOM   1520 O  O   . VAL B 2 168 ? 37.784  12.329  -14.688 1.00 40.75 ? 163 VAL B O   1 
ATOM   1521 C  CB  . VAL B 2 168 ? 39.569  12.864  -12.120 1.00 47.22 ? 163 VAL B CB  1 
ATOM   1522 C  CG1 . VAL B 2 168 ? 40.785  12.013  -12.574 1.00 40.28 ? 163 VAL B CG1 1 
ATOM   1523 C  CG2 . VAL B 2 168 ? 39.895  13.698  -10.874 1.00 38.11 ? 163 VAL B CG2 1 
ATOM   1524 N  N   . GLU B 2 169 ? 39.824  13.018  -15.434 1.00 47.86 ? 164 GLU B N   1 
ATOM   1525 C  CA  . GLU B 2 169 ? 39.866  12.181  -16.635 1.00 43.44 ? 164 GLU B CA  1 
ATOM   1526 C  C   . GLU B 2 169 ? 39.572  10.723  -16.303 1.00 42.64 ? 164 GLU B C   1 
ATOM   1527 O  O   . GLU B 2 169 ? 40.067  10.184  -15.312 1.00 46.34 ? 164 GLU B O   1 
ATOM   1528 C  CB  . GLU B 2 169 ? 41.239  12.279  -17.307 1.00 42.61 ? 164 GLU B CB  1 
ATOM   1529 C  CG  . GLU B 2 169 ? 41.715  13.687  -17.613 1.00 50.29 ? 164 GLU B CG  1 
ATOM   1530 C  CD  . GLU B 2 169 ? 42.428  14.338  -16.429 1.00 62.90 ? 164 GLU B CD  1 
ATOM   1531 O  OE1 . GLU B 2 169 ? 42.586  13.673  -15.374 1.00 57.51 ? 164 GLU B OE1 1 
ATOM   1532 O  OE2 . GLU B 2 169 ? 42.811  15.525  -16.554 1.00 62.92 ? 164 GLU B OE2 1 
ATOM   1533 N  N   . ARG B 2 170 ? 38.757  10.085  -17.139 1.00 46.59 ? 165 ARG B N   1 
ATOM   1534 C  CA  . ARG B 2 170 ? 38.351  8.707   -16.869 1.00 44.21 ? 165 ARG B CA  1 
ATOM   1535 C  C   . ARG B 2 170 ? 39.505  7.712   -16.754 1.00 42.82 ? 165 ARG B C   1 
ATOM   1536 O  O   . ARG B 2 170 ? 39.404  6.802   -15.918 1.00 43.40 ? 165 ARG B O   1 
ATOM   1537 C  CB  . ARG B 2 170 ? 37.349  8.252   -17.939 1.00 44.15 ? 165 ARG B CB  1 
ATOM   1538 C  CG  . ARG B 2 170 ? 36.381  7.178   -17.460 1.00 49.61 ? 165 ARG B CG  1 
ATOM   1539 C  CD  . ARG B 2 170 ? 35.351  6.794   -18.533 1.00 56.34 ? 165 ARG B CD  1 
ATOM   1540 N  NE  . ARG B 2 170 ? 34.034  7.388   -18.317 1.00 60.81 ? 165 ARG B NE  1 
ATOM   1541 C  CZ  . ARG B 2 170 ? 33.263  7.151   -17.261 1.00 62.22 ? 165 ARG B CZ  1 
ATOM   1542 N  NH1 . ARG B 2 170 ? 33.627  6.302   -16.311 1.00 55.54 ? 165 ARG B NH1 1 
ATOM   1543 N  NH2 . ARG B 2 170 ? 32.096  7.782   -17.153 1.00 63.72 ? 165 ARG B NH2 1 
ATOM   1544 N  N   . PRO B 2 171 ? 40.588  7.795   -17.542 1.00 47.73 ? 166 PRO B N   1 
ATOM   1545 C  CA  . PRO B 2 171 ? 41.714  6.866   -17.323 1.00 44.41 ? 166 PRO B CA  1 
ATOM   1546 C  C   . PRO B 2 171 ? 42.392  6.998   -15.971 1.00 42.37 ? 166 PRO B C   1 
ATOM   1547 O  O   . PRO B 2 171 ? 42.765  5.982   -15.367 1.00 45.35 ? 166 PRO B O   1 
ATOM   1548 C  CB  . PRO B 2 171 ? 42.670  7.223   -18.470 1.00 47.14 ? 166 PRO B CB  1 
ATOM   1549 C  CG  . PRO B 2 171 ? 41.759  7.656   -19.553 1.00 36.62 ? 166 PRO B CG  1 
ATOM   1550 C  CD  . PRO B 2 171 ? 40.724  8.478   -18.841 1.00 47.38 ? 166 PRO B CD  1 
ATOM   1551 N  N   . VAL B 2 172 ? 42.582  8.219   -15.480 1.00 42.07 ? 167 VAL B N   1 
ATOM   1552 C  CA  . VAL B 2 172 ? 43.128  8.394   -14.137 1.00 39.58 ? 167 VAL B CA  1 
ATOM   1553 C  C   . VAL B 2 172 ? 42.233  7.707   -13.107 1.00 43.46 ? 167 VAL B C   1 
ATOM   1554 O  O   . VAL B 2 172 ? 42.712  6.971   -12.230 1.00 44.86 ? 167 VAL B O   1 
ATOM   1555 C  CB  . VAL B 2 172 ? 43.298  9.892   -13.843 1.00 37.65 ? 167 VAL B CB  1 
ATOM   1556 C  CG1 . VAL B 2 172 ? 43.918  10.099  -12.497 1.00 42.14 ? 167 VAL B CG1 1 
ATOM   1557 C  CG2 . VAL B 2 172 ? 44.139  10.532  -14.930 1.00 38.13 ? 167 VAL B CG2 1 
ATOM   1558 N  N   . CYS B 2 173 ? 40.913  7.913   -13.223 1.00 37.60 ? 168 CYS B N   1 
ATOM   1559 C  CA  . CYS B 2 173 ? 39.955  7.231   -12.355 1.00 43.36 ? 168 CYS B CA  1 
ATOM   1560 C  C   . CYS B 2 173 ? 40.110  5.714   -12.441 1.00 45.72 ? 168 CYS B C   1 
ATOM   1561 O  O   . CYS B 2 173 ? 40.056  5.014   -11.420 1.00 43.97 ? 168 CYS B O   1 
ATOM   1562 C  CB  . CYS B 2 173 ? 38.512  7.636   -12.700 1.00 38.72 ? 168 CYS B CB  1 
ATOM   1563 S  SG  . CYS B 2 173 ? 38.072  9.392   -12.530 1.00 38.79 ? 168 CYS B SG  1 
ATOM   1564 N  N   . LYS B 2 174 ? 40.229  5.176   -13.660 1.00 44.22 ? 169 LYS B N   1 
ATOM   1565 C  CA  . LYS B 2 174 ? 40.350  3.727   -13.807 1.00 45.49 ? 169 LYS B CA  1 
ATOM   1566 C  C   . LYS B 2 174 ? 41.609  3.220   -13.111 1.00 47.84 ? 169 LYS B C   1 
ATOM   1567 O  O   . LYS B 2 174 ? 41.565  2.219   -12.384 1.00 53.43 ? 169 LYS B O   1 
ATOM   1568 C  CB  . LYS B 2 174 ? 40.328  3.329   -15.294 1.00 45.20 ? 169 LYS B CB  1 
ATOM   1569 C  CG  . LYS B 2 174 ? 40.174  1.822   -15.566 1.00 42.37 ? 169 LYS B CG  1 
ATOM   1570 C  CD  . LYS B 2 174 ? 41.511  1.102   -15.468 1.00 60.05 ? 169 LYS B CD  1 
ATOM   1571 C  CE  . LYS B 2 174 ? 41.373  -0.415  -15.446 1.00 60.09 ? 169 LYS B CE  1 
ATOM   1572 N  NZ  . LYS B 2 174 ? 42.283  -0.948  -14.370 1.00 61.55 ? 169 LYS B NZ  1 
ATOM   1573 N  N   . ASP B 2 175 ? 42.751  3.891   -13.337 1.00 50.10 ? 170 ASP B N   1 
ATOM   1574 C  CA  . ASP B 2 175 ? 44.024  3.451   -12.752 1.00 53.21 ? 170 ASP B CA  1 
ATOM   1575 C  C   . ASP B 2 175 ? 44.127  3.709   -11.256 1.00 50.04 ? 170 ASP B C   1 
ATOM   1576 O  O   . ASP B 2 175 ? 45.072  3.208   -10.635 1.00 49.07 ? 170 ASP B O   1 
ATOM   1577 C  CB  . ASP B 2 175 ? 45.233  4.122   -13.429 1.00 43.78 ? 170 ASP B CB  1 
ATOM   1578 C  CG  . ASP B 2 175 ? 45.216  3.976   -14.943 1.00 56.88 ? 170 ASP B CG  1 
ATOM   1579 O  OD1 . ASP B 2 175 ? 44.617  2.992   -15.441 1.00 59.71 ? 170 ASP B OD1 1 
ATOM   1580 O  OD2 . ASP B 2 175 ? 45.819  4.836   -15.637 1.00 58.44 ? 170 ASP B OD2 1 
ATOM   1581 N  N   . SER B 2 176 ? 43.232  4.513   -10.677 1.00 43.21 ? 171 SER B N   1 
ATOM   1582 C  CA  . SER B 2 176 ? 43.363  4.830   -9.259  1.00 44.46 ? 171 SER B CA  1 
ATOM   1583 C  C   . SER B 2 176 ? 42.837  3.721   -8.354  1.00 41.16 ? 171 SER B C   1 
ATOM   1584 O  O   . SER B 2 176 ? 43.142  3.723   -7.158  1.00 35.91 ? 171 SER B O   1 
ATOM   1585 C  CB  . SER B 2 176 ? 42.672  6.164   -8.944  1.00 40.06 ? 171 SER B CB  1 
ATOM   1586 O  OG  . SER B 2 176 ? 41.272  6.075   -9.075  1.00 41.28 ? 171 SER B OG  1 
ATOM   1587 N  N   . THR B 2 177 ? 42.075  2.772   -8.891  1.00 41.74 ? 172 THR B N   1 
ATOM   1588 C  CA  . THR B 2 177 ? 41.453  1.745   -8.069  1.00 43.36 ? 172 THR B CA  1 
ATOM   1589 C  C   . THR B 2 177 ? 41.397  0.450   -8.868  1.00 45.95 ? 172 THR B C   1 
ATOM   1590 O  O   . THR B 2 177 ? 41.350  0.463   -10.102 1.00 47.65 ? 172 THR B O   1 
ATOM   1591 C  CB  . THR B 2 177 ? 40.043  2.162   -7.602  1.00 37.84 ? 172 THR B CB  1 
ATOM   1592 O  OG1 . THR B 2 177 ? 39.414  1.070   -6.927  1.00 42.92 ? 172 THR B OG1 1 
ATOM   1593 C  CG2 . THR B 2 177 ? 39.174  2.575   -8.777  1.00 42.08 ? 172 THR B CG2 1 
ATOM   1594 N  N   . ARG B 2 178 ? 41.420  -0.666  -8.150  1.00 39.53 ? 173 ARG B N   1 
ATOM   1595 C  CA  . ARG B 2 178 ? 41.217  -1.974  -8.744  1.00 39.11 ? 173 ARG B CA  1 
ATOM   1596 C  C   . ARG B 2 178 ? 39.748  -2.366  -8.779  1.00 44.72 ? 173 ARG B C   1 
ATOM   1597 O  O   . ARG B 2 178 ? 39.411  -3.423  -9.324  1.00 43.56 ? 173 ARG B O   1 
ATOM   1598 C  CB  . ARG B 2 178 ? 42.047  -3.019  -8.007  1.00 42.91 ? 173 ARG B CB  1 
ATOM   1599 C  CG  . ARG B 2 178 ? 42.415  -2.596  -6.612  1.00 55.16 ? 173 ARG B CG  1 
ATOM   1600 C  CD  . ARG B 2 178 ? 43.134  -3.708  -5.881  1.00 54.54 ? 173 ARG B CD  1 
ATOM   1601 N  NE  . ARG B 2 178 ? 44.512  -3.876  -6.331  1.00 57.05 ? 173 ARG B NE  1 
ATOM   1602 C  CZ  . ARG B 2 178 ? 45.554  -3.251  -5.795  1.00 58.46 ? 173 ARG B CZ  1 
ATOM   1603 N  NH1 . ARG B 2 178 ? 45.399  -2.358  -4.825  1.00 50.37 ? 173 ARG B NH1 1 
ATOM   1604 N  NH2 . ARG B 2 178 ? 46.782  -3.544  -6.228  1.00 49.71 ? 173 ARG B NH2 1 
ATOM   1605 N  N   . ILE B 2 179 ? 38.878  -1.579  -8.145  1.00 46.16 ? 174 ILE B N   1 
ATOM   1606 C  CA  . ILE B 2 179 ? 37.447  -1.797  -8.274  1.00 41.24 ? 174 ILE B CA  1 
ATOM   1607 C  C   . ILE B 2 179 ? 37.039  -1.478  -9.706  1.00 45.84 ? 174 ILE B C   1 
ATOM   1608 O  O   . ILE B 2 179 ? 37.507  -0.494  -10.299 1.00 46.09 ? 174 ILE B O   1 
ATOM   1609 C  CB  . ILE B 2 179 ? 36.692  -0.929  -7.254  1.00 37.06 ? 174 ILE B CB  1 
ATOM   1610 C  CG1 . ILE B 2 179 ? 36.617  -1.634  -5.902  1.00 43.12 ? 174 ILE B CG1 1 
ATOM   1611 C  CG2 . ILE B 2 179 ? 35.314  -0.555  -7.754  1.00 36.49 ? 174 ILE B CG2 1 
ATOM   1612 C  CD1 . ILE B 2 179 ? 36.480  -0.675  -4.727  1.00 41.95 ? 174 ILE B CD1 1 
ATOM   1613 N  N   . ARG B 2 180 ? 36.194  -2.327  -10.289 1.00 45.20 ? 175 ARG B N   1 
ATOM   1614 C  CA  . ARG B 2 180 ? 35.740  -2.114  -11.661 1.00 44.02 ? 175 ARG B CA  1 
ATOM   1615 C  C   . ARG B 2 180 ? 34.772  -0.942  -11.698 1.00 47.78 ? 175 ARG B C   1 
ATOM   1616 O  O   . ARG B 2 180 ? 33.654  -1.043  -11.182 1.00 49.48 ? 175 ARG B O   1 
ATOM   1617 C  CB  . ARG B 2 180 ? 35.077  -3.374  -12.207 1.00 43.98 ? 175 ARG B CB  1 
ATOM   1618 C  CG  . ARG B 2 180 ? 34.530  -3.223  -13.617 1.00 44.90 ? 175 ARG B CG  1 
ATOM   1619 C  CD  . ARG B 2 180 ? 33.464  -4.286  -13.927 1.00 54.01 ? 175 ARG B CD  1 
ATOM   1620 N  NE  . ARG B 2 180 ? 32.602  -3.920  -15.050 1.00 60.89 ? 175 ARG B NE  1 
ATOM   1621 C  CZ  . ARG B 2 180 ? 31.296  -3.684  -14.960 1.00 70.56 ? 175 ARG B CZ  1 
ATOM   1622 N  NH1 . ARG B 2 180 ? 30.650  -3.777  -13.803 1.00 58.68 ? 175 ARG B NH1 1 
ATOM   1623 N  NH2 . ARG B 2 180 ? 30.617  -3.346  -16.060 1.00 67.42 ? 175 ARG B NH2 1 
ATOM   1624 N  N   . ILE B 2 181 ? 35.183  0.169   -12.329 1.00 45.96 ? 176 ILE B N   1 
ATOM   1625 C  CA  . ILE B 2 181 ? 34.314  1.329   -12.458 1.00 45.42 ? 176 ILE B CA  1 
ATOM   1626 C  C   . ILE B 2 181 ? 33.482  1.186   -13.726 1.00 44.27 ? 176 ILE B C   1 
ATOM   1627 O  O   . ILE B 2 181 ? 33.782  0.386   -14.610 1.00 54.44 ? 176 ILE B O   1 
ATOM   1628 C  CB  . ILE B 2 181 ? 35.103  2.656   -12.445 1.00 44.88 ? 176 ILE B CB  1 
ATOM   1629 C  CG1 . ILE B 2 181 ? 35.835  2.882   -13.759 1.00 47.02 ? 176 ILE B CG1 1 
ATOM   1630 C  CG2 . ILE B 2 181 ? 36.086  2.687   -11.297 1.00 43.47 ? 176 ILE B CG2 1 
ATOM   1631 C  CD1 . ILE B 2 181 ? 36.068  4.375   -14.063 1.00 52.49 ? 176 ILE B CD1 1 
ATOM   1632 N  N   . THR B 2 182 ? 32.393  1.943   -13.800 1.00 47.70 ? 177 THR B N   1 
ATOM   1633 C  CA  . THR B 2 182 ? 31.458  1.864   -14.912 1.00 46.67 ? 177 THR B CA  1 
ATOM   1634 C  C   . THR B 2 182 ? 31.181  3.265   -15.412 1.00 43.87 ? 177 THR B C   1 
ATOM   1635 O  O   . THR B 2 182 ? 31.532  4.255   -14.771 1.00 47.30 ? 177 THR B O   1 
ATOM   1636 C  CB  . THR B 2 182 ? 30.130  1.201   -14.517 1.00 47.76 ? 177 THR B CB  1 
ATOM   1637 O  OG1 . THR B 2 182 ? 29.302  2.163   -13.847 1.00 47.53 ? 177 THR B OG1 1 
ATOM   1638 C  CG2 . THR B 2 182 ? 30.367  0.013   -13.607 1.00 44.16 ? 177 THR B CG2 1 
ATOM   1639 N  N   . ASP B 2 183 ? 30.518  3.338   -16.561 1.00 49.67 ? 178 ASP B N   1 
ATOM   1640 C  CA  . ASP B 2 183 ? 30.160  4.623   -17.148 1.00 54.13 ? 178 ASP B CA  1 
ATOM   1641 C  C   . ASP B 2 183 ? 29.081  5.345   -16.354 1.00 51.34 ? 178 ASP B C   1 
ATOM   1642 O  O   . ASP B 2 183 ? 28.789  6.513   -16.641 1.00 49.14 ? 178 ASP B O   1 
ATOM   1643 C  CB  . ASP B 2 183 ? 29.709  4.411   -18.593 1.00 56.02 ? 178 ASP B CB  1 
ATOM   1644 C  CG  . ASP B 2 183 ? 30.563  3.386   -19.315 1.00 68.74 ? 178 ASP B CG  1 
ATOM   1645 O  OD1 . ASP B 2 183 ? 31.680  3.741   -19.781 1.00 61.40 ? 178 ASP B OD1 1 
ATOM   1646 O  OD2 . ASP B 2 183 ? 30.115  2.220   -19.396 1.00 74.26 ? 178 ASP B OD2 1 
ATOM   1647 N  N   . ASN B 2 184 ? 28.498  4.682   -15.364 1.00 47.08 ? 179 ASN B N   1 
ATOM   1648 C  CA  . ASN B 2 184 ? 27.534  5.280   -14.457 1.00 49.69 ? 179 ASN B CA  1 
ATOM   1649 C  C   . ASN B 2 184 ? 28.214  5.974   -13.291 1.00 46.47 ? 179 ASN B C   1 
ATOM   1650 O  O   . ASN B 2 184 ? 27.536  6.467   -12.382 1.00 42.72 ? 179 ASN B O   1 
ATOM   1651 C  CB  . ASN B 2 184 ? 26.589  4.199   -13.945 1.00 48.33 ? 179 ASN B CB  1 
ATOM   1652 C  CG  . ASN B 2 184 ? 25.888  3.484   -15.077 1.00 52.11 ? 179 ASN B CG  1 
ATOM   1653 O  OD1 . ASN B 2 184 ? 25.404  4.125   -16.016 1.00 50.47 ? 179 ASN B OD1 1 
ATOM   1654 N  ND2 . ASN B 2 184 ? 25.851  2.153   -15.016 1.00 47.12 ? 179 ASN B ND2 1 
ATOM   1655 N  N   . MET B 2 185 ? 29.535  6.039   -13.326 1.00 41.45 ? 180 MET B N   1 
ATOM   1656 C  CA  . MET B 2 185 ? 30.337  6.658   -12.298 1.00 40.91 ? 180 MET B CA  1 
ATOM   1657 C  C   . MET B 2 185 ? 31.225  7.723   -12.914 1.00 43.46 ? 180 MET B C   1 
ATOM   1658 O  O   . MET B 2 185 ? 31.601  7.645   -14.089 1.00 48.82 ? 180 MET B O   1 
ATOM   1659 C  CB  . MET B 2 185 ? 31.205  5.614   -11.614 1.00 36.54 ? 180 MET B CB  1 
ATOM   1660 C  CG  . MET B 2 185 ? 30.449  4.585   -10.860 1.00 31.85 ? 180 MET B CG  1 
ATOM   1661 S  SD  . MET B 2 185 ? 31.627  3.341   -10.325 1.00 36.16 ? 180 MET B SD  1 
ATOM   1662 C  CE  . MET B 2 185 ? 30.585  1.878   -10.204 1.00 39.39 ? 180 MET B CE  1 
ATOM   1663 N  N   . PHE B 2 186 ? 31.530  8.738   -12.117 1.00 41.09 ? 181 PHE B N   1 
ATOM   1664 C  CA  . PHE B 2 186 ? 32.662  9.598   -12.407 1.00 35.34 ? 181 PHE B CA  1 
ATOM   1665 C  C   . PHE B 2 186 ? 33.390  9.849   -11.100 1.00 38.10 ? 181 PHE B C   1 
ATOM   1666 O  O   . PHE B 2 186 ? 32.842  9.660   -10.014 1.00 36.05 ? 181 PHE B O   1 
ATOM   1667 C  CB  . PHE B 2 186 ? 32.255  10.899  -13.098 1.00 30.80 ? 181 PHE B CB  1 
ATOM   1668 C  CG  . PHE B 2 186 ? 31.507  11.879  -12.224 1.00 36.76 ? 181 PHE B CG  1 
ATOM   1669 C  CD1 . PHE B 2 186 ? 30.121  11.861  -12.163 1.00 38.92 ? 181 PHE B CD1 1 
ATOM   1670 C  CD2 . PHE B 2 186 ? 32.179  12.865  -11.526 1.00 40.32 ? 181 PHE B CD2 1 
ATOM   1671 C  CE1 . PHE B 2 186 ? 29.427  12.788  -11.399 1.00 37.03 ? 181 PHE B CE1 1 
ATOM   1672 C  CE2 . PHE B 2 186 ? 31.485  13.798  -10.759 1.00 39.35 ? 181 PHE B CE2 1 
ATOM   1673 C  CZ  . PHE B 2 186 ? 30.110  13.755  -10.699 1.00 37.01 ? 181 PHE B CZ  1 
ATOM   1674 N  N   . CYS B 2 187 ? 34.652  10.232  -11.205 1.00 35.67 ? 182 CYS B N   1 
ATOM   1675 C  CA  . CYS B 2 187 ? 35.433  10.482  -10.015 1.00 39.52 ? 182 CYS B CA  1 
ATOM   1676 C  C   . CYS B 2 187 ? 35.948  11.917  -10.055 1.00 41.50 ? 182 CYS B C   1 
ATOM   1677 O  O   . CYS B 2 187 ? 36.004  12.562  -11.111 1.00 40.82 ? 182 CYS B O   1 
ATOM   1678 C  CB  . CYS B 2 187 ? 36.558  9.429   -9.860  1.00 38.42 ? 182 CYS B CB  1 
ATOM   1679 S  SG  . CYS B 2 187 ? 38.203  9.799   -10.539 1.00 46.75 ? 182 CYS B SG  1 
ATOM   1680 N  N   . ALA B 2 188 ? 36.275  12.425  -8.869  1.00 40.35 ? 183 ALA B N   1 
ATOM   1681 C  CA  . ALA B 2 188 ? 36.694  13.811  -8.725  1.00 40.18 ? 183 ALA B CA  1 
ATOM   1682 C  C   . ALA B 2 188 ? 37.596  13.936  -7.511  1.00 38.89 ? 183 ALA B C   1 
ATOM   1683 O  O   . ALA B 2 188 ? 37.617  13.076  -6.617  1.00 42.17 ? 183 ALA B O   1 
ATOM   1684 C  CB  . ALA B 2 188 ? 35.492  14.766  -8.605  1.00 38.41 ? 183 ALA B CB  1 
ATOM   1685 N  N   . GLY B 2 189 ? 38.339  15.046  -7.493  1.00 38.29 ? 184 GLY B N   1 
ATOM   1686 C  CA  . GLY B 2 189 ? 39.385  15.286  -6.529  1.00 45.02 ? 184 GLY B CA  1 
ATOM   1687 C  C   . GLY B 2 189 ? 40.649  15.801  -7.159  1.00 43.11 ? 184 GLY B C   1 
ATOM   1688 O  O   . GLY B 2 189 ? 40.847  15.739  -8.400  1.00 39.68 ? 184 GLY B O   1 
ATOM   1689 N  N   . TYR B 2 190 A 41.531  16.337  -6.328  1.00 41.43 ? 184 TYR B N   1 
ATOM   1690 C  CA  . TYR B 2 190 A 42.822  16.830  -6.757  1.00 41.26 ? 184 TYR B CA  1 
ATOM   1691 C  C   . TYR B 2 190 A 43.846  15.701  -6.871  1.00 41.83 ? 184 TYR B C   1 
ATOM   1692 O  O   . TYR B 2 190 A 43.845  14.734  -6.099  1.00 36.56 ? 184 TYR B O   1 
ATOM   1693 C  CB  . TYR B 2 190 A 43.325  17.904  -5.799  1.00 36.97 ? 184 TYR B CB  1 
ATOM   1694 C  CG  . TYR B 2 190 A 42.525  19.191  -5.892  1.00 42.32 ? 184 TYR B CG  1 
ATOM   1695 C  CD1 . TYR B 2 190 A 42.611  20.007  -7.012  1.00 42.37 ? 184 TYR B CD1 1 
ATOM   1696 C  CD2 . TYR B 2 190 A 41.669  19.582  -4.868  1.00 41.57 ? 184 TYR B CD2 1 
ATOM   1697 C  CE1 . TYR B 2 190 A 41.881  21.180  -7.103  1.00 41.97 ? 184 TYR B CE1 1 
ATOM   1698 C  CE2 . TYR B 2 190 A 40.929  20.749  -4.953  1.00 35.53 ? 184 TYR B CE2 1 
ATOM   1699 C  CZ  . TYR B 2 190 A 41.037  21.543  -6.071  1.00 41.30 ? 184 TYR B CZ  1 
ATOM   1700 O  OH  . TYR B 2 190 A 40.309  22.710  -6.151  1.00 43.36 ? 184 TYR B OH  1 
ATOM   1701 N  N   . LYS B 2 191 ? 44.720  15.830  -7.859  1.00 47.24 ? 185 LYS B N   1 
ATOM   1702 C  CA  . LYS B 2 191 ? 45.873  14.957  -7.987  1.00 48.31 ? 185 LYS B CA  1 
ATOM   1703 C  C   . LYS B 2 191 ? 46.926  15.335  -6.949  1.00 44.43 ? 185 LYS B C   1 
ATOM   1704 O  O   . LYS B 2 191 ? 46.878  16.425  -6.375  1.00 45.42 ? 185 LYS B O   1 
ATOM   1705 C  CB  . LYS B 2 191 ? 46.409  15.049  -9.415  1.00 47.17 ? 185 LYS B CB  1 
ATOM   1706 C  CG  . LYS B 2 191 ? 45.324  14.658  -10.415 1.00 45.42 ? 185 LYS B CG  1 
ATOM   1707 C  CD  . LYS B 2 191 ? 45.625  15.033  -11.843 1.00 45.94 ? 185 LYS B CD  1 
ATOM   1708 C  CE  . LYS B 2 191 ? 44.437  14.647  -12.719 1.00 47.36 ? 185 LYS B CE  1 
ATOM   1709 N  NZ  . LYS B 2 191 ? 44.636  14.945  -14.162 1.00 56.34 ? 185 LYS B NZ  1 
ATOM   1710 N  N   . PRO B 2 192 ? 47.856  14.431  -6.633  1.00 47.12 ? 186 PRO B N   1 
ATOM   1711 C  CA  . PRO B 2 192 ? 48.876  14.793  -5.631  1.00 54.47 ? 186 PRO B CA  1 
ATOM   1712 C  C   . PRO B 2 192 ? 49.689  16.010  -6.059  1.00 58.30 ? 186 PRO B C   1 
ATOM   1713 O  O   . PRO B 2 192 ? 50.093  16.823  -5.214  1.00 54.34 ? 186 PRO B O   1 
ATOM   1714 C  CB  . PRO B 2 192 ? 49.739  13.528  -5.531  1.00 48.19 ? 186 PRO B CB  1 
ATOM   1715 C  CG  . PRO B 2 192 ? 48.862  12.427  -6.051  1.00 48.77 ? 186 PRO B CG  1 
ATOM   1716 C  CD  . PRO B 2 192 ? 48.036  13.056  -7.130  1.00 47.32 ? 186 PRO B CD  1 
ATOM   1717 N  N   . ASP B 2 193 A 49.871  16.186  -7.373  1.00 57.17 ? 186 ASP B N   1 
ATOM   1718 C  CA  . ASP B 2 193 A 50.678  17.282  -7.894  1.00 57.66 ? 186 ASP B CA  1 
ATOM   1719 C  C   . ASP B 2 193 A 50.020  18.636  -7.683  1.00 61.59 ? 186 ASP B C   1 
ATOM   1720 O  O   . ASP B 2 193 A 50.719  19.639  -7.509  1.00 62.59 ? 186 ASP B O   1 
ATOM   1721 C  CB  . ASP B 2 193 A 50.895  17.082  -9.394  1.00 57.60 ? 186 ASP B CB  1 
ATOM   1722 C  CG  . ASP B 2 193 A 51.992  16.085  -9.698  1.00 72.74 ? 186 ASP B CG  1 
ATOM   1723 O  OD1 . ASP B 2 193 A 52.547  15.490  -8.740  1.00 70.41 ? 186 ASP B OD1 1 
ATOM   1724 O  OD2 . ASP B 2 193 A 52.288  15.889  -10.903 1.00 78.43 ? 186 ASP B OD2 1 
ATOM   1725 N  N   . GLU B 2 194 B 48.693  18.687  -7.647  1.00 59.53 ? 186 GLU B N   1 
ATOM   1726 C  CA  . GLU B 2 194 B 48.019  19.976  -7.682  1.00 50.97 ? 186 GLU B CA  1 
ATOM   1727 C  C   . GLU B 2 194 B 48.047  20.704  -6.351  1.00 51.37 ? 186 GLU B C   1 
ATOM   1728 O  O   . GLU B 2 194 B 47.568  21.840  -6.283  1.00 56.06 ? 186 GLU B O   1 
ATOM   1729 C  CB  . GLU B 2 194 B 46.583  19.794  -8.153  1.00 50.82 ? 186 GLU B CB  1 
ATOM   1730 C  CG  . GLU B 2 194 B 46.476  19.066  -9.474  1.00 49.76 ? 186 GLU B CG  1 
ATOM   1731 C  CD  . GLU B 2 194 B 45.030  18.880  -9.896  1.00 55.07 ? 186 GLU B CD  1 
ATOM   1732 O  OE1 . GLU B 2 194 B 44.370  19.897  -10.200 1.00 56.87 ? 186 GLU B OE1 1 
ATOM   1733 O  OE2 . GLU B 2 194 B 44.542  17.724  -9.908  1.00 55.58 ? 186 GLU B OE2 1 
ATOM   1734 N  N   . GLY B 2 195 C 48.590  20.093  -5.302  1.00 49.70 ? 186 GLY B N   1 
ATOM   1735 C  CA  . GLY B 2 195 C 48.818  20.795  -4.051  1.00 46.85 ? 186 GLY B CA  1 
ATOM   1736 C  C   . GLY B 2 195 C 47.621  21.335  -3.279  1.00 53.33 ? 186 GLY B C   1 
ATOM   1737 O  O   . GLY B 2 195 C 47.817  22.020  -2.274  1.00 62.48 ? 186 GLY B O   1 
ATOM   1738 N  N   . LYS B 2 196 D 46.393  21.039  -3.700  1.00 50.67 ? 186 LYS B N   1 
ATOM   1739 C  CA  . LYS B 2 196 D 45.201  21.226  -2.881  1.00 41.90 ? 186 LYS B CA  1 
ATOM   1740 C  C   . LYS B 2 196 D 44.604  19.881  -2.520  1.00 43.10 ? 186 LYS B C   1 
ATOM   1741 O  O   . LYS B 2 196 D 44.925  18.853  -3.121  1.00 48.68 ? 186 LYS B O   1 
ATOM   1742 C  CB  . LYS B 2 196 D 44.125  22.055  -3.580  1.00 41.55 ? 186 LYS B CB  1 
ATOM   1743 C  CG  . LYS B 2 196 D 44.614  23.237  -4.362  1.00 43.66 ? 186 LYS B CG  1 
ATOM   1744 C  CD  . LYS B 2 196 D 43.652  24.401  -4.186  1.00 49.96 ? 186 LYS B CD  1 
ATOM   1745 C  CE  . LYS B 2 196 D 43.470  25.173  -5.487  1.00 49.87 ? 186 LYS B CE  1 
ATOM   1746 N  NZ  . LYS B 2 196 D 42.765  26.475  -5.282  1.00 59.35 ? 186 LYS B NZ  1 
ATOM   1747 N  N   . ARG B 2 197 ? 43.739  19.899  -1.514  1.00 37.51 ? 187 ARG B N   1 
ATOM   1748 C  CA  . ARG B 2 197 ? 43.113  18.688  -1.007  1.00 37.56 ? 187 ARG B CA  1 
ATOM   1749 C  C   . ARG B 2 197 ? 41.596  18.877  -0.951  1.00 38.92 ? 187 ARG B C   1 
ATOM   1750 O  O   . ARG B 2 197 ? 41.059  19.938  -1.308  1.00 34.74 ? 187 ARG B O   1 
ATOM   1751 C  CB  . ARG B 2 197 ? 43.678  18.319  0.370   1.00 36.12 ? 187 ARG B CB  1 
ATOM   1752 C  CG  . ARG B 2 197 ? 45.170  18.127  0.382   1.00 36.63 ? 187 ARG B CG  1 
ATOM   1753 C  CD  . ARG B 2 197 ? 45.640  17.427  1.643   1.00 36.54 ? 187 ARG B CD  1 
ATOM   1754 N  NE  . ARG B 2 197 ? 45.530  15.975  1.550   1.00 35.24 ? 187 ARG B NE  1 
ATOM   1755 C  CZ  . ARG B 2 197 ? 46.297  15.213  0.783   1.00 37.89 ? 187 ARG B CZ  1 
ATOM   1756 N  NH1 . ARG B 2 197 ? 47.287  15.725  0.067   1.00 37.33 ? 187 ARG B NH1 1 
ATOM   1757 N  NH2 . ARG B 2 197 ? 46.058  13.903  0.722   1.00 39.85 ? 187 ARG B NH2 1 
ATOM   1758 N  N   . GLY B 2 198 ? 40.906  17.841  -0.467  1.00 35.34 ? 188 GLY B N   1 
ATOM   1759 C  CA  . GLY B 2 198 ? 39.453  17.831  -0.423  1.00 35.82 ? 188 GLY B CA  1 
ATOM   1760 C  C   . GLY B 2 198 ? 38.873  16.496  -0.863  1.00 38.40 ? 188 GLY B C   1 
ATOM   1761 O  O   . GLY B 2 198 ? 39.426  15.828  -1.741  1.00 37.62 ? 188 GLY B O   1 
ATOM   1762 N  N   . ASP B 2 199 ? 37.775  16.079  -0.237  1.00 41.74 ? 189 ASP B N   1 
ATOM   1763 C  CA  . ASP B 2 199 ? 37.135  14.811  -0.563  1.00 39.05 ? 189 ASP B CA  1 
ATOM   1764 C  C   . ASP B 2 199 ? 35.827  14.691  0.205   1.00 40.20 ? 189 ASP B C   1 
ATOM   1765 O  O   . ASP B 2 199 ? 35.623  15.346  1.231   1.00 38.64 ? 189 ASP B O   1 
ATOM   1766 C  CB  . ASP B 2 199 ? 38.033  13.618  -0.236  1.00 34.89 ? 189 ASP B CB  1 
ATOM   1767 C  CG  . ASP B 2 199 ? 37.594  12.377  -0.938  1.00 33.25 ? 189 ASP B CG  1 
ATOM   1768 O  OD1 . ASP B 2 199 ? 36.610  12.460  -1.706  1.00 33.20 ? 189 ASP B OD1 1 
ATOM   1769 O  OD2 . ASP B 2 199 ? 38.217  11.323  -0.718  1.00 38.86 ? 189 ASP B OD2 1 
ATOM   1770 N  N   . ALA B 2 200 ? 34.945  13.837  -0.307  1.00 39.54 ? 190 ALA B N   1 
ATOM   1771 C  CA  . ALA B 2 200 ? 33.835  13.366  0.497   1.00 41.01 ? 190 ALA B CA  1 
ATOM   1772 C  C   . ALA B 2 200 ? 34.338  12.276  1.440   1.00 40.50 ? 190 ALA B C   1 
ATOM   1773 O  O   . ALA B 2 200 ? 35.469  11.798  1.328   1.00 36.03 ? 190 ALA B O   1 
ATOM   1774 C  CB  . ALA B 2 200 ? 32.704  12.857  -0.397  1.00 36.88 ? 190 ALA B CB  1 
ATOM   1775 N  N   . CYS B 2 201 ? 33.504  11.888  2.397   1.00 39.62 ? 191 CYS B N   1 
ATOM   1776 C  CA  . CYS B 2 201 ? 33.918  10.846  3.324   1.00 41.38 ? 191 CYS B CA  1 
ATOM   1777 C  C   . CYS B 2 201 ? 32.690  10.076  3.785   1.00 41.44 ? 191 CYS B C   1 
ATOM   1778 O  O   . CYS B 2 201 ? 31.557  10.364  3.377   1.00 42.80 ? 191 CYS B O   1 
ATOM   1779 C  CB  . CYS B 2 201 ? 34.695  11.448  4.505   1.00 41.11 ? 191 CYS B CB  1 
ATOM   1780 S  SG  . CYS B 2 201 ? 35.746  10.281  5.386   1.00 41.86 ? 191 CYS B SG  1 
ATOM   1781 N  N   . GLU B 2 202 ? 32.926  9.100   4.663   1.00 44.33 ? 192 GLU B N   1 
ATOM   1782 C  CA  . GLU B 2 202 ? 31.843  8.269   5.168   1.00 44.69 ? 192 GLU B CA  1 
ATOM   1783 C  C   . GLU B 2 202 ? 30.768  9.149   5.780   1.00 38.72 ? 192 GLU B C   1 
ATOM   1784 O  O   . GLU B 2 202 ? 31.056  10.011  6.607   1.00 44.92 ? 192 GLU B O   1 
ATOM   1785 C  CB  . GLU B 2 202 ? 32.381  7.274   6.191   1.00 48.09 ? 192 GLU B CB  1 
ATOM   1786 C  CG  . GLU B 2 202 ? 33.461  6.344   5.612   1.00 51.70 ? 192 GLU B CG  1 
ATOM   1787 C  CD  . GLU B 2 202 ? 33.061  4.876   5.710   1.00 61.09 ? 192 GLU B CD  1 
ATOM   1788 O  OE1 . GLU B 2 202 ? 31.977  4.587   6.275   1.00 68.76 ? 192 GLU B OE1 1 
ATOM   1789 O  OE2 . GLU B 2 202 ? 33.823  4.010   5.229   1.00 62.95 ? 192 GLU B OE2 1 
ATOM   1790 N  N   . GLY B 2 203 ? 29.531  8.943   5.365   1.00 34.91 ? 193 GLY B N   1 
ATOM   1791 C  CA  . GLY B 2 203 ? 28.413  9.727   5.834   1.00 32.79 ? 193 GLY B CA  1 
ATOM   1792 C  C   . GLY B 2 203 ? 27.924  10.728  4.821   1.00 38.84 ? 193 GLY B C   1 
ATOM   1793 O  O   . GLY B 2 203 ? 26.746  11.104  4.859   1.00 34.35 ? 193 GLY B O   1 
ATOM   1794 N  N   . ASP B 2 204 ? 28.785  11.138  3.886   1.00 39.70 ? 194 ASP B N   1 
ATOM   1795 C  CA  . ASP B 2 204 ? 28.381  12.086  2.858   1.00 35.33 ? 194 ASP B CA  1 
ATOM   1796 C  C   . ASP B 2 204 ? 27.594  11.443  1.714   1.00 32.48 ? 194 ASP B C   1 
ATOM   1797 O  O   . ASP B 2 204 ? 27.065  12.178  0.873   1.00 28.27 ? 194 ASP B O   1 
ATOM   1798 C  CB  . ASP B 2 204 ? 29.618  12.798  2.317   1.00 36.71 ? 194 ASP B CB  1 
ATOM   1799 C  CG  . ASP B 2 204 ? 30.168  13.837  3.286   1.00 36.72 ? 194 ASP B CG  1 
ATOM   1800 O  OD1 . ASP B 2 204 ? 29.381  14.653  3.812   1.00 33.75 ? 194 ASP B OD1 1 
ATOM   1801 O  OD2 . ASP B 2 204 ? 31.395  13.854  3.499   1.00 42.43 ? 194 ASP B OD2 1 
ATOM   1802 N  N   . SER B 2 205 ? 27.495  10.106  1.670   1.00 30.80 ? 195 SER B N   1 
ATOM   1803 C  CA  . SER B 2 205 ? 26.777  9.423   0.598   1.00 31.54 ? 195 SER B CA  1 
ATOM   1804 C  C   . SER B 2 205 ? 25.372  9.992   0.430   1.00 36.72 ? 195 SER B C   1 
ATOM   1805 O  O   . SER B 2 205 ? 24.679  10.301  1.410   1.00 36.07 ? 195 SER B O   1 
ATOM   1806 C  CB  . SER B 2 205 ? 26.671  7.919   0.880   1.00 35.22 ? 195 SER B CB  1 
ATOM   1807 O  OG  . SER B 2 205 ? 27.926  7.243   0.881   1.00 44.41 ? 195 SER B OG  1 
ATOM   1808 N  N   . GLY B 2 206 ? 24.947  10.113  -0.830  1.00 33.94 ? 196 GLY B N   1 
ATOM   1809 C  CA  . GLY B 2 206 ? 23.677  10.703  -1.151  1.00 32.00 ? 196 GLY B CA  1 
ATOM   1810 C  C   . GLY B 2 206 ? 23.698  12.206  -1.323  1.00 33.52 ? 196 GLY B C   1 
ATOM   1811 O  O   . GLY B 2 206 ? 22.733  12.767  -1.849  1.00 39.99 ? 196 GLY B O   1 
ATOM   1812 N  N   . GLY B 2 207 ? 24.749  12.883  -0.875  1.00 36.09 ? 197 GLY B N   1 
ATOM   1813 C  CA  . GLY B 2 207 ? 24.888  14.307  -1.108  1.00 33.43 ? 197 GLY B CA  1 
ATOM   1814 C  C   . GLY B 2 207 ? 25.092  14.640  -2.570  1.00 31.84 ? 197 GLY B C   1 
ATOM   1815 O  O   . GLY B 2 207 ? 25.419  13.779  -3.393  1.00 31.50 ? 197 GLY B O   1 
ATOM   1816 N  N   . PRO B 2 208 ? 24.839  15.890  -2.937  1.00 31.07 ? 198 PRO B N   1 
ATOM   1817 C  CA  . PRO B 2 208 ? 24.930  16.257  -4.351  1.00 28.45 ? 198 PRO B CA  1 
ATOM   1818 C  C   . PRO B 2 208 ? 26.309  16.750  -4.747  1.00 38.53 ? 198 PRO B C   1 
ATOM   1819 O  O   . PRO B 2 208 ? 27.009  17.429  -3.987  1.00 35.81 ? 198 PRO B O   1 
ATOM   1820 C  CB  . PRO B 2 208 ? 23.899  17.387  -4.478  1.00 29.08 ? 198 PRO B CB  1 
ATOM   1821 C  CG  . PRO B 2 208 ? 23.878  18.012  -3.138  1.00 28.43 ? 198 PRO B CG  1 
ATOM   1822 C  CD  . PRO B 2 208 ? 24.116  16.897  -2.144  1.00 32.31 ? 198 PRO B CD  1 
ATOM   1823 N  N   . PHE B 2 209 ? 26.686  16.403  -5.977  1.00 35.04 ? 199 PHE B N   1 
ATOM   1824 C  CA  . PHE B 2 209 ? 27.789  17.030  -6.685  1.00 30.14 ? 199 PHE B CA  1 
ATOM   1825 C  C   . PHE B 2 209 ? 27.131  18.015  -7.641  1.00 31.83 ? 199 PHE B C   1 
ATOM   1826 O  O   . PHE B 2 209 ? 26.407  17.604  -8.551  1.00 35.81 ? 199 PHE B O   1 
ATOM   1827 C  CB  . PHE B 2 209 ? 28.624  15.976  -7.417  1.00 35.81 ? 199 PHE B CB  1 
ATOM   1828 C  CG  . PHE B 2 209 ? 29.886  16.514  -8.062  1.00 40.15 ? 199 PHE B CG  1 
ATOM   1829 C  CD1 . PHE B 2 209 ? 29.846  17.133  -9.306  1.00 36.30 ? 199 PHE B CD1 1 
ATOM   1830 C  CD2 . PHE B 2 209 ? 31.115  16.375  -7.433  1.00 38.66 ? 199 PHE B CD2 1 
ATOM   1831 C  CE1 . PHE B 2 209 ? 30.994  17.618  -9.897  1.00 33.40 ? 199 PHE B CE1 1 
ATOM   1832 C  CE2 . PHE B 2 209 ? 32.263  16.854  -8.025  1.00 33.99 ? 199 PHE B CE2 1 
ATOM   1833 C  CZ  . PHE B 2 209 ? 32.200  17.479  -9.255  1.00 36.90 ? 199 PHE B CZ  1 
ATOM   1834 N  N   . VAL B 2 210 ? 27.307  19.311  -7.399  1.00 30.19 ? 200 VAL B N   1 
ATOM   1835 C  CA  . VAL B 2 210 ? 26.602  20.309  -8.190  1.00 32.01 ? 200 VAL B CA  1 
ATOM   1836 C  C   . VAL B 2 210 ? 27.610  21.184  -8.929  1.00 36.34 ? 200 VAL B C   1 
ATOM   1837 O  O   . VAL B 2 210 ? 28.783  21.285  -8.555  1.00 36.25 ? 200 VAL B O   1 
ATOM   1838 C  CB  . VAL B 2 210 ? 25.644  21.176  -7.330  1.00 35.07 ? 200 VAL B CB  1 
ATOM   1839 C  CG1 . VAL B 2 210 ? 24.588  20.302  -6.634  1.00 31.57 ? 200 VAL B CG1 1 
ATOM   1840 C  CG2 . VAL B 2 210 ? 26.406  22.027  -6.310  1.00 28.83 ? 200 VAL B CG2 1 
ATOM   1841 N  N   . MET B 2 211 ? 27.125  21.823  -9.997  1.00 37.28 ? 201 MET B N   1 
ATOM   1842 C  CA  . MET B 2 211 ? 27.900  22.724  -10.848 1.00 40.31 ? 201 MET B CA  1 
ATOM   1843 C  C   . MET B 2 211 ? 26.993  23.884  -11.227 1.00 40.61 ? 201 MET B C   1 
ATOM   1844 O  O   . MET B 2 211 ? 25.798  23.685  -11.461 1.00 40.54 ? 201 MET B O   1 
ATOM   1845 C  CB  . MET B 2 211 ? 28.415  22.041  -12.137 1.00 37.47 ? 201 MET B CB  1 
ATOM   1846 C  CG  . MET B 2 211 ? 28.951  20.629  -11.958 1.00 37.03 ? 201 MET B CG  1 
ATOM   1847 S  SD  . MET B 2 211 ? 29.999  19.934  -13.292 1.00 37.42 ? 201 MET B SD  1 
ATOM   1848 C  CE  . MET B 2 211 ? 31.026  21.333  -13.800 1.00 34.59 ? 201 MET B CE  1 
ATOM   1849 N  N   . LYS B 2 212 ? 27.541  25.098  -11.261 1.00 39.56 ? 202 LYS B N   1 
ATOM   1850 C  CA  . LYS B 2 212 ? 26.761  26.273  -11.631 1.00 40.92 ? 202 LYS B CA  1 
ATOM   1851 C  C   . LYS B 2 212 ? 27.002  26.579  -13.103 1.00 43.69 ? 202 LYS B C   1 
ATOM   1852 O  O   . LYS B 2 212 ? 28.135  26.870  -13.500 1.00 37.35 ? 202 LYS B O   1 
ATOM   1853 C  CB  . LYS B 2 212 ? 27.108  27.495  -10.785 1.00 39.78 ? 202 LYS B CB  1 
ATOM   1854 C  CG  . LYS B 2 212 ? 26.425  28.752  -11.325 1.00 38.02 ? 202 LYS B CG  1 
ATOM   1855 C  CD  . LYS B 2 212 ? 26.557  29.915  -10.384 1.00 35.79 ? 202 LYS B CD  1 
ATOM   1856 C  CE  . LYS B 2 212 ? 25.504  30.944  -10.681 1.00 39.25 ? 202 LYS B CE  1 
ATOM   1857 N  NZ  . LYS B 2 212 ? 25.476  31.985  -9.647  1.00 34.70 ? 202 LYS B NZ  1 
ATOM   1858 N  N   . SER B 2 213 ? 25.930  26.547  -13.894 1.00 47.85 ? 203 SER B N   1 
ATOM   1859 C  CA  . SER B 2 213 ? 26.051  26.648  -15.345 1.00 47.59 ? 203 SER B CA  1 
ATOM   1860 C  C   . SER B 2 213 ? 26.340  28.091  -15.751 1.00 45.25 ? 203 SER B C   1 
ATOM   1861 O  O   . SER B 2 213 ? 25.546  28.979  -15.455 1.00 49.50 ? 203 SER B O   1 
ATOM   1862 C  CB  . SER B 2 213 ? 24.773  26.179  -16.026 1.00 46.73 ? 203 SER B CB  1 
ATOM   1863 O  OG  . SER B 2 213 ? 24.765  26.590  -17.384 1.00 51.34 ? 203 SER B OG  1 
ATOM   1864 N  N   . PRO B 2 214 ? 27.429  28.328  -16.496 1.00 42.78 ? 204 PRO B N   1 
ATOM   1865 C  CA  . PRO B 2 214 ? 27.713  29.693  -16.973 1.00 48.57 ? 204 PRO B CA  1 
ATOM   1866 C  C   . PRO B 2 214 ? 26.722  30.196  -18.008 1.00 48.68 ? 204 PRO B C   1 
ATOM   1867 O  O   . PRO B 2 214 ? 26.711  31.403  -18.293 1.00 45.04 ? 204 PRO B O   1 
ATOM   1868 C  CB  . PRO B 2 214 ? 29.118  29.559  -17.591 1.00 46.29 ? 204 PRO B CB  1 
ATOM   1869 C  CG  . PRO B 2 214 ? 29.490  28.109  -17.499 1.00 41.48 ? 204 PRO B CG  1 
ATOM   1870 C  CD  . PRO B 2 214 ? 28.291  27.321  -17.114 1.00 44.55 ? 204 PRO B CD  1 
ATOM   1871 N  N   . PHE B 2 215 A 25.899  29.314  -18.580 1.00 49.60 ? 204 PHE B N   1 
ATOM   1872 C  CA  . PHE B 2 215 A 24.947  29.718  -19.607 1.00 51.89 ? 204 PHE B CA  1 
ATOM   1873 C  C   . PHE B 2 215 A 23.680  30.319  -19.009 1.00 54.30 ? 204 PHE B C   1 
ATOM   1874 O  O   . PHE B 2 215 A 23.137  31.288  -19.551 1.00 53.94 ? 204 PHE B O   1 
ATOM   1875 C  CB  . PHE B 2 215 A 24.617  28.521  -20.502 1.00 48.61 ? 204 PHE B CB  1 
ATOM   1876 C  CG  . PHE B 2 215 A 25.824  27.722  -20.885 1.00 54.75 ? 204 PHE B CG  1 
ATOM   1877 C  CD1 . PHE B 2 215 A 26.859  28.314  -21.614 1.00 51.17 ? 204 PHE B CD1 1 
ATOM   1878 C  CD2 . PHE B 2 215 A 25.938  26.382  -20.527 1.00 57.53 ? 204 PHE B CD2 1 
ATOM   1879 C  CE1 . PHE B 2 215 A 27.993  27.587  -21.972 1.00 55.42 ? 204 PHE B CE1 1 
ATOM   1880 C  CE2 . PHE B 2 215 A 27.076  25.633  -20.891 1.00 58.20 ? 204 PHE B CE2 1 
ATOM   1881 C  CZ  . PHE B 2 215 A 28.104  26.243  -21.613 1.00 57.57 ? 204 PHE B CZ  1 
ATOM   1882 N  N   . ASN B 2 216 B 23.180  29.768  -17.902 1.00 53.71 ? 204 ASN B N   1 
ATOM   1883 C  CA  . ASN B 2 216 B 21.943  30.277  -17.325 1.00 50.42 ? 204 ASN B CA  1 
ATOM   1884 C  C   . ASN B 2 216 B 22.011  30.496  -15.814 1.00 55.65 ? 204 ASN B C   1 
ATOM   1885 O  O   . ASN B 2 216 B 20.961  30.701  -15.186 1.00 53.64 ? 204 ASN B O   1 
ATOM   1886 C  CB  . ASN B 2 216 B 20.789  29.334  -17.679 1.00 47.84 ? 204 ASN B CB  1 
ATOM   1887 C  CG  . ASN B 2 216 B 20.966  27.957  -17.102 1.00 51.02 ? 204 ASN B CG  1 
ATOM   1888 O  OD1 . ASN B 2 216 B 21.970  27.667  -16.442 1.00 53.78 ? 204 ASN B OD1 1 
ATOM   1889 N  ND2 . ASN B 2 216 B 19.986  27.089  -17.341 1.00 46.53 ? 204 ASN B ND2 1 
ATOM   1890 N  N   . ASN B 2 217 ? 23.203  30.413  -15.212 1.00 55.45 ? 205 ASN B N   1 
ATOM   1891 C  CA  . ASN B 2 217 ? 23.417  30.666  -13.778 1.00 55.00 ? 205 ASN B CA  1 
ATOM   1892 C  C   . ASN B 2 217 ? 22.554  29.791  -12.880 1.00 50.13 ? 205 ASN B C   1 
ATOM   1893 O  O   . ASN B 2 217 ? 22.298  30.153  -11.732 1.00 54.28 ? 205 ASN B O   1 
ATOM   1894 C  CB  . ASN B 2 217 ? 23.188  32.137  -13.413 1.00 49.13 ? 205 ASN B CB  1 
ATOM   1895 C  CG  . ASN B 2 217 ? 23.826  33.069  -14.393 1.00 66.15 ? 205 ASN B CG  1 
ATOM   1896 O  OD1 . ASN B 2 217 ? 23.135  33.711  -15.191 1.00 64.28 ? 205 ASN B OD1 1 
ATOM   1897 N  ND2 . ASN B 2 217 ? 25.165  33.154  -14.353 1.00 66.50 ? 205 ASN B ND2 1 
ATOM   1898 N  N   . ARG B 2 218 ? 22.124  28.628  -13.356 1.00 48.70 ? 206 ARG B N   1 
ATOM   1899 C  CA  . ARG B 2 218 ? 21.364  27.713  -12.521 1.00 43.47 ? 206 ARG B CA  1 
ATOM   1900 C  C   . ARG B 2 218 ? 22.309  26.629  -12.035 1.00 43.08 ? 206 ARG B C   1 
ATOM   1901 O  O   . ARG B 2 218 ? 23.293  26.302  -12.701 1.00 43.74 ? 206 ARG B O   1 
ATOM   1902 C  CB  . ARG B 2 218 ? 20.186  27.095  -13.285 1.00 43.81 ? 206 ARG B CB  1 
ATOM   1903 C  CG  . ARG B 2 218 ? 19.021  28.076  -13.499 1.00 54.35 ? 206 ARG B CG  1 
ATOM   1904 C  CD  . ARG B 2 218 ? 18.030  27.691  -14.631 1.00 47.06 ? 206 ARG B CD  1 
ATOM   1905 N  NE  . ARG B 2 218 ? 16.674  27.509  -14.116 1.00 52.22 ? 206 ARG B NE  1 
ATOM   1906 C  CZ  . ARG B 2 218 ? 15.708  28.418  -14.145 1.00 47.17 ? 206 ARG B CZ  1 
ATOM   1907 N  NH1 . ARG B 2 218 ? 15.885  29.599  -14.709 1.00 40.90 ? 206 ARG B NH1 1 
ATOM   1908 N  NH2 . ARG B 2 218 ? 14.529  28.128  -13.602 1.00 51.27 ? 206 ARG B NH2 1 
ATOM   1909 N  N   . TRP B 2 219 ? 22.030  26.101  -10.852 1.00 40.34 ? 207 TRP B N   1 
ATOM   1910 C  CA  . TRP B 2 219 ? 22.817  25.009  -10.311 1.00 36.99 ? 207 TRP B CA  1 
ATOM   1911 C  C   . TRP B 2 219 ? 22.226  23.687  -10.767 1.00 39.33 ? 207 TRP B C   1 
ATOM   1912 O  O   . TRP B 2 219 ? 21.004  23.504  -10.763 1.00 36.49 ? 207 TRP B O   1 
ATOM   1913 C  CB  . TRP B 2 219 ? 22.855  25.078  -8.787  1.00 39.00 ? 207 TRP B CB  1 
ATOM   1914 C  CG  . TRP B 2 219 ? 23.642  26.225  -8.281  1.00 38.87 ? 207 TRP B CG  1 
ATOM   1915 C  CD1 . TRP B 2 219 ? 23.187  27.493  -8.035  1.00 36.92 ? 207 TRP B CD1 1 
ATOM   1916 C  CD2 . TRP B 2 219 ? 25.040  26.229  -7.975  1.00 36.40 ? 207 TRP B CD2 1 
ATOM   1917 N  NE1 . TRP B 2 219 ? 24.220  28.285  -7.587  1.00 38.33 ? 207 TRP B NE1 1 
ATOM   1918 C  CE2 . TRP B 2 219 ? 25.367  27.534  -7.539  1.00 37.74 ? 207 TRP B CE2 1 
ATOM   1919 C  CE3 . TRP B 2 219 ? 26.047  25.256  -8.025  1.00 34.94 ? 207 TRP B CE3 1 
ATOM   1920 C  CZ2 . TRP B 2 219 ? 26.653  27.889  -7.149  1.00 33.28 ? 207 TRP B CZ2 1 
ATOM   1921 C  CZ3 . TRP B 2 219 ? 27.322  25.608  -7.643  1.00 35.13 ? 207 TRP B CZ3 1 
ATOM   1922 C  CH2 . TRP B 2 219 ? 27.614  26.918  -7.211  1.00 38.09 ? 207 TRP B CH2 1 
ATOM   1923 N  N   . TYR B 2 220 ? 23.098  22.773  -11.177 1.00 38.78 ? 208 TYR B N   1 
ATOM   1924 C  CA  . TYR B 2 220 ? 22.694  21.468  -11.671 1.00 38.84 ? 208 TYR B CA  1 
ATOM   1925 C  C   . TYR B 2 220 ? 23.407  20.399  -10.867 1.00 35.13 ? 208 TYR B C   1 
ATOM   1926 O  O   . TYR B 2 220 ? 24.602  20.523  -10.590 1.00 39.27 ? 208 TYR B O   1 
ATOM   1927 C  CB  . TYR B 2 220 ? 23.025  21.297  -13.156 1.00 38.00 ? 208 TYR B CB  1 
ATOM   1928 C  CG  . TYR B 2 220 ? 22.228  22.170  -14.097 1.00 44.16 ? 208 TYR B CG  1 
ATOM   1929 C  CD1 . TYR B 2 220 ? 22.678  23.456  -14.436 1.00 41.54 ? 208 TYR B CD1 1 
ATOM   1930 C  CD2 . TYR B 2 220 ? 21.035  21.706  -14.683 1.00 44.18 ? 208 TYR B CD2 1 
ATOM   1931 C  CE1 . TYR B 2 220 ? 21.956  24.270  -15.323 1.00 42.68 ? 208 TYR B CE1 1 
ATOM   1932 C  CE2 . TYR B 2 220 ? 20.298  22.515  -15.577 1.00 39.53 ? 208 TYR B CE2 1 
ATOM   1933 C  CZ  . TYR B 2 220 ? 20.767  23.792  -15.891 1.00 46.35 ? 208 TYR B CZ  1 
ATOM   1934 O  OH  . TYR B 2 220 ? 20.055  24.597  -16.759 1.00 42.04 ? 208 TYR B OH  1 
ATOM   1935 N  N   . GLN B 2 221 ? 22.673  19.355  -10.492 1.00 34.56 ? 209 GLN B N   1 
ATOM   1936 C  CA  . GLN B 2 221 ? 23.249  18.197  -9.819  1.00 34.60 ? 209 GLN B CA  1 
ATOM   1937 C  C   . GLN B 2 221 ? 23.759  17.178  -10.848 1.00 36.00 ? 209 GLN B C   1 
ATOM   1938 O  O   . GLN B 2 221 ? 22.972  16.466  -11.480 1.00 35.64 ? 209 GLN B O   1 
ATOM   1939 C  CB  . GLN B 2 221 ? 22.221  17.552  -8.896  1.00 31.05 ? 209 GLN B CB  1 
ATOM   1940 C  CG  . GLN B 2 221 ? 22.804  16.342  -8.176  1.00 32.06 ? 209 GLN B CG  1 
ATOM   1941 C  CD  . GLN B 2 221 ? 21.898  15.831  -7.102  1.00 30.34 ? 209 GLN B CD  1 
ATOM   1942 O  OE1 . GLN B 2 221 ? 20.807  16.356  -6.915  1.00 39.81 ? 209 GLN B OE1 1 
ATOM   1943 N  NE2 . GLN B 2 221 ? 22.329  14.797  -6.391  1.00 29.33 ? 209 GLN B NE2 1 
ATOM   1944 N  N   . MET B 2 222 ? 25.075  17.072  -10.988 1.00 36.24 ? 210 MET B N   1 
ATOM   1945 C  CA  . MET B 2 222 ? 25.662  16.085  -11.884 1.00 34.47 ? 210 MET B CA  1 
ATOM   1946 C  C   . MET B 2 222 ? 25.936  14.760  -11.195 1.00 36.07 ? 210 MET B C   1 
ATOM   1947 O  O   . MET B 2 222 ? 26.023  13.722  -11.868 1.00 33.74 ? 210 MET B O   1 
ATOM   1948 C  CB  . MET B 2 222 ? 26.961  16.630  -12.483 1.00 33.55 ? 210 MET B CB  1 
ATOM   1949 C  CG  . MET B 2 222 ? 26.874  18.096  -12.867 1.00 32.67 ? 210 MET B CG  1 
ATOM   1950 S  SD  . MET B 2 222 ? 25.731  18.484  -14.201 1.00 42.53 ? 210 MET B SD  1 
ATOM   1951 C  CE  . MET B 2 222 ? 25.723  16.960  -15.150 1.00 43.96 ? 210 MET B CE  1 
ATOM   1952 N  N   . GLY B 2 223 ? 26.063  14.757  -9.872  1.00 33.68 ? 211 GLY B N   1 
ATOM   1953 C  CA  . GLY B 2 223 ? 26.503  13.540  -9.227  1.00 33.23 ? 211 GLY B CA  1 
ATOM   1954 C  C   . GLY B 2 223 ? 25.868  13.329  -7.876  1.00 31.90 ? 211 GLY B C   1 
ATOM   1955 O  O   . GLY B 2 223 ? 25.242  14.222  -7.298  1.00 33.36 ? 211 GLY B O   1 
ATOM   1956 N  N   . ILE B 2 224 ? 26.023  12.101  -7.398  1.00 28.77 ? 212 ILE B N   1 
ATOM   1957 C  CA  . ILE B 2 224 ? 25.636  11.700  -6.058  1.00 29.06 ? 212 ILE B CA  1 
ATOM   1958 C  C   . ILE B 2 224 ? 26.856  11.070  -5.415  1.00 33.44 ? 212 ILE B C   1 
ATOM   1959 O  O   . ILE B 2 224 ? 27.435  10.127  -5.972  1.00 36.58 ? 212 ILE B O   1 
ATOM   1960 C  CB  . ILE B 2 224 ? 24.461  10.701  -6.067  1.00 31.18 ? 212 ILE B CB  1 
ATOM   1961 C  CG1 . ILE B 2 224 ? 23.235  11.289  -6.786  1.00 35.45 ? 212 ILE B CG1 1 
ATOM   1962 C  CG2 . ILE B 2 224 ? 24.120  10.282  -4.662  1.00 29.56 ? 212 ILE B CG2 1 
ATOM   1963 C  CD1 . ILE B 2 224 ? 22.155  10.249  -7.111  1.00 32.46 ? 212 ILE B CD1 1 
ATOM   1964 N  N   . VAL B 2 225 ? 27.242  11.578  -4.246  1.00 29.80 ? 213 VAL B N   1 
ATOM   1965 C  CA  . VAL B 2 225 ? 28.314  10.976  -3.471  1.00 29.10 ? 213 VAL B CA  1 
ATOM   1966 C  C   . VAL B 2 225 ? 28.018  9.497   -3.317  1.00 34.50 ? 213 VAL B C   1 
ATOM   1967 O  O   . VAL B 2 225 ? 26.970  9.119   -2.777  1.00 33.31 ? 213 VAL B O   1 
ATOM   1968 C  CB  . VAL B 2 225 ? 28.448  11.642  -2.096  1.00 27.29 ? 213 VAL B CB  1 
ATOM   1969 C  CG1 . VAL B 2 225 ? 29.536  10.975  -1.322  1.00 21.93 ? 213 VAL B CG1 1 
ATOM   1970 C  CG2 . VAL B 2 225 ? 28.716  13.110  -2.264  1.00 29.22 ? 213 VAL B CG2 1 
ATOM   1971 N  N   . SER B 2 226 ? 28.932  8.647   -3.780  1.00 31.26 ? 214 SER B N   1 
ATOM   1972 C  CA  . SER B 2 226 ? 28.683  7.217   -3.772  1.00 31.64 ? 214 SER B CA  1 
ATOM   1973 C  C   . SER B 2 226 ? 29.749  6.423   -3.003  1.00 36.87 ? 214 SER B C   1 
ATOM   1974 O  O   . SER B 2 226 ? 29.388  5.683   -2.087  1.00 39.61 ? 214 SER B O   1 
ATOM   1975 C  CB  . SER B 2 226 ? 28.564  6.721   -5.215  1.00 34.29 ? 214 SER B CB  1 
ATOM   1976 O  OG  . SER B 2 226 ? 28.579  5.311   -5.251  1.00 36.72 ? 214 SER B OG  1 
ATOM   1977 N  N   . TRP B 2 227 ? 31.028  6.526   -3.350  1.00 38.13 ? 215 TRP B N   1 
ATOM   1978 C  CA  . TRP B 2 227 ? 31.977  5.661   -2.644  1.00 36.69 ? 215 TRP B CA  1 
ATOM   1979 C  C   . TRP B 2 227 ? 33.416  6.118   -2.824  1.00 42.17 ? 215 TRP B C   1 
ATOM   1980 O  O   . TRP B 2 227 ? 33.745  6.917   -3.701  1.00 41.57 ? 215 TRP B O   1 
ATOM   1981 C  CB  . TRP B 2 227 ? 31.866  4.201   -3.097  1.00 41.62 ? 215 TRP B CB  1 
ATOM   1982 C  CG  . TRP B 2 227 ? 32.167  3.964   -4.561  1.00 39.66 ? 215 TRP B CG  1 
ATOM   1983 C  CD1 . TRP B 2 227 ? 31.278  4.037   -5.600  1.00 39.18 ? 215 TRP B CD1 1 
ATOM   1984 C  CD2 . TRP B 2 227 ? 33.434  3.603   -5.143  1.00 38.77 ? 215 TRP B CD2 1 
ATOM   1985 N  NE1 . TRP B 2 227 ? 31.912  3.745   -6.787  1.00 41.96 ? 215 TRP B NE1 1 
ATOM   1986 C  CE2 . TRP B 2 227 ? 33.232  3.476   -6.538  1.00 39.73 ? 215 TRP B CE2 1 
ATOM   1987 C  CE3 . TRP B 2 227 ? 34.716  3.384   -4.626  1.00 38.73 ? 215 TRP B CE3 1 
ATOM   1988 C  CZ2 . TRP B 2 227 ? 34.265  3.141   -7.419  1.00 37.13 ? 215 TRP B CZ2 1 
ATOM   1989 C  CZ3 . TRP B 2 227 ? 35.741  3.045   -5.504  1.00 35.46 ? 215 TRP B CZ3 1 
ATOM   1990 C  CH2 . TRP B 2 227 ? 35.509  2.934   -6.885  1.00 37.80 ? 215 TRP B CH2 1 
ATOM   1991 N  N   . GLY B 2 228 ? 34.275  5.580   -1.967  1.00 45.25 ? 216 GLY B N   1 
ATOM   1992 C  CA  . GLY B 2 228 ? 35.706  5.790   -2.081  1.00 38.10 ? 216 GLY B CA  1 
ATOM   1993 C  C   . GLY B 2 228 ? 36.441  4.822   -1.182  1.00 40.09 ? 216 GLY B C   1 
ATOM   1994 O  O   . GLY B 2 228 ? 35.838  4.085   -0.391  1.00 37.89 ? 216 GLY B O   1 
ATOM   1995 N  N   . GLU B 2 229 ? 37.764  4.832   -1.318  1.00 35.30 ? 217 GLU B N   1 
ATOM   1996 C  CA  . GLU B 2 229 ? 38.654  4.050   -0.468  1.00 37.21 ? 217 GLU B CA  1 
ATOM   1997 C  C   . GLU B 2 229 ? 39.457  5.026   0.395   1.00 39.88 ? 217 GLU B C   1 
ATOM   1998 O  O   . GLU B 2 229 ? 40.428  5.640   -0.063  1.00 45.29 ? 217 GLU B O   1 
ATOM   1999 C  CB  . GLU B 2 229 ? 39.539  3.141   -1.316  1.00 40.24 ? 217 GLU B CB  1 
ATOM   2000 C  CG  . GLU B 2 229 ? 38.741  2.255   -2.287  1.00 40.28 ? 217 GLU B CG  1 
ATOM   2001 C  CD  . GLU B 2 229 ? 39.622  1.506   -3.290  1.00 43.38 ? 217 GLU B CD  1 
ATOM   2002 O  OE1 . GLU B 2 229 ? 39.946  2.076   -4.358  1.00 37.88 ? 217 GLU B OE1 1 
ATOM   2003 O  OE2 . GLU B 2 229 ? 39.996  0.347   -2.998  1.00 43.72 ? 217 GLU B OE2 1 
ATOM   2004 N  N   . GLY B 2 230 ? 39.036  5.193   1.637   1.00 40.57 ? 219 GLY B N   1 
ATOM   2005 C  CA  . GLY B 2 230 ? 39.592  6.240   2.462   1.00 39.97 ? 219 GLY B CA  1 
ATOM   2006 C  C   . GLY B 2 230 ? 39.068  7.583   1.994   1.00 38.76 ? 219 GLY B C   1 
ATOM   2007 O  O   . GLY B 2 230 ? 38.331  7.705   1.012   1.00 37.51 ? 219 GLY B O   1 
ATOM   2008 N  N   . CYS B 2 231 ? 39.504  8.619   2.693   1.00 36.82 ? 220 CYS B N   1 
ATOM   2009 C  CA  . CYS B 2 231 ? 39.083  9.978   2.389   1.00 44.45 ? 220 CYS B CA  1 
ATOM   2010 C  C   . CYS B 2 231 ? 40.312  10.859  2.189   1.00 39.46 ? 220 CYS B C   1 
ATOM   2011 O  O   . CYS B 2 231 ? 41.224  10.850  3.014   1.00 40.02 ? 220 CYS B O   1 
ATOM   2012 C  CB  . CYS B 2 231 ? 38.174  10.513  3.510   1.00 36.64 ? 220 CYS B CB  1 
ATOM   2013 S  SG  . CYS B 2 231 ? 36.815  9.349   3.912   1.00 41.61 ? 220 CYS B SG  1 
ATOM   2014 N  N   . ASP B 2 232 ? 40.348  11.593  1.083   1.00 37.70 ? 221 ASP B N   1 
ATOM   2015 C  CA  . ASP B 2 232 ? 41.416  12.558  0.830   1.00 39.60 ? 221 ASP B CA  1 
ATOM   2016 C  C   . ASP B 2 232 ? 42.803  11.922  0.836   1.00 35.23 ? 221 ASP B C   1 
ATOM   2017 O  O   . ASP B 2 232 ? 43.779  12.563  1.217   1.00 36.95 ? 221 ASP B O   1 
ATOM   2018 C  CB  . ASP B 2 232 ? 41.368  13.689  1.850   1.00 37.51 ? 221 ASP B CB  1 
ATOM   2019 C  CG  . ASP B 2 232 ? 42.117  14.896  1.387   1.00 39.52 ? 221 ASP B CG  1 
ATOM   2020 O  OD1 . ASP B 2 232 ? 41.974  15.256  0.200   1.00 38.25 ? 221 ASP B OD1 1 
ATOM   2021 O  OD2 . ASP B 2 232 ? 42.865  15.469  2.207   1.00 42.31 ? 221 ASP B OD2 1 
ATOM   2022 N  N   . ARG B 2 233 A 42.910  10.659  0.432   1.00 36.90 ? 221 ARG B N   1 
ATOM   2023 C  CA  . ARG B 2 233 A 44.210  10.013  0.296   1.00 37.84 ? 221 ARG B CA  1 
ATOM   2024 C  C   . ARG B 2 233 A 44.854  10.391  -1.032  1.00 39.89 ? 221 ARG B C   1 
ATOM   2025 O  O   . ARG B 2 233 A 44.176  10.492  -2.062  1.00 40.81 ? 221 ARG B O   1 
ATOM   2026 C  CB  . ARG B 2 233 A 44.082  8.493   0.401   1.00 35.22 ? 221 ARG B CB  1 
ATOM   2027 C  CG  . ARG B 2 233 A 43.340  7.999   1.658   1.00 38.47 ? 221 ARG B CG  1 
ATOM   2028 C  CD  . ARG B 2 233 A 43.558  6.508   1.845   1.00 38.98 ? 221 ARG B CD  1 
ATOM   2029 N  NE  . ARG B 2 233 A 43.051  5.996   3.116   1.00 43.06 ? 221 ARG B NE  1 
ATOM   2030 C  CZ  . ARG B 2 233 A 43.319  4.780   3.586   1.00 46.46 ? 221 ARG B CZ  1 
ATOM   2031 N  NH1 . ARG B 2 233 A 44.084  3.932   2.916   1.00 45.90 ? 221 ARG B NH1 1 
ATOM   2032 N  NH2 . ARG B 2 233 A 42.800  4.401   4.754   1.00 40.32 ? 221 ARG B NH2 1 
ATOM   2033 N  N   . ASP B 2 234 ? 46.169  10.609  -1.001  1.00 41.04 ? 222 ASP B N   1 
ATOM   2034 C  CA  . ASP B 2 234 ? 46.882  10.972  -2.221  1.00 43.06 ? 222 ASP B CA  1 
ATOM   2035 C  C   . ASP B 2 234 ? 46.773  9.857   -3.252  1.00 40.28 ? 222 ASP B C   1 
ATOM   2036 O  O   . ASP B 2 234 ? 46.947  8.678   -2.928  1.00 41.84 ? 222 ASP B O   1 
ATOM   2037 C  CB  . ASP B 2 234 ? 48.348  11.280  -1.913  1.00 42.44 ? 222 ASP B CB  1 
ATOM   2038 C  CG  . ASP B 2 234 ? 48.551  12.694  -1.387  1.00 47.41 ? 222 ASP B CG  1 
ATOM   2039 O  OD1 . ASP B 2 234 ? 47.563  13.475  -1.321  1.00 45.18 ? 222 ASP B OD1 1 
ATOM   2040 O  OD2 . ASP B 2 234 ? 49.707  13.023  -1.048  1.00 51.70 ? 222 ASP B OD2 1 
ATOM   2041 N  N   . GLY B 2 235 ? 46.482  10.235  -4.499  1.00 39.72 ? 223 GLY B N   1 
ATOM   2042 C  CA  . GLY B 2 235 ? 46.312  9.274   -5.571  1.00 35.62 ? 223 GLY B CA  1 
ATOM   2043 C  C   . GLY B 2 235 ? 44.952  8.602   -5.634  1.00 36.05 ? 223 GLY B C   1 
ATOM   2044 O  O   . GLY B 2 235 ? 44.674  7.897   -6.616  1.00 33.54 ? 223 GLY B O   1 
ATOM   2045 N  N   . LYS B 2 236 ? 44.107  8.766   -4.620  1.00 36.01 ? 224 LYS B N   1 
ATOM   2046 C  CA  . LYS B 2 236 ? 42.733  8.285   -4.667  1.00 35.84 ? 224 LYS B CA  1 
ATOM   2047 C  C   . LYS B 2 236 ? 41.772  9.430   -4.965  1.00 35.76 ? 224 LYS B C   1 
ATOM   2048 O  O   . LYS B 2 236 ? 42.113  10.613  -4.855  1.00 36.14 ? 224 LYS B O   1 
ATOM   2049 C  CB  . LYS B 2 236 ? 42.350  7.591   -3.360  1.00 38.26 ? 224 LYS B CB  1 
ATOM   2050 C  CG  . LYS B 2 236 ? 43.390  6.612   -2.846  1.00 30.98 ? 224 LYS B CG  1 
ATOM   2051 C  CD  . LYS B 2 236 ? 43.570  5.468   -3.820  1.00 37.09 ? 224 LYS B CD  1 
ATOM   2052 C  CE  . LYS B 2 236 ? 42.288  4.681   -4.017  1.00 35.00 ? 224 LYS B CE  1 
ATOM   2053 N  NZ  . LYS B 2 236 ? 42.589  3.326   -4.566  1.00 26.75 ? 224 LYS B NZ  1 
ATOM   2054 N  N   . TYR B 2 237 ? 40.565  9.060   -5.380  1.00 36.52 ? 225 TYR B N   1 
ATOM   2055 C  CA  . TYR B 2 237 ? 39.548  10.031  -5.757  1.00 35.80 ? 225 TYR B CA  1 
ATOM   2056 C  C   . TYR B 2 237 ? 38.205  9.546   -5.250  1.00 37.65 ? 225 TYR B C   1 
ATOM   2057 O  O   . TYR B 2 237 ? 37.984  8.340   -5.123  1.00 42.54 ? 225 TYR B O   1 
ATOM   2058 C  CB  . TYR B 2 237 ? 39.510  10.224  -7.286  1.00 37.06 ? 225 TYR B CB  1 
ATOM   2059 C  CG  . TYR B 2 237 ? 40.858  10.621  -7.837  1.00 39.04 ? 225 TYR B CG  1 
ATOM   2060 C  CD1 . TYR B 2 237 ? 41.813  9.660   -8.165  1.00 37.27 ? 225 TYR B CD1 1 
ATOM   2061 C  CD2 . TYR B 2 237 ? 41.198  11.961  -7.979  1.00 39.77 ? 225 TYR B CD2 1 
ATOM   2062 C  CE1 . TYR B 2 237 ? 43.064  10.027  -8.628  1.00 38.69 ? 225 TYR B CE1 1 
ATOM   2063 C  CE2 . TYR B 2 237 ? 42.438  12.333  -8.441  1.00 41.37 ? 225 TYR B CE2 1 
ATOM   2064 C  CZ  . TYR B 2 237 ? 43.368  11.367  -8.767  1.00 42.19 ? 225 TYR B CZ  1 
ATOM   2065 O  OH  . TYR B 2 237 ? 44.604  11.754  -9.238  1.00 44.71 ? 225 TYR B OH  1 
ATOM   2066 N  N   . GLY B 2 238 ? 37.301  10.483  -4.965  1.00 36.03 ? 226 GLY B N   1 
ATOM   2067 C  CA  . GLY B 2 238 ? 35.941  10.092  -4.640  1.00 32.14 ? 226 GLY B CA  1 
ATOM   2068 C  C   . GLY B 2 238 ? 35.134  9.804   -5.897  1.00 35.73 ? 226 GLY B C   1 
ATOM   2069 O  O   . GLY B 2 238 ? 35.338  10.416  -6.948  1.00 34.48 ? 226 GLY B O   1 
ATOM   2070 N  N   . PHE B 2 239 ? 34.154  8.899   -5.773  1.00 34.88 ? 227 PHE B N   1 
ATOM   2071 C  CA  . PHE B 2 239 ? 33.352  8.434   -6.896  1.00 36.70 ? 227 PHE B CA  1 
ATOM   2072 C  C   . PHE B 2 239 ? 31.881  8.763   -6.673  1.00 35.59 ? 227 PHE B C   1 
ATOM   2073 O  O   . PHE B 2 239 ? 31.323  8.515   -5.596  1.00 33.55 ? 227 PHE B O   1 
ATOM   2074 C  CB  . PHE B 2 239 ? 33.515  6.915   -7.114  1.00 36.54 ? 227 PHE B CB  1 
ATOM   2075 C  CG  . PHE B 2 239 ? 34.759  6.545   -7.886  1.00 41.44 ? 227 PHE B CG  1 
ATOM   2076 C  CD1 . PHE B 2 239 ? 35.993  6.486   -7.256  1.00 38.97 ? 227 PHE B CD1 1 
ATOM   2077 C  CD2 . PHE B 2 239 ? 34.697  6.278   -9.254  1.00 42.65 ? 227 PHE B CD2 1 
ATOM   2078 C  CE1 . PHE B 2 239 ? 37.158  6.157   -7.982  1.00 45.39 ? 227 PHE B CE1 1 
ATOM   2079 C  CE2 . PHE B 2 239 ? 35.853  5.948   -9.987  1.00 44.11 ? 227 PHE B CE2 1 
ATOM   2080 C  CZ  . PHE B 2 239 ? 37.086  5.882   -9.349  1.00 41.66 ? 227 PHE B CZ  1 
ATOM   2081 N  N   . TYR B 2 240 ? 31.258  9.231   -7.744  1.00 34.30 ? 228 TYR B N   1 
ATOM   2082 C  CA  . TYR B 2 240 ? 29.950  9.846   -7.760  1.00 33.98 ? 228 TYR B CA  1 
ATOM   2083 C  C   . TYR B 2 240 ? 29.076  9.177   -8.808  1.00 40.40 ? 228 TYR B C   1 
ATOM   2084 O  O   . TYR B 2 240 ? 29.507  8.942   -9.951  1.00 37.07 ? 228 TYR B O   1 
ATOM   2085 C  CB  . TYR B 2 240 ? 30.067  11.336  -8.083  1.00 34.19 ? 228 TYR B CB  1 
ATOM   2086 C  CG  . TYR B 2 240 ? 30.861  12.103  -7.060  1.00 39.30 ? 228 TYR B CG  1 
ATOM   2087 C  CD1 . TYR B 2 240 ? 32.256  12.006  -7.004  1.00 34.11 ? 228 TYR B CD1 1 
ATOM   2088 C  CD2 . TYR B 2 240 ? 30.217  12.931  -6.140  1.00 36.45 ? 228 TYR B CD2 1 
ATOM   2089 C  CE1 . TYR B 2 240 ? 32.970  12.704  -6.069  1.00 33.06 ? 228 TYR B CE1 1 
ATOM   2090 C  CE2 . TYR B 2 240 ? 30.931  13.643  -5.199  1.00 34.31 ? 228 TYR B CE2 1 
ATOM   2091 C  CZ  . TYR B 2 240 ? 32.303  13.523  -5.170  1.00 34.67 ? 228 TYR B CZ  1 
ATOM   2092 O  OH  . TYR B 2 240 ? 32.995  14.228  -4.224  1.00 30.06 ? 228 TYR B OH  1 
ATOM   2093 N  N   . THR B 2 241 ? 27.834  8.913   -8.411  1.00 37.42 ? 229 THR B N   1 
ATOM   2094 C  CA  . THR B 2 241 ? 26.851  8.389   -9.340  1.00 38.17 ? 229 THR B CA  1 
ATOM   2095 C  C   . THR B 2 241 ? 26.597  9.424   -10.423 1.00 39.04 ? 229 THR B C   1 
ATOM   2096 O  O   . THR B 2 241 ? 26.372  10.600  -10.127 1.00 35.41 ? 229 THR B O   1 
ATOM   2097 C  CB  . THR B 2 241 ? 25.562  8.060   -8.595  1.00 36.68 ? 229 THR B CB  1 
ATOM   2098 O  OG1 . THR B 2 241 ? 25.748  6.846   -7.858  1.00 38.16 ? 229 THR B OG1 1 
ATOM   2099 C  CG2 . THR B 2 241 ? 24.438  7.856   -9.585  1.00 38.90 ? 229 THR B CG2 1 
ATOM   2100 N  N   . HIS B 2 242 ? 26.660  8.987   -11.682 1.00 42.85 ? 230 HIS B N   1 
ATOM   2101 C  CA  . HIS B 2 242 ? 26.506  9.870   -12.840 1.00 39.57 ? 230 HIS B CA  1 
ATOM   2102 C  C   . HIS B 2 242 ? 25.019  10.153  -13.013 1.00 41.72 ? 230 HIS B C   1 
ATOM   2103 O  O   . HIS B 2 242 ? 24.268  9.303   -13.495 1.00 41.66 ? 230 HIS B O   1 
ATOM   2104 C  CB  . HIS B 2 242 ? 27.101  9.210   -14.075 1.00 39.49 ? 230 HIS B CB  1 
ATOM   2105 C  CG  . HIS B 2 242 ? 27.256  10.126  -15.244 1.00 42.63 ? 230 HIS B CG  1 
ATOM   2106 N  ND1 . HIS B 2 242 ? 26.202  10.835  -15.780 1.00 43.67 ? 230 HIS B ND1 1 
ATOM   2107 C  CD2 . HIS B 2 242 ? 28.338  10.431  -15.999 1.00 40.38 ? 230 HIS B CD2 1 
ATOM   2108 C  CE1 . HIS B 2 242 ? 26.631  11.547  -16.806 1.00 37.55 ? 230 HIS B CE1 1 
ATOM   2109 N  NE2 . HIS B 2 242 ? 27.922  11.315  -16.964 1.00 40.08 ? 230 HIS B NE2 1 
ATOM   2110 N  N   . VAL B 2 243 ? 24.577  11.342  -12.599 1.00 41.74 ? 231 VAL B N   1 
ATOM   2111 C  CA  . VAL B 2 243 ? 23.138  11.582  -12.522 1.00 42.58 ? 231 VAL B CA  1 
ATOM   2112 C  C   . VAL B 2 243 ? 22.505  11.552  -13.904 1.00 44.58 ? 231 VAL B C   1 
ATOM   2113 O  O   . VAL B 2 243 ? 21.450  10.932  -14.094 1.00 40.39 ? 231 VAL B O   1 
ATOM   2114 C  CB  . VAL B 2 243 ? 22.832  12.896  -11.780 1.00 39.67 ? 231 VAL B CB  1 
ATOM   2115 C  CG1 . VAL B 2 243 ? 21.412  13.389  -12.095 1.00 34.58 ? 231 VAL B CG1 1 
ATOM   2116 C  CG2 . VAL B 2 243 ? 22.989  12.674  -10.293 1.00 39.68 ? 231 VAL B CG2 1 
ATOM   2117 N  N   . PHE B 2 244 ? 23.136  12.195  -14.897 1.00 45.25 ? 232 PHE B N   1 
ATOM   2118 C  CA  . PHE B 2 244 ? 22.488  12.271  -16.200 1.00 41.69 ? 232 PHE B CA  1 
ATOM   2119 C  C   . PHE B 2 244 ? 22.304  10.894  -16.814 1.00 41.79 ? 232 PHE B C   1 
ATOM   2120 O  O   . PHE B 2 244 ? 21.267  10.620  -17.424 1.00 44.64 ? 232 PHE B O   1 
ATOM   2121 C  CB  . PHE B 2 244 ? 23.245  13.158  -17.181 1.00 44.65 ? 232 PHE B CB  1 
ATOM   2122 C  CG  . PHE B 2 244 ? 22.604  13.173  -18.548 1.00 47.80 ? 232 PHE B CG  1 
ATOM   2123 C  CD1 . PHE B 2 244 ? 21.513  14.005  -18.799 1.00 49.16 ? 232 PHE B CD1 1 
ATOM   2124 C  CD2 . PHE B 2 244 ? 23.049  12.328  -19.562 1.00 48.70 ? 232 PHE B CD2 1 
ATOM   2125 C  CE1 . PHE B 2 244 ? 20.877  14.010  -20.049 1.00 52.64 ? 232 PHE B CE1 1 
ATOM   2126 C  CE2 . PHE B 2 244 ? 22.423  12.322  -20.817 1.00 51.26 ? 232 PHE B CE2 1 
ATOM   2127 C  CZ  . PHE B 2 244 ? 21.336  13.170  -21.065 1.00 47.19 ? 232 PHE B CZ  1 
ATOM   2128 N  N   . ARG B 2 245 ? 23.290  10.013  -16.658 1.00 42.72 ? 233 ARG B N   1 
ATOM   2129 C  CA  . ARG B 2 245 ? 23.200  8.692   -17.269 1.00 43.28 ? 233 ARG B CA  1 
ATOM   2130 C  C   . ARG B 2 245 ? 21.962  7.931   -16.814 1.00 46.53 ? 233 ARG B C   1 
ATOM   2131 O  O   . ARG B 2 245 ? 21.449  7.074   -17.543 1.00 52.90 ? 233 ARG B O   1 
ATOM   2132 C  CB  . ARG B 2 245 ? 24.466  7.894   -16.963 1.00 44.85 ? 233 ARG B CB  1 
ATOM   2133 C  CG  . ARG B 2 245 ? 24.736  6.831   -18.003 1.00 52.22 ? 233 ARG B CG  1 
ATOM   2134 C  CD  . ARG B 2 245 ? 26.185  6.801   -18.411 1.00 54.00 ? 233 ARG B CD  1 
ATOM   2135 N  NE  . ARG B 2 245 ? 26.408  5.957   -19.582 1.00 62.16 ? 233 ARG B NE  1 
ATOM   2136 C  CZ  . ARG B 2 245 ? 26.425  4.628   -19.564 1.00 67.80 ? 233 ARG B CZ  1 
ATOM   2137 N  NH1 . ARG B 2 245 ? 26.196  3.948   -18.451 1.00 64.50 ? 233 ARG B NH1 1 
ATOM   2138 N  NH2 . ARG B 2 245 ? 26.712  3.963   -20.685 1.00 67.92 ? 233 ARG B NH2 1 
ATOM   2139 N  N   . LEU B 2 246 ? 21.449  8.246   -15.633 1.00 47.99 ? 234 LEU B N   1 
ATOM   2140 C  CA  . LEU B 2 246 ? 20.274  7.580   -15.099 1.00 48.23 ? 234 LEU B CA  1 
ATOM   2141 C  C   . LEU B 2 246 ? 19.037  8.468   -15.139 1.00 52.70 ? 234 LEU B C   1 
ATOM   2142 O  O   . LEU B 2 246 ? 18.005  8.095   -14.564 1.00 51.55 ? 234 LEU B O   1 
ATOM   2143 C  CB  . LEU B 2 246 ? 20.554  7.138   -13.663 1.00 44.24 ? 234 LEU B CB  1 
ATOM   2144 C  CG  . LEU B 2 246 ? 21.865  6.375   -13.464 1.00 50.62 ? 234 LEU B CG  1 
ATOM   2145 C  CD1 . LEU B 2 246 ? 22.140  6.180   -11.993 1.00 45.83 ? 234 LEU B CD1 1 
ATOM   2146 C  CD2 . LEU B 2 246 ? 21.836  5.019   -14.173 1.00 53.14 ? 234 LEU B CD2 1 
ATOM   2147 N  N   . LYS B 2 247 ? 19.115  9.637   -15.798 1.00 49.11 ? 235 LYS B N   1 
ATOM   2148 C  CA  . LYS B 2 247 ? 18.004  10.589  -15.749 1.00 53.55 ? 235 LYS B CA  1 
ATOM   2149 C  C   . LYS B 2 247 ? 16.734  9.982   -16.321 1.00 58.77 ? 235 LYS B C   1 
ATOM   2150 O  O   . LYS B 2 247 ? 15.630  10.227  -15.807 1.00 53.91 ? 235 LYS B O   1 
ATOM   2151 C  CB  . LYS B 2 247 ? 18.334  11.884  -16.489 1.00 47.79 ? 235 LYS B CB  1 
ATOM   2152 C  CG  . LYS B 2 247 ? 17.197  12.889  -16.332 1.00 47.64 ? 235 LYS B CG  1 
ATOM   2153 C  CD  . LYS B 2 247 ? 17.509  14.239  -16.907 1.00 45.02 ? 235 LYS B CD  1 
ATOM   2154 C  CE  . LYS B 2 247 ? 16.435  15.222  -16.522 1.00 44.25 ? 235 LYS B CE  1 
ATOM   2155 N  NZ  . LYS B 2 247 ? 16.687  16.534  -17.165 1.00 49.48 ? 235 LYS B NZ  1 
ATOM   2156 N  N   . LYS B 2 248 ? 16.877  9.206   -17.400 1.00 56.86 ? 236 LYS B N   1 
ATOM   2157 C  CA  . LYS B 2 248 ? 15.770  8.449   -17.958 1.00 59.16 ? 236 LYS B CA  1 
ATOM   2158 C  C   . LYS B 2 248 ? 14.995  7.789   -16.822 1.00 55.41 ? 236 LYS B C   1 
ATOM   2159 O  O   . LYS B 2 248 ? 13.823  8.111   -16.578 1.00 59.42 ? 236 LYS B O   1 
ATOM   2160 C  CB  . LYS B 2 248 ? 16.318  7.420   -18.959 1.00 59.33 ? 236 LYS B CB  1 
ATOM   2161 C  CG  . LYS B 2 248 ? 17.713  6.856   -18.578 1.00 60.91 ? 236 LYS B CG  1 
ATOM   2162 C  CD  . LYS B 2 248 ? 17.605  5.538   -17.792 1.00 62.56 ? 236 LYS B CD  1 
ATOM   2163 C  CE  . LYS B 2 248 ? 18.945  5.088   -17.192 1.00 62.37 ? 236 LYS B CE  1 
ATOM   2164 N  NZ  . LYS B 2 248 ? 18.881  3.758   -16.471 1.00 53.37 ? 236 LYS B NZ  1 
ATOM   2165 N  N   . TRP B 2 249 ? 15.699  6.975   -16.031 1.00 50.40 ? 237 TRP B N   1 
ATOM   2166 C  CA  . TRP B 2 249 ? 15.065  6.266   -14.927 1.00 57.43 ? 237 TRP B CA  1 
ATOM   2167 C  C   . TRP B 2 249 ? 14.349  7.237   -13.997 1.00 55.20 ? 237 TRP B C   1 
ATOM   2168 O  O   . TRP B 2 249 ? 13.152  7.081   -13.715 1.00 58.09 ? 237 TRP B O   1 
ATOM   2169 C  CB  . TRP B 2 249 ? 16.116  5.463   -14.156 1.00 51.72 ? 237 TRP B CB  1 
ATOM   2170 C  CG  . TRP B 2 249 ? 15.588  4.806   -12.926 1.00 51.97 ? 237 TRP B CG  1 
ATOM   2171 C  CD1 . TRP B 2 249 ? 14.871  3.658   -12.872 1.00 56.19 ? 237 TRP B CD1 1 
ATOM   2172 C  CD2 . TRP B 2 249 ? 15.736  5.249   -11.562 1.00 59.29 ? 237 TRP B CD2 1 
ATOM   2173 N  NE1 . TRP B 2 249 ? 14.556  3.346   -11.569 1.00 57.35 ? 237 TRP B NE1 1 
ATOM   2174 C  CE2 . TRP B 2 249 ? 15.071  4.309   -10.743 1.00 58.73 ? 237 TRP B CE2 1 
ATOM   2175 C  CE3 . TRP B 2 249 ? 16.361  6.350   -10.954 1.00 58.52 ? 237 TRP B CE3 1 
ATOM   2176 C  CZ2 . TRP B 2 249 ? 15.015  4.429   -9.342  1.00 53.89 ? 237 TRP B CZ2 1 
ATOM   2177 C  CZ3 . TRP B 2 249 ? 16.297  6.470   -9.554  1.00 51.42 ? 237 TRP B CZ3 1 
ATOM   2178 C  CH2 . TRP B 2 249 ? 15.630  5.515   -8.773  1.00 47.57 ? 237 TRP B CH2 1 
ATOM   2179 N  N   . ILE B 2 250 ? 15.044  8.299   -13.584 1.00 52.19 ? 238 ILE B N   1 
ATOM   2180 C  CA  . ILE B 2 250 ? 14.429  9.276   -12.690 1.00 56.24 ? 238 ILE B CA  1 
ATOM   2181 C  C   . ILE B 2 250 ? 13.096  9.745   -13.267 1.00 59.23 ? 238 ILE B C   1 
ATOM   2182 O  O   . ILE B 2 250 ? 12.037  9.561   -12.644 1.00 57.89 ? 238 ILE B O   1 
ATOM   2183 C  CB  . ILE B 2 250 ? 15.399  10.442  -12.403 1.00 54.63 ? 238 ILE B CB  1 
ATOM   2184 C  CG1 . ILE B 2 250 ? 16.697  9.918   -11.776 1.00 49.20 ? 238 ILE B CG1 1 
ATOM   2185 C  CG2 . ILE B 2 250 ? 14.786  11.446  -11.442 1.00 47.28 ? 238 ILE B CG2 1 
ATOM   2186 C  CD1 . ILE B 2 250 ? 17.850  10.866  -11.885 1.00 39.02 ? 238 ILE B CD1 1 
ATOM   2187 N  N   . GLN B 2 251 ? 13.111  10.247  -14.517 1.00 60.89 ? 239 GLN B N   1 
ATOM   2188 C  CA  . GLN B 2 251 ? 11.881  10.787  -15.100 1.00 58.70 ? 239 GLN B CA  1 
ATOM   2189 C  C   . GLN B 2 251 ? 10.805  9.708   -15.143 1.00 62.69 ? 239 GLN B C   1 
ATOM   2190 O  O   . GLN B 2 251 ? 9.673   9.924   -14.683 1.00 61.01 ? 239 GLN B O   1 
ATOM   2191 C  CB  . GLN B 2 251 ? 12.133  11.341  -16.510 1.00 60.14 ? 239 GLN B CB  1 
ATOM   2192 C  CG  . GLN B 2 251 ? 12.772  12.740  -16.632 1.00 61.72 ? 239 GLN B CG  1 
ATOM   2193 C  CD  . GLN B 2 251 ? 12.200  13.782  -15.671 1.00 71.94 ? 239 GLN B CD  1 
ATOM   2194 O  OE1 . GLN B 2 251 ? 11.096  14.298  -15.871 1.00 74.45 ? 239 GLN B OE1 1 
ATOM   2195 N  NE2 . GLN B 2 251 ? 12.970  14.118  -14.640 1.00 72.74 ? 239 GLN B NE2 1 
ATOM   2196 N  N   . LYS B 2 252 ? 11.176  8.505   -15.599 1.00 56.56 ? 240 LYS B N   1 
ATOM   2197 C  CA  . LYS B 2 252 ? 10.220  7.409   -15.646 1.00 56.33 ? 240 LYS B CA  1 
ATOM   2198 C  C   . LYS B 2 252 ? 9.497   7.301   -14.314 1.00 63.33 ? 240 LYS B C   1 
ATOM   2199 O  O   . LYS B 2 252 ? 8.276   7.506   -14.240 1.00 66.58 ? 240 LYS B O   1 
ATOM   2200 C  CB  . LYS B 2 252 ? 10.936  6.101   -16.001 1.00 57.37 ? 240 LYS B CB  1 
ATOM   2201 C  CG  . LYS B 2 252 ? 10.062  4.847   -15.955 1.00 59.36 ? 240 LYS B CG  1 
ATOM   2202 C  CD  . LYS B 2 252 ? 10.752  3.635   -16.605 1.00 60.54 ? 240 LYS B CD  1 
ATOM   2203 C  CE  . LYS B 2 252 ? 12.097  3.307   -15.945 1.00 65.16 ? 240 LYS B CE  1 
ATOM   2204 N  NZ  . LYS B 2 252 ? 12.719  2.034   -16.444 1.00 63.07 ? 240 LYS B NZ  1 
ATOM   2205 N  N   . VAL B 2 253 ? 10.270  7.128   -13.230 1.00 64.76 ? 241 VAL B N   1 
ATOM   2206 C  CA  . VAL B 2 253 ? 9.675   6.919   -11.910 1.00 63.23 ? 241 VAL B CA  1 
ATOM   2207 C  C   . VAL B 2 253 ? 8.715   8.051   -11.586 1.00 60.87 ? 241 VAL B C   1 
ATOM   2208 O  O   . VAL B 2 253 ? 7.532   7.828   -11.291 1.00 67.90 ? 241 VAL B O   1 
ATOM   2209 C  CB  . VAL B 2 253 ? 10.768  6.800   -10.834 1.00 61.30 ? 241 VAL B CB  1 
ATOM   2210 C  CG1 . VAL B 2 253 ? 10.133  6.716   -9.451  1.00 60.22 ? 241 VAL B CG1 1 
ATOM   2211 C  CG2 . VAL B 2 253 ? 11.663  5.605   -11.099 1.00 55.81 ? 241 VAL B CG2 1 
ATOM   2212 N  N   . ILE B 2 254 ? 9.189   9.288   -11.725 1.00 55.38 ? 242 ILE B N   1 
ATOM   2213 C  CA  . ILE B 2 254 ? 8.381   10.424  -11.302 1.00 61.67 ? 242 ILE B CA  1 
ATOM   2214 C  C   . ILE B 2 254 ? 7.093   10.492  -12.116 1.00 66.81 ? 242 ILE B C   1 
ATOM   2215 O  O   . ILE B 2 254 ? 6.009   10.772  -11.581 1.00 62.44 ? 242 ILE B O   1 
ATOM   2216 C  CB  . ILE B 2 254 ? 9.212   11.716  -11.388 1.00 57.83 ? 242 ILE B CB  1 
ATOM   2217 C  CG1 . ILE B 2 254 ? 10.231  11.740  -10.245 1.00 57.38 ? 242 ILE B CG1 1 
ATOM   2218 C  CG2 . ILE B 2 254 ? 8.318   12.941  -11.329 1.00 60.12 ? 242 ILE B CG2 1 
ATOM   2219 C  CD1 . ILE B 2 254 ? 11.203  12.895  -10.308 1.00 56.77 ? 242 ILE B CD1 1 
ATOM   2220 N  N   . ASP B 2 255 ? 7.181   10.199  -13.415 1.00 67.10 ? 243 ASP B N   1 
ATOM   2221 C  CA  . ASP B 2 255 ? 5.988   10.292  -14.241 1.00 67.22 ? 243 ASP B CA  1 
ATOM   2222 C  C   . ASP B 2 255 ? 5.037   9.143   -13.941 1.00 69.22 ? 243 ASP B C   1 
ATOM   2223 O  O   . ASP B 2 255 ? 3.815   9.325   -13.976 1.00 67.33 ? 243 ASP B O   1 
ATOM   2224 C  CB  . ASP B 2 255 ? 6.380   10.365  -15.717 1.00 69.53 ? 243 ASP B CB  1 
ATOM   2225 C  CG  . ASP B 2 255 ? 7.089   11.687  -16.064 1.00 73.73 ? 243 ASP B CG  1 
ATOM   2226 O  OD1 . ASP B 2 255 ? 6.905   12.669  -15.306 1.00 72.42 ? 243 ASP B OD1 1 
ATOM   2227 O  OD2 . ASP B 2 255 ? 7.824   11.751  -17.079 1.00 68.33 ? 243 ASP B OD2 1 
ATOM   2228 N  N   . GLN B 2 256 ? 5.569   7.969   -13.603 1.00 66.70 ? 244 GLN B N   1 
ATOM   2229 C  CA  . GLN B 2 256 ? 4.687   6.837   -13.351 1.00 66.20 ? 244 GLN B CA  1 
ATOM   2230 C  C   . GLN B 2 256 ? 3.930   7.050   -12.046 1.00 70.83 ? 244 GLN B C   1 
ATOM   2231 O  O   . GLN B 2 256 ? 2.724   6.781   -11.962 1.00 70.31 ? 244 GLN B O   1 
ATOM   2232 C  CB  . GLN B 2 256 ? 5.505   5.549   -13.315 1.00 70.82 ? 244 GLN B CB  1 
ATOM   2233 C  CG  . GLN B 2 256 ? 4.713   4.263   -13.213 1.00 74.65 ? 244 GLN B CG  1 
ATOM   2234 C  CD  . GLN B 2 256 ? 5.610   3.029   -13.325 1.00 86.97 ? 244 GLN B CD  1 
ATOM   2235 O  OE1 . GLN B 2 256 ? 6.730   3.097   -13.856 1.00 84.42 ? 244 GLN B OE1 1 
ATOM   2236 N  NE2 . GLN B 2 256 ? 5.127   1.899   -12.812 1.00 84.90 ? 244 GLN B NE2 1 
ATOM   2237 N  N   . PHE B 2 257 ? 4.620   7.564   -11.030 1.00 71.53 ? 245 PHE B N   1 
ATOM   2238 C  CA  . PHE B 2 257 ? 4.045   7.782   -9.710  1.00 72.73 ? 245 PHE B CA  1 
ATOM   2239 C  C   . PHE B 2 257 ? 4.020   9.268   -9.363  1.00 63.71 ? 245 PHE B C   1 
ATOM   2240 O  O   . PHE B 2 257 ? 4.270   9.637   -8.215  1.00 59.33 ? 245 PHE B O   1 
ATOM   2241 C  CB  . PHE B 2 257 ? 4.833   7.013   -8.650  1.00 66.07 ? 245 PHE B CB  1 
ATOM   2242 C  CG  . PHE B 2 257 ? 5.207   5.617   -9.064  1.00 68.29 ? 245 PHE B CG  1 
ATOM   2243 C  CD1 . PHE B 2 257 ? 6.394   5.373   -9.740  1.00 71.23 ? 245 PHE B CD1 1 
ATOM   2244 C  CD2 . PHE B 2 257 ? 4.384   4.544   -8.761  1.00 73.45 ? 245 PHE B CD2 1 
ATOM   2245 C  CE1 . PHE B 2 257 ? 6.751   4.082   -10.119 1.00 73.83 ? 245 PHE B CE1 1 
ATOM   2246 C  CE2 . PHE B 2 257 ? 4.733   3.251   -9.136  1.00 77.34 ? 245 PHE B CE2 1 
ATOM   2247 C  CZ  . PHE B 2 257 ? 5.920   3.021   -9.816  1.00 76.03 ? 245 PHE B CZ  1 
ATOM   2248 N  N   . ALA C 1 7   B -7.363  25.941  26.148  1.00 57.69 ? 1   ALA C N   1 
ATOM   2249 C  CA  . ALA C 1 7   B -6.748  25.676  27.435  1.00 49.64 ? 1   ALA C CA  1 
ATOM   2250 C  C   . ALA C 1 7   B -6.144  26.950  28.019  1.00 51.46 ? 1   ALA C C   1 
ATOM   2251 O  O   . ALA C 1 7   B -5.548  27.795  27.333  1.00 48.70 ? 1   ALA C O   1 
ATOM   2252 C  CB  . ALA C 1 7   B -5.680  24.580  27.319  1.00 39.50 ? 1   ALA C CB  1 
ATOM   2253 N  N   . ASP C 1 8   A -6.334  27.074  29.319  1.00 50.50 ? 1   ASP C N   1 
ATOM   2254 C  CA  . ASP C 1 8   A -5.655  28.060  30.129  1.00 44.41 ? 1   ASP C CA  1 
ATOM   2255 C  C   . ASP C 1 8   A -4.331  27.520  30.702  1.00 43.56 ? 1   ASP C C   1 
ATOM   2256 O  O   . ASP C 1 8   A -3.757  28.128  31.617  1.00 41.50 ? 1   ASP C O   1 
ATOM   2257 C  CB  . ASP C 1 8   A -6.608  28.478  31.249  1.00 45.67 ? 1   ASP C CB  1 
ATOM   2258 C  CG  . ASP C 1 8   A -6.239  29.784  31.856  1.00 48.21 ? 1   ASP C CG  1 
ATOM   2259 O  OD1 . ASP C 1 8   A -5.644  30.618  31.134  1.00 44.86 ? 1   ASP C OD1 1 
ATOM   2260 O  OD2 . ASP C 1 8   A -6.544  29.965  33.056  1.00 55.65 ? 1   ASP C OD2 1 
ATOM   2261 N  N   . CYS C 1 9   ? -3.836  26.394  30.179  1.00 39.37 ? 1   CYS C N   1 
ATOM   2262 C  CA  . CYS C 1 9   ? -2.819  25.615  30.878  1.00 36.50 ? 1   CYS C CA  1 
ATOM   2263 C  C   . CYS C 1 9   ? -1.509  26.384  31.008  1.00 34.84 ? 1   CYS C C   1 
ATOM   2264 O  O   . CYS C 1 9   ? -1.182  27.264  30.206  1.00 35.76 ? 1   CYS C O   1 
ATOM   2265 C  CB  . CYS C 1 9   ? -2.545  24.309  30.141  1.00 31.96 ? 1   CYS C CB  1 
ATOM   2266 S  SG  . CYS C 1 9   ? -1.954  24.585  28.430  1.00 38.58 ? 1   CYS C SG  1 
ATOM   2267 N  N   . GLY C 1 10  ? -0.707  25.970  31.978  1.00 32.44 ? 2   GLY C N   1 
ATOM   2268 C  CA  . GLY C 1 10  ? 0.652   26.456  32.064  1.00 32.78 ? 2   GLY C CA  1 
ATOM   2269 C  C   . GLY C 1 10  ? 0.800   27.887  32.519  1.00 31.69 ? 2   GLY C C   1 
ATOM   2270 O  O   . GLY C 1 10  ? 1.928   28.392  32.543  1.00 32.03 ? 2   GLY C O   1 
ATOM   2271 N  N   . LEU C 1 11  ? -0.292  28.566  32.853  1.00 32.13 ? 3   LEU C N   1 
ATOM   2272 C  CA  . LEU C 1 11  ? -0.240  29.910  33.408  1.00 31.80 ? 3   LEU C CA  1 
ATOM   2273 C  C   . LEU C 1 11  ? -0.690  29.844  34.862  1.00 33.79 ? 3   LEU C C   1 
ATOM   2274 O  O   . LEU C 1 11  ? -1.834  29.467  35.146  1.00 33.95 ? 3   LEU C O   1 
ATOM   2275 C  CB  . LEU C 1 11  ? -1.102  30.868  32.590  1.00 32.83 ? 3   LEU C CB  1 
ATOM   2276 C  CG  . LEU C 1 11  ? -0.561  31.081  31.168  1.00 32.37 ? 3   LEU C CG  1 
ATOM   2277 C  CD1 . LEU C 1 11  ? -1.477  31.955  30.357  1.00 34.04 ? 3   LEU C CD1 1 
ATOM   2278 C  CD2 . LEU C 1 11  ? 0.820   31.676  31.190  1.00 29.21 ? 3   LEU C CD2 1 
ATOM   2279 N  N   . ARG C 1 12  ? 0.218   30.220  35.791  1.00 34.52 ? 4   ARG C N   1 
ATOM   2280 C  CA  . ARG C 1 12  ? -0.067  29.958  37.203  1.00 33.42 ? 4   ARG C CA  1 
ATOM   2281 C  C   . ARG C 1 12  ? -0.839  31.113  37.826  1.00 34.95 ? 4   ARG C C   1 
ATOM   2282 O  O   . ARG C 1 12  ? -0.414  32.271  37.702  1.00 34.01 ? 4   ARG C O   1 
ATOM   2283 C  CB  . ARG C 1 12  ? 1.218   29.719  37.970  1.00 28.99 ? 4   ARG C CB  1 
ATOM   2284 C  CG  . ARG C 1 12  ? 2.068   28.648  37.318  1.00 31.15 ? 4   ARG C CG  1 
ATOM   2285 C  CD  . ARG C 1 12  ? 3.430   28.604  37.916  1.00 30.08 ? 4   ARG C CD  1 
ATOM   2286 N  NE  . ARG C 1 12  ? 4.224   29.757  37.532  1.00 31.54 ? 4   ARG C NE  1 
ATOM   2287 C  CZ  . ARG C 1 12  ? 5.428   30.010  38.024  1.00 35.96 ? 4   ARG C CZ  1 
ATOM   2288 N  NH1 . ARG C 1 12  ? 5.974   29.222  38.940  1.00 31.71 ? 4   ARG C NH1 1 
ATOM   2289 N  NH2 . ARG C 1 12  ? 6.097   31.079  37.590  1.00 33.08 ? 4   ARG C NH2 1 
ATOM   2290 N  N   . PRO C 1 13  ? -1.961  30.823  38.499  1.00 34.58 ? 5   PRO C N   1 
ATOM   2291 C  CA  . PRO C 1 13  ? -2.707  31.883  39.192  1.00 36.84 ? 5   PRO C CA  1 
ATOM   2292 C  C   . PRO C 1 13  ? -1.836  32.804  40.020  1.00 37.38 ? 5   PRO C C   1 
ATOM   2293 O  O   . PRO C 1 13  ? -1.989  34.027  39.949  1.00 41.52 ? 5   PRO C O   1 
ATOM   2294 C  CB  . PRO C 1 13  ? -3.692  31.084  40.047  1.00 37.72 ? 5   PRO C CB  1 
ATOM   2295 C  CG  . PRO C 1 13  ? -3.977  29.875  39.220  1.00 35.58 ? 5   PRO C CG  1 
ATOM   2296 C  CD  . PRO C 1 13  ? -2.702  29.551  38.486  1.00 33.33 ? 5   PRO C CD  1 
ATOM   2297 N  N   . LEU C 1 14  ? -0.930  32.254  40.810  1.00 34.55 ? 6   LEU C N   1 
ATOM   2298 C  CA  . LEU C 1 14  ? -0.118  33.082  41.693  1.00 37.51 ? 6   LEU C CA  1 
ATOM   2299 C  C   . LEU C 1 14  ? 1.129   33.678  41.028  1.00 38.67 ? 6   LEU C C   1 
ATOM   2300 O  O   . LEU C 1 14  ? 1.905   34.355  41.717  1.00 36.82 ? 6   LEU C O   1 
ATOM   2301 C  CB  . LEU C 1 14  ? 0.300   32.268  42.914  1.00 34.46 ? 6   LEU C CB  1 
ATOM   2302 C  CG  . LEU C 1 14  ? -0.853  31.793  43.787  1.00 35.03 ? 6   LEU C CG  1 
ATOM   2303 C  CD1 . LEU C 1 14  ? -0.392  31.729  45.203  1.00 33.09 ? 6   LEU C CD1 1 
ATOM   2304 C  CD2 . LEU C 1 14  ? -2.055  32.721  43.670  1.00 40.27 ? 6   LEU C CD2 1 
ATOM   2305 N  N   . PHE C 1 15  ? 1.385   33.438  39.739  1.00 33.58 ? 7   PHE C N   1 
ATOM   2306 C  CA  . PHE C 1 15  ? 2.590   34.047  39.183  1.00 37.36 ? 7   PHE C CA  1 
ATOM   2307 C  C   . PHE C 1 15  ? 2.335   34.735  37.848  1.00 37.85 ? 7   PHE C C   1 
ATOM   2308 O  O   . PHE C 1 15  ? 2.219   35.964  37.803  1.00 37.40 ? 7   PHE C O   1 
ATOM   2309 C  CB  . PHE C 1 15  ? 3.700   33.001  39.082  1.00 34.72 ? 7   PHE C CB  1 
ATOM   2310 C  CG  . PHE C 1 15  ? 4.240   32.583  40.426  1.00 35.00 ? 7   PHE C CG  1 
ATOM   2311 C  CD1 . PHE C 1 15  ? 5.222   33.332  41.061  1.00 33.10 ? 7   PHE C CD1 1 
ATOM   2312 C  CD2 . PHE C 1 15  ? 3.728   31.474  41.083  1.00 35.11 ? 7   PHE C CD2 1 
ATOM   2313 C  CE1 . PHE C 1 15  ? 5.712   32.959  42.311  1.00 30.09 ? 7   PHE C CE1 1 
ATOM   2314 C  CE2 . PHE C 1 15  ? 4.218   31.099  42.343  1.00 34.05 ? 7   PHE C CE2 1 
ATOM   2315 C  CZ  . PHE C 1 15  ? 5.214   31.846  42.946  1.00 31.00 ? 7   PHE C CZ  1 
ATOM   2316 N  N   . GLU C 1 16  ? 2.187   33.959  36.772  1.00 35.60 ? 8   GLU C N   1 
ATOM   2317 C  CA  . GLU C 1 16  ? 1.942   34.548  35.457  1.00 33.95 ? 8   GLU C CA  1 
ATOM   2318 C  C   . GLU C 1 16  ? 0.706   35.439  35.469  1.00 36.37 ? 8   GLU C C   1 
ATOM   2319 O  O   . GLU C 1 16  ? 0.736   36.552  34.935  1.00 39.97 ? 8   GLU C O   1 
ATOM   2320 C  CB  . GLU C 1 16  ? 1.768   33.436  34.408  1.00 35.46 ? 8   GLU C CB  1 
ATOM   2321 C  CG  . GLU C 1 16  ? 3.060   32.824  33.899  1.00 30.78 ? 8   GLU C CG  1 
ATOM   2322 C  CD  . GLU C 1 16  ? 3.618   31.821  34.897  1.00 35.90 ? 8   GLU C CD  1 
ATOM   2323 O  OE1 . GLU C 1 16  ? 2.817   31.228  35.667  1.00 33.12 ? 8   GLU C OE1 1 
ATOM   2324 O  OE2 . GLU C 1 16  ? 4.854   31.647  34.936  1.00 36.09 ? 8   GLU C OE2 1 
ATOM   2325 N  N   . LYS C 1 17  ? -0.382  34.981  36.099  1.00 37.37 ? 9   LYS C N   1 
ATOM   2326 C  CA  . LYS C 1 17  ? -1.640  35.720  36.060  1.00 39.29 ? 9   LYS C CA  1 
ATOM   2327 C  C   . LYS C 1 17  ? -1.619  37.022  36.855  1.00 43.32 ? 9   LYS C C   1 
ATOM   2328 O  O   . LYS C 1 17  ? -2.515  37.851  36.668  1.00 41.90 ? 9   LYS C O   1 
ATOM   2329 C  CB  . LYS C 1 17  ? -2.784  34.829  36.544  1.00 38.69 ? 9   LYS C CB  1 
ATOM   2330 C  CG  . LYS C 1 17  ? -3.040  33.642  35.610  1.00 42.21 ? 9   LYS C CG  1 
ATOM   2331 C  CD  . LYS C 1 17  ? -4.525  33.271  35.538  1.00 48.15 ? 9   LYS C CD  1 
ATOM   2332 C  CE  . LYS C 1 17  ? -4.753  31.752  35.452  1.00 42.65 ? 9   LYS C CE  1 
ATOM   2333 N  NZ  . LYS C 1 17  ? -5.801  31.337  36.454  1.00 46.18 ? 9   LYS C NZ  1 
ATOM   2334 N  N   . LYS C 1 18  ? -0.652  37.227  37.749  1.00 41.03 ? 10  LYS C N   1 
ATOM   2335 C  CA  . LYS C 1 18  ? -0.526  38.520  38.412  1.00 41.53 ? 10  LYS C CA  1 
ATOM   2336 C  C   . LYS C 1 18  ? 0.808   39.194  38.099  1.00 45.05 ? 10  LYS C C   1 
ATOM   2337 O  O   . LYS C 1 18  ? 1.275   40.032  38.877  1.00 46.73 ? 10  LYS C O   1 
ATOM   2338 C  CB  . LYS C 1 18  ? -0.749  38.391  39.915  1.00 40.40 ? 10  LYS C CB  1 
ATOM   2339 C  CG  . LYS C 1 18  ? 0.088   37.382  40.586  1.00 41.42 ? 10  LYS C CG  1 
ATOM   2340 C  CD  . LYS C 1 18  ? -0.777  36.586  41.541  1.00 44.19 ? 10  LYS C CD  1 
ATOM   2341 C  CE  . LYS C 1 18  ? -1.221  37.404  42.754  1.00 46.11 ? 10  LYS C CE  1 
ATOM   2342 N  NZ  . LYS C 1 18  ? -2.368  36.736  43.456  1.00 49.61 ? 10  LYS C NZ  1 
ATOM   2343 N  N   . SER C 1 19  ? 1.433   38.822  36.982  1.00 43.60 ? 11  SER C N   1 
ATOM   2344 C  CA  . SER C 1 19  ? 2.689   39.406  36.513  1.00 42.14 ? 11  SER C CA  1 
ATOM   2345 C  C   . SER C 1 19  ? 3.775   39.405  37.587  1.00 43.62 ? 11  SER C C   1 
ATOM   2346 O  O   . SER C 1 19  ? 4.389   40.430  37.884  1.00 47.52 ? 11  SER C O   1 
ATOM   2347 C  CB  . SER C 1 19  ? 2.450   40.817  35.985  1.00 47.04 ? 11  SER C CB  1 
ATOM   2348 O  OG  . SER C 1 19  ? 1.539   40.799  34.900  1.00 45.53 ? 11  SER C OG  1 
ATOM   2349 N  N   . LEU C 1 20  ? 4.032   38.220  38.145  1.00 44.38 ? 12  LEU C N   1 
ATOM   2350 C  CA  . LEU C 1 20  ? 5.050   38.002  39.162  1.00 39.14 ? 12  LEU C CA  1 
ATOM   2351 C  C   . LEU C 1 20  ? 5.948   36.824  38.784  1.00 37.78 ? 12  LEU C C   1 
ATOM   2352 O  O   . LEU C 1 20  ? 5.456   35.765  38.374  1.00 38.62 ? 12  LEU C O   1 
ATOM   2353 C  CB  . LEU C 1 20  ? 4.407   37.718  40.516  1.00 38.57 ? 12  LEU C CB  1 
ATOM   2354 C  CG  . LEU C 1 20  ? 3.777   38.823  41.347  1.00 39.29 ? 12  LEU C CG  1 
ATOM   2355 C  CD1 . LEU C 1 20  ? 3.106   38.164  42.554  1.00 30.87 ? 12  LEU C CD1 1 
ATOM   2356 C  CD2 . LEU C 1 20  ? 4.859   39.821  41.805  1.00 41.54 ? 12  LEU C CD2 1 
ATOM   2357 N  N   . GLU C 1 21  ? 7.261   37.011  38.957  1.00 33.01 ? 13  GLU C N   1 
ATOM   2358 C  CA  . GLU C 1 21  ? 8.267   35.980  38.725  1.00 33.54 ? 13  GLU C CA  1 
ATOM   2359 C  C   . GLU C 1 21  ? 8.419   35.095  39.953  1.00 35.40 ? 13  GLU C C   1 
ATOM   2360 O  O   . GLU C 1 21  ? 8.334   35.581  41.090  1.00 34.39 ? 13  GLU C O   1 
ATOM   2361 C  CB  . GLU C 1 21  ? 9.634   36.613  38.425  1.00 33.44 ? 13  GLU C CB  1 
ATOM   2362 C  CG  . GLU C 1 21  ? 9.975   36.804  36.974  1.00 37.33 ? 13  GLU C CG  1 
ATOM   2363 C  CD  . GLU C 1 21  ? 11.472  37.033  36.720  1.00 39.71 ? 13  GLU C CD  1 
ATOM   2364 O  OE1 . GLU C 1 21  ? 12.311  36.727  37.584  1.00 36.40 ? 13  GLU C OE1 1 
ATOM   2365 O  OE2 . GLU C 1 21  ? 11.816  37.527  35.630  1.00 46.00 ? 13  GLU C OE2 1 
ATOM   2366 N  N   . ASP C 1 22  ? 8.681   33.799  39.732  1.00 29.18 ? 14  ASP C N   1 
ATOM   2367 C  CA  . ASP C 1 22  ? 9.150   32.994  40.859  1.00 37.28 ? 14  ASP C CA  1 
ATOM   2368 C  C   . ASP C 1 22  ? 10.659  33.221  41.066  1.00 35.08 ? 14  ASP C C   1 
ATOM   2369 O  O   . ASP C 1 22  ? 11.306  33.993  40.345  1.00 32.89 ? 14  ASP C O   1 
ATOM   2370 C  CB  . ASP C 1 22  ? 8.778   31.511  40.693  1.00 31.86 ? 14  ASP C CB  1 
ATOM   2371 C  CG  . ASP C 1 22  ? 9.575   30.785  39.605  1.00 32.90 ? 14  ASP C CG  1 
ATOM   2372 O  OD1 . ASP C 1 22  ? 10.818  30.923  39.527  1.00 34.55 ? 14  ASP C OD1 1 
ATOM   2373 O  OD2 . ASP C 1 22  ? 8.944   30.023  38.838  1.00 33.30 ? 14  ASP C OD2 1 
ATOM   2374 N  N   . LYS C 1 23  A 11.206  32.630  42.140  1.00 30.13 ? 14  LYS C N   1 
ATOM   2375 C  CA  . LYS C 1 23  A 12.613  32.900  42.552  1.00 33.63 ? 14  LYS C CA  1 
ATOM   2376 C  C   . LYS C 1 23  A 13.666  32.428  41.544  1.00 32.29 ? 14  LYS C C   1 
ATOM   2377 O  O   . LYS C 1 23  A 14.757  33.061  41.589  1.00 31.82 ? 14  LYS C O   1 
ATOM   2378 C  CB  . LYS C 1 23  A 12.895  32.274  43.923  1.00 34.02 ? 14  LYS C CB  1 
ATOM   2379 C  CG  . LYS C 1 23  A 12.517  33.147  45.106  1.00 40.33 ? 14  LYS C CG  1 
ATOM   2380 C  CD  . LYS C 1 23  A 12.340  32.344  46.387  1.00 48.62 ? 14  LYS C CD  1 
ATOM   2381 C  CE  . LYS C 1 23  A 12.358  33.202  47.609  1.00 51.63 ? 14  LYS C CE  1 
ATOM   2382 N  NZ  . LYS C 1 23  A 12.167  32.404  48.822  1.00 48.16 ? 14  LYS C NZ  1 
ATOM   2383 N  N   . THR C 1 24  B 13.372  31.428  40.685  1.00 29.14 ? 14  THR C N   1 
ATOM   2384 C  CA  . THR C 1 24  B 14.446  30.894  39.855  1.00 32.45 ? 14  THR C CA  1 
ATOM   2385 C  C   . THR C 1 24  B 14.130  30.744  38.363  1.00 36.51 ? 14  THR C C   1 
ATOM   2386 O  O   . THR C 1 24  B 15.020  30.326  37.610  1.00 36.22 ? 14  THR C O   1 
ATOM   2387 C  CB  . THR C 1 24  B 14.924  29.523  40.385  1.00 34.72 ? 14  THR C CB  1 
ATOM   2388 O  OG1 . THR C 1 24  B 14.026  28.475  39.979  1.00 34.37 ? 14  THR C OG1 1 
ATOM   2389 C  CG2 . THR C 1 24  B 15.061  29.529  41.901  1.00 28.26 ? 14  THR C CG2 1 
ATOM   2390 N  N   . GLU C 1 25  C 12.933  31.114  37.898  1.00 30.94 ? 14  GLU C N   1 
ATOM   2391 C  CA  . GLU C 1 25  C 12.630  30.928  36.481  1.00 34.77 ? 14  GLU C CA  1 
ATOM   2392 C  C   . GLU C 1 25  C 13.580  31.718  35.584  1.00 33.98 ? 14  GLU C C   1 
ATOM   2393 O  O   . GLU C 1 25  C 13.833  31.317  34.431  1.00 31.36 ? 14  GLU C O   1 
ATOM   2394 C  CB  . GLU C 1 25  C 11.188  31.335  36.189  1.00 35.08 ? 14  GLU C CB  1 
ATOM   2395 C  CG  . GLU C 1 25  C 10.892  32.794  36.452  1.00 32.17 ? 14  GLU C CG  1 
ATOM   2396 C  CD  . GLU C 1 25  C 9.442   33.108  36.226  1.00 34.11 ? 14  GLU C CD  1 
ATOM   2397 O  OE1 . GLU C 1 25  C 9.063   33.382  35.071  1.00 33.92 ? 14  GLU C OE1 1 
ATOM   2398 O  OE2 . GLU C 1 25  C 8.667   33.042  37.203  1.00 36.55 ? 14  GLU C OE2 1 
ATOM   2399 N  N   . ARG C 1 26  D 14.116  32.838  36.084  1.00 31.39 ? 14  ARG C N   1 
ATOM   2400 C  CA  . ARG C 1 26  D 15.060  33.597  35.274  1.00 36.84 ? 14  ARG C CA  1 
ATOM   2401 C  C   . ARG C 1 26  D 16.258  32.744  34.871  1.00 36.68 ? 14  ARG C C   1 
ATOM   2402 O  O   . ARG C 1 26  D 16.824  32.937  33.781  1.00 32.07 ? 14  ARG C O   1 
ATOM   2403 C  CB  . ARG C 1 26  D 15.524  34.851  36.024  1.00 40.18 ? 14  ARG C CB  1 
ATOM   2404 C  CG  . ARG C 1 26  D 16.205  35.869  35.098  1.00 37.50 ? 14  ARG C CG  1 
ATOM   2405 C  CD  . ARG C 1 26  D 16.404  37.210  35.759  1.00 36.85 ? 14  ARG C CD  1 
ATOM   2406 N  NE  . ARG C 1 26  D 15.142  37.910  35.964  1.00 37.87 ? 14  ARG C NE  1 
ATOM   2407 C  CZ  . ARG C 1 26  D 15.041  39.214  36.196  1.00 40.25 ? 14  ARG C CZ  1 
ATOM   2408 N  NH1 . ARG C 1 26  D 16.107  39.998  36.196  1.00 39.16 ? 14  ARG C NH1 1 
ATOM   2409 N  NH2 . ARG C 1 26  D 13.844  39.739  36.460  1.00 35.80 ? 14  ARG C NH2 1 
ATOM   2410 N  N   . GLU C 1 27  E 16.645  31.784  35.724  1.00 33.62 ? 14  GLU C N   1 
ATOM   2411 C  CA  . GLU C 1 27  E 17.732  30.885  35.362  1.00 35.71 ? 14  GLU C CA  1 
ATOM   2412 C  C   . GLU C 1 27  E 17.373  30.092  34.114  1.00 35.30 ? 14  GLU C C   1 
ATOM   2413 O  O   . GLU C 1 27  E 18.208  29.919  33.214  1.00 35.45 ? 14  GLU C O   1 
ATOM   2414 C  CB  . GLU C 1 27  E 18.066  29.944  36.520  1.00 36.51 ? 14  GLU C CB  1 
ATOM   2415 C  CG  . GLU C 1 27  E 19.286  29.057  36.230  1.00 34.94 ? 14  GLU C CG  1 
ATOM   2416 C  CD  . GLU C 1 27  E 19.467  27.943  37.243  1.00 36.37 ? 14  GLU C CD  1 
ATOM   2417 O  OE1 . GLU C 1 27  E 18.477  27.604  37.939  1.00 40.35 ? 14  GLU C OE1 1 
ATOM   2418 O  OE2 . GLU C 1 27  E 20.598  27.409  37.340  1.00 35.08 ? 14  GLU C OE2 1 
ATOM   2419 N  N   . LEU C 1 28  F 16.125  29.626  34.031  1.00 30.96 ? 14  LEU C N   1 
ATOM   2420 C  CA  . LEU C 1 28  F 15.677  28.914  32.842  1.00 29.52 ? 14  LEU C CA  1 
ATOM   2421 C  C   . LEU C 1 28  F 15.782  29.806  31.616  1.00 31.92 ? 14  LEU C C   1 
ATOM   2422 O  O   . LEU C 1 28  F 16.449  29.463  30.613  1.00 37.07 ? 14  LEU C O   1 
ATOM   2423 C  CB  . LEU C 1 28  F 14.234  28.462  33.048  1.00 27.41 ? 14  LEU C CB  1 
ATOM   2424 C  CG  . LEU C 1 28  F 13.894  27.174  33.813  1.00 33.76 ? 14  LEU C CG  1 
ATOM   2425 C  CD1 . LEU C 1 28  F 15.110  26.471  34.413  1.00 29.53 ? 14  LEU C CD1 1 
ATOM   2426 C  CD2 . LEU C 1 28  F 12.849  27.439  34.881  1.00 27.34 ? 14  LEU C CD2 1 
ATOM   2427 N  N   . LEU C 1 29  G 15.174  30.994  31.715  1.00 32.93 ? 14  LEU C N   1 
ATOM   2428 C  CA  . LEU C 1 29  G 15.188  31.948  30.609  1.00 37.10 ? 14  LEU C CA  1 
ATOM   2429 C  C   . LEU C 1 29  G 16.604  32.184  30.091  1.00 38.12 ? 14  LEU C C   1 
ATOM   2430 O  O   . LEU C 1 29  G 16.862  32.107  28.884  1.00 40.45 ? 14  LEU C O   1 
ATOM   2431 C  CB  . LEU C 1 29  G 14.551  33.257  31.059  1.00 38.71 ? 14  LEU C CB  1 
ATOM   2432 C  CG  . LEU C 1 29  G 14.556  34.365  30.016  1.00 43.07 ? 14  LEU C CG  1 
ATOM   2433 C  CD1 . LEU C 1 29  G 13.439  34.082  29.023  1.00 41.99 ? 14  LEU C CD1 1 
ATOM   2434 C  CD2 . LEU C 1 29  G 14.380  35.738  30.682  1.00 42.46 ? 14  LEU C CD2 1 
ATOM   2435 N  N   . GLU C 1 30  H 17.542  32.437  30.998  1.00 37.58 ? 14  GLU C N   1 
ATOM   2436 C  CA  . GLU C 1 30  H 18.909  32.717  30.592  1.00 39.17 ? 14  GLU C CA  1 
ATOM   2437 C  C   . GLU C 1 30  H 19.637  31.473  30.119  1.00 44.25 ? 14  GLU C C   1 
ATOM   2438 O  O   . GLU C 1 30  H 20.611  31.591  29.368  1.00 47.97 ? 14  GLU C O   1 
ATOM   2439 C  CB  . GLU C 1 30  H 19.664  33.381  31.735  1.00 38.75 ? 14  GLU C CB  1 
ATOM   2440 C  CG  . GLU C 1 30  H 19.215  34.812  31.921  1.00 41.84 ? 14  GLU C CG  1 
ATOM   2441 C  CD  . GLU C 1 30  H 19.812  35.470  33.127  1.00 46.65 ? 14  GLU C CD  1 
ATOM   2442 O  OE1 . GLU C 1 30  H 20.778  34.920  33.707  1.00 51.07 ? 14  GLU C OE1 1 
ATOM   2443 O  OE2 . GLU C 1 30  H 19.308  36.549  33.490  1.00 44.64 ? 14  GLU C OE2 1 
ATOM   2444 N  N   . SER C 1 31  I 19.200  30.286  30.540  1.00 39.61 ? 14  SER C N   1 
ATOM   2445 C  CA  . SER C 1 31  I 19.735  29.072  29.941  1.00 35.38 ? 14  SER C CA  1 
ATOM   2446 C  C   . SER C 1 31  I 19.434  29.032  28.455  1.00 37.11 ? 14  SER C C   1 
ATOM   2447 O  O   . SER C 1 31  I 20.138  28.360  27.696  1.00 37.91 ? 14  SER C O   1 
ATOM   2448 C  CB  . SER C 1 31  I 19.167  27.832  30.632  1.00 36.18 ? 14  SER C CB  1 
ATOM   2449 O  OG  . SER C 1 31  I 17.906  27.453  30.079  1.00 37.78 ? 14  SER C OG  1 
ATOM   2450 N  N   . TYR C 1 32  J 18.370  29.706  28.020  1.00 40.76 ? 14  TYR C N   1 
ATOM   2451 C  CA  . TYR C 1 32  J 18.123  29.727  26.570  1.00 46.27 ? 14  TYR C CA  1 
ATOM   2452 C  C   . TYR C 1 32  J 19.211  30.454  25.777  1.00 50.39 ? 14  TYR C C   1 
ATOM   2453 O  O   . TYR C 1 32  J 19.456  30.107  24.615  1.00 50.32 ? 14  TYR C O   1 
ATOM   2454 C  CB  . TYR C 1 32  J 16.773  30.345  26.270  1.00 42.52 ? 14  TYR C CB  1 
ATOM   2455 C  CG  . TYR C 1 32  J 15.660  29.491  26.788  1.00 40.63 ? 14  TYR C CG  1 
ATOM   2456 C  CD1 . TYR C 1 32  J 15.736  28.112  26.701  1.00 37.75 ? 14  TYR C CD1 1 
ATOM   2457 C  CD2 . TYR C 1 32  J 14.540  30.061  27.388  1.00 41.24 ? 14  TYR C CD2 1 
ATOM   2458 C  CE1 . TYR C 1 32  J 14.704  27.308  27.175  1.00 43.94 ? 14  TYR C CE1 1 
ATOM   2459 C  CE2 . TYR C 1 32  J 13.506  29.275  27.870  1.00 39.09 ? 14  TYR C CE2 1 
ATOM   2460 C  CZ  . TYR C 1 32  J 13.590  27.900  27.763  1.00 43.89 ? 14  TYR C CZ  1 
ATOM   2461 O  OH  . TYR C 1 32  J 12.564  27.111  28.246  1.00 44.57 ? 14  TYR C OH  1 
ATOM   2462 N  N   . ILE C 1 33  K 19.823  31.492  26.338  1.00 60.66 ? 14  ILE C N   1 
ATOM   2463 C  CA  . ILE C 1 33  K 20.829  32.285  25.599  1.00 64.12 ? 14  ILE C CA  1 
ATOM   2464 C  C   . ILE C 1 33  K 22.147  31.516  25.455  1.00 52.40 ? 14  ILE C C   1 
ATOM   2465 O  O   . ILE C 1 33  K 22.573  31.202  24.340  1.00 57.44 ? 14  ILE C O   1 
ATOM   2466 C  CB  . ILE C 1 33  K 21.080  33.675  26.273  1.00 63.73 ? 14  ILE C CB  1 
ATOM   2467 C  CG1 . ILE C 1 33  K 21.991  33.523  27.500  1.00 65.72 ? 14  ILE C CG1 1 
ATOM   2468 C  CG2 . ILE C 1 33  K 19.758  34.387  26.599  1.00 61.37 ? 14  ILE C CG2 1 
ATOM   2469 C  CD1 . ILE C 1 33  K 21.956  34.687  28.468  1.00 65.93 ? 14  ILE C CD1 1 
ATOM   2470 N  N   . ILE D 2 1   ? 14.329  15.007  45.825  1.00 35.39 ? 16  ILE D N   1 
ATOM   2471 C  CA  . ILE D 2 1   ? 15.114  16.027  45.137  1.00 32.38 ? 16  ILE D CA  1 
ATOM   2472 C  C   . ILE D 2 1   ? 16.390  16.336  45.934  1.00 38.10 ? 16  ILE D C   1 
ATOM   2473 O  O   . ILE D 2 1   ? 16.332  16.792  47.086  1.00 36.59 ? 16  ILE D O   1 
ATOM   2474 C  CB  . ILE D 2 1   ? 14.297  17.316  44.919  1.00 31.55 ? 16  ILE D CB  1 
ATOM   2475 C  CG1 . ILE D 2 1   ? 12.992  17.057  44.150  1.00 29.91 ? 16  ILE D CG1 1 
ATOM   2476 C  CG2 . ILE D 2 1   ? 15.139  18.336  44.160  1.00 36.55 ? 16  ILE D CG2 1 
ATOM   2477 C  CD1 . ILE D 2 1   ? 13.181  16.857  42.680  1.00 28.01 ? 16  ILE D CD1 1 
ATOM   2478 N  N   . VAL D 2 2   ? 17.547  16.136  45.306  1.00 37.87 ? 17  VAL D N   1 
ATOM   2479 C  CA  . VAL D 2 2   ? 18.837  16.401  45.933  1.00 37.08 ? 17  VAL D CA  1 
ATOM   2480 C  C   . VAL D 2 2   ? 19.329  17.763  45.463  1.00 35.71 ? 17  VAL D C   1 
ATOM   2481 O  O   . VAL D 2 2   ? 19.211  18.099  44.280  1.00 36.76 ? 17  VAL D O   1 
ATOM   2482 C  CB  . VAL D 2 2   ? 19.856  15.292  45.595  1.00 40.48 ? 17  VAL D CB  1 
ATOM   2483 C  CG1 . VAL D 2 2   ? 21.189  15.568  46.281  1.00 38.80 ? 17  VAL D CG1 1 
ATOM   2484 C  CG2 . VAL D 2 2   ? 19.308  13.907  45.982  1.00 38.05 ? 17  VAL D CG2 1 
ATOM   2485 N  N   . GLU D 2 3   ? 19.855  18.560  46.391  1.00 34.61 ? 18  GLU D N   1 
ATOM   2486 C  CA  . GLU D 2 3   ? 20.396  19.887  46.077  1.00 40.17 ? 18  GLU D CA  1 
ATOM   2487 C  C   . GLU D 2 3   ? 19.322  20.830  45.530  1.00 35.58 ? 18  GLU D C   1 
ATOM   2488 O  O   . GLU D 2 3   ? 19.617  21.749  44.760  1.00 36.22 ? 18  GLU D O   1 
ATOM   2489 C  CB  . GLU D 2 3   ? 21.578  19.800  45.100  1.00 37.52 ? 18  GLU D CB  1 
ATOM   2490 C  CG  . GLU D 2 3   ? 22.808  19.087  45.673  1.00 45.33 ? 18  GLU D CG  1 
ATOM   2491 C  CD  . GLU D 2 3   ? 23.258  19.661  47.013  1.00 46.23 ? 18  GLU D CD  1 
ATOM   2492 O  OE1 . GLU D 2 3   ? 23.537  20.884  47.087  1.00 44.18 ? 18  GLU D OE1 1 
ATOM   2493 O  OE2 . GLU D 2 3   ? 23.319  18.885  47.994  1.00 44.60 ? 18  GLU D OE2 1 
ATOM   2494 N  N   . GLY D 2 4   ? 18.075  20.626  45.915  1.00 32.19 ? 19  GLY D N   1 
ATOM   2495 C  CA  . GLY D 2 4   ? 16.997  21.496  45.502  1.00 33.03 ? 19  GLY D CA  1 
ATOM   2496 C  C   . GLY D 2 4   ? 16.735  22.560  46.537  1.00 31.02 ? 19  GLY D C   1 
ATOM   2497 O  O   . GLY D 2 4   ? 17.564  22.832  47.406  1.00 37.94 ? 19  GLY D O   1 
ATOM   2498 N  N   . SER D 2 5   ? 15.557  23.160  46.455  1.00 31.36 ? 20  SER D N   1 
ATOM   2499 C  CA  . SER D 2 5   ? 15.138  24.127  47.458  1.00 31.25 ? 20  SER D CA  1 
ATOM   2500 C  C   . SER D 2 5   ? 13.628  24.041  47.643  1.00 32.15 ? 20  SER D C   1 
ATOM   2501 O  O   . SER D 2 5   ? 12.927  23.321  46.925  1.00 30.67 ? 20  SER D O   1 
ATOM   2502 C  CB  . SER D 2 5   ? 15.549  25.530  47.057  1.00 29.09 ? 20  SER D CB  1 
ATOM   2503 O  OG  . SER D 2 5   ? 15.107  25.775  45.737  1.00 38.14 ? 20  SER D OG  1 
ATOM   2504 N  N   . ASP D 2 6   ? 13.132  24.801  48.611  1.00 30.76 ? 21  ASP D N   1 
ATOM   2505 C  CA  . ASP D 2 6   ? 11.708  24.805  48.896  1.00 28.69 ? 21  ASP D CA  1 
ATOM   2506 C  C   . ASP D 2 6   ? 10.977  25.587  47.829  1.00 35.57 ? 21  ASP D C   1 
ATOM   2507 O  O   . ASP D 2 6   ? 11.334  26.730  47.522  1.00 38.40 ? 21  ASP D O   1 
ATOM   2508 C  CB  . ASP D 2 6   ? 11.412  25.410  50.257  1.00 26.20 ? 21  ASP D CB  1 
ATOM   2509 C  CG  . ASP D 2 6   ? 11.983  24.597  51.378  1.00 32.35 ? 21  ASP D CG  1 
ATOM   2510 O  OD1 . ASP D 2 6   ? 12.583  23.545  51.099  1.00 40.04 ? 21  ASP D OD1 1 
ATOM   2511 O  OD2 . ASP D 2 6   ? 11.845  25.007  52.543  1.00 36.19 ? 21  ASP D OD2 1 
ATOM   2512 N  N   . ALA D 2 7   ? 9.950   24.962  47.269  1.00 34.26 ? 22  ALA D N   1 
ATOM   2513 C  CA  . ALA D 2 7   ? 9.106   25.631  46.308  1.00 29.92 ? 22  ALA D CA  1 
ATOM   2514 C  C   . ALA D 2 7   ? 8.350   26.760  46.989  1.00 31.95 ? 22  ALA D C   1 
ATOM   2515 O  O   . ALA D 2 7   ? 7.992   26.664  48.160  1.00 33.00 ? 22  ALA D O   1 
ATOM   2516 C  CB  . ALA D 2 7   ? 8.143   24.619  45.684  1.00 31.50 ? 22  ALA D CB  1 
ATOM   2517 N  N   . GLU D 2 8   ? 8.125   27.846  46.260  1.00 33.01 ? 23  GLU D N   1 
ATOM   2518 C  CA  . GLU D 2 8   ? 7.159   28.809  46.740  1.00 30.01 ? 23  GLU D CA  1 
ATOM   2519 C  C   . GLU D 2 8   ? 5.763   28.230  46.547  1.00 37.79 ? 23  GLU D C   1 
ATOM   2520 O  O   . GLU D 2 8   ? 5.547   27.303  45.753  1.00 32.94 ? 23  GLU D O   1 
ATOM   2521 C  CB  . GLU D 2 8   ? 7.311   30.146  46.016  1.00 34.14 ? 23  GLU D CB  1 
ATOM   2522 C  CG  . GLU D 2 8   ? 8.755   30.681  46.010  1.00 39.36 ? 23  GLU D CG  1 
ATOM   2523 C  CD  . GLU D 2 8   ? 9.082   31.532  44.778  1.00 41.46 ? 23  GLU D CD  1 
ATOM   2524 O  OE1 . GLU D 2 8   ? 8.489   32.627  44.647  1.00 44.79 ? 23  GLU D OE1 1 
ATOM   2525 O  OE2 . GLU D 2 8   ? 9.918   31.103  43.938  1.00 36.64 ? 23  GLU D OE2 1 
ATOM   2526 N  N   . ILE D 2 9   ? 4.811   28.781  47.301  1.00 37.74 ? 24  ILE D N   1 
ATOM   2527 C  CA  . ILE D 2 9   ? 3.425   28.334  47.234  1.00 33.05 ? 24  ILE D CA  1 
ATOM   2528 C  C   . ILE D 2 9   ? 2.858   28.665  45.866  1.00 27.88 ? 24  ILE D C   1 
ATOM   2529 O  O   . ILE D 2 9   ? 3.052   29.770  45.351  1.00 29.88 ? 24  ILE D O   1 
ATOM   2530 C  CB  . ILE D 2 9   ? 2.603   28.992  48.348  1.00 31.13 ? 24  ILE D CB  1 
ATOM   2531 C  CG1 . ILE D 2 9   ? 2.694   28.150  49.612  1.00 38.31 ? 24  ILE D CG1 1 
ATOM   2532 C  CG2 . ILE D 2 9   ? 1.180   29.180  47.905  1.00 27.13 ? 24  ILE D CG2 1 
ATOM   2533 C  CD1 . ILE D 2 9   ? 2.495   28.945  50.856  1.00 44.71 ? 24  ILE D CD1 1 
ATOM   2534 N  N   . GLY D 2 10  ? 2.208   27.691  45.243  1.00 33.76 ? 25  GLY D N   1 
ATOM   2535 C  CA  . GLY D 2 10  ? 1.643   27.920  43.931  1.00 36.11 ? 25  GLY D CA  1 
ATOM   2536 C  C   . GLY D 2 10  ? 2.655   27.928  42.812  1.00 32.76 ? 25  GLY D C   1 
ATOM   2537 O  O   . GLY D 2 10  ? 2.294   28.241  41.668  1.00 31.97 ? 25  GLY D O   1 
ATOM   2538 N  N   . MET D 2 11  ? 3.919   27.643  43.119  1.00 30.94 ? 26  MET D N   1 
ATOM   2539 C  CA  . MET D 2 11  ? 4.956   27.621  42.100  1.00 34.22 ? 26  MET D CA  1 
ATOM   2540 C  C   . MET D 2 11  ? 4.731   26.507  41.090  1.00 36.25 ? 26  MET D C   1 
ATOM   2541 O  O   . MET D 2 11  ? 5.079   26.662  39.908  1.00 35.06 ? 26  MET D O   1 
ATOM   2542 C  CB  . MET D 2 11  ? 6.315   27.476  42.764  1.00 33.99 ? 26  MET D CB  1 
ATOM   2543 C  CG  . MET D 2 11  ? 7.479   27.560  41.846  1.00 31.40 ? 26  MET D CG  1 
ATOM   2544 S  SD  . MET D 2 11  ? 8.886   27.084  42.839  1.00 37.94 ? 26  MET D SD  1 
ATOM   2545 C  CE  . MET D 2 11  ? 10.166  28.077  42.051  1.00 32.65 ? 26  MET D CE  1 
ATOM   2546 N  N   . SER D 2 12  ? 4.132   25.394  41.525  1.00 32.19 ? 27  SER D N   1 
ATOM   2547 C  CA  . SER D 2 12  ? 3.977   24.195  40.698  1.00 28.49 ? 27  SER D CA  1 
ATOM   2548 C  C   . SER D 2 12  ? 2.558   23.682  40.870  1.00 29.31 ? 27  SER D C   1 
ATOM   2549 O  O   . SER D 2 12  ? 2.330   22.574  41.360  1.00 31.45 ? 27  SER D O   1 
ATOM   2550 C  CB  . SER D 2 12  ? 5.016   23.146  41.100  1.00 27.52 ? 27  SER D CB  1 
ATOM   2551 O  OG  . SER D 2 12  ? 4.993   21.979  40.304  1.00 26.07 ? 27  SER D OG  1 
ATOM   2552 N  N   . PRO D 2 13  ? 1.561   24.479  40.478  1.00 31.70 ? 28  PRO D N   1 
ATOM   2553 C  CA  . PRO D 2 13  ? 0.173   24.137  40.831  1.00 29.14 ? 28  PRO D CA  1 
ATOM   2554 C  C   . PRO D 2 13  ? -0.343  22.869  40.165  1.00 30.61 ? 28  PRO D C   1 
ATOM   2555 O  O   . PRO D 2 13  ? -1.470  22.457  40.462  1.00 30.44 ? 28  PRO D O   1 
ATOM   2556 C  CB  . PRO D 2 13  ? -0.615  25.372  40.372  1.00 29.62 ? 28  PRO D CB  1 
ATOM   2557 C  CG  . PRO D 2 13  ? 0.182   25.885  39.192  1.00 29.51 ? 28  PRO D CG  1 
ATOM   2558 C  CD  . PRO D 2 13  ? 1.636   25.634  39.558  1.00 29.90 ? 28  PRO D CD  1 
ATOM   2559 N  N   . TRP D 2 14  ? 0.417   22.255  39.261  1.00 26.47 ? 29  TRP D N   1 
ATOM   2560 C  CA  . TRP D 2 14  ? 0.033   20.997  38.637  1.00 26.57 ? 29  TRP D CA  1 
ATOM   2561 C  C   . TRP D 2 14  ? 0.604   19.780  39.370  1.00 28.35 ? 29  TRP D C   1 
ATOM   2562 O  O   . TRP D 2 14  ? 0.441   18.643  38.901  1.00 26.48 ? 29  TRP D O   1 
ATOM   2563 C  CB  . TRP D 2 14  ? 0.488   21.000  37.167  1.00 27.25 ? 29  TRP D CB  1 
ATOM   2564 C  CG  . TRP D 2 14  ? 1.780   21.715  36.968  1.00 26.80 ? 29  TRP D CG  1 
ATOM   2565 C  CD1 . TRP D 2 14  ? 3.026   21.215  37.184  1.00 26.94 ? 29  TRP D CD1 1 
ATOM   2566 C  CD2 . TRP D 2 14  ? 1.967   23.077  36.540  1.00 30.45 ? 29  TRP D CD2 1 
ATOM   2567 N  NE1 . TRP D 2 14  ? 3.982   22.164  36.890  1.00 27.60 ? 29  TRP D NE1 1 
ATOM   2568 C  CE2 . TRP D 2 14  ? 3.359   23.315  36.495  1.00 24.80 ? 29  TRP D CE2 1 
ATOM   2569 C  CE3 . TRP D 2 14  ? 1.097   24.116  36.206  1.00 31.10 ? 29  TRP D CE3 1 
ATOM   2570 C  CZ2 . TRP D 2 14  ? 3.899   24.542  36.130  1.00 24.79 ? 29  TRP D CZ2 1 
ATOM   2571 C  CZ3 . TRP D 2 14  ? 1.643   25.336  35.826  1.00 31.57 ? 29  TRP D CZ3 1 
ATOM   2572 C  CH2 . TRP D 2 14  ? 3.033   25.536  35.800  1.00 28.08 ? 29  TRP D CH2 1 
ATOM   2573 N  N   . GLN D 2 15  ? 1.292   19.996  40.488  1.00 26.36 ? 30  GLN D N   1 
ATOM   2574 C  CA  . GLN D 2 15  ? 1.924   18.913  41.221  1.00 26.42 ? 30  GLN D CA  1 
ATOM   2575 C  C   . GLN D 2 15  ? 0.871   18.001  41.828  1.00 26.53 ? 30  GLN D C   1 
ATOM   2576 O  O   . GLN D 2 15  ? -0.084  18.472  42.448  1.00 27.77 ? 30  GLN D O   1 
ATOM   2577 C  CB  . GLN D 2 15  ? 2.798   19.503  42.321  1.00 30.30 ? 30  GLN D CB  1 
ATOM   2578 C  CG  . GLN D 2 15  ? 3.908   18.590  42.820  1.00 32.65 ? 30  GLN D CG  1 
ATOM   2579 C  CD  . GLN D 2 15  ? 5.039   18.445  41.815  1.00 31.78 ? 30  GLN D CD  1 
ATOM   2580 O  OE1 . GLN D 2 15  ? 5.247   19.317  40.945  1.00 31.54 ? 30  GLN D OE1 1 
ATOM   2581 N  NE2 . GLN D 2 15  ? 5.784   17.344  41.931  1.00 28.56 ? 30  GLN D NE2 1 
ATOM   2582 N  N   . VAL D 2 16  ? 1.043   16.694  41.667  1.00 26.42 ? 31  VAL D N   1 
ATOM   2583 C  CA  . VAL D 2 16  ? 0.120   15.716  42.227  1.00 28.26 ? 31  VAL D CA  1 
ATOM   2584 C  C   . VAL D 2 16  ? 0.928   14.715  43.029  1.00 27.27 ? 31  VAL D C   1 
ATOM   2585 O  O   . VAL D 2 16  ? 2.042   14.351  42.633  1.00 26.77 ? 31  VAL D O   1 
ATOM   2586 C  CB  . VAL D 2 16  ? -0.693  14.993  41.135  1.00 26.84 ? 31  VAL D CB  1 
ATOM   2587 C  CG1 . VAL D 2 16  ? -1.563  13.904  41.746  1.00 25.36 ? 31  VAL D CG1 1 
ATOM   2588 C  CG2 . VAL D 2 16  ? -1.549  15.990  40.392  1.00 29.58 ? 31  VAL D CG2 1 
ATOM   2589 N  N   . MET D 2 17  ? 0.379   14.302  44.172  1.00 27.58 ? 32  MET D N   1 
ATOM   2590 C  CA  . MET D 2 17  ? 0.921   13.204  44.958  1.00 26.81 ? 32  MET D CA  1 
ATOM   2591 C  C   . MET D 2 17  ? 0.103   11.962  44.679  1.00 22.41 ? 32  MET D C   1 
ATOM   2592 O  O   . MET D 2 17  ? -1.129  12.022  44.647  1.00 23.66 ? 32  MET D O   1 
ATOM   2593 C  CB  . MET D 2 17  ? 0.880   13.488  46.465  1.00 26.98 ? 32  MET D CB  1 
ATOM   2594 C  CG  . MET D 2 17  ? 1.626   14.718  46.944  1.00 26.37 ? 32  MET D CG  1 
ATOM   2595 S  SD  . MET D 2 17  ? 1.385   14.976  48.723  1.00 31.68 ? 32  MET D SD  1 
ATOM   2596 C  CE  . MET D 2 17  ? 3.043   15.067  49.336  1.00 32.61 ? 32  MET D CE  1 
ATOM   2597 N  N   . LEU D 2 18  ? 0.793   10.834  44.564  1.00 26.89 ? 33  LEU D N   1 
ATOM   2598 C  CA  . LEU D 2 18  ? 0.190   9.529   44.351  1.00 26.14 ? 33  LEU D CA  1 
ATOM   2599 C  C   . LEU D 2 18  ? 0.441   8.684   45.590  1.00 28.18 ? 33  LEU D C   1 
ATOM   2600 O  O   . LEU D 2 18  ? 1.605   8.402   45.929  1.00 30.50 ? 33  LEU D O   1 
ATOM   2601 C  CB  . LEU D 2 18  ? 0.783   8.861   43.112  1.00 24.11 ? 33  LEU D CB  1 
ATOM   2602 C  CG  . LEU D 2 18  ? 0.335   7.444   42.762  1.00 28.77 ? 33  LEU D CG  1 
ATOM   2603 C  CD1 . LEU D 2 18  ? -1.077  7.462   42.206  1.00 30.82 ? 33  LEU D CD1 1 
ATOM   2604 C  CD2 . LEU D 2 18  ? 1.295   6.785   41.764  1.00 30.64 ? 33  LEU D CD2 1 
ATOM   2605 N  N   . PHE D 2 19  ? -0.652  8.278   46.242  1.00 29.65 ? 34  PHE D N   1 
ATOM   2606 C  CA  . PHE D 2 19  ? -0.663  7.525   47.485  1.00 32.21 ? 34  PHE D CA  1 
ATOM   2607 C  C   . PHE D 2 19  ? -1.216  6.126   47.262  1.00 33.27 ? 34  PHE D C   1 
ATOM   2608 O  O   . PHE D 2 19  ? -2.199  5.940   46.531  1.00 34.57 ? 34  PHE D O   1 
ATOM   2609 C  CB  . PHE D 2 19  ? -1.546  8.210   48.530  1.00 30.90 ? 34  PHE D CB  1 
ATOM   2610 C  CG  . PHE D 2 19  ? -0.906  9.385   49.195  1.00 31.42 ? 34  PHE D CG  1 
ATOM   2611 C  CD1 . PHE D 2 19  ? -0.986  10.641  48.618  1.00 26.87 ? 34  PHE D CD1 1 
ATOM   2612 C  CD2 . PHE D 2 19  ? -0.245  9.240   50.415  1.00 34.97 ? 34  PHE D CD2 1 
ATOM   2613 C  CE1 . PHE D 2 19  ? -0.406  11.727  49.237  1.00 32.74 ? 34  PHE D CE1 1 
ATOM   2614 C  CE2 . PHE D 2 19  ? 0.341   10.329  51.042  1.00 29.77 ? 34  PHE D CE2 1 
ATOM   2615 C  CZ  . PHE D 2 19  ? 0.253   11.577  50.455  1.00 28.22 ? 34  PHE D CZ  1 
ATOM   2616 N  N   . ARG D 2 20  ? -0.592  5.159   47.919  1.00 34.51 ? 35  ARG D N   1 
ATOM   2617 C  CA  . ARG D 2 20  ? -1.247  3.899   48.215  1.00 33.67 ? 35  ARG D CA  1 
ATOM   2618 C  C   . ARG D 2 20  ? -2.304  4.123   49.286  1.00 37.40 ? 35  ARG D C   1 
ATOM   2619 O  O   . ARG D 2 20  ? -2.124  4.945   50.189  1.00 37.67 ? 35  ARG D O   1 
ATOM   2620 C  CB  . ARG D 2 20  ? -0.209  2.886   48.672  1.00 40.57 ? 35  ARG D CB  1 
ATOM   2621 C  CG  . ARG D 2 20  ? -0.736  1.509   48.957  1.00 46.28 ? 35  ARG D CG  1 
ATOM   2622 C  CD  . ARG D 2 20  ? 0.214   0.750   49.869  1.00 47.51 ? 35  ARG D CD  1 
ATOM   2623 N  NE  . ARG D 2 20  ? 0.386   -0.622  49.415  1.00 53.03 ? 35  ARG D NE  1 
ATOM   2624 C  CZ  . ARG D 2 20  ? 1.528   -1.116  48.947  1.00 63.77 ? 35  ARG D CZ  1 
ATOM   2625 N  NH1 . ARG D 2 20  ? 2.629   -0.373  48.868  1.00 55.83 ? 35  ARG D NH1 1 
ATOM   2626 N  NH2 . ARG D 2 20  ? 1.569   -2.385  48.549  1.00 61.30 ? 35  ARG D NH2 1 
ATOM   2627 N  N   . LYS D 2 21  ? -3.436  3.423   49.159  1.00 42.56 ? 36  LYS D N   1 
ATOM   2628 C  CA  . LYS D 2 21  ? -4.539  3.583   50.112  1.00 44.11 ? 36  LYS D CA  1 
ATOM   2629 C  C   . LYS D 2 21  ? -4.246  2.905   51.449  1.00 43.32 ? 36  LYS D C   1 
ATOM   2630 O  O   . LYS D 2 21  ? -4.281  3.545   52.506  1.00 46.78 ? 36  LYS D O   1 
ATOM   2631 C  CB  . LYS D 2 21  ? -5.818  3.006   49.521  1.00 38.44 ? 36  LYS D CB  1 
ATOM   2632 C  CG  . LYS D 2 21  ? -6.756  3.993   48.928  1.00 36.29 ? 36  LYS D CG  1 
ATOM   2633 C  CD  . LYS D 2 21  ? -7.986  3.232   48.549  1.00 35.34 ? 36  LYS D CD  1 
ATOM   2634 C  CE  . LYS D 2 21  ? -8.987  4.074   47.819  1.00 39.27 ? 36  LYS D CE  1 
ATOM   2635 N  NZ  . LYS D 2 21  ? -10.034 3.182   47.262  1.00 43.00 ? 36  LYS D NZ  1 
ATOM   2636 N  N   . SER D 2 22  A -3.947  1.612   51.421  1.00 45.22 ? 36  SER D N   1 
ATOM   2637 C  CA  . SER D 2 22  A -3.771  0.858   52.653  1.00 45.55 ? 36  SER D CA  1 
ATOM   2638 C  C   . SER D 2 22  A -2.560  -0.063  52.559  1.00 49.82 ? 36  SER D C   1 
ATOM   2639 O  O   . SER D 2 22  A -2.574  -1.050  51.812  1.00 55.37 ? 36  SER D O   1 
ATOM   2640 C  CB  . SER D 2 22  A -5.018  0.051   52.989  1.00 51.92 ? 36  SER D CB  1 
ATOM   2641 O  OG  . SER D 2 22  A -5.056  -0.202  54.382  1.00 58.09 ? 36  SER D OG  1 
ATOM   2642 N  N   . PRO D 2 23  ? -1.509  0.208   53.325  1.00 55.43 ? 37  PRO D N   1 
ATOM   2643 C  CA  . PRO D 2 23  ? -1.354  1.385   54.187  1.00 54.53 ? 37  PRO D CA  1 
ATOM   2644 C  C   . PRO D 2 23  ? -1.177  2.682   53.404  1.00 51.53 ? 37  PRO D C   1 
ATOM   2645 O  O   . PRO D 2 23  ? -0.506  2.668   52.377  1.00 49.19 ? 37  PRO D O   1 
ATOM   2646 C  CB  . PRO D 2 23  ? -0.078  1.064   54.989  1.00 52.41 ? 37  PRO D CB  1 
ATOM   2647 C  CG  . PRO D 2 23  ? 0.290   -0.396  54.686  1.00 53.11 ? 37  PRO D CG  1 
ATOM   2648 C  CD  . PRO D 2 23  ? -0.318  -0.660  53.341  1.00 51.61 ? 37  PRO D CD  1 
ATOM   2649 N  N   . GLN D 2 24  ? -1.619  3.801   53.975  1.00 50.23 ? 38  GLN D N   1 
ATOM   2650 C  CA  . GLN D 2 24  ? -1.434  5.117   53.311  1.00 51.78 ? 38  GLN D CA  1 
ATOM   2651 C  C   . GLN D 2 24  ? 0.054   5.491   53.241  1.00 51.69 ? 38  GLN D C   1 
ATOM   2652 O  O   . GLN D 2 24  ? 0.618   5.831   54.297  1.00 58.82 ? 38  GLN D O   1 
ATOM   2653 C  CB  . GLN D 2 24  ? -2.233  6.203   54.029  1.00 51.09 ? 38  GLN D CB  1 
ATOM   2654 C  CG  . GLN D 2 24  ? -3.234  6.919   53.130  1.00 61.07 ? 38  GLN D CG  1 
ATOM   2655 C  CD  . GLN D 2 24  ? -2.824  8.335   52.790  1.00 74.18 ? 38  GLN D CD  1 
ATOM   2656 O  OE1 . GLN D 2 24  ? -1.975  8.939   53.455  1.00 81.07 ? 38  GLN D OE1 1 
ATOM   2657 N  NE2 . GLN D 2 24  ? -3.429  8.882   51.746  1.00 65.75 ? 38  GLN D NE2 1 
ATOM   2658 N  N   . GLU D 2 25  ? 0.661   5.420   52.055  1.00 41.15 ? 39  GLU D N   1 
ATOM   2659 C  CA  . GLU D 2 25  ? 2.027   5.838   51.858  1.00 43.39 ? 39  GLU D CA  1 
ATOM   2660 C  C   . GLU D 2 25  ? 2.156   6.598   50.543  1.00 38.48 ? 39  GLU D C   1 
ATOM   2661 O  O   . GLU D 2 25  ? 1.573   6.212   49.527  1.00 37.79 ? 39  GLU D O   1 
ATOM   2662 C  CB  . GLU D 2 25  ? 2.963   4.629   51.921  1.00 45.45 ? 39  GLU D CB  1 
ATOM   2663 C  CG  . GLU D 2 25  ? 2.945   3.750   50.697  1.00 50.49 ? 39  GLU D CG  1 
ATOM   2664 C  CD  . GLU D 2 25  ? 4.101   2.754   50.662  1.00 58.94 ? 39  GLU D CD  1 
ATOM   2665 O  OE1 . GLU D 2 25  ? 3.977   1.683   51.311  1.00 62.51 ? 39  GLU D OE1 1 
ATOM   2666 O  OE2 . GLU D 2 25  ? 5.105   3.035   49.955  1.00 54.64 ? 39  GLU D OE2 1 
ATOM   2667 N  N   . LEU D 2 26  ? 2.906   7.703   50.586  1.00 36.32 ? 40  LEU D N   1 
ATOM   2668 C  CA  . LEU D 2 26  ? 3.325   8.421   49.388  1.00 34.44 ? 40  LEU D CA  1 
ATOM   2669 C  C   . LEU D 2 26  ? 4.158   7.525   48.478  1.00 32.70 ? 40  LEU D C   1 
ATOM   2670 O  O   . LEU D 2 26  ? 5.260   7.099   48.843  1.00 26.00 ? 40  LEU D O   1 
ATOM   2671 C  CB  . LEU D 2 26  ? 4.113   9.664   49.770  1.00 32.01 ? 40  LEU D CB  1 
ATOM   2672 C  CG  . LEU D 2 26  ? 4.411   10.618  48.629  1.00 26.80 ? 40  LEU D CG  1 
ATOM   2673 C  CD1 . LEU D 2 26  ? 3.121   10.974  47.901  1.00 29.00 ? 40  LEU D CD1 1 
ATOM   2674 C  CD2 . LEU D 2 26  ? 5.068   11.841  49.231  1.00 32.25 ? 40  LEU D CD2 1 
ATOM   2675 N  N   . LEU D 2 27  ? 3.627   7.213   47.300  1.00 31.03 ? 41  LEU D N   1 
ATOM   2676 C  CA  . LEU D 2 27  ? 4.366   6.379   46.370  1.00 29.32 ? 41  LEU D CA  1 
ATOM   2677 C  C   . LEU D 2 27  ? 5.156   7.215   45.377  1.00 32.48 ? 41  LEU D C   1 
ATOM   2678 O  O   . LEU D 2 27  ? 6.316   6.908   45.084  1.00 27.88 ? 41  LEU D O   1 
ATOM   2679 C  CB  . LEU D 2 27  ? 3.412   5.463   45.611  1.00 31.05 ? 41  LEU D CB  1 
ATOM   2680 C  CG  . LEU D 2 27  ? 2.565   4.474   46.392  1.00 37.74 ? 41  LEU D CG  1 
ATOM   2681 C  CD1 . LEU D 2 27  ? 1.571   3.845   45.429  1.00 35.87 ? 41  LEU D CD1 1 
ATOM   2682 C  CD2 . LEU D 2 27  ? 3.452   3.414   47.042  1.00 33.52 ? 41  LEU D CD2 1 
ATOM   2683 N  N   . CYS D 2 28  ? 4.526   8.244   44.814  1.00 34.48 ? 42  CYS D N   1 
ATOM   2684 C  CA  . CYS D 2 28  ? 5.155   8.881   43.667  1.00 28.74 ? 42  CYS D CA  1 
ATOM   2685 C  C   . CYS D 2 28  ? 4.671   10.312  43.525  1.00 33.23 ? 42  CYS D C   1 
ATOM   2686 O  O   . CYS D 2 28  ? 3.695   10.739  44.162  1.00 28.42 ? 42  CYS D O   1 
ATOM   2687 C  CB  . CYS D 2 28  ? 4.856   8.101   42.380  1.00 22.84 ? 42  CYS D CB  1 
ATOM   2688 S  SG  . CYS D 2 28  ? 6.082   6.860   42.069  0.82 29.39 ? 42  CYS D SG  1 
ATOM   2689 N  N   . GLY D 2 29  ? 5.339   11.028  42.611  1.00 26.78 ? 43  GLY D N   1 
ATOM   2690 C  CA  . GLY D 2 29  ? 4.817   12.271  42.101  1.00 26.53 ? 43  GLY D CA  1 
ATOM   2691 C  C   . GLY D 2 29  ? 3.990   12.020  40.864  1.00 26.43 ? 43  GLY D C   1 
ATOM   2692 O  O   . GLY D 2 29  ? 3.869   10.889  40.399  1.00 28.74 ? 43  GLY D O   1 
ATOM   2693 N  N   . ALA D 2 30  ? 3.387   13.097  40.352  1.00 28.94 ? 44  ALA D N   1 
ATOM   2694 C  CA  . ALA D 2 30  ? 2.502   13.048  39.184  1.00 27.46 ? 44  ALA D CA  1 
ATOM   2695 C  C   . ALA D 2 30  ? 2.161   14.487  38.830  1.00 25.45 ? 44  ALA D C   1 
ATOM   2696 O  O   . ALA D 2 30  ? 2.493   15.408  39.579  1.00 28.48 ? 44  ALA D O   1 
ATOM   2697 C  CB  . ALA D 2 30  ? 1.229   12.235  39.455  1.00 22.10 ? 44  ALA D CB  1 
ATOM   2698 N  N   . SER D 2 31  ? 1.483   14.681  37.696  1.00 22.58 ? 45  SER D N   1 
ATOM   2699 C  CA  . SER D 2 31  ? 1.128   16.038  37.283  1.00 25.43 ? 45  SER D CA  1 
ATOM   2700 C  C   . SER D 2 31  ? -0.285  16.108  36.722  1.00 25.75 ? 45  SER D C   1 
ATOM   2701 O  O   . SER D 2 31  ? -0.782  15.165  36.096  1.00 26.43 ? 45  SER D O   1 
ATOM   2702 C  CB  . SER D 2 31  ? 2.116   16.588  36.246  1.00 24.72 ? 45  SER D CB  1 
ATOM   2703 O  OG  . SER D 2 31  ? 1.898   15.974  34.983  1.00 27.99 ? 45  SER D OG  1 
ATOM   2704 N  N   . LEU D 2 32  ? -0.891  17.280  36.884  1.00 26.23 ? 46  LEU D N   1 
ATOM   2705 C  CA  . LEU D 2 32  ? -2.253  17.538  36.427  1.00 26.94 ? 46  LEU D CA  1 
ATOM   2706 C  C   . LEU D 2 32  ? -2.213  18.173  35.037  1.00 30.51 ? 46  LEU D C   1 
ATOM   2707 O  O   . LEU D 2 32  ? -1.569  19.213  34.842  1.00 32.11 ? 46  LEU D O   1 
ATOM   2708 C  CB  . LEU D 2 32  ? -2.965  18.466  37.406  1.00 27.06 ? 46  LEU D CB  1 
ATOM   2709 C  CG  . LEU D 2 32  ? -4.455  18.690  37.180  1.00 30.64 ? 46  LEU D CG  1 
ATOM   2710 C  CD1 . LEU D 2 32  ? -5.223  17.413  37.571  1.00 29.57 ? 46  LEU D CD1 1 
ATOM   2711 C  CD2 . LEU D 2 32  ? -4.938  19.937  37.948  1.00 25.48 ? 46  LEU D CD2 1 
ATOM   2712 N  N   . ILE D 2 33  ? -2.885  17.548  34.073  1.00 28.00 ? 47  ILE D N   1 
ATOM   2713 C  CA  . ILE D 2 33  ? -2.917  18.063  32.702  1.00 27.91 ? 47  ILE D CA  1 
ATOM   2714 C  C   . ILE D 2 33  ? -4.313  18.479  32.255  1.00 32.02 ? 47  ILE D C   1 
ATOM   2715 O  O   . ILE D 2 33  ? -4.444  19.098  31.187  1.00 32.04 ? 47  ILE D O   1 
ATOM   2716 C  CB  . ILE D 2 33  ? -2.311  17.058  31.701  1.00 28.83 ? 47  ILE D CB  1 
ATOM   2717 C  CG1 . ILE D 2 33  ? -3.115  15.749  31.676  1.00 26.63 ? 47  ILE D CG1 1 
ATOM   2718 C  CG2 . ILE D 2 33  ? -0.804  16.857  31.981  1.00 24.02 ? 47  ILE D CG2 1 
ATOM   2719 C  CD1 . ILE D 2 33  ? -2.600  14.728  30.673  1.00 29.58 ? 47  ILE D CD1 1 
ATOM   2720 N  N   . SER D 2 34  ? -5.356  18.146  33.002  1.00 32.24 ? 48  SER D N   1 
ATOM   2721 C  CA  . SER D 2 34  ? -6.692  18.667  32.748  1.00 30.91 ? 48  SER D CA  1 
ATOM   2722 C  C   . SER D 2 34  ? -7.468  18.542  34.049  1.00 32.54 ? 48  SER D C   1 
ATOM   2723 O  O   . SER D 2 34  ? -6.890  18.259  35.104  1.00 35.18 ? 48  SER D O   1 
ATOM   2724 C  CB  . SER D 2 34  ? -7.378  17.928  31.588  1.00 26.16 ? 48  SER D CB  1 
ATOM   2725 O  OG  . SER D 2 34  ? -8.066  16.762  32.020  1.00 28.77 ? 48  SER D OG  1 
ATOM   2726 N  N   . ASP D 2 35  ? -8.779  18.768  33.977  1.00 32.85 ? 49  ASP D N   1 
ATOM   2727 C  CA  . ASP D 2 35  ? -9.637  18.611  35.140  1.00 31.95 ? 49  ASP D CA  1 
ATOM   2728 C  C   . ASP D 2 35  ? -9.743  17.156  35.578  1.00 33.75 ? 49  ASP D C   1 
ATOM   2729 O  O   . ASP D 2 35  ? -10.200 16.898  36.691  1.00 36.29 ? 49  ASP D O   1 
ATOM   2730 C  CB  . ASP D 2 35  ? -11.033 19.186  34.843  1.00 32.45 ? 49  ASP D CB  1 
ATOM   2731 C  CG  . ASP D 2 35  ? -11.881 18.301  33.895  1.00 36.27 ? 49  ASP D CG  1 
ATOM   2732 O  OD1 . ASP D 2 35  ? -11.334 17.501  33.087  1.00 41.37 ? 49  ASP D OD1 1 
ATOM   2733 O  OD2 . ASP D 2 35  ? -13.123 18.426  33.944  1.00 33.27 ? 49  ASP D OD2 1 
ATOM   2734 N  N   . ARG D 2 36  ? -9.360  16.196  34.724  1.00 32.49 ? 50  ARG D N   1 
ATOM   2735 C  CA  . ARG D 2 36  ? -9.580  14.797  35.067  1.00 34.18 ? 50  ARG D CA  1 
ATOM   2736 C  C   . ARG D 2 36  ? -8.442  13.863  34.677  1.00 33.10 ? 50  ARG D C   1 
ATOM   2737 O  O   . ARG D 2 36  ? -8.602  12.646  34.806  1.00 35.09 ? 50  ARG D O   1 
ATOM   2738 C  CB  . ARG D 2 36  ? -10.864 14.307  34.413  1.00 38.48 ? 50  ARG D CB  1 
ATOM   2739 C  CG  . ARG D 2 36  ? -10.760 14.237  32.909  1.00 40.14 ? 50  ARG D CG  1 
ATOM   2740 C  CD  . ARG D 2 36  ? -12.119 14.066  32.304  1.00 41.10 ? 50  ARG D CD  1 
ATOM   2741 N  NE  . ARG D 2 36  ? -12.945 15.249  32.500  1.00 37.59 ? 50  ARG D NE  1 
ATOM   2742 C  CZ  . ARG D 2 36  ? -14.188 15.348  32.053  1.00 40.31 ? 50  ARG D CZ  1 
ATOM   2743 N  NH1 . ARG D 2 36  ? -14.775 14.337  31.416  1.00 33.28 ? 50  ARG D NH1 1 
ATOM   2744 N  NH2 . ARG D 2 36  ? -14.855 16.486  32.240  1.00 33.61 ? 50  ARG D NH2 1 
ATOM   2745 N  N   . TRP D 2 37  ? -7.327  14.366  34.171  1.00 28.40 ? 51  TRP D N   1 
ATOM   2746 C  CA  . TRP D 2 37  ? -6.263  13.496  33.700  1.00 31.06 ? 51  TRP D CA  1 
ATOM   2747 C  C   . TRP D 2 37  ? -4.969  13.848  34.407  1.00 31.53 ? 51  TRP D C   1 
ATOM   2748 O  O   . TRP D 2 37  ? -4.530  15.006  34.390  1.00 28.03 ? 51  TRP D O   1 
ATOM   2749 C  CB  . TRP D 2 37  ? -6.074  13.596  32.183  1.00 31.58 ? 51  TRP D CB  1 
ATOM   2750 C  CG  . TRP D 2 37  ? -7.130  12.837  31.374  1.00 35.89 ? 51  TRP D CG  1 
ATOM   2751 C  CD1 . TRP D 2 37  ? -8.113  13.380  30.593  1.00 32.16 ? 51  TRP D CD1 1 
ATOM   2752 C  CD2 . TRP D 2 37  ? -7.292  11.413  31.282  1.00 35.88 ? 51  TRP D CD2 1 
ATOM   2753 N  NE1 . TRP D 2 37  ? -8.863  12.387  30.019  1.00 36.07 ? 51  TRP D NE1 1 
ATOM   2754 C  CE2 . TRP D 2 37  ? -8.386  11.172  30.430  1.00 34.08 ? 51  TRP D CE2 1 
ATOM   2755 C  CE3 . TRP D 2 37  ? -6.616  10.317  31.839  1.00 35.51 ? 51  TRP D CE3 1 
ATOM   2756 C  CZ2 . TRP D 2 37  ? -8.812  9.890   30.112  1.00 36.88 ? 51  TRP D CZ2 1 
ATOM   2757 C  CZ3 . TRP D 2 37  ? -7.053  9.037   31.530  1.00 30.47 ? 51  TRP D CZ3 1 
ATOM   2758 C  CH2 . TRP D 2 37  ? -8.133  8.838   30.675  1.00 34.78 ? 51  TRP D CH2 1 
ATOM   2759 N  N   . VAL D 2 38  ? -4.336  12.827  34.966  1.00 29.77 ? 52  VAL D N   1 
ATOM   2760 C  CA  . VAL D 2 38  ? -3.114  12.968  35.734  1.00 31.77 ? 52  VAL D CA  1 
ATOM   2761 C  C   . VAL D 2 38  ? -2.064  12.094  35.071  1.00 29.46 ? 52  VAL D C   1 
ATOM   2762 O  O   . VAL D 2 38  ? -2.315  10.917  34.795  1.00 29.13 ? 52  VAL D O   1 
ATOM   2763 C  CB  . VAL D 2 38  ? -3.316  12.542  37.200  1.00 28.79 ? 52  VAL D CB  1 
ATOM   2764 C  CG1 . VAL D 2 38  ? -1.987  12.558  37.934  1.00 24.68 ? 52  VAL D CG1 1 
ATOM   2765 C  CG2 . VAL D 2 38  ? -4.351  13.432  37.892  1.00 28.39 ? 52  VAL D CG2 1 
ATOM   2766 N  N   . LEU D 2 39  ? -0.887  12.659  34.849  1.00 29.96 ? 53  LEU D N   1 
ATOM   2767 C  CA  . LEU D 2 39  ? 0.224   11.963  34.223  1.00 28.41 ? 53  LEU D CA  1 
ATOM   2768 C  C   . LEU D 2 39  ? 1.146   11.433  35.310  1.00 28.08 ? 53  LEU D C   1 
ATOM   2769 O  O   . LEU D 2 39  ? 1.335   12.084  36.340  1.00 26.85 ? 53  LEU D O   1 
ATOM   2770 C  CB  . LEU D 2 39  ? 0.984   12.933  33.313  1.00 25.99 ? 53  LEU D CB  1 
ATOM   2771 C  CG  . LEU D 2 39  ? 1.627   12.540  31.981  1.00 33.41 ? 53  LEU D CG  1 
ATOM   2772 C  CD1 . LEU D 2 39  ? 0.726   11.688  31.127  1.00 35.83 ? 53  LEU D CD1 1 
ATOM   2773 C  CD2 . LEU D 2 39  ? 2.023   13.772  31.206  1.00 31.60 ? 53  LEU D CD2 1 
ATOM   2774 N  N   . THR D 2 40  ? 1.737   10.260  35.078  1.00 30.66 ? 54  THR D N   1 
ATOM   2775 C  CA  . THR D 2 40  ? 2.750   9.756   36.009  1.00 27.87 ? 54  THR D CA  1 
ATOM   2776 C  C   . THR D 2 40  ? 3.583   8.689   35.302  1.00 27.99 ? 54  THR D C   1 
ATOM   2777 O  O   . THR D 2 40  ? 3.350   8.354   34.139  1.00 29.09 ? 54  THR D O   1 
ATOM   2778 C  CB  . THR D 2 40  ? 2.120   9.207   37.298  1.00 27.57 ? 54  THR D CB  1 
ATOM   2779 O  OG1 . THR D 2 40  ? 3.155   8.898   38.242  1.00 22.83 ? 54  THR D OG1 1 
ATOM   2780 C  CG2 . THR D 2 40  ? 1.322   7.955   37.017  1.00 26.16 ? 54  THR D CG2 1 
ATOM   2781 N  N   . ALA D 2 41  ? 4.551   8.141   36.019  1.00 24.74 ? 55  ALA D N   1 
ATOM   2782 C  CA  . ALA D 2 41  ? 5.422   7.131   35.448  1.00 27.11 ? 55  ALA D CA  1 
ATOM   2783 C  C   . ALA D 2 41  ? 4.778   5.772   35.620  1.00 32.70 ? 55  ALA D C   1 
ATOM   2784 O  O   . ALA D 2 41  ? 4.158   5.487   36.651  1.00 31.38 ? 55  ALA D O   1 
ATOM   2785 C  CB  . ALA D 2 41  ? 6.805   7.123   36.112  1.00 25.73 ? 55  ALA D CB  1 
ATOM   2786 N  N   . ALA D 2 42  ? 4.953   4.928   34.609  1.00 30.78 ? 56  ALA D N   1 
ATOM   2787 C  CA  . ALA D 2 42  ? 4.330   3.618   34.636  1.00 30.41 ? 56  ALA D CA  1 
ATOM   2788 C  C   . ALA D 2 42  ? 4.873   2.767   35.788  1.00 28.51 ? 56  ALA D C   1 
ATOM   2789 O  O   . ALA D 2 42  ? 4.118   2.019   36.424  1.00 28.86 ? 56  ALA D O   1 
ATOM   2790 C  CB  . ALA D 2 42  ? 4.531   2.932   33.275  1.00 28.32 ? 56  ALA D CB  1 
ATOM   2791 N  N   . HIS D 2 43  ? 6.176   2.860   36.079  1.00 27.13 ? 57  HIS D N   1 
ATOM   2792 C  CA  . HIS D 2 43  ? 6.722   1.961   37.099  1.00 29.72 ? 57  HIS D CA  1 
ATOM   2793 C  C   . HIS D 2 43  ? 6.219   2.284   38.498  1.00 28.20 ? 57  HIS D C   1 
ATOM   2794 O  O   . HIS D 2 43  ? 6.364   1.452   39.388  1.00 27.29 ? 57  HIS D O   1 
ATOM   2795 C  CB  . HIS D 2 43  ? 8.250   1.960   37.077  1.00 23.98 ? 57  HIS D CB  1 
ATOM   2796 C  CG  . HIS D 2 43  ? 8.882   3.070   37.862  1.00 29.57 ? 57  HIS D CG  1 
ATOM   2797 N  ND1 . HIS D 2 43  ? 9.438   4.179   37.264  1.00 31.24 ? 57  HIS D ND1 1 
ATOM   2798 C  CD2 . HIS D 2 43  ? 9.089   3.221   39.194  1.00 32.39 ? 57  HIS D CD2 1 
ATOM   2799 C  CE1 . HIS D 2 43  ? 9.939   4.976   38.194  1.00 34.30 ? 57  HIS D CE1 1 
ATOM   2800 N  NE2 . HIS D 2 43  ? 9.730   4.420   39.374  1.00 31.88 ? 57  HIS D NE2 1 
ATOM   2801 N  N   . CYS D 2 44  ? 5.663   3.477   38.717  1.00 26.89 ? 58  CYS D N   1 
ATOM   2802 C  CA  . CYS D 2 44  ? 5.012   3.779   39.991  1.00 31.24 ? 58  CYS D CA  1 
ATOM   2803 C  C   . CYS D 2 44  ? 3.805   2.881   40.237  1.00 34.12 ? 58  CYS D C   1 
ATOM   2804 O  O   . CYS D 2 44  ? 3.433   2.627   41.391  1.00 29.65 ? 58  CYS D O   1 
ATOM   2805 C  CB  . CYS D 2 44  ? 4.581   5.245   40.020  1.00 30.54 ? 58  CYS D CB  1 
ATOM   2806 S  SG  . CYS D 2 44  ? 5.962   6.407   40.088  1.00 33.89 ? 58  CYS D SG  1 
ATOM   2807 N  N   . LEU D 2 45  ? 3.175   2.411   39.169  1.00 31.38 ? 59  LEU D N   1 
ATOM   2808 C  CA  . LEU D 2 45  ? 1.988   1.588   39.257  1.00 31.41 ? 59  LEU D CA  1 
ATOM   2809 C  C   . LEU D 2 45  ? 2.274   0.116   39.046  1.00 32.91 ? 59  LEU D C   1 
ATOM   2810 O  O   . LEU D 2 45  ? 1.680   -0.733  39.720  1.00 33.34 ? 59  LEU D O   1 
ATOM   2811 C  CB  . LEU D 2 45  ? 0.975   2.035   38.210  1.00 34.86 ? 59  LEU D CB  1 
ATOM   2812 C  CG  . LEU D 2 45  ? 0.640   3.512   38.121  1.00 37.98 ? 59  LEU D CG  1 
ATOM   2813 C  CD1 . LEU D 2 45  ? -0.225  3.699   36.893  1.00 36.85 ? 59  LEU D CD1 1 
ATOM   2814 C  CD2 . LEU D 2 45  ? -0.105  3.910   39.372  1.00 37.50 ? 59  LEU D CD2 1 
ATOM   2815 N  N   . LEU D 2 46  ? 3.156   -0.203  38.107  1.00 31.71 ? 60  LEU D N   1 
ATOM   2816 C  CA  . LEU D 2 46  ? 3.363   -1.581  37.679  1.00 29.29 ? 60  LEU D CA  1 
ATOM   2817 C  C   . LEU D 2 46  ? 4.860   -1.816  37.535  1.00 32.92 ? 60  LEU D C   1 
ATOM   2818 O  O   . LEU D 2 46  ? 5.492   -1.320  36.595  1.00 30.79 ? 60  LEU D O   1 
ATOM   2819 C  CB  . LEU D 2 46  ? 2.629   -1.854  36.369  1.00 23.14 ? 60  LEU D CB  1 
ATOM   2820 C  CG  . LEU D 2 46  ? 2.909   -3.208  35.715  1.00 31.61 ? 60  LEU D CG  1 
ATOM   2821 C  CD1 . LEU D 2 46  ? 2.344   -4.391  36.551  1.00 26.05 ? 60  LEU D CD1 1 
ATOM   2822 C  CD2 . LEU D 2 46  ? 2.376   -3.222  34.277  1.00 26.64 ? 60  LEU D CD2 1 
ATOM   2823 N  N   . TYR D 2 47  A 5.432   -2.575  38.460  1.00 30.83 ? 60  TYR D N   1 
ATOM   2824 C  CA  . TYR D 2 47  A 6.825   -2.982  38.343  1.00 33.27 ? 60  TYR D CA  1 
ATOM   2825 C  C   . TYR D 2 47  A 6.962   -4.395  38.892  1.00 36.60 ? 60  TYR D C   1 
ATOM   2826 O  O   . TYR D 2 47  A 7.242   -4.595  40.085  1.00 32.29 ? 60  TYR D O   1 
ATOM   2827 C  CB  . TYR D 2 47  A 7.762   -2.004  39.052  1.00 30.96 ? 60  TYR D CB  1 
ATOM   2828 C  CG  . TYR D 2 47  A 9.195   -2.176  38.618  1.00 26.76 ? 60  TYR D CG  1 
ATOM   2829 C  CD1 . TYR D 2 47  A 9.548   -2.052  37.283  1.00 29.11 ? 60  TYR D CD1 1 
ATOM   2830 C  CD2 . TYR D 2 47  A 10.182  -2.492  39.535  1.00 27.60 ? 60  TYR D CD2 1 
ATOM   2831 C  CE1 . TYR D 2 47  A 10.850  -2.221  36.869  1.00 26.80 ? 60  TYR D CE1 1 
ATOM   2832 C  CE2 . TYR D 2 47  A 11.484  -2.658  39.140  1.00 29.29 ? 60  TYR D CE2 1 
ATOM   2833 C  CZ  . TYR D 2 47  A 11.817  -2.525  37.800  1.00 31.01 ? 60  TYR D CZ  1 
ATOM   2834 O  OH  . TYR D 2 47  A 13.124  -2.698  37.393  1.00 32.65 ? 60  TYR D OH  1 
ATOM   2835 N  N   . PRO D 2 48  B 6.785   -5.403  38.030  1.00 35.48 ? 60  PRO D N   1 
ATOM   2836 C  CA  . PRO D 2 48  B 6.848   -6.810  38.452  1.00 27.87 ? 60  PRO D CA  1 
ATOM   2837 C  C   . PRO D 2 48  B 8.149   -7.158  39.158  1.00 32.52 ? 60  PRO D C   1 
ATOM   2838 O  O   . PRO D 2 48  B 8.119   -7.889  40.160  1.00 28.63 ? 60  PRO D O   1 
ATOM   2839 C  CB  . PRO D 2 48  B 6.701   -7.572  37.132  1.00 33.60 ? 60  PRO D CB  1 
ATOM   2840 C  CG  . PRO D 2 48  B 5.856   -6.671  36.295  1.00 34.70 ? 60  PRO D CG  1 
ATOM   2841 C  CD  . PRO D 2 48  B 6.298   -5.265  36.642  1.00 33.63 ? 60  PRO D CD  1 
ATOM   2842 N  N   . PRO D 2 49  C 9.334   -6.684  38.681  1.00 33.28 ? 60  PRO D N   1 
ATOM   2843 C  CA  . PRO D 2 49  C 10.565  -7.068  39.395  1.00 28.42 ? 60  PRO D CA  1 
ATOM   2844 C  C   . PRO D 2 49  C 10.518  -6.751  40.890  1.00 31.14 ? 60  PRO D C   1 
ATOM   2845 O  O   . PRO D 2 49  C 11.260  -7.351  41.667  1.00 39.38 ? 60  PRO D O   1 
ATOM   2846 C  CB  . PRO D 2 49  C 11.660  -6.270  38.676  1.00 29.12 ? 60  PRO D CB  1 
ATOM   2847 C  CG  . PRO D 2 49  C 11.110  -5.976  37.336  1.00 28.37 ? 60  PRO D CG  1 
ATOM   2848 C  CD  . PRO D 2 49  C 9.638   -5.837  37.508  1.00 28.47 ? 60  PRO D CD  1 
ATOM   2849 N  N   . TRP D 2 50  D 9.675   -5.811  41.313  1.00 32.85 ? 60  TRP D N   1 
ATOM   2850 C  CA  . TRP D 2 50  D 9.490   -5.489  42.728  1.00 36.08 ? 60  TRP D CA  1 
ATOM   2851 C  C   . TRP D 2 50  D 8.134   -5.934  43.283  1.00 39.01 ? 60  TRP D C   1 
ATOM   2852 O  O   . TRP D 2 50  D 7.744   -5.479  44.363  1.00 40.14 ? 60  TRP D O   1 
ATOM   2853 C  CB  . TRP D 2 50  D 9.664   -3.989  42.958  1.00 31.78 ? 60  TRP D CB  1 
ATOM   2854 C  CG  . TRP D 2 50  D 11.072  -3.493  42.757  1.00 35.05 ? 60  TRP D CG  1 
ATOM   2855 C  CD1 . TRP D 2 50  D 12.183  -4.246  42.520  1.00 33.39 ? 60  TRP D CD1 1 
ATOM   2856 C  CD2 . TRP D 2 50  D 11.516  -2.126  42.785  1.00 36.61 ? 60  TRP D CD2 1 
ATOM   2857 N  NE1 . TRP D 2 50  D 13.288  -3.442  42.406  1.00 32.66 ? 60  TRP D NE1 1 
ATOM   2858 C  CE2 . TRP D 2 50  D 12.906  -2.135  42.556  1.00 36.88 ? 60  TRP D CE2 1 
ATOM   2859 C  CE3 . TRP D 2 50  D 10.873  -0.898  42.990  1.00 29.68 ? 60  TRP D CE3 1 
ATOM   2860 C  CZ2 . TRP D 2 50  D 13.665  -0.962  42.524  1.00 34.94 ? 60  TRP D CZ2 1 
ATOM   2861 C  CZ3 . TRP D 2 50  D 11.629  0.265   42.955  1.00 34.42 ? 60  TRP D CZ3 1 
ATOM   2862 C  CH2 . TRP D 2 50  D 13.008  0.221   42.729  1.00 34.11 ? 60  TRP D CH2 1 
ATOM   2863 N  N   . ASP D 2 51  E 7.375   -6.746  42.544  1.00 35.33 ? 60  ASP D N   1 
ATOM   2864 C  CA  . ASP D 2 51  E 6.056   -7.214  42.988  1.00 39.95 ? 60  ASP D CA  1 
ATOM   2865 C  C   . ASP D 2 51  E 5.052   -6.060  43.142  1.00 37.03 ? 60  ASP D C   1 
ATOM   2866 O  O   . ASP D 2 51  E 4.255   -6.025  44.078  1.00 39.44 ? 60  ASP D O   1 
ATOM   2867 C  CB  . ASP D 2 51  E 6.180   -8.027  44.291  1.00 42.56 ? 60  ASP D CB  1 
ATOM   2868 C  CG  . ASP D 2 51  E 5.017   -9.005  44.499  1.00 44.06 ? 60  ASP D CG  1 
ATOM   2869 O  OD1 . ASP D 2 51  E 4.181   -9.139  43.583  1.00 47.98 ? 60  ASP D OD1 1 
ATOM   2870 O  OD2 . ASP D 2 51  E 4.949   -9.655  45.572  1.00 49.90 ? 60  ASP D OD2 1 
ATOM   2871 N  N   . LYS D 2 52  F 5.058   -5.121  42.203  1.00 40.52 ? 60  LYS D N   1 
ATOM   2872 C  CA  . LYS D 2 52  F 4.114   -4.001  42.202  1.00 40.99 ? 60  LYS D CA  1 
ATOM   2873 C  C   . LYS D 2 52  F 3.160   -4.133  41.020  1.00 35.08 ? 60  LYS D C   1 
ATOM   2874 O  O   . LYS D 2 52  F 3.597   -4.215  39.865  1.00 35.92 ? 60  LYS D O   1 
ATOM   2875 C  CB  . LYS D 2 52  F 4.840   -2.656  42.162  1.00 35.91 ? 60  LYS D CB  1 
ATOM   2876 C  CG  . LYS D 2 52  F 5.775   -2.479  43.333  1.00 42.62 ? 60  LYS D CG  1 
ATOM   2877 C  CD  . LYS D 2 52  F 5.026   -1.902  44.523  1.00 48.54 ? 60  LYS D CD  1 
ATOM   2878 C  CE  . LYS D 2 52  F 5.315   -2.685  45.803  1.00 50.65 ? 60  LYS D CE  1 
ATOM   2879 N  NZ  . LYS D 2 52  F 6.769   -2.897  45.994  1.00 44.85 ? 60  LYS D NZ  1 
ATOM   2880 N  N   . ASN D 2 53  G 1.861   -4.180  41.319  1.00 32.13 ? 60  ASN D N   1 
ATOM   2881 C  CA  . ASN D 2 53  G 0.785   -4.168  40.316  1.00 37.76 ? 60  ASN D CA  1 
ATOM   2882 C  C   . ASN D 2 53  G -0.430  -3.520  40.992  1.00 35.66 ? 60  ASN D C   1 
ATOM   2883 O  O   . ASN D 2 53  G -1.361  -4.193  41.421  1.00 36.16 ? 60  ASN D O   1 
ATOM   2884 C  CB  . ASN D 2 53  G 0.458   -5.560  39.767  1.00 33.34 ? 60  ASN D CB  1 
ATOM   2885 C  CG  . ASN D 2 53  G -0.477  -5.516  38.574  1.00 34.53 ? 60  ASN D CG  1 
ATOM   2886 O  OD1 . ASN D 2 53  G -1.055  -4.475  38.290  1.00 40.51 ? 60  ASN D OD1 1 
ATOM   2887 N  ND2 . ASN D 2 53  G -0.643  -6.651  37.875  1.00 39.85 ? 60  ASN D ND2 1 
ATOM   2888 N  N   . PHE D 2 54  H -0.375  -2.190  41.122  1.00 39.96 ? 60  PHE D N   1 
ATOM   2889 C  CA  . PHE D 2 54  H -1.474  -1.391  41.654  1.00 41.75 ? 60  PHE D CA  1 
ATOM   2890 C  C   . PHE D 2 54  H -2.506  -1.144  40.561  1.00 46.22 ? 60  PHE D C   1 
ATOM   2891 O  O   . PHE D 2 54  H -2.160  -0.966  39.388  1.00 50.43 ? 60  PHE D O   1 
ATOM   2892 C  CB  . PHE D 2 54  H -0.977  -0.034  42.174  1.00 33.31 ? 60  PHE D CB  1 
ATOM   2893 C  CG  . PHE D 2 54  H 0.005   -0.128  43.312  1.00 36.15 ? 60  PHE D CG  1 
ATOM   2894 C  CD1 . PHE D 2 54  H -0.392  -0.594  44.564  1.00 36.17 ? 60  PHE D CD1 1 
ATOM   2895 C  CD2 . PHE D 2 54  H 1.332   0.263   43.135  1.00 37.96 ? 60  PHE D CD2 1 
ATOM   2896 C  CE1 . PHE D 2 54  H 0.519   -0.686  45.624  1.00 42.57 ? 60  PHE D CE1 1 
ATOM   2897 C  CE2 . PHE D 2 54  H 2.258   0.179   44.192  1.00 41.30 ? 60  PHE D CE2 1 
ATOM   2898 C  CZ  . PHE D 2 54  H 1.850   -0.293  45.438  1.00 43.71 ? 60  PHE D CZ  1 
ATOM   2899 N  N   . THR D 2 55  I -3.779  -1.112  40.950  1.00 43.32 ? 60  THR D N   1 
ATOM   2900 C  CA  . THR D 2 55  I -4.828  -0.662  40.040  1.00 44.85 ? 60  THR D CA  1 
ATOM   2901 C  C   . THR D 2 55  I -5.551  0.540   40.641  1.00 46.42 ? 60  THR D C   1 
ATOM   2902 O  O   . THR D 2 55  I -5.202  1.023   41.724  1.00 42.19 ? 60  THR D O   1 
ATOM   2903 C  CB  . THR D 2 55  I -5.820  -1.785  39.724  1.00 46.95 ? 60  THR D CB  1 
ATOM   2904 O  OG1 . THR D 2 55  I -6.497  -2.186  40.927  1.00 45.53 ? 60  THR D OG1 1 
ATOM   2905 C  CG2 . THR D 2 55  I -5.082  -2.974  39.104  1.00 44.93 ? 60  THR D CG2 1 
ATOM   2906 N  N   . GLU D 2 56  ? -6.593  0.991   39.926  1.00 47.83 ? 61  GLU D N   1 
ATOM   2907 C  CA  . GLU D 2 56  ? -7.321  2.197   40.315  1.00 45.72 ? 61  GLU D CA  1 
ATOM   2908 C  C   . GLU D 2 56  ? -7.782  2.142   41.768  1.00 41.80 ? 61  GLU D C   1 
ATOM   2909 O  O   . GLU D 2 56  ? -7.705  3.140   42.493  1.00 41.25 ? 61  GLU D O   1 
ATOM   2910 C  CB  . GLU D 2 56  ? -8.515  2.430   39.377  1.00 43.57 ? 61  GLU D CB  1 
ATOM   2911 C  CG  . GLU D 2 56  ? -9.370  1.210   39.085  1.00 40.98 ? 61  GLU D CG  1 
ATOM   2912 C  CD  . GLU D 2 56  ? -8.830  0.396   37.936  1.00 46.25 ? 61  GLU D CD  1 
ATOM   2913 O  OE1 . GLU D 2 56  ? -7.786  0.789   37.384  1.00 44.46 ? 61  GLU D OE1 1 
ATOM   2914 O  OE2 . GLU D 2 56  ? -9.454  -0.625  37.567  1.00 55.57 ? 61  GLU D OE2 1 
ATOM   2915 N  N   . ASN D 2 57  ? -8.263  0.992   42.218  1.00 43.91 ? 62  ASN D N   1 
ATOM   2916 C  CA  . ASN D 2 57  ? -8.858  0.962   43.546  1.00 45.59 ? 62  ASN D CA  1 
ATOM   2917 C  C   . ASN D 2 57  ? -7.839  0.956   44.680  1.00 41.83 ? 62  ASN D C   1 
ATOM   2918 O  O   . ASN D 2 57  ? -8.219  1.233   45.821  1.00 43.38 ? 62  ASN D O   1 
ATOM   2919 C  CB  . ASN D 2 57  ? -9.820  -0.210  43.636  1.00 50.77 ? 62  ASN D CB  1 
ATOM   2920 C  CG  . ASN D 2 57  ? -11.172 0.125   43.000  1.00 63.58 ? 62  ASN D CG  1 
ATOM   2921 O  OD1 . ASN D 2 57  ? -11.538 1.309   42.857  1.00 54.34 ? 62  ASN D OD1 1 
ATOM   2922 N  ND2 . ASN D 2 57  ? -11.909 -0.906  42.597  1.00 70.71 ? 62  ASN D ND2 1 
ATOM   2923 N  N   . ASP D 2 58  ? -6.558  0.741   44.391  1.00 44.42 ? 63  ASP D N   1 
ATOM   2924 C  CA  . ASP D 2 58  ? -5.511  0.698   45.407  1.00 36.36 ? 63  ASP D CA  1 
ATOM   2925 C  C   . ASP D 2 58  ? -4.915  2.062   45.722  1.00 38.46 ? 63  ASP D C   1 
ATOM   2926 O  O   . ASP D 2 58  ? -4.054  2.157   46.603  1.00 38.73 ? 63  ASP D O   1 
ATOM   2927 C  CB  . ASP D 2 58  ? -4.375  -0.227  44.963  1.00 38.33 ? 63  ASP D CB  1 
ATOM   2928 C  CG  . ASP D 2 58  ? -4.853  -1.621  44.634  1.00 42.54 ? 63  ASP D CG  1 
ATOM   2929 O  OD1 . ASP D 2 58  ? -5.621  -2.176  45.441  1.00 42.09 ? 63  ASP D OD1 1 
ATOM   2930 O  OD2 . ASP D 2 58  ? -4.468  -2.155  43.567  1.00 45.65 ? 63  ASP D OD2 1 
ATOM   2931 N  N   . LEU D 2 59  ? -5.347  3.120   45.041  1.00 41.99 ? 64  LEU D N   1 
ATOM   2932 C  CA  . LEU D 2 59  ? -4.621  4.381   45.037  1.00 33.48 ? 64  LEU D CA  1 
ATOM   2933 C  C   . LEU D 2 59  ? -5.552  5.561   45.268  1.00 33.88 ? 64  LEU D C   1 
ATOM   2934 O  O   . LEU D 2 59  ? -6.770  5.473   45.090  1.00 34.22 ? 64  LEU D O   1 
ATOM   2935 C  CB  . LEU D 2 59  ? -3.901  4.571   43.703  1.00 36.09 ? 64  LEU D CB  1 
ATOM   2936 C  CG  . LEU D 2 59  ? -2.989  3.427   43.273  1.00 34.14 ? 64  LEU D CG  1 
ATOM   2937 C  CD1 . LEU D 2 59  ? -2.791  3.448   41.787  1.00 33.74 ? 64  LEU D CD1 1 
ATOM   2938 C  CD2 . LEU D 2 59  ? -1.681  3.603   43.968  1.00 31.08 ? 64  LEU D CD2 1 
ATOM   2939 N  N   . LEU D 2 60  ? -4.952  6.664   45.698  1.00 31.43 ? 65  LEU D N   1 
ATOM   2940 C  CA  . LEU D 2 60  ? -5.602  7.963   45.639  1.00 31.86 ? 65  LEU D CA  1 
ATOM   2941 C  C   . LEU D 2 60  ? -4.541  9.013   45.338  1.00 29.76 ? 65  LEU D C   1 
ATOM   2942 O  O   . LEU D 2 60  ? -3.342  8.777   45.500  1.00 29.39 ? 65  LEU D O   1 
ATOM   2943 C  CB  . LEU D 2 60  ? -6.353  8.291   46.932  1.00 29.29 ? 65  LEU D CB  1 
ATOM   2944 C  CG  . LEU D 2 60  ? -5.541  8.263   48.225  1.00 35.34 ? 65  LEU D CG  1 
ATOM   2945 C  CD1 . LEU D 2 60  ? -4.855  9.599   48.527  1.00 29.10 ? 65  LEU D CD1 1 
ATOM   2946 C  CD2 . LEU D 2 60  ? -6.433  7.825   49.397  1.00 34.44 ? 65  LEU D CD2 1 
ATOM   2947 N  N   . VAL D 2 61  ? -4.988  10.190  44.913  1.00 29.06 ? 66  VAL D N   1 
ATOM   2948 C  CA  . VAL D 2 61  ? -4.071  11.286  44.622  1.00 30.42 ? 66  VAL D CA  1 
ATOM   2949 C  C   . VAL D 2 61  ? -4.475  12.493  45.449  1.00 29.42 ? 66  VAL D C   1 
ATOM   2950 O  O   . VAL D 2 61  ? -5.633  12.639  45.850  1.00 30.78 ? 66  VAL D O   1 
ATOM   2951 C  CB  . VAL D 2 61  ? -4.043  11.662  43.126  1.00 26.21 ? 66  VAL D CB  1 
ATOM   2952 C  CG1 . VAL D 2 61  ? -3.764  10.442  42.281  1.00 28.03 ? 66  VAL D CG1 1 
ATOM   2953 C  CG2 . VAL D 2 61  ? -5.333  12.303  42.739  1.00 26.08 ? 66  VAL D CG2 1 
ATOM   2954 N  N   . ARG D 2 62  ? -3.502  13.356  45.709  1.00 30.86 ? 67  ARG D N   1 
ATOM   2955 C  CA  . ARG D 2 62  ? -3.762  14.637  46.360  1.00 31.55 ? 67  ARG D CA  1 
ATOM   2956 C  C   . ARG D 2 62  ? -3.197  15.757  45.507  1.00 31.95 ? 67  ARG D C   1 
ATOM   2957 O  O   . ARG D 2 62  ? -2.047  15.682  45.045  1.00 28.47 ? 67  ARG D O   1 
ATOM   2958 C  CB  . ARG D 2 62  ? -3.153  14.705  47.748  1.00 30.96 ? 67  ARG D CB  1 
ATOM   2959 C  CG  . ARG D 2 62  ? -3.704  13.697  48.693  1.00 36.22 ? 67  ARG D CG  1 
ATOM   2960 C  CD  . ARG D 2 62  ? -2.972  13.805  50.006  1.00 35.71 ? 67  ARG D CD  1 
ATOM   2961 N  NE  . ARG D 2 62  ? -3.370  12.740  50.911  1.00 38.27 ? 67  ARG D NE  1 
ATOM   2962 C  CZ  . ARG D 2 62  ? -4.307  12.885  51.836  1.00 43.78 ? 67  ARG D CZ  1 
ATOM   2963 N  NH1 . ARG D 2 62  ? -4.938  14.042  52.002  1.00 39.49 ? 67  ARG D NH1 1 
ATOM   2964 N  NH2 . ARG D 2 62  ? -4.620  11.848  52.607  1.00 40.38 ? 67  ARG D NH2 1 
ATOM   2965 N  N   . ILE D 2 63  ? -3.993  16.809  45.341  1.00 31.20 ? 68  ILE D N   1 
ATOM   2966 C  CA  . ILE D 2 63  ? -3.685  17.886  44.414  1.00 31.80 ? 68  ILE D CA  1 
ATOM   2967 C  C   . ILE D 2 63  ? -3.686  19.211  45.168  1.00 35.38 ? 68  ILE D C   1 
ATOM   2968 O  O   . ILE D 2 63  ? -4.564  19.463  46.007  1.00 35.12 ? 68  ILE D O   1 
ATOM   2969 C  CB  . ILE D 2 63  ? -4.688  17.896  43.247  1.00 32.37 ? 68  ILE D CB  1 
ATOM   2970 C  CG1 . ILE D 2 63  ? -4.785  16.486  42.646  1.00 34.47 ? 68  ILE D CG1 1 
ATOM   2971 C  CG2 . ILE D 2 63  ? -4.255  18.903  42.208  1.00 31.98 ? 68  ILE D CG2 1 
ATOM   2972 C  CD1 . ILE D 2 63  ? -5.848  16.307  41.565  1.00 30.90 ? 68  ILE D CD1 1 
ATOM   2973 N  N   . GLY D 2 64  ? -2.696  20.054  44.859  1.00 32.64 ? 69  GLY D N   1 
ATOM   2974 C  CA  . GLY D 2 64  ? -2.614  21.401  45.386  1.00 33.55 ? 69  GLY D CA  1 
ATOM   2975 C  C   . GLY D 2 64  ? -1.791  21.539  46.649  1.00 31.04 ? 69  GLY D C   1 
ATOM   2976 O  O   . GLY D 2 64  ? -1.888  22.562  47.334  1.00 32.07 ? 69  GLY D O   1 
ATOM   2977 N  N   . LYS D 2 65  ? -0.971  20.553  46.970  1.00 33.86 ? 70  LYS D N   1 
ATOM   2978 C  CA  . LYS D 2 65  ? -0.297  20.513  48.253  1.00 35.64 ? 70  LYS D CA  1 
ATOM   2979 C  C   . LYS D 2 65  ? 1.062   21.194  48.221  1.00 36.95 ? 70  LYS D C   1 
ATOM   2980 O  O   . LYS D 2 65  ? 1.730   21.282  47.185  1.00 37.01 ? 70  LYS D O   1 
ATOM   2981 C  CB  . LYS D 2 65  ? -0.138  19.070  48.720  1.00 39.25 ? 70  LYS D CB  1 
ATOM   2982 C  CG  . LYS D 2 65  ? -1.388  18.506  49.347  1.00 36.37 ? 70  LYS D CG  1 
ATOM   2983 C  CD  . LYS D 2 65  ? -1.100  17.250  50.140  1.00 33.35 ? 70  LYS D CD  1 
ATOM   2984 C  CE  . LYS D 2 65  ? -0.179  17.555  51.280  1.00 36.49 ? 70  LYS D CE  1 
ATOM   2985 N  NZ  . LYS D 2 65  ? -0.698  18.693  52.087  1.00 40.38 ? 70  LYS D NZ  1 
ATOM   2986 N  N   . HIS D 2 66  ? 1.473   21.656  49.399  1.00 39.71 ? 71  HIS D N   1 
ATOM   2987 C  CA  . HIS D 2 66  ? 2.785   22.252  49.603  1.00 40.58 ? 71  HIS D CA  1 
ATOM   2988 C  C   . HIS D 2 66  ? 3.587   21.462  50.627  1.00 45.92 ? 71  HIS D C   1 
ATOM   2989 O  O   . HIS D 2 66  ? 4.676   20.959  50.300  1.00 42.83 ? 71  HIS D O   1 
ATOM   2990 C  CB  . HIS D 2 66  ? 2.632   23.721  50.035  1.00 38.33 ? 71  HIS D CB  1 
ATOM   2991 C  CG  . HIS D 2 66  ? 3.921   24.479  50.047  1.00 39.21 ? 71  HIS D CG  1 
ATOM   2992 N  ND1 . HIS D 2 66  ? 4.537   24.883  51.212  1.00 39.41 ? 71  HIS D ND1 1 
ATOM   2993 C  CD2 . HIS D 2 66  ? 4.712   24.906  49.035  1.00 38.53 ? 71  HIS D CD2 1 
ATOM   2994 C  CE1 . HIS D 2 66  ? 5.660   25.512  50.916  1.00 38.50 ? 71  HIS D CE1 1 
ATOM   2995 N  NE2 . HIS D 2 66  ? 5.791   25.537  49.601  1.00 35.83 ? 71  HIS D NE2 1 
ATOM   2996 N  N   . SER D 2 67  ? 3.079   21.331  51.858  1.00 43.42 ? 72  SER D N   1 
ATOM   2997 C  CA  . SER D 2 67  ? 3.756   20.543  52.877  1.00 44.01 ? 72  SER D CA  1 
ATOM   2998 C  C   . SER D 2 67  ? 3.393   19.076  52.737  1.00 41.53 ? 72  SER D C   1 
ATOM   2999 O  O   . SER D 2 67  ? 2.213   18.735  52.678  1.00 44.38 ? 72  SER D O   1 
ATOM   3000 C  CB  . SER D 2 67  ? 3.386   21.031  54.269  1.00 47.03 ? 72  SER D CB  1 
ATOM   3001 O  OG  . SER D 2 67  ? 3.655   20.026  55.228  1.00 54.44 ? 72  SER D OG  1 
ATOM   3002 N  N   . ARG D 2 68  ? 4.410   18.206  52.751  1.00 47.08 ? 73  ARG D N   1 
ATOM   3003 C  CA  . ARG D 2 68  ? 4.174   16.769  52.625  1.00 44.05 ? 73  ARG D CA  1 
ATOM   3004 C  C   . ARG D 2 68  ? 3.249   16.259  53.713  1.00 42.02 ? 73  ARG D C   1 
ATOM   3005 O  O   . ARG D 2 68  ? 2.389   15.407  53.466  1.00 45.38 ? 73  ARG D O   1 
ATOM   3006 C  CB  . ARG D 2 68  ? 5.489   15.998  52.684  1.00 43.48 ? 73  ARG D CB  1 
ATOM   3007 C  CG  . ARG D 2 68  ? 5.278   14.479  52.730  1.00 45.36 ? 73  ARG D CG  1 
ATOM   3008 C  CD  . ARG D 2 68  ? 6.589   13.719  52.535  1.00 51.51 ? 73  ARG D CD  1 
ATOM   3009 N  NE  . ARG D 2 68  ? 7.590   14.096  53.530  1.00 54.94 ? 73  ARG D NE  1 
ATOM   3010 C  CZ  . ARG D 2 68  ? 7.634   13.625  54.772  1.00 55.72 ? 73  ARG D CZ  1 
ATOM   3011 N  NH1 . ARG D 2 68  ? 6.743   12.751  55.219  1.00 53.85 ? 73  ARG D NH1 1 
ATOM   3012 N  NH2 . ARG D 2 68  ? 8.600   14.036  55.584  1.00 56.51 ? 73  ARG D NH2 1 
ATOM   3013 N  N   . THR D 2 69  ? 3.403   16.783  54.921  1.00 46.30 ? 74  THR D N   1 
ATOM   3014 C  CA  . THR D 2 69  ? 2.772   16.238  56.110  1.00 48.96 ? 74  THR D CA  1 
ATOM   3015 C  C   . THR D 2 69  ? 1.513   17.008  56.498  1.00 56.23 ? 74  THR D C   1 
ATOM   3016 O  O   . THR D 2 69  ? 0.408   16.449  56.489  1.00 57.59 ? 74  THR D O   1 
ATOM   3017 C  CB  . THR D 2 69  ? 3.800   16.245  57.246  1.00 49.94 ? 74  THR D CB  1 
ATOM   3018 O  OG1 . THR D 2 69  ? 4.641   17.406  57.117  1.00 55.27 ? 74  THR D OG1 1 
ATOM   3019 C  CG2 . THR D 2 69  ? 4.668   15.003  57.155  1.00 47.53 ? 74  THR D CG2 1 
ATOM   3020 N  N   . ARG D 2 70  ? 1.660   18.285  56.841  1.00 47.10 ? 75  ARG D N   1 
ATOM   3021 C  CA  . ARG D 2 70  ? 0.541   19.040  57.383  1.00 59.53 ? 75  ARG D CA  1 
ATOM   3022 C  C   . ARG D 2 70  ? -0.637  19.116  56.401  1.00 55.16 ? 75  ARG D C   1 
ATOM   3023 O  O   . ARG D 2 70  ? -0.460  19.323  55.197  1.00 53.89 ? 75  ARG D O   1 
ATOM   3024 C  CB  . ARG D 2 70  ? 1.027   20.433  57.773  1.00 62.81 ? 75  ARG D CB  1 
ATOM   3025 C  CG  . ARG D 2 70  ? 1.765   20.449  59.113  1.00 66.20 ? 75  ARG D CG  1 
ATOM   3026 C  CD  . ARG D 2 70  ? 1.688   21.821  59.770  1.00 71.03 ? 75  ARG D CD  1 
ATOM   3027 N  NE  . ARG D 2 70  ? 2.482   22.792  59.019  1.00 95.41 ? 75  ARG D NE  1 
ATOM   3028 C  CZ  . ARG D 2 70  ? 2.002   23.662  58.134  1.00 93.81 ? 75  ARG D CZ  1 
ATOM   3029 N  NH1 . ARG D 2 70  ? 0.706   23.743  57.871  1.00 94.72 ? 75  ARG D NH1 1 
ATOM   3030 N  NH2 . ARG D 2 70  ? 2.846   24.468  57.493  1.00 92.86 ? 75  ARG D NH2 1 
ATOM   3031 N  N   . TYR D 2 71  ? -1.849  18.910  56.926  1.00 56.38 ? 76  TYR D N   1 
ATOM   3032 C  CA  . TYR D 2 71  ? -3.072  19.032  56.134  1.00 50.25 ? 76  TYR D CA  1 
ATOM   3033 C  C   . TYR D 2 71  ? -3.415  20.502  55.921  1.00 49.73 ? 76  TYR D C   1 
ATOM   3034 O  O   . TYR D 2 71  ? -3.399  21.298  56.865  1.00 47.32 ? 76  TYR D O   1 
ATOM   3035 C  CB  . TYR D 2 71  ? -4.241  18.320  56.826  1.00 48.32 ? 76  TYR D CB  1 
ATOM   3036 C  CG  . TYR D 2 71  ? -5.590  18.545  56.155  1.00 50.07 ? 76  TYR D CG  1 
ATOM   3037 C  CD1 . TYR D 2 71  ? -5.990  17.757  55.077  1.00 46.25 ? 76  TYR D CD1 1 
ATOM   3038 C  CD2 . TYR D 2 71  ? -6.453  19.552  56.588  1.00 45.19 ? 76  TYR D CD2 1 
ATOM   3039 C  CE1 . TYR D 2 71  ? -7.207  17.957  54.460  1.00 43.09 ? 76  TYR D CE1 1 
ATOM   3040 C  CE2 . TYR D 2 71  ? -7.671  19.763  55.966  1.00 46.55 ? 76  TYR D CE2 1 
ATOM   3041 C  CZ  . TYR D 2 71  ? -8.038  18.963  54.901  1.00 45.21 ? 76  TYR D CZ  1 
ATOM   3042 O  OH  . TYR D 2 71  ? -9.245  19.159  54.279  1.00 46.40 ? 76  TYR D OH  1 
ATOM   3043 N  N   . GLU D 2 72  ? -3.814  20.839  54.693  1.00 47.92 ? 77  GLU D N   1 
ATOM   3044 C  CA  . GLU D 2 72  ? -3.942  22.231  54.249  1.00 46.65 ? 77  GLU D CA  1 
ATOM   3045 C  C   . GLU D 2 72  ? -5.398  22.552  53.892  1.00 45.23 ? 77  GLU D C   1 
ATOM   3046 O  O   . GLU D 2 72  ? -5.826  22.327  52.755  1.00 42.25 ? 77  GLU D O   1 
ATOM   3047 C  CB  . GLU D 2 72  ? -2.949  22.482  53.052  1.00 42.72 ? 77  GLU D CB  1 
ATOM   3048 C  CG  . GLU D 2 72  ? -1.470  22.274  53.447  1.00 40.66 ? 77  GLU D CG  1 
ATOM   3049 C  CD  . GLU D 2 72  ? -0.483  22.118  52.265  1.00 47.10 ? 77  GLU D CD  1 
ATOM   3050 O  OE1 . GLU D 2 72  ? -0.778  21.367  51.304  1.00 42.10 ? 77  GLU D OE1 1 
ATOM   3051 O  OE2 . GLU D 2 72  ? 0.617   22.727  52.322  1.00 44.67 ? 77  GLU D OE2 1 
ATOM   3052 N  N   . ARG D 2 73  A -6.137  23.058  54.895  1.00 45.79 ? 77  ARG D N   1 
ATOM   3053 C  CA  . ARG D 2 73  A -7.598  23.336  54.773  1.00 46.25 ? 77  ARG D CA  1 
ATOM   3054 C  C   . ARG D 2 73  A -7.934  24.225  53.575  1.00 45.22 ? 77  ARG D C   1 
ATOM   3055 O  O   . ARG D 2 73  A -7.248  25.250  53.391  1.00 44.95 ? 77  ARG D O   1 
ATOM   3056 C  CB  . ARG D 2 73  A -8.090  23.983  56.072  1.00 50.00 ? 77  ARG D CB  1 
ATOM   3057 C  CG  . ARG D 2 73  A -9.599  24.104  56.222  1.00 50.00 ? 77  ARG D CG  1 
ATOM   3058 C  CD  . ARG D 2 73  A -9.954  25.356  57.006  1.00 50.00 ? 77  ARG D CD  1 
ATOM   3059 N  NE  . ARG D 2 73  A -11.291 25.285  57.603  1.00 50.00 ? 77  ARG D NE  1 
ATOM   3060 C  CZ  . ARG D 2 73  A -11.560 24.755  58.789  1.00 50.00 ? 77  ARG D CZ  1 
ATOM   3061 N  NH1 . ARG D 2 73  A -10.578 24.480  59.629  1.00 50.00 ? 77  ARG D NH1 1 
ATOM   3062 N  NH2 . ARG D 2 73  A -12.810 24.504  59.133  1.00 50.00 ? 77  ARG D NH2 1 
ATOM   3063 N  N   . ASN D 2 74  ? -8.948  23.827  52.805  1.00 44.33 ? 78  ASN D N   1 
ATOM   3064 C  CA  . ASN D 2 74  ? -9.416  24.608  51.663  1.00 39.64 ? 78  ASN D CA  1 
ATOM   3065 C  C   . ASN D 2 74  ? -8.353  24.800  50.585  1.00 45.96 ? 78  ASN D C   1 
ATOM   3066 O  O   . ASN D 2 74  ? -8.589  25.523  49.614  1.00 49.03 ? 78  ASN D O   1 
ATOM   3067 C  CB  . ASN D 2 74  ? -9.936  25.959  52.117  1.00 45.76 ? 78  ASN D CB  1 
ATOM   3068 C  CG  . ASN D 2 74  ? -10.957 25.841  53.228  1.00 53.09 ? 78  ASN D CG  1 
ATOM   3069 O  OD1 . ASN D 2 74  ? -11.643 24.825  53.348  1.00 55.38 ? 78  ASN D OD1 1 
ATOM   3070 N  ND2 . ASN D 2 74  ? -11.075 26.891  54.040  1.00 49.13 ? 78  ASN D ND2 1 
ATOM   3071 N  N   . ILE D 2 75  ? -7.178  24.189  50.737  1.00 42.30 ? 79  ILE D N   1 
ATOM   3072 C  CA  . ILE D 2 75  ? -6.180  24.250  49.677  1.00 37.47 ? 79  ILE D CA  1 
ATOM   3073 C  C   . ILE D 2 75  ? -6.208  22.934  48.924  1.00 38.49 ? 79  ILE D C   1 
ATOM   3074 O  O   . ILE D 2 75  ? -6.576  22.882  47.746  1.00 39.85 ? 79  ILE D O   1 
ATOM   3075 C  CB  . ILE D 2 75  ? -4.756  24.493  50.202  1.00 41.43 ? 79  ILE D CB  1 
ATOM   3076 C  CG1 . ILE D 2 75  ? -4.690  25.704  51.140  1.00 43.54 ? 79  ILE D CG1 1 
ATOM   3077 C  CG2 . ILE D 2 75  ? -3.800  24.622  49.020  1.00 39.50 ? 79  ILE D CG2 1 
ATOM   3078 C  CD1 . ILE D 2 75  ? -5.227  26.948  50.528  1.00 43.20 ? 79  ILE D CD1 1 
ATOM   3079 N  N   . GLU D 2 76  ? -5.854  21.857  49.616  1.00 37.08 ? 80  GLU D N   1 
ATOM   3080 C  CA  . GLU D 2 76  ? -5.642  20.575  48.975  1.00 35.20 ? 80  GLU D CA  1 
ATOM   3081 C  C   . GLU D 2 76  ? -6.957  19.848  48.731  1.00 36.37 ? 80  GLU D C   1 
ATOM   3082 O  O   . GLU D 2 76  ? -7.946  20.045  49.440  1.00 36.68 ? 80  GLU D O   1 
ATOM   3083 C  CB  . GLU D 2 76  ? -4.708  19.713  49.817  1.00 32.98 ? 80  GLU D CB  1 
ATOM   3084 C  CG  . GLU D 2 76  ? -5.219  19.408  51.202  1.00 35.85 ? 80  GLU D CG  1 
ATOM   3085 C  CD  . GLU D 2 76  ? -4.288  18.468  51.955  1.00 41.15 ? 80  GLU D CD  1 
ATOM   3086 O  OE1 . GLU D 2 76  ? -4.478  17.235  51.848  1.00 39.67 ? 80  GLU D OE1 1 
ATOM   3087 O  OE2 . GLU D 2 76  ? -3.359  18.962  52.642  1.00 43.44 ? 80  GLU D OE2 1 
ATOM   3088 N  N   . LYS D 2 77  ? -6.965  19.023  47.687  1.00 34.52 ? 81  LYS D N   1 
ATOM   3089 C  CA  . LYS D 2 77  ? -8.113  18.195  47.358  1.00 35.50 ? 81  LYS D CA  1 
ATOM   3090 C  C   . LYS D 2 77  ? -7.655  16.751  47.223  1.00 36.83 ? 81  LYS D C   1 
ATOM   3091 O  O   . LYS D 2 77  ? -6.544  16.477  46.751  1.00 34.23 ? 81  LYS D O   1 
ATOM   3092 C  CB  . LYS D 2 77  ? -8.784  18.649  46.076  1.00 30.91 ? 81  LYS D CB  1 
ATOM   3093 C  CG  . LYS D 2 77  ? -9.123  20.118  46.046  1.00 38.49 ? 81  LYS D CG  1 
ATOM   3094 C  CD  . LYS D 2 77  ? -10.139 20.452  47.108  1.00 36.98 ? 81  LYS D CD  1 
ATOM   3095 C  CE  . LYS D 2 77  ? -10.536 21.910  47.039  1.00 38.06 ? 81  LYS D CE  1 
ATOM   3096 N  NZ  . LYS D 2 77  ? -11.484 22.252  48.137  1.00 42.82 ? 81  LYS D NZ  1 
ATOM   3097 N  N   . ILE D 2 78  ? -8.514  15.827  47.638  1.00 36.05 ? 82  ILE D N   1 
ATOM   3098 C  CA  . ILE D 2 78  ? -8.228  14.405  47.553  1.00 33.00 ? 82  ILE D CA  1 
ATOM   3099 C  C   . ILE D 2 78  ? -9.082  13.865  46.424  1.00 37.68 ? 82  ILE D C   1 
ATOM   3100 O  O   . ILE D 2 78  ? -10.231 14.296  46.245  1.00 37.08 ? 82  ILE D O   1 
ATOM   3101 C  CB  . ILE D 2 78  ? -8.537  13.667  48.873  1.00 37.80 ? 82  ILE D CB  1 
ATOM   3102 C  CG1 . ILE D 2 78  ? -7.523  14.023  49.955  1.00 43.01 ? 82  ILE D CG1 1 
ATOM   3103 C  CG2 . ILE D 2 78  ? -8.549  12.149  48.673  1.00 41.13 ? 82  ILE D CG2 1 
ATOM   3104 C  CD1 . ILE D 2 78  ? -8.111  14.085  51.374  1.00 45.92 ? 82  ILE D CD1 1 
ATOM   3105 N  N   . SER D 2 79  ? -8.534  12.926  45.661  1.00 32.71 ? 83  SER D N   1 
ATOM   3106 C  CA  . SER D 2 79  ? -9.344  12.324  44.630  1.00 29.55 ? 83  SER D CA  1 
ATOM   3107 C  C   . SER D 2 79  ? -9.009  10.858  44.446  1.00 37.35 ? 83  SER D C   1 
ATOM   3108 O  O   . SER D 2 79  ? -7.844  10.446  44.523  1.00 35.13 ? 83  SER D O   1 
ATOM   3109 C  CB  . SER D 2 79  ? -9.169  13.024  43.298  1.00 33.97 ? 83  SER D CB  1 
ATOM   3110 O  OG  . SER D 2 79  ? -9.818  12.221  42.320  1.00 42.70 ? 83  SER D OG  1 
ATOM   3111 N  N   . MET D 2 80  ? -10.046 10.091  44.141  1.00 38.21 ? 84  MET D N   1 
ATOM   3112 C  CA  . MET D 2 80  ? -9.889  8.708   43.752  1.00 35.50 ? 84  MET D CA  1 
ATOM   3113 C  C   . MET D 2 80  ? -9.720  8.645   42.245  1.00 36.79 ? 84  MET D C   1 
ATOM   3114 O  O   . MET D 2 80  ? -9.876  9.640   41.530  1.00 34.63 ? 84  MET D O   1 
ATOM   3115 C  CB  . MET D 2 80  ? -11.086 7.881   44.200  1.00 32.55 ? 84  MET D CB  1 
ATOM   3116 C  CG  . MET D 2 80  ? -11.370 8.016   45.673  1.00 35.86 ? 84  MET D CG  1 
ATOM   3117 S  SD  . MET D 2 80  ? -10.131 7.144   46.645  1.00 44.23 ? 84  MET D SD  1 
ATOM   3118 C  CE  . MET D 2 80  ? -10.735 7.472   48.303  1.00 45.65 ? 84  MET D CE  1 
ATOM   3119 N  N   . LEU D 2 81  ? -9.386  7.458   41.771  1.00 34.93 ? 85  LEU D N   1 
ATOM   3120 C  CA  . LEU D 2 81  ? -9.091  7.219   40.373  1.00 33.56 ? 85  LEU D CA  1 
ATOM   3121 C  C   . LEU D 2 81  ? -10.178 6.339   39.789  1.00 34.43 ? 85  LEU D C   1 
ATOM   3122 O  O   . LEU D 2 81  ? -10.528 5.314   40.379  1.00 36.53 ? 85  LEU D O   1 
ATOM   3123 C  CB  . LEU D 2 81  ? -7.719  6.560   40.222  1.00 31.93 ? 85  LEU D CB  1 
ATOM   3124 C  CG  . LEU D 2 81  ? -6.599  7.468   40.723  1.00 32.66 ? 85  LEU D CG  1 
ATOM   3125 C  CD1 . LEU D 2 81  ? -5.256  6.812   40.582  1.00 29.25 ? 85  LEU D CD1 1 
ATOM   3126 C  CD2 . LEU D 2 81  ? -6.638  8.782   39.949  1.00 36.66 ? 85  LEU D CD2 1 
ATOM   3127 N  N   . GLU D 2 82  ? -10.739 6.753   38.656  1.00 37.34 ? 86  GLU D N   1 
ATOM   3128 C  CA  . GLU D 2 82  ? -11.615 5.835   37.941  1.00 37.33 ? 86  GLU D CA  1 
ATOM   3129 C  C   . GLU D 2 82  ? -10.810 4.803   37.172  1.00 37.39 ? 86  GLU D C   1 
ATOM   3130 O  O   . GLU D 2 82  ? -11.141 3.612   37.200  1.00 40.24 ? 86  GLU D O   1 
ATOM   3131 C  CB  . GLU D 2 82  ? -12.537 6.591   36.990  1.00 40.08 ? 86  GLU D CB  1 
ATOM   3132 C  CG  . GLU D 2 82  ? -13.282 5.714   35.980  1.00 38.11 ? 86  GLU D CG  1 
ATOM   3133 C  CD  . GLU D 2 82  ? -14.324 6.523   35.229  1.00 48.16 ? 86  GLU D CD  1 
ATOM   3134 O  OE1 . GLU D 2 82  ? -15.171 7.117   35.936  1.00 55.08 ? 86  GLU D OE1 1 
ATOM   3135 O  OE2 . GLU D 2 82  ? -14.300 6.590   33.968  1.00 46.11 ? 86  GLU D OE2 1 
ATOM   3136 N  N   . LYS D 2 83  ? -9.748  5.221   36.485  1.00 38.84 ? 87  LYS D N   1 
ATOM   3137 C  CA  . LYS D 2 83  ? -9.057  4.209   35.691  1.00 34.09 ? 87  LYS D CA  1 
ATOM   3138 C  C   . LYS D 2 83  ? -7.573  4.518   35.521  1.00 34.54 ? 87  LYS D C   1 
ATOM   3139 O  O   . LYS D 2 83  ? -7.148  5.674   35.549  1.00 34.89 ? 87  LYS D O   1 
ATOM   3140 C  CB  . LYS D 2 83  ? -9.734  4.028   34.325  1.00 36.61 ? 87  LYS D CB  1 
ATOM   3141 C  CG  . LYS D 2 83  ? -9.511  2.639   33.702  1.00 37.47 ? 87  LYS D CG  1 
ATOM   3142 C  CD  . LYS D 2 83  ? -10.030 1.526   34.618  1.00 42.81 ? 87  LYS D CD  1 
ATOM   3143 C  CE  . LYS D 2 83  ? -9.626  0.132   34.104  1.00 56.06 ? 87  LYS D CE  1 
ATOM   3144 N  NZ  . LYS D 2 83  ? -10.312 -1.002  34.833  1.00 53.79 ? 87  LYS D NZ  1 
ATOM   3145 N  N   . ILE D 2 84  ? -6.796  3.452   35.351  1.00 34.32 ? 88  ILE D N   1 
ATOM   3146 C  CA  . ILE D 2 84  ? -5.359  3.501   35.098  1.00 36.07 ? 88  ILE D CA  1 
ATOM   3147 C  C   . ILE D 2 84  ? -5.100  3.003   33.675  1.00 36.08 ? 88  ILE D C   1 
ATOM   3148 O  O   . ILE D 2 84  ? -5.676  1.996   33.249  1.00 38.29 ? 88  ILE D O   1 
ATOM   3149 C  CB  . ILE D 2 84  ? -4.613  2.644   36.151  1.00 35.00 ? 88  ILE D CB  1 
ATOM   3150 C  CG1 . ILE D 2 84  ? -4.050  3.521   37.255  1.00 41.55 ? 88  ILE D CG1 1 
ATOM   3151 C  CG2 . ILE D 2 84  ? -3.471  1.853   35.547  1.00 38.01 ? 88  ILE D CG2 1 
ATOM   3152 C  CD1 . ILE D 2 84  ? -5.061  4.397   37.936  1.00 35.71 ? 88  ILE D CD1 1 
ATOM   3153 N  N   . TYR D 2 85  ? -4.230  3.698   32.940  1.00 31.20 ? 89  TYR D N   1 
ATOM   3154 C  CA  . TYR D 2 85  ? -3.866  3.312   31.580  1.00 33.36 ? 89  TYR D CA  1 
ATOM   3155 C  C   . TYR D 2 85  ? -2.346  3.322   31.457  1.00 33.70 ? 89  TYR D C   1 
ATOM   3156 O  O   . TYR D 2 85  ? -1.728  4.390   31.436  1.00 31.14 ? 89  TYR D O   1 
ATOM   3157 C  CB  . TYR D 2 85  ? -4.512  4.253   30.549  1.00 33.17 ? 89  TYR D CB  1 
ATOM   3158 C  CG  . TYR D 2 85  ? -6.020  4.347   30.681  1.00 30.57 ? 89  TYR D CG  1 
ATOM   3159 C  CD1 . TYR D 2 85  ? -6.866  3.438   30.033  1.00 31.97 ? 89  TYR D CD1 1 
ATOM   3160 C  CD2 . TYR D 2 85  ? -6.598  5.319   31.494  1.00 35.07 ? 89  TYR D CD2 1 
ATOM   3161 C  CE1 . TYR D 2 85  ? -8.263  3.520   30.180  1.00 36.96 ? 89  TYR D CE1 1 
ATOM   3162 C  CE2 . TYR D 2 85  ? -7.980  5.410   31.649  1.00 36.27 ? 89  TYR D CE2 1 
ATOM   3163 C  CZ  . TYR D 2 85  ? -8.807  4.519   30.991  1.00 38.93 ? 89  TYR D CZ  1 
ATOM   3164 O  OH  . TYR D 2 85  ? -10.167 4.645   31.177  1.00 39.53 ? 89  TYR D OH  1 
ATOM   3165 N  N   . ILE D 2 86  ? -1.749  2.139   31.380  1.00 34.57 ? 90  ILE D N   1 
ATOM   3166 C  CA  . ILE D 2 86  ? -0.318  1.980   31.142  1.00 32.53 ? 90  ILE D CA  1 
ATOM   3167 C  C   . ILE D 2 86  ? -0.070  1.914   29.641  1.00 34.87 ? 90  ILE D C   1 
ATOM   3168 O  O   . ILE D 2 86  ? -0.871  1.353   28.884  1.00 36.82 ? 90  ILE D O   1 
ATOM   3169 C  CB  . ILE D 2 86  ? 0.211   0.710   31.836  1.00 34.80 ? 90  ILE D CB  1 
ATOM   3170 C  CG1 . ILE D 2 86  ? -0.307  0.597   33.279  1.00 33.96 ? 90  ILE D CG1 1 
ATOM   3171 C  CG2 . ILE D 2 86  ? 1.711   0.638   31.767  1.00 30.40 ? 90  ILE D CG2 1 
ATOM   3172 C  CD1 . ILE D 2 86  ? 0.480   1.310   34.283  1.00 30.79 ? 90  ILE D CD1 1 
ATOM   3173 N  N   . HIS D 2 87  ? 1.035   2.483   29.201  1.00 35.02 ? 91  HIS D N   1 
ATOM   3174 C  CA  . HIS D 2 87  ? 1.411   2.336   27.810  1.00 33.60 ? 91  HIS D CA  1 
ATOM   3175 C  C   . HIS D 2 87  ? 1.610   0.857   27.490  1.00 36.09 ? 91  HIS D C   1 
ATOM   3176 O  O   . HIS D 2 87  ? 2.333   0.160   28.217  1.00 33.17 ? 91  HIS D O   1 
ATOM   3177 C  CB  . HIS D 2 87  ? 2.684   3.118   27.509  1.00 35.24 ? 91  HIS D CB  1 
ATOM   3178 C  CG  . HIS D 2 87  ? 2.943   3.292   26.046  1.00 34.17 ? 91  HIS D CG  1 
ATOM   3179 N  ND1 . HIS D 2 87  ? 3.217   2.234   25.209  1.00 37.61 ? 91  HIS D ND1 1 
ATOM   3180 C  CD2 . HIS D 2 87  ? 2.949   4.397   25.269  1.00 35.77 ? 91  HIS D CD2 1 
ATOM   3181 C  CE1 . HIS D 2 87  ? 3.385   2.680   23.978  1.00 39.58 ? 91  HIS D CE1 1 
ATOM   3182 N  NE2 . HIS D 2 87  ? 3.237   3.992   23.989  1.00 40.30 ? 91  HIS D NE2 1 
ATOM   3183 N  N   . PRO D 2 88  ? 1.017   0.349   26.409  1.00 35.88 ? 92  PRO D N   1 
ATOM   3184 C  CA  . PRO D 2 88  ? 1.130   -1.090  26.129  1.00 34.99 ? 92  PRO D CA  1 
ATOM   3185 C  C   . PRO D 2 88  ? 2.553   -1.560  25.856  1.00 39.40 ? 92  PRO D C   1 
ATOM   3186 O  O   . PRO D 2 88  ? 2.845   -2.738  26.100  1.00 41.64 ? 92  PRO D O   1 
ATOM   3187 C  CB  . PRO D 2 88  ? 0.233   -1.274  24.901  1.00 32.39 ? 92  PRO D CB  1 
ATOM   3188 C  CG  . PRO D 2 88  ? 0.191   0.089   24.257  1.00 37.92 ? 92  PRO D CG  1 
ATOM   3189 C  CD  . PRO D 2 88  ? 0.207   1.057   25.405  1.00 37.57 ? 92  PRO D CD  1 
ATOM   3190 N  N   . ARG D 2 89  ? 3.468   -0.689  25.422  1.00 36.01 ? 93  ARG D N   1 
ATOM   3191 C  CA  . ARG D 2 89  ? 4.843   -1.108  25.165  1.00 34.11 ? 93  ARG D CA  1 
ATOM   3192 C  C   . ARG D 2 89  ? 5.813   -0.673  26.260  1.00 38.57 ? 93  ARG D C   1 
ATOM   3193 O  O   . ARG D 2 89  ? 7.036   -0.693  26.046  1.00 40.50 ? 93  ARG D O   1 
ATOM   3194 C  CB  . ARG D 2 89  ? 5.299   -0.598  23.803  1.00 39.98 ? 93  ARG D CB  1 
ATOM   3195 C  CG  . ARG D 2 89  ? 4.540   -1.279  22.667  1.00 41.04 ? 93  ARG D CG  1 
ATOM   3196 C  CD  . ARG D 2 89  ? 5.311   -1.264  21.372  1.00 52.17 ? 93  ARG D CD  1 
ATOM   3197 N  NE  . ARG D 2 89  ? 5.126   -0.029  20.625  1.00 54.84 ? 93  ARG D NE  1 
ATOM   3198 C  CZ  . ARG D 2 89  ? 5.956   0.400   19.685  1.00 61.76 ? 93  ARG D CZ  1 
ATOM   3199 N  NH1 . ARG D 2 89  ? 7.037   -0.292  19.350  1.00 63.42 ? 93  ARG D NH1 1 
ATOM   3200 N  NH2 . ARG D 2 89  ? 5.696   1.550   19.064  1.00 62.44 ? 93  ARG D NH2 1 
ATOM   3201 N  N   . TYR D 2 90  ? 5.294   -0.332  27.441  1.00 35.28 ? 94  TYR D N   1 
ATOM   3202 C  CA  . TYR D 2 90  ? 6.133   -0.079  28.602  1.00 33.50 ? 94  TYR D CA  1 
ATOM   3203 C  C   . TYR D 2 90  ? 7.014   -1.290  28.871  1.00 34.01 ? 94  TYR D C   1 
ATOM   3204 O  O   . TYR D 2 90  ? 6.532   -2.421  28.986  1.00 35.36 ? 94  TYR D O   1 
ATOM   3205 C  CB  . TYR D 2 90  ? 5.242   0.223   29.806  1.00 30.48 ? 94  TYR D CB  1 
ATOM   3206 C  CG  . TYR D 2 90  ? 5.864   0.074   31.167  1.00 26.66 ? 94  TYR D CG  1 
ATOM   3207 C  CD1 . TYR D 2 90  ? 7.095   0.652   31.469  1.00 34.18 ? 94  TYR D CD1 1 
ATOM   3208 C  CD2 . TYR D 2 90  ? 5.209   -0.618  32.163  1.00 26.52 ? 94  TYR D CD2 1 
ATOM   3209 C  CE1 . TYR D 2 90  ? 7.660   0.536   32.749  1.00 30.99 ? 94  TYR D CE1 1 
ATOM   3210 C  CE2 . TYR D 2 90  ? 5.748   -0.734  33.441  1.00 31.07 ? 94  TYR D CE2 1 
ATOM   3211 C  CZ  . TYR D 2 90  ? 6.974   -0.150  33.734  1.00 31.57 ? 94  TYR D CZ  1 
ATOM   3212 O  OH  . TYR D 2 90  ? 7.524   -0.289  34.994  1.00 28.41 ? 94  TYR D OH  1 
ATOM   3213 N  N   . ASN D 2 91  ? 8.306   -1.057  28.957  1.00 32.41 ? 95  ASN D N   1 
ATOM   3214 C  CA  . ASN D 2 91  ? 9.270   -2.138  29.017  1.00 31.51 ? 95  ASN D CA  1 
ATOM   3215 C  C   . ASN D 2 91  ? 9.861   -2.141  30.415  1.00 33.01 ? 95  ASN D C   1 
ATOM   3216 O  O   . ASN D 2 91  ? 10.909  -1.550  30.661  1.00 38.32 ? 95  ASN D O   1 
ATOM   3217 C  CB  . ASN D 2 91  ? 10.332  -1.967  27.962  1.00 33.92 ? 95  ASN D CB  1 
ATOM   3218 C  CG  . ASN D 2 91  ? 11.262  -3.158  27.875  1.00 40.81 ? 95  ASN D CG  1 
ATOM   3219 O  OD1 . ASN D 2 91  ? 11.442  -3.900  28.849  1.00 41.14 ? 95  ASN D OD1 1 
ATOM   3220 N  ND2 . ASN D 2 91  ? 11.876  -3.343  26.707  1.00 41.42 ? 95  ASN D ND2 1 
ATOM   3221 N  N   . TRP D 2 92  ? 9.193   -2.827  31.325  1.00 32.36 ? 96  TRP D N   1 
ATOM   3222 C  CA  . TRP D 2 92  ? 9.707   -2.953  32.678  1.00 35.21 ? 96  TRP D CA  1 
ATOM   3223 C  C   . TRP D 2 92  ? 10.740  -4.065  32.807  1.00 36.37 ? 96  TRP D C   1 
ATOM   3224 O  O   . TRP D 2 92  ? 11.389  -4.166  33.851  1.00 40.19 ? 96  TRP D O   1 
ATOM   3225 C  CB  . TRP D 2 92  ? 8.555   -3.205  33.665  1.00 35.90 ? 96  TRP D CB  1 
ATOM   3226 C  CG  . TRP D 2 92  ? 7.692   -4.374  33.276  1.00 36.03 ? 96  TRP D CG  1 
ATOM   3227 C  CD1 . TRP D 2 92  ? 6.522   -4.328  32.581  1.00 38.08 ? 96  TRP D CD1 1 
ATOM   3228 C  CD2 . TRP D 2 92  ? 7.954   -5.763  33.534  1.00 39.15 ? 96  TRP D CD2 1 
ATOM   3229 N  NE1 . TRP D 2 92  ? 6.024   -5.603  32.400  1.00 41.73 ? 96  TRP D NE1 1 
ATOM   3230 C  CE2 . TRP D 2 92  ? 6.886   -6.501  32.973  1.00 39.79 ? 96  TRP D CE2 1 
ATOM   3231 C  CE3 . TRP D 2 92  ? 8.982   -6.454  34.191  1.00 37.40 ? 96  TRP D CE3 1 
ATOM   3232 C  CZ2 . TRP D 2 92  ? 6.814   -7.891  33.048  1.00 38.47 ? 96  TRP D CZ2 1 
ATOM   3233 C  CZ3 . TRP D 2 92  ? 8.905   -7.833  34.272  1.00 39.06 ? 96  TRP D CZ3 1 
ATOM   3234 C  CH2 . TRP D 2 92  ? 7.828   -8.538  33.701  1.00 42.32 ? 96  TRP D CH2 1 
ATOM   3235 N  N   . ARG D 2 93  ? 10.875  -4.931  31.805  1.00 35.05 ? 97  ARG D N   1 
ATOM   3236 C  CA  . ARG D 2 93  ? 11.878  -5.985  31.901  1.00 35.31 ? 97  ARG D CA  1 
ATOM   3237 C  C   . ARG D 2 93  ? 13.277  -5.417  31.727  1.00 35.75 ? 97  ARG D C   1 
ATOM   3238 O  O   . ARG D 2 93  ? 14.195  -5.753  32.482  1.00 32.06 ? 97  ARG D O   1 
ATOM   3239 C  CB  . ARG D 2 93  ? 11.608  -7.062  30.839  1.00 41.31 ? 97  ARG D CB  1 
ATOM   3240 C  CG  . ARG D 2 93  ? 10.438  -7.983  31.141  1.00 44.12 ? 97  ARG D CG  1 
ATOM   3241 C  CD  . ARG D 2 93  ? 10.305  -9.100  30.098  1.00 49.28 ? 97  ARG D CD  1 
ATOM   3242 N  NE  . ARG D 2 93  ? 9.499   -10.216 30.588  1.00 51.42 ? 97  ARG D NE  1 
ATOM   3243 C  CZ  . ARG D 2 93  ? 8.181   -10.313 30.446  1.00 56.13 ? 97  ARG D CZ  1 
ATOM   3244 N  NH1 . ARG D 2 93  ? 7.475   -9.369  29.834  1.00 49.37 ? 97  ARG D NH1 1 
ATOM   3245 N  NH2 . ARG D 2 93  ? 7.554   -11.383 30.929  1.00 50.05 ? 97  ARG D NH2 1 
ATOM   3246 N  N   . GLU D 2 94  A 13.436  -4.511  30.767  1.00 40.26 ? 97  GLU D N   1 
ATOM   3247 C  CA  . GLU D 2 94  A 14.747  -4.108  30.279  1.00 44.32 ? 97  GLU D CA  1 
ATOM   3248 C  C   . GLU D 2 94  A 15.201  -2.834  30.967  1.00 39.48 ? 97  GLU D C   1 
ATOM   3249 O  O   . GLU D 2 94  A 16.017  -2.870  31.900  1.00 34.23 ? 97  GLU D O   1 
ATOM   3250 C  CB  . GLU D 2 94  A 14.704  -3.870  28.760  1.00 40.53 ? 97  GLU D CB  1 
ATOM   3251 C  CG  . GLU D 2 94  A 14.954  -5.089  27.871  1.00 45.41 ? 97  GLU D CG  1 
ATOM   3252 C  CD  . GLU D 2 94  A 14.990  -4.721  26.379  1.00 55.93 ? 97  GLU D CD  1 
ATOM   3253 O  OE1 . GLU D 2 94  A 14.089  -5.176  25.623  1.00 52.99 ? 97  GLU D OE1 1 
ATOM   3254 O  OE2 . GLU D 2 94  A 15.922  -3.972  25.970  1.00 54.47 ? 97  GLU D OE2 1 
ATOM   3255 N  N   . ASN D 2 95  ? 14.603  -1.704  30.542  1.00 34.90 ? 98  ASN D N   1 
ATOM   3256 C  CA  . ASN D 2 95  ? 15.204  -0.403  30.792  1.00 37.48 ? 98  ASN D CA  1 
ATOM   3257 C  C   . ASN D 2 95  ? 14.176  0.685   31.050  1.00 37.26 ? 98  ASN D C   1 
ATOM   3258 O  O   . ASN D 2 95  ? 14.505  1.863   30.896  1.00 39.50 ? 98  ASN D O   1 
ATOM   3259 C  CB  . ASN D 2 95  ? 16.050  0.023   29.596  1.00 32.10 ? 98  ASN D CB  1 
ATOM   3260 C  CG  . ASN D 2 95  ? 15.258  0.004   28.301  1.00 39.21 ? 98  ASN D CG  1 
ATOM   3261 O  OD1 . ASN D 2 95  ? 14.070  -0.359  28.273  1.00 37.13 ? 98  ASN D OD1 1 
ATOM   3262 N  ND2 . ASN D 2 95  ? 15.913  0.390   27.214  1.00 40.04 ? 98  ASN D ND2 1 
ATOM   3263 N  N   . LEU D 2 96  ? 12.941  0.330   31.393  1.00 39.73 ? 99  LEU D N   1 
ATOM   3264 C  CA  . LEU D 2 96  ? 11.879  1.307   31.632  1.00 35.31 ? 99  LEU D CA  1 
ATOM   3265 C  C   . LEU D 2 96  ? 11.582  2.154   30.399  1.00 35.00 ? 99  LEU D C   1 
ATOM   3266 O  O   . LEU D 2 96  ? 11.251  3.335   30.522  1.00 39.69 ? 99  LEU D O   1 
ATOM   3267 C  CB  . LEU D 2 96  ? 12.215  2.210   32.822  1.00 31.84 ? 99  LEU D CB  1 
ATOM   3268 C  CG  . LEU D 2 96  ? 12.442  1.418   34.109  1.00 31.89 ? 99  LEU D CG  1 
ATOM   3269 C  CD1 . LEU D 2 96  ? 13.014  2.291   35.220  1.00 33.76 ? 99  LEU D CD1 1 
ATOM   3270 C  CD2 . LEU D 2 96  ? 11.149  0.798   34.522  1.00 29.03 ? 99  LEU D CD2 1 
ATOM   3271 N  N   . ASP D 2 97  ? 11.717  1.587   29.201  1.00 33.91 ? 100 ASP D N   1 
ATOM   3272 C  CA  . ASP D 2 97  ? 11.322  2.326   28.007  1.00 32.98 ? 100 ASP D CA  1 
ATOM   3273 C  C   . ASP D 2 97  ? 9.822   2.578   28.036  1.00 31.94 ? 100 ASP D C   1 
ATOM   3274 O  O   . ASP D 2 97  ? 9.037   1.687   28.366  1.00 36.15 ? 100 ASP D O   1 
ATOM   3275 C  CB  . ASP D 2 97  ? 11.712  1.563   26.735  1.00 34.28 ? 100 ASP D CB  1 
ATOM   3276 C  CG  . ASP D 2 97  ? 11.400  2.343   25.456  1.00 35.57 ? 100 ASP D CG  1 
ATOM   3277 O  OD1 . ASP D 2 97  ? 11.370  3.589   25.489  1.00 38.12 ? 100 ASP D OD1 1 
ATOM   3278 O  OD2 . ASP D 2 97  ? 11.183  1.714   24.401  1.00 40.68 ? 100 ASP D OD2 1 
ATOM   3279 N  N   . ARG D 2 98  ? 9.431   3.807   27.704  1.00 32.32 ? 101 ARG D N   1 
ATOM   3280 C  CA  . ARG D 2 98  ? 8.031   4.236   27.706  1.00 31.74 ? 101 ARG D CA  1 
ATOM   3281 C  C   . ARG D 2 98  ? 7.440   4.160   29.110  1.00 30.01 ? 101 ARG D C   1 
ATOM   3282 O  O   . ARG D 2 98  ? 6.357   3.621   29.321  1.00 27.18 ? 101 ARG D O   1 
ATOM   3283 C  CB  . ARG D 2 98  ? 7.188   3.425   26.716  1.00 36.48 ? 101 ARG D CB  1 
ATOM   3284 C  CG  . ARG D 2 98  ? 7.551   3.645   25.253  1.00 40.52 ? 101 ARG D CG  1 
ATOM   3285 C  CD  . ARG D 2 98  ? 6.589   2.924   24.320  1.00 40.21 ? 101 ARG D CD  1 
ATOM   3286 N  NE  . ARG D 2 98  ? 6.986   3.059   22.922  1.00 48.77 ? 101 ARG D NE  1 
ATOM   3287 C  CZ  . ARG D 2 98  ? 7.948   2.348   22.347  1.00 50.25 ? 101 ARG D CZ  1 
ATOM   3288 N  NH1 . ARG D 2 98  ? 8.655   1.459   23.032  1.00 46.62 ? 101 ARG D NH1 1 
ATOM   3289 N  NH2 . ARG D 2 98  ? 8.224   2.550   21.058  1.00 56.07 ? 101 ARG D NH2 1 
ATOM   3290 N  N   . ASP D 2 99  ? 8.167   4.711   30.081  1.00 32.53 ? 102 ASP D N   1 
ATOM   3291 C  CA  . ASP D 2 99  ? 7.741   4.708   31.484  1.00 30.08 ? 102 ASP D CA  1 
ATOM   3292 C  C   . ASP D 2 99  ? 6.702   5.815   31.671  1.00 29.08 ? 102 ASP D C   1 
ATOM   3293 O  O   . ASP D 2 99  ? 6.988   6.899   32.186  1.00 27.91 ? 102 ASP D O   1 
ATOM   3294 C  CB  . ASP D 2 99  ? 8.954   4.903   32.387  1.00 29.26 ? 102 ASP D CB  1 
ATOM   3295 C  CG  . ASP D 2 99  ? 8.645   4.680   33.860  1.00 31.16 ? 102 ASP D CG  1 
ATOM   3296 O  OD1 . ASP D 2 99  ? 7.481   4.337   34.176  1.00 30.37 ? 102 ASP D OD1 1 
ATOM   3297 O  OD2 . ASP D 2 99  ? 9.572   4.842   34.701  1.00 27.30 ? 102 ASP D OD2 1 
ATOM   3298 N  N   . ILE D 2 100 ? 5.469   5.539   31.231  1.00 28.66 ? 103 ILE D N   1 
ATOM   3299 C  CA  . ILE D 2 100 ? 4.408   6.547   31.233  1.00 28.51 ? 103 ILE D CA  1 
ATOM   3300 C  C   . ILE D 2 100 ? 3.059   5.885   31.499  1.00 28.56 ? 103 ILE D C   1 
ATOM   3301 O  O   . ILE D 2 100 ? 2.806   4.749   31.086  1.00 26.61 ? 103 ILE D O   1 
ATOM   3302 C  CB  . ILE D 2 100 ? 4.382   7.348   29.908  1.00 28.08 ? 103 ILE D CB  1 
ATOM   3303 C  CG1 . ILE D 2 100 ? 3.354   8.487   29.999  1.00 27.24 ? 103 ILE D CG1 1 
ATOM   3304 C  CG2 . ILE D 2 100 ? 4.134   6.423   28.718  1.00 24.72 ? 103 ILE D CG2 1 
ATOM   3305 C  CD1 . ILE D 2 100 ? 3.533   9.570   28.977  1.00 27.09 ? 103 ILE D CD1 1 
ATOM   3306 N  N   . ALA D 2 101 ? 2.170   6.631   32.156  1.00 27.56 ? 104 ALA D N   1 
ATOM   3307 C  CA  . ALA D 2 101 ? 0.858   6.131   32.550  1.00 28.08 ? 104 ALA D CA  1 
ATOM   3308 C  C   . ALA D 2 101 ? -0.089  7.301   32.759  1.00 30.01 ? 104 ALA D C   1 
ATOM   3309 O  O   . ALA D 2 101 ? 0.320   8.397   33.178  1.00 31.53 ? 104 ALA D O   1 
ATOM   3310 C  CB  . ALA D 2 101 ? 0.922   5.281   33.837  1.00 28.05 ? 104 ALA D CB  1 
ATOM   3311 N  N   . LEU D 2 102 ? -1.365  7.042   32.492  1.00 28.06 ? 105 LEU D N   1 
ATOM   3312 C  CA  . LEU D 2 102 ? -2.416  8.030   32.661  1.00 30.69 ? 105 LEU D CA  1 
ATOM   3313 C  C   . LEU D 2 102 ? -3.386  7.556   33.731  1.00 32.32 ? 105 LEU D C   1 
ATOM   3314 O  O   . LEU D 2 102 ? -3.707  6.364   33.820  1.00 29.34 ? 105 LEU D O   1 
ATOM   3315 C  CB  . LEU D 2 102 ? -3.164  8.288   31.353  1.00 28.26 ? 105 LEU D CB  1 
ATOM   3316 C  CG  . LEU D 2 102 ? -2.500  9.345   30.479  1.00 32.80 ? 105 LEU D CG  1 
ATOM   3317 C  CD1 . LEU D 2 102 ? -3.060  9.318   29.064  1.00 33.79 ? 105 LEU D CD1 1 
ATOM   3318 C  CD2 . LEU D 2 102 ? -2.675  10.723  31.109  1.00 31.83 ? 105 LEU D CD2 1 
ATOM   3319 N  N   . MET D 2 103 ? -3.861  8.498   34.538  1.00 28.22 ? 106 MET D N   1 
ATOM   3320 C  CA  . MET D 2 103 ? -4.823  8.199   35.583  1.00 31.39 ? 106 MET D CA  1 
ATOM   3321 C  C   . MET D 2 103 ? -6.001  9.137   35.413  1.00 29.93 ? 106 MET D C   1 
ATOM   3322 O  O   . MET D 2 103 ? -5.825  10.357  35.334  1.00 31.29 ? 106 MET D O   1 
ATOM   3323 C  CB  . MET D 2 103 ? -4.175  8.319   36.968  1.00 27.14 ? 106 MET D CB  1 
ATOM   3324 C  CG  . MET D 2 103 ? -2.985  7.374   37.110  1.00 27.58 ? 106 MET D CG  1 
ATOM   3325 S  SD  . MET D 2 103 ? -2.144  7.357   38.710  1.00 34.92 ? 106 MET D SD  1 
ATOM   3326 C  CE  . MET D 2 103 ? -1.847  9.101   38.992  1.00 21.57 ? 106 MET D CE  1 
ATOM   3327 N  N   . LYS D 2 104 ? -7.186  8.559   35.295  1.00 29.00 ? 107 LYS D N   1 
ATOM   3328 C  CA  . LYS D 2 104 ? -8.424  9.309   35.192  1.00 32.75 ? 107 LYS D CA  1 
ATOM   3329 C  C   . LYS D 2 104 ? -9.064  9.360   36.567  1.00 32.55 ? 107 LYS D C   1 
ATOM   3330 O  O   . LYS D 2 104 ? -9.371  8.305   37.159  1.00 33.49 ? 107 LYS D O   1 
ATOM   3331 C  CB  . LYS D 2 104 ? -9.386  8.680   34.180  1.00 32.63 ? 107 LYS D CB  1 
ATOM   3332 C  CG  . LYS D 2 104 ? -10.559 9.582   33.798  1.00 36.97 ? 107 LYS D CG  1 
ATOM   3333 C  CD  . LYS D 2 104 ? -11.593 8.827   32.960  1.00 35.36 ? 107 LYS D CD  1 
ATOM   3334 C  CE  . LYS D 2 104 ? -12.906 9.569   32.871  1.00 33.16 ? 107 LYS D CE  1 
ATOM   3335 N  NZ  . LYS D 2 104 ? -13.891 8.704   32.196  1.00 38.32 ? 107 LYS D NZ  1 
ATOM   3336 N  N   . LEU D 2 105 ? -9.295  10.582  37.031  1.00 28.80 ? 108 LEU D N   1 
ATOM   3337 C  CA  . LEU D 2 105 ? -9.918  10.828  38.309  1.00 30.59 ? 108 LEU D CA  1 
ATOM   3338 C  C   . LEU D 2 105 ? -11.383 10.441  38.242  1.00 37.95 ? 108 LEU D C   1 
ATOM   3339 O  O   . LEU D 2 105 ? -12.020 10.538  37.187  1.00 37.10 ? 108 LEU D O   1 
ATOM   3340 C  CB  . LEU D 2 105 ? -9.803  12.307  38.675  1.00 36.61 ? 108 LEU D CB  1 
ATOM   3341 C  CG  . LEU D 2 105 ? -8.452  13.024  38.625  1.00 31.17 ? 108 LEU D CG  1 
ATOM   3342 C  CD1 . LEU D 2 105 ? -8.657  14.456  39.075  1.00 26.58 ? 108 LEU D CD1 1 
ATOM   3343 C  CD2 . LEU D 2 105 ? -7.445  12.305  39.498  1.00 23.99 ? 108 LEU D CD2 1 
ATOM   3344 N  N   . LYS D 2 106 ? -11.906 9.963   39.383  1.00 40.83 ? 109 LYS D N   1 
ATOM   3345 C  CA  . LYS D 2 106 ? -13.326 9.629   39.484  1.00 41.99 ? 109 LYS D CA  1 
ATOM   3346 C  C   . LYS D 2 106 ? -14.211 10.832  39.202  1.00 43.14 ? 109 LYS D C   1 
ATOM   3347 O  O   . LYS D 2 106 ? -15.283 10.693  38.595  1.00 39.42 ? 109 LYS D O   1 
ATOM   3348 C  CB  . LYS D 2 106 ? -13.645 9.055   40.859  1.00 37.39 ? 109 LYS D CB  1 
ATOM   3349 C  CG  . LYS D 2 106 ? -13.296 7.587   40.978  1.00 41.94 ? 109 LYS D CG  1 
ATOM   3350 C  CD  . LYS D 2 106 ? -14.536 6.701   40.983  1.00 38.13 ? 109 LYS D CD  1 
ATOM   3351 C  CE  . LYS D 2 106 ? -14.132 5.275   41.314  1.00 52.43 ? 109 LYS D CE  1 
ATOM   3352 N  NZ  . LYS D 2 106 ? -13.945 5.060   42.796  1.00 53.60 ? 109 LYS D NZ  1 
ATOM   3353 N  N   . LYS D 2 107 ? -13.809 12.010  39.690  1.00 38.26 ? 110 LYS D N   1 
ATOM   3354 C  CA  . LYS D 2 107 ? -14.545 13.256  39.535  1.00 38.25 ? 110 LYS D CA  1 
ATOM   3355 C  C   . LYS D 2 107 ? -13.584 14.369  39.148  1.00 37.14 ? 110 LYS D C   1 
ATOM   3356 O  O   . LYS D 2 107 ? -12.458 14.422  39.666  1.00 37.18 ? 110 LYS D O   1 
ATOM   3357 C  CB  . LYS D 2 107 ? -15.294 13.646  40.816  1.00 41.80 ? 110 LYS D CB  1 
ATOM   3358 C  CG  . LYS D 2 107 ? -16.358 12.627  41.190  1.00 47.01 ? 110 LYS D CG  1 
ATOM   3359 C  CD  . LYS D 2 107 ? -16.386 12.346  42.673  1.00 45.35 ? 110 LYS D CD  1 
ATOM   3360 C  CE  . LYS D 2 107 ? -16.959 10.982  42.942  1.00 45.53 ? 110 LYS D CE  1 
ATOM   3361 N  NZ  . LYS D 2 107 ? -17.826 11.062  44.160  1.00 50.19 ? 110 LYS D NZ  1 
ATOM   3362 N  N   . PRO D 2 108 ? -13.976 15.240  38.224  1.00 39.81 ? 111 PRO D N   1 
ATOM   3363 C  CA  . PRO D 2 108 ? -13.121 16.385  37.897  1.00 36.19 ? 111 PRO D CA  1 
ATOM   3364 C  C   . PRO D 2 108 ? -12.812 17.188  39.147  1.00 40.52 ? 111 PRO D C   1 
ATOM   3365 O  O   . PRO D 2 108 ? -13.665 17.350  40.021  1.00 46.00 ? 111 PRO D O   1 
ATOM   3366 C  CB  . PRO D 2 108 ? -13.967 17.187  36.904  1.00 31.83 ? 111 PRO D CB  1 
ATOM   3367 C  CG  . PRO D 2 108 ? -14.918 16.197  36.350  1.00 36.76 ? 111 PRO D CG  1 
ATOM   3368 C  CD  . PRO D 2 108 ? -15.244 15.276  37.481  1.00 36.71 ? 111 PRO D CD  1 
ATOM   3369 N  N   . VAL D 2 109 ? -11.571 17.653  39.248  1.00 33.69 ? 112 VAL D N   1 
ATOM   3370 C  CA  . VAL D 2 109 ? -11.140 18.497  40.354  1.00 34.82 ? 112 VAL D CA  1 
ATOM   3371 C  C   . VAL D 2 109 ? -11.344 19.945  39.937  1.00 31.96 ? 112 VAL D C   1 
ATOM   3372 O  O   . VAL D 2 109 ? -11.277 20.273  38.752  1.00 34.80 ? 112 VAL D O   1 
ATOM   3373 C  CB  . VAL D 2 109 ? -9.668  18.190  40.738  1.00 36.41 ? 112 VAL D CB  1 
ATOM   3374 C  CG1 . VAL D 2 109 ? -8.742  18.364  39.544  1.00 33.89 ? 112 VAL D CG1 1 
ATOM   3375 C  CG2 . VAL D 2 109 ? -9.199  19.048  41.942  1.00 33.90 ? 112 VAL D CG2 1 
ATOM   3376 N  N   . ALA D 2 110 ? -11.610 20.825  40.899  1.00 34.71 ? 113 ALA D N   1 
ATOM   3377 C  CA  . ALA D 2 110 ? -11.809 22.237  40.589  1.00 34.65 ? 113 ALA D CA  1 
ATOM   3378 C  C   . ALA D 2 110 ? -10.480 22.981  40.603  1.00 34.87 ? 113 ALA D C   1 
ATOM   3379 O  O   . ALA D 2 110 ? -9.636  22.760  41.477  1.00 34.54 ? 113 ALA D O   1 
ATOM   3380 C  CB  . ALA D 2 110 ? -12.785 22.885  41.568  1.00 27.21 ? 113 ALA D CB  1 
ATOM   3381 N  N   . PHE D 2 111 ? -10.281 23.838  39.607  1.00 33.86 ? 114 PHE D N   1 
ATOM   3382 C  CA  . PHE D 2 111 ? -9.063  24.624  39.560  1.00 33.76 ? 114 PHE D CA  1 
ATOM   3383 C  C   . PHE D 2 111 ? -9.125  25.761  40.562  1.00 35.68 ? 114 PHE D C   1 
ATOM   3384 O  O   . PHE D 2 111 ? -10.200 26.224  40.952  1.00 37.19 ? 114 PHE D O   1 
ATOM   3385 C  CB  . PHE D 2 111 ? -8.820  25.168  38.161  1.00 35.31 ? 114 PHE D CB  1 
ATOM   3386 C  CG  . PHE D 2 111 ? -8.583  24.102  37.150  1.00 36.77 ? 114 PHE D CG  1 
ATOM   3387 C  CD1 . PHE D 2 111 ? -8.116  22.853  37.546  1.00 38.91 ? 114 PHE D CD1 1 
ATOM   3388 C  CD2 . PHE D 2 111 ? -8.835  24.329  35.812  1.00 33.71 ? 114 PHE D CD2 1 
ATOM   3389 C  CE1 . PHE D 2 111 ? -7.890  21.850  36.604  1.00 41.39 ? 114 PHE D CE1 1 
ATOM   3390 C  CE2 . PHE D 2 111 ? -8.630  23.342  34.872  1.00 33.53 ? 114 PHE D CE2 1 
ATOM   3391 C  CZ  . PHE D 2 111 ? -8.158  22.097  35.263  1.00 39.61 ? 114 PHE D CZ  1 
ATOM   3392 N  N   . SER D 2 112 ? -7.950  26.230  40.953  1.00 33.08 ? 115 SER D N   1 
ATOM   3393 C  CA  . SER D 2 112 ? -7.842  27.249  41.980  1.00 30.05 ? 115 SER D CA  1 
ATOM   3394 C  C   . SER D 2 112 ? -6.494  27.933  41.827  1.00 37.69 ? 115 SER D C   1 
ATOM   3395 O  O   . SER D 2 112 ? -5.771  27.725  40.844  1.00 37.23 ? 115 SER D O   1 
ATOM   3396 C  CB  . SER D 2 112 ? -7.986  26.631  43.369  1.00 31.35 ? 115 SER D CB  1 
ATOM   3397 O  OG  . SER D 2 112 ? -6.807  25.917  43.710  1.00 32.19 ? 115 SER D OG  1 
ATOM   3398 N  N   . ASP D 2 113 ? -6.160  28.767  42.801  1.00 34.75 ? 116 ASP D N   1 
ATOM   3399 C  CA  . ASP D 2 113 ? -4.832  29.354  42.825  1.00 36.04 ? 116 ASP D CA  1 
ATOM   3400 C  C   . ASP D 2 113 ? -3.743  28.304  43.033  1.00 38.25 ? 116 ASP D C   1 
ATOM   3401 O  O   . ASP D 2 113 ? -2.570  28.572  42.730  1.00 36.90 ? 116 ASP D O   1 
ATOM   3402 C  CB  . ASP D 2 113 ? -4.784  30.429  43.911  1.00 37.56 ? 116 ASP D CB  1 
ATOM   3403 C  CG  . ASP D 2 113 ? -5.543  31.693  43.516  1.00 40.51 ? 116 ASP D CG  1 
ATOM   3404 O  OD1 . ASP D 2 113 ? -6.144  31.725  42.402  1.00 45.65 ? 116 ASP D OD1 1 
ATOM   3405 O  OD2 . ASP D 2 113 ? -5.530  32.654  44.314  1.00 38.57 ? 116 ASP D OD2 1 
ATOM   3406 N  N   . TYR D 2 114 ? -4.104  27.120  43.555  1.00 35.21 ? 117 TYR D N   1 
ATOM   3407 C  CA  . TYR D 2 114 ? -3.139  26.087  43.915  1.00 35.15 ? 117 TYR D CA  1 
ATOM   3408 C  C   . TYR D 2 114 ? -3.215  24.843  43.047  1.00 32.21 ? 117 TYR D C   1 
ATOM   3409 O  O   . TYR D 2 114 ? -2.387  23.945  43.210  1.00 34.34 ? 117 TYR D O   1 
ATOM   3410 C  CB  . TYR D 2 114 ? -3.329  25.663  45.378  1.00 34.29 ? 117 TYR D CB  1 
ATOM   3411 C  CG  . TYR D 2 114 ? -3.428  26.827  46.319  1.00 39.95 ? 117 TYR D CG  1 
ATOM   3412 C  CD1 . TYR D 2 114 ? -2.286  27.460  46.797  1.00 37.44 ? 117 TYR D CD1 1 
ATOM   3413 C  CD2 . TYR D 2 114 ? -4.669  27.307  46.726  1.00 36.60 ? 117 TYR D CD2 1 
ATOM   3414 C  CE1 . TYR D 2 114 ? -2.389  28.532  47.668  1.00 40.97 ? 117 TYR D CE1 1 
ATOM   3415 C  CE2 . TYR D 2 114 ? -4.777  28.373  47.585  1.00 34.04 ? 117 TYR D CE2 1 
ATOM   3416 C  CZ  . TYR D 2 114 ? -3.643  28.979  48.058  1.00 38.18 ? 117 TYR D CZ  1 
ATOM   3417 O  OH  . TYR D 2 114 ? -3.762  30.047  48.917  1.00 48.21 ? 117 TYR D OH  1 
ATOM   3418 N  N   . ILE D 2 115 ? -4.191  24.759  42.161  1.00 32.56 ? 118 ILE D N   1 
ATOM   3419 C  CA  . ILE D 2 115 ? -4.465  23.570  41.380  1.00 31.05 ? 118 ILE D CA  1 
ATOM   3420 C  C   . ILE D 2 115 ? -4.696  24.031  39.953  1.00 33.19 ? 118 ILE D C   1 
ATOM   3421 O  O   . ILE D 2 115 ? -5.721  24.661  39.656  1.00 34.87 ? 118 ILE D O   1 
ATOM   3422 C  CB  . ILE D 2 115 ? -5.681  22.818  41.923  1.00 33.98 ? 118 ILE D CB  1 
ATOM   3423 C  CG1 . ILE D 2 115 ? -5.375  22.370  43.369  1.00 34.18 ? 118 ILE D CG1 1 
ATOM   3424 C  CG2 . ILE D 2 115 ? -6.064  21.692  40.983  1.00 29.84 ? 118 ILE D CG2 1 
ATOM   3425 C  CD1 . ILE D 2 115 ? -6.450  21.574  44.017  1.00 30.68 ? 118 ILE D CD1 1 
ATOM   3426 N  N   . HIS D 2 116 ? -3.765  23.723  39.077  1.00 29.73 ? 119 HIS D N   1 
ATOM   3427 C  CA  . HIS D 2 116 ? -3.863  24.252  37.730  1.00 31.00 ? 119 HIS D CA  1 
ATOM   3428 C  C   . HIS D 2 116 ? -3.040  23.400  36.771  1.00 33.19 ? 119 HIS D C   1 
ATOM   3429 O  O   . HIS D 2 116 ? -1.871  23.075  37.056  1.00 30.29 ? 119 HIS D O   1 
ATOM   3430 C  CB  . HIS D 2 116 ? -3.408  25.708  37.694  1.00 30.05 ? 119 HIS D CB  1 
ATOM   3431 C  CG  . HIS D 2 116 ? -3.822  26.421  36.448  1.00 39.98 ? 119 HIS D CG  1 
ATOM   3432 N  ND1 . HIS D 2 116 ? -5.007  27.126  36.352  1.00 40.94 ? 119 HIS D ND1 1 
ATOM   3433 C  CD2 . HIS D 2 116 ? -3.230  26.510  35.232  1.00 37.21 ? 119 HIS D CD2 1 
ATOM   3434 C  CE1 . HIS D 2 116 ? -5.120  27.625  35.132  1.00 39.39 ? 119 HIS D CE1 1 
ATOM   3435 N  NE2 . HIS D 2 116 ? -4.060  27.261  34.431  1.00 36.14 ? 119 HIS D NE2 1 
ATOM   3436 N  N   . PRO D 2 117 ? -3.608  23.040  35.622  1.00 34.09 ? 120 PRO D N   1 
ATOM   3437 C  CA  . PRO D 2 117 ? -2.948  22.080  34.724  1.00 32.51 ? 120 PRO D CA  1 
ATOM   3438 C  C   . PRO D 2 117 ? -1.813  22.704  33.923  1.00 30.40 ? 120 PRO D C   1 
ATOM   3439 O  O   . PRO D 2 117 ? -1.825  23.893  33.592  1.00 31.83 ? 120 PRO D O   1 
ATOM   3440 C  CB  . PRO D 2 117 ? -4.085  21.639  33.797  1.00 30.17 ? 120 PRO D CB  1 
ATOM   3441 C  CG  . PRO D 2 117 ? -4.963  22.821  33.754  1.00 31.83 ? 120 PRO D CG  1 
ATOM   3442 C  CD  . PRO D 2 117 ? -4.934  23.434  35.128  1.00 29.30 ? 120 PRO D CD  1 
ATOM   3443 N  N   . VAL D 2 118 ? -0.811  21.861  33.615  1.00 28.00 ? 121 VAL D N   1 
ATOM   3444 C  CA  . VAL D 2 118 ? 0.355   22.212  32.806  1.00 29.76 ? 121 VAL D CA  1 
ATOM   3445 C  C   . VAL D 2 118 ? 0.041   21.845  31.353  1.00 30.38 ? 121 VAL D C   1 
ATOM   3446 O  O   . VAL D 2 118 ? -0.824  21.003  31.085  1.00 28.98 ? 121 VAL D O   1 
ATOM   3447 C  CB  . VAL D 2 118 ? 1.631   21.498  33.338  1.00 25.01 ? 121 VAL D CB  1 
ATOM   3448 C  CG1 . VAL D 2 118 ? 1.559   20.009  33.101  1.00 23.35 ? 121 VAL D CG1 1 
ATOM   3449 C  CG2 . VAL D 2 118 ? 2.900   22.038  32.692  1.00 24.69 ? 121 VAL D CG2 1 
ATOM   3450 N  N   . CYS D 2 119 ? 0.688   22.523  30.402  1.00 26.75 ? 122 CYS D N   1 
ATOM   3451 C  CA  . CYS D 2 119 ? 0.506   22.217  28.983  1.00 28.22 ? 122 CYS D CA  1 
ATOM   3452 C  C   . CYS D 2 119 ? 1.363   21.031  28.572  1.00 28.24 ? 122 CYS D C   1 
ATOM   3453 O  O   . CYS D 2 119 ? 2.442   20.793  29.125  1.00 28.38 ? 122 CYS D O   1 
ATOM   3454 C  CB  . CYS D 2 119 ? 0.869   23.410  28.098  1.00 25.04 ? 122 CYS D CB  1 
ATOM   3455 S  SG  . CYS D 2 119 ? 0.082   24.927  28.569  1.00 34.14 ? 122 CYS D SG  1 
ATOM   3456 N  N   . LEU D 2 120 ? 0.879   20.297  27.648  1.00 29.79 ? 123 LEU D N   1 
ATOM   3457 C  CA  . LEU D 2 120 ? 1.756   19.375  26.939  1.00 30.96 ? 123 LEU D CA  1 
ATOM   3458 C  C   . LEU D 2 120 ? 2.345   20.055  25.709  1.00 29.35 ? 123 LEU D C   1 
ATOM   3459 O  O   . LEU D 2 120 ? 1.677   20.867  25.079  1.00 31.16 ? 123 LEU D O   1 
ATOM   3460 C  CB  . LEU D 2 120 ? 0.992   18.122  26.522  1.00 28.20 ? 123 LEU D CB  1 
ATOM   3461 C  CG  . LEU D 2 120 ? 0.437   17.344  27.723  1.00 25.72 ? 123 LEU D CG  1 
ATOM   3462 C  CD1 . LEU D 2 120 ? 0.094   15.929  27.334  1.00 21.40 ? 123 LEU D CD1 1 
ATOM   3463 C  CD2 . LEU D 2 120 ? 1.462   17.356  28.854  1.00 25.69 ? 123 LEU D CD2 1 
ATOM   3464 N  N   . PRO D 2 121 ? 3.583   19.745  25.330  1.00 30.39 ? 124 PRO D N   1 
ATOM   3465 C  CA  . PRO D 2 121 ? 4.224   20.456  24.219  1.00 36.71 ? 124 PRO D CA  1 
ATOM   3466 C  C   . PRO D 2 121 ? 3.750   19.976  22.855  1.00 38.67 ? 124 PRO D C   1 
ATOM   3467 O  O   . PRO D 2 121 ? 3.421   18.805  22.655  1.00 40.38 ? 124 PRO D O   1 
ATOM   3468 C  CB  . PRO D 2 121 ? 5.713   20.138  24.411  1.00 34.88 ? 124 PRO D CB  1 
ATOM   3469 C  CG  . PRO D 2 121 ? 5.710   18.790  25.055  1.00 28.46 ? 124 PRO D CG  1 
ATOM   3470 C  CD  . PRO D 2 121 ? 4.475   18.736  25.929  1.00 29.24 ? 124 PRO D CD  1 
ATOM   3471 N  N   . ASP D 2 122 ? 3.678   20.924  21.919  1.00 41.53 ? 125 ASP D N   1 
ATOM   3472 C  CA  . ASP D 2 122 ? 3.540   20.621  20.496  1.00 43.19 ? 125 ASP D CA  1 
ATOM   3473 C  C   . ASP D 2 122 ? 4.913   20.285  19.911  1.00 44.19 ? 125 ASP D C   1 
ATOM   3474 O  O   . ASP D 2 122 ? 5.943   20.335  20.599  1.00 42.52 ? 125 ASP D O   1 
ATOM   3475 C  CB  . ASP D 2 122 ? 2.921   21.806  19.751  1.00 40.30 ? 125 ASP D CB  1 
ATOM   3476 C  CG  . ASP D 2 122 ? 3.739   23.075  19.918  1.00 43.28 ? 125 ASP D CG  1 
ATOM   3477 O  OD1 . ASP D 2 122 ? 3.736   23.634  21.037  1.00 48.60 ? 125 ASP D OD1 1 
ATOM   3478 O  OD2 . ASP D 2 122 ? 4.416   23.495  18.959  1.00 41.26 ? 125 ASP D OD2 1 
ATOM   3479 N  N   . ARG D 2 123 ? 4.946   19.974  18.611  1.00 40.66 ? 126 ARG D N   1 
ATOM   3480 C  CA  . ARG D 2 123 ? 6.209   19.555  18.007  1.00 44.24 ? 126 ARG D CA  1 
ATOM   3481 C  C   . ARG D 2 123 ? 7.233   20.691  17.996  1.00 41.62 ? 126 ARG D C   1 
ATOM   3482 O  O   . ARG D 2 123 ? 8.385   20.501  18.405  1.00 39.99 ? 126 ARG D O   1 
ATOM   3483 C  CB  . ARG D 2 123 ? 5.975   19.020  16.598  1.00 45.58 ? 126 ARG D CB  1 
ATOM   3484 C  CG  . ARG D 2 123 ? 7.254   18.542  15.931  1.00 38.09 ? 126 ARG D CG  1 
ATOM   3485 C  CD  . ARG D 2 123 ? 6.940   17.854  14.626  1.00 43.00 ? 126 ARG D CD  1 
ATOM   3486 N  NE  . ARG D 2 123 ? 7.198   16.419  14.670  1.00 52.42 ? 126 ARG D NE  1 
ATOM   3487 C  CZ  . ARG D 2 123 ? 6.262   15.480  14.615  1.00 53.82 ? 126 ARG D CZ  1 
ATOM   3488 N  NH1 . ARG D 2 123 ? 4.974   15.789  14.523  1.00 50.23 ? 126 ARG D NH1 1 
ATOM   3489 N  NH2 . ARG D 2 123 ? 6.628   14.199  14.611  1.00 51.39 ? 126 ARG D NH2 1 
ATOM   3490 N  N   . GLU D 2 124 ? 6.834   21.880  17.534  1.00 41.05 ? 127 GLU D N   1 
ATOM   3491 C  CA  . GLU D 2 124 ? 7.779   22.995  17.462  1.00 48.65 ? 127 GLU D CA  1 
ATOM   3492 C  C   . GLU D 2 124 ? 8.335   23.340  18.842  1.00 44.05 ? 127 GLU D C   1 
ATOM   3493 O  O   . GLU D 2 124 ? 9.554   23.519  19.009  1.00 40.29 ? 127 GLU D O   1 
ATOM   3494 C  CB  . GLU D 2 124 ? 7.118   24.222  16.815  1.00 47.79 ? 127 GLU D CB  1 
ATOM   3495 C  CG  . GLU D 2 124 ? 7.362   24.349  15.310  1.00 53.04 ? 127 GLU D CG  1 
ATOM   3496 C  CD  . GLU D 2 124 ? 8.513   25.306  14.971  1.00 61.08 ? 127 GLU D CD  1 
ATOM   3497 O  OE1 . GLU D 2 124 ? 8.743   26.238  15.779  1.00 68.50 ? 127 GLU D OE1 1 
ATOM   3498 O  OE2 . GLU D 2 124 ? 9.180   25.134  13.908  1.00 50.74 ? 127 GLU D OE2 1 
ATOM   3499 N  N   . THR D 2 125 ? 7.458   23.422  19.849  1.00 42.01 ? 128 THR D N   1 
ATOM   3500 C  CA  . THR D 2 125 ? 7.927   23.733  21.198  1.00 41.87 ? 128 THR D CA  1 
ATOM   3501 C  C   . THR D 2 125 ? 8.925   22.689  21.679  1.00 41.67 ? 128 THR D C   1 
ATOM   3502 O  O   . THR D 2 125 ? 10.008  23.031  22.179  1.00 41.02 ? 128 THR D O   1 
ATOM   3503 C  CB  . THR D 2 125 ? 6.762   23.830  22.177  1.00 37.65 ? 128 THR D CB  1 
ATOM   3504 O  OG1 . THR D 2 125 ? 5.775   24.741  21.685  1.00 43.08 ? 128 THR D OG1 1 
ATOM   3505 C  CG2 . THR D 2 125 ? 7.260   24.342  23.497  1.00 40.24 ? 128 THR D CG2 1 
ATOM   3506 N  N   . ALA D 2 126 ? 8.593   21.408  21.492  1.00 34.69 ? 129 ALA D N   1 
ATOM   3507 C  CA  . ALA D 2 126 ? 9.481   20.352  21.957  1.00 36.28 ? 129 ALA D CA  1 
ATOM   3508 C  C   . ALA D 2 126 ? 10.830  20.404  21.255  1.00 37.68 ? 129 ALA D C   1 
ATOM   3509 O  O   . ALA D 2 126 ? 11.873  20.216  21.889  1.00 38.85 ? 129 ALA D O   1 
ATOM   3510 C  CB  . ALA D 2 126 ? 8.828   18.985  21.761  1.00 38.02 ? 129 ALA D CB  1 
ATOM   3511 N  N   . ALA D 2 127 A 10.835  20.659  19.948  1.00 38.76 ? 129 ALA D N   1 
ATOM   3512 C  CA  . ALA D 2 127 A 12.103  20.711  19.229  1.00 41.51 ? 129 ALA D CA  1 
ATOM   3513 C  C   . ALA D 2 127 A 12.933  21.911  19.671  1.00 39.68 ? 129 ALA D C   1 
ATOM   3514 O  O   . ALA D 2 127 A 14.165  21.822  19.745  1.00 34.96 ? 129 ALA D O   1 
ATOM   3515 C  CB  . ALA D 2 127 A 11.859  20.738  17.714  1.00 38.48 ? 129 ALA D CB  1 
ATOM   3516 N  N   . SER D 2 128 B 12.267  23.040  19.972  1.00 41.30 ? 129 SER D N   1 
ATOM   3517 C  CA  . SER D 2 128 B 12.969  24.270  20.348  1.00 36.26 ? 129 SER D CA  1 
ATOM   3518 C  C   . SER D 2 128 B 13.545  24.202  21.755  1.00 35.77 ? 129 SER D C   1 
ATOM   3519 O  O   . SER D 2 128 B 14.634  24.728  22.004  1.00 36.00 ? 129 SER D O   1 
ATOM   3520 C  CB  . SER D 2 128 B 12.028  25.459  20.228  1.00 35.63 ? 129 SER D CB  1 
ATOM   3521 O  OG  . SER D 2 128 B 11.571  25.572  18.895  1.00 43.15 ? 129 SER D OG  1 
ATOM   3522 N  N   . LEU D 2 129 C 12.830  23.580  22.694  1.00 35.90 ? 129 LEU D N   1 
ATOM   3523 C  CA  . LEU D 2 129 C 13.211  23.613  24.101  1.00 35.05 ? 129 LEU D CA  1 
ATOM   3524 C  C   . LEU D 2 129 C 14.004  22.391  24.554  1.00 35.54 ? 129 LEU D C   1 
ATOM   3525 O  O   . LEU D 2 129 C 14.857  22.517  25.437  1.00 35.18 ? 129 LEU D O   1 
ATOM   3526 C  CB  . LEU D 2 129 C 11.961  23.750  24.978  1.00 36.93 ? 129 LEU D CB  1 
ATOM   3527 C  CG  . LEU D 2 129 C 11.007  24.900  24.637  1.00 31.83 ? 129 LEU D CG  1 
ATOM   3528 C  CD1 . LEU D 2 129 C 9.928   24.998  25.686  1.00 34.25 ? 129 LEU D CD1 1 
ATOM   3529 C  CD2 . LEU D 2 129 C 11.747  26.223  24.516  1.00 30.10 ? 129 LEU D CD2 1 
ATOM   3530 N  N   . LEU D 2 130 ? 13.761  21.214  23.977  1.00 32.56 ? 130 LEU D N   1 
ATOM   3531 C  CA  . LEU D 2 130 ? 14.477  20.006  24.382  1.00 33.06 ? 130 LEU D CA  1 
ATOM   3532 C  C   . LEU D 2 130 ? 15.858  19.952  23.724  1.00 36.49 ? 130 LEU D C   1 
ATOM   3533 O  O   . LEU D 2 130 ? 16.134  19.141  22.836  1.00 38.80 ? 130 LEU D O   1 
ATOM   3534 C  CB  . LEU D 2 130 ? 13.669  18.767  24.036  1.00 40.89 ? 130 LEU D CB  1 
ATOM   3535 C  CG  . LEU D 2 130 ? 12.897  18.068  25.150  1.00 39.88 ? 130 LEU D CG  1 
ATOM   3536 C  CD1 . LEU D 2 130 ? 12.711  16.607  24.762  1.00 33.23 ? 130 LEU D CD1 1 
ATOM   3537 C  CD2 . LEU D 2 130 ? 13.617  18.198  26.478  1.00 28.34 ? 130 LEU D CD2 1 
ATOM   3538 N  N   . GLN D 2 131 ? 16.737  20.854  24.159  1.00 34.74 ? 131 GLN D N   1 
ATOM   3539 C  CA  . GLN D 2 131 ? 18.068  20.960  23.574  1.00 36.13 ? 131 GLN D CA  1 
ATOM   3540 C  C   . GLN D 2 131 ? 19.123  21.002  24.664  1.00 33.20 ? 131 GLN D C   1 
ATOM   3541 O  O   . GLN D 2 131 ? 18.924  21.662  25.687  1.00 35.73 ? 131 GLN D O   1 
ATOM   3542 C  CB  . GLN D 2 131 ? 18.179  22.197  22.698  1.00 37.53 ? 131 GLN D CB  1 
ATOM   3543 C  CG  . GLN D 2 131 ? 17.296  22.149  21.478  1.00 40.07 ? 131 GLN D CG  1 
ATOM   3544 C  CD  . GLN D 2 131 ? 17.697  23.174  20.448  1.00 37.42 ? 131 GLN D CD  1 
ATOM   3545 O  OE1 . GLN D 2 131 ? 18.667  22.989  19.735  1.00 43.24 ? 131 GLN D OE1 1 
ATOM   3546 N  NE2 . GLN D 2 131 ? 16.954  24.262  20.374  1.00 37.09 ? 131 GLN D NE2 1 
ATOM   3547 N  N   . ALA D 2 132 ? 20.243  20.308  24.439  1.00 30.57 ? 132 ALA D N   1 
ATOM   3548 C  CA  . ALA D 2 132 ? 21.348  20.302  25.399  1.00 33.64 ? 132 ALA D CA  1 
ATOM   3549 C  C   . ALA D 2 132 ? 21.730  21.718  25.833  1.00 33.33 ? 132 ALA D C   1 
ATOM   3550 O  O   . ALA D 2 132 ? 21.771  22.648  25.024  1.00 33.47 ? 132 ALA D O   1 
ATOM   3551 C  CB  . ALA D 2 132 ? 22.563  19.593  24.792  1.00 33.33 ? 132 ALA D CB  1 
ATOM   3552 N  N   . GLY D 2 133 ? 22.025  21.870  27.125  1.00 31.62 ? 133 GLY D N   1 
ATOM   3553 C  CA  . GLY D 2 133 ? 22.303  23.150  27.738  1.00 27.81 ? 133 GLY D CA  1 
ATOM   3554 C  C   . GLY D 2 133 ? 21.086  23.912  28.249  1.00 30.59 ? 133 GLY D C   1 
ATOM   3555 O  O   . GLY D 2 133 ? 21.208  24.658  29.226  1.00 34.52 ? 133 GLY D O   1 
ATOM   3556 N  N   . TYR D 2 134 ? 19.916  23.735  27.641  1.00 26.94 ? 134 TYR D N   1 
ATOM   3557 C  CA  . TYR D 2 134 ? 18.716  24.382  28.161  1.00 31.47 ? 134 TYR D CA  1 
ATOM   3558 C  C   . TYR D 2 134 ? 18.275  23.747  29.477  1.00 32.27 ? 134 TYR D C   1 
ATOM   3559 O  O   . TYR D 2 134 ? 18.363  22.531  29.665  1.00 30.92 ? 134 TYR D O   1 
ATOM   3560 C  CB  . TYR D 2 134 ? 17.574  24.311  27.154  1.00 32.32 ? 134 TYR D CB  1 
ATOM   3561 C  CG  . TYR D 2 134 ? 17.791  25.116  25.895  1.00 38.10 ? 134 TYR D CG  1 
ATOM   3562 C  CD1 . TYR D 2 134 ? 19.013  25.728  25.626  1.00 36.98 ? 134 TYR D CD1 1 
ATOM   3563 C  CD2 . TYR D 2 134 ? 16.771  25.263  24.969  1.00 35.43 ? 134 TYR D CD2 1 
ATOM   3564 C  CE1 . TYR D 2 134 ? 19.201  26.451  24.473  1.00 34.61 ? 134 TYR D CE1 1 
ATOM   3565 C  CE2 . TYR D 2 134 ? 16.958  25.990  23.818  1.00 35.75 ? 134 TYR D CE2 1 
ATOM   3566 C  CZ  . TYR D 2 134 ? 18.174  26.575  23.574  1.00 34.44 ? 134 TYR D CZ  1 
ATOM   3567 O  OH  . TYR D 2 134 ? 18.347  27.284  22.418  1.00 36.68 ? 134 TYR D OH  1 
ATOM   3568 N  N   . LYS D 2 135 ? 17.775  24.574  30.388  1.00 32.96 ? 135 LYS D N   1 
ATOM   3569 C  CA  . LYS D 2 135 ? 17.444  24.124  31.729  1.00 30.28 ? 135 LYS D CA  1 
ATOM   3570 C  C   . LYS D 2 135 ? 15.945  23.918  31.861  1.00 29.44 ? 135 LYS D C   1 
ATOM   3571 O  O   . LYS D 2 135 ? 15.148  24.725  31.367  1.00 25.90 ? 135 LYS D O   1 
ATOM   3572 C  CB  . LYS D 2 135 ? 17.940  25.120  32.779  1.00 29.76 ? 135 LYS D CB  1 
ATOM   3573 C  CG  . LYS D 2 135 ? 19.453  25.116  32.912  1.00 33.60 ? 135 LYS D CG  1 
ATOM   3574 C  CD  . LYS D 2 135 ? 19.962  26.131  33.916  1.00 34.25 ? 135 LYS D CD  1 
ATOM   3575 C  CE  . LYS D 2 135 ? 21.468  26.022  34.050  1.00 30.95 ? 135 LYS D CE  1 
ATOM   3576 N  NZ  . LYS D 2 135 ? 22.028  27.027  34.996  1.00 35.46 ? 135 LYS D NZ  1 
ATOM   3577 N  N   . GLY D 2 136 ? 15.576  22.817  32.511  1.00 31.98 ? 136 GLY D N   1 
ATOM   3578 C  CA  . GLY D 2 136 ? 14.207  22.564  32.910  1.00 28.33 ? 136 GLY D CA  1 
ATOM   3579 C  C   . GLY D 2 136 ? 14.128  22.458  34.418  1.00 26.92 ? 136 GLY D C   1 
ATOM   3580 O  O   . GLY D 2 136 ? 15.136  22.561  35.124  1.00 25.12 ? 136 GLY D O   1 
ATOM   3581 N  N   . ARG D 2 137 ? 12.905  22.234  34.906  1.00 26.22 ? 137 ARG D N   1 
ATOM   3582 C  CA  . ARG D 2 137 ? 12.665  22.272  36.343  1.00 27.93 ? 137 ARG D CA  1 
ATOM   3583 C  C   . ARG D 2 137 ? 12.003  20.978  36.783  1.00 27.84 ? 137 ARG D C   1 
ATOM   3584 O  O   . ARG D 2 137 ? 11.086  20.490  36.116  1.00 25.22 ? 137 ARG D O   1 
ATOM   3585 C  CB  . ARG D 2 137 ? 11.796  23.470  36.721  1.00 25.54 ? 137 ARG D CB  1 
ATOM   3586 C  CG  . ARG D 2 137 ? 11.344  23.483  38.160  1.00 28.53 ? 137 ARG D CG  1 
ATOM   3587 C  CD  . ARG D 2 137 ? 10.434  24.678  38.425  1.00 28.60 ? 137 ARG D CD  1 
ATOM   3588 N  NE  . ARG D 2 137 ? 11.206  25.915  38.474  1.00 33.46 ? 137 ARG D NE  1 
ATOM   3589 C  CZ  . ARG D 2 137 ? 10.683  27.133  38.574  1.00 35.53 ? 137 ARG D CZ  1 
ATOM   3590 N  NH1 . ARG D 2 137 ? 9.368   27.324  38.631  1.00 32.41 ? 137 ARG D NH1 1 
ATOM   3591 N  NH2 . ARG D 2 137 ? 11.499  28.189  38.593  1.00 31.37 ? 137 ARG D NH2 1 
ATOM   3592 N  N   . VAL D 2 138 ? 12.494  20.417  37.891  1.00 27.32 ? 138 VAL D N   1 
ATOM   3593 C  CA  . VAL D 2 138 ? 12.006  19.159  38.446  1.00 31.18 ? 138 VAL D CA  1 
ATOM   3594 C  C   . VAL D 2 138 ? 11.565  19.387  39.883  1.00 32.65 ? 138 VAL D C   1 
ATOM   3595 O  O   . VAL D 2 138 ? 12.247  20.074  40.657  1.00 29.15 ? 138 VAL D O   1 
ATOM   3596 C  CB  . VAL D 2 138 ? 13.057  18.038  38.405  1.00 27.17 ? 138 VAL D CB  1 
ATOM   3597 C  CG1 . VAL D 2 138 ? 12.366  16.690  38.623  1.00 24.71 ? 138 VAL D CG1 1 
ATOM   3598 C  CG2 . VAL D 2 138 ? 13.797  18.070  37.094  1.00 27.81 ? 138 VAL D CG2 1 
ATOM   3599 N  N   . THR D 2 139 ? 10.431  18.783  40.236  1.00 31.51 ? 139 THR D N   1 
ATOM   3600 C  CA  . THR D 2 139 ? 9.783   18.987  41.525  1.00 35.62 ? 139 THR D CA  1 
ATOM   3601 C  C   . THR D 2 139 ? 9.326   17.649  42.077  1.00 37.49 ? 139 THR D C   1 
ATOM   3602 O  O   . THR D 2 139 ? 8.918   16.765  41.312  1.00 34.21 ? 139 THR D O   1 
ATOM   3603 C  CB  . THR D 2 139 ? 8.583   19.905  41.399  1.00 32.53 ? 139 THR D CB  1 
ATOM   3604 O  OG1 . THR D 2 139 ? 7.801   19.487  40.266  1.00 31.72 ? 139 THR D OG1 1 
ATOM   3605 C  CG2 . THR D 2 139 ? 9.055   21.340  41.231  1.00 28.38 ? 139 THR D CG2 1 
ATOM   3606 N  N   . GLY D 2 140 ? 9.417   17.505  43.396  1.00 29.63 ? 140 GLY D N   1 
ATOM   3607 C  CA  . GLY D 2 140 ? 8.957   16.279  44.030  1.00 28.76 ? 140 GLY D CA  1 
ATOM   3608 C  C   . GLY D 2 140 ? 9.151   16.309  45.535  1.00 36.04 ? 140 GLY D C   1 
ATOM   3609 O  O   . GLY D 2 140 ? 9.849   17.175  46.084  1.00 33.69 ? 140 GLY D O   1 
ATOM   3610 N  N   . TRP D 2 141 ? 8.480   15.354  46.195  1.00 32.68 ? 141 TRP D N   1 
ATOM   3611 C  CA  . TRP D 2 141 ? 8.624   15.063  47.616  1.00 28.91 ? 141 TRP D CA  1 
ATOM   3612 C  C   . TRP D 2 141 ? 9.510   13.851  47.885  1.00 32.21 ? 141 TRP D C   1 
ATOM   3613 O  O   . TRP D 2 141 ? 9.428   13.268  48.971  1.00 34.10 ? 141 TRP D O   1 
ATOM   3614 C  CB  . TRP D 2 141 ? 7.255   14.840  48.261  1.00 31.33 ? 141 TRP D CB  1 
ATOM   3615 C  CG  . TRP D 2 141 ? 6.471   16.093  48.535  1.00 34.77 ? 141 TRP D CG  1 
ATOM   3616 C  CD1 . TRP D 2 141 ? 6.620   16.941  49.599  1.00 35.10 ? 141 TRP D CD1 1 
ATOM   3617 C  CD2 . TRP D 2 141 ? 5.410   16.633  47.738  1.00 31.96 ? 141 TRP D CD2 1 
ATOM   3618 N  NE1 . TRP D 2 141 ? 5.723   17.979  49.508  1.00 34.43 ? 141 TRP D NE1 1 
ATOM   3619 C  CE2 . TRP D 2 141 ? 4.965   17.813  48.379  1.00 32.63 ? 141 TRP D CE2 1 
ATOM   3620 C  CE3 . TRP D 2 141 ? 4.795   16.235  46.546  1.00 26.52 ? 141 TRP D CE3 1 
ATOM   3621 C  CZ2 . TRP D 2 141 ? 3.925   18.596  47.870  1.00 35.87 ? 141 TRP D CZ2 1 
ATOM   3622 C  CZ3 . TRP D 2 141 ? 3.776   17.003  46.041  1.00 31.81 ? 141 TRP D CZ3 1 
ATOM   3623 C  CH2 . TRP D 2 141 ? 3.335   18.175  46.709  1.00 37.21 ? 141 TRP D CH2 1 
ATOM   3624 N  N   . GLY D 2 142 ? 10.298  13.419  46.902  1.00 31.33 ? 142 GLY D N   1 
ATOM   3625 C  CA  . GLY D 2 142 ? 11.196  12.295  47.080  1.00 30.25 ? 142 GLY D CA  1 
ATOM   3626 C  C   . GLY D 2 142 ? 12.380  12.613  47.997  1.00 33.82 ? 142 GLY D C   1 
ATOM   3627 O  O   . GLY D 2 142 ? 12.547  13.714  48.519  1.00 32.90 ? 142 GLY D O   1 
ATOM   3628 N  N   . ASN D 2 143 ? 13.235  11.607  48.168  1.00 38.33 ? 143 ASN D N   1 
ATOM   3629 C  CA  . ASN D 2 143 ? 14.356  11.699  49.102  1.00 43.11 ? 143 ASN D CA  1 
ATOM   3630 C  C   . ASN D 2 143 ? 15.293  12.851  48.766  1.00 41.89 ? 143 ASN D C   1 
ATOM   3631 O  O   . ASN D 2 143 ? 15.559  13.144  47.594  1.00 40.77 ? 143 ASN D O   1 
ATOM   3632 C  CB  . ASN D 2 143 ? 15.144  10.388  49.105  1.00 40.26 ? 143 ASN D CB  1 
ATOM   3633 C  CG  . ASN D 2 143 ? 14.337  9.250   49.655  1.00 39.24 ? 143 ASN D CG  1 
ATOM   3634 O  OD1 . ASN D 2 143 ? 13.327  9.466   50.346  1.00 40.28 ? 143 ASN D OD1 1 
ATOM   3635 N  ND2 . ASN D 2 143 ? 14.747  8.034   49.342  1.00 35.51 ? 143 ASN D ND2 1 
ATOM   3636 N  N   . LEU D 2 144 ? 15.823  13.479  49.816  1.00 42.40 ? 144 LEU D N   1 
ATOM   3637 C  CA  . LEU D 2 144 ? 16.774  14.566  49.664  1.00 37.42 ? 144 LEU D CA  1 
ATOM   3638 C  C   . LEU D 2 144 ? 18.195  14.076  49.408  1.00 39.15 ? 144 LEU D C   1 
ATOM   3639 O  O   . LEU D 2 144 ? 19.022  14.848  48.911  1.00 41.31 ? 144 LEU D O   1 
ATOM   3640 C  CB  . LEU D 2 144 ? 16.738  15.456  50.908  1.00 37.15 ? 144 LEU D CB  1 
ATOM   3641 C  CG  . LEU D 2 144 ? 15.448  16.234  51.193  1.00 42.81 ? 144 LEU D CG  1 
ATOM   3642 C  CD1 . LEU D 2 144 ? 15.463  16.822  52.590  1.00 40.02 ? 144 LEU D CD1 1 
ATOM   3643 C  CD2 . LEU D 2 144 ? 15.229  17.343  50.172  1.00 39.05 ? 144 LEU D CD2 1 
ATOM   3644 N  N   . LYS D 2 145 ? 18.510  12.830  49.751  1.00 46.00 ? 145 LYS D N   1 
ATOM   3645 C  CA  . LYS D 2 145 ? 19.829  12.275  49.461  1.00 49.97 ? 145 LYS D CA  1 
ATOM   3646 C  C   . LYS D 2 145 ? 19.686  10.797  49.130  1.00 46.15 ? 145 LYS D C   1 
ATOM   3647 O  O   . LYS D 2 145 ? 18.719  10.143  49.525  1.00 46.81 ? 145 LYS D O   1 
ATOM   3648 C  CB  . LYS D 2 145 ? 20.804  12.462  50.643  1.00 48.72 ? 145 LYS D CB  1 
ATOM   3649 C  CG  . LYS D 2 145 ? 22.309  12.355  50.288  1.00 56.08 ? 145 LYS D CG  1 
ATOM   3650 C  CD  . LYS D 2 145 ? 22.645  13.026  48.942  1.00 56.69 ? 145 LYS D CD  1 
ATOM   3651 C  CE  . LYS D 2 145 ? 23.257  14.431  49.128  1.00 55.42 ? 145 LYS D CE  1 
ATOM   3652 N  NZ  . LYS D 2 145 ? 24.074  14.878  47.951  1.00 46.43 ? 145 LYS D NZ  1 
ATOM   3653 N  N   . GLU D 2 146 ? 20.671  10.281  48.397  1.00 49.02 ? 146 GLU D N   1 
ATOM   3654 C  CA  . GLU D 2 146 ? 20.833  8.842   48.223  1.00 49.21 ? 146 GLU D CA  1 
ATOM   3655 C  C   . GLU D 2 146 ? 21.101  8.208   49.587  1.00 56.44 ? 146 GLU D C   1 
ATOM   3656 O  O   . GLU D 2 146 ? 22.021  8.625   50.298  1.00 60.15 ? 146 GLU D O   1 
ATOM   3657 C  CB  . GLU D 2 146 ? 21.990  8.597   47.253  1.00 45.39 ? 146 GLU D CB  1 
ATOM   3658 C  CG  . GLU D 2 146 ? 22.367  7.171   46.952  1.00 45.35 ? 146 GLU D CG  1 
ATOM   3659 C  CD  . GLU D 2 146 ? 23.476  7.114   45.918  1.00 43.16 ? 146 GLU D CD  1 
ATOM   3660 O  OE1 . GLU D 2 146 ? 23.465  7.957   45.005  1.00 41.63 ? 146 GLU D OE1 1 
ATOM   3661 O  OE2 . GLU D 2 146 ? 24.372  6.250   46.012  1.00 46.43 ? 146 GLU D OE2 1 
ATOM   3662 N  N   . THR D 2 147 ? 20.301  7.202   49.947  1.00 60.14 ? 147 THR D N   1 
ATOM   3663 C  CA  . THR D 2 147 ? 20.281  6.637   51.311  1.00 79.77 ? 147 THR D CA  1 
ATOM   3664 C  C   . THR D 2 147 ? 21.631  6.647   52.043  1.00 87.15 ? 147 THR D C   1 
ATOM   3665 O  O   . THR D 2 147 ? 21.980  7.640   52.700  1.00 78.98 ? 147 THR D O   1 
ATOM   3666 C  CB  . THR D 2 147 ? 19.765  5.160   51.307  1.00 89.45 ? 147 THR D CB  1 
ATOM   3667 O  OG1 . THR D 2 147 ? 18.392  5.115   50.898  1.00 96.67 ? 147 THR D OG1 1 
ATOM   3668 C  CG2 . THR D 2 147 ? 19.900  4.523   52.692  1.00 86.07 ? 147 THR D CG2 1 
ATOM   3669 N  N   . GLY D 2 155 ? 15.426  12.827  55.928  1.00 61.35 ? 150 GLY D N   1 
ATOM   3670 C  CA  . GLY D 2 155 ? 15.593  12.374  54.557  1.00 57.57 ? 150 GLY D CA  1 
ATOM   3671 C  C   . GLY D 2 155 ? 14.426  12.669  53.616  1.00 58.86 ? 150 GLY D C   1 
ATOM   3672 O  O   . GLY D 2 155 ? 14.569  12.611  52.385  1.00 49.32 ? 150 GLY D O   1 
ATOM   3673 N  N   . GLN D 2 156 ? 13.253  12.953  54.183  1.00 54.42 ? 151 GLN D N   1 
ATOM   3674 C  CA  . GLN D 2 156 ? 12.097  13.301  53.375  1.00 49.87 ? 151 GLN D CA  1 
ATOM   3675 C  C   . GLN D 2 156 ? 11.747  14.761  53.605  1.00 49.49 ? 151 GLN D C   1 
ATOM   3676 O  O   . GLN D 2 156 ? 11.611  15.184  54.761  1.00 49.36 ? 151 GLN D O   1 
ATOM   3677 C  CB  . GLN D 2 156 ? 10.889  12.414  53.702  1.00 51.02 ? 151 GLN D CB  1 
ATOM   3678 C  CG  . GLN D 2 156 ? 11.233  11.032  54.223  1.00 61.11 ? 151 GLN D CG  1 
ATOM   3679 C  CD  . GLN D 2 156 ? 10.001  10.144  54.374  1.00 67.84 ? 151 GLN D CD  1 
ATOM   3680 O  OE1 . GLN D 2 156 ? 9.093   10.437  55.157  1.00 66.43 ? 151 GLN D OE1 1 
ATOM   3681 N  NE2 . GLN D 2 156 ? 9.969   9.051   53.623  1.00 69.78 ? 151 GLN D NE2 1 
ATOM   3682 N  N   . PRO D 2 157 ? 11.602  15.564  52.557  1.00 47.62 ? 152 PRO D N   1 
ATOM   3683 C  CA  . PRO D 2 157 ? 11.387  16.996  52.770  1.00 44.77 ? 152 PRO D CA  1 
ATOM   3684 C  C   . PRO D 2 157 ? 10.019  17.247  53.365  1.00 46.27 ? 152 PRO D C   1 
ATOM   3685 O  O   . PRO D 2 157 ? 9.090   16.450  53.212  1.00 48.17 ? 152 PRO D O   1 
ATOM   3686 C  CB  . PRO D 2 157 ? 11.493  17.588  51.367  1.00 39.40 ? 152 PRO D CB  1 
ATOM   3687 C  CG  . PRO D 2 157 ? 11.037  16.470  50.487  1.00 42.29 ? 152 PRO D CG  1 
ATOM   3688 C  CD  . PRO D 2 157 ? 11.499  15.194  51.138  1.00 40.08 ? 152 PRO D CD  1 
ATOM   3689 N  N   . SER D 2 158 ? 9.911   18.377  54.058  1.00 46.53 ? 153 SER D N   1 
ATOM   3690 C  CA  . SER D 2 158 ? 8.644   18.795  54.637  1.00 46.90 ? 153 SER D CA  1 
ATOM   3691 C  C   . SER D 2 158 ? 7.764   19.491  53.610  1.00 48.20 ? 153 SER D C   1 
ATOM   3692 O  O   . SER D 2 158 ? 6.542   19.293  53.591  1.00 48.57 ? 153 SER D O   1 
ATOM   3693 C  CB  . SER D 2 158 ? 8.916   19.730  55.806  1.00 48.43 ? 153 SER D CB  1 
ATOM   3694 O  OG  . SER D 2 158 ? 9.872   20.697  55.401  1.00 46.67 ? 153 SER D OG  1 
ATOM   3695 N  N   . VAL D 2 159 ? 8.371   20.309  52.755  1.00 42.96 ? 154 VAL D N   1 
ATOM   3696 C  CA  . VAL D 2 159 ? 7.646   21.007  51.712  1.00 37.12 ? 154 VAL D CA  1 
ATOM   3697 C  C   . VAL D 2 159 ? 8.273   20.616  50.387  1.00 32.93 ? 154 VAL D C   1 
ATOM   3698 O  O   . VAL D 2 159 ? 9.431   20.186  50.320  1.00 34.59 ? 154 VAL D O   1 
ATOM   3699 C  CB  . VAL D 2 159 ? 7.661   22.535  51.924  1.00 39.20 ? 154 VAL D CB  1 
ATOM   3700 C  CG1 . VAL D 2 159 ? 7.406   22.856  53.378  1.00 33.79 ? 154 VAL D CG1 1 
ATOM   3701 C  CG2 . VAL D 2 159 ? 8.972   23.114  51.514  1.00 35.85 ? 154 VAL D CG2 1 
ATOM   3702 N  N   . LEU D 2 160 ? 7.466   20.748  49.332  1.00 35.70 ? 155 LEU D N   1 
ATOM   3703 C  CA  . LEU D 2 160 ? 7.828   20.367  47.968  1.00 32.13 ? 155 LEU D CA  1 
ATOM   3704 C  C   . LEU D 2 160 ? 9.209   20.886  47.562  1.00 35.03 ? 155 LEU D C   1 
ATOM   3705 O  O   . LEU D 2 160 ? 9.575   22.031  47.850  1.00 32.01 ? 155 LEU D O   1 
ATOM   3706 C  CB  . LEU D 2 160 ? 6.766   20.915  47.015  1.00 35.38 ? 155 LEU D CB  1 
ATOM   3707 C  CG  . LEU D 2 160 ? 6.934   20.582  45.539  1.00 33.49 ? 155 LEU D CG  1 
ATOM   3708 C  CD1 . LEU D 2 160 ? 7.079   19.080  45.417  1.00 34.47 ? 155 LEU D CD1 1 
ATOM   3709 C  CD2 . LEU D 2 160 ? 5.729   21.080  44.764  1.00 27.88 ? 155 LEU D CD2 1 
ATOM   3710 N  N   . GLN D 2 161 ? 9.991   20.033  46.908  1.00 29.24 ? 156 GLN D N   1 
ATOM   3711 C  CA  . GLN D 2 161 ? 11.322  20.438  46.484  1.00 30.65 ? 156 GLN D CA  1 
ATOM   3712 C  C   . GLN D 2 161 ? 11.388  20.712  44.982  1.00 32.45 ? 156 GLN D C   1 
ATOM   3713 O  O   . GLN D 2 161 ? 10.701  20.078  44.168  1.00 31.28 ? 156 GLN D O   1 
ATOM   3714 C  CB  . GLN D 2 161 ? 12.352  19.380  46.865  1.00 29.81 ? 156 GLN D CB  1 
ATOM   3715 C  CG  . GLN D 2 161 ? 12.523  19.204  48.348  1.00 31.15 ? 156 GLN D CG  1 
ATOM   3716 C  CD  . GLN D 2 161 ? 13.122  20.425  49.007  1.00 33.68 ? 156 GLN D CD  1 
ATOM   3717 O  OE1 . GLN D 2 161 ? 14.320  20.687  48.881  1.00 34.80 ? 156 GLN D OE1 1 
ATOM   3718 N  NE2 . GLN D 2 161 ? 12.284  21.197  49.692  1.00 29.83 ? 156 GLN D NE2 1 
ATOM   3719 N  N   . VAL D 2 162 ? 12.282  21.625  44.623  1.00 33.61 ? 157 VAL D N   1 
ATOM   3720 C  CA  . VAL D 2 162 ? 12.412  22.105  43.255  1.00 31.02 ? 157 VAL D CA  1 
ATOM   3721 C  C   . VAL D 2 162 ? 13.894  22.278  42.931  1.00 30.08 ? 157 VAL D C   1 
ATOM   3722 O  O   . VAL D 2 162 ? 14.688  22.670  43.790  1.00 28.84 ? 157 VAL D O   1 
ATOM   3723 C  CB  . VAL D 2 162 ? 11.617  23.412  43.071  1.00 27.55 ? 157 VAL D CB  1 
ATOM   3724 C  CG1 . VAL D 2 162 ? 12.072  24.447  44.067  1.00 29.96 ? 157 VAL D CG1 1 
ATOM   3725 C  CG2 . VAL D 2 162 ? 11.758  23.915  41.687  1.00 27.29 ? 157 VAL D CG2 1 
ATOM   3726 N  N   . VAL D 2 163 ? 14.265  21.954  41.692  1.00 30.78 ? 158 VAL D N   1 
ATOM   3727 C  CA  . VAL D 2 163 ? 15.640  22.086  41.224  1.00 30.07 ? 158 VAL D CA  1 
ATOM   3728 C  C   . VAL D 2 163 ? 15.610  22.263  39.704  1.00 34.77 ? 158 VAL D C   1 
ATOM   3729 O  O   . VAL D 2 163 ? 14.804  21.632  39.012  1.00 31.56 ? 158 VAL D O   1 
ATOM   3730 C  CB  . VAL D 2 163 ? 16.508  20.872  41.651  1.00 31.76 ? 158 VAL D CB  1 
ATOM   3731 C  CG1 . VAL D 2 163 ? 16.068  19.592  40.945  1.00 33.30 ? 158 VAL D CG1 1 
ATOM   3732 C  CG2 . VAL D 2 163 ? 17.986  21.122  41.370  1.00 31.13 ? 158 VAL D CG2 1 
ATOM   3733 N  N   . ASN D 2 164 ? 16.475  23.157  39.192  1.00 35.06 ? 159 ASN D N   1 
ATOM   3734 C  CA  . ASN D 2 164 ? 16.648  23.408  37.763  1.00 28.71 ? 159 ASN D CA  1 
ATOM   3735 C  C   . ASN D 2 164 ? 17.878  22.657  37.273  1.00 31.85 ? 159 ASN D C   1 
ATOM   3736 O  O   . ASN D 2 164 ? 18.937  22.723  37.901  1.00 32.82 ? 159 ASN D O   1 
ATOM   3737 C  CB  . ASN D 2 164 ? 16.822  24.902  37.464  1.00 28.44 ? 159 ASN D CB  1 
ATOM   3738 C  CG  . ASN D 2 164 ? 15.624  25.750  37.895  1.00 35.69 ? 159 ASN D CG  1 
ATOM   3739 O  OD1 . ASN D 2 164 ? 14.470  25.284  37.884  1.00 28.14 ? 159 ASN D OD1 1 
ATOM   3740 N  ND2 . ASN D 2 164 ? 15.894  27.020  38.263  1.00 33.73 ? 159 ASN D ND2 1 
ATOM   3741 N  N   . LEU D 2 165 ? 17.745  21.963  36.146  1.00 26.40 ? 160 LEU D N   1 
ATOM   3742 C  CA  . LEU D 2 165 ? 18.821  21.146  35.636  1.00 27.61 ? 160 LEU D CA  1 
ATOM   3743 C  C   . LEU D 2 165 ? 18.868  21.236  34.115  1.00 29.24 ? 160 LEU D C   1 
ATOM   3744 O  O   . LEU D 2 165 ? 17.817  21.244  33.457  1.00 29.75 ? 160 LEU D O   1 
ATOM   3745 C  CB  . LEU D 2 165 ? 18.668  19.683  36.064  1.00 28.85 ? 160 LEU D CB  1 
ATOM   3746 C  CG  . LEU D 2 165 ? 18.412  19.356  37.539  1.00 26.37 ? 160 LEU D CG  1 
ATOM   3747 C  CD1 . LEU D 2 165 ? 17.849  17.956  37.623  1.00 30.20 ? 160 LEU D CD1 1 
ATOM   3748 C  CD2 . LEU D 2 165 ? 19.673  19.450  38.349  1.00 27.76 ? 160 LEU D CD2 1 
ATOM   3749 N  N   . PRO D 2 166 ? 20.063  21.275  33.534  1.00 29.00 ? 161 PRO D N   1 
ATOM   3750 C  CA  . PRO D 2 166 ? 20.174  21.368  32.072  1.00 32.81 ? 161 PRO D CA  1 
ATOM   3751 C  C   . PRO D 2 166 ? 19.960  20.035  31.358  1.00 30.82 ? 161 PRO D C   1 
ATOM   3752 O  O   . PRO D 2 166 ? 20.398  18.973  31.813  1.00 29.24 ? 161 PRO D O   1 
ATOM   3753 C  CB  . PRO D 2 166 ? 21.614  21.869  31.868  1.00 31.34 ? 161 PRO D CB  1 
ATOM   3754 C  CG  . PRO D 2 166 ? 22.371  21.312  33.058  1.00 29.67 ? 161 PRO D CG  1 
ATOM   3755 C  CD  . PRO D 2 166 ? 21.382  21.171  34.197  1.00 29.54 ? 161 PRO D CD  1 
ATOM   3756 N  N   . ILE D 2 167 ? 19.302  20.103  30.200  1.00 26.99 ? 162 ILE D N   1 
ATOM   3757 C  CA  . ILE D 2 167 ? 19.293  18.955  29.310  1.00 28.92 ? 162 ILE D CA  1 
ATOM   3758 C  C   . ILE D 2 167 ? 20.722  18.645  28.880  1.00 32.89 ? 162 ILE D C   1 
ATOM   3759 O  O   . ILE D 2 167 ? 21.537  19.551  28.666  1.00 31.93 ? 162 ILE D O   1 
ATOM   3760 C  CB  . ILE D 2 167 ? 18.381  19.231  28.105  1.00 27.58 ? 162 ILE D CB  1 
ATOM   3761 C  CG1 . ILE D 2 167 ? 16.927  19.238  28.564  1.00 25.32 ? 162 ILE D CG1 1 
ATOM   3762 C  CG2 . ILE D 2 167 ? 18.563  18.170  27.025  1.00 26.34 ? 162 ILE D CG2 1 
ATOM   3763 C  CD1 . ILE D 2 167 ? 16.088  20.168  27.767  1.00 27.83 ? 162 ILE D CD1 1 
ATOM   3764 N  N   . VAL D 2 168 ? 21.034  17.349  28.765  1.00 35.45 ? 163 VAL D N   1 
ATOM   3765 C  CA  . VAL D 2 168 ? 22.380  16.853  28.483  1.00 33.11 ? 163 VAL D CA  1 
ATOM   3766 C  C   . VAL D 2 168 ? 22.426  16.259  27.082  1.00 34.91 ? 163 VAL D C   1 
ATOM   3767 O  O   . VAL D 2 168 ? 21.448  15.657  26.623  1.00 36.61 ? 163 VAL D O   1 
ATOM   3768 C  CB  . VAL D 2 168 ? 22.803  15.803  29.522  1.00 31.40 ? 163 VAL D CB  1 
ATOM   3769 C  CG1 . VAL D 2 168 ? 24.050  15.015  29.060  1.00 31.67 ? 163 VAL D CG1 1 
ATOM   3770 C  CG2 . VAL D 2 168 ? 23.035  16.474  30.837  1.00 32.46 ? 163 VAL D CG2 1 
ATOM   3771 N  N   . GLU D 2 169 ? 23.558  16.444  26.403  1.00 35.90 ? 164 GLU D N   1 
ATOM   3772 C  CA  . GLU D 2 169 ? 23.816  15.792  25.117  1.00 40.24 ? 164 GLU D CA  1 
ATOM   3773 C  C   . GLU D 2 169 ? 23.501  14.298  25.170  1.00 39.84 ? 164 GLU D C   1 
ATOM   3774 O  O   . GLU D 2 169 ? 23.952  13.588  26.078  1.00 36.68 ? 164 GLU D O   1 
ATOM   3775 C  CB  . GLU D 2 169 ? 25.290  15.990  24.726  1.00 36.34 ? 164 GLU D CB  1 
ATOM   3776 C  CG  . GLU D 2 169 ? 25.698  17.447  24.488  1.00 43.27 ? 164 GLU D CG  1 
ATOM   3777 C  CD  . GLU D 2 169 ? 26.145  18.211  25.765  1.00 50.43 ? 164 GLU D CD  1 
ATOM   3778 O  OE1 . GLU D 2 169 ? 25.916  17.745  26.908  1.00 49.00 ? 164 GLU D OE1 1 
ATOM   3779 O  OE2 . GLU D 2 169 ? 26.700  19.331  25.596  1.00 57.23 ? 164 GLU D OE2 1 
ATOM   3780 N  N   . ARG D 2 170 ? 22.756  13.819  24.165  1.00 36.17 ? 165 ARG D N   1 
ATOM   3781 C  CA  . ARG D 2 170 ? 22.375  12.408  24.124  1.00 34.99 ? 165 ARG D CA  1 
ATOM   3782 C  C   . ARG D 2 170 ? 23.561  11.442  24.102  1.00 37.23 ? 165 ARG D C   1 
ATOM   3783 O  O   . ARG D 2 170 ? 23.432  10.354  24.690  1.00 37.96 ? 165 ARG D O   1 
ATOM   3784 C  CB  . ARG D 2 170 ? 21.449  12.147  22.928  1.00 36.56 ? 165 ARG D CB  1 
ATOM   3785 C  CG  . ARG D 2 170 ? 20.790  10.770  22.977  1.00 35.87 ? 165 ARG D CG  1 
ATOM   3786 C  CD  . ARG D 2 170 ? 19.647  10.669  21.993  1.00 36.49 ? 165 ARG D CD  1 
ATOM   3787 N  NE  . ARG D 2 170 ? 18.479  11.348  22.527  1.00 43.75 ? 165 ARG D NE  1 
ATOM   3788 C  CZ  . ARG D 2 170 ? 17.578  10.775  23.313  1.00 41.31 ? 165 ARG D CZ  1 
ATOM   3789 N  NH1 . ARG D 2 170 ? 17.660  9.491   23.631  1.00 34.48 ? 165 ARG D NH1 1 
ATOM   3790 N  NH2 . ARG D 2 170 ? 16.582  11.516  23.809  1.00 33.93 ? 165 ARG D NH2 1 
ATOM   3791 N  N   . PRO D 2 171 ? 24.689  11.725  23.417  1.00 39.75 ? 166 PRO D N   1 
ATOM   3792 C  CA  . PRO D 2 171 ? 25.862  10.834  23.564  1.00 34.71 ? 166 PRO D CA  1 
ATOM   3793 C  C   . PRO D 2 171 ? 26.413  10.778  24.970  1.00 36.56 ? 166 PRO D C   1 
ATOM   3794 O  O   . PRO D 2 171 ? 26.820  9.694   25.414  1.00 35.87 ? 166 PRO D O   1 
ATOM   3795 C  CB  . PRO D 2 171 ? 26.878  11.427  22.582  1.00 31.01 ? 166 PRO D CB  1 
ATOM   3796 C  CG  . PRO D 2 171 ? 26.001  11.938  21.472  1.00 33.08 ? 166 PRO D CG  1 
ATOM   3797 C  CD  . PRO D 2 171 ? 24.815  12.565  22.208  1.00 36.33 ? 166 PRO D CD  1 
ATOM   3798 N  N   . VAL D 2 172 ? 26.461  11.905  25.686  1.00 31.33 ? 167 VAL D N   1 
ATOM   3799 C  CA  . VAL D 2 172 ? 26.823  11.846  27.104  1.00 37.78 ? 167 VAL D CA  1 
ATOM   3800 C  C   . VAL D 2 172 ? 25.822  10.979  27.880  1.00 43.10 ? 167 VAL D C   1 
ATOM   3801 O  O   . VAL D 2 172 ? 26.211  10.223  28.788  1.00 38.01 ? 167 VAL D O   1 
ATOM   3802 C  CB  . VAL D 2 172 ? 26.936  13.266  27.701  1.00 39.95 ? 167 VAL D CB  1 
ATOM   3803 C  CG1 . VAL D 2 172 ? 27.254  13.208  29.189  1.00 30.67 ? 167 VAL D CG1 1 
ATOM   3804 C  CG2 . VAL D 2 172 ? 27.985  14.082  26.959  1.00 39.20 ? 167 VAL D CG2 1 
ATOM   3805 N  N   . CYS D 2 173 ? 24.510  11.115  27.576  1.00 38.45 ? 168 CYS D N   1 
ATOM   3806 C  CA  . CYS D 2 173 ? 23.486  10.300  28.241  1.00 39.34 ? 168 CYS D CA  1 
ATOM   3807 C  C   . CYS D 2 173 ? 23.758  8.816   28.033  1.00 38.73 ? 168 CYS D C   1 
ATOM   3808 O  O   . CYS D 2 173 ? 23.803  8.027   28.983  1.00 35.81 ? 168 CYS D O   1 
ATOM   3809 C  CB  . CYS D 2 173 ? 22.085  10.634  27.725  1.00 36.70 ? 168 CYS D CB  1 
ATOM   3810 S  SG  . CYS D 2 173 ? 21.488  12.263  28.153  1.00 41.68 ? 168 CYS D SG  1 
ATOM   3811 N  N   . LYS D 2 174 ? 24.050  8.451   26.786  1.00 38.07 ? 169 LYS D N   1 
ATOM   3812 C  CA  . LYS D 2 174 ? 24.346  7.032   26.461  1.00 42.77 ? 169 LYS D CA  1 
ATOM   3813 C  C   . LYS D 2 174 ? 25.616  6.558   27.181  1.00 40.57 ? 169 LYS D C   1 
ATOM   3814 O  O   . LYS D 2 174 ? 25.567  5.482   27.805  1.00 43.45 ? 169 LYS D O   1 
ATOM   3815 C  CB  . LYS D 2 174 ? 24.525  6.878   24.949  1.00 41.93 ? 169 LYS D CB  1 
ATOM   3816 C  CG  . LYS D 2 174 ? 23.521  5.960   24.278  1.00 51.09 ? 169 LYS D CG  1 
ATOM   3817 C  CD  . LYS D 2 174 ? 24.168  4.704   23.710  1.00 63.87 ? 169 LYS D CD  1 
ATOM   3818 C  CE  . LYS D 2 174 ? 24.294  4.757   22.222  1.00 53.96 ? 169 LYS D CE  1 
ATOM   3819 N  NZ  . LYS D 2 174 ? 24.631  3.444   21.664  1.00 67.82 ? 169 LYS D NZ  1 
ATOM   3820 N  N   . ASP D 2 175 ? 26.705  7.325   27.109  1.00 37.82 ? 170 ASP D N   1 
ATOM   3821 C  CA  . ASP D 2 175 ? 27.956  6.852   27.687  1.00 40.69 ? 170 ASP D CA  1 
ATOM   3822 C  C   . ASP D 2 175 ? 27.949  6.921   29.195  1.00 39.56 ? 170 ASP D C   1 
ATOM   3823 O  O   . ASP D 2 175 ? 28.869  6.384   29.808  1.00 40.98 ? 170 ASP D O   1 
ATOM   3824 C  CB  . ASP D 2 175 ? 29.164  7.631   27.164  1.00 41.00 ? 170 ASP D CB  1 
ATOM   3825 C  CG  . ASP D 2 175 ? 29.208  7.714   25.663  1.00 48.63 ? 170 ASP D CG  1 
ATOM   3826 O  OD1 . ASP D 2 175 ? 28.475  6.963   25.009  1.00 54.84 ? 170 ASP D OD1 1 
ATOM   3827 O  OD2 . ASP D 2 175 ? 29.952  8.581   25.130  1.00 56.13 ? 170 ASP D OD2 1 
ATOM   3828 N  N   . SER D 2 176 ? 26.959  7.575   29.811  1.00 38.25 ? 171 SER D N   1 
ATOM   3829 C  CA  . SER D 2 176 ? 26.989  7.705   31.266  1.00 37.43 ? 171 SER D CA  1 
ATOM   3830 C  C   . SER D 2 176 ? 26.574  6.425   31.972  1.00 39.51 ? 171 SER D C   1 
ATOM   3831 O  O   . SER D 2 176 ? 26.847  6.270   33.171  1.00 35.38 ? 171 SER D O   1 
ATOM   3832 C  CB  . SER D 2 176 ? 26.073  8.844   31.729  1.00 34.93 ? 171 SER D CB  1 
ATOM   3833 O  OG  . SER D 2 176 ? 24.699  8.535   31.486  1.00 31.90 ? 171 SER D OG  1 
ATOM   3834 N  N   . THR D 2 177 ? 25.970  5.489   31.250  1.00 39.55 ? 172 THR D N   1 
ATOM   3835 C  CA  . THR D 2 177 ? 25.317  4.359   31.886  1.00 42.66 ? 172 THR D CA  1 
ATOM   3836 C  C   . THR D 2 177 ? 25.483  3.119   31.019  1.00 39.72 ? 172 THR D C   1 
ATOM   3837 O  O   . THR D 2 177 ? 25.676  3.201   29.800  1.00 39.85 ? 172 THR D O   1 
ATOM   3838 C  CB  . THR D 2 177 ? 23.813  4.669   32.131  1.00 35.34 ? 172 THR D CB  1 
ATOM   3839 O  OG1 . THR D 2 177 ? 23.249  3.700   33.023  1.00 34.96 ? 172 THR D OG1 1 
ATOM   3840 C  CG2 . THR D 2 177 ? 23.032  4.658   30.818  1.00 30.59 ? 172 THR D CG2 1 
ATOM   3841 N  N   . ARG D 2 178 ? 25.396  1.962   31.668  1.00 40.10 ? 173 ARG D N   1 
ATOM   3842 C  CA  . ARG D 2 178 ? 25.382  0.712   30.923  1.00 46.52 ? 173 ARG D CA  1 
ATOM   3843 C  C   . ARG D 2 178 ? 23.984  0.302   30.481  1.00 42.79 ? 173 ARG D C   1 
ATOM   3844 O  O   . ARG D 2 178 ? 23.862  -0.505  29.549  1.00 44.41 ? 173 ARG D O   1 
ATOM   3845 C  CB  . ARG D 2 178 ? 25.986  -0.410  31.779  1.00 48.93 ? 173 ARG D CB  1 
ATOM   3846 C  CG  . ARG D 2 178 ? 27.495  -0.593  31.632  1.00 54.45 ? 173 ARG D CG  1 
ATOM   3847 C  CD  . ARG D 2 178 ? 27.936  -0.411  30.180  1.00 64.04 ? 173 ARG D CD  1 
ATOM   3848 N  NE  . ARG D 2 178 ? 29.133  -1.189  29.876  1.00 83.92 ? 173 ARG D NE  1 
ATOM   3849 C  CZ  . ARG D 2 178 ? 29.123  -2.435  29.412  1.00 80.94 ? 173 ARG D CZ  1 
ATOM   3850 N  NH1 . ARG D 2 178 ? 27.989  -3.096  29.226  1.00 72.43 ? 173 ARG D NH1 1 
ATOM   3851 N  NH2 . ARG D 2 178 ? 30.279  -3.038  29.145  1.00 77.92 ? 173 ARG D NH2 1 
ATOM   3852 N  N   . ILE D 2 179 ? 22.940  0.900   31.069  1.00 34.75 ? 174 ILE D N   1 
ATOM   3853 C  CA  . ILE D 2 179 ? 21.562  0.613   30.679  1.00 37.44 ? 174 ILE D CA  1 
ATOM   3854 C  C   . ILE D 2 179 ? 21.293  1.161   29.278  1.00 36.04 ? 174 ILE D C   1 
ATOM   3855 O  O   . ILE D 2 179 ? 21.660  2.295   28.954  1.00 36.66 ? 174 ILE D O   1 
ATOM   3856 C  CB  . ILE D 2 179 ? 20.594  1.198   31.733  1.00 35.35 ? 174 ILE D CB  1 
ATOM   3857 C  CG1 . ILE D 2 179 ? 20.727  0.458   33.072  1.00 32.55 ? 174 ILE D CG1 1 
ATOM   3858 C  CG2 . ILE D 2 179 ? 19.138  1.197   31.256  1.00 31.92 ? 174 ILE D CG2 1 
ATOM   3859 C  CD1 . ILE D 2 179 ? 19.937  1.086   34.214  1.00 30.62 ? 174 ILE D CD1 1 
ATOM   3860 N  N   . ARG D 2 180 ? 20.628  0.364   28.443  1.00 37.82 ? 175 ARG D N   1 
ATOM   3861 C  CA  . ARG D 2 180 ? 20.327  0.778   27.073  1.00 38.90 ? 175 ARG D CA  1 
ATOM   3862 C  C   . ARG D 2 180 ? 19.254  1.859   27.096  1.00 44.59 ? 175 ARG D C   1 
ATOM   3863 O  O   . ARG D 2 180 ? 18.103  1.588   27.475  1.00 44.59 ? 175 ARG D O   1 
ATOM   3864 C  CB  . ARG D 2 180 ? 19.875  -0.411  26.220  1.00 36.07 ? 175 ARG D CB  1 
ATOM   3865 C  CG  . ARG D 2 180 ? 19.439  0.013   24.794  1.00 41.95 ? 175 ARG D CG  1 
ATOM   3866 C  CD  . ARG D 2 180 ? 18.948  -1.122  23.893  1.00 42.13 ? 175 ARG D CD  1 
ATOM   3867 N  NE  . ARG D 2 180 ? 17.683  -1.697  24.340  1.00 50.18 ? 175 ARG D NE  1 
ATOM   3868 C  CZ  . ARG D 2 180 ? 16.492  -1.366  23.857  1.00 50.28 ? 175 ARG D CZ  1 
ATOM   3869 N  NH1 . ARG D 2 180 ? 16.361  -0.447  22.912  1.00 55.85 ? 175 ARG D NH1 1 
ATOM   3870 N  NH2 . ARG D 2 180 ? 15.402  -1.963  24.340  1.00 49.51 ? 175 ARG D NH2 1 
ATOM   3871 N  N   . ILE D 2 181 ? 19.624  3.098   26.699  1.00 39.52 ? 176 ILE D N   1 
ATOM   3872 C  CA  . ILE D 2 181 ? 18.657  4.190   26.647  1.00 37.20 ? 176 ILE D CA  1 
ATOM   3873 C  C   . ILE D 2 181 ? 18.017  4.220   25.267  1.00 37.31 ? 176 ILE D C   1 
ATOM   3874 O  O   . ILE D 2 181 ? 18.532  3.658   24.301  1.00 36.71 ? 176 ILE D O   1 
ATOM   3875 C  CB  . ILE D 2 181 ? 19.288  5.549   27.012  1.00 35.73 ? 176 ILE D CB  1 
ATOM   3876 C  CG1 . ILE D 2 181 ? 19.893  6.231   25.794  1.00 40.93 ? 176 ILE D CG1 1 
ATOM   3877 C  CG2 . ILE D 2 181 ? 20.378  5.367   28.058  1.00 38.78 ? 176 ILE D CG2 1 
ATOM   3878 C  CD1 . ILE D 2 181 ? 20.510  7.587   26.129  1.00 42.05 ? 176 ILE D CD1 1 
ATOM   3879 N  N   . THR D 2 182 ? 16.862  4.871   25.182  1.00 36.50 ? 177 THR D N   1 
ATOM   3880 C  CA  . THR D 2 182 ? 16.083  4.935   23.960  1.00 32.53 ? 177 THR D CA  1 
ATOM   3881 C  C   . THR D 2 182 ? 15.717  6.386   23.682  1.00 35.44 ? 177 THR D C   1 
ATOM   3882 O  O   . THR D 2 182 ? 15.920  7.274   24.513  1.00 36.53 ? 177 THR D O   1 
ATOM   3883 C  CB  . THR D 2 182 ? 14.809  4.084   24.058  1.00 36.66 ? 177 THR D CB  1 
ATOM   3884 O  OG1 . THR D 2 182 ? 13.812  4.805   24.803  1.00 31.87 ? 177 THR D OG1 1 
ATOM   3885 C  CG2 . THR D 2 182 ? 15.098  2.718   24.720  1.00 32.35 ? 177 THR D CG2 1 
ATOM   3886 N  N   . ASP D 2 183 ? 15.182  6.624   22.486  1.00 35.09 ? 178 ASP D N   1 
ATOM   3887 C  CA  . ASP D 2 183 ? 14.735  7.957   22.109  1.00 34.73 ? 178 ASP D CA  1 
ATOM   3888 C  C   . ASP D 2 183 ? 13.486  8.386   22.877  1.00 39.42 ? 178 ASP D C   1 
ATOM   3889 O  O   . ASP D 2 183 ? 13.003  9.513   22.678  1.00 38.23 ? 178 ASP D O   1 
ATOM   3890 C  CB  . ASP D 2 183 ? 14.467  8.016   20.600  1.00 37.69 ? 178 ASP D CB  1 
ATOM   3891 C  CG  . ASP D 2 183 ? 15.727  7.790   19.740  1.00 43.39 ? 178 ASP D CG  1 
ATOM   3892 O  OD1 . ASP D 2 183 ? 16.871  7.765   20.256  1.00 40.46 ? 178 ASP D OD1 1 
ATOM   3893 O  OD2 . ASP D 2 183 ? 15.557  7.622   18.519  1.00 43.50 ? 178 ASP D OD2 1 
ATOM   3894 N  N   . ASN D 2 184 ? 12.898  7.493   23.673  1.00 33.85 ? 179 ASN D N   1 
ATOM   3895 C  CA  . ASN D 2 184 ? 11.772  7.840   24.528  1.00 34.78 ? 179 ASN D CA  1 
ATOM   3896 C  C   . ASN D 2 184 ? 12.238  8.347   25.874  1.00 33.78 ? 179 ASN D C   1 
ATOM   3897 O  O   . ASN D 2 184 ? 11.414  8.543   26.772  1.00 33.16 ? 179 ASN D O   1 
ATOM   3898 C  CB  . ASN D 2 184 ? 10.833  6.643   24.717  1.00 37.24 ? 179 ASN D CB  1 
ATOM   3899 C  CG  . ASN D 2 184 ? 10.379  6.048   23.397  1.00 35.66 ? 179 ASN D CG  1 
ATOM   3900 O  OD1 . ASN D 2 184 ? 9.919   6.765   22.512  1.00 29.68 ? 179 ASN D OD1 1 
ATOM   3901 N  ND2 . ASN D 2 184 ? 10.505  4.726   23.263  1.00 37.64 ? 179 ASN D ND2 1 
ATOM   3902 N  N   . MET D 2 185 ? 13.547  8.504   26.047  1.00 33.06 ? 180 MET D N   1 
ATOM   3903 C  CA  . MET D 2 185 ? 14.115  9.080   27.250  1.00 33.96 ? 180 MET D CA  1 
ATOM   3904 C  C   . MET D 2 185 ? 15.020  10.241  26.855  1.00 32.59 ? 180 MET D C   1 
ATOM   3905 O  O   . MET D 2 185 ? 15.498  10.318  25.719  1.00 30.71 ? 180 MET D O   1 
ATOM   3906 C  CB  . MET D 2 185 ? 14.898  8.059   28.071  1.00 33.88 ? 180 MET D CB  1 
ATOM   3907 C  CG  . MET D 2 185 ? 14.398  6.648   27.974  1.00 30.05 ? 180 MET D CG  1 
ATOM   3908 S  SD  . MET D 2 185 ? 15.691  5.518   28.549  1.00 35.54 ? 180 MET D SD  1 
ATOM   3909 C  CE  . MET D 2 185 ? 14.689  4.070   28.856  1.00 38.49 ? 180 MET D CE  1 
ATOM   3910 N  N   . PHE D 2 186 ? 15.180  11.186  27.781  1.00 32.47 ? 181 PHE D N   1 
ATOM   3911 C  CA  . PHE D 2 186 ? 16.265  12.164  27.724  1.00 30.91 ? 181 PHE D CA  1 
ATOM   3912 C  C   . PHE D 2 186 ? 16.877  12.264  29.115  1.00 31.72 ? 181 PHE D C   1 
ATOM   3913 O  O   . PHE D 2 186 ? 16.282  11.832  30.108  1.00 32.55 ? 181 PHE D O   1 
ATOM   3914 C  CB  . PHE D 2 186 ? 15.807  13.550  27.205  1.00 28.17 ? 181 PHE D CB  1 
ATOM   3915 C  CG  . PHE D 2 186 ? 14.850  14.260  28.114  1.00 33.90 ? 181 PHE D CG  1 
ATOM   3916 C  CD1 . PHE D 2 186 ? 15.314  15.019  29.189  1.00 32.20 ? 181 PHE D CD1 1 
ATOM   3917 C  CD2 . PHE D 2 186 ? 13.481  14.186  27.895  1.00 34.19 ? 181 PHE D CD2 1 
ATOM   3918 C  CE1 . PHE D 2 186 ? 14.424  15.676  30.032  1.00 30.52 ? 181 PHE D CE1 1 
ATOM   3919 C  CE2 . PHE D 2 186 ? 12.582  14.847  28.742  1.00 31.48 ? 181 PHE D CE2 1 
ATOM   3920 C  CZ  . PHE D 2 186 ? 13.054  15.584  29.805  1.00 29.64 ? 181 PHE D CZ  1 
ATOM   3921 N  N   . CYS D 2 187 ? 18.100  12.768  29.204  1.00 27.36 ? 182 CYS D N   1 
ATOM   3922 C  CA  . CYS D 2 187 ? 18.685  12.833  30.532  1.00 33.10 ? 182 CYS D CA  1 
ATOM   3923 C  C   . CYS D 2 187 ? 19.062  14.275  30.855  1.00 30.84 ? 182 CYS D C   1 
ATOM   3924 O  O   . CYS D 2 187 ? 19.103  15.137  29.977  1.00 29.35 ? 182 CYS D O   1 
ATOM   3925 C  CB  . CYS D 2 187 ? 19.861  11.838  30.673  1.00 32.22 ? 182 CYS D CB  1 
ATOM   3926 S  SG  . CYS D 2 187 ? 21.501  12.381  30.172  1.00 39.90 ? 182 CYS D SG  1 
ATOM   3927 N  N   . ALA D 2 188 ? 19.237  14.548  32.148  1.00 34.83 ? 183 ALA D N   1 
ATOM   3928 C  CA  . ALA D 2 188 ? 19.549  15.902  32.600  1.00 33.43 ? 183 ALA D CA  1 
ATOM   3929 C  C   . ALA D 2 188 ? 20.338  15.859  33.897  1.00 29.19 ? 183 ALA D C   1 
ATOM   3930 O  O   . ALA D 2 188 ? 20.331  14.862  34.630  1.00 31.17 ? 183 ALA D O   1 
ATOM   3931 C  CB  . ALA D 2 188 ? 18.291  16.754  32.798  1.00 29.50 ? 183 ALA D CB  1 
ATOM   3932 N  N   . GLY D 2 189 ? 20.985  16.973  34.181  1.00 27.25 ? 184 GLY D N   1 
ATOM   3933 C  CA  . GLY D 2 189 ? 21.909  17.108  35.294  1.00 33.37 ? 184 GLY D CA  1 
ATOM   3934 C  C   . GLY D 2 189 ? 23.157  17.861  34.854  1.00 34.29 ? 184 GLY D C   1 
ATOM   3935 O  O   . GLY D 2 189 ? 23.434  18.031  33.672  1.00 34.18 ? 184 GLY D O   1 
ATOM   3936 N  N   . TYR D 2 190 A 23.908  18.359  35.834  1.00 34.58 ? 184 TYR D N   1 
ATOM   3937 C  CA  . TYR D 2 190 A 25.157  19.047  35.549  1.00 34.44 ? 184 TYR D CA  1 
ATOM   3938 C  C   . TYR D 2 190 A 26.288  18.034  35.386  1.00 39.62 ? 184 TYR D C   1 
ATOM   3939 O  O   . TYR D 2 190 A 26.326  17.005  36.063  1.00 40.14 ? 184 TYR D O   1 
ATOM   3940 C  CB  . TYR D 2 190 A 25.498  20.041  36.671  1.00 36.56 ? 184 TYR D CB  1 
ATOM   3941 C  CG  . TYR D 2 190 A 24.534  21.214  36.782  1.00 42.01 ? 184 TYR D CG  1 
ATOM   3942 C  CD1 . TYR D 2 190 A 24.614  22.301  35.908  1.00 37.82 ? 184 TYR D CD1 1 
ATOM   3943 C  CD2 . TYR D 2 190 A 23.531  21.228  37.755  1.00 38.19 ? 184 TYR D CD2 1 
ATOM   3944 C  CE1 . TYR D 2 190 A 23.714  23.372  36.000  1.00 35.78 ? 184 TYR D CE1 1 
ATOM   3945 C  CE2 . TYR D 2 190 A 22.632  22.284  37.853  1.00 33.44 ? 184 TYR D CE2 1 
ATOM   3946 C  CZ  . TYR D 2 190 A 22.723  23.352  36.978  1.00 39.46 ? 184 TYR D CZ  1 
ATOM   3947 O  OH  . TYR D 2 190 A 21.827  24.399  37.092  1.00 39.75 ? 184 TYR D OH  1 
ATOM   3948 N  N   . LYS D 2 191 ? 27.223  18.337  34.486  1.00 42.68 ? 185 LYS D N   1 
ATOM   3949 C  CA  . LYS D 2 191 ? 28.447  17.549  34.405  1.00 41.82 ? 185 LYS D CA  1 
ATOM   3950 C  C   . LYS D 2 191 ? 29.338  17.887  35.597  1.00 42.19 ? 185 LYS D C   1 
ATOM   3951 O  O   . LYS D 2 191 ? 29.160  18.923  36.237  1.00 42.32 ? 185 LYS D O   1 
ATOM   3952 C  CB  . LYS D 2 191 ? 29.149  17.794  33.070  1.00 39.51 ? 185 LYS D CB  1 
ATOM   3953 C  CG  . LYS D 2 191 ? 28.198  17.597  31.907  1.00 37.82 ? 185 LYS D CG  1 
ATOM   3954 C  CD  . LYS D 2 191 ? 28.889  17.574  30.573  1.00 43.42 ? 185 LYS D CD  1 
ATOM   3955 C  CE  . LYS D 2 191 ? 28.021  18.188  29.459  1.00 49.30 ? 185 LYS D CE  1 
ATOM   3956 N  NZ  . LYS D 2 191 ? 28.347  19.623  29.247  1.00 54.84 ? 185 LYS D NZ  1 
ATOM   3957 N  N   . PRO D 2 192 ? 30.277  16.999  35.943  1.00 47.18 ? 186 PRO D N   1 
ATOM   3958 C  CA  . PRO D 2 192 ? 31.061  17.208  37.175  1.00 48.21 ? 186 PRO D CA  1 
ATOM   3959 C  C   . PRO D 2 192 ? 31.856  18.499  37.189  1.00 46.82 ? 186 PRO D C   1 
ATOM   3960 O  O   . PRO D 2 192 ? 32.035  19.087  38.263  1.00 46.42 ? 186 PRO D O   1 
ATOM   3961 C  CB  . PRO D 2 192 ? 31.988  15.982  37.211  1.00 42.12 ? 186 PRO D CB  1 
ATOM   3962 C  CG  . PRO D 2 192 ? 31.340  14.979  36.338  1.00 37.99 ? 186 PRO D CG  1 
ATOM   3963 C  CD  . PRO D 2 192 ? 30.636  15.739  35.272  1.00 45.02 ? 186 PRO D CD  1 
ATOM   3964 N  N   . ASP D 2 193 A 32.338  18.954  36.029  1.00 48.96 ? 186 ASP D N   1 
ATOM   3965 C  CA  . ASP D 2 193 A 33.144  20.171  35.965  1.00 56.14 ? 186 ASP D CA  1 
ATOM   3966 C  C   . ASP D 2 193 A 32.322  21.434  36.196  1.00 57.49 ? 186 ASP D C   1 
ATOM   3967 O  O   . ASP D 2 193 A 32.896  22.467  36.559  1.00 60.03 ? 186 ASP D O   1 
ATOM   3968 C  CB  . ASP D 2 193 A 33.883  20.259  34.624  1.00 57.97 ? 186 ASP D CB  1 
ATOM   3969 C  CG  . ASP D 2 193 A 33.012  19.861  33.443  1.00 67.51 ? 186 ASP D CG  1 
ATOM   3970 O  OD1 . ASP D 2 193 A 33.208  18.732  32.937  1.00 70.50 ? 186 ASP D OD1 1 
ATOM   3971 O  OD2 . ASP D 2 193 A 32.140  20.664  33.018  1.00 63.86 ? 186 ASP D OD2 1 
ATOM   3972 N  N   . GLU D 2 194 B 30.999  21.376  35.993  1.00 54.59 ? 186 GLU D N   1 
ATOM   3973 C  CA  . GLU D 2 194 B 30.138  22.554  35.998  1.00 47.62 ? 186 GLU D CA  1 
ATOM   3974 C  C   . GLU D 2 194 B 29.841  23.104  37.392  1.00 50.60 ? 186 GLU D C   1 
ATOM   3975 O  O   . GLU D 2 194 B 29.238  24.175  37.508  1.00 52.88 ? 186 GLU D O   1 
ATOM   3976 C  CB  . GLU D 2 194 B 28.837  22.216  35.278  1.00 39.46 ? 186 GLU D CB  1 
ATOM   3977 C  CG  . GLU D 2 194 B 29.067  21.865  33.816  1.00 46.37 ? 186 GLU D CG  1 
ATOM   3978 C  CD  . GLU D 2 194 B 27.779  21.669  33.039  1.00 42.80 ? 186 GLU D CD  1 
ATOM   3979 O  OE1 . GLU D 2 194 B 26.763  21.287  33.656  1.00 38.14 ? 186 GLU D OE1 1 
ATOM   3980 O  OE2 . GLU D 2 194 B 27.789  21.901  31.807  1.00 47.61 ? 186 GLU D OE2 1 
ATOM   3981 N  N   . GLY D 2 195 C 30.265  22.436  38.449  1.00 48.67 ? 186 GLY D N   1 
ATOM   3982 C  CA  . GLY D 2 195 C 30.184  23.048  39.761  1.00 54.62 ? 186 GLY D CA  1 
ATOM   3983 C  C   . GLY D 2 195 C 28.808  23.394  40.298  1.00 56.45 ? 186 GLY D C   1 
ATOM   3984 O  O   . GLY D 2 195 C 28.708  24.023  41.353  1.00 63.66 ? 186 GLY D O   1 
ATOM   3985 N  N   . LYS D 2 196 D 27.741  23.011  39.606  1.00 52.15 ? 186 LYS D N   1 
ATOM   3986 C  CA  . LYS D 2 196 D 26.430  22.948  40.234  1.00 41.70 ? 186 LYS D CA  1 
ATOM   3987 C  C   . LYS D 2 196 D 26.021  21.480  40.347  1.00 43.76 ? 186 LYS D C   1 
ATOM   3988 O  O   . LYS D 2 196 D 26.557  20.600  39.664  1.00 44.71 ? 186 LYS D O   1 
ATOM   3989 C  CB  . LYS D 2 196 D 25.374  23.740  39.451  1.00 45.92 ? 186 LYS D CB  1 
ATOM   3990 C  CG  . LYS D 2 196 D 25.527  25.269  39.470  1.00 48.89 ? 186 LYS D CG  1 
ATOM   3991 C  CD  . LYS D 2 196 D 24.192  25.991  39.202  1.00 37.21 ? 186 LYS D CD  1 
ATOM   3992 C  CE  . LYS D 2 196 D 23.135  25.623  40.264  1.00 47.18 ? 186 LYS D CE  1 
ATOM   3993 N  NZ  . LYS D 2 196 D 21.715  26.083  40.025  1.00 42.97 ? 186 LYS D NZ  1 
ATOM   3994 N  N   . ARG D 2 197 ? 25.082  21.212  41.242  1.00 42.35 ? 187 ARG D N   1 
ATOM   3995 C  CA  . ARG D 2 197 ? 24.610  19.863  41.503  1.00 39.31 ? 187 ARG D CA  1 
ATOM   3996 C  C   . ARG D 2 197 ? 23.096  19.856  41.409  1.00 38.67 ? 187 ARG D C   1 
ATOM   3997 O  O   . ARG D 2 197 ? 22.468  20.878  41.110  1.00 37.94 ? 187 ARG D O   1 
ATOM   3998 C  CB  . ARG D 2 197 ? 25.040  19.364  42.888  1.00 39.56 ? 187 ARG D CB  1 
ATOM   3999 C  CG  . ARG D 2 197 ? 26.492  19.520  43.185  1.00 35.99 ? 187 ARG D CG  1 
ATOM   4000 C  CD  . ARG D 2 197 ? 26.865  18.604  44.326  1.00 36.23 ? 187 ARG D CD  1 
ATOM   4001 N  NE  . ARG D 2 197 ? 26.917  17.228  43.873  1.00 32.21 ? 187 ARG D NE  1 
ATOM   4002 C  CZ  . ARG D 2 197 ? 27.920  16.717  43.180  1.00 35.64 ? 187 ARG D CZ  1 
ATOM   4003 N  NH1 . ARG D 2 197 ? 29.003  17.425  42.919  1.00 38.22 ? 187 ARG D NH1 1 
ATOM   4004 N  NH2 . ARG D 2 197 ? 27.822  15.474  42.717  1.00 38.32 ? 187 ARG D NH2 1 
ATOM   4005 N  N   . GLY D 2 198 ? 22.508  18.687  41.665  1.00 36.98 ? 188 GLY D N   1 
ATOM   4006 C  CA  . GLY D 2 198 ? 21.068  18.550  41.595  1.00 37.73 ? 188 GLY D CA  1 
ATOM   4007 C  C   . GLY D 2 198 ? 20.619  17.306  40.864  1.00 35.19 ? 188 GLY D C   1 
ATOM   4008 O  O   . GLY D 2 198 ? 21.212  16.929  39.854  1.00 36.89 ? 188 GLY D O   1 
ATOM   4009 N  N   . ASP D 2 199 ? 19.536  16.693  41.329  1.00 37.71 ? 189 ASP D N   1 
ATOM   4010 C  CA  . ASP D 2 199 ? 19.040  15.465  40.729  1.00 35.71 ? 189 ASP D CA  1 
ATOM   4011 C  C   . ASP D 2 199 ? 17.679  15.135  41.338  1.00 38.59 ? 189 ASP D C   1 
ATOM   4012 O  O   . ASP D 2 199 ? 17.338  15.595  42.437  1.00 38.92 ? 189 ASP D O   1 
ATOM   4013 C  CB  . ASP D 2 199 ? 20.033  14.318  40.966  1.00 32.52 ? 189 ASP D CB  1 
ATOM   4014 C  CG  . ASP D 2 199 ? 19.825  13.166  40.020  1.00 32.91 ? 189 ASP D CG  1 
ATOM   4015 O  OD1 . ASP D 2 199 ? 18.954  13.299  39.126  1.00 28.96 ? 189 ASP D OD1 1 
ATOM   4016 O  OD2 . ASP D 2 199 ? 20.525  12.135  40.184  1.00 29.68 ? 189 ASP D OD2 1 
ATOM   4017 N  N   . ALA D 2 200 ? 16.894  14.351  40.603  1.00 32.91 ? 190 ALA D N   1 
ATOM   4018 C  CA  . ALA D 2 200 ? 15.787  13.673  41.252  1.00 32.21 ? 190 ALA D CA  1 
ATOM   4019 C  C   . ALA D 2 200 ? 16.333  12.454  41.991  1.00 35.10 ? 190 ALA D C   1 
ATOM   4020 O  O   . ALA D 2 200 ? 17.495  12.069  41.816  1.00 32.52 ? 190 ALA D O   1 
ATOM   4021 C  CB  . ALA D 2 200 ? 14.715  13.276  40.238  1.00 30.16 ? 190 ALA D CB  1 
ATOM   4022 N  N   . CYS D 2 201 ? 15.493  11.844  42.829  1.00 33.68 ? 191 CYS D N   1 
ATOM   4023 C  CA  . CYS D 2 201 ? 15.912  10.682  43.613  1.00 29.36 ? 191 CYS D CA  1 
ATOM   4024 C  C   . CYS D 2 201 ? 14.706  9.783   43.880  1.00 33.47 ? 191 CYS D C   1 
ATOM   4025 O  O   . CYS D 2 201 ? 13.609  9.996   43.346  1.00 33.33 ? 191 CYS D O   1 
ATOM   4026 C  CB  . CYS D 2 201 ? 16.597  11.143  44.902  1.00 36.13 ? 191 CYS D CB  1 
ATOM   4027 S  SG  . CYS D 2 201 ? 17.634  9.892   45.686  1.00 38.58 ? 191 CYS D SG  1 
ATOM   4028 N  N   . GLU D 2 202 ? 14.919  8.754   44.697  1.00 32.23 ? 192 GLU D N   1 
ATOM   4029 C  CA  . GLU D 2 202 ? 13.855  7.811   45.014  1.00 35.30 ? 192 GLU D CA  1 
ATOM   4030 C  C   . GLU D 2 202 ? 12.625  8.564   45.516  1.00 35.15 ? 192 GLU D C   1 
ATOM   4031 O  O   . GLU D 2 202 ? 12.729  9.456   46.364  1.00 38.50 ? 192 GLU D O   1 
ATOM   4032 C  CB  . GLU D 2 202 ? 14.336  6.808   46.078  1.00 40.80 ? 192 GLU D CB  1 
ATOM   4033 C  CG  . GLU D 2 202 ? 15.576  5.976   45.717  1.00 41.35 ? 192 GLU D CG  1 
ATOM   4034 C  CD  . GLU D 2 202 ? 15.205  4.646   45.085  1.00 44.66 ? 192 GLU D CD  1 
ATOM   4035 O  OE1 . GLU D 2 202 ? 14.023  4.267   45.237  1.00 40.93 ? 192 GLU D OE1 1 
ATOM   4036 O  OE2 . GLU D 2 202 ? 16.073  3.993   44.447  1.00 39.89 ? 192 GLU D OE2 1 
ATOM   4037 N  N   . GLY D 2 203 ? 11.471  8.256   44.943  1.00 31.99 ? 193 GLY D N   1 
ATOM   4038 C  CA  . GLY D 2 203 ? 10.236  8.894   45.323  1.00 28.44 ? 193 GLY D CA  1 
ATOM   4039 C  C   . GLY D 2 203 ? 9.760   9.970   44.367  1.00 31.82 ? 193 GLY D C   1 
ATOM   4040 O  O   . GLY D 2 203 ? 8.558   10.251  44.322  1.00 33.71 ? 193 GLY D O   1 
ATOM   4041 N  N   . ASP D 2 204 ? 10.664  10.572  43.596  1.00 29.60 ? 194 ASP D N   1 
ATOM   4042 C  CA  . ASP D 2 204 ? 10.282  11.628  42.669  1.00 26.02 ? 194 ASP D CA  1 
ATOM   4043 C  C   . ASP D 2 204 ? 9.669   11.122  41.362  1.00 26.01 ? 194 ASP D C   1 
ATOM   4044 O  O   . ASP D 2 204 ? 9.122   11.938  40.617  1.00 27.68 ? 194 ASP D O   1 
ATOM   4045 C  CB  . ASP D 2 204 ? 11.512  12.507  42.377  1.00 25.78 ? 194 ASP D CB  1 
ATOM   4046 C  CG  . ASP D 2 204 ? 11.973  13.323  43.613  1.00 31.28 ? 194 ASP D CG  1 
ATOM   4047 O  OD1 . ASP D 2 204 ? 11.098  13.843  44.366  1.00 28.77 ? 194 ASP D OD1 1 
ATOM   4048 O  OD2 . ASP D 2 204 ? 13.205  13.459  43.833  1.00 28.12 ? 194 ASP D OD2 1 
ATOM   4049 N  N   . SER D 2 205 ? 9.713   9.815   41.074  1.00 27.57 ? 195 SER D N   1 
ATOM   4050 C  CA  . SER D 2 205 ? 9.192   9.293   39.804  1.00 29.63 ? 195 SER D CA  1 
ATOM   4051 C  C   . SER D 2 205 ? 7.740   9.711   39.574  1.00 29.13 ? 195 SER D C   1 
ATOM   4052 O  O   . SER D 2 205 ? 6.914   9.710   40.494  1.00 27.55 ? 195 SER D O   1 
ATOM   4053 C  CB  . SER D 2 205 ? 9.298   7.762   39.743  1.00 28.14 ? 195 SER D CB  1 
ATOM   4054 O  OG  . SER D 2 205 ? 10.580  7.233   40.111  1.00 33.08 ? 195 SER D OG  1 
ATOM   4055 N  N   . GLY D 2 206 ? 7.431   10.046  38.318  1.00 29.48 ? 196 GLY D N   1 
ATOM   4056 C  CA  . GLY D 2 206 ? 6.141   10.575  37.929  1.00 25.64 ? 196 GLY D CA  1 
ATOM   4057 C  C   . GLY D 2 206 ? 6.005   12.087  38.061  1.00 31.23 ? 196 GLY D C   1 
ATOM   4058 O  O   . GLY D 2 206 ? 5.088   12.681  37.467  1.00 29.01 ? 196 GLY D O   1 
ATOM   4059 N  N   . GLY D 2 207 ? 6.880   12.730  38.821  1.00 29.19 ? 197 GLY D N   1 
ATOM   4060 C  CA  . GLY D 2 207 ? 6.877   14.167  38.868  1.00 30.72 ? 197 GLY D CA  1 
ATOM   4061 C  C   . GLY D 2 207 ? 7.285   14.739  37.526  1.00 30.03 ? 197 GLY D C   1 
ATOM   4062 O  O   . GLY D 2 207 ? 7.901   14.065  36.692  1.00 29.49 ? 197 GLY D O   1 
ATOM   4063 N  N   . PRO D 2 208 ? 6.942   15.995  37.285  1.00 28.17 ? 198 PRO D N   1 
ATOM   4064 C  CA  . PRO D 2 208 ? 7.194   16.584  35.968  1.00 24.94 ? 198 PRO D CA  1 
ATOM   4065 C  C   . PRO D 2 208 ? 8.539   17.272  35.843  1.00 24.46 ? 198 PRO D C   1 
ATOM   4066 O  O   . PRO D 2 208 ? 9.071   17.850  36.792  1.00 27.51 ? 198 PRO D O   1 
ATOM   4067 C  CB  . PRO D 2 208 ? 6.063   17.609  35.839  1.00 21.37 ? 198 PRO D CB  1 
ATOM   4068 C  CG  . PRO D 2 208 ? 5.863   18.065  37.262  1.00 26.51 ? 198 PRO D CG  1 
ATOM   4069 C  CD  . PRO D 2 208 ? 6.100   16.852  38.135  1.00 26.28 ? 198 PRO D CD  1 
ATOM   4070 N  N   . PHE D 2 209 ? 9.082   17.186  34.633  1.00 23.53 ? 199 PHE D N   1 
ATOM   4071 C  CA  . PHE D 2 209 ? 10.172  18.040  34.168  1.00 26.65 ? 199 PHE D CA  1 
ATOM   4072 C  C   . PHE D 2 209 ? 9.540   19.093  33.270  1.00 24.71 ? 199 PHE D C   1 
ATOM   4073 O  O   . PHE D 2 209 ? 9.026   18.765  32.199  1.00 25.73 ? 199 PHE D O   1 
ATOM   4074 C  CB  . PHE D 2 209 ? 11.216  17.214  33.419  1.00 26.13 ? 199 PHE D CB  1 
ATOM   4075 C  CG  . PHE D 2 209 ? 12.402  17.998  32.930  1.00 26.00 ? 199 PHE D CG  1 
ATOM   4076 C  CD1 . PHE D 2 209 ? 12.359  18.671  31.726  1.00 26.37 ? 199 PHE D CD1 1 
ATOM   4077 C  CD2 . PHE D 2 209 ? 13.593  18.002  33.647  1.00 28.64 ? 199 PHE D CD2 1 
ATOM   4078 C  CE1 . PHE D 2 209 ? 13.475  19.361  31.259  1.00 27.26 ? 199 PHE D CE1 1 
ATOM   4079 C  CE2 . PHE D 2 209 ? 14.706  18.691  33.186  1.00 26.83 ? 199 PHE D CE2 1 
ATOM   4080 C  CZ  . PHE D 2 209 ? 14.648  19.369  31.989  1.00 25.67 ? 199 PHE D CZ  1 
ATOM   4081 N  N   . VAL D 2 210 ? 9.534   20.349  33.714  1.00 27.27 ? 200 VAL D N   1 
ATOM   4082 C  CA  . VAL D 2 210 ? 8.803   21.393  33.005  1.00 22.96 ? 200 VAL D CA  1 
ATOM   4083 C  C   . VAL D 2 210 ? 9.777   22.457  32.513  1.00 26.60 ? 200 VAL D C   1 
ATOM   4084 O  O   . VAL D 2 210 ? 10.892  22.618  33.029  1.00 26.85 ? 200 VAL D O   1 
ATOM   4085 C  CB  . VAL D 2 210 ? 7.699   22.024  33.879  1.00 22.53 ? 200 VAL D CB  1 
ATOM   4086 C  CG1 . VAL D 2 210 ? 6.768   20.955  34.408  1.00 20.85 ? 200 VAL D CG1 1 
ATOM   4087 C  CG2 . VAL D 2 210 ? 8.310   22.836  35.035  1.00 24.22 ? 200 VAL D CG2 1 
ATOM   4088 N  N   . MET D 2 211 ? 9.327   23.194  31.499  1.00 26.36 ? 201 MET D N   1 
ATOM   4089 C  CA  . MET D 2 211 ? 10.099  24.251  30.855  1.00 28.25 ? 201 MET D CA  1 
ATOM   4090 C  C   . MET D 2 211 ? 9.159   25.402  30.533  1.00 27.47 ? 201 MET D C   1 
ATOM   4091 O  O   . MET D 2 211 ? 8.013   25.174  30.158  1.00 26.10 ? 201 MET D O   1 
ATOM   4092 C  CB  . MET D 2 211 ? 10.794  23.751  29.578  1.00 23.55 ? 201 MET D CB  1 
ATOM   4093 C  CG  . MET D 2 211 ? 11.879  22.741  29.854  1.00 28.08 ? 201 MET D CG  1 
ATOM   4094 S  SD  . MET D 2 211 ? 12.822  22.270  28.373  1.00 30.18 ? 201 MET D SD  1 
ATOM   4095 C  CE  . MET D 2 211 ? 14.209  23.399  28.502  1.00 28.83 ? 201 MET D CE  1 
ATOM   4096 N  N   . LYS D 2 212 ? 9.623   26.639  30.714  1.00 32.77 ? 202 LYS D N   1 
ATOM   4097 C  CA  . LYS D 2 212 ? 8.796   27.818  30.456  1.00 36.56 ? 202 LYS D CA  1 
ATOM   4098 C  C   . LYS D 2 212 ? 9.139   28.375  29.081  1.00 33.77 ? 202 LYS D C   1 
ATOM   4099 O  O   . LYS D 2 212 ? 10.295  28.717  28.816  1.00 34.14 ? 202 LYS D O   1 
ATOM   4100 C  CB  . LYS D 2 212 ? 8.984   28.881  31.543  1.00 35.63 ? 202 LYS D CB  1 
ATOM   4101 C  CG  . LYS D 2 212 ? 8.307   30.207  31.231  1.00 34.56 ? 202 LYS D CG  1 
ATOM   4102 C  CD  . LYS D 2 212 ? 8.076   31.025  32.498  1.00 33.20 ? 202 LYS D CD  1 
ATOM   4103 C  CE  . LYS D 2 212 ? 7.285   32.286  32.182  1.00 31.66 ? 202 LYS D CE  1 
ATOM   4104 N  NZ  . LYS D 2 212 ? 6.660   32.830  33.391  1.00 30.42 ? 202 LYS D NZ  1 
ATOM   4105 N  N   . SER D 2 213 ? 8.155   28.435  28.210  1.00 35.46 ? 203 SER D N   1 
ATOM   4106 C  CA  . SER D 2 213 ? 8.423   28.811  26.829  1.00 35.25 ? 203 SER D CA  1 
ATOM   4107 C  C   . SER D 2 213 ? 8.684   30.308  26.741  1.00 34.89 ? 203 SER D C   1 
ATOM   4108 O  O   . SER D 2 213 ? 7.882   31.105  27.240  1.00 37.87 ? 203 SER D O   1 
ATOM   4109 C  CB  . SER D 2 213 ? 7.248   28.428  25.925  1.00 37.22 ? 203 SER D CB  1 
ATOM   4110 O  OG  . SER D 2 213 ? 7.258   29.181  24.715  1.00 37.04 ? 203 SER D OG  1 
ATOM   4111 N  N   . PRO D 2 214 ? 9.795   30.737  26.143  1.00 36.88 ? 204 PRO D N   1 
ATOM   4112 C  CA  . PRO D 2 214 ? 9.991   32.172  25.921  1.00 33.06 ? 204 PRO D CA  1 
ATOM   4113 C  C   . PRO D 2 214 ? 9.054   32.742  24.863  1.00 36.38 ? 204 PRO D C   1 
ATOM   4114 O  O   . PRO D 2 214 ? 8.907   33.970  24.788  1.00 39.35 ? 204 PRO D O   1 
ATOM   4115 C  CB  . PRO D 2 214 ? 11.453  32.268  25.473  1.00 29.80 ? 204 PRO D CB  1 
ATOM   4116 C  CG  . PRO D 2 214 ? 11.871  30.865  25.110  1.00 37.09 ? 204 PRO D CG  1 
ATOM   4117 C  CD  . PRO D 2 214 ? 10.702  29.933  25.308  1.00 38.57 ? 204 PRO D CD  1 
ATOM   4118 N  N   . PHE D 2 215 A 8.403   31.892  24.062  1.00 33.28 ? 204 PHE D N   1 
ATOM   4119 C  CA  . PHE D 2 215 A 7.540   32.392  22.999  1.00 35.49 ? 204 PHE D CA  1 
ATOM   4120 C  C   . PHE D 2 215 A 6.173   32.793  23.529  1.00 38.97 ? 204 PHE D C   1 
ATOM   4121 O  O   . PHE D 2 215 A 5.649   33.844  23.139  1.00 39.10 ? 204 PHE D O   1 
ATOM   4122 C  CB  . PHE D 2 215 A 7.446   31.351  21.887  1.00 36.03 ? 204 PHE D CB  1 
ATOM   4123 C  CG  . PHE D 2 215 A 8.781   30.792  21.536  1.00 33.50 ? 204 PHE D CG  1 
ATOM   4124 C  CD1 . PHE D 2 215 A 9.772   31.634  21.063  1.00 29.83 ? 204 PHE D CD1 1 
ATOM   4125 C  CD2 . PHE D 2 215 A 9.085   29.464  21.787  1.00 31.85 ? 204 PHE D CD2 1 
ATOM   4126 C  CE1 . PHE D 2 215 A 11.048  31.160  20.802  1.00 31.80 ? 204 PHE D CE1 1 
ATOM   4127 C  CE2 . PHE D 2 215 A 10.356  28.969  21.532  1.00 36.21 ? 204 PHE D CE2 1 
ATOM   4128 C  CZ  . PHE D 2 215 A 11.346  29.824  21.032  1.00 35.93 ? 204 PHE D CZ  1 
ATOM   4129 N  N   . ASN D 2 216 B 5.601   32.023  24.464  1.00 34.90 ? 204 ASN D N   1 
ATOM   4130 C  CA  . ASN D 2 216 B 4.281   32.375  24.969  1.00 34.10 ? 204 ASN D CA  1 
ATOM   4131 C  C   . ASN D 2 216 B 4.192   32.392  26.493  1.00 34.53 ? 204 ASN D C   1 
ATOM   4132 O  O   . ASN D 2 216 B 3.085   32.525  27.032  1.00 34.93 ? 204 ASN D O   1 
ATOM   4133 C  CB  . ASN D 2 216 B 3.203   31.446  24.380  1.00 34.61 ? 204 ASN D CB  1 
ATOM   4134 C  CG  . ASN D 2 216 B 3.362   29.970  24.791  1.00 38.89 ? 204 ASN D CG  1 
ATOM   4135 O  OD1 . ASN D 2 216 B 4.194   29.608  25.650  1.00 37.10 ? 204 ASN D OD1 1 
ATOM   4136 N  ND2 . ASN D 2 216 B 2.536   29.110  24.177  1.00 25.96 ? 204 ASN D ND2 1 
ATOM   4137 N  N   . ASN D 2 217 ? 5.317   32.285  27.198  1.00 33.14 ? 205 ASN D N   1 
ATOM   4138 C  CA  . ASN D 2 217 ? 5.352   32.366  28.662  1.00 35.56 ? 205 ASN D CA  1 
ATOM   4139 C  C   . ASN D 2 217 ? 4.486   31.321  29.362  1.00 36.63 ? 205 ASN D C   1 
ATOM   4140 O  O   . ASN D 2 217 ? 4.002   31.565  30.463  1.00 37.68 ? 205 ASN D O   1 
ATOM   4141 C  CB  . ASN D 2 217 ? 4.937   33.753  29.147  1.00 38.97 ? 205 ASN D CB  1 
ATOM   4142 C  CG  . ASN D 2 217 ? 6.122   34.645  29.382  1.00 52.78 ? 205 ASN D CG  1 
ATOM   4143 O  OD1 . ASN D 2 217 ? 6.853   34.993  28.434  1.00 49.42 ? 205 ASN D OD1 1 
ATOM   4144 N  ND2 . ASN D 2 217 ? 6.347   35.012  30.650  1.00 52.72 ? 205 ASN D ND2 1 
ATOM   4145 N  N   . ARG D 2 218 ? 4.249   30.169  28.746  1.00 36.29 ? 206 ARG D N   1 
ATOM   4146 C  CA  . ARG D 2 218 ? 3.508   29.091  29.380  1.00 29.72 ? 206 ARG D CA  1 
ATOM   4147 C  C   . ARG D 2 218 ? 4.467   27.991  29.808  1.00 30.52 ? 206 ARG D C   1 
ATOM   4148 O  O   . ARG D 2 218 ? 5.542   27.818  29.224  1.00 31.52 ? 206 ARG D O   1 
ATOM   4149 C  CB  . ARG D 2 218 ? 2.449   28.518  28.440  1.00 32.18 ? 206 ARG D CB  1 
ATOM   4150 C  CG  . ARG D 2 218 ? 1.369   29.486  28.072  1.00 33.57 ? 206 ARG D CG  1 
ATOM   4151 C  CD  . ARG D 2 218 ? 0.379   28.834  27.147  1.00 33.10 ? 206 ARG D CD  1 
ATOM   4152 N  NE  . ARG D 2 218 ? -0.745  29.716  26.866  1.00 38.14 ? 206 ARG D NE  1 
ATOM   4153 C  CZ  . ARG D 2 218 ? -1.994  29.504  27.259  1.00 39.91 ? 206 ARG D CZ  1 
ATOM   4154 N  NH1 . ARG D 2 218 ? -2.321  28.453  27.994  1.00 40.12 ? 206 ARG D NH1 1 
ATOM   4155 N  NH2 . ARG D 2 218 ? -2.941  30.363  26.899  1.00 36.56 ? 206 ARG D NH2 1 
ATOM   4156 N  N   . TRP D 2 219 ? 4.078   27.249  30.839  1.00 29.32 ? 207 TRP D N   1 
ATOM   4157 C  CA  . TRP D 2 219 ? 4.873   26.113  31.290  1.00 29.78 ? 207 TRP D CA  1 
ATOM   4158 C  C   . TRP D 2 219 ? 4.465   24.845  30.537  1.00 27.81 ? 207 TRP D C   1 
ATOM   4159 O  O   . TRP D 2 219 ? 3.279   24.592  30.303  1.00 30.12 ? 207 TRP D O   1 
ATOM   4160 C  CB  . TRP D 2 219 ? 4.725   25.934  32.807  1.00 33.18 ? 207 TRP D CB  1 
ATOM   4161 C  CG  . TRP D 2 219 ? 5.402   27.034  33.620  1.00 29.11 ? 207 TRP D CG  1 
ATOM   4162 C  CD1 . TRP D 2 219 ? 4.837   28.205  34.045  1.00 30.71 ? 207 TRP D CD1 1 
ATOM   4163 C  CD2 . TRP D 2 219 ? 6.769   27.060  34.073  1.00 30.49 ? 207 TRP D CD2 1 
ATOM   4164 N  NE1 . TRP D 2 219 ? 5.765   28.953  34.747  1.00 33.12 ? 207 TRP D NE1 1 
ATOM   4165 C  CE2 . TRP D 2 219 ? 6.957   28.274  34.776  1.00 33.13 ? 207 TRP D CE2 1 
ATOM   4166 C  CE3 . TRP D 2 219 ? 7.855   26.177  33.952  1.00 29.51 ? 207 TRP D CE3 1 
ATOM   4167 C  CZ2 . TRP D 2 219 ? 8.196   28.630  35.353  1.00 32.08 ? 207 TRP D CZ2 1 
ATOM   4168 C  CZ3 . TRP D 2 219 ? 9.082   26.530  34.540  1.00 26.56 ? 207 TRP D CZ3 1 
ATOM   4169 C  CH2 . TRP D 2 219 ? 9.236   27.745  35.225  1.00 27.33 ? 207 TRP D CH2 1 
ATOM   4170 N  N   . TYR D 2 220 ? 5.455   24.065  30.118  1.00 26.24 ? 208 TYR D N   1 
ATOM   4171 C  CA  . TYR D 2 220 ? 5.229   22.855  29.339  1.00 27.71 ? 208 TYR D CA  1 
ATOM   4172 C  C   . TYR D 2 220 ? 5.901   21.691  30.050  1.00 28.69 ? 208 TYR D C   1 
ATOM   4173 O  O   . TYR D 2 220 ? 7.061   21.807  30.466  1.00 28.77 ? 208 TYR D O   1 
ATOM   4174 C  CB  . TYR D 2 220 ? 5.791   23.006  27.924  1.00 24.78 ? 208 TYR D CB  1 
ATOM   4175 C  CG  . TYR D 2 220 ? 4.946   23.872  27.022  1.00 32.00 ? 208 TYR D CG  1 
ATOM   4176 C  CD1 . TYR D 2 220 ? 3.950   23.321  26.221  1.00 35.66 ? 208 TYR D CD1 1 
ATOM   4177 C  CD2 . TYR D 2 220 ? 5.135   25.242  26.971  1.00 34.79 ? 208 TYR D CD2 1 
ATOM   4178 C  CE1 . TYR D 2 220 ? 3.153   24.130  25.386  1.00 35.42 ? 208 TYR D CE1 1 
ATOM   4179 C  CE2 . TYR D 2 220 ? 4.355   26.049  26.153  1.00 36.34 ? 208 TYR D CE2 1 
ATOM   4180 C  CZ  . TYR D 2 220 ? 3.369   25.491  25.366  1.00 35.41 ? 208 TYR D CZ  1 
ATOM   4181 O  OH  . TYR D 2 220 ? 2.612   26.308  24.564  1.00 32.40 ? 208 TYR D OH  1 
ATOM   4182 N  N   . GLN D 2 221 ? 5.201   20.565  30.173  1.00 23.96 ? 209 GLN D N   1 
ATOM   4183 C  CA  . GLN D 2 221 ? 5.833   19.370  30.729  1.00 28.21 ? 209 GLN D CA  1 
ATOM   4184 C  C   . GLN D 2 221 ? 6.525   18.616  29.596  1.00 28.34 ? 209 GLN D C   1 
ATOM   4185 O  O   . GLN D 2 221 ? 5.862   17.986  28.750  1.00 24.78 ? 209 GLN D O   1 
ATOM   4186 C  CB  . GLN D 2 221 ? 4.839   18.472  31.464  1.00 23.41 ? 209 GLN D CB  1 
ATOM   4187 C  CG  . GLN D 2 221 ? 5.538   17.258  32.097  1.00 22.49 ? 209 GLN D CG  1 
ATOM   4188 C  CD  . GLN D 2 221 ? 4.607   16.377  32.952  1.00 28.91 ? 209 GLN D CD  1 
ATOM   4189 O  OE1 . GLN D 2 221 ? 3.422   16.697  33.155  1.00 25.83 ? 209 GLN D OE1 1 
ATOM   4190 N  NE2 . GLN D 2 221 ? 5.145   15.256  33.444  1.00 24.56 ? 209 GLN D NE2 1 
ATOM   4191 N  N   . MET D 2 222 ? 7.860   18.662  29.598  1.00 21.12 ? 210 MET D N   1 
ATOM   4192 C  CA  . MET D 2 222 ? 8.657   17.942  28.617  1.00 25.31 ? 210 MET D CA  1 
ATOM   4193 C  C   . MET D 2 222 ? 8.986   16.509  29.038  1.00 28.29 ? 210 MET D C   1 
ATOM   4194 O  O   . MET D 2 222 ? 9.269   15.667  28.173  1.00 31.03 ? 210 MET D O   1 
ATOM   4195 C  CB  . MET D 2 222 ? 9.973   18.680  28.385  1.00 24.58 ? 210 MET D CB  1 
ATOM   4196 C  CG  . MET D 2 222 ? 9.857   20.134  27.945  1.00 28.32 ? 210 MET D CG  1 
ATOM   4197 S  SD  . MET D 2 222 ? 8.526   20.436  26.802  1.00 37.15 ? 210 MET D SD  1 
ATOM   4198 C  CE  . MET D 2 222 ? 9.233   19.707  25.342  1.00 32.29 ? 210 MET D CE  1 
ATOM   4199 N  N   . GLY D 2 223 ? 8.978   16.212  30.337  1.00 25.17 ? 211 GLY D N   1 
ATOM   4200 C  CA  . GLY D 2 223 ? 9.454   14.928  30.813  1.00 29.95 ? 211 GLY D CA  1 
ATOM   4201 C  C   . GLY D 2 223 ? 8.752   14.456  32.072  1.00 27.10 ? 211 GLY D C   1 
ATOM   4202 O  O   . GLY D 2 223 ? 8.064   15.222  32.753  1.00 22.41 ? 211 GLY D O   1 
ATOM   4203 N  N   . ILE D 2 224 ? 8.959   13.168  32.373  1.00 25.55 ? 212 ILE D N   1 
ATOM   4204 C  CA  . ILE D 2 224 ? 8.494   12.526  33.598  1.00 26.44 ? 212 ILE D CA  1 
ATOM   4205 C  C   . ILE D 2 224 ? 9.683   11.863  34.289  1.00 27.48 ? 212 ILE D C   1 
ATOM   4206 O  O   . ILE D 2 224 ? 10.397  11.068  33.666  1.00 29.02 ? 212 ILE D O   1 
ATOM   4207 C  CB  . ILE D 2 224 ? 7.395   11.480  33.312  1.00 30.05 ? 212 ILE D CB  1 
ATOM   4208 C  CG1 . ILE D 2 224 ? 6.234   12.102  32.530  1.00 27.35 ? 212 ILE D CG1 1 
ATOM   4209 C  CG2 . ILE D 2 224 ? 6.893   10.827  34.607  1.00 21.30 ? 212 ILE D CG2 1 
ATOM   4210 C  CD1 . ILE D 2 224 ? 5.337   11.082  31.880  1.00 22.22 ? 212 ILE D CD1 1 
ATOM   4211 N  N   . VAL D 2 225 ? 9.888   12.178  35.579  1.00 27.02 ? 213 VAL D N   1 
ATOM   4212 C  CA  . VAL D 2 225 ? 10.912  11.524  36.401  1.00 31.61 ? 213 VAL D CA  1 
ATOM   4213 C  C   . VAL D 2 225 ? 10.776  10.010  36.287  1.00 30.55 ? 213 VAL D C   1 
ATOM   4214 O  O   . VAL D 2 225 ? 9.738   9.446   36.649  1.00 27.57 ? 213 VAL D O   1 
ATOM   4215 C  CB  . VAL D 2 225 ? 10.821  11.940  37.887  1.00 33.12 ? 213 VAL D CB  1 
ATOM   4216 C  CG1 . VAL D 2 225 ? 12.029  11.419  38.656  1.00 27.40 ? 213 VAL D CG1 1 
ATOM   4217 C  CG2 . VAL D 2 225 ? 10.708  13.455  38.045  1.00 33.26 ? 213 VAL D CG2 1 
ATOM   4218 N  N   . SER D 2 226 ? 11.828  9.343   35.806  1.00 30.07 ? 214 SER D N   1 
ATOM   4219 C  CA  . SER D 2 226 ? 11.775  7.903   35.549  1.00 31.50 ? 214 SER D CA  1 
ATOM   4220 C  C   . SER D 2 226 ? 12.865  7.118   36.267  1.00 33.53 ? 214 SER D C   1 
ATOM   4221 O  O   . SER D 2 226 ? 12.543  6.190   37.025  1.00 32.94 ? 214 SER D O   1 
ATOM   4222 C  CB  . SER D 2 226 ? 11.832  7.632   34.043  1.00 26.85 ? 214 SER D CB  1 
ATOM   4223 O  OG  . SER D 2 226 ? 11.841  6.238   33.832  1.00 31.00 ? 214 SER D OG  1 
ATOM   4224 N  N   . TRP D 2 227 ? 14.149  7.424   36.054  1.00 33.51 ? 215 TRP D N   1 
ATOM   4225 C  CA  . TRP D 2 227 ? 15.145  6.589   36.724  1.00 35.38 ? 215 TRP D CA  1 
ATOM   4226 C  C   . TRP D 2 227 ? 16.527  7.230   36.734  1.00 37.91 ? 215 TRP D C   1 
ATOM   4227 O  O   . TRP D 2 227 ? 16.824  8.153   35.967  1.00 33.43 ? 215 TRP D O   1 
ATOM   4228 C  CB  . TRP D 2 227 ? 15.249  5.192   36.085  1.00 32.24 ? 215 TRP D CB  1 
ATOM   4229 C  CG  . TRP D 2 227 ? 15.583  5.183   34.624  1.00 32.36 ? 215 TRP D CG  1 
ATOM   4230 C  CD1 . TRP D 2 227 ? 14.705  5.298   33.583  1.00 32.07 ? 215 TRP D CD1 1 
ATOM   4231 C  CD2 . TRP D 2 227 ? 16.883  5.025   34.036  1.00 28.87 ? 215 TRP D CD2 1 
ATOM   4232 N  NE1 . TRP D 2 227 ? 15.382  5.218   32.386  1.00 33.26 ? 215 TRP D NE1 1 
ATOM   4233 C  CE2 . TRP D 2 227 ? 16.720  5.048   32.642  1.00 28.01 ? 215 TRP D CE2 1 
ATOM   4234 C  CE3 . TRP D 2 227 ? 18.165  4.857   34.554  1.00 31.65 ? 215 TRP D CE3 1 
ATOM   4235 C  CZ2 . TRP D 2 227 ? 17.801  4.936   31.756  1.00 26.24 ? 215 TRP D CZ2 1 
ATOM   4236 C  CZ3 . TRP D 2 227 ? 19.240  4.732   33.662  1.00 31.74 ? 215 TRP D CZ3 1 
ATOM   4237 C  CH2 . TRP D 2 227 ? 19.044  4.772   32.284  1.00 22.82 ? 215 TRP D CH2 1 
ATOM   4238 N  N   . GLY D 2 228 ? 17.379  6.676   37.599  1.00 33.48 ? 216 GLY D N   1 
ATOM   4239 C  CA  . GLY D 2 228 ? 18.791  7.001   37.675  1.00 35.83 ? 216 GLY D CA  1 
ATOM   4240 C  C   . GLY D 2 228 ? 19.489  5.905   38.455  1.00 37.22 ? 216 GLY D C   1 
ATOM   4241 O  O   . GLY D 2 228 ? 18.850  5.033   39.049  1.00 34.52 ? 216 GLY D O   1 
ATOM   4242 N  N   . GLU D 2 229 ? 20.820  5.962   38.456  1.00 35.60 ? 217 GLU D N   1 
ATOM   4243 C  CA  . GLU D 2 229 ? 21.653  5.040   39.226  1.00 34.24 ? 217 GLU D CA  1 
ATOM   4244 C  C   . GLU D 2 229 ? 22.270  5.854   40.354  1.00 33.40 ? 217 GLU D C   1 
ATOM   4245 O  O   . GLU D 2 229 ? 23.263  6.559   40.160  1.00 38.00 ? 217 GLU D O   1 
ATOM   4246 C  CB  . GLU D 2 229 ? 22.705  4.387   38.338  1.00 35.34 ? 217 GLU D CB  1 
ATOM   4247 C  CG  . GLU D 2 229 ? 22.091  3.549   37.239  1.00 33.83 ? 217 GLU D CG  1 
ATOM   4248 C  CD  . GLU D 2 229 ? 23.124  3.012   36.272  1.00 39.97 ? 217 GLU D CD  1 
ATOM   4249 O  OE1 . GLU D 2 229 ? 23.687  3.814   35.508  1.00 44.53 ? 217 GLU D OE1 1 
ATOM   4250 O  OE2 . GLU D 2 229 ? 23.372  1.787   36.266  1.00 46.84 ? 217 GLU D OE2 1 
ATOM   4251 N  N   . GLY D 2 230 ? 21.683  5.756   41.529  1.00 31.59 ? 219 GLY D N   1 
ATOM   4252 C  CA  . GLY D 2 230 ? 22.016  6.680   42.584  1.00 32.81 ? 219 GLY D CA  1 
ATOM   4253 C  C   . GLY D 2 230 ? 21.380  8.021   42.301  1.00 34.96 ? 219 GLY D C   1 
ATOM   4254 O  O   . GLY D 2 230 ? 20.627  8.202   41.342  1.00 34.64 ? 219 GLY D O   1 
ATOM   4255 N  N   . CYS D 2 231 ? 21.674  8.982   43.173  1.00 38.89 ? 220 CYS D N   1 
ATOM   4256 C  CA  . CYS D 2 231 ? 21.190  10.350  43.022  1.00 39.82 ? 220 CYS D CA  1 
ATOM   4257 C  C   . CYS D 2 231 ? 22.359  11.330  43.080  1.00 36.36 ? 220 CYS D C   1 
ATOM   4258 O  O   . CYS D 2 231 ? 23.196  11.246  43.981  1.00 34.34 ? 220 CYS D O   1 
ATOM   4259 C  CB  . CYS D 2 231 ? 20.152  10.659  44.102  1.00 37.50 ? 220 CYS D CB  1 
ATOM   4260 S  SG  . CYS D 2 231 ? 18.965  9.285   44.267  1.00 41.41 ? 220 CYS D SG  1 
ATOM   4261 N  N   . ASP D 2 232 ? 22.438  12.225  42.093  1.00 38.51 ? 221 ASP D N   1 
ATOM   4262 C  CA  . ASP D 2 232 ? 23.417  13.319  42.084  1.00 35.69 ? 221 ASP D CA  1 
ATOM   4263 C  C   . ASP D 2 232 ? 24.868  12.827  42.163  1.00 40.26 ? 221 ASP D C   1 
ATOM   4264 O  O   . ASP D 2 232 ? 25.729  13.484  42.770  1.00 37.39 ? 221 ASP D O   1 
ATOM   4265 C  CB  . ASP D 2 232 ? 23.133  14.313  43.214  1.00 34.14 ? 221 ASP D CB  1 
ATOM   4266 C  CG  . ASP D 2 232 ? 23.864  15.632  43.032  1.00 34.85 ? 221 ASP D CG  1 
ATOM   4267 O  OD1 . ASP D 2 232 ? 23.952  16.126  41.886  1.00 32.60 ? 221 ASP D OD1 1 
ATOM   4268 O  OD2 . ASP D 2 232 ? 24.346  16.175  44.043  1.00 38.09 ? 221 ASP D OD2 1 
ATOM   4269 N  N   . ARG D 2 233 A 25.155  11.667  41.572  1.00 37.50 ? 221 ARG D N   1 
ATOM   4270 C  CA  . ARG D 2 233 A 26.525  11.188  41.464  1.00 33.93 ? 221 ARG D CA  1 
ATOM   4271 C  C   . ARG D 2 233 A 27.232  11.865  40.293  1.00 40.00 ? 221 ARG D C   1 
ATOM   4272 O  O   . ARG D 2 233 A 26.632  12.100  39.235  1.00 41.93 ? 221 ARG D O   1 
ATOM   4273 C  CB  . ARG D 2 233 A 26.557  9.670   41.276  1.00 35.81 ? 221 ARG D CB  1 
ATOM   4274 C  CG  . ARG D 2 233 A 25.975  8.862   42.437  1.00 39.30 ? 221 ARG D CG  1 
ATOM   4275 C  CD  . ARG D 2 233 A 26.098  7.350   42.170  1.00 38.12 ? 221 ARG D CD  1 
ATOM   4276 N  NE  . ARG D 2 233 A 25.584  6.551   43.279  1.00 41.41 ? 221 ARG D NE  1 
ATOM   4277 C  CZ  . ARG D 2 233 A 25.644  5.226   43.331  1.00 40.82 ? 221 ARG D CZ  1 
ATOM   4278 N  NH1 . ARG D 2 233 A 26.189  4.519   42.355  1.00 36.05 ? 221 ARG D NH1 1 
ATOM   4279 N  NH2 . ARG D 2 233 A 25.153  4.592   44.394  1.00 36.50 ? 221 ARG D NH2 1 
ATOM   4280 N  N   . ASP D 2 234 ? 28.515  12.182  40.481  1.00 36.64 ? 222 ASP D N   1 
ATOM   4281 C  CA  . ASP D 2 234 ? 29.276  12.782  39.391  1.00 40.72 ? 222 ASP D CA  1 
ATOM   4282 C  C   . ASP D 2 234 ? 29.334  11.834  38.197  1.00 40.80 ? 222 ASP D C   1 
ATOM   4283 O  O   . ASP D 2 234 ? 29.550  10.626  38.346  1.00 44.81 ? 222 ASP D O   1 
ATOM   4284 C  CB  . ASP D 2 234 ? 30.693  13.129  39.845  1.00 37.49 ? 222 ASP D CB  1 
ATOM   4285 C  CG  . ASP D 2 234 ? 30.725  14.269  40.837  1.00 42.37 ? 222 ASP D CG  1 
ATOM   4286 O  OD1 . ASP D 2 234 ? 29.687  14.955  41.035  1.00 38.18 ? 222 ASP D OD1 1 
ATOM   4287 O  OD2 . ASP D 2 234 ? 31.807  14.473  41.428  1.00 43.97 ? 222 ASP D OD2 1 
ATOM   4288 N  N   . GLY D 2 235 ? 29.121  12.378  37.005  1.00 32.59 ? 223 GLY D N   1 
ATOM   4289 C  CA  . GLY D 2 235 ? 29.158  11.568  35.809  1.00 37.79 ? 223 GLY D CA  1 
ATOM   4290 C  C   . GLY D 2 235 ? 27.902  10.774  35.535  1.00 42.85 ? 223 GLY D C   1 
ATOM   4291 O  O   . GLY D 2 235 ? 27.758  10.243  34.422  1.00 37.62 ? 223 GLY D O   1 
ATOM   4292 N  N   . LYS D 2 236 ? 26.981  10.696  36.496  1.00 37.99 ? 224 LYS D N   1 
ATOM   4293 C  CA  . LYS D 2 236 ? 25.668  10.112  36.277  1.00 42.50 ? 224 LYS D CA  1 
ATOM   4294 C  C   . LYS D 2 236 ? 24.652  11.215  36.010  1.00 38.93 ? 224 LYS D C   1 
ATOM   4295 O  O   . LYS D 2 236 ? 24.861  12.379  36.355  1.00 35.83 ? 224 LYS D O   1 
ATOM   4296 C  CB  . LYS D 2 236 ? 25.219  9.294   37.494  1.00 43.06 ? 224 LYS D CB  1 
ATOM   4297 C  CG  . LYS D 2 236 ? 26.189  8.222   37.934  1.00 42.92 ? 224 LYS D CG  1 
ATOM   4298 C  CD  . LYS D 2 236 ? 26.606  7.349   36.764  1.00 37.96 ? 224 LYS D CD  1 
ATOM   4299 C  CE  . LYS D 2 236 ? 25.516  6.386   36.372  1.00 40.35 ? 224 LYS D CE  1 
ATOM   4300 N  NZ  . LYS D 2 236 ? 26.045  5.312   35.469  1.00 40.04 ? 224 LYS D NZ  1 
ATOM   4301 N  N   . TYR D 2 237 ? 23.526  10.829  35.414  1.00 37.72 ? 225 TYR D N   1 
ATOM   4302 C  CA  . TYR D 2 237 ? 22.475  11.781  35.087  1.00 39.24 ? 225 TYR D CA  1 
ATOM   4303 C  C   . TYR D 2 237 ? 21.116  11.176  35.367  1.00 34.81 ? 225 TYR D C   1 
ATOM   4304 O  O   . TYR D 2 237 ? 20.941  9.959   35.306  1.00 38.97 ? 225 TYR D O   1 
ATOM   4305 C  CB  . TYR D 2 237 ? 22.562  12.215  33.628  1.00 37.53 ? 225 TYR D CB  1 
ATOM   4306 C  CG  . TYR D 2 237 ? 23.909  12.807  33.357  1.00 42.11 ? 225 TYR D CG  1 
ATOM   4307 C  CD1 . TYR D 2 237 ? 24.204  14.124  33.741  1.00 38.57 ? 225 TYR D CD1 1 
ATOM   4308 C  CD2 . TYR D 2 237 ? 24.909  12.040  32.790  1.00 37.86 ? 225 TYR D CD2 1 
ATOM   4309 C  CE1 . TYR D 2 237 ? 25.455  14.664  33.526  1.00 42.06 ? 225 TYR D CE1 1 
ATOM   4310 C  CE2 . TYR D 2 237 ? 26.155  12.569  32.559  1.00 44.45 ? 225 TYR D CE2 1 
ATOM   4311 C  CZ  . TYR D 2 237 ? 26.438  13.879  32.926  1.00 44.19 ? 225 TYR D CZ  1 
ATOM   4312 O  OH  . TYR D 2 237 ? 27.709  14.380  32.695  1.00 41.32 ? 225 TYR D OH  1 
ATOM   4313 N  N   . GLY D 2 238 ? 20.151  12.036  35.665  1.00 31.21 ? 226 GLY D N   1 
ATOM   4314 C  CA  . GLY D 2 238 ? 18.784  11.572  35.795  1.00 29.98 ? 226 GLY D CA  1 
ATOM   4315 C  C   . GLY D 2 238 ? 18.142  11.380  34.435  1.00 27.28 ? 226 GLY D C   1 
ATOM   4316 O  O   . GLY D 2 238 ? 18.509  12.030  33.451  1.00 32.25 ? 226 GLY D O   1 
ATOM   4317 N  N   . PHE D 2 239 ? 17.190  10.455  34.368  1.00 26.17 ? 227 PHE D N   1 
ATOM   4318 C  CA  . PHE D 2 239 ? 16.549  10.086  33.113  1.00 29.70 ? 227 PHE D CA  1 
ATOM   4319 C  C   . PHE D 2 239 ? 15.045  10.275  33.212  1.00 29.20 ? 227 PHE D C   1 
ATOM   4320 O  O   . PHE D 2 239 ? 14.414  9.876   34.212  1.00 26.99 ? 227 PHE D O   1 
ATOM   4321 C  CB  . PHE D 2 239 ? 16.884  8.641   32.721  1.00 27.75 ? 227 PHE D CB  1 
ATOM   4322 C  CG  . PHE D 2 239 ? 18.229  8.503   32.042  1.00 28.99 ? 227 PHE D CG  1 
ATOM   4323 C  CD1 . PHE D 2 239 ? 19.407  8.574   32.776  1.00 26.62 ? 227 PHE D CD1 1 
ATOM   4324 C  CD2 . PHE D 2 239 ? 18.315  8.307   30.669  1.00 29.42 ? 227 PHE D CD2 1 
ATOM   4325 C  CE1 . PHE D 2 239 ? 20.640  8.456   32.142  1.00 31.40 ? 227 PHE D CE1 1 
ATOM   4326 C  CE2 . PHE D 2 239 ? 19.549  8.184   30.036  1.00 31.53 ? 227 PHE D CE2 1 
ATOM   4327 C  CZ  . PHE D 2 239 ? 20.710  8.268   30.770  1.00 29.06 ? 227 PHE D CZ  1 
ATOM   4328 N  N   . TYR D 2 240 ? 14.491  10.844  32.134  1.00 29.43 ? 228 TYR D N   1 
ATOM   4329 C  CA  . TYR D 2 240 ? 13.126  11.343  32.065  1.00 30.98 ? 228 TYR D CA  1 
ATOM   4330 C  C   . TYR D 2 240 ? 12.420  10.780  30.838  1.00 31.42 ? 228 TYR D C   1 
ATOM   4331 O  O   . TYR D 2 240 ? 12.994  10.716  29.738  1.00 34.98 ? 228 TYR D O   1 
ATOM   4332 C  CB  . TYR D 2 240 ? 13.112  12.889  32.023  1.00 30.78 ? 228 TYR D CB  1 
ATOM   4333 C  CG  . TYR D 2 240 ? 13.799  13.527  33.219  1.00 29.33 ? 228 TYR D CG  1 
ATOM   4334 C  CD1 . TYR D 2 240 ? 15.198  13.625  33.282  1.00 27.05 ? 228 TYR D CD1 1 
ATOM   4335 C  CD2 . TYR D 2 240 ? 13.058  13.987  34.302  1.00 25.11 ? 228 TYR D CD2 1 
ATOM   4336 C  CE1 . TYR D 2 240 ? 15.828  14.170  34.381  1.00 26.67 ? 228 TYR D CE1 1 
ATOM   4337 C  CE2 . TYR D 2 240 ? 13.684  14.543  35.418  1.00 24.37 ? 228 TYR D CE2 1 
ATOM   4338 C  CZ  . TYR D 2 240 ? 15.063  14.636  35.450  1.00 26.95 ? 228 TYR D CZ  1 
ATOM   4339 O  OH  . TYR D 2 240 ? 15.680  15.192  36.552  1.00 26.91 ? 228 TYR D OH  1 
ATOM   4340 N  N   . THR D 2 241 ? 11.181  10.356  31.047  1.00 27.15 ? 229 THR D N   1 
ATOM   4341 C  CA  . THR D 2 241 ? 10.330  9.939   29.947  1.00 30.17 ? 229 THR D CA  1 
ATOM   4342 C  C   . THR D 2 241 ? 10.062  11.136  29.042  1.00 32.09 ? 229 THR D C   1 
ATOM   4343 O  O   . THR D 2 241 ? 9.702   12.222  29.508  1.00 30.95 ? 229 THR D O   1 
ATOM   4344 C  CB  . THR D 2 241 ? 9.010   9.355   30.485  1.00 27.53 ? 229 THR D CB  1 
ATOM   4345 O  OG1 . THR D 2 241 ? 9.283   8.242   31.351  1.00 28.48 ? 229 THR D OG1 1 
ATOM   4346 C  CG2 . THR D 2 241 ? 8.144   8.863   29.352  1.00 26.02 ? 229 THR D CG2 1 
ATOM   4347 N  N   . HIS D 2 242 ? 10.249  10.933  27.747  1.00 33.21 ? 230 HIS D N   1 
ATOM   4348 C  CA  . HIS D 2 242 ? 10.099  11.978  26.734  1.00 33.59 ? 230 HIS D CA  1 
ATOM   4349 C  C   . HIS D 2 242 ? 8.611   12.175  26.438  1.00 29.59 ? 230 HIS D C   1 
ATOM   4350 O  O   . HIS D 2 242 ? 8.007   11.393  25.697  1.00 31.95 ? 230 HIS D O   1 
ATOM   4351 C  CB  . HIS D 2 242 ? 10.876  11.566  25.486  1.00 31.29 ? 230 HIS D CB  1 
ATOM   4352 C  CG  . HIS D 2 242 ? 11.127  12.669  24.512  1.00 31.85 ? 230 HIS D CG  1 
ATOM   4353 N  ND1 . HIS D 2 242 ? 10.112  13.417  23.949  1.00 34.66 ? 230 HIS D ND1 1 
ATOM   4354 C  CD2 . HIS D 2 242 ? 12.278  13.112  23.952  1.00 32.20 ? 230 HIS D CD2 1 
ATOM   4355 C  CE1 . HIS D 2 242 ? 10.631  14.287  23.102  1.00 32.07 ? 230 HIS D CE1 1 
ATOM   4356 N  NE2 . HIS D 2 242 ? 11.942  14.121  23.085  1.00 37.28 ? 230 HIS D NE2 1 
ATOM   4357 N  N   . VAL D 2 243 ? 8.011   13.238  26.981  1.00 25.83 ? 231 VAL D N   1 
ATOM   4358 C  CA  . VAL D 2 243 ? 6.558   13.371  26.879  1.00 29.44 ? 231 VAL D CA  1 
ATOM   4359 C  C   . VAL D 2 243 ? 6.108   13.535  25.428  1.00 30.11 ? 231 VAL D C   1 
ATOM   4360 O  O   . VAL D 2 243 ? 5.105   12.944  25.020  1.00 27.58 ? 231 VAL D O   1 
ATOM   4361 C  CB  . VAL D 2 243 ? 6.023   14.516  27.760  1.00 29.05 ? 231 VAL D CB  1 
ATOM   4362 C  CG1 . VAL D 2 243 ? 4.503   14.641  27.553  1.00 24.87 ? 231 VAL D CG1 1 
ATOM   4363 C  CG2 . VAL D 2 243 ? 6.316   14.244  29.243  1.00 27.97 ? 231 VAL D CG2 1 
ATOM   4364 N  N   . PHE D 2 244 ? 6.806   14.348  24.626  1.00 31.47 ? 232 PHE D N   1 
ATOM   4365 C  CA  . PHE D 2 244 ? 6.291   14.579  23.278  1.00 31.64 ? 232 PHE D CA  1 
ATOM   4366 C  C   . PHE D 2 244 ? 6.294   13.300  22.434  1.00 32.33 ? 232 PHE D C   1 
ATOM   4367 O  O   . PHE D 2 244 ? 5.334   13.046  21.700  1.00 32.84 ? 232 PHE D O   1 
ATOM   4368 C  CB  . PHE D 2 244 ? 7.049   15.694  22.554  1.00 36.87 ? 232 PHE D CB  1 
ATOM   4369 C  CG  . PHE D 2 244 ? 6.562   15.893  21.149  1.00 37.55 ? 232 PHE D CG  1 
ATOM   4370 C  CD1 . PHE D 2 244 ? 5.330   16.482  20.914  1.00 34.95 ? 232 PHE D CD1 1 
ATOM   4371 C  CD2 . PHE D 2 244 ? 7.294   15.419  20.066  1.00 32.88 ? 232 PHE D CD2 1 
ATOM   4372 C  CE1 . PHE D 2 244 ? 4.856   16.625  19.623  1.00 33.16 ? 232 PHE D CE1 1 
ATOM   4373 C  CE2 . PHE D 2 244 ? 6.816   15.555  18.773  1.00 28.70 ? 232 PHE D CE2 1 
ATOM   4374 C  CZ  . PHE D 2 244 ? 5.603   16.163  18.556  1.00 32.64 ? 232 PHE D CZ  1 
ATOM   4375 N  N   . ARG D 2 245 ? 7.341   12.466  22.538  1.00 30.46 ? 233 ARG D N   1 
ATOM   4376 C  CA  . ARG D 2 245 ? 7.375   11.250  21.723  1.00 30.42 ? 233 ARG D CA  1 
ATOM   4377 C  C   . ARG D 2 245 ? 6.169   10.351  21.957  1.00 31.40 ? 233 ARG D C   1 
ATOM   4378 O  O   . ARG D 2 245 ? 5.798   9.578   21.070  1.00 39.38 ? 233 ARG D O   1 
ATOM   4379 C  CB  . ARG D 2 245 ? 8.633   10.429  21.989  1.00 32.92 ? 233 ARG D CB  1 
ATOM   4380 C  CG  . ARG D 2 245 ? 9.889   11.208  21.856  1.00 41.85 ? 233 ARG D CG  1 
ATOM   4381 C  CD  . ARG D 2 245 ? 10.314  11.384  20.453  1.00 45.97 ? 233 ARG D CD  1 
ATOM   4382 N  NE  . ARG D 2 245 ? 10.682  10.111  19.874  1.00 55.34 ? 233 ARG D NE  1 
ATOM   4383 C  CZ  . ARG D 2 245 ? 11.886  9.860   19.392  1.00 60.88 ? 233 ARG D CZ  1 
ATOM   4384 N  NH1 . ARG D 2 245 ? 12.852  10.777  19.422  1.00 68.13 ? 233 ARG D NH1 1 
ATOM   4385 N  NH2 . ARG D 2 245 ? 12.126  8.667   18.862  1.00 59.44 ? 233 ARG D NH2 1 
ATOM   4386 N  N   . LEU D 2 246 ? 5.553   10.410  23.129  1.00 30.77 ? 234 LEU D N   1 
ATOM   4387 C  CA  . LEU D 2 246 ? 4.413   9.556   23.414  1.00 29.64 ? 234 LEU D CA  1 
ATOM   4388 C  C   . LEU D 2 246 ? 3.108   10.339  23.432  1.00 32.65 ? 234 LEU D C   1 
ATOM   4389 O  O   . LEU D 2 246 ? 2.057   9.790   23.812  1.00 33.16 ? 234 LEU D O   1 
ATOM   4390 C  CB  . LEU D 2 246 ? 4.646   8.797   24.724  1.00 35.35 ? 234 LEU D CB  1 
ATOM   4391 C  CG  . LEU D 2 246 ? 6.028   8.125   24.798  1.00 36.29 ? 234 LEU D CG  1 
ATOM   4392 C  CD1 . LEU D 2 246 ? 6.474   7.865   26.215  1.00 33.63 ? 234 LEU D CD1 1 
ATOM   4393 C  CD2 . LEU D 2 246 ? 6.033   6.825   24.019  1.00 42.47 ? 234 LEU D CD2 1 
ATOM   4394 N  N   . LYS D 2 247 ? 3.137   11.600  22.981  1.00 31.54 ? 235 LYS D N   1 
ATOM   4395 C  CA  . LYS D 2 247 ? 1.938   12.431  23.067  1.00 37.21 ? 235 LYS D CA  1 
ATOM   4396 C  C   . LYS D 2 247 ? 0.779   11.795  22.320  1.00 34.84 ? 235 LYS D C   1 
ATOM   4397 O  O   . LYS D 2 247 ? -0.365  11.821  22.782  1.00 34.66 ? 235 LYS D O   1 
ATOM   4398 C  CB  . LYS D 2 247 ? 2.209   13.825  22.507  1.00 34.43 ? 235 LYS D CB  1 
ATOM   4399 C  CG  . LYS D 2 247 ? 1.019   14.768  22.670  1.00 36.07 ? 235 LYS D CG  1 
ATOM   4400 C  CD  . LYS D 2 247 ? 1.316   16.106  22.022  1.00 35.35 ? 235 LYS D CD  1 
ATOM   4401 C  CE  . LYS D 2 247 ? 0.219   17.110  22.295  1.00 36.88 ? 235 LYS D CE  1 
ATOM   4402 N  NZ  . LYS D 2 247 ? 0.407   18.280  21.390  1.00 43.45 ? 235 LYS D NZ  1 
ATOM   4403 N  N   . LYS D 2 248 ? 1.072   11.216  21.162  1.00 36.47 ? 236 LYS D N   1 
ATOM   4404 C  CA  . LYS D 2 248 ? 0.091   10.482  20.384  1.00 34.87 ? 236 LYS D CA  1 
ATOM   4405 C  C   . LYS D 2 248 ? -0.732  9.554   21.271  1.00 37.56 ? 236 LYS D C   1 
ATOM   4406 O  O   . LYS D 2 248 ? -1.960  9.695   21.384  1.00 41.13 ? 236 LYS D O   1 
ATOM   4407 C  CB  . LYS D 2 248 ? 0.849   9.720   19.302  1.00 43.87 ? 236 LYS D CB  1 
ATOM   4408 C  CG  . LYS D 2 248 ? 2.286   9.268   19.771  1.00 44.74 ? 236 LYS D CG  1 
ATOM   4409 C  CD  . LYS D 2 248 ? 2.277   7.857   20.413  1.00 38.95 ? 236 LYS D CD  1 
ATOM   4410 C  CE  . LYS D 2 248 ? 3.629   7.433   20.956  1.00 46.01 ? 236 LYS D CE  1 
ATOM   4411 N  NZ  . LYS D 2 248 ? 3.698   5.983   21.366  1.00 50.55 ? 236 LYS D NZ  1 
ATOM   4412 N  N   . TRP D 2 249 ? -0.053  8.639   21.965  1.00 34.88 ? 237 TRP D N   1 
ATOM   4413 C  CA  . TRP D 2 249 ? -0.743  7.687   22.827  1.00 33.74 ? 237 TRP D CA  1 
ATOM   4414 C  C   . TRP D 2 249 ? -1.576  8.433   23.858  1.00 33.86 ? 237 TRP D C   1 
ATOM   4415 O  O   . TRP D 2 249 ? -2.770  8.156   24.047  1.00 34.40 ? 237 TRP D O   1 
ATOM   4416 C  CB  . TRP D 2 249 ? 0.283   6.761   23.476  1.00 33.68 ? 237 TRP D CB  1 
ATOM   4417 C  CG  . TRP D 2 249 ? -0.279  5.861   24.471  1.00 34.79 ? 237 TRP D CG  1 
ATOM   4418 C  CD1 . TRP D 2 249 ? -0.906  4.684   24.239  1.00 33.66 ? 237 TRP D CD1 1 
ATOM   4419 C  CD2 . TRP D 2 249 ? -0.276  6.051   25.891  1.00 38.33 ? 237 TRP D CD2 1 
ATOM   4420 N  NE1 . TRP D 2 249 ? -1.305  4.121   25.427  1.00 39.84 ? 237 TRP D NE1 1 
ATOM   4421 C  CE2 . TRP D 2 249 ? -0.935  4.947   26.458  1.00 41.80 ? 237 TRP D CE2 1 
ATOM   4422 C  CE3 . TRP D 2 249 ? 0.209   7.053   26.737  1.00 35.05 ? 237 TRP D CE3 1 
ATOM   4423 C  CZ2 . TRP D 2 249 ? -1.113  4.809   27.847  1.00 40.97 ? 237 TRP D CZ2 1 
ATOM   4424 C  CZ3 . TRP D 2 249 ? 0.030   6.915   28.120  1.00 36.82 ? 237 TRP D CZ3 1 
ATOM   4425 C  CH2 . TRP D 2 249 ? -0.624  5.806   28.656  1.00 34.64 ? 237 TRP D CH2 1 
ATOM   4426 N  N   . ILE D 2 250 ? -0.974  9.455   24.463  1.00 35.78 ? 238 ILE D N   1 
ATOM   4427 C  CA  . ILE D 2 250 ? -1.681  10.278  25.435  1.00 37.63 ? 238 ILE D CA  1 
ATOM   4428 C  C   . ILE D 2 250 ? -3.023  10.721  24.865  1.00 39.86 ? 238 ILE D C   1 
ATOM   4429 O  O   . ILE D 2 250 ? -4.087  10.426  25.433  1.00 42.52 ? 238 ILE D O   1 
ATOM   4430 C  CB  . ILE D 2 250 ? -0.808  11.473  25.851  1.00 32.72 ? 238 ILE D CB  1 
ATOM   4431 C  CG1 . ILE D 2 250 ? 0.385   10.976  26.674  1.00 38.02 ? 238 ILE D CG1 1 
ATOM   4432 C  CG2 . ILE D 2 250 ? -1.624  12.461  26.632  1.00 36.60 ? 238 ILE D CG2 1 
ATOM   4433 C  CD1 . ILE D 2 250 ? 1.564   11.958  26.778  1.00 37.82 ? 238 ILE D CD1 1 
ATOM   4434 N  N   . GLN D 2 251 ? -2.994  11.363  23.685  1.00 38.85 ? 239 GLN D N   1 
ATOM   4435 C  CA  . GLN D 2 251 ? -4.234  11.891  23.121  1.00 40.11 ? 239 GLN D CA  1 
ATOM   4436 C  C   . GLN D 2 251 ? -5.220  10.769  22.855  1.00 39.19 ? 239 GLN D C   1 
ATOM   4437 O  O   . GLN D 2 251 ? -6.407  10.885  23.192  1.00 37.81 ? 239 GLN D O   1 
ATOM   4438 C  CB  . GLN D 2 251 ? -3.972  12.695  21.843  1.00 34.23 ? 239 GLN D CB  1 
ATOM   4439 C  CG  . GLN D 2 251 ? -3.651  14.181  22.072  1.00 41.94 ? 239 GLN D CG  1 
ATOM   4440 C  CD  . GLN D 2 251 ? -4.793  14.967  22.739  1.00 55.42 ? 239 GLN D CD  1 
ATOM   4441 O  OE1 . GLN D 2 251 ? -5.911  14.458  22.916  1.00 53.21 ? 239 GLN D OE1 1 
ATOM   4442 N  NE2 . GLN D 2 251 ? -4.514  16.222  23.094  1.00 49.90 ? 239 GLN D NE2 1 
ATOM   4443 N  N   . LYS D 2 252 ? -4.736  9.662   22.281  1.00 37.50 ? 240 LYS D N   1 
ATOM   4444 C  CA  . LYS D 2 252 ? -5.607  8.526   22.028  1.00 39.81 ? 240 LYS D CA  1 
ATOM   4445 C  C   . LYS D 2 252 ? -6.381  8.198   23.300  1.00 39.29 ? 240 LYS D C   1 
ATOM   4446 O  O   . LYS D 2 252 ? -7.620  8.258   23.327  1.00 41.42 ? 240 LYS D O   1 
ATOM   4447 C  CB  . LYS D 2 252 ? -4.783  7.334   21.506  1.00 39.25 ? 240 LYS D CB  1 
ATOM   4448 C  CG  . LYS D 2 252 ? -5.617  6.187   20.912  1.00 39.61 ? 240 LYS D CG  1 
ATOM   4449 C  CD  . LYS D 2 252 ? -5.005  4.791   21.153  1.00 51.09 ? 240 LYS D CD  1 
ATOM   4450 C  CE  . LYS D 2 252 ? -4.945  4.405   22.652  1.00 61.00 ? 240 LYS D CE  1 
ATOM   4451 N  NZ  . LYS D 2 252 ? -6.139  3.622   23.169  1.00 61.46 ? 240 LYS D NZ  1 
ATOM   4452 N  N   . VAL D 2 253 ? -5.648  7.971   24.400  1.00 42.34 ? 241 VAL D N   1 
ATOM   4453 C  CA  . VAL D 2 253 ? -6.289  7.604   25.664  1.00 42.45 ? 241 VAL D CA  1 
ATOM   4454 C  C   . VAL D 2 253 ? -7.298  8.667   26.063  1.00 37.38 ? 241 VAL D C   1 
ATOM   4455 O  O   . VAL D 2 253 ? -8.471  8.375   26.343  1.00 38.93 ? 241 VAL D O   1 
ATOM   4456 C  CB  . VAL D 2 253 ? -5.229  7.396   26.757  1.00 42.19 ? 241 VAL D CB  1 
ATOM   4457 C  CG1 . VAL D 2 253 ? -5.901  7.138   28.094  1.00 39.28 ? 241 VAL D CG1 1 
ATOM   4458 C  CG2 . VAL D 2 253 ? -4.281  6.272   26.356  1.00 35.63 ? 241 VAL D CG2 1 
ATOM   4459 N  N   . ILE D 2 254 ? -6.865  9.929   26.029  1.00 35.13 ? 242 ILE D N   1 
ATOM   4460 C  CA  . ILE D 2 254 ? -7.717  11.015  26.493  1.00 36.87 ? 242 ILE D CA  1 
ATOM   4461 C  C   . ILE D 2 254 ? -8.972  11.079  25.657  1.00 37.65 ? 242 ILE D C   1 
ATOM   4462 O  O   . ILE D 2 254 ? -10.076 11.268  26.181  1.00 39.90 ? 242 ILE D O   1 
ATOM   4463 C  CB  . ILE D 2 254 ? -6.958  12.348  26.450  1.00 36.35 ? 242 ILE D CB  1 
ATOM   4464 C  CG1 . ILE D 2 254 ? -5.893  12.380  27.551  1.00 36.67 ? 242 ILE D CG1 1 
ATOM   4465 C  CG2 . ILE D 2 254 ? -7.930  13.500  26.558  1.00 29.44 ? 242 ILE D CG2 1 
ATOM   4466 C  CD1 . ILE D 2 254 ? -4.989  13.590  27.457  1.00 35.02 ? 242 ILE D CD1 1 
ATOM   4467 N  N   . ASP D 2 255 ? -8.837  10.873  24.344  1.00 45.21 ? 243 ASP D N   1 
ATOM   4468 C  CA  . ASP D 2 255 ? -10.020 10.994  23.501  1.00 39.86 ? 243 ASP D CA  1 
ATOM   4469 C  C   . ASP D 2 255 ? -10.950 9.829   23.746  1.00 39.90 ? 243 ASP D C   1 
ATOM   4470 O  O   . ASP D 2 255 ? -12.168 10.007  23.838  1.00 36.82 ? 243 ASP D O   1 
ATOM   4471 C  CB  . ASP D 2 255 ? -9.634  11.033  22.028  1.00 40.10 ? 243 ASP D CB  1 
ATOM   4472 C  CG  . ASP D 2 255 ? -8.886  12.290  21.658  1.00 51.99 ? 243 ASP D CG  1 
ATOM   4473 O  OD1 . ASP D 2 255 ? -8.834  13.201  22.518  1.00 52.88 ? 243 ASP D OD1 1 
ATOM   4474 O  OD2 . ASP D 2 255 ? -8.369  12.372  20.511  1.00 47.43 ? 243 ASP D OD2 1 
ATOM   4475 N  N   . GLN D 2 256 ? -10.380 8.643   23.955  1.00 36.94 ? 244 GLN D N   1 
ATOM   4476 C  CA  . GLN D 2 256 ? -11.225 7.470   24.014  1.00 37.81 ? 244 GLN D CA  1 
ATOM   4477 C  C   . GLN D 2 256 ? -11.989 7.385   25.327  1.00 40.60 ? 244 GLN D C   1 
ATOM   4478 O  O   . GLN D 2 256 ? -13.185 7.091   25.319  1.00 39.60 ? 244 GLN D O   1 
ATOM   4479 C  CB  . GLN D 2 256 ? -10.385 6.225   23.784  1.00 37.80 ? 244 GLN D CB  1 
ATOM   4480 C  CG  . GLN D 2 256 ? -11.105 4.952   24.157  1.00 42.92 ? 244 GLN D CG  1 
ATOM   4481 C  CD  . GLN D 2 256 ? -10.666 3.790   23.311  1.00 51.58 ? 244 GLN D CD  1 
ATOM   4482 O  OE1 . GLN D 2 256 ? -11.262 2.712   23.354  1.00 48.50 ? 244 GLN D OE1 1 
ATOM   4483 N  NE2 . GLN D 2 256 ? -9.614  4.002   22.516  1.00 59.83 ? 244 GLN D NE2 1 
ATOM   4484 N  N   . PHE D 2 257 ? -11.331 7.676   26.452  1.00 43.54 ? 245 PHE D N   1 
ATOM   4485 C  CA  . PHE D 2 257 ? -11.915 7.485   27.774  1.00 41.03 ? 245 PHE D CA  1 
ATOM   4486 C  C   . PHE D 2 257 ? -12.130 8.781   28.543  1.00 38.44 ? 245 PHE D C   1 
ATOM   4487 O  O   . PHE D 2 257 ? -12.458 8.726   29.728  1.00 38.00 ? 245 PHE D O   1 
ATOM   4488 C  CB  . PHE D 2 257 ? -11.039 6.556   28.617  1.00 42.04 ? 245 PHE D CB  1 
ATOM   4489 C  CG  . PHE D 2 257 ? -10.629 5.285   27.919  1.00 41.90 ? 245 PHE D CG  1 
ATOM   4490 C  CD1 . PHE D 2 257 ? -11.499 4.195   27.858  1.00 41.84 ? 245 PHE D CD1 1 
ATOM   4491 C  CD2 . PHE D 2 257 ? -9.365  5.166   27.351  1.00 39.05 ? 245 PHE D CD2 1 
ATOM   4492 C  CE1 . PHE D 2 257 ? -11.121 3.018   27.224  1.00 36.36 ? 245 PHE D CE1 1 
ATOM   4493 C  CE2 . PHE D 2 257 ? -8.971  3.982   26.711  1.00 38.23 ? 245 PHE D CE2 1 
ATOM   4494 C  CZ  . PHE D 2 257 ? -9.852  2.914   26.646  1.00 40.51 ? 245 PHE D CZ  1 
ATOM   4495 N  N   . GLY D 2 258 ? -11.965 9.946   27.916  1.00 40.64 ? 246 GLY D N   1 
ATOM   4496 C  CA  . GLY D 2 258 ? -12.175 11.185  28.653  1.00 38.12 ? 246 GLY D CA  1 
ATOM   4497 C  C   . GLY D 2 258 ? -13.571 11.311  29.245  1.00 42.49 ? 246 GLY D C   1 
ATOM   4498 O  O   . GLY D 2 258 ? -13.747 11.871  30.335  1.00 40.52 ? 246 GLY D O   1 
ATOM   4499 N  N   . GLU D 2 259 ? -14.577 10.795  28.547  1.00 42.85 ? 247 GLU D N   1 
ATOM   4500 C  CA  . GLU D 2 259 ? -15.957 11.081  28.890  1.00 38.23 ? 247 GLU D CA  1 
ATOM   4501 C  C   . GLU D 2 259 ? -16.428 10.190  30.026  1.00 45.29 ? 247 GLU D C   1 
ATOM   4502 O  O   . GLU D 2 259 ? -16.141 8.990   30.058  1.00 45.18 ? 247 GLU D O   1 
ATOM   4503 C  CB  . GLU D 2 259 ? -16.849 10.889  27.675  1.00 37.94 ? 247 GLU D CB  1 
ATOM   4504 C  CG  . GLU D 2 259 ? -17.299 12.198  27.063  1.00 48.20 ? 247 GLU D CG  1 
ATOM   4505 C  CD  . GLU D 2 259 ? -18.266 12.010  25.915  1.00 50.25 ? 247 GLU D CD  1 
ATOM   4506 O  OE1 . GLU D 2 259 ? -18.479 10.845  25.509  1.00 47.02 ? 247 GLU D OE1 1 
ATOM   4507 O  OE2 . GLU D 2 259 ? -18.823 13.030  25.441  1.00 52.10 ? 247 GLU D OE2 1 
ATOM   4508 N  N   . TYR D 2 260 ? -17.136 10.793  30.969  1.00 41.28 ? 248 TYR D N   1 
ATOM   4509 C  CA  . TYR D 2 260 ? -17.758 10.042  32.039  1.00 47.02 ? 248 TYR D CA  1 
ATOM   4510 C  C   . TYR D 2 260 ? -19.090 9.488   31.557  1.00 42.45 ? 248 TYR D C   1 
ATOM   4511 O  O   . TYR D 2 260 ? -19.700 10.017  30.635  1.00 44.77 ? 248 TYR D O   1 
ATOM   4512 C  CB  . TYR D 2 260 ? -17.982 10.936  33.261  1.00 45.86 ? 248 TYR D CB  1 
ATOM   4513 C  CG  . TYR D 2 260 ? -16.737 11.385  33.989  1.00 39.78 ? 248 TYR D CG  1 
ATOM   4514 C  CD1 . TYR D 2 260 ? -16.035 10.509  34.811  1.00 40.86 ? 248 TYR D CD1 1 
ATOM   4515 C  CD2 . TYR D 2 260 ? -16.275 12.689  33.872  1.00 36.32 ? 248 TYR D CD2 1 
ATOM   4516 C  CE1 . TYR D 2 260 ? -14.918 10.911  35.501  1.00 38.35 ? 248 TYR D CE1 1 
ATOM   4517 C  CE2 . TYR D 2 260 ? -15.153 13.113  34.561  1.00 40.08 ? 248 TYR D CE2 1 
ATOM   4518 C  CZ  . TYR D 2 260 ? -14.470 12.218  35.375  1.00 42.27 ? 248 TYR D CZ  1 
ATOM   4519 O  OH  . TYR D 2 260 ? -13.340 12.627  36.065  1.00 38.16 ? 248 TYR D OH  1 
ATOM   4520 N  N   . LEU D 2 261 ? -19.564 8.438   32.229  1.00 46.12 ? 249 LEU D N   1 
ATOM   4521 C  CA  . LEU D 2 261 ? -20.798 7.779   31.803  1.00 50.99 ? 249 LEU D CA  1 
ATOM   4522 C  C   . LEU D 2 261 ? -22.001 8.722   31.855  1.00 44.49 ? 249 LEU D C   1 
ATOM   4523 O  O   . LEU D 2 261 ? -22.875 8.673   30.980  1.00 40.00 ? 249 LEU D O   1 
ATOM   4524 C  CB  . LEU D 2 261 ? -21.043 6.534   32.657  1.00 54.12 ? 249 LEU D CB  1 
ATOM   4525 C  CG  . LEU D 2 261 ? -20.183 5.354   32.197  1.00 49.29 ? 249 LEU D CG  1 
ATOM   4526 C  CD1 . LEU D 2 261 ? -19.938 4.360   33.318  1.00 52.36 ? 249 LEU D CD1 1 
ATOM   4527 C  CD2 . LEU D 2 261 ? -20.829 4.682   31.014  1.00 46.80 ? 249 LEU D CD2 1 
ATOM   4528 N  N   . GLU D 2 262 ? -22.061 9.597   32.862  1.00 47.30 ? 250 GLU D N   1 
ATOM   4529 C  CA  . GLU D 2 262 ? -23.154 10.566  32.898  1.00 49.77 ? 250 GLU D CA  1 
ATOM   4530 C  C   . GLU D 2 262 ? -23.075 11.570  31.759  1.00 46.06 ? 250 GLU D C   1 
ATOM   4531 O  O   . GLU D 2 262 ? -24.043 12.295  31.527  1.00 45.14 ? 250 GLU D O   1 
ATOM   4532 C  CB  . GLU D 2 262 ? -23.183 11.329  34.232  1.00 46.10 ? 250 GLU D CB  1 
ATOM   4533 C  CG  . GLU D 2 262 ? -21.923 12.119  34.571  1.00 54.28 ? 250 GLU D CG  1 
ATOM   4534 C  CD  . GLU D 2 262 ? -20.813 11.300  35.220  1.00 57.19 ? 250 GLU D CD  1 
ATOM   4535 O  OE1 . GLU D 2 262 ? -20.918 10.054  35.286  1.00 59.15 ? 250 GLU D OE1 1 
ATOM   4536 O  OE2 . GLU D 2 262 ? -19.825 11.927  35.668  1.00 58.40 ? 250 GLU D OE2 1 
ATOM   4537 N  N   . ASP D 2 263 ? -21.941 11.644  31.067  1.00 48.67 ? 251 ASP D N   1 
ATOM   4538 C  CA  . ASP D 2 263 ? -21.808 12.507  29.907  1.00 45.39 ? 251 ASP D CA  1 
ATOM   4539 C  C   . ASP D 2 263 ? -22.326 11.868  28.626  1.00 44.23 ? 251 ASP D C   1 
ATOM   4540 O  O   . ASP D 2 263 ? -22.535 12.583  27.649  1.00 44.36 ? 251 ASP D O   1 
ATOM   4541 C  CB  . ASP D 2 263 ? -20.343 12.912  29.686  1.00 49.52 ? 251 ASP D CB  1 
ATOM   4542 C  CG  . ASP D 2 263 ? -19.768 13.764  30.817  1.00 52.01 ? 251 ASP D CG  1 
ATOM   4543 O  OD1 . ASP D 2 263 ? -20.542 14.456  31.524  1.00 46.55 ? 251 ASP D OD1 1 
ATOM   4544 O  OD2 . ASP D 2 263 ? -18.517 13.749  30.966  1.00 53.28 ? 251 ASP D OD2 1 
ATOM   4545 N  N   . GLN D 2 264 ? -22.536 10.555  28.583  1.00 43.55 ? 252 GLN D N   1 
ATOM   4546 C  CA  . GLN D 2 264 ? -22.889 9.956   27.302  1.00 45.65 ? 252 GLN D CA  1 
ATOM   4547 C  C   . GLN D 2 264 ? -24.317 9.418   27.238  1.00 50.32 ? 252 GLN D C   1 
ATOM   4548 O  O   . GLN D 2 264 ? -24.543 8.320   26.718  1.00 52.51 ? 252 GLN D O   1 
ATOM   4549 C  CB  . GLN D 2 264 ? -21.895 8.845   26.957  1.00 51.33 ? 252 GLN D CB  1 
ATOM   4550 C  CG  . GLN D 2 264 ? -20.471 9.100   27.429  1.00 51.06 ? 252 GLN D CG  1 
ATOM   4551 C  CD  . GLN D 2 264 ? -19.624 7.838   27.442  1.00 55.63 ? 252 GLN D CD  1 
ATOM   4552 O  OE1 . GLN D 2 264 ? -19.957 6.858   28.112  1.00 57.75 ? 252 GLN D OE1 1 
ATOM   4553 N  NE2 . GLN D 2 264 ? -18.538 7.844   26.664  1.00 57.53 ? 252 GLN D NE2 1 
ATOM   4554 N  N   . VAL D 2 265 ? -25.297 10.185  27.707  1.00 47.74 ? 253 VAL D N   1 
ATOM   4555 C  CA  . VAL D 2 265 ? -26.667 9.695   27.677  1.00 49.64 ? 253 VAL D CA  1 
ATOM   4556 C  C   . VAL D 2 265 ? -27.389 10.167  26.414  1.00 39.15 ? 253 VAL D C   1 
ATOM   4557 O  O   . VAL D 2 265 ? -27.590 11.368  26.218  1.00 46.16 ? 253 VAL D O   1 
ATOM   4558 C  CB  . VAL D 2 265 ? -27.436 10.128  28.933  1.00 51.38 ? 253 VAL D CB  1 
ATOM   4559 C  CG1 . VAL D 2 265 ? -28.944 9.908   28.737  1.00 41.16 ? 253 VAL D CG1 1 
ATOM   4560 C  CG2 . VAL D 2 265 ? -26.894 9.412   30.165  1.00 46.49 ? 253 VAL D CG2 1 
ATOM   4561 N  N   . PHE E 3 1   ? 34.875  2.101   1.196   1.00 37.59 ? 1   PHE E N   1 
ATOM   4562 C  CA  . PHE E 3 1   ? 34.193  1.717   -0.031  1.00 33.02 ? 1   PHE E CA  1 
ATOM   4563 C  C   . PHE E 3 1   ? 32.763  2.314   -0.016  1.00 37.78 ? 1   PHE E C   1 
ATOM   4564 O  O   . PHE E 3 1   ? 32.669  3.467   -0.320  1.00 41.12 ? 1   PHE E O   1 
ATOM   4565 C  CB  . PHE E 3 1   ? 34.316  0.264   -0.403  1.00 36.48 ? 1   PHE E CB  1 
ATOM   4566 C  CG  . PHE E 3 1   ? 33.482  -0.188  -1.589  1.00 34.35 ? 1   PHE E CG  1 
ATOM   4567 C  CD1 . PHE E 3 1   ? 32.900  -1.455  -1.569  1.00 31.97 ? 1   PHE E CD1 1 
ATOM   4568 C  CD2 . PHE E 3 1   ? 33.318  0.631   -2.684  1.00 31.91 ? 1   PHE E CD2 1 
ATOM   4569 C  CE1 . PHE E 3 1   ? 32.148  -1.901  -2.647  1.00 29.59 ? 1   PHE E CE1 1 
ATOM   4570 C  CE2 . PHE E 3 1   ? 32.556  0.181   -3.759  1.00 34.36 ? 1   PHE E CE2 1 
ATOM   4571 C  CZ  . PHE E 3 1   ? 31.979  -1.079  -3.740  1.00 31.98 ? 1   PHE E CZ  1 
ATOM   4572 N  N   . PRO E 3 2   ? 31.440  1.618   0.218   1.00 38.11 ? 2   PRO E N   1 
ATOM   4573 C  CA  . PRO E 3 2   ? 30.083  2.511   0.091   1.00 38.15 ? 2   PRO E CA  1 
ATOM   4574 C  C   . PRO E 3 2   ? 30.136  3.700   1.012   1.00 33.63 ? 2   PRO E C   1 
ATOM   4575 O  O   . PRO E 3 2   ? 30.480  3.616   2.137   1.00 32.61 ? 2   PRO E O   1 
ATOM   4576 C  CB  . PRO E 3 2   ? 29.021  1.703   0.362   1.00 36.58 ? 2   PRO E CB  1 
ATOM   4577 C  CG  . PRO E 3 2   ? 29.588  0.357   0.926   1.00 34.76 ? 2   PRO E CG  1 
ATOM   4578 C  CD  . PRO E 3 2   ? 31.130  0.367   0.587   1.00 36.11 ? 2   PRO E CD  1 
HETATM 4579 N  N   . PCS E 3 3   ? 29.763  5.008   0.470   1.00 35.71 ? 3   PCS E N   1 
HETATM 4580 C  CA  . PCS E 3 3   ? 29.766  6.215   1.348   1.00 36.63 ? 3   PCS E CA  1 
HETATM 4581 C  C   . PCS E 3 3   ? 28.397  6.439   2.032   1.00 37.27 ? 3   PCS E C   1 
HETATM 4582 C  CB  . PCS E 3 3   ? 30.357  7.394   0.589   1.00 37.39 ? 3   PCS E CB  1 
HETATM 4583 O  O   . PCS E 3 3   ? 28.289  7.312   2.845   1.00 33.64 ? 3   PCS E O   1 
HETATM 4584 C  CD1 . PCS E 3 3   ? 32.744  8.254   0.161   1.00 34.51 ? 3   PCS E CD1 1 
HETATM 4585 C  CG  . PCS E 3 3   ? 31.884  7.402   0.874   1.00 32.40 ? 3   PCS E CG  1 
HETATM 4586 C  CD2 . PCS E 3 3   ? 32.400  6.565   1.883   1.00 40.08 ? 3   PCS E CD2 1 
HETATM 4587 C  CE2 . PCS E 3 3   ? 33.766  6.545   2.182   1.00 37.43 ? 3   PCS E CE2 1 
HETATM 4588 C  CZ  . PCS E 3 3   ? 34.629  7.392   1.452   1.00 40.15 ? 3   PCS E CZ  1 
HETATM 4589 C  CE1 . PCS E 3 3   ? 34.106  8.242   0.442   1.00 41.37 ? 3   PCS E CE1 1 
HETATM 4590 C  CT  . PCS E 3 3   ? 27.196  5.452   1.719   1.00 33.79 ? 3   PCS E CT  1 
ATOM   4591 N  N   . PHE F 3 1   ? 17.934  2.598   40.445  1.00 37.59 ? 1   PHE F N   1 
ATOM   4592 C  CA  . PHE F 3 1   ? 17.449  2.392   39.089  1.00 33.02 ? 1   PHE F CA  1 
ATOM   4593 C  C   . PHE F 3 1   ? 15.987  2.895   38.999  1.00 37.78 ? 1   PHE F C   1 
ATOM   4594 O  O   . PHE F 3 1   ? 15.841  4.076   38.876  1.00 41.12 ? 1   PHE F O   1 
ATOM   4595 C  CB  . PHE F 3 1   ? 17.735  1.034   38.506  1.00 36.48 ? 1   PHE F CB  1 
ATOM   4596 C  CG  . PHE F 3 1   ? 17.100  0.746   37.157  1.00 34.35 ? 1   PHE F CG  1 
ATOM   4597 C  CD1 . PHE F 3 1   ? 16.623  -0.537  36.889  1.00 31.97 ? 1   PHE F CD1 1 
ATOM   4598 C  CD2 . PHE F 3 1   ? 17.014  1.730   36.198  1.00 31.91 ? 1   PHE F CD2 1 
ATOM   4599 C  CE1 . PHE F 3 1   ? 16.055  -0.833  35.658  1.00 29.59 ? 1   PHE F CE1 1 
ATOM   4600 C  CE2 . PHE F 3 1   ? 16.436  1.429   34.968  1.00 34.36 ? 1   PHE F CE2 1 
ATOM   4601 C  CZ  . PHE F 3 1   ? 15.964  0.154   34.700  1.00 31.98 ? 1   PHE F CZ  1 
ATOM   4602 N  N   . PRO F 3 2   ? 14.704  2.096   38.928  1.00 38.11 ? 2   PRO F N   1 
ATOM   4603 C  CA  . PRO F 3 2   ? 13.308  2.918   38.758  1.00 38.15 ? 2   PRO F CA  1 
ATOM   4604 C  C   . PRO F 3 2   ? 13.147  3.933   39.858  1.00 33.63 ? 2   PRO F C   1 
ATOM   4605 O  O   . PRO F 3 2   ? 13.348  3.676   40.992  1.00 32.61 ? 2   PRO F O   1 
ATOM   4606 C  CB  . PRO F 3 2   ? 12.288  2.017   38.742  1.00 36.58 ? 2   PRO F CB  1 
ATOM   4607 C  CG  . PRO F 3 2   ? 12.883  0.628   39.154  1.00 34.76 ? 2   PRO F CG  1 
ATOM   4608 C  CD  . PRO F 3 2   ? 14.450  0.784   39.041  1.00 36.11 ? 2   PRO F CD  1 
HETATM 4609 N  N   . PCS F 3 3   ? 12.744  5.291   39.489  1.00 35.71 ? 3   PCS F N   1 
HETATM 4610 C  CA  . PCS F 3 3   ? 12.537  6.327   40.543  1.00 36.63 ? 3   PCS F CA  1 
HETATM 4611 C  C   . PCS F 3 3   ? 11.078  6.352   41.055  1.00 37.27 ? 3   PCS F C   1 
HETATM 4612 C  CB  . PCS F 3 3   ? 13.125  7.651   40.077  1.00 37.39 ? 3   PCS F CB  1 
HETATM 4613 O  O   . PCS F 3 3   ? 10.796  7.065   41.975  1.00 33.64 ? 3   PCS F O   1 
HETATM 4614 C  CD1 . PCS F 3 3   ? 15.471  8.706   40.135  1.00 34.51 ? 3   PCS F CD1 1 
HETATM 4615 C  CG  . PCS F 3 3   ? 14.597  7.696   40.571  1.00 32.40 ? 3   PCS F CG  1 
HETATM 4616 C  CD2 . PCS F 3 3   ? 15.044  6.729   41.493  1.00 40.08 ? 3   PCS F CD2 1 
HETATM 4617 C  CE2 . PCS F 3 3   ? 16.356  6.736   41.975  1.00 37.43 ? 3   PCS F CE2 1 
HETATM 4618 C  CZ  . PCS F 3 3   ? 17.236  7.743   41.521  1.00 40.15 ? 3   PCS F CZ  1 
HETATM 4619 C  CE1 . PCS F 3 3   ? 16.782  8.723   40.599  1.00 41.37 ? 3   PCS F CE1 1 
HETATM 4620 C  CT  . PCS F 3 3   ? 10.010  5.367   40.419  1.00 33.79 ? 3   PCS F CT  1 
HETATM 4621 NA NA  . NA  G 4 .   ? 42.781  11.999  -3.187  1.00 41.23 ? 301 NA  B NA  1 
HETATM 4622 NA NA  . NA  H 4 .   ? 24.857  13.317  38.435  1.00 50.00 ? 301 NA  D NA  1 
HETATM 4623 O  O   . HOH I 5 .   ? 39.349  27.280  -10.257 1.00 37.20 ? 101 HOH A O   1 
HETATM 4624 O  O   . HOH J 5 .   ? 16.434  19.160  13.637  1.00 40.53 ? 401 HOH B O   1 
HETATM 4625 O  O   . HOH J 5 .   ? 18.766  31.307  -15.439 1.00 49.78 ? 402 HOH B O   1 
HETATM 4626 O  O   . HOH J 5 .   ? 27.028  34.811  2.722   1.00 37.54 ? 403 HOH B O   1 
HETATM 4627 O  O   . HOH J 5 .   ? 38.834  0.433   -12.129 1.00 42.55 ? 404 HOH B O   1 
HETATM 4628 O  O   . HOH J 5 .   ? 5.542   5.531   5.944   1.00 48.34 ? 405 HOH B O   1 
HETATM 4629 O  O   . HOH J 5 .   ? 45.824  14.638  -2.692  1.00 50.00 ? 406 HOH B O   1 
HETATM 4630 O  O   . HOH J 5 .   ? 39.806  -1.668  -1.453  1.00 38.20 ? 407 HOH B O   1 
HETATM 4631 O  O   . HOH J 5 .   ? 23.097  16.262  2.968   1.00 34.89 ? 408 HOH B O   1 
HETATM 4632 O  O   . HOH J 5 .   ? 12.114  26.868  5.562   1.00 37.23 ? 409 HOH B O   1 
HETATM 4633 O  O   . HOH J 5 .   ? 17.933  22.350  2.291   1.00 35.25 ? 410 HOH B O   1 
HETATM 4634 O  O   . HOH J 5 .   ? 26.129  14.479  1.596   1.00 32.59 ? 411 HOH B O   1 
HETATM 4635 O  O   . HOH J 5 .   ? 41.374  16.175  -3.715  1.00 35.21 ? 412 HOH B O   1 
HETATM 4636 O  O   . HOH J 5 .   ? 45.316  13.408  -4.351  1.00 40.79 ? 413 HOH B O   1 
HETATM 4637 O  O   . HOH J 5 .   ? 38.572  18.057  7.064   1.00 35.86 ? 414 HOH B O   1 
HETATM 4638 O  O   . HOH J 5 .   ? 29.604  -5.774  -1.716  1.00 47.75 ? 415 HOH B O   1 
HETATM 4639 O  O   . HOH J 5 .   ? 31.002  17.043  6.349   1.00 28.67 ? 416 HOH B O   1 
HETATM 4640 O  O   . HOH J 5 .   ? 43.338  14.528  4.675   1.00 37.76 ? 417 HOH B O   1 
HETATM 4641 O  O   . HOH J 5 .   ? 25.242  22.284  -2.949  1.00 29.29 ? 418 HOH B O   1 
HETATM 4642 O  O   . HOH J 5 .   ? 35.451  23.230  8.565   1.00 37.02 ? 419 HOH B O   1 
HETATM 4643 O  O   . HOH J 5 .   ? 11.716  32.139  13.930  1.00 48.10 ? 420 HOH B O   1 
HETATM 4644 O  O   . HOH J 5 .   ? 41.705  13.273  -5.179  1.00 34.77 ? 421 HOH B O   1 
HETATM 4645 O  O   . HOH J 5 .   ? 31.165  29.086  2.567   1.00 42.31 ? 422 HOH B O   1 
HETATM 4646 O  O   . HOH J 5 .   ? 42.959  14.360  -2.220  1.00 36.66 ? 423 HOH B O   1 
HETATM 4647 O  O   . HOH J 5 .   ? 21.188  13.320  -4.087  1.00 34.38 ? 424 HOH B O   1 
HETATM 4648 O  O   . HOH J 5 .   ? 10.100  25.063  11.084  1.00 47.17 ? 425 HOH B O   1 
HETATM 4649 O  O   . HOH J 5 .   ? 11.079  29.191  6.466   1.00 39.87 ? 426 HOH B O   1 
HETATM 4650 O  O   . HOH J 5 .   ? 40.675  11.625  -2.020  1.00 50.00 ? 427 HOH B O   1 
HETATM 4651 O  O   . HOH J 5 .   ? 8.051   20.100  9.233   1.00 41.08 ? 428 HOH B O   1 
HETATM 4652 O  O   . HOH J 5 .   ? 25.078  13.435  13.102  1.00 45.39 ? 429 HOH B O   1 
HETATM 4653 O  O   . HOH J 5 .   ? 26.960  20.184  -3.315  1.00 32.17 ? 430 HOH B O   1 
HETATM 4654 O  O   . HOH J 5 .   ? 9.534   26.012  4.507   1.00 41.95 ? 431 HOH B O   1 
HETATM 4655 O  O   . HOH J 5 .   ? 28.606  4.245   -8.005  1.00 34.43 ? 432 HOH B O   1 
HETATM 4656 O  O   . HOH J 5 .   ? 35.419  19.990  5.835   1.00 36.53 ? 433 HOH B O   1 
HETATM 4657 O  O   . HOH J 5 .   ? 38.809  7.288   -2.467  1.00 36.78 ? 434 HOH B O   1 
HETATM 4658 O  O   . HOH J 5 .   ? 43.048  4.409   -0.461  1.00 44.97 ? 435 HOH B O   1 
HETATM 4659 O  O   . HOH J 5 .   ? 26.623  4.646   -10.146 1.00 42.35 ? 436 HOH B O   1 
HETATM 4660 O  O   . HOH J 5 .   ? 25.878  25.053  -3.450  1.00 34.77 ? 437 HOH B O   1 
HETATM 4661 O  O   . HOH J 5 .   ? 22.880  10.838  14.413  1.00 34.17 ? 438 HOH B O   1 
HETATM 4662 O  O   . HOH J 5 .   ? 39.373  13.372  -3.501  1.00 35.31 ? 439 HOH B O   1 
HETATM 4663 O  O   . HOH J 5 .   ? 6.274   24.143  -2.497  1.00 49.69 ? 440 HOH B O   1 
HETATM 4664 O  O   . HOH J 5 .   ? 25.267  10.187  12.664  1.00 40.45 ? 441 HOH B O   1 
HETATM 4665 O  O   . HOH J 5 .   ? 37.959  20.482  7.367   1.00 44.14 ? 442 HOH B O   1 
HETATM 4666 O  O   . HOH J 5 .   ? 24.453  -4.587  -16.254 1.00 52.71 ? 443 HOH B O   1 
HETATM 4667 O  O   . HOH K 5 .   ? 12.771  26.097  30.699  1.00 32.12 ? 101 HOH C O   1 
HETATM 4668 O  O   . HOH K 5 .   ? 6.095   34.158  36.319  1.00 30.27 ? 102 HOH C O   1 
HETATM 4669 O  O   . HOH K 5 .   ? 13.475  34.105  38.566  1.00 32.98 ? 103 HOH C O   1 
HETATM 4670 O  O   . HOH K 5 .   ? -0.371  29.504  41.165  1.00 34.52 ? 104 HOH C O   1 
HETATM 4671 O  O   . HOH K 5 .   ? 12.469  38.674  39.844  1.00 38.95 ? 105 HOH C O   1 
HETATM 4672 O  O   . HOH K 5 .   ? 12.657  36.758  41.592  1.00 33.61 ? 106 HOH C O   1 
HETATM 4673 O  O   . HOH L 5 .   ? 27.683  21.443  28.813  1.00 45.30 ? 401 HOH D O   1 
HETATM 4674 O  O   . HOH L 5 .   ? -26.509 13.032  25.096  1.00 38.22 ? 402 HOH D O   1 
HETATM 4675 O  O   . HOH L 5 .   ? 14.520  -2.864  39.361  1.00 30.25 ? 403 HOH D O   1 
HETATM 4676 O  O   . HOH L 5 .   ? 20.716  9.410   39.232  1.00 35.95 ? 404 HOH D O   1 
HETATM 4677 O  O   . HOH L 5 .   ? 29.387  10.298  32.603  1.00 35.19 ? 405 HOH D O   1 
HETATM 4678 O  O   . HOH L 5 .   ? 23.189  12.520  39.778  1.00 50.00 ? 406 HOH D O   1 
HETATM 4679 O  O   . HOH L 5 .   ? -7.299  24.325  45.893  1.00 34.13 ? 407 HOH D O   1 
HETATM 4680 O  O   . HOH L 5 .   ? 18.219  6.933   22.151  1.00 33.25 ? 408 HOH D O   1 
HETATM 4681 O  O   . HOH L 5 .   ? 6.997   10.032  56.400  1.00 57.09 ? 409 HOH D O   1 
HETATM 4682 O  O   . HOH L 5 .   ? 28.169  15.895  39.320  1.00 36.97 ? 410 HOH D O   1 
HETATM 4683 O  O   . HOH L 5 .   ? 6.698   33.525  46.104  1.00 39.03 ? 411 HOH D O   1 
HETATM 4684 O  O   . HOH L 5 .   ? 3.440   24.501  43.733  1.00 32.07 ? 412 HOH D O   1 
HETATM 4685 O  O   . HOH L 5 .   ? -0.780  20.842  42.838  1.00 20.57 ? 413 HOH D O   1 
HETATM 4686 O  O   . HOH L 5 .   ? 12.253  15.988  47.449  1.00 30.67 ? 414 HOH D O   1 
HETATM 4687 O  O   . HOH L 5 .   ? 2.832   19.562  17.265  1.00 42.89 ? 415 HOH D O   1 
HETATM 4688 O  O   . HOH L 5 .   ? 25.556  15.603  39.968  1.00 37.54 ? 416 HOH D O   1 
HETATM 4689 O  O   . HOH L 5 .   ? 4.648   15.378  43.115  1.00 31.03 ? 417 HOH D O   1 
HETATM 4690 O  O   . HOH L 5 .   ? 6.970   -7.124  28.656  1.00 41.28 ? 418 HOH D O   1 
HETATM 4691 O  O   . HOH L 5 .   ? 4.116   13.382  35.158  1.00 26.82 ? 419 HOH D O   1 
HETATM 4692 O  O   . HOH L 5 .   ? 5.252   21.389  56.791  1.00 52.96 ? 420 HOH D O   1 
HETATM 4693 O  O   . HOH L 5 .   ? 12.088  5.796   30.845  1.00 29.88 ? 421 HOH D O   1 
HETATM 4694 O  O   . HOH L 5 .   ? -3.270  -4.491  43.314  1.00 47.26 ? 422 HOH D O   1 
HETATM 4695 O  O   . HOH L 5 .   ? 27.576  14.892  37.027  1.00 36.73 ? 423 HOH D O   1 
HETATM 4696 O  O   . HOH L 5 .   ? 28.754  10.111  29.614  1.00 37.79 ? 424 HOH D O   1 
HETATM 4697 O  O   . HOH L 5 .   ? 11.479  21.293  53.333  1.00 36.62 ? 425 HOH D O   1 
HETATM 4698 O  O   . HOH L 5 .   ? 8.670   20.708  38.022  1.00 24.26 ? 426 HOH D O   1 
HETATM 4699 O  O   . HOH L 5 .   ? 23.916  8.286   34.082  1.00 35.85 ? 427 HOH D O   1 
HETATM 4700 O  O   . HOH L 5 .   ? 20.830  22.910  42.616  1.00 37.01 ? 428 HOH D O   1 
HETATM 4701 O  O   . HOH L 5 .   ? -6.968  28.093  38.415  1.00 38.81 ? 429 HOH D O   1 
HETATM 4702 O  O   . HOH L 5 .   ? -5.566  34.352  41.761  1.00 40.59 ? 430 HOH D O   1 
HETATM 4703 O  O   . HOH L 5 .   ? 20.537  18.887  22.079  1.00 41.77 ? 431 HOH D O   1 
HETATM 4704 O  O   . HOH L 5 .   ? 23.583  17.804  38.544  1.00 32.11 ? 432 HOH D O   1 
HETATM 4705 O  O   . HOH L 5 .   ? 13.793  15.211  21.301  1.00 39.41 ? 433 HOH D O   1 
HETATM 4706 O  O   . HOH L 5 .   ? 19.125  14.133  26.273  1.00 28.15 ? 434 HOH D O   1 
HETATM 4707 O  O   . HOH L 5 .   ? 10.706  6.685   28.751  1.00 31.35 ? 435 HOH D O   1 
HETATM 4708 O  O   . HOH L 5 .   ? -9.235  5.349   43.745  1.00 31.85 ? 436 HOH D O   1 
HETATM 4709 O  O   . HOH L 5 .   ? 7.030   25.210  38.479  1.00 28.00 ? 437 HOH D O   1 
HETATM 4710 O  O   . HOH L 5 .   ? 11.772  4.035   43.541  1.00 39.17 ? 438 HOH D O   1 
HETATM 4711 O  O   . HOH L 5 .   ? 6.616   22.520  38.044  1.00 24.91 ? 439 HOH D O   1 
HETATM 4712 O  O   . HOH L 5 .   ? 5.970   30.421  49.306  1.00 40.58 ? 440 HOH D O   1 
HETATM 4713 O  O   . HOH L 5 .   ? 23.368  9.421   40.100  1.00 33.33 ? 441 HOH D O   1 
HETATM 4714 O  O   . HOH L 5 .   ? -0.332  18.264  45.300  1.00 36.56 ? 442 HOH D O   1 
HETATM 4715 O  O   . HOH L 5 .   ? 22.166  8.479   37.440  1.00 37.67 ? 443 HOH D O   1 
HETATM 4716 O  O   . HOH L 5 .   ? 24.240  20.150  29.477  1.00 33.34 ? 444 HOH D O   1 
HETATM 4717 O  O   . HOH L 5 .   ? 5.883   27.374  22.864  1.00 35.37 ? 445 HOH D O   1 
HETATM 4718 O  O   . HOH L 5 .   ? 21.416  14.705  38.003  1.00 31.29 ? 446 HOH D O   1 
HETATM 4719 O  O   . HOH L 5 .   ? -12.411 24.050  37.613  1.00 32.61 ? 447 HOH D O   1 
HETATM 4720 O  O   . HOH L 5 .   ? 4.328   22.798  16.111  1.00 40.23 ? 448 HOH D O   1 
HETATM 4721 O  O   . HOH L 5 .   ? -0.400  24.661  50.364  1.00 41.86 ? 449 HOH D O   1 
HETATM 4722 O  O   . HOH L 5 .   ? 25.096  19.665  31.854  1.00 34.47 ? 450 HOH D O   1 
HETATM 4723 O  O   . HOH L 5 .   ? 24.322  15.149  37.214  1.00 35.74 ? 451 HOH D O   1 
HETATM 4724 O  O   . HOH L 5 .   ? 15.364  4.275   20.703  1.00 35.91 ? 452 HOH D O   1 
HETATM 4725 O  O   . HOH L 5 .   ? -3.311  -0.379  31.265  1.00 41.56 ? 453 HOH D O   1 
HETATM 4726 O  O   . HOH L 5 .   ? 15.544  22.011  51.259  1.00 41.41 ? 454 HOH D O   1 
HETATM 4727 O  O   . HOH L 5 .   ? 32.809  17.279  41.634  1.00 49.62 ? 455 HOH D O   1 
HETATM 4728 O  O   . HOH L 5 .   ? 29.991  11.523  24.613  1.00 47.64 ? 456 HOH D O   1 
HETATM 4729 O  O   . HOH L 5 .   ? -9.504  16.198  29.460  1.00 38.73 ? 457 HOH D O   1 
HETATM 4730 O  O   . HOH L 5 .   ? -8.336  29.995  44.447  1.00 26.05 ? 458 HOH D O   1 
HETATM 4731 O  O   . HOH L 5 .   ? 24.865  26.498  34.141  1.00 33.58 ? 459 HOH D O   1 
HETATM 4732 O  O   . HOH L 5 .   ? -29.398 13.738  27.188  1.00 43.85 ? 460 HOH D O   1 
HETATM 4733 O  O   . HOH L 5 .   ? 17.481  -3.778  21.976  1.00 49.37 ? 461 HOH D O   1 
HETATM 4734 O  O   . HOH L 5 .   ? -10.876 14.366  28.559  1.00 37.15 ? 462 HOH D O   1 
HETATM 4735 O  O   . HOH L 5 .   ? 0.001   25.059  47.915  1.00 40.61 ? 463 HOH D O   1 
HETATM 4736 O  O   . HOH L 5 .   ? 8.739   -4.178  26.074  1.00 45.40 ? 464 HOH D O   1 
HETATM 4737 O  O   . HOH L 5 .   ? 8.523   -5.534  29.533  1.00 35.13 ? 465 HOH D O   1 
HETATM 4738 O  O   . HOH L 5 .   ? -5.072  17.268  26.237  1.00 42.23 ? 466 HOH D O   1 
HETATM 4739 O  O   . HOH L 5 .   ? 16.007  14.793  22.798  1.00 43.58 ? 467 HOH D O   1 
HETATM 4740 O  O   . HOH L 5 .   ? 17.972  14.944  24.299  1.00 31.18 ? 468 HOH D O   1 
HETATM 4741 O  O   . HOH L 5 .   ? 14.118  20.553  53.431  1.00 39.26 ? 469 HOH D O   1 
HETATM 4742 O  O   . HOH L 5 .   ? -31.499 11.794  23.540  1.00 39.14 ? 470 HOH D O   1 
HETATM 4743 O  O   . HOH L 5 .   ? -30.708 9.651   22.294  1.00 40.85 ? 471 HOH D O   1 
# 
