data_9IF9
# 
_entry.id   9IF9 
# 
_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   9IF9         pdb_00009if9 10.2210/pdb9if9/pdb 
WWPDB D_1292145520 ?            ?                   
# 
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 2025-03-05 ? 
2 'Structure model' 1 1 2025-03-26 ? 
# 
_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.country'                 
2 2 'Structure model' '_citation.journal_abbrev'          
3 2 'Structure model' '_citation.journal_id_CSD'          
4 2 'Structure model' '_citation.journal_id_ISSN'         
5 2 'Structure model' '_citation.journal_volume'          
6 2 'Structure model' '_citation.pdbx_database_id_DOI'    
7 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IF9 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 s.j.smerdon@bham.ac.uk Stephen Smerdon J 'principal investigator/group leader' 0000-0001-5688-8465 
4 manuel.stucki@uzh.ch.  Manuel  Stucki  ? 'principal investigator/group leader' 0000-0002-9974-0134 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Stewart, M.J.'      1 0000-0002-4421-5623 
'Torres Esteban, M.' 2 ?                   
'Smerdon, S.J.'      3 0000-0001-5688-8465 
'Stucki, M.'         4 0000-0002-9974-0134 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Life Sci Alliance' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2575-1077 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'MDC1 mediates Pellino recruitment to sites of DNA double-strand breaks.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.26508/lsa.202403074 
_citation.pdbx_database_id_PubMed   40049731 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Torres Esteban, M.' 1 ?                   
primary 'Stewart, M.J.'      2 ?                   
primary 'Bragginton, E.'     3 0000-0003-0256-6537 
primary 'Meroni, A.'         4 0000-0003-3568-8207 
primary 'Pellizzari, A.'     5 ?                   
primary 'Jeanrenaud, A.'     6 ?                   
primary 'Smerdon, S.J.'      7 0000-0001-5688-8465 
primary 'Stucki, M.'         8 0000-0002-9974-0134 
# 
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 'E3 ubiquitin-protein ligase pellino homolog 1' 27566.004 2  2.3.2.27 ?       ? ? 
2 polymer     syn 'Mediator of DNA damage checkpoint protein 1'   1381.249  2  ?        'A1 Y2' ? ? 
3 non-polymer syn 'SULFATE ION'                                   96.063    5  ?        ?       ? ? 
4 water       nat water                                           18.015    70 ?        ?       ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Pellino-1,Pellino-related intracellular-signaling molecule,RING-type E3 ubiquitin transferase pellino homolog 1' 
2 'Nuclear factor with BRCT domains 1'                                                                              
# 
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  
;APVKYGELIVLGYNGSLPNGDRGRRKSRFALFKRPKANGVKPSTVHIACTPQAAKAISNKDQHSISYTLSRAQTVVVEYT
HDSNTDMFQIGRSTESPIDFVVTDTVPGSQSNSDTQSVQSTISRFACRIICERNPPFTARIYAAGFDSSKNIFLGEKAAK
WKTSDGQMDGLTTNGVLVMHPRNGFTEDSKPGIWREISVCGNVFSLRETRSAQQRGKMVEIETNQLQDGSLIDLCGATLL
WRTAEGLSHTP
;
;APVKYGELIVLGYNGSLPNGDRGRRKSRFALFKRPKANGVKPSTVHIACTPQAAKAISNKDQHSISYTLSRAQTVVVEYT
HDSNTDMFQIGRSTESPIDFVVTDTVPGSQSNSDTQSVQSTISRFACRIICERNPPFTARIYAAGFDSSKNIFLGEKAAK
WKTSDGQMDGLTTNGVLVMHPRNGFTEDSKPGIWREISVCGNVFSLRETRSAQQRGKMVEIETNQLQDGSLIDLCGATLL
WRTAEGLSHTP
;
B,A ? 
2 'polypeptide(L)' no yes 'AYEDSE(TPO)QPFD' AYEDSETQPFD C,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'SULFATE ION' SO4 
4 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   PRO n 
1 3   VAL n 
1 4   LYS n 
1 5   TYR n 
1 6   GLY n 
1 7   GLU n 
1 8   LEU n 
1 9   ILE n 
1 10  VAL n 
1 11  LEU n 
1 12  GLY n 
1 13  TYR n 
1 14  ASN n 
1 15  GLY n 
1 16  SER n 
1 17  LEU n 
1 18  PRO n 
1 19  ASN n 
1 20  GLY n 
1 21  ASP n 
1 22  ARG n 
1 23  GLY n 
1 24  ARG n 
1 25  ARG n 
1 26  LYS n 
1 27  SER n 
1 28  ARG n 
1 29  PHE n 
1 30  ALA n 
1 31  LEU n 
1 32  PHE n 
1 33  LYS n 
1 34  ARG n 
1 35  PRO n 
1 36  LYS n 
1 37  ALA n 
1 38  ASN n 
1 39  GLY n 
1 40  VAL n 
1 41  LYS n 
1 42  PRO n 
1 43  SER n 
1 44  THR n 
1 45  VAL n 
1 46  HIS n 
1 47  ILE n 
1 48  ALA n 
1 49  CYS n 
1 50  THR n 
1 51  PRO n 
1 52  GLN n 
1 53  ALA n 
1 54  ALA n 
1 55  LYS n 
1 56  ALA n 
1 57  ILE n 
1 58  SER n 
1 59  ASN n 
1 60  LYS n 
1 61  ASP n 
1 62  GLN n 
1 63  HIS n 
1 64  SER n 
1 65  ILE n 
1 66  SER n 
1 67  TYR n 
1 68  THR n 
1 69  LEU n 
1 70  SER n 
1 71  ARG n 
1 72  ALA n 
1 73  GLN n 
1 74  THR n 
1 75  VAL n 
1 76  VAL n 
1 77  VAL n 
1 78  GLU n 
1 79  TYR n 
1 80  THR n 
1 81  HIS n 
1 82  ASP n 
1 83  SER n 
1 84  ASN n 
1 85  THR n 
1 86  ASP n 
1 87  MET n 
1 88  PHE n 
1 89  GLN n 
1 90  ILE n 
1 91  GLY n 
1 92  ARG n 
1 93  SER n 
1 94  THR n 
1 95  GLU n 
1 96  SER n 
1 97  PRO n 
1 98  ILE n 
1 99  ASP n 
1 100 PHE n 
1 101 VAL n 
1 102 VAL n 
1 103 THR n 
1 104 ASP n 
1 105 THR n 
1 106 VAL n 
1 107 PRO n 
1 108 GLY n 
1 109 SER n 
1 110 GLN n 
1 111 SER n 
1 112 ASN n 
1 113 SER n 
1 114 ASP n 
1 115 THR n 
1 116 GLN n 
1 117 SER n 
1 118 VAL n 
1 119 GLN n 
1 120 SER n 
1 121 THR n 
1 122 ILE n 
1 123 SER n 
1 124 ARG n 
1 125 PHE n 
1 126 ALA n 
1 127 CYS n 
1 128 ARG n 
1 129 ILE n 
1 130 ILE n 
1 131 CYS n 
1 132 GLU n 
1 133 ARG n 
1 134 ASN n 
1 135 PRO n 
1 136 PRO n 
1 137 PHE n 
1 138 THR n 
1 139 ALA n 
1 140 ARG n 
1 141 ILE n 
1 142 TYR n 
1 143 ALA n 
1 144 ALA n 
1 145 GLY n 
1 146 PHE n 
1 147 ASP n 
1 148 SER n 
1 149 SER n 
1 150 LYS n 
1 151 ASN n 
1 152 ILE n 
1 153 PHE n 
1 154 LEU n 
1 155 GLY n 
1 156 GLU n 
1 157 LYS n 
1 158 ALA n 
1 159 ALA n 
1 160 LYS n 
1 161 TRP n 
1 162 LYS n 
1 163 THR n 
1 164 SER n 
1 165 ASP n 
1 166 GLY n 
1 167 GLN n 
1 168 MET n 
1 169 ASP n 
1 170 GLY n 
1 171 LEU n 
1 172 THR n 
1 173 THR n 
1 174 ASN n 
1 175 GLY n 
1 176 VAL n 
1 177 LEU n 
1 178 VAL n 
1 179 MET n 
1 180 HIS n 
1 181 PRO n 
1 182 ARG n 
1 183 ASN n 
1 184 GLY n 
1 185 PHE n 
1 186 THR n 
1 187 GLU n 
1 188 ASP n 
1 189 SER n 
1 190 LYS n 
1 191 PRO n 
1 192 GLY n 
1 193 ILE n 
1 194 TRP n 
1 195 ARG n 
1 196 GLU n 
1 197 ILE n 
1 198 SER n 
1 199 VAL n 
1 200 CYS n 
1 201 GLY n 
1 202 ASN n 
1 203 VAL n 
1 204 PHE n 
1 205 SER n 
1 206 LEU n 
1 207 ARG n 
1 208 GLU n 
1 209 THR n 
1 210 ARG n 
1 211 SER n 
1 212 ALA n 
1 213 GLN n 
1 214 GLN n 
1 215 ARG n 
1 216 GLY n 
1 217 LYS n 
1 218 MET n 
1 219 VAL n 
1 220 GLU n 
1 221 ILE n 
1 222 GLU n 
1 223 THR n 
1 224 ASN n 
1 225 GLN n 
1 226 LEU n 
1 227 GLN n 
1 228 ASP n 
1 229 GLY n 
1 230 SER n 
1 231 LEU n 
1 232 ILE n 
1 233 ASP n 
1 234 LEU n 
1 235 CYS n 
1 236 GLY n 
1 237 ALA n 
1 238 THR n 
1 239 LEU n 
1 240 LEU n 
1 241 TRP n 
1 242 ARG n 
1 243 THR n 
1 244 ALA n 
1 245 GLU n 
1 246 GLY n 
1 247 LEU n 
1 248 SER n 
1 249 HIS n 
1 250 THR n 
1 251 PRO n 
2 1   ALA n 
2 2   TYR n 
2 3   GLU n 
2 4   ASP n 
2 5   SER n 
2 6   GLU n 
2 7   TPO n 
2 8   GLN n 
2 9   PRO n 
2 10  PHE n 
2 11  ASP n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   251 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PELI1, PRISM' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   'N-terminal GST tag, N-terminal precission protease cleavage, ColE1' 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pGEX-6P-1 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_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       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       11 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_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 
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 
SO4 non-polymer         . 'SULFATE ION'    ?                  'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE        ?                  'C4 H9 N O3'     119.119 
TPO 'L-peptide linking' n PHOSPHOTHREONINE PHOSPHONOTHREONINE 'C4 H10 N O6 P'  199.099 
TRP 'L-peptide linking' y TRYPTOPHAN       ?                  'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE         ?                  'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE           ?                  'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   13  13  ALA ALA B . n 
A 1 2   PRO 2   14  14  PRO PRO B . n 
A 1 3   VAL 3   15  15  VAL VAL B . n 
A 1 4   LYS 4   16  16  LYS LYS B . n 
A 1 5   TYR 5   17  17  TYR TYR B . n 
A 1 6   GLY 6   18  18  GLY GLY B . n 
A 1 7   GLU 7   19  19  GLU GLU B . n 
A 1 8   LEU 8   20  20  LEU LEU B . n 
A 1 9   ILE 9   21  21  ILE ILE B . n 
A 1 10  VAL 10  22  22  VAL VAL B . n 
A 1 11  LEU 11  23  23  LEU LEU B . n 
A 1 12  GLY 12  24  24  GLY GLY B . n 
A 1 13  TYR 13  25  25  TYR TYR B . n 
A 1 14  ASN 14  26  26  ASN ASN B . n 
A 1 15  GLY 15  27  27  GLY GLY B . n 
A 1 16  SER 16  28  28  SER SER B . n 
A 1 17  LEU 17  29  29  LEU LEU B . n 
A 1 18  PRO 18  30  30  PRO PRO B . n 
A 1 19  ASN 19  31  ?   ?   ?   B . n 
A 1 20  GLY 20  32  ?   ?   ?   B . n 
A 1 21  ASP 21  33  ?   ?   ?   B . n 
A 1 22  ARG 22  34  ?   ?   ?   B . n 
A 1 23  GLY 23  35  35  GLY GLY B . n 
A 1 24  ARG 24  36  36  ARG ARG B . n 
A 1 25  ARG 25  37  37  ARG ARG B . n 
A 1 26  LYS 26  38  38  LYS LYS B . n 
A 1 27  SER 27  39  39  SER SER B . n 
A 1 28  ARG 28  40  40  ARG ARG B . n 
A 1 29  PHE 29  41  41  PHE PHE B . n 
A 1 30  ALA 30  42  42  ALA ALA B . n 
A 1 31  LEU 31  43  43  LEU LEU B . n 
A 1 32  PHE 32  44  44  PHE PHE B . n 
A 1 33  LYS 33  45  45  LYS LYS B . n 
A 1 34  ARG 34  46  46  ARG ARG B . n 
A 1 35  PRO 35  47  47  PRO PRO B . n 
A 1 36  LYS 36  48  48  LYS LYS B . n 
A 1 37  ALA 37  49  49  ALA ALA B . n 
A 1 38  ASN 38  50  50  ASN ASN B . n 
A 1 39  GLY 39  51  51  GLY GLY B . n 
A 1 40  VAL 40  52  52  VAL VAL B . n 
A 1 41  LYS 41  53  53  LYS LYS B . n 
A 1 42  PRO 42  54  54  PRO PRO B . n 
A 1 43  SER 43  55  55  SER SER B . n 
A 1 44  THR 44  56  56  THR THR B . n 
A 1 45  VAL 45  57  57  VAL VAL B . n 
A 1 46  HIS 46  58  58  HIS HIS B . n 
A 1 47  ILE 47  59  59  ILE ILE B . n 
A 1 48  ALA 48  60  60  ALA ALA B . n 
A 1 49  CYS 49  61  61  CYS CYS B . n 
A 1 50  THR 50  62  62  THR THR B . n 
A 1 51  PRO 51  63  63  PRO PRO B . n 
A 1 52  GLN 52  64  64  GLN GLN B . n 
A 1 53  ALA 53  65  65  ALA ALA B . n 
A 1 54  ALA 54  66  66  ALA ALA B . n 
A 1 55  LYS 55  67  67  LYS LYS B . n 
A 1 56  ALA 56  68  68  ALA ALA B . n 
A 1 57  ILE 57  69  69  ILE ILE B . n 
A 1 58  SER 58  70  70  SER SER B . n 
A 1 59  ASN 59  71  71  ASN ASN B . n 
A 1 60  LYS 60  72  72  LYS LYS B . n 
A 1 61  ASP 61  73  73  ASP ASP B . n 
A 1 62  GLN 62  74  74  GLN GLN B . n 
A 1 63  HIS 63  75  75  HIS HIS B . n 
A 1 64  SER 64  76  76  SER SER B . n 
A 1 65  ILE 65  77  77  ILE ILE B . n 
A 1 66  SER 66  78  78  SER SER B . n 
A 1 67  TYR 67  79  79  TYR TYR B . n 
A 1 68  THR 68  80  80  THR THR B . n 
A 1 69  LEU 69  81  81  LEU LEU B . n 
A 1 70  SER 70  82  82  SER SER B . n 
A 1 71  ARG 71  83  83  ARG ARG B . n 
A 1 72  ALA 72  84  84  ALA ALA B . n 
A 1 73  GLN 73  85  85  GLN GLN B . n 
A 1 74  THR 74  86  86  THR THR B . n 
A 1 75  VAL 75  87  87  VAL VAL B . n 
A 1 76  VAL 76  88  88  VAL VAL B . n 
A 1 77  VAL 77  89  89  VAL VAL B . n 
A 1 78  GLU 78  90  90  GLU GLU B . n 
A 1 79  TYR 79  91  91  TYR TYR B . n 
A 1 80  THR 80  92  92  THR THR B . n 
A 1 81  HIS 81  93  93  HIS HIS B . n 
A 1 82  ASP 82  94  94  ASP ASP B . n 
A 1 83  SER 83  95  95  SER SER B . n 
A 1 84  ASN 84  96  96  ASN ASN B . n 
A 1 85  THR 85  97  97  THR THR B . n 
A 1 86  ASP 86  98  98  ASP ASP B . n 
A 1 87  MET 87  99  99  MET MET B . n 
A 1 88  PHE 88  100 100 PHE PHE B . n 
A 1 89  GLN 89  101 101 GLN GLN B . n 
A 1 90  ILE 90  102 102 ILE ILE B . n 
A 1 91  GLY 91  103 103 GLY GLY B . n 
A 1 92  ARG 92  104 104 ARG ARG B . n 
A 1 93  SER 93  105 105 SER SER B . n 
A 1 94  THR 94  106 106 THR THR B . n 
A 1 95  GLU 95  107 107 GLU GLU B . n 
A 1 96  SER 96  108 108 SER SER B . n 
A 1 97  PRO 97  109 109 PRO PRO B . n 
A 1 98  ILE 98  110 110 ILE ILE B . n 
A 1 99  ASP 99  111 111 ASP ASP B . n 
A 1 100 PHE 100 112 112 PHE PHE B . n 
A 1 101 VAL 101 113 113 VAL VAL B . n 
A 1 102 VAL 102 114 114 VAL VAL B . n 
A 1 103 THR 103 115 115 THR THR B . n 
A 1 104 ASP 104 116 116 ASP ASP B . n 
A 1 105 THR 105 117 117 THR THR B . n 
A 1 106 VAL 106 118 118 VAL VAL B . n 
A 1 107 PRO 107 119 119 PRO PRO B . n 
A 1 108 GLY 108 120 ?   ?   ?   B . n 
A 1 109 SER 109 121 ?   ?   ?   B . n 
A 1 110 GLN 110 122 ?   ?   ?   B . n 
A 1 111 SER 111 123 ?   ?   ?   B . n 
A 1 112 ASN 112 124 ?   ?   ?   B . n 
A 1 113 SER 113 125 ?   ?   ?   B . n 
A 1 114 ASP 114 126 ?   ?   ?   B . n 
A 1 115 THR 115 127 ?   ?   ?   B . n 
A 1 116 GLN 116 128 ?   ?   ?   B . n 
A 1 117 SER 117 129 ?   ?   ?   B . n 
A 1 118 VAL 118 130 130 VAL VAL B . n 
A 1 119 GLN 119 131 131 GLN GLN B . n 
A 1 120 SER 120 132 132 SER SER B . n 
A 1 121 THR 121 133 133 THR THR B . n 
A 1 122 ILE 122 134 134 ILE ILE B . n 
A 1 123 SER 123 135 135 SER SER B . n 
A 1 124 ARG 124 136 136 ARG ARG B . n 
A 1 125 PHE 125 137 137 PHE PHE B . n 
A 1 126 ALA 126 138 138 ALA ALA B . n 
A 1 127 CYS 127 139 139 CYS CYS B . n 
A 1 128 ARG 128 140 140 ARG ARG B . n 
A 1 129 ILE 129 141 141 ILE ILE B . n 
A 1 130 ILE 130 142 142 ILE ILE B . n 
A 1 131 CYS 131 143 143 CYS CYS B . n 
A 1 132 GLU 132 144 144 GLU GLU B . n 
A 1 133 ARG 133 145 145 ARG ARG B . n 
A 1 134 ASN 134 146 146 ASN ASN B . n 
A 1 135 PRO 135 147 147 PRO PRO B . n 
A 1 136 PRO 136 148 148 PRO PRO B . n 
A 1 137 PHE 137 149 149 PHE PHE B . n 
A 1 138 THR 138 150 150 THR THR B . n 
A 1 139 ALA 139 151 151 ALA ALA B . n 
A 1 140 ARG 140 152 152 ARG ARG B . n 
A 1 141 ILE 141 153 153 ILE ILE B . n 
A 1 142 TYR 142 154 154 TYR TYR B . n 
A 1 143 ALA 143 155 155 ALA ALA B . n 
A 1 144 ALA 144 156 156 ALA ALA B . n 
A 1 145 GLY 145 157 157 GLY GLY B . n 
A 1 146 PHE 146 158 158 PHE PHE B . n 
A 1 147 ASP 147 159 159 ASP ASP B . n 
A 1 148 SER 148 160 160 SER SER B . n 
A 1 149 SER 149 161 161 SER SER B . n 
A 1 150 LYS 150 162 162 LYS LYS B . n 
A 1 151 ASN 151 163 163 ASN ASN B . n 
A 1 152 ILE 152 164 164 ILE ILE B . n 
A 1 153 PHE 153 165 165 PHE PHE B . n 
A 1 154 LEU 154 166 166 LEU LEU B . n 
A 1 155 GLY 155 167 167 GLY GLY B . n 
A 1 156 GLU 156 168 168 GLU GLU B . n 
A 1 157 LYS 157 169 169 LYS LYS B . n 
A 1 158 ALA 158 170 170 ALA ALA B . n 
A 1 159 ALA 159 171 171 ALA ALA B . n 
A 1 160 LYS 160 172 172 LYS LYS B . n 
A 1 161 TRP 161 173 173 TRP TRP B . n 
A 1 162 LYS 162 174 174 LYS LYS B . n 
A 1 163 THR 163 175 175 THR THR B . n 
A 1 164 SER 164 176 176 SER SER B . n 
A 1 165 ASP 165 177 177 ASP ASP B . n 
A 1 166 GLY 166 178 178 GLY GLY B . n 
A 1 167 GLN 167 179 179 GLN GLN B . n 
A 1 168 MET 168 180 180 MET MET B . n 
A 1 169 ASP 169 181 181 ASP ASP B . n 
A 1 170 GLY 170 182 182 GLY GLY B . n 
A 1 171 LEU 171 183 183 LEU LEU B . n 
A 1 172 THR 172 184 184 THR THR B . n 
A 1 173 THR 173 185 185 THR THR B . n 
A 1 174 ASN 174 186 186 ASN ASN B . n 
A 1 175 GLY 175 187 187 GLY GLY B . n 
A 1 176 VAL 176 188 188 VAL VAL B . n 
A 1 177 LEU 177 189 189 LEU LEU B . n 
A 1 178 VAL 178 190 190 VAL VAL B . n 
A 1 179 MET 179 191 191 MET MET B . n 
A 1 180 HIS 180 192 192 HIS HIS B . n 
A 1 181 PRO 181 193 193 PRO PRO B . n 
A 1 182 ARG 182 194 194 ARG ARG B . n 
A 1 183 ASN 183 195 195 ASN ASN B . n 
A 1 184 GLY 184 196 196 GLY GLY B . n 
A 1 185 PHE 185 197 197 PHE PHE B . n 
A 1 186 THR 186 198 198 THR THR B . n 
A 1 187 GLU 187 199 199 GLU GLU B . n 
A 1 188 ASP 188 200 200 ASP ASP B . n 
A 1 189 SER 189 201 201 SER SER B . n 
A 1 190 LYS 190 202 202 LYS LYS B . n 
A 1 191 PRO 191 203 203 PRO PRO B . n 
A 1 192 GLY 192 204 204 GLY GLY B . n 
A 1 193 ILE 193 205 205 ILE ILE B . n 
A 1 194 TRP 194 206 206 TRP TRP B . n 
A 1 195 ARG 195 207 207 ARG ARG B . n 
A 1 196 GLU 196 208 208 GLU GLU B . n 
A 1 197 ILE 197 209 209 ILE ILE B . n 
A 1 198 SER 198 210 210 SER SER B . n 
A 1 199 VAL 199 211 211 VAL VAL B . n 
A 1 200 CYS 200 212 212 CYS CYS B . n 
A 1 201 GLY 201 213 213 GLY GLY B . n 
A 1 202 ASN 202 214 214 ASN ASN B . n 
A 1 203 VAL 203 215 215 VAL VAL B . n 
A 1 204 PHE 204 216 216 PHE PHE B . n 
A 1 205 SER 205 217 217 SER SER B . n 
A 1 206 LEU 206 218 218 LEU LEU B . n 
A 1 207 ARG 207 219 219 ARG ARG B . n 
A 1 208 GLU 208 220 220 GLU GLU B . n 
A 1 209 THR 209 221 221 THR THR B . n 
A 1 210 ARG 210 222 222 ARG ARG B . n 
A 1 211 SER 211 223 223 SER SER B . n 
A 1 212 ALA 212 224 224 ALA ALA B . n 
A 1 213 GLN 213 225 225 GLN GLN B . n 
A 1 214 GLN 214 226 226 GLN GLN B . n 
A 1 215 ARG 215 227 227 ARG ARG B . n 
A 1 216 GLY 216 228 228 GLY GLY B . n 
A 1 217 LYS 217 229 229 LYS LYS B . n 
A 1 218 MET 218 230 230 MET MET B . n 
A 1 219 VAL 219 231 231 VAL VAL B . n 
A 1 220 GLU 220 232 232 GLU GLU B . n 
A 1 221 ILE 221 233 233 ILE ILE B . n 
A 1 222 GLU 222 234 234 GLU GLU B . n 
A 1 223 THR 223 235 235 THR THR B . n 
A 1 224 ASN 224 236 236 ASN ASN B . n 
A 1 225 GLN 225 237 237 GLN GLN B . n 
A 1 226 LEU 226 238 238 LEU LEU B . n 
A 1 227 GLN 227 239 239 GLN GLN B . n 
A 1 228 ASP 228 240 240 ASP ASP B . n 
A 1 229 GLY 229 241 241 GLY GLY B . n 
A 1 230 SER 230 242 242 SER SER B . n 
A 1 231 LEU 231 243 243 LEU LEU B . n 
A 1 232 ILE 232 244 244 ILE ILE B . n 
A 1 233 ASP 233 245 245 ASP ASP B . n 
A 1 234 LEU 234 246 246 LEU LEU B . n 
A 1 235 CYS 235 247 247 CYS CYS B . n 
A 1 236 GLY 236 248 248 GLY GLY B . n 
A 1 237 ALA 237 249 249 ALA ALA B . n 
A 1 238 THR 238 250 250 THR THR B . n 
A 1 239 LEU 239 251 251 LEU LEU B . n 
A 1 240 LEU 240 252 252 LEU LEU B . n 
A 1 241 TRP 241 253 253 TRP TRP B . n 
A 1 242 ARG 242 254 254 ARG ARG B . n 
A 1 243 THR 243 255 255 THR THR B . n 
A 1 244 ALA 244 256 256 ALA ALA B . n 
A 1 245 GLU 245 257 257 GLU GLU B . n 
A 1 246 GLY 246 258 258 GLY GLY B . n 
A 1 247 LEU 247 259 259 LEU LEU B . n 
A 1 248 SER 248 260 260 SER SER B . n 
A 1 249 HIS 249 261 261 HIS HIS B . n 
A 1 250 THR 250 262 262 THR THR B . n 
A 1 251 PRO 251 263 263 PRO PRO B . n 
B 1 1   ALA 1   13  13  ALA ALA A . n 
B 1 2   PRO 2   14  14  PRO PRO A . n 
B 1 3   VAL 3   15  15  VAL VAL A . n 
B 1 4   LYS 4   16  16  LYS LYS A . n 
B 1 5   TYR 5   17  17  TYR TYR A . n 
B 1 6   GLY 6   18  18  GLY GLY A . n 
B 1 7   GLU 7   19  19  GLU GLU A . n 
B 1 8   LEU 8   20  20  LEU LEU A . n 
B 1 9   ILE 9   21  21  ILE ILE A . n 
B 1 10  VAL 10  22  22  VAL VAL A . n 
B 1 11  LEU 11  23  23  LEU LEU A . n 
B 1 12  GLY 12  24  24  GLY GLY A . n 
B 1 13  TYR 13  25  25  TYR TYR A . n 
B 1 14  ASN 14  26  26  ASN ASN A . n 
B 1 15  GLY 15  27  27  GLY GLY A . n 
B 1 16  SER 16  28  28  SER SER A . n 
B 1 17  LEU 17  29  29  LEU LEU A . n 
B 1 18  PRO 18  30  30  PRO PRO A . n 
B 1 19  ASN 19  31  31  ASN ASN A . n 
B 1 20  GLY 20  32  32  GLY GLY A . n 
B 1 21  ASP 21  33  ?   ?   ?   A . n 
B 1 22  ARG 22  34  ?   ?   ?   A . n 
B 1 23  GLY 23  35  ?   ?   ?   A . n 
B 1 24  ARG 24  36  ?   ?   ?   A . n 
B 1 25  ARG 25  37  ?   ?   ?   A . n 
B 1 26  LYS 26  38  38  LYS LYS A . n 
B 1 27  SER 27  39  39  SER SER A . n 
B 1 28  ARG 28  40  40  ARG ARG A . n 
B 1 29  PHE 29  41  41  PHE PHE A . n 
B 1 30  ALA 30  42  42  ALA ALA A . n 
B 1 31  LEU 31  43  43  LEU LEU A . n 
B 1 32  PHE 32  44  44  PHE PHE A . n 
B 1 33  LYS 33  45  45  LYS LYS A . n 
B 1 34  ARG 34  46  46  ARG ARG A . n 
B 1 35  PRO 35  47  47  PRO PRO A . n 
B 1 36  LYS 36  48  48  LYS LYS A . n 
B 1 37  ALA 37  49  49  ALA ALA A . n 
B 1 38  ASN 38  50  50  ASN ASN A . n 
B 1 39  GLY 39  51  51  GLY GLY A . n 
B 1 40  VAL 40  52  52  VAL VAL A . n 
B 1 41  LYS 41  53  53  LYS LYS A . n 
B 1 42  PRO 42  54  54  PRO PRO A . n 
B 1 43  SER 43  55  55  SER SER A . n 
B 1 44  THR 44  56  56  THR THR A . n 
B 1 45  VAL 45  57  57  VAL VAL A . n 
B 1 46  HIS 46  58  58  HIS HIS A . n 
B 1 47  ILE 47  59  59  ILE ILE A . n 
B 1 48  ALA 48  60  60  ALA ALA A . n 
B 1 49  CYS 49  61  61  CYS CYS A . n 
B 1 50  THR 50  62  62  THR THR A . n 
B 1 51  PRO 51  63  63  PRO PRO A . n 
B 1 52  GLN 52  64  64  GLN GLN A . n 
B 1 53  ALA 53  65  65  ALA ALA A . n 
B 1 54  ALA 54  66  66  ALA ALA A . n 
B 1 55  LYS 55  67  67  LYS LYS A . n 
B 1 56  ALA 56  68  68  ALA ALA A . n 
B 1 57  ILE 57  69  69  ILE ILE A . n 
B 1 58  SER 58  70  70  SER SER A . n 
B 1 59  ASN 59  71  71  ASN ASN A . n 
B 1 60  LYS 60  72  72  LYS LYS A . n 
B 1 61  ASP 61  73  73  ASP ASP A . n 
B 1 62  GLN 62  74  74  GLN GLN A . n 
B 1 63  HIS 63  75  75  HIS HIS A . n 
B 1 64  SER 64  76  76  SER SER A . n 
B 1 65  ILE 65  77  77  ILE ILE A . n 
B 1 66  SER 66  78  78  SER SER A . n 
B 1 67  TYR 67  79  79  TYR TYR A . n 
B 1 68  THR 68  80  80  THR THR A . n 
B 1 69  LEU 69  81  81  LEU LEU A . n 
B 1 70  SER 70  82  82  SER SER A . n 
B 1 71  ARG 71  83  83  ARG ARG A . n 
B 1 72  ALA 72  84  84  ALA ALA A . n 
B 1 73  GLN 73  85  85  GLN GLN A . n 
B 1 74  THR 74  86  86  THR THR A . n 
B 1 75  VAL 75  87  87  VAL VAL A . n 
B 1 76  VAL 76  88  88  VAL VAL A . n 
B 1 77  VAL 77  89  89  VAL VAL A . n 
B 1 78  GLU 78  90  90  GLU GLU A . n 
B 1 79  TYR 79  91  91  TYR TYR A . n 
B 1 80  THR 80  92  92  THR THR A . n 
B 1 81  HIS 81  93  93  HIS HIS A . n 
B 1 82  ASP 82  94  94  ASP ASP A . n 
B 1 83  SER 83  95  95  SER SER A . n 
B 1 84  ASN 84  96  96  ASN ASN A . n 
B 1 85  THR 85  97  97  THR THR A . n 
B 1 86  ASP 86  98  98  ASP ASP A . n 
B 1 87  MET 87  99  99  MET MET A . n 
B 1 88  PHE 88  100 100 PHE PHE A . n 
B 1 89  GLN 89  101 101 GLN GLN A . n 
B 1 90  ILE 90  102 102 ILE ILE A . n 
B 1 91  GLY 91  103 103 GLY GLY A . n 
B 1 92  ARG 92  104 104 ARG ARG A . n 
B 1 93  SER 93  105 105 SER SER A . n 
B 1 94  THR 94  106 106 THR THR A . n 
B 1 95  GLU 95  107 107 GLU GLU A . n 
B 1 96  SER 96  108 108 SER SER A . n 
B 1 97  PRO 97  109 109 PRO PRO A . n 
B 1 98  ILE 98  110 110 ILE ILE A . n 
B 1 99  ASP 99  111 111 ASP ASP A . n 
B 1 100 PHE 100 112 112 PHE PHE A . n 
B 1 101 VAL 101 113 113 VAL VAL A . n 
B 1 102 VAL 102 114 114 VAL VAL A . n 
B 1 103 THR 103 115 115 THR THR A . n 
B 1 104 ASP 104 116 116 ASP ASP A . n 
B 1 105 THR 105 117 117 THR THR A . n 
B 1 106 VAL 106 118 ?   ?   ?   A . n 
B 1 107 PRO 107 119 ?   ?   ?   A . n 
B 1 108 GLY 108 120 ?   ?   ?   A . n 
B 1 109 SER 109 121 ?   ?   ?   A . n 
B 1 110 GLN 110 122 ?   ?   ?   A . n 
B 1 111 SER 111 123 ?   ?   ?   A . n 
B 1 112 ASN 112 124 ?   ?   ?   A . n 
B 1 113 SER 113 125 ?   ?   ?   A . n 
B 1 114 ASP 114 126 ?   ?   ?   A . n 
B 1 115 THR 115 127 ?   ?   ?   A . n 
B 1 116 GLN 116 128 ?   ?   ?   A . n 
B 1 117 SER 117 129 ?   ?   ?   A . n 
B 1 118 VAL 118 130 130 VAL VAL A . n 
B 1 119 GLN 119 131 131 GLN GLN A . n 
B 1 120 SER 120 132 132 SER SER A . n 
B 1 121 THR 121 133 133 THR THR A . n 
B 1 122 ILE 122 134 134 ILE ILE A . n 
B 1 123 SER 123 135 135 SER SER A . n 
B 1 124 ARG 124 136 136 ARG ARG A . n 
B 1 125 PHE 125 137 137 PHE PHE A . n 
B 1 126 ALA 126 138 138 ALA ALA A . n 
B 1 127 CYS 127 139 139 CYS CYS A . n 
B 1 128 ARG 128 140 140 ARG ARG A . n 
B 1 129 ILE 129 141 141 ILE ILE A . n 
B 1 130 ILE 130 142 142 ILE ILE A . n 
B 1 131 CYS 131 143 143 CYS CYS A . n 
B 1 132 GLU 132 144 144 GLU GLU A . n 
B 1 133 ARG 133 145 145 ARG ARG A . n 
B 1 134 ASN 134 146 146 ASN ASN A . n 
B 1 135 PRO 135 147 147 PRO PRO A . n 
B 1 136 PRO 136 148 148 PRO PRO A . n 
B 1 137 PHE 137 149 149 PHE PHE A . n 
B 1 138 THR 138 150 150 THR THR A . n 
B 1 139 ALA 139 151 151 ALA ALA A . n 
B 1 140 ARG 140 152 152 ARG ARG A . n 
B 1 141 ILE 141 153 153 ILE ILE A . n 
B 1 142 TYR 142 154 154 TYR TYR A . n 
B 1 143 ALA 143 155 155 ALA ALA A . n 
B 1 144 ALA 144 156 156 ALA ALA A . n 
B 1 145 GLY 145 157 157 GLY GLY A . n 
B 1 146 PHE 146 158 158 PHE PHE A . n 
B 1 147 ASP 147 159 159 ASP ASP A . n 
B 1 148 SER 148 160 160 SER SER A . n 
B 1 149 SER 149 161 161 SER SER A . n 
B 1 150 LYS 150 162 162 LYS LYS A . n 
B 1 151 ASN 151 163 163 ASN ASN A . n 
B 1 152 ILE 152 164 164 ILE ILE A . n 
B 1 153 PHE 153 165 165 PHE PHE A . n 
B 1 154 LEU 154 166 166 LEU LEU A . n 
B 1 155 GLY 155 167 167 GLY GLY A . n 
B 1 156 GLU 156 168 168 GLU GLU A . n 
B 1 157 LYS 157 169 169 LYS LYS A . n 
B 1 158 ALA 158 170 170 ALA ALA A . n 
B 1 159 ALA 159 171 171 ALA ALA A . n 
B 1 160 LYS 160 172 172 LYS LYS A . n 
B 1 161 TRP 161 173 173 TRP TRP A . n 
B 1 162 LYS 162 174 174 LYS LYS A . n 
B 1 163 THR 163 175 175 THR THR A . n 
B 1 164 SER 164 176 176 SER SER A . n 
B 1 165 ASP 165 177 177 ASP ASP A . n 
B 1 166 GLY 166 178 178 GLY GLY A . n 
B 1 167 GLN 167 179 179 GLN GLN A . n 
B 1 168 MET 168 180 180 MET MET A . n 
B 1 169 ASP 169 181 181 ASP ASP A . n 
B 1 170 GLY 170 182 182 GLY GLY A . n 
B 1 171 LEU 171 183 183 LEU LEU A . n 
B 1 172 THR 172 184 184 THR THR A . n 
B 1 173 THR 173 185 185 THR THR A . n 
B 1 174 ASN 174 186 186 ASN ASN A . n 
B 1 175 GLY 175 187 187 GLY GLY A . n 
B 1 176 VAL 176 188 188 VAL VAL A . n 
B 1 177 LEU 177 189 189 LEU LEU A . n 
B 1 178 VAL 178 190 190 VAL VAL A . n 
B 1 179 MET 179 191 191 MET MET A . n 
B 1 180 HIS 180 192 192 HIS HIS A . n 
B 1 181 PRO 181 193 193 PRO PRO A . n 
B 1 182 ARG 182 194 194 ARG ARG A . n 
B 1 183 ASN 183 195 195 ASN ASN A . n 
B 1 184 GLY 184 196 196 GLY GLY A . n 
B 1 185 PHE 185 197 ?   ?   ?   A . n 
B 1 186 THR 186 198 ?   ?   ?   A . n 
B 1 187 GLU 187 199 ?   ?   ?   A . n 
B 1 188 ASP 188 200 ?   ?   ?   A . n 
B 1 189 SER 189 201 ?   ?   ?   A . n 
B 1 190 LYS 190 202 ?   ?   ?   A . n 
B 1 191 PRO 191 203 203 PRO PRO A . n 
B 1 192 GLY 192 204 204 GLY GLY A . n 
B 1 193 ILE 193 205 205 ILE ILE A . n 
B 1 194 TRP 194 206 206 TRP TRP A . n 
B 1 195 ARG 195 207 207 ARG ARG A . n 
B 1 196 GLU 196 208 208 GLU GLU A . n 
B 1 197 ILE 197 209 209 ILE ILE A . n 
B 1 198 SER 198 210 210 SER SER A . n 
B 1 199 VAL 199 211 211 VAL VAL A . n 
B 1 200 CYS 200 212 212 CYS CYS A . n 
B 1 201 GLY 201 213 213 GLY GLY A . n 
B 1 202 ASN 202 214 214 ASN ASN A . n 
B 1 203 VAL 203 215 215 VAL VAL A . n 
B 1 204 PHE 204 216 216 PHE PHE A . n 
B 1 205 SER 205 217 217 SER SER A . n 
B 1 206 LEU 206 218 218 LEU LEU A . n 
B 1 207 ARG 207 219 219 ARG ARG A . n 
B 1 208 GLU 208 220 220 GLU GLU A . n 
B 1 209 THR 209 221 221 THR THR A . n 
B 1 210 ARG 210 222 222 ARG ARG A . n 
B 1 211 SER 211 223 223 SER SER A . n 
B 1 212 ALA 212 224 224 ALA ALA A . n 
B 1 213 GLN 213 225 225 GLN GLN A . n 
B 1 214 GLN 214 226 226 GLN GLN A . n 
B 1 215 ARG 215 227 227 ARG ARG A . n 
B 1 216 GLY 216 228 228 GLY GLY A . n 
B 1 217 LYS 217 229 229 LYS LYS A . n 
B 1 218 MET 218 230 230 MET MET A . n 
B 1 219 VAL 219 231 231 VAL VAL A . n 
B 1 220 GLU 220 232 232 GLU GLU A . n 
B 1 221 ILE 221 233 233 ILE ILE A . n 
B 1 222 GLU 222 234 234 GLU GLU A . n 
B 1 223 THR 223 235 235 THR THR A . n 
B 1 224 ASN 224 236 236 ASN ASN A . n 
B 1 225 GLN 225 237 237 GLN GLN A . n 
B 1 226 LEU 226 238 238 LEU LEU A . n 
B 1 227 GLN 227 239 239 GLN GLN A . n 
B 1 228 ASP 228 240 240 ASP ASP A . n 
B 1 229 GLY 229 241 241 GLY GLY A . n 
B 1 230 SER 230 242 242 SER SER A . n 
B 1 231 LEU 231 243 243 LEU LEU A . n 
B 1 232 ILE 232 244 244 ILE ILE A . n 
B 1 233 ASP 233 245 245 ASP ASP A . n 
B 1 234 LEU 234 246 246 LEU LEU A . n 
B 1 235 CYS 235 247 247 CYS CYS A . n 
B 1 236 GLY 236 248 248 GLY GLY A . n 
B 1 237 ALA 237 249 249 ALA ALA A . n 
B 1 238 THR 238 250 250 THR THR A . n 
B 1 239 LEU 239 251 251 LEU LEU A . n 
B 1 240 LEU 240 252 252 LEU LEU A . n 
B 1 241 TRP 241 253 253 TRP TRP A . n 
B 1 242 ARG 242 254 254 ARG ARG A . n 
B 1 243 THR 243 255 255 THR THR A . n 
B 1 244 ALA 244 256 ?   ?   ?   A . n 
B 1 245 GLU 245 257 ?   ?   ?   A . n 
B 1 246 GLY 246 258 ?   ?   ?   A . n 
B 1 247 LEU 247 259 ?   ?   ?   A . n 
B 1 248 SER 248 260 ?   ?   ?   A . n 
B 1 249 HIS 249 261 ?   ?   ?   A . n 
B 1 250 THR 250 262 ?   ?   ?   A . n 
B 1 251 PRO 251 263 ?   ?   ?   A . n 
C 2 1   ALA 1   1   1   ALA ALA C . n 
C 2 2   TYR 2   2   2   TYR TYR C . n 
C 2 3   GLU 3   3   3   GLU GLU C . n 
C 2 4   ASP 4   4   4   ASP ASP C . n 
C 2 5   SER 5   5   5   SER SER C . n 
C 2 6   GLU 6   6   6   GLU GLU C . n 
C 2 7   TPO 7   7   7   TPO TPO C . n 
C 2 8   GLN 8   8   8   GLN GLN C . n 
C 2 9   PRO 9   9   9   PRO PRO C . n 
C 2 10  PHE 10  10  10  PHE PHE C . n 
C 2 11  ASP 11  11  11  ASP ASP C . n 
D 2 1   ALA 1   1   1   ALA ALA D . n 
D 2 2   TYR 2   2   2   TYR TYR D . n 
D 2 3   GLU 3   3   3   GLU GLU D . n 
D 2 4   ASP 4   4   4   ASP ASP D . n 
D 2 5   SER 5   5   5   SER SER D . n 
D 2 6   GLU 6   6   6   GLU GLU D . n 
D 2 7   TPO 7   7   7   TPO TPO D . n 
D 2 8   GLN 8   8   8   GLN GLN D . n 
D 2 9   PRO 9   9   9   PRO PRO D . n 
D 2 10  PHE 10  10  10  PHE PHE D . n 
D 2 11  ASP 11  11  11  ASP ASP D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        TPO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   TPO 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 SO4 1  301 1  SO4 SO4 B . 
F 3 SO4 1  302 3  SO4 SO4 B . 
G 3 SO4 1  303 5  SO4 SO4 B . 
H 3 SO4 1  301 2  SO4 SO4 A . 
I 3 SO4 1  302 4  SO4 SO4 A . 
J 4 HOH 1  401 7  HOH HOH B . 
J 4 HOH 2  402 3  HOH HOH B . 
J 4 HOH 3  403 21 HOH HOH B . 
J 4 HOH 4  404 54 HOH HOH B . 
J 4 HOH 5  405 1  HOH HOH B . 
J 4 HOH 6  406 67 HOH HOH B . 
J 4 HOH 7  407 34 HOH HOH B . 
J 4 HOH 8  408 24 HOH HOH B . 
J 4 HOH 9  409 16 HOH HOH B . 
J 4 HOH 10 410 62 HOH HOH B . 
J 4 HOH 11 411 22 HOH HOH B . 
J 4 HOH 12 412 35 HOH HOH B . 
J 4 HOH 13 413 40 HOH HOH B . 
J 4 HOH 14 414 66 HOH HOH B . 
J 4 HOH 15 415 33 HOH HOH B . 
J 4 HOH 16 416 9  HOH HOH B . 
J 4 HOH 17 417 51 HOH HOH B . 
J 4 HOH 18 418 68 HOH HOH B . 
J 4 HOH 19 419 18 HOH HOH B . 
J 4 HOH 20 420 58 HOH HOH B . 
J 4 HOH 21 421 65 HOH HOH B . 
J 4 HOH 22 422 28 HOH HOH B . 
J 4 HOH 23 423 55 HOH HOH B . 
J 4 HOH 24 424 29 HOH HOH B . 
J 4 HOH 25 425 2  HOH HOH B . 
J 4 HOH 26 426 26 HOH HOH B . 
J 4 HOH 27 427 53 HOH HOH B . 
J 4 HOH 28 428 8  HOH HOH B . 
J 4 HOH 29 429 37 HOH HOH B . 
J 4 HOH 30 430 15 HOH HOH B . 
K 4 HOH 1  401 48 HOH HOH A . 
K 4 HOH 2  402 30 HOH HOH A . 
K 4 HOH 3  403 20 HOH HOH A . 
K 4 HOH 4  404 19 HOH HOH A . 
K 4 HOH 5  405 32 HOH HOH A . 
K 4 HOH 6  406 5  HOH HOH A . 
K 4 HOH 7  407 41 HOH HOH A . 
K 4 HOH 8  408 47 HOH HOH A . 
K 4 HOH 9  409 11 HOH HOH A . 
K 4 HOH 10 410 12 HOH HOH A . 
K 4 HOH 11 411 64 HOH HOH A . 
K 4 HOH 12 412 4  HOH HOH A . 
K 4 HOH 13 413 38 HOH HOH A . 
K 4 HOH 14 414 52 HOH HOH A . 
K 4 HOH 15 415 27 HOH HOH A . 
K 4 HOH 16 416 36 HOH HOH A . 
K 4 HOH 17 417 50 HOH HOH A . 
K 4 HOH 18 418 44 HOH HOH A . 
K 4 HOH 19 419 56 HOH HOH A . 
K 4 HOH 20 420 14 HOH HOH A . 
K 4 HOH 21 421 13 HOH HOH A . 
K 4 HOH 22 422 31 HOH HOH A . 
K 4 HOH 23 423 43 HOH HOH A . 
K 4 HOH 24 424 45 HOH HOH A . 
K 4 HOH 25 425 57 HOH HOH A . 
K 4 HOH 26 426 61 HOH HOH A . 
K 4 HOH 27 427 10 HOH HOH A . 
K 4 HOH 28 428 70 HOH HOH A . 
K 4 HOH 29 429 6  HOH HOH A . 
K 4 HOH 30 430 69 HOH HOH A . 
K 4 HOH 31 431 60 HOH HOH A . 
K 4 HOH 32 432 25 HOH HOH A . 
K 4 HOH 33 433 49 HOH HOH A . 
K 4 HOH 34 434 17 HOH HOH A . 
K 4 HOH 35 435 59 HOH HOH A . 
K 4 HOH 36 436 46 HOH HOH A . 
K 4 HOH 37 437 63 HOH HOH A . 
K 4 HOH 38 438 39 HOH HOH A . 
K 4 HOH 39 439 23 HOH HOH A . 
L 4 HOH 1  101 42 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    ? ? ? 1.21.2-5419    1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC  ? ? ? 1.0.5          2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless   ? ? ? 0.7.9          3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.21.2-5419    4 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? 'Jan 10, 2022' 5 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? 2.3.94         6 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IF9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.853 
_cell.length_a_esd                 ? 
_cell.length_b                     75.087 
_cell.length_b_esd                 ? 
_cell.length_c                     165.134 
_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                         9IF9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9IF9 
_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             2.97 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.56 
_exptl_crystal.description                  'Orthorhombic crystals, colorless and transparent, with well-formed morphology.' 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    NA 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Tris pH 8.0, 1.5M Ammonium sulphate, 20% (w/v) PEG400' 
_exptl_crystal_grow.pdbx_pH_range   8.0 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             NA 
_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                      NA 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-08-03 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Double crystal' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9795 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9IF9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.55 
_reflns.d_resolution_low                               68.35 
_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                                     15881 
_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                           91.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.224 
_reflns.pdbx_Rpim_I_all                                0.062 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.215 
_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 
8.08 68.35 ? 21.1 ? ? ? ? 794 ? ? ? ? ? ? ? ? ? ? ? 11.5 ? ? ? 0.063 0.019 ? 1 1 0.999 ? ? 99.9 ? 0.06  ? ? ? ? ? ? ? ? ? 
2.55 2.77  ? 1.3  ? ? ? ? 794 ? ? ? ? ? ? ? ? ? ? ? 8.3  ? ? ? 1.803 0.626 ? 2 1 0.464 ? ? 63.1 ? 1.682 ? ? ? ? ? ? ? ? ? 
# 
_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                                 9IF9 
_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                            2.55 
_refine.ls_d_res_low                             50.34 
_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                     15869 
_refine.ls_number_reflns_R_free                  15869 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    71.19 
_refine.ls_percent_reflns_R_free                 5 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2108 
_refine.ls_R_factor_R_free                       0.2108 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2108 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       LS_WUNIT_K1 
_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                 20.27 
_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                            0.20 
_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                       2.55 
_refine_hist.d_res_low                        50.34 
_refine_hist.number_atoms_solvent             70 
_refine_hist.number_atoms_total               3817 
_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        3722 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         25 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009 ? 3801 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.017 ? 5145 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 8.849 ? 517  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.056 ? 574  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011 ? 661  ? 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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 2.55 2.57  . . 12  12  2.00   . . . . 0.2610 . . . . . . . . . . . . . . . 0.2610 
'X-RAY DIFFRACTION' 2.58 2.60  . . 45  45  7.00   . . . . 0.3123 . . . . . . . . . . . . . . . 0.3123 
'X-RAY DIFFRACTION' 2.61 2.64  . . 82  82  11.00  . . . . 0.3310 . . . . . . . . . . . . . . . 0.3310 
'X-RAY DIFFRACTION' 2.64 2.67  . . 129 129 18.00  . . . . 0.3339 . . . . . . . . . . . . . . . 0.3339 
'X-RAY DIFFRACTION' 2.67 2.70  . . 168 168 23.00  . . . . 0.2855 . . . . . . . . . . . . . . . 0.2855 
'X-RAY DIFFRACTION' 2.70 2.74  . . 210 210 29.00  . . . . 0.3120 . . . . . . . . . . . . . . . 0.3120 
'X-RAY DIFFRACTION' 2.74 2.78  . . 246 246 33.00  . . . . 0.2859 . . . . . . . . . . . . . . . 0.2859 
'X-RAY DIFFRACTION' 2.78 2.82  . . 281 281 40.00  . . . . 0.3037 . . . . . . . . . . . . . . . 0.3037 
'X-RAY DIFFRACTION' 2.82 2.87  . . 323 323 44.00  . . . . 0.2739 . . . . . . . . . . . . . . . 0.2739 
'X-RAY DIFFRACTION' 2.87 2.91  . . 358 358 49.00  . . . . 0.2582 . . . . . . . . . . . . . . . 0.2582 
'X-RAY DIFFRACTION' 2.91 2.96  . . 393 393 54.00  . . . . 0.2505 . . . . . . . . . . . . . . . 0.2505 
'X-RAY DIFFRACTION' 2.96 3.02  . . 487 487 67.00  . . . . 0.2672 . . . . . . . . . . . . . . . 0.2672 
'X-RAY DIFFRACTION' 3.02 3.08  . . 574 574 78.00  . . . . 0.2623 . . . . . . . . . . . . . . . 0.2623 
'X-RAY DIFFRACTION' 3.08 3.14  . . 640 640 86.00  . . . . 0.2459 . . . . . . . . . . . . . . . 0.2459 
'X-RAY DIFFRACTION' 3.14 3.21  . . 655 655 91.00  . . . . 0.2501 . . . . . . . . . . . . . . . 0.2501 
'X-RAY DIFFRACTION' 3.21 3.28  . . 713 713 94.00  . . . . 0.2422 . . . . . . . . . . . . . . . 0.2422 
'X-RAY DIFFRACTION' 3.28 3.36  . . 699 699 98.00  . . . . 0.2330 . . . . . . . . . . . . . . . 0.2330 
'X-RAY DIFFRACTION' 3.36 3.45  . . 738 738 100.00 . . . . 0.2108 . . . . . . . . . . . . . . . 0.2108 
'X-RAY DIFFRACTION' 3.45 3.56  . . 754 754 100.00 . . . . 0.2121 . . . . . . . . . . . . . . . 0.2121 
'X-RAY DIFFRACTION' 3.56 3.67  . . 720 720 99.00  . . . . 0.2045 . . . . . . . . . . . . . . . 0.2045 
'X-RAY DIFFRACTION' 3.67 3.80  . . 755 755 99.00  . . . . 0.1932 . . . . . . . . . . . . . . . 0.1932 
'X-RAY DIFFRACTION' 3.80 3.95  . . 735 735 100.00 . . . . 0.1857 . . . . . . . . . . . . . . . 0.1857 
'X-RAY DIFFRACTION' 3.96 4.13  . . 743 743 100.00 . . . . 0.1670 . . . . . . . . . . . . . . . 0.1670 
'X-RAY DIFFRACTION' 4.13 4.35  . . 757 757 100.00 . . . . 0.1601 . . . . . . . . . . . . . . . 0.1601 
'X-RAY DIFFRACTION' 4.35 4.62  . . 737 737 100.00 . . . . 0.1574 . . . . . . . . . . . . . . . 0.1574 
'X-RAY DIFFRACTION' 4.63 4.98  . . 772 772 100.00 . . . . 0.1642 . . . . . . . . . . . . . . . 0.1642 
'X-RAY DIFFRACTION' 4.98 5.48  . . 756 756 100.00 . . . . 0.1951 . . . . . . . . . . . . . . . 0.1951 
'X-RAY DIFFRACTION' 5.48 6.27  . . 761 761 100.00 . . . . 0.2294 . . . . . . . . . . . . . . . 0.2294 
'X-RAY DIFFRACTION' 6.27 7.90  . . 789 789 100.00 . . . . 0.2198 . . . . . . . . . . . . . . . 0.2198 
'X-RAY DIFFRACTION' 7.92 50.34 . . 837 837 99.00  . . . . 0.2445 . . . . . . . . . . . . . . . 0.2445 
# 
_struct.entry_id                     9IF9 
_struct.title                        'Crystal structure of the Pellino 1 FHA domain in complex with a MDC1-TQxF phosphopeptide.' 
_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        9IF9 
_struct_keywords.text            
'FHA, phosphopeptide binding domain, RING, E3 ligase, DNA damage, DNA repair, PEPTIDE BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'PEPTIDE BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
# 
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 PELI1_HUMAN Q96FA3 ? 1 
;APVKYGELIVLGYNGSLPNGDRGRRKSRFALFKRPKANGVKPSTVHIACTPQAAKAISNKDQHSISYTLSRAQTVVVEYT
HDSNTDMFQIGRSTESPIDFVVTDTVPGSQSNSDTQSVQSTISRFACRIICERNPPFTARIYAAGFDSSKNIFLGEKAAK
WKTSDGQMDGLTTNGVLVMHPRNGFTEDSKPGIWREISVCGNVFSLRETRSAQQRGKMVEIETNQLQDGSLIDLCGATLL
WRTAEGLSHTP
;
13  
2 UNP MDC1_HUMAN  Q14676 ? 2 EDSETQPFD 761 
# 
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 9IF9 B 1 ? 251 ? Q96FA3 13  ? 263 ? 13 263 
2 1 9IF9 A 1 ? 251 ? Q96FA3 13  ? 263 ? 13 263 
3 2 9IF9 C 3 ? 11  ? Q14676 761 ? 769 ? 3  11  
4 2 9IF9 D 3 ? 11  ? Q14676 761 ? 769 ? 3  11  
# 
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 
3 9IF9 ALA C 1 ? UNP Q14676 ? ? 'expression tag' 1 1 
3 9IF9 TYR C 2 ? UNP Q14676 ? ? 'expression tag' 2 2 
4 9IF9 ALA D 1 ? UNP Q14676 ? ? 'expression tag' 1 3 
4 9IF9 TYR D 2 ? UNP Q14676 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? tetrameric 4 
2 author_defined_assembly ? tetrameric 4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4740  ? 
1 MORE         -78   ? 
1 'SSA (A^2)'  23590 ? 
2 'ABSA (A^2)' 5960  ? 
2 MORE         -79   ? 
2 'SSA (A^2)'  22360 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 B,C,H,I,K               
1 2 A,D,E,F,G,J,L           
2 1 A,B,C,D,E,F,G,H,I,J,K,L 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 immunoprecipitation                ? 
2 1 'isothermal titration calorimetry' ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z           1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 
1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000  
2 'crystal symmetry operation' 2_555 -x+1/2,-y,z+1/2 -1.0000000000 0.0000000000 0.0000000000 26.4265000000 0.0000000000 
-1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 82.5670000000 
# 
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 THR A 50 ? ASN A 59 ? THR B 62 ASN B 71 1 ? 10 
HELX_P HELX_P2 AA2 THR B 50 ? ASN B 59 ? THR A 62 ASN A 71 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? A CYS 49 SG ? ? ? 1_555 B CYS 49 SG ? ? B CYS 61 A CYS 61 2_554 ? ? ? ? ? ? ? 2.060 ? ? 
covale1 covale both ? C GLU 6  C  ? ? ? 1_555 C TPO 7  N  ? ? C GLU 6  C TPO 7  1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale2 covale both ? C TPO 7  C  ? ? ? 1_555 C GLN 8  N  ? ? C TPO 7  C GLN 8  1_555 ? ? ? ? ? ? ? 1.324 ? ? 
covale3 covale both ? D GLU 6  C  ? ? ? 1_555 D TPO 7  N  ? ? D GLU 6  D TPO 7  1_555 ? ? ? ? ? ? ? 1.322 ? ? 
covale4 covale both ? D TPO 7  C  ? ? ? 1_555 D GLN 8  N  ? ? D TPO 7  D GLN 8  1_555 ? ? ? ? ? ? ? 1.326 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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 TPO C 7  ? .   . .  . TPO C 7  ? 1_555 .   . .  . .     .  .  THR 1 TPO Phosphorylation 'Named protein modification' 
2 TPO D 7  ? .   . .  . TPO D 7  ? 1_555 .   . .  . .     .  .  THR 1 TPO Phosphorylation 'Named protein modification' 
3 CYS A 49 ? CYS B 49 ? CYS B 61 ? 1_555 CYS A 61 ? 2_554 SG SG .   . .   None            'Disulfide bridge'           
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 135 A . ? PRO 147 B PRO 136 A ? PRO 148 B 1 4.96 
2 PRO 135 B . ? PRO 147 A PRO 136 B ? PRO 148 A 1 2.87 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 2 ? 
AA5 ? 7 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 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 ? parallel      
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? 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 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 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 ARG A 28  ? PHE A 32  ? ARG B 40  PHE B 44  
AA1 2 LYS A 4   ? VAL A 10  ? LYS B 16  VAL B 22  
AA1 3 THR A 238 ? ARG A 242 ? THR B 250 ARG B 254 
AA1 4 LEU A 231 ? ASP A 233 ? LEU B 243 ASP B 245 
AA1 5 VAL A 176 ? MET A 179 ? VAL B 188 MET B 191 
AA1 6 ARG A 195 ? ILE A 197 ? ARG B 207 ILE B 209 
AA1 7 VAL A 203 ? PHE A 204 ? VAL B 215 PHE B 216 
AA2 1 GLY A 39  ? HIS A 46  ? GLY B 51  HIS B 58  
AA2 2 GLN A 73  ? ASP A 82  ? GLN B 85  ASP B 94  
AA2 3 HIS A 63  ? SER A 70  ? HIS B 75  SER B 82  
AA2 4 ASN A 151 ? LEU A 154 ? ASN B 163 LEU B 166 
AA3 1 PHE A 100 ? VAL A 101 ? PHE B 112 VAL B 113 
AA3 2 THR A 85  ? GLY A 91  ? THR B 97  GLY B 103 
AA3 3 CYS A 127 ? GLU A 132 ? CYS B 139 GLU B 144 
AA3 4 ALA A 139 ? ALA A 143 ? ALA B 151 ALA B 155 
AA4 1 LYS A 160 ? LYS A 162 ? LYS B 172 LYS B 174 
AA4 2 MET A 168 ? GLY A 170 ? MET B 180 GLY B 182 
AA5 1 ARG B 28  ? PHE B 32  ? ARG A 40  PHE A 44  
AA5 2 LYS B 4   ? LEU B 11  ? LYS A 16  LEU A 23  
AA5 3 THR B 238 ? ARG B 242 ? THR A 250 ARG A 254 
AA5 4 SER B 230 ? ASP B 233 ? SER A 242 ASP A 245 
AA5 5 VAL B 176 ? MET B 179 ? VAL A 188 MET A 191 
AA5 6 ARG B 195 ? ILE B 197 ? ARG A 207 ILE A 209 
AA5 7 VAL B 203 ? PHE B 204 ? VAL A 215 PHE A 216 
AA6 1 GLY B 39  ? HIS B 46  ? GLY A 51  HIS A 58  
AA6 2 THR B 74  ? ASP B 82  ? THR A 86  ASP A 94  
AA6 3 HIS B 63  ? THR B 68  ? HIS A 75  THR A 80  
AA6 4 ASN B 151 ? LEU B 154 ? ASN A 163 LEU A 166 
AA7 1 PHE B 100 ? VAL B 101 ? PHE A 112 VAL A 113 
AA7 2 THR B 85  ? GLY B 91  ? THR A 97  GLY A 103 
AA7 3 CYS B 127 ? GLU B 132 ? CYS A 139 GLU A 144 
AA7 4 ALA B 139 ? ALA B 143 ? ALA A 151 ALA A 155 
AA8 1 ALA B 159 ? LYS B 162 ? ALA A 171 LYS A 174 
AA8 2 MET B 168 ? LEU B 171 ? MET A 180 LEU A 183 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 31  ? O LEU B 43  N GLY A 6   ? N GLY B 18  
AA1 2 3 N GLU A 7   ? N GLU B 19  O ARG A 242 ? O ARG B 254 
AA1 3 4 O LEU A 239 ? O LEU B 251 N ILE A 232 ? N ILE B 244 
AA1 4 5 O ASP A 233 ? O ASP B 245 N LEU A 177 ? N LEU B 189 
AA1 5 6 N VAL A 178 ? N VAL B 190 O ARG A 195 ? O ARG B 207 
AA1 6 7 N GLU A 196 ? N GLU B 208 O PHE A 204 ? O PHE B 216 
AA2 1 2 N THR A 44  ? N THR B 56  O GLU A 78  ? O GLU B 90  
AA2 2 3 O VAL A 75  ? O VAL B 87  N TYR A 67  ? N TYR B 79  
AA2 3 4 N SER A 66  ? N SER B 78  O ILE A 152 ? O ILE B 164 
AA3 1 2 O PHE A 100 ? O PHE B 112 N GLY A 91  ? N GLY B 103 
AA3 2 3 N PHE A 88  ? N PHE B 100 O ILE A 129 ? O ILE B 141 
AA3 3 4 N ILE A 130 ? N ILE B 142 O ARG A 140 ? O ARG B 152 
AA4 1 2 N TRP A 161 ? N TRP B 173 O ASP A 169 ? O ASP B 181 
AA5 1 2 O PHE B 29  ? O PHE A 41  N LEU B 8   ? N LEU A 20  
AA5 2 3 N ILE B 9   ? N ILE A 21  O LEU B 240 ? O LEU A 252 
AA5 3 4 O LEU B 239 ? O LEU A 251 N ILE B 232 ? N ILE A 244 
AA5 4 5 O ASP B 233 ? O ASP A 245 N LEU B 177 ? N LEU A 189 
AA5 5 6 N VAL B 176 ? N VAL A 188 O ILE B 197 ? O ILE A 209 
AA5 6 7 N GLU B 196 ? N GLU A 208 O PHE B 204 ? O PHE A 216 
AA6 1 2 N GLY B 39  ? N GLY A 51  O ASP B 82  ? O ASP A 94  
AA6 2 3 O VAL B 77  ? O VAL A 89  N ILE B 65  ? N ILE A 77  
AA6 3 4 N THR B 68  ? N THR A 80  O LEU B 154 ? O LEU A 166 
AA7 1 2 O PHE B 100 ? O PHE A 112 N GLY B 91  ? N GLY A 103 
AA7 2 3 N PHE B 88  ? N PHE A 100 O ILE B 129 ? O ILE A 141 
AA7 3 4 N ILE B 130 ? N ILE A 142 O ARG B 140 ? O ARG A 152 
AA8 1 2 N ALA B 159 ? N ALA A 171 O LEU B 171 ? O LEU A 183 
# 
_pdbx_entry_details.entry_id                   9IF9 
_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 O   B HOH 425 ? ? O B HOH 428 ? ? 2.04 
2 1 O   A HOH 412 ? ? O A HOH 422 ? ? 2.11 
3 1 N   B ALA 13  ? ? O B HOH 401 ? ? 2.16 
4 1 OE1 A GLU 208 ? ? O A HOH 401 ? ? 2.17 
5 1 O   A HOH 430 ? ? O A HOH 437 ? ? 2.18 
6 1 O   A SER 28  ? ? O A HOH 402 ? ? 2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             C 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              29 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             N 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_2              30 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_3              30 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                131.18 
_pdbx_validate_rmsd_angle.angle_target_value         119.30 
_pdbx_validate_rmsd_angle.angle_deviation            11.88 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.50 
_pdbx_validate_rmsd_angle.linker_flag                Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER B 55  ? ? -152.29 -131.10 
2  1 CYS B 61  ? ? -66.67  61.74   
3  1 ALA B 156 ? ? 68.72   150.41  
4  1 ILE B 233 ? ? 73.29   -53.64  
5  1 CYS B 247 ? ? 57.41   76.55   
6  1 SER A 55  ? ? -146.46 -135.40 
7  1 ALA A 156 ? ? 69.91   148.96  
8  1 ASP A 159 ? ? -72.91  -162.06 
9  1 ASN A 195 ? ? -84.06  -122.42 
10 1 CYS A 247 ? ? 69.21   68.44   
# 
_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     36 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.170 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 C TPO 7 C TPO 7 ? THR 'modified residue' 
2 D TPO 7 D TPO 7 ? THR 'modified residue' 
# 
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 B ASN 31  ? A ASN 19  
2  1 Y 1 B GLY 32  ? A GLY 20  
3  1 Y 1 B ASP 33  ? A ASP 21  
4  1 Y 1 B ARG 34  ? A ARG 22  
5  1 Y 1 B GLY 120 ? A GLY 108 
6  1 Y 1 B SER 121 ? A SER 109 
7  1 Y 1 B GLN 122 ? A GLN 110 
8  1 Y 1 B SER 123 ? A SER 111 
9  1 Y 1 B ASN 124 ? A ASN 112 
10 1 Y 1 B SER 125 ? A SER 113 
11 1 Y 1 B ASP 126 ? A ASP 114 
12 1 Y 1 B THR 127 ? A THR 115 
13 1 Y 1 B GLN 128 ? A GLN 116 
14 1 Y 1 B SER 129 ? A SER 117 
15 1 Y 1 A ASP 33  ? B ASP 21  
16 1 Y 1 A ARG 34  ? B ARG 22  
17 1 Y 1 A GLY 35  ? B GLY 23  
18 1 Y 1 A ARG 36  ? B ARG 24  
19 1 Y 1 A ARG 37  ? B ARG 25  
20 1 Y 1 A VAL 118 ? B VAL 106 
21 1 Y 1 A PRO 119 ? B PRO 107 
22 1 Y 1 A GLY 120 ? B GLY 108 
23 1 Y 1 A SER 121 ? B SER 109 
24 1 Y 1 A GLN 122 ? B GLN 110 
25 1 Y 1 A SER 123 ? B SER 111 
26 1 Y 1 A ASN 124 ? B ASN 112 
27 1 Y 1 A SER 125 ? B SER 113 
28 1 Y 1 A ASP 126 ? B ASP 114 
29 1 Y 1 A THR 127 ? B THR 115 
30 1 Y 1 A GLN 128 ? B GLN 116 
31 1 Y 1 A SER 129 ? B SER 117 
32 1 Y 1 A PHE 197 ? B PHE 185 
33 1 Y 1 A THR 198 ? B THR 186 
34 1 Y 1 A GLU 199 ? B GLU 187 
35 1 Y 1 A ASP 200 ? B ASP 188 
36 1 Y 1 A SER 201 ? B SER 189 
37 1 Y 1 A LYS 202 ? B LYS 190 
38 1 Y 1 A ALA 256 ? B ALA 244 
39 1 Y 1 A GLU 257 ? B GLU 245 
40 1 Y 1 A GLY 258 ? B GLY 246 
41 1 Y 1 A LEU 259 ? B LEU 247 
42 1 Y 1 A SER 260 ? B SER 248 
43 1 Y 1 A HIS 261 ? B HIS 249 
44 1 Y 1 A THR 262 ? B THR 250 
45 1 Y 1 A PRO 263 ? B PRO 251 
# 
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 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
SO4 S    S N N 304 
SO4 O1   O N N 305 
SO4 O2   O N N 306 
SO4 O3   O N N 307 
SO4 O4   O N N 308 
THR N    N N N 309 
THR CA   C N S 310 
THR C    C N N 311 
THR O    O N N 312 
THR CB   C N R 313 
THR OG1  O N N 314 
THR CG2  C N N 315 
THR OXT  O N N 316 
THR H    H N N 317 
THR H2   H N N 318 
THR HA   H N N 319 
THR HB   H N N 320 
THR HG1  H N N 321 
THR HG21 H N N 322 
THR HG22 H N N 323 
THR HG23 H N N 324 
THR HXT  H N N 325 
TPO N    N N N 326 
TPO CA   C N S 327 
TPO CB   C N R 328 
TPO CG2  C N N 329 
TPO OG1  O N N 330 
TPO P    P N N 331 
TPO O1P  O N N 332 
TPO O2P  O N N 333 
TPO O3P  O N N 334 
TPO C    C N N 335 
TPO O    O N N 336 
TPO OXT  O N N 337 
TPO H    H N N 338 
TPO H2   H N N 339 
TPO HA   H N N 340 
TPO HB   H N N 341 
TPO HG21 H N N 342 
TPO HG22 H N N 343 
TPO HG23 H N N 344 
TPO HOP2 H N N 345 
TPO HOP3 H N N 346 
TPO HXT  H N N 347 
TRP N    N N N 348 
TRP CA   C N S 349 
TRP C    C N N 350 
TRP O    O N N 351 
TRP CB   C N N 352 
TRP CG   C Y N 353 
TRP CD1  C Y N 354 
TRP CD2  C Y N 355 
TRP NE1  N Y N 356 
TRP CE2  C Y N 357 
TRP CE3  C Y N 358 
TRP CZ2  C Y N 359 
TRP CZ3  C Y N 360 
TRP CH2  C Y N 361 
TRP OXT  O N N 362 
TRP H    H N N 363 
TRP H2   H N N 364 
TRP HA   H N N 365 
TRP HB2  H N N 366 
TRP HB3  H N N 367 
TRP HD1  H N N 368 
TRP HE1  H N N 369 
TRP HE3  H N N 370 
TRP HZ2  H N N 371 
TRP HZ3  H N N 372 
TRP HH2  H N N 373 
TRP HXT  H N N 374 
TYR N    N N N 375 
TYR CA   C N S 376 
TYR C    C N N 377 
TYR O    O N N 378 
TYR CB   C N N 379 
TYR CG   C Y N 380 
TYR CD1  C Y N 381 
TYR CD2  C Y N 382 
TYR CE1  C Y N 383 
TYR CE2  C Y N 384 
TYR CZ   C Y N 385 
TYR OH   O N N 386 
TYR OXT  O N N 387 
TYR H    H N N 388 
TYR H2   H N N 389 
TYR HA   H N N 390 
TYR HB2  H N N 391 
TYR HB3  H N N 392 
TYR HD1  H N N 393 
TYR HD2  H N N 394 
TYR HE1  H N N 395 
TYR HE2  H N N 396 
TYR HH   H N N 397 
TYR HXT  H N N 398 
VAL N    N N N 399 
VAL CA   C N S 400 
VAL C    C N N 401 
VAL O    O N N 402 
VAL CB   C N N 403 
VAL CG1  C N N 404 
VAL CG2  C N N 405 
VAL OXT  O N N 406 
VAL H    H N N 407 
VAL H2   H N N 408 
VAL HA   H N N 409 
VAL HB   H N N 410 
VAL HG11 H N N 411 
VAL HG12 H N N 412 
VAL HG13 H N N 413 
VAL HG21 H N N 414 
VAL HG22 H N N 415 
VAL HG23 H N N 416 
VAL HXT  H N N 417 
# 
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 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
SO4 S   O1   doub N N 290 
SO4 S   O2   doub N N 291 
SO4 S   O3   sing N N 292 
SO4 S   O4   sing N N 293 
THR N   CA   sing N N 294 
THR N   H    sing N N 295 
THR N   H2   sing N N 296 
THR CA  C    sing N N 297 
THR CA  CB   sing N N 298 
THR CA  HA   sing N N 299 
THR C   O    doub N N 300 
THR C   OXT  sing N N 301 
THR CB  OG1  sing N N 302 
THR CB  CG2  sing N N 303 
THR CB  HB   sing N N 304 
THR OG1 HG1  sing N N 305 
THR CG2 HG21 sing N N 306 
THR CG2 HG22 sing N N 307 
THR CG2 HG23 sing N N 308 
THR OXT HXT  sing N N 309 
TPO N   CA   sing N N 310 
TPO N   H    sing N N 311 
TPO N   H2   sing N N 312 
TPO CA  CB   sing N N 313 
TPO CA  C    sing N N 314 
TPO CA  HA   sing N N 315 
TPO CB  CG2  sing N N 316 
TPO CB  OG1  sing N N 317 
TPO CB  HB   sing N N 318 
TPO CG2 HG21 sing N N 319 
TPO CG2 HG22 sing N N 320 
TPO CG2 HG23 sing N N 321 
TPO OG1 P    sing N N 322 
TPO P   O1P  doub N N 323 
TPO P   O2P  sing N N 324 
TPO P   O3P  sing N N 325 
TPO O2P HOP2 sing N N 326 
TPO O3P HOP3 sing N N 327 
TPO C   O    doub N N 328 
TPO C   OXT  sing N N 329 
TPO 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 
'Swiss National Science Foundation'                              Switzerland      31003A_163141 1 
'Swiss National Science Foundation'                              Switzerland      310030_189141 2 
'Biotechnology and Biological Sciences Research Council (BBSRC)' 'United Kingdom' BB/T00746X/1  3 
'Cancer Research UK'                                             'United Kingdom' FC001003      4 
'Medical Research Council (MRC, United Kingdom)'                 'United Kingdom' FC001003      5 
'Wellcome Trust'                                                 'United Kingdom' FC001003      6 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   1,2 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3EGA 
_pdbx_initial_refinement_model.details          'Pellino 2 FHA Domain' 
# 
_atom_sites.entry_id                    9IF9 
_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]   0.018920 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013318 
_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]   0.006056 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA A 1 1   ? 10.896  33.243  -26.059 1.00 41.71 ? 13  ALA B N   1 
ATOM   2    C CA  . ALA A 1 1   ? 10.853  32.014  -25.253 1.00 48.68 ? 13  ALA B CA  1 
ATOM   3    C C   . ALA A 1 1   ? 10.113  30.892  -25.972 1.00 48.59 ? 13  ALA B C   1 
ATOM   4    O O   . ALA A 1 1   ? 8.946   31.035  -26.348 1.00 50.52 ? 13  ALA B O   1 
ATOM   5    C CB  . ALA A 1 1   ? 10.200  32.280  -23.894 1.00 51.16 ? 13  ALA B CB  1 
ATOM   6    N N   . PRO A 1 2   ? 10.787  29.763  -26.153 1.00 49.66 ? 14  PRO B N   1 
ATOM   7    C CA  . PRO A 1 2   ? 10.188  28.676  -26.934 1.00 48.48 ? 14  PRO B CA  1 
ATOM   8    C C   . PRO A 1 2   ? 9.103   27.990  -26.125 1.00 47.01 ? 14  PRO B C   1 
ATOM   9    O O   . PRO A 1 2   ? 9.172   27.908  -24.894 1.00 48.26 ? 14  PRO B O   1 
ATOM   10   C CB  . PRO A 1 2   ? 11.368  27.732  -27.195 1.00 42.68 ? 14  PRO B CB  1 
ATOM   11   C CG  . PRO A 1 2   ? 12.225  27.915  -25.946 1.00 46.36 ? 14  PRO B CG  1 
ATOM   12   C CD  . PRO A 1 2   ? 12.057  29.367  -25.516 1.00 39.82 ? 14  PRO B CD  1 
ATOM   13   N N   . VAL A 1 3   ? 8.084   27.506  -26.834 1.00 38.05 ? 15  VAL B N   1 
ATOM   14   C CA  . VAL A 1 3   ? 7.011   26.752  -26.197 1.00 31.56 ? 15  VAL B CA  1 
ATOM   15   C C   . VAL A 1 3   ? 7.558   25.420  -25.706 1.00 28.89 ? 15  VAL B C   1 
ATOM   16   O O   . VAL A 1 3   ? 8.185   24.677  -26.468 1.00 33.06 ? 15  VAL B O   1 
ATOM   17   C CB  . VAL A 1 3   ? 5.852   26.553  -27.186 1.00 34.70 ? 15  VAL B CB  1 
ATOM   18   C CG1 . VAL A 1 3   ? 4.766   25.640  -26.586 1.00 34.69 ? 15  VAL B CG1 1 
ATOM   19   C CG2 . VAL A 1 3   ? 5.271   27.911  -27.608 1.00 35.06 ? 15  VAL B CG2 1 
ATOM   20   N N   . LYS A 1 4   ? 7.343   25.113  -24.426 1.00 28.13 ? 16  LYS B N   1 
ATOM   21   C CA  . LYS A 1 4   ? 7.748   23.822  -23.863 1.00 27.03 ? 16  LYS B CA  1 
ATOM   22   C C   . LYS A 1 4   ? 6.580   22.850  -24.007 1.00 30.96 ? 16  LYS B C   1 
ATOM   23   O O   . LYS A 1 4   ? 5.593   22.930  -23.271 1.00 34.09 ? 16  LYS B O   1 
ATOM   24   C CB  . LYS A 1 4   ? 8.185   23.971  -22.409 1.00 29.52 ? 16  LYS B CB  1 
ATOM   25   C CG  . LYS A 1 4   ? 8.851   22.723  -21.839 1.00 27.26 ? 16  LYS B CG  1 
ATOM   26   C CD  . LYS A 1 4   ? 8.698   22.561  -20.326 1.00 29.46 ? 16  LYS B CD  1 
ATOM   27   C CE  . LYS A 1 4   ? 9.999   21.999  -19.701 1.00 32.40 ? 16  LYS B CE  1 
ATOM   28   N NZ  . LYS A 1 4   ? 9.847   21.564  -18.279 1.00 31.41 ? 16  LYS B NZ  1 
ATOM   29   N N   . TYR A 1 5   ? 6.685   21.942  -24.982 1.00 26.31 ? 17  TYR B N   1 
ATOM   30   C CA  . TYR A 1 5   ? 5.674   20.903  -25.166 1.00 23.56 ? 17  TYR B CA  1 
ATOM   31   C C   . TYR A 1 5   ? 5.524   20.041  -23.913 1.00 26.09 ? 17  TYR B C   1 
ATOM   32   O O   . TYR A 1 5   ? 4.404   19.721  -23.500 1.00 25.38 ? 17  TYR B O   1 
ATOM   33   C CB  . TYR A 1 5   ? 6.040   20.019  -26.361 1.00 22.11 ? 17  TYR B CB  1 
ATOM   34   C CG  . TYR A 1 5   ? 6.028   20.704  -27.708 1.00 23.29 ? 17  TYR B CG  1 
ATOM   35   C CD1 . TYR A 1 5   ? 4.996   21.559  -28.073 1.00 21.57 ? 17  TYR B CD1 1 
ATOM   36   C CD2 . TYR A 1 5   ? 7.051   20.486  -28.622 1.00 23.55 ? 17  TYR B CD2 1 
ATOM   37   C CE1 . TYR A 1 5   ? 4.986   22.178  -29.299 1.00 18.42 ? 17  TYR B CE1 1 
ATOM   38   C CE2 . TYR A 1 5   ? 7.039   21.096  -29.857 1.00 23.98 ? 17  TYR B CE2 1 
ATOM   39   C CZ  . TYR A 1 5   ? 6.008   21.944  -30.184 1.00 22.55 ? 17  TYR B CZ  1 
ATOM   40   O OH  . TYR A 1 5   ? 6.015   22.550  -31.419 1.00 25.34 ? 17  TYR B OH  1 
ATOM   41   N N   . GLY A 1 6   ? 6.635   19.666  -23.295 1.00 26.59 ? 18  GLY B N   1 
ATOM   42   C CA  . GLY A 1 6   ? 6.609   18.749  -22.174 1.00 22.77 ? 18  GLY B CA  1 
ATOM   43   C C   . GLY A 1 6   ? 7.974   18.147  -21.905 1.00 22.21 ? 18  GLY B C   1 
ATOM   44   O O   . GLY A 1 6   ? 8.951   18.408  -22.594 1.00 22.92 ? 18  GLY B O   1 
ATOM   45   N N   . GLU A 1 7   ? 8.015   17.319  -20.878 1.00 22.71 ? 19  GLU B N   1 
ATOM   46   C CA  . GLU A 1 7   ? 9.279   16.793  -20.399 1.00 26.98 ? 19  GLU B CA  1 
ATOM   47   C C   . GLU A 1 7   ? 9.171   15.290  -20.200 1.00 29.67 ? 19  GLU B C   1 
ATOM   48   O O   . GLU A 1 7   ? 8.156   14.789  -19.702 1.00 28.15 ? 19  GLU B O   1 
ATOM   49   C CB  . GLU A 1 7   ? 9.674   17.466  -19.091 1.00 31.22 ? 19  GLU B CB  1 
ATOM   50   C CG  . GLU A 1 7   ? 11.110  17.920  -19.013 1.00 36.31 ? 19  GLU B CG  1 
ATOM   51   C CD  . GLU A 1 7   ? 11.391  18.646  -17.713 1.00 50.34 ? 19  GLU B CD  1 
ATOM   52   O OE1 . GLU A 1 7   ? 10.754  18.276  -16.699 1.00 58.09 ? 19  GLU B OE1 1 
ATOM   53   O OE2 . GLU A 1 7   ? 12.230  19.583  -17.704 1.00 51.05 ? 19  GLU B OE2 1 
ATOM   54   N N   . LEU A 1 8   ? 10.216  14.576  -20.595 1.00 24.94 ? 20  LEU B N   1 
ATOM   55   C CA  . LEU A 1 8   ? 10.271  13.140  -20.421 1.00 23.20 ? 20  LEU B CA  1 
ATOM   56   C C   . LEU A 1 8   ? 11.218  12.850  -19.271 1.00 29.39 ? 20  LEU B C   1 
ATOM   57   O O   . LEU A 1 8   ? 12.289  13.453  -19.188 1.00 34.59 ? 20  LEU B O   1 
ATOM   58   C CB  . LEU A 1 8   ? 10.747  12.466  -21.703 1.00 24.26 ? 20  LEU B CB  1 
ATOM   59   C CG  . LEU A 1 8   ? 9.757   12.347  -22.860 1.00 22.72 ? 20  LEU B CG  1 
ATOM   60   C CD1 . LEU A 1 8   ? 10.513  12.284  -24.154 1.00 21.41 ? 20  LEU B CD1 1 
ATOM   61   C CD2 . LEU A 1 8   ? 8.910   11.104  -22.703 1.00 25.55 ? 20  LEU B CD2 1 
ATOM   62   N N   . ILE A 1 9   ? 10.821  11.946  -18.379 1.00 31.53 ? 21  ILE B N   1 
ATOM   63   C CA  . ILE A 1 9   ? 11.596  11.597  -17.190 1.00 32.47 ? 21  ILE B CA  1 
ATOM   64   C C   . ILE A 1 9   ? 11.782  10.087  -17.158 1.00 33.28 ? 21  ILE B C   1 
ATOM   65   O O   . ILE A 1 9   ? 10.803  9.336   -17.263 1.00 31.94 ? 21  ILE B O   1 
ATOM   66   C CB  . ILE A 1 9   ? 10.913  12.086  -15.897 1.00 30.86 ? 21  ILE B CB  1 
ATOM   67   C CG1 . ILE A 1 9   ? 10.662  13.589  -15.946 1.00 32.43 ? 21  ILE B CG1 1 
ATOM   68   C CG2 . ILE A 1 9   ? 11.734  11.718  -14.676 1.00 34.47 ? 21  ILE B CG2 1 
ATOM   69   C CD1 . ILE A 1 9   ? 9.229   13.949  -15.790 1.00 32.03 ? 21  ILE B CD1 1 
ATOM   70   N N   . VAL A 1 10  ? 13.026  9.646   -16.988 1.00 33.16 ? 22  VAL B N   1 
ATOM   71   C CA  . VAL A 1 10  ? 13.330  8.217   -16.967 1.00 30.65 ? 22  VAL B CA  1 
ATOM   72   C C   . VAL A 1 10  ? 13.049  7.651   -15.580 1.00 35.22 ? 22  VAL B C   1 
ATOM   73   O O   . VAL A 1 10  ? 13.518  8.184   -14.564 1.00 38.17 ? 22  VAL B O   1 
ATOM   74   C CB  . VAL A 1 10  ? 14.784  7.969   -17.384 1.00 31.04 ? 22  VAL B CB  1 
ATOM   75   C CG1 . VAL A 1 10  ? 15.166  6.523   -17.126 1.00 32.09 ? 22  VAL B CG1 1 
ATOM   76   C CG2 . VAL A 1 10  ? 14.972  8.328   -18.839 1.00 36.41 ? 22  VAL B CG2 1 
ATOM   77   N N   . LEU A 1 11  ? 12.285  6.559   -15.533 1.00 33.37 ? 23  LEU B N   1 
ATOM   78   C CA  . LEU A 1 11  ? 11.941  5.908   -14.269 1.00 38.27 ? 23  LEU B CA  1 
ATOM   79   C C   . LEU A 1 11  ? 12.973  4.815   -14.028 1.00 47.76 ? 23  LEU B C   1 
ATOM   80   O O   . LEU A 1 11  ? 12.785  3.669   -14.426 1.00 53.22 ? 23  LEU B O   1 
ATOM   81   C CB  . LEU A 1 11  ? 10.521  5.359   -14.313 1.00 29.57 ? 23  LEU B CB  1 
ATOM   82   C CG  . LEU A 1 11  ? 9.450   6.236   -13.672 1.00 28.28 ? 23  LEU B CG  1 
ATOM   83   C CD1 . LEU A 1 11  ? 9.725   7.690   -13.962 1.00 32.63 ? 23  LEU B CD1 1 
ATOM   84   C CD2 . LEU A 1 11  ? 8.084   5.869   -14.200 1.00 24.71 ? 23  LEU B CD2 1 
ATOM   85   N N   . GLY A 1 12  ? 14.064  5.178   -13.355 1.00 46.87 ? 24  GLY B N   1 
ATOM   86   C CA  . GLY A 1 12  ? 15.236  4.316   -13.296 1.00 49.74 ? 24  GLY B CA  1 
ATOM   87   C C   . GLY A 1 12  ? 14.957  2.990   -12.604 1.00 59.59 ? 24  GLY B C   1 
ATOM   88   O O   . GLY A 1 12  ? 14.389  2.950   -11.505 1.00 58.49 ? 24  GLY B O   1 
ATOM   89   N N   . TYR A 1 13  ? 15.375  1.890   -13.257 1.00 65.37 ? 25  TYR B N   1 
ATOM   90   C CA  . TYR A 1 13  ? 15.252  0.527   -12.731 1.00 64.70 ? 25  TYR B CA  1 
ATOM   91   C C   . TYR A 1 13  ? 16.277  0.246   -11.627 1.00 64.54 ? 25  TYR B C   1 
ATOM   92   O O   . TYR A 1 13  ? 16.023  -0.572  -10.730 1.00 62.01 ? 25  TYR B O   1 
ATOM   93   C CB  . TYR A 1 13  ? 15.427  -0.513  -13.870 1.00 60.98 ? 25  TYR B CB  1 
ATOM   94   C CG  . TYR A 1 13  ? 14.381  -0.513  -15.004 1.00 61.51 ? 25  TYR B CG  1 
ATOM   95   C CD1 . TYR A 1 13  ? 13.227  0.267   -14.934 1.00 61.02 ? 25  TYR B CD1 1 
ATOM   96   C CD2 . TYR A 1 13  ? 14.558  -1.296  -16.151 1.00 61.73 ? 25  TYR B CD2 1 
ATOM   97   C CE1 . TYR A 1 13  ? 12.276  0.272   -15.968 1.00 52.25 ? 25  TYR B CE1 1 
ATOM   98   C CE2 . TYR A 1 13  ? 13.604  -1.295  -17.189 1.00 56.93 ? 25  TYR B CE2 1 
ATOM   99   C CZ  . TYR A 1 13  ? 12.466  -0.499  -17.086 1.00 47.84 ? 25  TYR B CZ  1 
ATOM   100  O OH  . TYR A 1 13  ? 11.509  -0.464  -18.081 1.00 44.40 ? 25  TYR B OH  1 
ATOM   101  N N   . ASN A 1 14  ? 17.433  0.913   -11.678 1.00 67.61 ? 26  ASN B N   1 
ATOM   102  C CA  . ASN A 1 14  ? 18.525  0.597   -10.762 1.00 66.77 ? 26  ASN B CA  1 
ATOM   103  C C   . ASN A 1 14  ? 18.129  0.838   -9.308  1.00 67.55 ? 26  ASN B C   1 
ATOM   104  O O   . ASN A 1 14  ? 18.434  0.019   -8.430  1.00 67.37 ? 26  ASN B O   1 
ATOM   105  C CB  . ASN A 1 14  ? 19.761  1.417   -11.137 1.00 62.75 ? 26  ASN B CB  1 
ATOM   106  C CG  . ASN A 1 14  ? 19.399  2.786   -11.689 1.00 73.46 ? 26  ASN B CG  1 
ATOM   107  O OD1 . ASN A 1 14  ? 18.970  3.672   -10.946 1.00 74.88 ? 26  ASN B OD1 1 
ATOM   108  N ND2 . ASN A 1 14  ? 19.538  2.956   -13.005 1.00 74.35 ? 26  ASN B ND2 1 
ATOM   109  N N   . GLY A 1 15  ? 17.423  1.935   -9.033  1.00 64.07 ? 27  GLY B N   1 
ATOM   110  C CA  . GLY A 1 15  ? 17.226  2.343   -7.656  1.00 58.37 ? 27  GLY B CA  1 
ATOM   111  C C   . GLY A 1 15  ? 18.347  3.190   -7.107  1.00 57.11 ? 27  GLY B C   1 
ATOM   112  O O   . GLY A 1 15  ? 18.516  3.260   -5.885  1.00 50.58 ? 27  GLY B O   1 
ATOM   113  N N   . SER A 1 16  ? 19.144  3.805   -7.984  1.00 61.80 ? 28  SER B N   1 
ATOM   114  C CA  . SER A 1 16  ? 20.137  4.807   -7.617  1.00 58.68 ? 28  SER B CA  1 
ATOM   115  C C   . SER A 1 16  ? 19.466  6.168   -7.435  1.00 53.64 ? 28  SER B C   1 
ATOM   116  O O   . SER A 1 16  ? 18.248  6.320   -7.584  1.00 55.62 ? 28  SER B O   1 
ATOM   117  C CB  . SER A 1 16  ? 21.261  4.862   -8.663  1.00 62.37 ? 28  SER B CB  1 
ATOM   118  O OG  . SER A 1 16  ? 20.791  5.013   -10.001 1.00 64.54 ? 28  SER B OG  1 
ATOM   119  N N   . LEU A 1 17  ? 20.270  7.174   -7.102  1.00 52.54 ? 29  LEU B N   1 
ATOM   120  C CA  . LEU A 1 17  ? 19.734  8.516   -6.902  1.00 50.21 ? 29  LEU B CA  1 
ATOM   121  C C   . LEU A 1 17  ? 19.620  9.239   -8.237  1.00 49.12 ? 29  LEU B C   1 
ATOM   122  O O   . LEU A 1 17  ? 20.647  9.499   -8.881  1.00 46.11 ? 29  LEU B O   1 
ATOM   123  C CB  . LEU A 1 17  ? 20.598  9.325   -5.951  1.00 43.77 ? 29  LEU B CB  1 
ATOM   124  C CG  . LEU A 1 17  ? 19.779  10.072  -4.906  1.00 35.62 ? 29  LEU B CG  1 
ATOM   125  C CD1 . LEU A 1 17  ? 18.609  9.215   -4.452  1.00 38.27 ? 29  LEU B CD1 1 
ATOM   126  C CD2 . LEU A 1 17  ? 20.632  10.431  -3.733  1.00 34.82 ? 29  LEU B CD2 1 
ATOM   127  N N   . PRO A 1 18  ? 18.402  9.603   -8.672  1.00 47.92 ? 30  PRO B N   1 
ATOM   128  C CA  . PRO A 1 18  ? 17.971  10.233  -9.929  1.00 47.63 ? 30  PRO B CA  1 
ATOM   129  C C   . PRO A 1 18  ? 18.831  11.394  -10.444 1.00 39.50 ? 30  PRO B C   1 
ATOM   130  O O   . PRO A 1 18  ? 19.025  12.365  -9.722  1.00 49.72 ? 30  PRO B O   1 
ATOM   131  C CB  . PRO A 1 18  ? 16.568  10.713  -9.573  1.00 42.19 ? 30  PRO B CB  1 
ATOM   132  C CG  . PRO A 1 18  ? 16.071  9.615   -8.639  1.00 36.42 ? 30  PRO B CG  1 
ATOM   133  C CD  . PRO A 1 18  ? 17.253  9.320   -7.786  1.00 39.58 ? 30  PRO B CD  1 
ATOM   134  N N   . GLY A 1 23  ? 19.526  16.544  -20.206 1.00 49.77 ? 35  GLY B N   1 
ATOM   135  C CA  . GLY A 1 23  ? 20.328  16.341  -21.411 1.00 53.10 ? 35  GLY B CA  1 
ATOM   136  C C   . GLY A 1 23  ? 20.013  15.199  -22.381 1.00 53.16 ? 35  GLY B C   1 
ATOM   137  O O   . GLY A 1 23  ? 19.251  14.298  -22.030 1.00 53.82 ? 35  GLY B O   1 
ATOM   138  N N   . ARG A 1 24  ? 20.567  15.204  -23.592 1.00 54.96 ? 36  ARG B N   1 
ATOM   139  C CA  . ARG A 1 24  ? 20.211  14.161  -24.590 1.00 54.59 ? 36  ARG B CA  1 
ATOM   140  C C   . ARG A 1 24  ? 20.451  12.761  -24.013 1.00 52.07 ? 36  ARG B C   1 
ATOM   141  O O   . ARG A 1 24  ? 19.680  11.842  -24.344 1.00 47.25 ? 36  ARG B O   1 
ATOM   142  C CB  . ARG A 1 24  ? 21.039  14.284  -25.872 1.00 30.00 ? 36  ARG B CB  1 
ATOM   143  C CG  . ARG A 1 24  ? 20.764  13.212  -26.915 1.00 30.00 ? 36  ARG B CG  1 
ATOM   144  C CD  . ARG A 1 24  ? 20.826  13.758  -28.327 1.00 30.00 ? 36  ARG B CD  1 
ATOM   145  N NE  . ARG A 1 24  ? 20.820  12.671  -29.310 1.00 30.00 ? 36  ARG B NE  1 
ATOM   146  C CZ  . ARG A 1 24  ? 21.903  12.115  -29.833 1.00 30.00 ? 36  ARG B CZ  1 
ATOM   147  N NH1 . ARG A 1 24  ? 22.987  11.938  -29.101 1.00 30.00 ? 36  ARG B NH1 1 
ATOM   148  N NH2 . ARG A 1 24  ? 21.894  11.735  -31.094 1.00 30.00 ? 36  ARG B NH2 1 
ATOM   149  N N   . ARG A 1 25  ? 21.505  12.603  -23.215 1.00 51.59 ? 37  ARG B N   1 
ATOM   150  C CA  . ARG A 1 25  ? 21.767  11.312  -22.583 1.00 58.37 ? 37  ARG B CA  1 
ATOM   151  C C   . ARG A 1 25  ? 21.508  11.248  -21.082 1.00 62.32 ? 37  ARG B C   1 
ATOM   152  O O   . ARG A 1 25  ? 21.826  10.231  -20.449 1.00 63.29 ? 37  ARG B O   1 
ATOM   153  C CB  . ARG A 1 25  ? 23.252  11.015  -22.863 1.00 63.11 ? 37  ARG B CB  1 
ATOM   154  C CG  . ARG A 1 25  ? 23.685  11.233  -24.309 1.00 50.47 ? 37  ARG B CG  1 
ATOM   155  C CD  . ARG A 1 25  ? 24.449  10.040  -24.848 1.00 48.51 ? 37  ARG B CD  1 
ATOM   156  N NE  . ARG A 1 25  ? 25.153  10.406  -26.073 1.00 56.26 ? 37  ARG B NE  1 
ATOM   157  C CZ  . ARG A 1 25  ? 26.232  9.792   -26.542 1.00 55.46 ? 37  ARG B CZ  1 
ATOM   158  N NH1 . ARG A 1 25  ? 26.790  8.783   -25.893 1.00 46.95 ? 37  ARG B NH1 1 
ATOM   159  N NH2 . ARG A 1 25  ? 26.764  10.203  -27.691 1.00 56.32 ? 37  ARG B NH2 1 
ATOM   160  N N   . LYS A 1 26  ? 20.944  12.312  -20.503 1.00 55.99 ? 38  LYS B N   1 
ATOM   161  C CA  . LYS A 1 26  ? 20.682  12.436  -19.076 1.00 48.07 ? 38  LYS B CA  1 
ATOM   162  C C   . LYS A 1 26  ? 19.374  11.699  -18.750 1.00 49.70 ? 38  LYS B C   1 
ATOM   163  O O   . LYS A 1 26  ? 18.932  10.848  -19.531 1.00 48.52 ? 38  LYS B O   1 
ATOM   164  C CB  . LYS A 1 26  ? 20.679  13.928  -18.705 1.00 42.83 ? 38  LYS B CB  1 
ATOM   165  C CG  . LYS A 1 26  ? 20.706  14.307  -17.205 1.00 50.19 ? 38  LYS B CG  1 
ATOM   166  C CD  . LYS A 1 26  ? 19.539  15.251  -16.803 1.00 44.75 ? 38  LYS B CD  1 
ATOM   167  C CE  . LYS A 1 26  ? 19.625  15.671  -15.327 1.00 46.84 ? 38  LYS B CE  1 
ATOM   168  N NZ  . LYS A 1 26  ? 20.518  16.863  -15.087 1.00 34.29 ? 38  LYS B NZ  1 
ATOM   169  N N   . SER A 1 27  ? 18.751  11.981  -17.604 1.00 50.22 ? 39  SER B N   1 
ATOM   170  C CA  . SER A 1 27  ? 17.547  11.280  -17.153 1.00 40.99 ? 39  SER B CA  1 
ATOM   171  C C   . SER A 1 27  ? 16.259  12.020  -17.453 1.00 39.12 ? 39  SER B C   1 
ATOM   172  O O   . SER A 1 27  ? 15.183  11.440  -17.278 1.00 36.93 ? 39  SER B O   1 
ATOM   173  C CB  . SER A 1 27  ? 17.592  11.058  -15.640 1.00 51.57 ? 39  SER B CB  1 
ATOM   174  O OG  . SER A 1 27  ? 18.114  12.219  -14.995 1.00 59.14 ? 39  SER B OG  1 
ATOM   175  N N   . ARG A 1 28  ? 16.342  13.303  -17.787 1.00 40.84 ? 40  ARG B N   1 
ATOM   176  C CA  . ARG A 1 28  ? 15.194  14.129  -18.116 1.00 35.77 ? 40  ARG B CA  1 
ATOM   177  C C   . ARG A 1 28  ? 15.513  14.854  -19.406 1.00 37.10 ? 40  ARG B C   1 
ATOM   178  O O   . ARG A 1 28  ? 16.648  15.295  -19.608 1.00 44.98 ? 40  ARG B O   1 
ATOM   179  C CB  . ARG A 1 28  ? 14.884  15.145  -17.009 1.00 34.59 ? 40  ARG B CB  1 
ATOM   180  C CG  . ARG A 1 28  ? 14.943  14.524  -15.614 1.00 43.28 ? 40  ARG B CG  1 
ATOM   181  C CD  . ARG A 1 28  ? 15.086  15.560  -14.528 1.00 47.43 ? 40  ARG B CD  1 
ATOM   182  N NE  . ARG A 1 28  ? 13.804  16.173  -14.248 1.00 54.45 ? 40  ARG B NE  1 
ATOM   183  C CZ  . ARG A 1 28  ? 13.448  17.373  -14.689 1.00 60.05 ? 40  ARG B CZ  1 
ATOM   184  N NH1 . ARG A 1 28  ? 14.224  18.074  -15.513 1.00 55.25 ? 40  ARG B NH1 1 
ATOM   185  N NH2 . ARG A 1 28  ? 12.267  17.867  -14.328 1.00 61.25 ? 40  ARG B NH2 1 
ATOM   186  N N   . PHE A 1 29  ? 14.521  14.969  -20.281 1.00 34.62 ? 41  PHE B N   1 
ATOM   187  C CA  . PHE A 1 29  ? 14.674  15.706  -21.527 1.00 30.94 ? 41  PHE B CA  1 
ATOM   188  C C   . PHE A 1 29  ? 13.388  16.464  -21.809 1.00 28.11 ? 41  PHE B C   1 
ATOM   189  O O   . PHE A 1 29  ? 12.317  15.860  -21.898 1.00 27.81 ? 41  PHE B O   1 
ATOM   190  C CB  . PHE A 1 29  ? 14.992  14.757  -22.678 1.00 38.87 ? 41  PHE B CB  1 
ATOM   191  C CG  . PHE A 1 29  ? 15.296  15.452  -23.979 1.00 43.44 ? 41  PHE B CG  1 
ATOM   192  C CD1 . PHE A 1 29  ? 16.465  16.195  -24.129 1.00 42.44 ? 41  PHE B CD1 1 
ATOM   193  C CD2 . PHE A 1 29  ? 14.398  15.379  -25.046 1.00 37.97 ? 41  PHE B CD2 1 
ATOM   194  C CE1 . PHE A 1 29  ? 16.750  16.836  -25.318 1.00 41.45 ? 41  PHE B CE1 1 
ATOM   195  C CE2 . PHE A 1 29  ? 14.665  16.022  -26.234 1.00 33.95 ? 41  PHE B CE2 1 
ATOM   196  C CZ  . PHE A 1 29  ? 15.850  16.753  -26.375 1.00 43.06 ? 41  PHE B CZ  1 
ATOM   197  N N   . ALA A 1 30  ? 13.488  17.778  -21.933 1.00 27.32 ? 42  ALA B N   1 
ATOM   198  C CA  . ALA A 1 30  ? 12.341  18.578  -22.328 1.00 29.21 ? 42  ALA B CA  1 
ATOM   199  C C   . ALA A 1 30  ? 12.217  18.613  -23.847 1.00 34.77 ? 42  ALA B C   1 
ATOM   200  O O   . ALA A 1 30  ? 13.197  18.461  -24.582 1.00 38.98 ? 42  ALA B O   1 
ATOM   201  C CB  . ALA A 1 30  ? 12.435  20.004  -21.786 1.00 27.14 ? 42  ALA B CB  1 
ATOM   202  N N   . LEU A 1 31  ? 10.991  18.800  -24.312 1.00 30.92 ? 43  LEU B N   1 
ATOM   203  C CA  . LEU A 1 31  ? 10.700  18.913  -25.728 1.00 25.17 ? 43  LEU B CA  1 
ATOM   204  C C   . LEU A 1 31  ? 10.217  20.332  -25.953 1.00 24.69 ? 43  LEU B C   1 
ATOM   205  O O   . LEU A 1 31  ? 9.329   20.804  -25.240 1.00 26.69 ? 43  LEU B O   1 
ATOM   206  C CB  . LEU A 1 31  ? 9.652   17.883  -26.151 1.00 27.08 ? 43  LEU B CB  1 
ATOM   207  C CG  . LEU A 1 31  ? 10.167  16.467  -26.436 1.00 27.12 ? 43  LEU B CG  1 
ATOM   208  C CD1 . LEU A 1 31  ? 10.872  15.865  -25.247 1.00 24.82 ? 43  LEU B CD1 1 
ATOM   209  C CD2 . LEU A 1 31  ? 9.020   15.556  -26.866 1.00 25.43 ? 43  LEU B CD2 1 
ATOM   210  N N   . PHE A 1 32  ? 10.846  21.030  -26.883 1.00 30.69 ? 44  PHE B N   1 
ATOM   211  C CA  . PHE A 1 32  ? 10.570  22.437  -27.122 1.00 28.07 ? 44  PHE B CA  1 
ATOM   212  C C   . PHE A 1 32  ? 10.193  22.617  -28.580 1.00 27.18 ? 44  PHE B C   1 
ATOM   213  O O   . PHE A 1 32  ? 10.763  21.951  -29.450 1.00 28.06 ? 44  PHE B O   1 
ATOM   214  C CB  . PHE A 1 32  ? 11.786  23.302  -26.794 1.00 27.76 ? 44  PHE B CB  1 
ATOM   215  C CG  . PHE A 1 32  ? 11.939  23.603  -25.337 1.00 30.04 ? 44  PHE B CG  1 
ATOM   216  C CD1 . PHE A 1 32  ? 11.214  24.631  -24.754 1.00 34.79 ? 44  PHE B CD1 1 
ATOM   217  C CD2 . PHE A 1 32  ? 12.814  22.862  -24.540 1.00 31.37 ? 44  PHE B CD2 1 
ATOM   218  C CE1 . PHE A 1 32  ? 11.356  24.923  -23.398 1.00 35.66 ? 44  PHE B CE1 1 
ATOM   219  C CE2 . PHE A 1 32  ? 12.956  23.141  -23.186 1.00 27.27 ? 44  PHE B CE2 1 
ATOM   220  C CZ  . PHE A 1 32  ? 12.225  24.171  -22.614 1.00 32.34 ? 44  PHE B CZ  1 
ATOM   221  N N   . LYS A 1 33  ? 9.220   23.501  -28.831 1.00 25.85 ? 45  LYS B N   1 
ATOM   222  C CA  . LYS A 1 33  ? 8.882   23.922  -30.189 1.00 25.45 ? 45  LYS B CA  1 
ATOM   223  C C   . LYS A 1 33  ? 10.146  24.325  -30.929 1.00 28.77 ? 45  LYS B C   1 
ATOM   224  O O   . LYS A 1 33  ? 10.952  25.107  -30.415 1.00 29.00 ? 45  LYS B O   1 
ATOM   225  C CB  . LYS A 1 33  ? 7.912   25.102  -30.159 1.00 25.65 ? 45  LYS B CB  1 
ATOM   226  C CG  . LYS A 1 33  ? 7.439   25.534  -31.517 1.00 22.01 ? 45  LYS B CG  1 
ATOM   227  C CD  . LYS A 1 33  ? 6.032   26.067  -31.430 1.00 23.26 ? 45  LYS B CD  1 
ATOM   228  C CE  . LYS A 1 33  ? 5.780   27.063  -32.535 1.00 20.15 ? 45  LYS B CE  1 
ATOM   229  N NZ  . LYS A 1 33  ? 4.700   28.003  -32.191 1.00 22.68 ? 45  LYS B NZ  1 
ATOM   230  N N   . ARG A 1 34  ? 10.332  23.745  -32.207 1.00 29.70 ? 46  ARG B N   1 
ATOM   231  C CA  . ARG A 1 34  ? 11.528  23.934  -33.015 1.00 28.42 ? 46  ARG B CA  1 
ATOM   232  C C   . ARG A 1 34  ? 11.408  25.185  -33.880 1.00 32.67 ? 46  ARG B C   1 
ATOM   233  O O   . ARG A 1 34  ? 10.298  25.565  -34.287 1.00 33.05 ? 46  ARG B O   1 
ATOM   234  C CB  . ARG A 1 34  ? 11.769  22.725  -33.922 1.00 32.36 ? 46  ARG B CB  1 
ATOM   235  C CG  . ARG A 1 34  ? 12.296  21.486  -33.219 1.00 33.05 ? 46  ARG B CG  1 
ATOM   236  C CD  . ARG A 1 34  ? 12.897  20.460  -34.193 1.00 36.59 ? 46  ARG B CD  1 
ATOM   237  N NE  . ARG A 1 34  ? 12.668  19.077  -33.773 1.00 33.99 ? 46  ARG B NE  1 
ATOM   238  C CZ  . ARG A 1 34  ? 13.532  18.330  -33.094 1.00 31.61 ? 46  ARG B CZ  1 
ATOM   239  N NH1 . ARG A 1 34  ? 14.686  18.817  -32.662 1.00 33.60 ? 46  ARG B NH1 1 
ATOM   240  N NH2 . ARG A 1 34  ? 13.230  17.060  -32.835 1.00 31.30 ? 46  ARG B NH2 1 
ATOM   241  N N   . PRO A 1 35  ? 12.553  25.838  -34.149 1.00 35.59 ? 47  PRO B N   1 
ATOM   242  C CA  . PRO A 1 35  ? 12.546  27.019  -35.043 1.00 34.00 ? 47  PRO B CA  1 
ATOM   243  C C   . PRO A 1 35  ? 11.835  26.815  -36.382 1.00 35.28 ? 47  PRO B C   1 
ATOM   244  O O   . PRO A 1 35  ? 10.996  27.651  -36.755 1.00 30.68 ? 47  PRO B O   1 
ATOM   245  C CB  . PRO A 1 35  ? 14.042  27.313  -35.220 1.00 23.54 ? 47  PRO B CB  1 
ATOM   246  C CG  . PRO A 1 35  ? 14.691  26.774  -33.994 1.00 25.46 ? 47  PRO B CG  1 
ATOM   247  C CD  . PRO A 1 35  ? 13.763  25.801  -33.309 1.00 29.53 ? 47  PRO B CD  1 
ATOM   248  N N   . LYS A 1 36  ? 12.150  25.738  -37.120 1.00 35.69 ? 48  LYS B N   1 
ATOM   249  C CA  . LYS A 1 36  ? 11.383  25.315  -38.291 1.00 37.59 ? 48  LYS B CA  1 
ATOM   250  C C   . LYS A 1 36  ? 10.792  23.923  -38.046 1.00 35.96 ? 48  LYS B C   1 
ATOM   251  O O   . LYS A 1 36  ? 11.479  23.018  -37.555 1.00 35.96 ? 48  LYS B O   1 
ATOM   252  C CB  . LYS A 1 36  ? 12.266  25.329  -39.575 1.00 36.95 ? 48  LYS B CB  1 
ATOM   253  C CG  . LYS A 1 36  ? 11.571  25.014  -40.969 1.00 40.11 ? 48  LYS B CG  1 
ATOM   254  C CD  . LYS A 1 36  ? 10.028  25.288  -41.082 1.00 43.06 ? 48  LYS B CD  1 
ATOM   255  C CE  . LYS A 1 36  ? 9.433   24.714  -42.405 1.00 47.72 ? 48  LYS B CE  1 
ATOM   256  N NZ  . LYS A 1 36  ? 7.924   24.788  -42.584 1.00 36.53 ? 48  LYS B NZ  1 
ATOM   257  N N   . ALA A 1 37  ? 9.512   23.763  -38.392 1.00 30.50 ? 49  ALA B N   1 
ATOM   258  C CA  . ALA A 1 37  ? 8.816   22.492  -38.209 1.00 32.62 ? 49  ALA B CA  1 
ATOM   259  C C   . ALA A 1 37  ? 9.476   21.348  -38.969 1.00 32.48 ? 49  ALA B C   1 
ATOM   260  O O   . ALA A 1 37  ? 9.816   21.488  -40.144 1.00 36.33 ? 49  ALA B O   1 
ATOM   261  C CB  . ALA A 1 37  ? 7.375   22.624  -38.675 1.00 34.40 ? 49  ALA B CB  1 
ATOM   262  N N   . ASN A 1 38  ? 9.596   20.191  -38.308 1.00 31.07 ? 50  ASN B N   1 
ATOM   263  C CA  . ASN A 1 38  ? 10.269  19.014  -38.851 1.00 30.89 ? 50  ASN B CA  1 
ATOM   264  C C   . ASN A 1 38  ? 9.369   17.787  -38.866 1.00 28.57 ? 50  ASN B C   1 
ATOM   265  O O   . ASN A 1 38  ? 9.857   16.666  -39.060 1.00 31.80 ? 50  ASN B O   1 
ATOM   266  C CB  . ASN A 1 38  ? 11.528  18.694  -38.038 1.00 32.08 ? 50  ASN B CB  1 
ATOM   267  C CG  . ASN A 1 38  ? 11.202  17.967  -36.752 1.00 30.19 ? 50  ASN B CG  1 
ATOM   268  O OD1 . ASN A 1 38  ? 10.332  18.387  -35.998 1.00 32.57 ? 50  ASN B OD1 1 
ATOM   269  N ND2 . ASN A 1 38  ? 11.884  16.867  -36.505 1.00 30.34 ? 50  ASN B ND2 1 
ATOM   270  N N   . GLY A 1 39  ? 8.090   17.952  -38.639 1.00 27.56 ? 51  GLY B N   1 
ATOM   271  C CA  . GLY A 1 39  ? 7.225   16.805  -38.560 1.00 25.51 ? 51  GLY B CA  1 
ATOM   272  C C   . GLY A 1 39  ? 6.852   16.269  -39.921 1.00 29.45 ? 51  GLY B C   1 
ATOM   273  O O   . GLY A 1 39  ? 6.838   16.964  -40.938 1.00 31.79 ? 51  GLY B O   1 
ATOM   274  N N   . VAL A 1 40  ? 6.540   14.985  -39.942 1.00 31.99 ? 52  VAL B N   1 
ATOM   275  C CA  . VAL A 1 40  ? 6.109   14.331  -41.163 1.00 29.30 ? 52  VAL B CA  1 
ATOM   276  C C   . VAL A 1 40  ? 4.679   13.870  -40.958 1.00 29.58 ? 52  VAL B C   1 
ATOM   277  O O   . VAL A 1 40  ? 4.178   13.815  -39.828 1.00 32.98 ? 52  VAL B O   1 
ATOM   278  C CB  . VAL A 1 40  ? 7.007   13.144  -41.508 1.00 27.22 ? 52  VAL B CB  1 
ATOM   279  C CG1 . VAL A 1 40  ? 8.358   13.641  -41.996 1.00 25.12 ? 52  VAL B CG1 1 
ATOM   280  C CG2 . VAL A 1 40  ? 7.138   12.268  -40.298 1.00 22.72 ? 52  VAL B CG2 1 
ATOM   281  N N   . LYS A 1 41  ? 4.030   13.521  -42.066 1.00 27.86 ? 53  LYS B N   1 
ATOM   282  C CA  . LYS A 1 41  ? 2.658   13.037  -42.088 1.00 26.31 ? 53  LYS B CA  1 
ATOM   283  C C   . LYS A 1 41  ? 2.539   12.021  -43.198 1.00 25.60 ? 53  LYS B C   1 
ATOM   284  O O   . LYS A 1 41  ? 3.355   12.028  -44.139 1.00 27.22 ? 53  LYS B O   1 
ATOM   285  C CB  . LYS A 1 41  ? 1.678   14.201  -42.294 1.00 24.41 ? 53  LYS B CB  1 
ATOM   286  C CG  . LYS A 1 41  ? 1.314   14.405  -43.753 1.00 30.27 ? 53  LYS B CG  1 
ATOM   287  C CD  . LYS A 1 41  ? 0.360   15.564  -44.002 1.00 34.83 ? 53  LYS B CD  1 
ATOM   288  C CE  . LYS A 1 41  ? 1.115   16.880  -44.179 1.00 35.90 ? 53  LYS B CE  1 
ATOM   289  N NZ  . LYS A 1 41  ? 0.171   18.047  -44.218 1.00 46.43 ? 53  LYS B NZ  1 
ATOM   290  N N   . PRO A 1 42  ? 1.563   11.105  -43.155 1.00 23.66 ? 54  PRO B N   1 
ATOM   291  C CA  . PRO A 1 42  ? 1.434   10.090  -44.205 1.00 24.94 ? 54  PRO B CA  1 
ATOM   292  C C   . PRO A 1 42  ? 1.234   10.705  -45.586 1.00 26.90 ? 54  PRO B C   1 
ATOM   293  O O   . PRO A 1 42  ? 0.735   11.823  -45.724 1.00 27.25 ? 54  PRO B O   1 
ATOM   294  C CB  . PRO A 1 42  ? 0.205   9.284   -43.772 1.00 24.51 ? 54  PRO B CB  1 
ATOM   295  C CG  . PRO A 1 42  ? 0.200   9.432   -42.293 1.00 21.22 ? 54  PRO B CG  1 
ATOM   296  C CD  . PRO A 1 42  ? 0.588   10.865  -42.069 1.00 21.97 ? 54  PRO B CD  1 
ATOM   297  N N   . SER A 1 43  ? 1.646   9.961   -46.616 1.00 30.93 ? 55  SER B N   1 
ATOM   298  C CA  . SER A 1 43  ? 1.568   10.430  -48.001 1.00 27.65 ? 55  SER B CA  1 
ATOM   299  C C   . SER A 1 43  ? 1.435   9.260   -48.971 1.00 29.69 ? 55  SER B C   1 
ATOM   300  O O   . SER A 1 43  ? 0.594   8.386   -48.760 1.00 32.35 ? 55  SER B O   1 
ATOM   301  C CB  . SER A 1 43  ? 2.792   11.280  -48.354 1.00 30.41 ? 55  SER B CB  1 
ATOM   302  O OG  . SER A 1 43  ? 2.623   11.969  -49.581 1.00 29.82 ? 55  SER B OG  1 
ATOM   303  N N   . THR A 1 44  ? 2.243   9.222   -50.032 1.00 31.02 ? 56  THR B N   1 
ATOM   304  C CA  . THR A 1 44  ? 1.951   8.322   -51.147 1.00 29.42 ? 56  THR B CA  1 
ATOM   305  C C   . THR A 1 44  ? 2.274   6.875   -50.792 1.00 29.10 ? 56  THR B C   1 
ATOM   306  O O   . THR A 1 44  ? 3.273   6.589   -50.127 1.00 30.78 ? 56  THR B O   1 
ATOM   307  C CB  . THR A 1 44  ? 2.732   8.742   -52.397 1.00 29.13 ? 56  THR B CB  1 
ATOM   308  O OG1 . THR A 1 44  ? 2.580   10.148  -52.620 1.00 28.27 ? 56  THR B OG1 1 
ATOM   309  C CG2 . THR A 1 44  ? 2.217   8.012   -53.608 1.00 29.47 ? 56  THR B CG2 1 
ATOM   310  N N   . VAL A 1 45  ? 1.422   5.961   -51.251 1.00 29.41 ? 57  VAL B N   1 
ATOM   311  C CA  . VAL A 1 45  ? 1.563   4.525   -51.028 1.00 27.35 ? 57  VAL B CA  1 
ATOM   312  C C   . VAL A 1 45  ? 2.036   3.874   -52.323 1.00 27.84 ? 57  VAL B C   1 
ATOM   313  O O   . VAL A 1 45  ? 1.499   4.155   -53.403 1.00 28.02 ? 57  VAL B O   1 
ATOM   314  C CB  . VAL A 1 45  ? 0.229   3.900   -50.568 1.00 26.49 ? 57  VAL B CB  1 
ATOM   315  C CG1 . VAL A 1 45  ? 0.360   2.397   -50.391 1.00 25.82 ? 57  VAL B CG1 1 
ATOM   316  C CG2 . VAL A 1 45  ? -0.259  4.564   -49.300 1.00 23.54 ? 57  VAL B CG2 1 
ATOM   317  N N   . HIS A 1 46  ? 3.035   2.995   -52.209 1.00 30.86 ? 58  HIS B N   1 
ATOM   318  C CA  . HIS A 1 46  ? 3.552   2.191   -53.313 1.00 27.50 ? 58  HIS B CA  1 
ATOM   319  C C   . HIS A 1 46  ? 3.425   0.715   -52.971 1.00 30.57 ? 58  HIS B C   1 
ATOM   320  O O   . HIS A 1 46  ? 3.695   0.311   -51.836 1.00 34.57 ? 58  HIS B O   1 
ATOM   321  C CB  . HIS A 1 46  ? 5.021   2.503   -53.582 1.00 26.00 ? 58  HIS B CB  1 
ATOM   322  C CG  . HIS A 1 46  ? 5.306   3.958   -53.776 1.00 27.78 ? 58  HIS B CG  1 
ATOM   323  N ND1 . HIS A 1 46  ? 4.986   4.636   -54.933 1.00 29.81 ? 58  HIS B ND1 1 
ATOM   324  C CD2 . HIS A 1 46  ? 5.861   4.872   -52.947 1.00 26.68 ? 58  HIS B CD2 1 
ATOM   325  C CE1 . HIS A 1 46  ? 5.351   5.900   -54.813 1.00 29.58 ? 58  HIS B CE1 1 
ATOM   326  N NE2 . HIS A 1 46  ? 5.884   6.069   -53.617 1.00 27.04 ? 58  HIS B NE2 1 
ATOM   327  N N   . ILE A 1 47  ? 3.042   -0.103  -53.950 1.00 32.39 ? 59  ILE B N   1 
ATOM   328  C CA  . ILE A 1 47  ? 2.804   -1.518  -53.702 1.00 31.08 ? 59  ILE B CA  1 
ATOM   329  C C   . ILE A 1 47  ? 3.756   -2.420  -54.475 1.00 30.20 ? 59  ILE B C   1 
ATOM   330  O O   . ILE A 1 47  ? 3.712   -3.648  -54.303 1.00 30.76 ? 59  ILE B O   1 
ATOM   331  C CB  . ILE A 1 47  ? 1.334   -1.886  -53.989 1.00 25.19 ? 59  ILE B CB  1 
ATOM   332  C CG1 . ILE A 1 47  ? 0.971   -1.625  -55.438 1.00 28.37 ? 59  ILE B CG1 1 
ATOM   333  C CG2 . ILE A 1 47  ? 0.436   -1.019  -53.178 1.00 21.21 ? 59  ILE B CG2 1 
ATOM   334  C CD1 . ILE A 1 47  ? -0.162  -2.494  -55.916 1.00 27.64 ? 59  ILE B CD1 1 
ATOM   335  N N   . ALA A 1 48  ? 4.633   -1.855  -55.297 1.00 26.26 ? 60  ALA B N   1 
ATOM   336  C CA  . ALA A 1 48  ? 5.628   -2.657  -55.985 1.00 30.74 ? 60  ALA B CA  1 
ATOM   337  C C   . ALA A 1 48  ? 6.838   -1.782  -56.261 1.00 29.33 ? 60  ALA B C   1 
ATOM   338  O O   . ALA A 1 48  ? 6.737   -0.555  -56.288 1.00 30.35 ? 60  ALA B O   1 
ATOM   339  C CB  . ALA A 1 48  ? 5.071   -3.247  -57.283 1.00 30.45 ? 60  ALA B CB  1 
ATOM   340  N N   . CYS A 1 49  ? 7.990   -2.418  -56.482 1.00 28.01 ? 61  CYS B N   1 
ATOM   341  C CA  . CYS A 1 49  ? 9.224   -1.648  -56.620 1.00 30.90 ? 61  CYS B CA  1 
ATOM   342  C C   . CYS A 1 49  ? 9.259   -0.770  -57.870 1.00 30.21 ? 61  CYS B C   1 
ATOM   343  O O   . CYS A 1 49  ? 10.132  -0.914  -58.736 1.00 26.86 ? 61  CYS B O   1 
ATOM   344  C CB  . CYS A 1 49  ? 10.447  -2.560  -56.598 1.00 25.88 ? 61  CYS B CB  1 
ATOM   345  S SG  . CYS A 1 49  ? 11.759  -1.765  -55.649 1.00 36.75 ? 61  CYS B SG  1 
ATOM   346  N N   . THR A 1 50  ? 8.324   0.168   -57.941 1.00 28.29 ? 62  THR B N   1 
ATOM   347  C CA  . THR A 1 50  ? 8.320   1.177   -58.977 1.00 29.84 ? 62  THR B CA  1 
ATOM   348  C C   . THR A 1 50  ? 9.446   2.183   -58.723 1.00 30.58 ? 62  THR B C   1 
ATOM   349  O O   . THR A 1 50  ? 9.929   2.307   -57.596 1.00 29.93 ? 62  THR B O   1 
ATOM   350  C CB  . THR A 1 50  ? 6.970   1.879   -58.993 1.00 30.03 ? 62  THR B CB  1 
ATOM   351  O OG1 . THR A 1 50  ? 6.820   2.641   -57.793 1.00 34.60 ? 62  THR B OG1 1 
ATOM   352  C CG2 . THR A 1 50  ? 5.860   0.839   -59.050 1.00 26.56 ? 62  THR B CG2 1 
ATOM   353  N N   . PRO A 1 51  ? 9.891   2.909   -59.756 1.00 27.79 ? 63  PRO B N   1 
ATOM   354  C CA  . PRO A 1 51  ? 11.045  3.793   -59.551 1.00 25.42 ? 63  PRO B CA  1 
ATOM   355  C C   . PRO A 1 51  ? 10.788  4.842   -58.498 1.00 29.04 ? 63  PRO B C   1 
ATOM   356  O O   . PRO A 1 51  ? 11.699  5.179   -57.728 1.00 28.62 ? 63  PRO B O   1 
ATOM   357  C CB  . PRO A 1 51  ? 11.259  4.408   -60.939 1.00 26.76 ? 63  PRO B CB  1 
ATOM   358  C CG  . PRO A 1 51  ? 10.611  3.474   -61.868 1.00 25.35 ? 63  PRO B CG  1 
ATOM   359  C CD  . PRO A 1 51  ? 9.403   2.995   -61.142 1.00 28.27 ? 63  PRO B CD  1 
ATOM   360  N N   . GLN A 1 52  ? 9.555   5.355   -58.433 1.00 30.67 ? 64  GLN B N   1 
ATOM   361  C CA  . GLN A 1 52  ? 9.201   6.253   -57.341 1.00 30.18 ? 64  GLN B CA  1 
ATOM   362  C C   . GLN A 1 52  ? 9.294   5.546   -56.001 1.00 26.70 ? 64  GLN B C   1 
ATOM   363  O O   . GLN A 1 52  ? 9.848   6.093   -55.040 1.00 29.21 ? 64  GLN B O   1 
ATOM   364  C CB  . GLN A 1 52  ? 7.801   6.824   -57.548 1.00 31.66 ? 64  GLN B CB  1 
ATOM   365  C CG  . GLN A 1 52  ? 7.710   8.314   -57.238 1.00 40.86 ? 64  GLN B CG  1 
ATOM   366  C CD  . GLN A 1 52  ? 8.717   9.170   -58.032 1.00 52.16 ? 64  GLN B CD  1 
ATOM   367  O OE1 . GLN A 1 52  ? 9.282   8.728   -59.045 1.00 54.22 ? 64  GLN B OE1 1 
ATOM   368  N NE2 . GLN A 1 52  ? 8.952   10.400  -57.559 1.00 47.91 ? 64  GLN B NE2 1 
ATOM   369  N N   . ALA A 1 53  ? 8.760   4.327   -55.916 1.00 26.80 ? 65  ALA B N   1 
ATOM   370  C CA  . ALA A 1 53  ? 8.890   3.550   -54.686 1.00 26.70 ? 65  ALA B CA  1 
ATOM   371  C C   . ALA A 1 53  ? 10.351  3.384   -54.298 1.00 28.13 ? 65  ALA B C   1 
ATOM   372  O O   . ALA A 1 53  ? 10.694  3.433   -53.115 1.00 26.44 ? 65  ALA B O   1 
ATOM   373  C CB  . ALA A 1 53  ? 8.231   2.185   -54.852 1.00 25.20 ? 65  ALA B CB  1 
ATOM   374  N N   . ALA A 1 54  ? 11.225  3.190   -55.290 1.00 28.53 ? 66  ALA B N   1 
ATOM   375  C CA  . ALA A 1 54  ? 12.653  3.064   -55.029 1.00 26.50 ? 66  ALA B CA  1 
ATOM   376  C C   . ALA A 1 54  ? 13.235  4.391   -54.577 1.00 30.09 ? 66  ALA B C   1 
ATOM   377  O O   . ALA A 1 54  ? 14.093  4.420   -53.686 1.00 29.65 ? 66  ALA B O   1 
ATOM   378  C CB  . ALA A 1 54  ? 13.372  2.561   -56.283 1.00 27.09 ? 66  ALA B CB  1 
ATOM   379  N N   . LYS A 1 55  ? 12.776  5.499   -55.178 1.00 28.24 ? 67  LYS B N   1 
ATOM   380  C CA  . LYS A 1 55  ? 13.188  6.823   -54.717 1.00 25.81 ? 67  LYS B CA  1 
ATOM   381  C C   . LYS A 1 55  ? 12.844  7.020   -53.245 1.00 30.80 ? 67  LYS B C   1 
ATOM   382  O O   . LYS A 1 55  ? 13.668  7.526   -52.479 1.00 34.19 ? 67  LYS B O   1 
ATOM   383  C CB  . LYS A 1 55  ? 12.544  7.918   -55.582 1.00 31.24 ? 67  LYS B CB  1 
ATOM   384  C CG  . LYS A 1 55  ? 13.299  9.268   -55.573 1.00 34.49 ? 67  LYS B CG  1 
ATOM   385  C CD  . LYS A 1 55  ? 14.824  9.011   -55.529 1.00 43.90 ? 67  LYS B CD  1 
ATOM   386  C CE  . LYS A 1 55  ? 15.682  10.269  -55.287 1.00 46.84 ? 67  LYS B CE  1 
ATOM   387  N NZ  . LYS A 1 55  ? 17.075  9.941   -54.777 1.00 41.18 ? 67  LYS B NZ  1 
ATOM   388  N N   . ALA A 1 56  ? 11.648  6.586   -52.819 1.00 31.18 ? 68  ALA B N   1 
ATOM   389  C CA  . ALA A 1 56  ? 11.228  6.776   -51.429 1.00 28.59 ? 68  ALA B CA  1 
ATOM   390  C C   . ALA A 1 56  ? 12.190  6.128   -50.434 1.00 25.85 ? 68  ALA B C   1 
ATOM   391  O O   . ALA A 1 56  ? 12.312  6.600   -49.298 1.00 30.52 ? 68  ALA B O   1 
ATOM   392  C CB  . ALA A 1 56  ? 9.811   6.231   -51.213 1.00 24.58 ? 68  ALA B CB  1 
ATOM   393  N N   . ILE A 1 57  ? 12.887  5.065   -50.824 1.00 25.61 ? 69  ILE B N   1 
ATOM   394  C CA  . ILE A 1 57  ? 13.735  4.356   -49.864 1.00 29.04 ? 69  ILE B CA  1 
ATOM   395  C C   . ILE A 1 57  ? 15.196  4.801   -49.955 1.00 26.74 ? 69  ILE B C   1 
ATOM   396  O O   . ILE A 1 57  ? 15.872  4.946   -48.931 1.00 24.11 ? 69  ILE B O   1 
ATOM   397  C CB  . ILE A 1 57  ? 13.598  2.820   -50.032 1.00 25.78 ? 69  ILE B CB  1 
ATOM   398  C CG1 . ILE A 1 57  ? 12.154  2.358   -49.857 1.00 22.84 ? 69  ILE B CG1 1 
ATOM   399  C CG2 . ILE A 1 57  ? 14.459  2.086   -49.039 1.00 22.59 ? 69  ILE B CG2 1 
ATOM   400  C CD1 . ILE A 1 57  ? 11.936  0.993   -50.381 1.00 24.24 ? 69  ILE B CD1 1 
ATOM   401  N N   . SER A 1 58  ? 15.717  5.025   -51.161 1.00 26.34 ? 70  SER B N   1 
ATOM   402  C CA  . SER A 1 58  ? 17.138  5.321   -51.276 1.00 30.04 ? 70  SER B CA  1 
ATOM   403  C C   . SER A 1 58  ? 17.431  6.802   -51.074 1.00 29.34 ? 70  SER B C   1 
ATOM   404  O O   . SER A 1 58  ? 18.557  7.172   -50.716 1.00 28.55 ? 70  SER B O   1 
ATOM   405  C CB  . SER A 1 58  ? 17.653  4.864   -52.636 1.00 27.55 ? 70  SER B CB  1 
ATOM   406  O OG  . SER A 1 58  ? 16.888  5.478   -53.636 1.00 31.84 ? 70  SER B OG  1 
ATOM   407  N N   . ASN A 1 59  ? 16.448  7.659   -51.303 1.00 26.65 ? 71  ASN B N   1 
ATOM   408  C CA  . ASN A 1 59  ? 16.638  9.080   -51.067 1.00 30.36 ? 71  ASN B CA  1 
ATOM   409  C C   . ASN A 1 59  ? 16.677  9.331   -49.567 1.00 33.76 ? 71  ASN B C   1 
ATOM   410  O O   . ASN A 1 59  ? 15.679  9.132   -48.861 1.00 35.31 ? 71  ASN B O   1 
ATOM   411  C CB  . ASN A 1 59  ? 15.533  9.883   -51.738 1.00 33.30 ? 71  ASN B CB  1 
ATOM   412  C CG  . ASN A 1 59  ? 15.672  11.361  -51.507 1.00 34.33 ? 71  ASN B CG  1 
ATOM   413  O OD1 . ASN A 1 59  ? 16.701  11.841  -51.017 1.00 33.99 ? 71  ASN B OD1 1 
ATOM   414  N ND2 . ASN A 1 59  ? 14.637  12.102  -51.869 1.00 34.01 ? 71  ASN B ND2 1 
ATOM   415  N N   . LYS A 1 60  ? 17.836  9.761   -49.076 1.00 32.03 ? 72  LYS B N   1 
ATOM   416  C CA  . LYS A 1 60  ? 17.990  9.970   -47.647 1.00 32.45 ? 72  LYS B CA  1 
ATOM   417  C C   . LYS A 1 60  ? 17.387  11.299  -47.191 1.00 38.10 ? 72  LYS B C   1 
ATOM   418  O O   . LYS A 1 60  ? 17.489  11.645  -46.005 1.00 35.55 ? 72  LYS B O   1 
ATOM   419  C CB  . LYS A 1 60  ? 19.466  9.852   -47.284 1.00 26.91 ? 72  LYS B CB  1 
ATOM   420  C CG  . LYS A 1 60  ? 19.897  8.416   -47.024 1.00 31.36 ? 72  LYS B CG  1 
ATOM   421  C CD  . LYS A 1 60  ? 21.258  8.118   -47.657 1.00 40.06 ? 72  LYS B CD  1 
ATOM   422  C CE  . LYS A 1 60  ? 21.256  6.788   -48.427 1.00 40.70 ? 72  LYS B CE  1 
ATOM   423  N NZ  . LYS A 1 60  ? 22.648  6.280   -48.668 1.00 41.92 ? 72  LYS B NZ  1 
ATOM   424  N N   . ASP A 1 61  ? 16.719  12.018  -48.098 1.00 36.85 ? 73  ASP B N   1 
ATOM   425  C CA  . ASP A 1 61  ? 16.006  13.252  -47.797 1.00 38.98 ? 73  ASP B CA  1 
ATOM   426  C C   . ASP A 1 61  ? 14.497  13.063  -47.758 1.00 36.97 ? 73  ASP B C   1 
ATOM   427  O O   . ASP A 1 61  ? 13.765  14.057  -47.720 1.00 39.16 ? 73  ASP B O   1 
ATOM   428  C CB  . ASP A 1 61  ? 16.345  14.322  -48.838 1.00 44.20 ? 73  ASP B CB  1 
ATOM   429  C CG  . ASP A 1 61  ? 17.672  15.013  -48.567 1.00 51.37 ? 73  ASP B CG  1 
ATOM   430  O OD1 . ASP A 1 61  ? 18.165  14.973  -47.411 1.00 55.69 ? 73  ASP B OD1 1 
ATOM   431  O OD2 . ASP A 1 61  ? 18.231  15.590  -49.527 1.00 50.15 ? 73  ASP B OD2 1 
ATOM   432  N N   . GLN A 1 62  ? 14.021  11.819  -47.813 1.00 33.97 ? 74  GLN B N   1 
ATOM   433  C CA  . GLN A 1 62  ? 12.600  11.487  -47.855 1.00 32.87 ? 74  GLN B CA  1 
ATOM   434  C C   . GLN A 1 62  ? 12.362  10.454  -46.774 1.00 33.56 ? 74  GLN B C   1 
ATOM   435  O O   . GLN A 1 62  ? 13.047  9.427   -46.751 1.00 35.66 ? 74  GLN B O   1 
ATOM   436  C CB  . GLN A 1 62  ? 12.201  10.903  -49.215 1.00 34.12 ? 74  GLN B CB  1 
ATOM   437  C CG  . GLN A 1 62  ? 11.011  11.532  -49.925 1.00 34.76 ? 74  GLN B CG  1 
ATOM   438  C CD  . GLN A 1 62  ? 10.954  11.071  -51.398 1.00 42.41 ? 74  GLN B CD  1 
ATOM   439  O OE1 . GLN A 1 62  ? 11.809  11.436  -52.216 1.00 40.57 ? 74  GLN B OE1 1 
ATOM   440  N NE2 . GLN A 1 62  ? 9.942   10.280  -51.737 1.00 42.44 ? 74  GLN B NE2 1 
ATOM   441  N N   . HIS A 1 63  ? 11.411  10.719  -45.883 1.00 28.83 ? 75  HIS B N   1 
ATOM   442  C CA  . HIS A 1 63  ? 10.983  9.687   -44.957 1.00 24.22 ? 75  HIS B CA  1 
ATOM   443  C C   . HIS A 1 63  ? 10.163  8.642   -45.689 1.00 27.59 ? 75  HIS B C   1 
ATOM   444  O O   . HIS A 1 63  ? 9.491   8.934   -46.679 1.00 29.62 ? 75  HIS B O   1 
ATOM   445  C CB  . HIS A 1 63  ? 10.162  10.285  -43.841 1.00 27.79 ? 75  HIS B CB  1 
ATOM   446  C CG  . HIS A 1 63  ? 10.900  11.313  -43.057 1.00 27.19 ? 75  HIS B CG  1 
ATOM   447  N ND1 . HIS A 1 63  ? 11.238  12.539  -43.586 1.00 28.07 ? 75  HIS B ND1 1 
ATOM   448  C CD2 . HIS A 1 63  ? 11.359  11.308  -41.784 1.00 24.82 ? 75  HIS B CD2 1 
ATOM   449  C CE1 . HIS A 1 63  ? 11.877  13.247  -42.672 1.00 29.54 ? 75  HIS B CE1 1 
ATOM   450  N NE2 . HIS A 1 63  ? 11.961  12.524  -41.569 1.00 26.75 ? 75  HIS B NE2 1 
ATOM   451  N N   . SER A 1 64  ? 10.230  7.408   -45.202 1.00 25.88 ? 76  SER B N   1 
ATOM   452  C CA  . SER A 1 64  ? 9.397   6.355   -45.761 1.00 24.24 ? 76  SER B CA  1 
ATOM   453  C C   . SER A 1 64  ? 9.308   5.212   -44.761 1.00 25.86 ? 76  SER B C   1 
ATOM   454  O O   . SER A 1 64  ? 10.170  5.059   -43.888 1.00 24.97 ? 76  SER B O   1 
ATOM   455  C CB  . SER A 1 64  ? 9.946   5.873   -47.107 1.00 23.67 ? 76  SER B CB  1 
ATOM   456  O OG  . SER A 1 64  ? 10.680  4.669   -46.949 1.00 28.82 ? 76  SER B OG  1 
ATOM   457  N N   . ILE A 1 65  ? 8.247   4.411   -44.905 1.00 24.53 ? 77  ILE B N   1 
ATOM   458  C CA  . ILE A 1 65  ? 7.994   3.240   -44.068 1.00 21.54 ? 77  ILE B CA  1 
ATOM   459  C C   . ILE A 1 65  ? 7.708   2.038   -44.959 1.00 25.09 ? 77  ILE B C   1 
ATOM   460  O O   . ILE A 1 65  ? 6.845   2.110   -45.841 1.00 24.13 ? 77  ILE B O   1 
ATOM   461  C CB  . ILE A 1 65  ? 6.813   3.476   -43.120 1.00 21.85 ? 77  ILE B CB  1 
ATOM   462  C CG1 . ILE A 1 65  ? 7.037   4.740   -42.309 1.00 21.10 ? 77  ILE B CG1 1 
ATOM   463  C CG2 . ILE A 1 65  ? 6.636   2.292   -42.228 1.00 23.38 ? 77  ILE B CG2 1 
ATOM   464  C CD1 . ILE A 1 65  ? 6.162   4.815   -41.114 1.00 24.14 ? 77  ILE B CD1 1 
ATOM   465  N N   . SER A 1 66  ? 8.408   0.929   -44.715 1.00 26.98 ? 78  SER B N   1 
ATOM   466  C CA  . SER A 1 66  ? 8.357   -0.248  -45.579 1.00 25.43 ? 78  SER B CA  1 
ATOM   467  C C   . SER A 1 66  ? 7.697   -1.406  -44.838 1.00 28.85 ? 78  SER B C   1 
ATOM   468  O O   . SER A 1 66  ? 8.235   -1.893  -43.838 1.00 29.98 ? 78  SER B O   1 
ATOM   469  C CB  . SER A 1 66  ? 9.762   -0.643  -46.034 1.00 23.35 ? 78  SER B CB  1 
ATOM   470  O OG  . SER A 1 66  ? 10.526  0.505   -46.356 1.00 24.79 ? 78  SER B OG  1 
ATOM   471  N N   . TYR A 1 67  ? 6.546   -1.863  -45.345 1.00 29.46 ? 79  TYR B N   1 
ATOM   472  C CA  . TYR A 1 67  ? 5.769   -2.942  -44.739 1.00 27.13 ? 79  TYR B CA  1 
ATOM   473  C C   . TYR A 1 67  ? 5.992   -4.224  -45.533 1.00 29.49 ? 79  TYR B C   1 
ATOM   474  O O   . TYR A 1 67  ? 5.469   -4.359  -46.644 1.00 29.80 ? 79  TYR B O   1 
ATOM   475  C CB  . TYR A 1 67  ? 4.286   -2.581  -44.722 1.00 26.26 ? 79  TYR B CB  1 
ATOM   476  C CG  . TYR A 1 67  ? 3.923   -1.426  -43.815 1.00 27.86 ? 79  TYR B CG  1 
ATOM   477  C CD1 . TYR A 1 67  ? 4.048   -0.113  -44.249 1.00 26.16 ? 79  TYR B CD1 1 
ATOM   478  C CD2 . TYR A 1 67  ? 3.428   -1.651  -42.532 1.00 26.77 ? 79  TYR B CD2 1 
ATOM   479  C CE1 . TYR A 1 67  ? 3.717   0.933   -43.431 1.00 25.94 ? 79  TYR B CE1 1 
ATOM   480  C CE2 . TYR A 1 67  ? 3.085   -0.606  -41.703 1.00 25.41 ? 79  TYR B CE2 1 
ATOM   481  C CZ  . TYR A 1 67  ? 3.239   0.685   -42.156 1.00 28.15 ? 79  TYR B CZ  1 
ATOM   482  O OH  . TYR A 1 67  ? 2.912   1.748   -41.349 1.00 29.03 ? 79  TYR B OH  1 
ATOM   483  N N   . THR A 1 68  ? 6.732   -5.175  -44.950 1.00 29.57 ? 80  THR B N   1 
ATOM   484  C CA  . THR A 1 68  ? 7.098   -6.433  -45.613 1.00 27.40 ? 80  THR B CA  1 
ATOM   485  C C   . THR A 1 68  ? 5.958   -7.439  -45.468 1.00 26.59 ? 80  THR B C   1 
ATOM   486  O O   . THR A 1 68  ? 5.943   -8.279  -44.565 1.00 30.13 ? 80  THR B O   1 
ATOM   487  C CB  . THR A 1 68  ? 8.397   -6.989  -45.035 1.00 27.30 ? 80  THR B CB  1 
ATOM   488  O OG1 . THR A 1 68  ? 9.429   -5.997  -45.103 1.00 27.25 ? 80  THR B OG1 1 
ATOM   489  C CG2 . THR A 1 68  ? 8.833   -8.253  -45.775 1.00 29.59 ? 80  THR B CG2 1 
ATOM   490  N N   . LEU A 1 69  ? 4.997   -7.376  -46.390 1.00 24.73 ? 81  LEU B N   1 
ATOM   491  C CA  . LEU A 1 69  ? 3.874   -8.309  -46.358 1.00 25.62 ? 81  LEU B CA  1 
ATOM   492  C C   . LEU A 1 69  ? 4.303   -9.729  -46.673 1.00 26.93 ? 81  LEU B C   1 
ATOM   493  O O   . LEU A 1 69  ? 3.748   -10.687 -46.121 1.00 29.17 ? 81  LEU B O   1 
ATOM   494  C CB  . LEU A 1 69  ? 2.813   -7.911  -47.369 1.00 30.16 ? 81  LEU B CB  1 
ATOM   495  C CG  . LEU A 1 69  ? 1.750   -6.896  -47.023 1.00 31.03 ? 81  LEU B CG  1 
ATOM   496  C CD1 . LEU A 1 69  ? 1.130   -6.412  -48.334 1.00 30.32 ? 81  LEU B CD1 1 
ATOM   497  C CD2 . LEU A 1 69  ? 0.730   -7.550  -46.117 1.00 30.40 ? 81  LEU B CD2 1 
ATOM   498  N N   . SER A 1 70  ? 5.243   -9.886  -47.600 1.00 29.69 ? 82  SER B N   1 
ATOM   499  C CA  . SER A 1 70  ? 5.530   -11.198 -48.158 1.00 30.99 ? 82  SER B CA  1 
ATOM   500  C C   . SER A 1 70  ? 6.928   -11.202 -48.757 1.00 31.16 ? 82  SER B C   1 
ATOM   501  O O   . SER A 1 70  ? 7.584   -10.159 -48.874 1.00 30.81 ? 82  SER B O   1 
ATOM   502  C CB  . SER A 1 70  ? 4.509   -11.575 -49.223 1.00 29.85 ? 82  SER B CB  1 
ATOM   503  O OG  . SER A 1 70  ? 5.069   -11.326 -50.500 1.00 33.63 ? 82  SER B OG  1 
ATOM   504  N N   . ARG A 1 71  ? 7.377   -12.404 -49.144 1.00 31.54 ? 83  ARG B N   1 
ATOM   505  C CA  . ARG A 1 71  ? 8.664   -12.491 -49.818 1.00 34.14 ? 83  ARG B CA  1 
ATOM   506  C C   . ARG A 1 71  ? 8.618   -11.722 -51.131 1.00 30.72 ? 83  ARG B C   1 
ATOM   507  O O   . ARG A 1 71  ? 9.637   -11.174 -51.561 1.00 30.87 ? 83  ARG B O   1 
ATOM   508  C CB  . ARG A 1 71  ? 9.069   -13.959 -50.038 1.00 31.30 ? 83  ARG B CB  1 
ATOM   509  C CG  . ARG A 1 71  ? 8.043   -14.808 -50.786 1.00 30.56 ? 83  ARG B CG  1 
ATOM   510  C CD  . ARG A 1 71  ? 8.517   -16.243 -51.095 1.00 29.23 ? 83  ARG B CD  1 
ATOM   511  N NE  . ARG A 1 71  ? 8.021   -16.696 -52.400 1.00 40.10 ? 83  ARG B NE  1 
ATOM   512  C CZ  . ARG A 1 71  ? 8.687   -16.580 -53.552 1.00 41.40 ? 83  ARG B CZ  1 
ATOM   513  N NH1 . ARG A 1 71  ? 9.933   -16.120 -53.595 1.00 34.30 ? 83  ARG B NH1 1 
ATOM   514  N NH2 . ARG A 1 71  ? 8.086   -16.921 -54.694 1.00 32.06 ? 83  ARG B NH2 1 
ATOM   515  N N   . ALA A 1 72  ? 7.431   -11.597 -51.736 1.00 29.63 ? 84  ALA B N   1 
ATOM   516  C CA  . ALA A 1 72  ? 7.281   -10.956 -53.039 1.00 29.59 ? 84  ALA B CA  1 
ATOM   517  C C   . ALA A 1 72  ? 6.795   -9.512  -52.974 1.00 31.19 ? 84  ALA B C   1 
ATOM   518  O O   . ALA A 1 72  ? 6.740   -8.852  -54.024 1.00 29.69 ? 84  ALA B O   1 
ATOM   519  C CB  . ALA A 1 72  ? 6.320   -11.760 -53.925 1.00 28.88 ? 84  ALA B CB  1 
ATOM   520  N N   . GLN A 1 73  ? 6.457   -8.999  -51.789 1.00 32.18 ? 85  GLN B N   1 
ATOM   521  C CA  . GLN A 1 73  ? 5.885   -7.665  -51.680 1.00 31.45 ? 85  GLN B CA  1 
ATOM   522  C C   . GLN A 1 73  ? 6.354   -6.975  -50.414 1.00 28.61 ? 85  GLN B C   1 
ATOM   523  O O   . GLN A 1 73  ? 6.266   -7.553  -49.330 1.00 27.80 ? 85  GLN B O   1 
ATOM   524  C CB  . GLN A 1 73  ? 4.357   -7.713  -51.678 1.00 28.43 ? 85  GLN B CB  1 
ATOM   525  C CG  . GLN A 1 73  ? 3.765   -6.338  -51.521 1.00 28.38 ? 85  GLN B CG  1 
ATOM   526  C CD  . GLN A 1 73  ? 2.401   -6.228  -52.134 1.00 28.78 ? 85  GLN B CD  1 
ATOM   527  O OE1 . GLN A 1 73  ? 1.504   -7.019  -51.823 1.00 30.30 ? 85  GLN B OE1 1 
ATOM   528  N NE2 . GLN A 1 73  ? 2.233   -5.256  -53.035 1.00 21.24 ? 85  GLN B NE2 1 
ATOM   529  N N   . THR A 1 74  ? 6.857   -5.746  -50.558 1.00 27.66 ? 86  THR B N   1 
ATOM   530  C CA  . THR A 1 74  ? 6.955   -4.814  -49.447 1.00 27.35 ? 86  THR B CA  1 
ATOM   531  C C   . THR A 1 74  ? 6.339   -3.498  -49.893 1.00 25.98 ? 86  THR B C   1 
ATOM   532  O O   . THR A 1 74  ? 6.551   -3.063  -51.025 1.00 27.17 ? 86  THR B O   1 
ATOM   533  C CB  . THR A 1 74  ? 8.417   -4.573  -48.935 1.00 28.29 ? 86  THR B CB  1 
ATOM   534  O OG1 . THR A 1 74  ? 8.898   -3.325  -49.429 1.00 28.56 ? 86  THR B OG1 1 
ATOM   535  C CG2 . THR A 1 74  ? 9.394   -5.712  -49.284 1.00 21.92 ? 86  THR B CG2 1 
ATOM   536  N N   . VAL A 1 75  ? 5.567   -2.870  -49.005 1.00 31.23 ? 87  VAL B N   1 
ATOM   537  C CA  . VAL A 1 75  ? 4.784   -1.677  -49.331 1.00 29.51 ? 87  VAL B CA  1 
ATOM   538  C C   . VAL A 1 75  ? 5.464   -0.447  -48.751 1.00 26.97 ? 87  VAL B C   1 
ATOM   539  O O   . VAL A 1 75  ? 5.698   -0.374  -47.538 1.00 27.44 ? 87  VAL B O   1 
ATOM   540  C CB  . VAL A 1 75  ? 3.352   -1.779  -48.784 1.00 29.11 ? 87  VAL B CB  1 
ATOM   541  C CG1 . VAL A 1 75  ? 2.678   -0.418  -48.842 1.00 26.10 ? 87  VAL B CG1 1 
ATOM   542  C CG2 . VAL A 1 75  ? 2.561   -2.830  -49.535 1.00 31.23 ? 87  VAL B CG2 1 
ATOM   543  N N   . VAL A 1 76  ? 5.711   0.549   -49.594 1.00 25.48 ? 88  VAL B N   1 
ATOM   544  C CA  . VAL A 1 76  ? 6.466   1.732   -49.205 1.00 25.92 ? 88  VAL B CA  1 
ATOM   545  C C   . VAL A 1 76  ? 5.505   2.918   -49.109 1.00 29.52 ? 88  VAL B C   1 
ATOM   546  O O   . VAL A 1 76  ? 5.043   3.455   -50.127 1.00 26.29 ? 88  VAL B O   1 
ATOM   547  C CB  . VAL A 1 76  ? 7.630   1.990   -50.169 1.00 19.89 ? 88  VAL B CB  1 
ATOM   548  C CG1 . VAL A 1 76  ? 8.436   3.185   -49.735 1.00 24.31 ? 88  VAL B CG1 1 
ATOM   549  C CG2 . VAL A 1 76  ? 8.518   0.776   -50.173 1.00 22.50 ? 88  VAL B CG2 1 
ATOM   550  N N   . VAL A 1 77  ? 5.211   3.314   -47.864 1.00 26.72 ? 89  VAL B N   1 
ATOM   551  C CA  . VAL A 1 77  ? 4.386   4.472   -47.536 1.00 23.32 ? 89  VAL B CA  1 
ATOM   552  C C   . VAL A 1 77  ? 5.309   5.660   -47.297 1.00 24.94 ? 89  VAL B C   1 
ATOM   553  O O   . VAL A 1 77  ? 6.138   5.641   -46.374 1.00 25.56 ? 89  VAL B O   1 
ATOM   554  C CB  . VAL A 1 77  ? 3.526   4.206   -46.289 1.00 23.38 ? 89  VAL B CB  1 
ATOM   555  C CG1 . VAL A 1 77  ? 2.638   5.408   -45.955 1.00 22.00 ? 89  VAL B CG1 1 
ATOM   556  C CG2 . VAL A 1 77  ? 2.719   2.950   -46.471 1.00 23.74 ? 89  VAL B CG2 1 
ATOM   557  N N   . GLU A 1 78  ? 5.173   6.696   -48.118 1.00 25.55 ? 90  GLU B N   1 
ATOM   558  C CA  . GLU A 1 78  ? 5.968   7.891   -47.905 1.00 25.77 ? 90  GLU B CA  1 
ATOM   559  C C   . GLU A 1 78  ? 5.357   8.736   -46.802 1.00 25.58 ? 90  GLU B C   1 
ATOM   560  O O   . GLU A 1 78  ? 4.169   8.629   -46.494 1.00 26.25 ? 90  GLU B O   1 
ATOM   561  C CB  . GLU A 1 78  ? 6.039   8.737   -49.163 1.00 27.58 ? 90  GLU B CB  1 
ATOM   562  C CG  . GLU A 1 78  ? 6.706   8.143   -50.350 1.00 28.17 ? 90  GLU B CG  1 
ATOM   563  C CD  . GLU A 1 78  ? 6.655   9.123   -51.499 1.00 34.33 ? 90  GLU B CD  1 
ATOM   564  O OE1 . GLU A 1 78  ? 6.977   10.321  -51.261 1.00 39.74 ? 90  GLU B OE1 1 
ATOM   565  O OE2 . GLU A 1 78  ? 6.231   8.720   -52.607 1.00 29.38 ? 90  GLU B OE2 1 
ATOM   566  N N   . TYR A 1 79  ? 6.189   9.586   -46.206 1.00 25.65 ? 91  TYR B N   1 
ATOM   567  C CA  . TYR A 1 79  ? 5.728   10.628  -45.298 1.00 29.66 ? 91  TYR B CA  1 
ATOM   568  C C   . TYR A 1 79  ? 6.357   11.953  -45.717 1.00 32.26 ? 91  TYR B C   1 
ATOM   569  O O   . TYR A 1 79  ? 7.580   12.049  -45.888 1.00 31.86 ? 91  TYR B O   1 
ATOM   570  C CB  . TYR A 1 79  ? 6.069   10.318  -43.829 1.00 27.57 ? 91  TYR B CB  1 
ATOM   571  C CG  . TYR A 1 79  ? 5.225   9.218   -43.187 1.00 27.58 ? 91  TYR B CG  1 
ATOM   572  C CD1 . TYR A 1 79  ? 5.236   7.926   -43.687 1.00 28.71 ? 91  TYR B CD1 1 
ATOM   573  C CD2 . TYR A 1 79  ? 4.452   9.464   -42.068 1.00 23.11 ? 91  TYR B CD2 1 
ATOM   574  C CE1 . TYR A 1 79  ? 4.479   6.927   -43.113 1.00 28.64 ? 91  TYR B CE1 1 
ATOM   575  C CE2 . TYR A 1 79  ? 3.697   8.464   -41.483 1.00 19.58 ? 91  TYR B CE2 1 
ATOM   576  C CZ  . TYR A 1 79  ? 3.719   7.201   -42.004 1.00 25.35 ? 91  TYR B CZ  1 
ATOM   577  O OH  . TYR A 1 79  ? 2.976   6.186   -41.433 1.00 31.29 ? 91  TYR B OH  1 
ATOM   578  N N   . THR A 1 80  ? 5.525   12.973  -45.877 1.00 31.80 ? 92  THR B N   1 
ATOM   579  C CA  . THR A 1 80  ? 5.986   14.281  -46.313 1.00 33.03 ? 92  THR B CA  1 
ATOM   580  C C   . THR A 1 80  ? 5.892   15.315  -45.200 1.00 31.24 ? 92  THR B C   1 
ATOM   581  O O   . THR A 1 80  ? 5.305   15.097  -44.132 1.00 28.43 ? 92  THR B O   1 
ATOM   582  C CB  . THR A 1 80  ? 5.193   14.760  -47.531 1.00 33.42 ? 92  THR B CB  1 
ATOM   583  O OG1 . THR A 1 80  ? 3.810   14.830  -47.180 1.00 36.17 ? 92  THR B OG1 1 
ATOM   584  C CG2 . THR A 1 80  ? 5.398   13.859  -48.773 1.00 43.56 ? 92  THR B CG2 1 
ATOM   585  N N   . HIS A 1 81  ? 6.502   16.458  -45.493 1.00 30.48 ? 93  HIS B N   1 
ATOM   586  C CA  . HIS A 1 81  ? 6.612   17.529  -44.524 1.00 29.87 ? 93  HIS B CA  1 
ATOM   587  C C   . HIS A 1 81  ? 5.240   17.906  -43.978 1.00 33.45 ? 93  HIS B C   1 
ATOM   588  O O   . HIS A 1 81  ? 4.229   17.886  -44.691 1.00 30.82 ? 93  HIS B O   1 
ATOM   589  C CB  . HIS A 1 81  ? 7.294   18.729  -45.168 1.00 25.89 ? 93  HIS B CB  1 
ATOM   590  C CG  . HIS A 1 81  ? 7.361   19.930  -44.288 1.00 26.91 ? 93  HIS B CG  1 
ATOM   591  N ND1 . HIS A 1 81  ? 8.374   20.116  -43.376 1.00 31.50 ? 93  HIS B ND1 1 
ATOM   592  C CD2 . HIS A 1 81  ? 6.561   21.020  -44.194 1.00 32.96 ? 93  HIS B CD2 1 
ATOM   593  C CE1 . HIS A 1 81  ? 8.193   21.267  -42.748 1.00 35.44 ? 93  HIS B CE1 1 
ATOM   594  N NE2 . HIS A 1 81  ? 7.099   21.836  -43.225 1.00 35.11 ? 93  HIS B NE2 1 
ATOM   595  N N   . ASP A 1 82  ? 5.209   18.172  -42.677 1.00 31.75 ? 94  ASP B N   1 
ATOM   596  C CA  . ASP A 1 82  ? 4.052   18.732  -42.003 1.00 28.64 ? 94  ASP B CA  1 
ATOM   597  C C   . ASP A 1 82  ? 4.521   19.988  -41.293 1.00 28.31 ? 94  ASP B C   1 
ATOM   598  O O   . ASP A 1 82  ? 5.248   19.905  -40.302 1.00 29.80 ? 94  ASP B O   1 
ATOM   599  C CB  . ASP A 1 82  ? 3.461   17.731  -41.028 1.00 29.64 ? 94  ASP B CB  1 
ATOM   600  C CG  . ASP A 1 82  ? 2.115   18.162  -40.510 1.00 33.75 ? 94  ASP B CG  1 
ATOM   601  O OD1 . ASP A 1 82  ? 1.673   19.287  -40.850 1.00 31.41 ? 94  ASP B OD1 1 
ATOM   602  O OD2 . ASP A 1 82  ? 1.515   17.386  -39.730 1.00 38.73 ? 94  ASP B OD2 1 
ATOM   603  N N   . SER A 1 83  ? 4.112   21.148  -41.807 1.00 28.37 ? 95  SER B N   1 
ATOM   604  C CA  . SER A 1 83  ? 4.541   22.415  -41.232 1.00 30.30 ? 95  SER B CA  1 
ATOM   605  C C   . SER A 1 83  ? 3.852   22.719  -39.904 1.00 32.73 ? 95  SER B C   1 
ATOM   606  O O   . SER A 1 83  ? 4.319   23.597  -39.168 1.00 30.55 ? 95  SER B O   1 
ATOM   607  C CB  . SER A 1 83  ? 4.284   23.541  -42.229 1.00 33.07 ? 95  SER B CB  1 
ATOM   608  O OG  . SER A 1 83  ? 2.978   23.435  -42.781 1.00 35.61 ? 95  SER B OG  1 
ATOM   609  N N   . ASN A 1 84  ? 2.762   22.013  -39.583 1.00 29.66 ? 96  ASN B N   1 
ATOM   610  C CA  . ASN A 1 84  ? 1.961   22.259  -38.392 1.00 27.08 ? 96  ASN B CA  1 
ATOM   611  C C   . ASN A 1 84  ? 2.430   21.481  -37.185 1.00 33.79 ? 96  ASN B C   1 
ATOM   612  O O   . ASN A 1 84  ? 1.750   21.485  -36.153 1.00 32.33 ? 96  ASN B O   1 
ATOM   613  C CB  . ASN A 1 84  ? 0.505   21.902  -38.650 1.00 29.42 ? 96  ASN B CB  1 
ATOM   614  C CG  . ASN A 1 84  ? -0.241  22.999  -39.313 1.00 31.79 ? 96  ASN B CG  1 
ATOM   615  O OD1 . ASN A 1 84  ? 0.017   23.347  -40.464 1.00 36.39 ? 96  ASN B OD1 1 
ATOM   616  N ND2 . ASN A 1 84  ? -1.187  23.566  -38.588 1.00 39.82 ? 96  ASN B ND2 1 
ATOM   617  N N   . THR A 1 85  ? 3.561   20.799  -37.282 1.00 33.51 ? 97  THR B N   1 
ATOM   618  C CA  . THR A 1 85  ? 3.835   19.779  -36.296 1.00 25.82 ? 97  THR B CA  1 
ATOM   619  C C   . THR A 1 85  ? 5.337   19.636  -36.116 1.00 25.64 ? 97  THR B C   1 
ATOM   620  O O   . THR A 1 85  ? 6.121   19.917  -37.020 1.00 27.12 ? 97  THR B O   1 
ATOM   621  C CB  . THR A 1 85  ? 3.163   18.470  -36.730 1.00 26.44 ? 97  THR B CB  1 
ATOM   622  O OG1 . THR A 1 85  ? 2.864   17.707  -35.574 1.00 34.59 ? 97  THR B OG1 1 
ATOM   623  C CG2 . THR A 1 85  ? 4.063   17.645  -37.607 1.00 27.37 ? 97  THR B CG2 1 
ATOM   624  N N   . ASP A 1 86  ? 5.724   19.226  -34.923 1.00 27.58 ? 98  ASP B N   1 
ATOM   625  C CA  . ASP A 1 86  ? 7.110   18.974  -34.570 1.00 27.44 ? 98  ASP B CA  1 
ATOM   626  C C   . ASP A 1 86  ? 7.227   17.517  -34.148 1.00 26.40 ? 98  ASP B C   1 
ATOM   627  O O   . ASP A 1 86  ? 6.334   16.980  -33.477 1.00 25.03 ? 98  ASP B O   1 
ATOM   628  C CB  . ASP A 1 86  ? 7.566   19.911  -33.437 1.00 29.61 ? 98  ASP B CB  1 
ATOM   629  C CG  . ASP A 1 86  ? 8.072   21.257  -33.955 1.00 33.43 ? 98  ASP B CG  1 
ATOM   630  O OD1 . ASP A 1 86  ? 8.562   21.299  -35.101 1.00 34.20 ? 98  ASP B OD1 1 
ATOM   631  O OD2 . ASP A 1 86  ? 7.934   22.276  -33.230 1.00 34.27 ? 98  ASP B OD2 1 
ATOM   632  N N   . MET A 1 87  ? 8.310   16.879  -34.576 1.00 22.22 ? 99  MET B N   1 
ATOM   633  C CA  . MET A 1 87  ? 8.552   15.467  -34.338 1.00 22.64 ? 99  MET B CA  1 
ATOM   634  C C   . MET A 1 87  ? 9.826   15.284  -33.528 1.00 26.27 ? 99  MET B C   1 
ATOM   635  O O   . MET A 1 87  ? 10.836  15.951  -33.781 1.00 26.48 ? 99  MET B O   1 
ATOM   636  C CB  . MET A 1 87  ? 8.655   14.680  -35.647 1.00 22.38 ? 99  MET B CB  1 
ATOM   637  C CG  . MET A 1 87  ? 8.832   13.196  -35.418 1.00 22.85 ? 99  MET B CG  1 
ATOM   638  S SD  . MET A 1 87  ? 8.711   12.205  -36.912 1.00 29.50 ? 99  MET B SD  1 
ATOM   639  C CE  . MET A 1 87  ? 10.227  12.607  -37.781 1.00 25.81 ? 99  MET B CE  1 
ATOM   640  N N   . PHE A 1 88  ? 9.758   14.361  -32.563 1.00 24.41 ? 100 PHE B N   1 
ATOM   641  C CA  . PHE A 1 88  ? 10.824  14.031  -31.629 1.00 23.44 ? 100 PHE B CA  1 
ATOM   642  C C   . PHE A 1 88  ? 10.913  12.515  -31.540 1.00 23.62 ? 100 PHE B C   1 
ATOM   643  O O   . PHE A 1 88  ? 9.891   11.832  -31.622 1.00 23.75 ? 100 PHE B O   1 
ATOM   644  C CB  . PHE A 1 88  ? 10.547  14.630  -30.237 1.00 23.41 ? 100 PHE B CB  1 
ATOM   645  C CG  . PHE A 1 88  ? 10.450  16.119  -30.240 1.00 25.46 ? 100 PHE B CG  1 
ATOM   646  C CD1 . PHE A 1 88  ? 9.264   16.748  -30.605 1.00 26.03 ? 100 PHE B CD1 1 
ATOM   647  C CD2 . PHE A 1 88  ? 11.544  16.894  -29.896 1.00 24.14 ? 100 PHE B CD2 1 
ATOM   648  C CE1 . PHE A 1 88  ? 9.176   18.127  -30.639 1.00 28.81 ? 100 PHE B CE1 1 
ATOM   649  C CE2 . PHE A 1 88  ? 11.465  18.265  -29.924 1.00 27.07 ? 100 PHE B CE2 1 
ATOM   650  C CZ  . PHE A 1 88  ? 10.283  18.888  -30.292 1.00 28.79 ? 100 PHE B CZ  1 
ATOM   651  N N   . GLN A 1 89  ? 12.118  11.988  -31.353 1.00 20.61 ? 101 GLN B N   1 
ATOM   652  C CA  . GLN A 1 89  ? 12.314  10.550  -31.398 1.00 23.96 ? 101 GLN B CA  1 
ATOM   653  C C   . GLN A 1 89  ? 13.160  10.069  -30.222 1.00 26.36 ? 101 GLN B C   1 
ATOM   654  O O   . GLN A 1 89  ? 14.114  10.737  -29.815 1.00 24.64 ? 101 GLN B O   1 
ATOM   655  C CB  . GLN A 1 89  ? 12.948  10.164  -32.734 1.00 24.91 ? 101 GLN B CB  1 
ATOM   656  C CG  . GLN A 1 89  ? 11.953  10.142  -33.869 1.00 22.02 ? 101 GLN B CG  1 
ATOM   657  C CD  . GLN A 1 89  ? 12.564  9.630   -35.133 1.00 26.37 ? 101 GLN B CD  1 
ATOM   658  O OE1 . GLN A 1 89  ? 11.864  9.214   -36.056 1.00 26.58 ? 101 GLN B OE1 1 
ATOM   659  N NE2 . GLN A 1 89  ? 13.890  9.666   -35.196 1.00 25.42 ? 101 GLN B NE2 1 
ATOM   660  N N   . ILE A 1 90  ? 12.800  8.900   -29.688 1.00 25.08 ? 102 ILE B N   1 
ATOM   661  C CA  . ILE A 1 90  ? 13.433  8.281   -28.529 1.00 26.29 ? 102 ILE B CA  1 
ATOM   662  C C   . ILE A 1 90  ? 13.965  6.918   -28.941 1.00 26.00 ? 102 ILE B C   1 
ATOM   663  O O   . ILE A 1 90  ? 13.338  6.235   -29.752 1.00 29.80 ? 102 ILE B O   1 
ATOM   664  C CB  . ILE A 1 90  ? 12.420  8.124   -27.371 1.00 29.85 ? 102 ILE B CB  1 
ATOM   665  C CG1 . ILE A 1 90  ? 11.611  9.401   -27.188 1.00 26.41 ? 102 ILE B CG1 1 
ATOM   666  C CG2 . ILE A 1 90  ? 13.100  7.720   -26.067 1.00 27.36 ? 102 ILE B CG2 1 
ATOM   667  C CD1 . ILE A 1 90  ? 10.616  9.304   -26.076 1.00 31.38 ? 102 ILE B CD1 1 
ATOM   668  N N   . GLY A 1 91  ? 15.089  6.491   -28.371 1.00 24.58 ? 103 GLY B N   1 
ATOM   669  C CA  . GLY A 1 91  ? 15.516  5.129   -28.627 1.00 26.94 ? 103 GLY B CA  1 
ATOM   670  C C   . GLY A 1 91  ? 16.920  4.846   -28.137 1.00 29.42 ? 103 GLY B C   1 
ATOM   671  O O   . GLY A 1 91  ? 17.562  5.685   -27.508 1.00 31.20 ? 103 GLY B O   1 
ATOM   672  N N   . ARG A 1 92  ? 17.384  3.630   -28.460 1.00 30.24 ? 104 ARG B N   1 
ATOM   673  C CA  . ARG A 1 92  ? 18.688  3.150   -28.011 1.00 29.31 ? 104 ARG B CA  1 
ATOM   674  C C   . ARG A 1 92  ? 19.832  3.788   -28.778 1.00 33.90 ? 104 ARG B C   1 
ATOM   675  O O   . ARG A 1 92  ? 20.889  4.056   -28.192 1.00 37.63 ? 104 ARG B O   1 
ATOM   676  C CB  . ARG A 1 92  ? 18.782  1.630   -28.148 1.00 32.43 ? 104 ARG B CB  1 
ATOM   677  C CG  . ARG A 1 92  ? 19.656  0.956   -27.101 1.00 36.92 ? 104 ARG B CG  1 
ATOM   678  C CD  . ARG A 1 92  ? 20.222  -0.419  -27.536 1.00 42.30 ? 104 ARG B CD  1 
ATOM   679  N NE  . ARG A 1 92  ? 19.266  -1.268  -28.240 1.00 39.24 ? 104 ARG B NE  1 
ATOM   680  C CZ  . ARG A 1 92  ? 19.511  -1.873  -29.395 1.00 42.01 ? 104 ARG B CZ  1 
ATOM   681  N NH1 . ARG A 1 92  ? 20.701  -1.810  -29.966 1.00 43.57 ? 104 ARG B NH1 1 
ATOM   682  N NH2 . ARG A 1 92  ? 18.536  -2.555  -29.994 1.00 44.89 ? 104 ARG B NH2 1 
ATOM   683  N N   . SER A 1 93  ? 19.646  4.032   -30.074 1.00 33.98 ? 105 SER B N   1 
ATOM   684  C CA  . SER A 1 93  ? 20.720  4.571   -30.888 1.00 33.54 ? 105 SER B CA  1 
ATOM   685  C C   . SER A 1 93  ? 21.107  5.964   -30.410 1.00 32.66 ? 105 SER B C   1 
ATOM   686  O O   . SER A 1 93  ? 20.337  6.661   -29.744 1.00 34.77 ? 105 SER B O   1 
ATOM   687  C CB  . SER A 1 93  ? 20.321  4.613   -32.365 1.00 33.83 ? 105 SER B CB  1 
ATOM   688  O OG  . SER A 1 93  ? 21.441  4.946   -33.176 1.00 34.17 ? 105 SER B OG  1 
ATOM   689  N N   . THR A 1 94  ? 22.338  6.353   -30.743 1.00 37.74 ? 106 THR B N   1 
ATOM   690  C CA  . THR A 1 94  ? 22.883  7.669   -30.429 1.00 35.71 ? 106 THR B CA  1 
ATOM   691  C C   . THR A 1 94  ? 23.046  8.535   -31.672 1.00 35.13 ? 106 THR B C   1 
ATOM   692  O O   . THR A 1 94  ? 23.643  9.616   -31.588 1.00 34.83 ? 106 THR B O   1 
ATOM   693  C CB  . THR A 1 94  ? 24.225  7.520   -29.713 1.00 34.48 ? 106 THR B CB  1 
ATOM   694  O OG1 . THR A 1 94  ? 25.054  6.600   -30.433 1.00 35.75 ? 106 THR B OG1 1 
ATOM   695  C CG2 . THR A 1 94  ? 24.009  6.947   -28.347 1.00 41.34 ? 106 THR B CG2 1 
ATOM   696  N N   . GLU A 1 95  ? 22.525  8.085   -32.819 1.00 33.73 ? 107 GLU B N   1 
ATOM   697  C CA  . GLU A 1 95  ? 22.674  8.786   -34.083 1.00 33.42 ? 107 GLU B CA  1 
ATOM   698  C C   . GLU A 1 95  ? 21.887  10.085  -34.048 1.00 32.70 ? 107 GLU B C   1 
ATOM   699  O O   . GLU A 1 95  ? 21.106  10.346  -33.132 1.00 35.85 ? 107 GLU B O   1 
ATOM   700  C CB  . GLU A 1 95  ? 22.193  7.919   -35.243 1.00 33.50 ? 107 GLU B CB  1 
ATOM   701  C CG  . GLU A 1 95  ? 23.101  6.744   -35.529 1.00 35.54 ? 107 GLU B CG  1 
ATOM   702  C CD  . GLU A 1 95  ? 22.742  5.984   -36.798 1.00 42.72 ? 107 GLU B CD  1 
ATOM   703  O OE1 . GLU A 1 95  ? 21.890  6.467   -37.575 1.00 38.70 ? 107 GLU B OE1 1 
ATOM   704  O OE2 . GLU A 1 95  ? 23.320  4.893   -37.016 1.00 44.54 ? 107 GLU B OE2 1 
ATOM   705  N N   . SER A 1 96  ? 22.100  10.920  -35.056 1.00 33.40 ? 108 SER B N   1 
ATOM   706  C CA  . SER A 1 96  ? 21.433  12.210  -35.047 1.00 36.67 ? 108 SER B CA  1 
ATOM   707  C C   . SER A 1 96  ? 19.902  12.129  -35.042 1.00 38.81 ? 108 SER B C   1 
ATOM   708  O O   . SER A 1 96  ? 19.292  13.053  -34.482 1.00 41.05 ? 108 SER B O   1 
ATOM   709  C CB  . SER A 1 96  ? 21.970  13.069  -36.208 1.00 35.87 ? 108 SER B CB  1 
ATOM   710  O OG  . SER A 1 96  ? 21.137  13.031  -37.361 1.00 44.46 ? 108 SER B OG  1 
ATOM   711  N N   . PRO A 1 97  ? 19.226  11.107  -35.595 1.00 34.33 ? 109 PRO B N   1 
ATOM   712  C CA  . PRO A 1 97  ? 17.750  11.122  -35.541 1.00 34.02 ? 109 PRO B CA  1 
ATOM   713  C C   . PRO A 1 97  ? 17.159  10.941  -34.141 1.00 35.52 ? 109 PRO B C   1 
ATOM   714  O O   . PRO A 1 97  ? 16.009  11.355  -33.916 1.00 30.14 ? 109 PRO B O   1 
ATOM   715  C CB  . PRO A 1 97  ? 17.350  9.968   -36.477 1.00 32.26 ? 109 PRO B CB  1 
ATOM   716  C CG  . PRO A 1 97  ? 18.588  9.199   -36.696 1.00 34.24 ? 109 PRO B CG  1 
ATOM   717  C CD  . PRO A 1 97  ? 19.686  10.196  -36.652 1.00 33.89 ? 109 PRO B CD  1 
ATOM   718  N N   . ILE A 1 98  ? 17.895  10.362  -33.196 1.00 31.92 ? 110 ILE B N   1 
ATOM   719  C CA  . ILE A 1 98  ? 17.392  10.169  -31.845 1.00 27.37 ? 110 ILE B CA  1 
ATOM   720  C C   . ILE A 1 98  ? 17.596  11.450  -31.059 1.00 27.45 ? 110 ILE B C   1 
ATOM   721  O O   . ILE A 1 98  ? 18.727  11.910  -30.890 1.00 32.28 ? 110 ILE B O   1 
ATOM   722  C CB  . ILE A 1 98  ? 18.091  8.996   -31.160 1.00 26.57 ? 110 ILE B CB  1 
ATOM   723  C CG1 . ILE A 1 98  ? 17.536  7.700   -31.728 1.00 24.95 ? 110 ILE B CG1 1 
ATOM   724  C CG2 . ILE A 1 98  ? 17.946  9.112   -29.644 1.00 25.51 ? 110 ILE B CG2 1 
ATOM   725  C CD1 . ILE A 1 98  ? 16.055  7.695   -31.803 1.00 23.88 ? 110 ILE B CD1 1 
ATOM   726  N N   . ASP A 1 99  ? 16.507  12.027  -30.571 1.00 28.38 ? 111 ASP B N   1 
ATOM   727  C CA  . ASP A 1 99  ? 16.612  13.247  -29.786 1.00 27.89 ? 111 ASP B CA  1 
ATOM   728  C C   . ASP A 1 99  ? 16.825  12.981  -28.306 1.00 29.75 ? 111 ASP B C   1 
ATOM   729  O O   . ASP A 1 99  ? 17.330  13.863  -27.603 1.00 33.33 ? 111 ASP B O   1 
ATOM   730  C CB  . ASP A 1 99  ? 15.368  14.108  -29.987 1.00 25.59 ? 111 ASP B CB  1 
ATOM   731  C CG  . ASP A 1 99  ? 15.200  14.537  -31.434 1.00 35.30 ? 111 ASP B CG  1 
ATOM   732  O OD1 . ASP A 1 99  ? 16.072  15.287  -31.940 1.00 36.31 ? 111 ASP B OD1 1 
ATOM   733  O OD2 . ASP A 1 99  ? 14.198  14.131  -32.067 1.00 32.74 ? 111 ASP B OD2 1 
ATOM   734  N N   . PHE A 1 100 ? 16.484  11.783  -27.827 1.00 32.01 ? 112 PHE B N   1 
ATOM   735  C CA  . PHE A 1 100 ? 16.647  11.407  -26.422 1.00 29.69 ? 112 PHE B CA  1 
ATOM   736  C C   . PHE A 1 100 ? 17.126  9.963   -26.372 1.00 32.90 ? 112 PHE B C   1 
ATOM   737  O O   . PHE A 1 100 ? 16.326  9.039   -26.554 1.00 30.45 ? 112 PHE B O   1 
ATOM   738  C CB  . PHE A 1 100 ? 15.357  11.562  -25.641 1.00 30.55 ? 112 PHE B CB  1 
ATOM   739  C CG  . PHE A 1 100 ? 15.530  11.348  -24.169 1.00 38.48 ? 112 PHE B CG  1 
ATOM   740  C CD1 . PHE A 1 100 ? 16.597  11.926  -23.494 1.00 39.69 ? 112 PHE B CD1 1 
ATOM   741  C CD2 . PHE A 1 100 ? 14.646  10.548  -23.456 1.00 39.35 ? 112 PHE B CD2 1 
ATOM   742  C CE1 . PHE A 1 100 ? 16.764  11.734  -22.126 1.00 39.51 ? 112 PHE B CE1 1 
ATOM   743  C CE2 . PHE A 1 100 ? 14.814  10.343  -22.080 1.00 42.35 ? 112 PHE B CE2 1 
ATOM   744  C CZ  . PHE A 1 100 ? 15.878  10.938  -21.421 1.00 41.62 ? 112 PHE B CZ  1 
ATOM   745  N N   . VAL A 1 101 ? 18.422  9.772   -26.110 1.00 37.06 ? 113 VAL B N   1 
ATOM   746  C CA  . VAL A 1 101 ? 18.956  8.424   -26.037 1.00 31.59 ? 113 VAL B CA  1 
ATOM   747  C C   . VAL A 1 101 ? 18.505  7.790   -24.733 1.00 33.17 ? 113 VAL B C   1 
ATOM   748  O O   . VAL A 1 101 ? 18.318  8.470   -23.718 1.00 39.54 ? 113 VAL B O   1 
ATOM   749  C CB  . VAL A 1 101 ? 20.488  8.420   -26.148 1.00 31.29 ? 113 VAL B CB  1 
ATOM   750  C CG1 . VAL A 1 101 ? 20.982  7.002   -26.393 1.00 34.38 ? 113 VAL B CG1 1 
ATOM   751  C CG2 . VAL A 1 101 ? 20.935  9.331   -27.245 1.00 34.68 ? 113 VAL B CG2 1 
ATOM   752  N N   . VAL A 1 102 ? 18.337  6.472   -24.753 1.00 32.39 ? 114 VAL B N   1 
ATOM   753  C CA  . VAL A 1 102 ? 17.748  5.739   -23.643 1.00 32.51 ? 114 VAL B CA  1 
ATOM   754  C C   . VAL A 1 102 ? 18.442  4.389   -23.540 1.00 35.95 ? 114 VAL B C   1 
ATOM   755  O O   . VAL A 1 102 ? 18.611  3.707   -24.554 1.00 34.69 ? 114 VAL B O   1 
ATOM   756  C CB  . VAL A 1 102 ? 16.233  5.576   -23.848 1.00 32.22 ? 114 VAL B CB  1 
ATOM   757  C CG1 . VAL A 1 102 ? 15.747  4.334   -23.167 1.00 39.26 ? 114 VAL B CG1 1 
ATOM   758  C CG2 . VAL A 1 102 ? 15.505  6.779   -23.307 1.00 27.83 ? 114 VAL B CG2 1 
ATOM   759  N N   . THR A 1 103 ? 18.852  4.006   -22.326 1.00 40.91 ? 115 THR B N   1 
ATOM   760  C CA  . THR A 1 103 ? 19.626  2.787   -22.099 1.00 39.50 ? 115 THR B CA  1 
ATOM   761  C C   . THR A 1 103 ? 18.866  1.820   -21.205 1.00 40.23 ? 115 THR B C   1 
ATOM   762  O O   . THR A 1 103 ? 17.846  2.154   -20.595 1.00 39.55 ? 115 THR B O   1 
ATOM   763  C CB  . THR A 1 103 ? 20.980  3.068   -21.434 1.00 38.35 ? 115 THR B CB  1 
ATOM   764  O OG1 . THR A 1 103 ? 20.789  3.111   -20.019 1.00 44.84 ? 115 THR B OG1 1 
ATOM   765  C CG2 . THR A 1 103 ? 21.544  4.397   -21.871 1.00 34.93 ? 115 THR B CG2 1 
ATOM   766  N N   . ASP A 1 104 ? 19.404  0.613   -21.106 1.00 43.31 ? 116 ASP B N   1 
ATOM   767  C CA  . ASP A 1 104 ? 18.866  -0.350  -20.164 1.00 49.45 ? 116 ASP B CA  1 
ATOM   768  C C   . ASP A 1 104 ? 19.294  0.021   -18.758 1.00 54.87 ? 116 ASP B C   1 
ATOM   769  O O   . ASP A 1 104 ? 20.489  0.026   -18.441 1.00 52.25 ? 116 ASP B O   1 
ATOM   770  C CB  . ASP A 1 104 ? 19.324  -1.753  -20.520 1.00 49.18 ? 116 ASP B CB  1 
ATOM   771  C CG  . ASP A 1 104 ? 18.313  -2.473  -21.379 1.00 54.06 ? 116 ASP B CG  1 
ATOM   772  O OD1 . ASP A 1 104 ? 17.276  -2.911  -20.812 1.00 58.48 ? 116 ASP B OD1 1 
ATOM   773  O OD2 . ASP A 1 104 ? 18.540  -2.569  -22.608 1.00 47.12 ? 116 ASP B OD2 1 
ATOM   774  N N   . THR A 1 105 ? 18.318  0.355   -17.926 1.00 60.65 ? 117 THR B N   1 
ATOM   775  C CA  . THR A 1 105 ? 18.591  0.742   -16.552 1.00 64.00 ? 117 THR B CA  1 
ATOM   776  C C   . THR A 1 105 ? 18.681  -0.448  -15.613 1.00 67.48 ? 117 THR B C   1 
ATOM   777  O O   . THR A 1 105 ? 19.064  -0.271  -14.456 1.00 66.90 ? 117 THR B O   1 
ATOM   778  C CB  . THR A 1 105 ? 17.510  1.704   -16.051 1.00 61.84 ? 117 THR B CB  1 
ATOM   779  O OG1 . THR A 1 105 ? 16.239  1.305   -16.582 1.00 66.24 ? 117 THR B OG1 1 
ATOM   780  C CG2 . THR A 1 105 ? 17.814  3.134   -16.491 1.00 61.84 ? 117 THR B CG2 1 
ATOM   781  N N   . VAL A 1 106 ? 18.363  -1.647  -16.092 1.00 75.67 ? 118 VAL B N   1 
ATOM   782  C CA  . VAL A 1 106 ? 18.192  -2.825  -15.242 1.00 75.09 ? 118 VAL B CA  1 
ATOM   783  C C   . VAL A 1 106 ? 19.483  -3.166  -14.498 1.00 81.02 ? 118 VAL B C   1 
ATOM   784  O O   . VAL A 1 106 ? 19.407  -3.714  -13.388 1.00 87.15 ? 118 VAL B O   1 
ATOM   785  C CB  . VAL A 1 106 ? 17.670  -4.031  -16.049 1.00 72.13 ? 118 VAL B CB  1 
ATOM   786  C CG1 . VAL A 1 106 ? 16.820  -4.940  -15.144 1.00 64.06 ? 118 VAL B CG1 1 
ATOM   787  C CG2 . VAL A 1 106 ? 16.889  -3.576  -17.323 1.00 63.38 ? 118 VAL B CG2 1 
ATOM   788  N N   . PRO A 1 107 ? 20.684  -2.925  -15.074 1.00 82.08 ? 119 PRO B N   1 
ATOM   789  C CA  . PRO A 1 107 ? 21.939  -2.977  -14.314 1.00 88.01 ? 119 PRO B CA  1 
ATOM   790  C C   . PRO A 1 107 ? 21.833  -2.362  -12.932 1.00 81.05 ? 119 PRO B C   1 
ATOM   791  O O   . PRO A 1 107 ? 22.235  -1.201  -12.718 1.00 85.14 ? 119 PRO B O   1 
ATOM   792  C CB  . PRO A 1 107 ? 22.901  -2.195  -15.217 1.00 84.95 ? 119 PRO B CB  1 
ATOM   793  C CG  . PRO A 1 107 ? 22.404  -2.499  -16.606 1.00 78.94 ? 119 PRO B CG  1 
ATOM   794  C CD  . PRO A 1 107 ? 20.995  -3.087  -16.512 1.00 77.25 ? 119 PRO B CD  1 
ATOM   795  N N   . VAL A 1 118 ? 25.973  -6.986  -24.833 1.00 61.85 ? 130 VAL B N   1 
ATOM   796  C CA  . VAL A 1 118 ? 25.544  -5.798  -25.572 1.00 65.97 ? 130 VAL B CA  1 
ATOM   797  C C   . VAL A 1 118 ? 24.155  -6.037  -26.178 1.00 67.08 ? 130 VAL B C   1 
ATOM   798  O O   . VAL A 1 118 ? 23.743  -5.352  -27.128 1.00 63.00 ? 130 VAL B O   1 
ATOM   799  C CB  . VAL A 1 118 ? 26.572  -5.402  -26.673 1.00 60.55 ? 130 VAL B CB  1 
ATOM   800  C CG1 . VAL A 1 118 ? 27.841  -4.838  -26.043 1.00 51.33 ? 130 VAL B CG1 1 
ATOM   801  C CG2 . VAL A 1 118 ? 26.872  -6.588  -27.622 1.00 55.30 ? 130 VAL B CG2 1 
ATOM   802  N N   . GLN A 1 119 ? 23.447  -7.026  -25.631 1.00 60.98 ? 131 GLN B N   1 
ATOM   803  C CA  . GLN A 1 119 ? 22.105  -7.360  -26.079 1.00 60.52 ? 131 GLN B CA  1 
ATOM   804  C C   . GLN A 1 119 ? 21.088  -6.476  -25.372 1.00 63.84 ? 131 GLN B C   1 
ATOM   805  O O   . GLN A 1 119 ? 21.180  -6.245  -24.161 1.00 68.58 ? 131 GLN B O   1 
ATOM   806  C CB  . GLN A 1 119 ? 21.797  -8.821  -25.783 1.00 62.83 ? 131 GLN B CB  1 
ATOM   807  C CG  . GLN A 1 119 ? 22.317  -9.250  -24.421 1.00 72.91 ? 131 GLN B CG  1 
ATOM   808  C CD  . GLN A 1 119 ? 22.314  -10.761 -24.228 1.00 82.35 ? 131 GLN B CD  1 
ATOM   809  O OE1 . GLN A 1 119 ? 22.572  -11.529 -25.167 1.00 79.87 ? 131 GLN B OE1 1 
ATOM   810  N NE2 . GLN A 1 119 ? 22.004  -11.196 -23.003 1.00 73.05 ? 131 GLN B NE2 1 
ATOM   811  N N   . SER A 1 120 ? 20.109  -5.991  -26.128 1.00 54.95 ? 132 SER B N   1 
ATOM   812  C CA  . SER A 1 120 ? 19.077  -5.142  -25.562 1.00 47.98 ? 132 SER B CA  1 
ATOM   813  C C   . SER A 1 120 ? 17.758  -5.402  -26.272 1.00 51.73 ? 132 SER B C   1 
ATOM   814  O O   . SER A 1 120 ? 17.728  -5.684  -27.474 1.00 54.38 ? 132 SER B O   1 
ATOM   815  C CB  . SER A 1 120 ? 19.447  -3.668  -25.673 1.00 45.00 ? 132 SER B CB  1 
ATOM   816  O OG  . SER A 1 120 ? 18.336  -2.861  -25.343 1.00 51.08 ? 132 SER B OG  1 
ATOM   817  N N   . THR A 1 121 ? 16.665  -5.303  -25.516 1.00 50.42 ? 133 THR B N   1 
ATOM   818  C CA  . THR A 1 121 ? 15.319  -5.382  -26.074 1.00 43.94 ? 133 THR B CA  1 
ATOM   819  C C   . THR A 1 121 ? 14.762  -4.019  -26.484 1.00 43.05 ? 133 THR B C   1 
ATOM   820  O O   . THR A 1 121 ? 13.635  -3.952  -26.985 1.00 42.55 ? 133 THR B O   1 
ATOM   821  C CB  . THR A 1 121 ? 14.370  -6.040  -25.069 1.00 44.27 ? 133 THR B CB  1 
ATOM   822  O OG1 . THR A 1 121 ? 14.742  -5.653  -23.737 1.00 50.88 ? 133 THR B OG1 1 
ATOM   823  C CG2 . THR A 1 121 ? 14.419  -7.554  -25.197 1.00 43.24 ? 133 THR B CG2 1 
ATOM   824  N N   . ILE A 1 122 ? 15.518  -2.941  -26.291 1.00 42.11 ? 134 ILE B N   1 
ATOM   825  C CA  . ILE A 1 122 ? 15.073  -1.593  -26.633 1.00 40.20 ? 134 ILE B CA  1 
ATOM   826  C C   . ILE A 1 122 ? 15.468  -1.297  -28.075 1.00 40.10 ? 134 ILE B C   1 
ATOM   827  O O   . ILE A 1 122 ? 16.625  -1.495  -28.468 1.00 40.84 ? 134 ILE B O   1 
ATOM   828  C CB  . ILE A 1 122 ? 15.683  -0.559  -25.670 1.00 38.84 ? 134 ILE B CB  1 
ATOM   829  C CG1 . ILE A 1 122 ? 15.283  -0.862  -24.226 1.00 39.52 ? 134 ILE B CG1 1 
ATOM   830  C CG2 . ILE A 1 122 ? 15.256  0.845   -26.043 1.00 36.38 ? 134 ILE B CG2 1 
ATOM   831  C CD1 . ILE A 1 122 ? 16.009  -0.023  -23.220 1.00 38.22 ? 134 ILE B CD1 1 
ATOM   832  N N   . SER A 1 123 ? 14.517  -0.823  -28.869 1.00 37.91 ? 135 SER B N   1 
ATOM   833  C CA  . SER A 1 123 ? 14.826  -0.549  -30.260 1.00 35.71 ? 135 SER B CA  1 
ATOM   834  C C   . SER A 1 123 ? 15.747  0.653   -30.401 1.00 34.00 ? 135 SER B C   1 
ATOM   835  O O   . SER A 1 123 ? 15.680  1.623   -29.641 1.00 31.09 ? 135 SER B O   1 
ATOM   836  C CB  . SER A 1 123 ? 13.556  -0.335  -31.068 1.00 31.59 ? 135 SER B CB  1 
ATOM   837  O OG  . SER A 1 123 ? 13.183  -1.567  -31.646 1.00 42.95 ? 135 SER B OG  1 
ATOM   838  N N   . ARG A 1 124 ? 16.619  0.570   -31.400 1.00 35.20 ? 136 ARG B N   1 
ATOM   839  C CA  . ARG A 1 124 ? 17.508  1.680   -31.694 1.00 30.93 ? 136 ARG B CA  1 
ATOM   840  C C   . ARG A 1 124 ? 16.729  2.948   -31.984 1.00 28.79 ? 136 ARG B C   1 
ATOM   841  O O   . ARG A 1 124 ? 17.165  4.049   -31.630 1.00 26.49 ? 136 ARG B O   1 
ATOM   842  C CB  . ARG A 1 124 ? 18.385  1.306   -32.869 1.00 33.53 ? 136 ARG B CB  1 
ATOM   843  C CG  . ARG A 1 124 ? 19.181  0.086   -32.567 1.00 36.70 ? 136 ARG B CG  1 
ATOM   844  C CD  . ARG A 1 124 ? 19.846  -0.404  -33.794 1.00 38.54 ? 136 ARG B CD  1 
ATOM   845  N NE  . ARG A 1 124 ? 19.107  -1.544  -34.317 1.00 50.12 ? 136 ARG B NE  1 
ATOM   846  C CZ  . ARG A 1 124 ? 19.046  -1.863  -35.602 1.00 49.81 ? 136 ARG B CZ  1 
ATOM   847  N NH1 . ARG A 1 124 ? 19.740  -1.196  -36.513 1.00 44.02 ? 136 ARG B NH1 1 
ATOM   848  N NH2 . ARG A 1 124 ? 18.276  -2.881  -35.982 1.00 47.36 ? 136 ARG B NH2 1 
ATOM   849  N N   . PHE A 1 125 ? 15.572  2.813   -32.623 1.00 29.49 ? 137 PHE B N   1 
ATOM   850  C CA  . PHE A 1 125 ? 14.672  3.934   -32.878 1.00 25.77 ? 137 PHE B CA  1 
ATOM   851  C C   . PHE A 1 125 ? 13.305  3.577   -32.300 1.00 27.27 ? 137 PHE B C   1 
ATOM   852  O O   . PHE A 1 125 ? 12.404  3.133   -33.010 1.00 29.74 ? 137 PHE B O   1 
ATOM   853  C CB  . PHE A 1 125 ? 14.636  4.212   -34.309 1.00 23.29 ? 137 PHE B CB  1 
ATOM   854  C CG  . PHE A 1 125 ? 15.985  4.495   -34.876 1.00 26.48 ? 137 PHE B CG  1 
ATOM   855  C CD1 . PHE A 1 125 ? 16.509  5.779   -34.839 1.00 29.00 ? 137 PHE B CD1 1 
ATOM   856  C CD2 . PHE A 1 125 ? 16.763  3.473   -35.390 1.00 26.06 ? 137 PHE B CD2 1 
ATOM   857  C CE1 . PHE A 1 125 ? 17.768  6.043   -35.339 1.00 26.39 ? 137 PHE B CE1 1 
ATOM   858  C CE2 . PHE A 1 125 ? 18.016  3.734   -35.890 1.00 22.68 ? 137 PHE B CE2 1 
ATOM   859  C CZ  . PHE A 1 125 ? 18.521  5.018   -35.857 1.00 25.71 ? 137 PHE B CZ  1 
ATOM   860  N N   . ALA A 1 126 ? 13.155  3.809   -30.993 1.00 27.92 ? 138 ALA B N   1 
ATOM   861  C CA  . ALA A 1 126 ? 12.043  3.237   -30.242 1.00 26.61 ? 138 ALA B CA  1 
ATOM   862  C C   . ALA A 1 126 ? 10.698  3.773   -30.714 1.00 23.69 ? 138 ALA B C   1 
ATOM   863  O O   . ALA A 1 126 ? 9.794   2.994   -31.040 1.00 26.90 ? 138 ALA B O   1 
ATOM   864  C CB  . ALA A 1 126 ? 12.232  3.514   -28.753 1.00 24.34 ? 138 ALA B CB  1 
ATOM   865  N N   . CYS A 1 127 ? 10.533  5.092   -30.723 1.00 21.27 ? 139 CYS B N   1 
ATOM   866  C CA  . CYS A 1 127 ? 9.248   5.689   -31.057 1.00 22.19 ? 139 CYS B CA  1 
ATOM   867  C C   . CYS A 1 127 ? 9.482   7.137   -31.459 1.00 23.11 ? 139 CYS B C   1 
ATOM   868  O O   . CYS A 1 127 ? 10.587  7.665   -31.315 1.00 25.10 ? 139 CYS B O   1 
ATOM   869  C CB  . CYS A 1 127 ? 8.279   5.587   -29.881 1.00 24.84 ? 139 CYS B CB  1 
ATOM   870  S SG  . CYS A 1 127 ? 8.735   6.573   -28.426 1.00 23.24 ? 139 CYS B SG  1 
ATOM   871  N N   . ARG A 1 128 ? 8.438   7.776   -31.983 1.00 21.13 ? 140 ARG B N   1 
ATOM   872  C CA  . ARG A 1 128 ? 8.471   9.208   -32.230 1.00 20.08 ? 140 ARG B CA  1 
ATOM   873  C C   . ARG A 1 128 ? 7.298   9.855   -31.507 1.00 22.29 ? 140 ARG B C   1 
ATOM   874  O O   . ARG A 1 128 ? 6.232   9.248   -31.359 1.00 23.75 ? 140 ARG B O   1 
ATOM   875  C CB  . ARG A 1 128 ? 8.429   9.534   -33.724 1.00 21.78 ? 140 ARG B CB  1 
ATOM   876  C CG  . ARG A 1 128 ? 7.453   8.691   -34.471 1.00 23.35 ? 140 ARG B CG  1 
ATOM   877  C CD  . ARG A 1 128 ? 7.876   8.404   -35.880 1.00 20.86 ? 140 ARG B CD  1 
ATOM   878  N NE  . ARG A 1 128 ? 7.326   7.105   -36.252 1.00 23.22 ? 140 ARG B NE  1 
ATOM   879  C CZ  . ARG A 1 128 ? 6.073   6.889   -36.630 1.00 24.69 ? 140 ARG B CZ  1 
ATOM   880  N NH1 . ARG A 1 128 ? 5.218   7.889   -36.803 1.00 26.93 ? 140 ARG B NH1 1 
ATOM   881  N NH2 . ARG A 1 128 ? 5.675   5.640   -36.861 1.00 21.80 ? 140 ARG B NH2 1 
ATOM   882  N N   . ILE A 1 129 ? 7.525   11.062  -30.998 1.00 19.58 ? 141 ILE B N   1 
ATOM   883  C CA  . ILE A 1 129 ? 6.504   11.868  -30.343 1.00 18.50 ? 141 ILE B CA  1 
ATOM   884  C C   . ILE A 1 129 ? 6.309   13.109  -31.183 1.00 22.62 ? 141 ILE B C   1 
ATOM   885  O O   . ILE A 1 129 ? 7.276   13.814  -31.483 1.00 26.55 ? 141 ILE B O   1 
ATOM   886  C CB  . ILE A 1 129 ? 6.900   12.253  -28.908 1.00 19.11 ? 141 ILE B CB  1 
ATOM   887  C CG1 . ILE A 1 129 ? 6.828   11.018  -27.994 1.00 22.10 ? 141 ILE B CG1 1 
ATOM   888  C CG2 . ILE A 1 129 ? 6.077   13.458  -28.429 1.00 16.66 ? 141 ILE B CG2 1 
ATOM   889  C CD1 . ILE A 1 129 ? 6.949   11.323  -26.494 1.00 23.27 ? 141 ILE B CD1 1 
ATOM   890  N N   . ILE A 1 130 ? 5.069   13.381  -31.562 1.00 24.66 ? 142 ILE B N   1 
ATOM   891  C CA  . ILE A 1 130 ? 4.762   14.435  -32.512 1.00 21.54 ? 142 ILE B CA  1 
ATOM   892  C C   . ILE A 1 130 ? 3.878   15.452  -31.808 1.00 22.22 ? 142 ILE B C   1 
ATOM   893  O O   . ILE A 1 130 ? 2.831   15.102  -31.247 1.00 20.78 ? 142 ILE B O   1 
ATOM   894  C CB  . ILE A 1 130 ? 4.095   13.870  -33.772 1.00 25.02 ? 142 ILE B CB  1 
ATOM   895  C CG1 . ILE A 1 130 ? 5.112   13.042  -34.562 1.00 21.10 ? 142 ILE B CG1 1 
ATOM   896  C CG2 . ILE A 1 130 ? 3.589   14.977  -34.637 1.00 24.34 ? 142 ILE B CG2 1 
ATOM   897  C CD1 . ILE A 1 130 ? 4.556   12.444  -35.791 1.00 19.42 ? 142 ILE B CD1 1 
ATOM   898  N N   . CYS A 1 131 ? 4.312   16.701  -31.810 1.00 23.11 ? 143 CYS B N   1 
ATOM   899  C CA  . CYS A 1 131 ? 3.686   17.732  -31.004 1.00 22.62 ? 143 CYS B CA  1 
ATOM   900  C C   . CYS A 1 131 ? 3.203   18.848  -31.903 1.00 22.19 ? 143 CYS B C   1 
ATOM   901  O O   . CYS A 1 131 ? 3.946   19.303  -32.770 1.00 24.55 ? 143 CYS B O   1 
ATOM   902  C CB  . CYS A 1 131 ? 4.669   18.305  -29.995 1.00 26.03 ? 143 CYS B CB  1 
ATOM   903  S SG  . CYS A 1 131 ? 5.428   17.117  -28.863 1.00 26.52 ? 143 CYS B SG  1 
ATOM   904  N N   . GLU A 1 132 ? 1.973   19.300  -31.677 1.00 23.41 ? 144 GLU B N   1 
ATOM   905  C CA  . GLU A 1 132 ? 1.448   20.428  -32.434 1.00 24.15 ? 144 GLU B CA  1 
ATOM   906  C C   . GLU A 1 132 ? 2.209   21.708  -32.102 1.00 24.43 ? 144 GLU B C   1 
ATOM   907  O O   . GLU A 1 132 ? 2.631   21.925  -30.970 1.00 24.98 ? 144 GLU B O   1 
ATOM   908  C CB  . GLU A 1 132 ? -0.041  20.604  -32.153 1.00 24.96 ? 144 GLU B CB  1 
ATOM   909  C CG  . GLU A 1 132 ? -0.839  19.406  -32.576 1.00 27.42 ? 144 GLU B CG  1 
ATOM   910  C CD  . GLU A 1 132 ? -1.013  19.367  -34.088 1.00 40.13 ? 144 GLU B CD  1 
ATOM   911  O OE1 . GLU A 1 132 ? -0.997  20.460  -34.706 1.00 45.30 ? 144 GLU B OE1 1 
ATOM   912  O OE2 . GLU A 1 132 ? -1.120  18.256  -34.668 1.00 36.50 ? 144 GLU B OE2 1 
ATOM   913  N N   . ARG A 1 133 ? 2.395   22.557  -33.106 1.00 28.80 ? 145 ARG B N   1 
ATOM   914  C CA  . ARG A 1 133 ? 3.144   23.793  -32.953 1.00 24.36 ? 145 ARG B CA  1 
ATOM   915  C C   . ARG A 1 133 ? 2.265   24.958  -32.542 1.00 22.99 ? 145 ARG B C   1 
ATOM   916  O O   . ARG A 1 133 ? 2.794   26.014  -32.191 1.00 23.19 ? 145 ARG B O   1 
ATOM   917  C CB  . ARG A 1 133 ? 3.855   24.137  -34.265 1.00 24.74 ? 145 ARG B CB  1 
ATOM   918  C CG  . ARG A 1 133 ? 4.843   23.085  -34.679 1.00 29.01 ? 145 ARG B CG  1 
ATOM   919  C CD  . ARG A 1 133 ? 5.551   23.416  -35.994 1.00 27.13 ? 145 ARG B CD  1 
ATOM   920  N NE  . ARG A 1 133 ? 6.076   24.772  -36.035 1.00 27.14 ? 145 ARG B NE  1 
ATOM   921  C CZ  . ARG A 1 133 ? 7.308   25.099  -35.669 1.00 32.87 ? 145 ARG B CZ  1 
ATOM   922  N NH1 . ARG A 1 133 ? 8.140   24.196  -35.168 1.00 29.74 ? 145 ARG B NH1 1 
ATOM   923  N NH2 . ARG A 1 133 ? 7.704   26.368  -35.777 1.00 30.53 ? 145 ARG B NH2 1 
ATOM   924  N N   . ASN A 1 134 ? 0.945   24.797  -32.606 1.00 22.31 ? 146 ASN B N   1 
ATOM   925  C CA  . ASN A 1 134 ? 0.000   25.787  -32.129 1.00 24.79 ? 146 ASN B CA  1 
ATOM   926  C C   . ASN A 1 134 ? -0.921  25.203  -31.059 1.00 28.95 ? 146 ASN B C   1 
ATOM   927  O O   . ASN A 1 134 ? -1.161  23.987  -31.034 1.00 31.21 ? 146 ASN B O   1 
ATOM   928  C CB  . ASN A 1 134 ? -0.822  26.343  -33.297 1.00 26.63 ? 146 ASN B CB  1 
ATOM   929  C CG  . ASN A 1 134 ? 0.044   27.083  -34.305 1.00 28.84 ? 146 ASN B CG  1 
ATOM   930  O OD1 . ASN A 1 134 ? 0.873   27.915  -33.927 1.00 28.28 ? 146 ASN B OD1 1 
ATOM   931  N ND2 . ASN A 1 134 ? -0.145  26.789  -35.592 1.00 26.82 ? 146 ASN B ND2 1 
ATOM   932  N N   . PRO A 1 135 ? -1.431  26.026  -30.155 1.00 28.50 ? 147 PRO B N   1 
ATOM   933  C CA  . PRO A 1 135 ? -2.198  25.520  -29.020 1.00 26.69 ? 147 PRO B CA  1 
ATOM   934  C C   . PRO A 1 135 ? -3.349  24.642  -29.478 1.00 25.63 ? 147 PRO B C   1 
ATOM   935  O O   . PRO A 1 135 ? -3.944  24.874  -30.549 1.00 29.91 ? 147 PRO B O   1 
ATOM   936  C CB  . PRO A 1 135 ? -2.691  26.785  -28.320 1.00 29.67 ? 147 PRO B CB  1 
ATOM   937  C CG  . PRO A 1 135 ? -1.604  27.799  -28.637 1.00 27.41 ? 147 PRO B CG  1 
ATOM   938  C CD  . PRO A 1 135 ? -1.198  27.488  -30.045 1.00 29.48 ? 147 PRO B CD  1 
ATOM   939  N N   . PRO A 1 136 ? -3.722  23.616  -28.689 1.00 28.28 ? 148 PRO B N   1 
ATOM   940  C CA  . PRO A 1 136 ? -3.215  23.273  -27.353 1.00 26.05 ? 148 PRO B CA  1 
ATOM   941  C C   . PRO A 1 136 ? -1.901  22.516  -27.358 1.00 26.93 ? 148 PRO B C   1 
ATOM   942  O O   . PRO A 1 136 ? -1.569  21.957  -26.328 1.00 30.43 ? 148 PRO B O   1 
ATOM   943  C CB  . PRO A 1 136 ? -4.345  22.416  -26.785 1.00 24.10 ? 148 PRO B CB  1 
ATOM   944  C CG  . PRO A 1 136 ? -4.873  21.673  -27.990 1.00 28.74 ? 148 PRO B CG  1 
ATOM   945  C CD  . PRO A 1 136 ? -4.637  22.576  -29.191 1.00 29.74 ? 148 PRO B CD  1 
ATOM   946  N N   . PHE A 1 137 ? -1.135  22.478  -28.453 1.00 23.85 ? 149 PHE B N   1 
ATOM   947  C CA  . PHE A 1 137 ? 0.177   21.828  -28.464 1.00 23.03 ? 149 PHE B CA  1 
ATOM   948  C C   . PHE A 1 137 ? 0.079   20.332  -28.146 1.00 26.65 ? 149 PHE B C   1 
ATOM   949  O O   . PHE A 1 137 ? 0.999   19.754  -27.547 1.00 23.24 ? 149 PHE B O   1 
ATOM   950  C CB  . PHE A 1 137 ? 1.134   22.493  -27.479 1.00 20.96 ? 149 PHE B CB  1 
ATOM   951  C CG  . PHE A 1 137 ? 1.278   23.961  -27.661 1.00 24.45 ? 149 PHE B CG  1 
ATOM   952  C CD1 . PHE A 1 137 ? 1.985   24.479  -28.722 1.00 25.62 ? 149 PHE B CD1 1 
ATOM   953  C CD2 . PHE A 1 137 ? 0.735   24.834  -26.739 1.00 28.73 ? 149 PHE B CD2 1 
ATOM   954  C CE1 . PHE A 1 137 ? 2.133   25.838  -28.869 1.00 26.52 ? 149 PHE B CE1 1 
ATOM   955  C CE2 . PHE A 1 137 ? 0.882   26.196  -26.878 1.00 25.00 ? 149 PHE B CE2 1 
ATOM   956  C CZ  . PHE A 1 137 ? 1.581   26.700  -27.944 1.00 26.11 ? 149 PHE B CZ  1 
ATOM   957  N N   . THR A 1 138 ? -1.043  19.704  -28.518 1.00 26.75 ? 150 THR B N   1 
ATOM   958  C CA  . THR A 1 138 ? -1.258  18.286  -28.231 1.00 23.27 ? 150 THR B CA  1 
ATOM   959  C C   . THR A 1 138 ? -0.114  17.436  -28.770 1.00 22.14 ? 150 THR B C   1 
ATOM   960  O O   . THR A 1 138 ? 0.329   17.617  -29.908 1.00 23.69 ? 150 THR B O   1 
ATOM   961  C CB  . THR A 1 138 ? -2.573  17.803  -28.851 1.00 23.83 ? 150 THR B CB  1 
ATOM   962  O OG1 . THR A 1 138 ? -3.689  18.455  -28.220 1.00 28.72 ? 150 THR B OG1 1 
ATOM   963  C CG2 . THR A 1 138 ? -2.712  16.300  -28.682 1.00 20.38 ? 150 THR B CG2 1 
ATOM   964  N N   . ALA A 1 139 ? 0.350   16.492  -27.949 1.00 23.30 ? 151 ALA B N   1 
ATOM   965  C CA  . ALA A 1 139 ? 1.428   15.573  -28.304 1.00 23.38 ? 151 ALA B CA  1 
ATOM   966  C C   . ALA A 1 139 ? 0.898   14.147  -28.491 1.00 22.12 ? 151 ALA B C   1 
ATOM   967  O O   . ALA A 1 139 ? 0.228   13.599  -27.608 1.00 21.22 ? 151 ALA B O   1 
ATOM   968  C CB  . ALA A 1 139 ? 2.531   15.606  -27.242 1.00 14.97 ? 151 ALA B CB  1 
ATOM   969  N N   . ARG A 1 140 ? 1.215   13.544  -29.635 1.00 21.75 ? 152 ARG B N   1 
ATOM   970  C CA  . ARG A 1 140 ? 0.805   12.184  -29.962 1.00 22.14 ? 152 ARG B CA  1 
ATOM   971  C C   . ARG A 1 140 ? 2.031   11.282  -30.080 1.00 21.28 ? 152 ARG B C   1 
ATOM   972  O O   . ARG A 1 140 ? 3.124   11.736  -30.432 1.00 21.25 ? 152 ARG B O   1 
ATOM   973  C CB  . ARG A 1 140 ? 0.000   12.149  -31.276 1.00 24.09 ? 152 ARG B CB  1 
ATOM   974  C CG  . ARG A 1 140 ? -1.468  12.553  -31.104 1.00 22.59 ? 152 ARG B CG  1 
ATOM   975  C CD  . ARG A 1 140 ? -2.208  12.762  -32.410 1.00 15.44 ? 152 ARG B CD  1 
ATOM   976  N NE  . ARG A 1 140 ? -3.538  13.311  -32.176 1.00 20.89 ? 152 ARG B NE  1 
ATOM   977  C CZ  . ARG A 1 140 ? -3.803  14.611  -32.107 1.00 20.84 ? 152 ARG B CZ  1 
ATOM   978  N NH1 . ARG A 1 140 ? -2.843  15.517  -32.217 1.00 16.11 ? 152 ARG B NH1 1 
ATOM   979  N NH2 . ARG A 1 140 ? -5.062  15.011  -31.921 1.00 21.28 ? 152 ARG B NH2 1 
ATOM   980  N N   . ILE A 1 141 ? 1.849   9.999   -29.776 1.00 20.60 ? 153 ILE B N   1 
ATOM   981  C CA  . ILE A 1 141 ? 2.946   9.037   -29.759 1.00 22.89 ? 153 ILE B CA  1 
ATOM   982  C C   . ILE A 1 141 ? 2.714   7.959   -30.819 1.00 22.88 ? 153 ILE B C   1 
ATOM   983  O O   . ILE A 1 141 ? 1.585   7.505   -31.032 1.00 21.47 ? 153 ILE B O   1 
ATOM   984  C CB  . ILE A 1 141 ? 3.126   8.411   -28.359 1.00 21.10 ? 153 ILE B CB  1 
ATOM   985  C CG1 . ILE A 1 141 ? 4.381   7.543   -28.327 1.00 22.47 ? 153 ILE B CG1 1 
ATOM   986  C CG2 . ILE A 1 141 ? 1.888   7.624   -27.921 1.00 21.67 ? 153 ILE B CG2 1 
ATOM   987  C CD1 . ILE A 1 141 ? 5.121   7.645   -27.041 1.00 25.46 ? 153 ILE B CD1 1 
ATOM   988  N N   . TYR A 1 142 ? 3.791   7.572   -31.500 1.00 20.70 ? 154 TYR B N   1 
ATOM   989  C CA  . TYR A 1 142 ? 3.765   6.549   -32.535 1.00 23.72 ? 154 TYR B CA  1 
ATOM   990  C C   . TYR A 1 142 ? 4.890   5.569   -32.259 1.00 21.80 ? 154 TYR B C   1 
ATOM   991  O O   . TYR A 1 142 ? 5.901   5.925   -31.657 1.00 23.35 ? 154 TYR B O   1 
ATOM   992  C CB  . TYR A 1 142 ? 3.916   7.151   -33.958 1.00 22.18 ? 154 TYR B CB  1 
ATOM   993  C CG  . TYR A 1 142 ? 2.899   8.220   -34.234 1.00 19.70 ? 154 TYR B CG  1 
ATOM   994  C CD1 . TYR A 1 142 ? 3.080   9.508   -33.750 1.00 20.15 ? 154 TYR B CD1 1 
ATOM   995  C CD2 . TYR A 1 142 ? 1.728   7.931   -34.923 1.00 19.44 ? 154 TYR B CD2 1 
ATOM   996  C CE1 . TYR A 1 142 ? 2.130   10.493  -33.958 1.00 22.55 ? 154 TYR B CE1 1 
ATOM   997  C CE2 . TYR A 1 142 ? 0.768   8.914   -35.146 1.00 20.10 ? 154 TYR B CE2 1 
ATOM   998  C CZ  . TYR A 1 142 ? 0.980   10.197  -34.664 1.00 20.32 ? 154 TYR B CZ  1 
ATOM   999  O OH  . TYR A 1 142 ? 0.039   11.177  -34.875 1.00 17.29 ? 154 TYR B OH  1 
ATOM   1000 N N   . ALA A 1 143 ? 4.703   4.330   -32.687 1.00 24.28 ? 155 ALA B N   1 
ATOM   1001 C CA  . ALA A 1 143 ? 5.718   3.308   -32.496 1.00 26.03 ? 155 ALA B CA  1 
ATOM   1002 C C   . ALA A 1 143 ? 6.767   3.386   -33.600 1.00 27.05 ? 155 ALA B C   1 
ATOM   1003 O O   . ALA A 1 143 ? 6.452   3.689   -34.759 1.00 27.97 ? 155 ALA B O   1 
ATOM   1004 C CB  . ALA A 1 143 ? 5.072   1.923   -32.477 1.00 24.81 ? 155 ALA B CB  1 
ATOM   1005 N N   . ALA A 1 144 ? 8.028   3.121   -33.220 1.00 23.00 ? 156 ALA B N   1 
ATOM   1006 C CA  . ALA A 1 144 ? 9.200   3.109   -34.100 1.00 20.06 ? 156 ALA B CA  1 
ATOM   1007 C C   . ALA A 1 144 ? 9.543   4.500   -34.590 1.00 21.53 ? 156 ALA B C   1 
ATOM   1008 O O   . ALA A 1 144 ? 8.664   5.351   -34.736 1.00 24.55 ? 156 ALA B O   1 
ATOM   1009 C CB  . ALA A 1 144 ? 9.006   2.188   -35.304 1.00 17.84 ? 156 ALA B CB  1 
ATOM   1010 N N   . GLY A 1 145 ? 10.820  4.748   -34.855 1.00 20.08 ? 157 GLY B N   1 
ATOM   1011 C CA  . GLY A 1 145 ? 11.244  6.018   -35.392 1.00 20.97 ? 157 GLY B CA  1 
ATOM   1012 C C   . GLY A 1 145 ? 12.046  5.796   -36.657 1.00 25.28 ? 157 GLY B C   1 
ATOM   1013 O O   . GLY A 1 145 ? 12.356  4.656   -37.026 1.00 25.67 ? 157 GLY B O   1 
ATOM   1014 N N   . PHE A 1 146 ? 12.390  6.905   -37.308 1.00 23.69 ? 158 PHE B N   1 
ATOM   1015 C CA  . PHE A 1 146 ? 13.114  6.848   -38.569 1.00 26.52 ? 158 PHE B CA  1 
ATOM   1016 C C   . PHE A 1 146 ? 14.621  6.755   -38.348 1.00 31.09 ? 158 PHE B C   1 
ATOM   1017 O O   . PHE A 1 146 ? 15.171  7.430   -37.475 1.00 34.90 ? 158 PHE B O   1 
ATOM   1018 C CB  . PHE A 1 146 ? 12.774  8.064   -39.419 1.00 25.16 ? 158 PHE B CB  1 
ATOM   1019 C CG  . PHE A 1 146 ? 11.323  8.170   -39.731 1.00 26.87 ? 158 PHE B CG  1 
ATOM   1020 C CD1 . PHE A 1 146 ? 10.793  7.496   -40.813 1.00 27.42 ? 158 PHE B CD1 1 
ATOM   1021 C CD2 . PHE A 1 146 ? 10.477  8.917   -38.927 1.00 24.61 ? 158 PHE B CD2 1 
ATOM   1022 C CE1 . PHE A 1 146 ? 9.444   7.575   -41.096 1.00 26.95 ? 158 PHE B CE1 1 
ATOM   1023 C CE2 . PHE A 1 146 ? 9.141   8.997   -39.206 1.00 22.97 ? 158 PHE B CE2 1 
ATOM   1024 C CZ  . PHE A 1 146 ? 8.621   8.330   -40.295 1.00 23.84 ? 158 PHE B CZ  1 
ATOM   1025 N N   . ASP A 1 147 ? 15.282  5.902   -39.144 1.00 30.88 ? 159 ASP B N   1 
ATOM   1026 C CA  . ASP A 1 147 ? 16.722  5.679   -39.080 1.00 28.55 ? 159 ASP B CA  1 
ATOM   1027 C C   . ASP A 1 147 ? 17.457  6.862   -39.717 1.00 28.98 ? 159 ASP B C   1 
ATOM   1028 O O   . ASP A 1 147 ? 16.858  7.879   -40.072 1.00 26.55 ? 159 ASP B O   1 
ATOM   1029 C CB  . ASP A 1 147 ? 17.061  4.339   -39.739 1.00 31.95 ? 159 ASP B CB  1 
ATOM   1030 C CG  . ASP A 1 147 ? 16.889  4.343   -41.285 1.00 37.32 ? 159 ASP B CG  1 
ATOM   1031 O OD1 . ASP A 1 147 ? 16.307  5.292   -41.882 1.00 32.13 ? 159 ASP B OD1 1 
ATOM   1032 O OD2 . ASP A 1 147 ? 17.302  3.330   -41.908 1.00 40.57 ? 159 ASP B OD2 1 
ATOM   1033 N N   . SER A 1 148 ? 18.775  6.743   -39.878 1.00 28.80 ? 160 SER B N   1 
ATOM   1034 C CA  . SER A 1 148 ? 19.521  7.826   -40.500 1.00 31.81 ? 160 SER B CA  1 
ATOM   1035 C C   . SER A 1 148 ? 19.256  7.956   -41.998 1.00 31.61 ? 160 SER B C   1 
ATOM   1036 O O   . SER A 1 148 ? 19.680  8.945   -42.606 1.00 28.52 ? 160 SER B O   1 
ATOM   1037 C CB  . SER A 1 148 ? 21.007  7.637   -40.241 1.00 37.38 ? 160 SER B CB  1 
ATOM   1038 O OG  . SER A 1 148 ? 21.348  8.200   -38.988 1.00 36.69 ? 160 SER B OG  1 
ATOM   1039 N N   . SER A 1 149 ? 18.565  7.000   -42.602 1.00 33.19 ? 161 SER B N   1 
ATOM   1040 C CA  . SER A 1 149 ? 18.109  7.106   -43.980 1.00 30.15 ? 161 SER B CA  1 
ATOM   1041 C C   . SER A 1 149 ? 16.717  7.706   -44.070 1.00 29.42 ? 161 SER B C   1 
ATOM   1042 O O   . SER A 1 149 ? 16.179  7.843   -45.176 1.00 30.03 ? 161 SER B O   1 
ATOM   1043 C CB  . SER A 1 149 ? 18.110  5.723   -44.624 1.00 28.29 ? 161 SER B CB  1 
ATOM   1044 O OG  . SER A 1 149 ? 19.408  5.172   -44.547 1.00 36.05 ? 161 SER B OG  1 
ATOM   1045 N N   . LYS A 1 150 ? 16.133  8.051   -42.924 1.00 27.96 ? 162 LYS B N   1 
ATOM   1046 C CA  . LYS A 1 150 ? 14.747  8.485   -42.824 1.00 27.50 ? 162 LYS B CA  1 
ATOM   1047 C C   . LYS A 1 150 ? 13.776  7.368   -43.221 1.00 28.24 ? 162 LYS B C   1 
ATOM   1048 O O   . LYS A 1 150 ? 12.680  7.627   -43.728 1.00 26.18 ? 162 LYS B O   1 
ATOM   1049 C CB  . LYS A 1 150 ? 14.524  9.763   -43.639 1.00 29.12 ? 162 LYS B CB  1 
ATOM   1050 C CG  . LYS A 1 150 ? 15.120  11.022  -42.974 1.00 25.95 ? 162 LYS B CG  1 
ATOM   1051 C CD  . LYS A 1 150 ? 14.817  12.294  -43.761 1.00 29.17 ? 162 LYS B CD  1 
ATOM   1052 C CE  . LYS A 1 150 ? 15.613  13.477  -43.248 1.00 32.54 ? 162 LYS B CE  1 
ATOM   1053 N NZ  . LYS A 1 150 ? 16.748  13.807  -44.151 1.00 37.27 ? 162 LYS B NZ  1 
ATOM   1054 N N   . ASN A 1 151 ? 14.153  6.111   -42.961 1.00 26.38 ? 163 ASN B N   1 
ATOM   1055 C CA  . ASN A 1 151 ? 13.335  4.954   -43.305 1.00 28.60 ? 163 ASN B CA  1 
ATOM   1056 C C   . ASN A 1 151 ? 12.926  4.174   -42.056 1.00 28.17 ? 163 ASN B C   1 
ATOM   1057 O O   . ASN A 1 151 ? 13.727  3.975   -41.136 1.00 28.83 ? 163 ASN B O   1 
ATOM   1058 C CB  . ASN A 1 151 ? 14.088  4.023   -44.271 1.00 31.47 ? 163 ASN B CB  1 
ATOM   1059 C CG  . ASN A 1 151 ? 14.297  4.643   -45.672 1.00 30.04 ? 163 ASN B CG  1 
ATOM   1060 O OD1 . ASN A 1 151 ? 13.600  5.584   -46.071 1.00 26.52 ? 163 ASN B OD1 1 
ATOM   1061 N ND2 . ASN A 1 151 ? 15.247  4.082   -46.430 1.00 27.07 ? 163 ASN B ND2 1 
ATOM   1062 N N   . ILE A 1 152 ? 11.676  3.734   -42.010 1.00 24.19 ? 164 ILE B N   1 
ATOM   1063 C CA  . ILE A 1 152 ? 11.231  2.798   -40.988 1.00 21.96 ? 164 ILE B CA  1 
ATOM   1064 C C   . ILE A 1 152 ? 10.926  1.501   -41.696 1.00 24.01 ? 164 ILE B C   1 
ATOM   1065 O O   . ILE A 1 152 ? 10.406  1.516   -42.820 1.00 26.18 ? 164 ILE B O   1 
ATOM   1066 C CB  . ILE A 1 152 ? 10.005  3.287   -40.202 1.00 22.73 ? 164 ILE B CB  1 
ATOM   1067 C CG1 . ILE A 1 152 ? 10.364  4.529   -39.403 1.00 22.16 ? 164 ILE B CG1 1 
ATOM   1068 C CG2 . ILE A 1 152 ? 9.510   2.218   -39.262 1.00 16.14 ? 164 ILE B CG2 1 
ATOM   1069 C CD1 . ILE A 1 152 ? 9.196   5.125   -38.719 1.00 21.44 ? 164 ILE B CD1 1 
ATOM   1070 N N   . PHE A 1 153 ? 11.302  0.387   -41.060 1.00 23.14 ? 165 PHE B N   1 
ATOM   1071 C CA  . PHE A 1 153 ? 11.153  -0.947  -41.624 1.00 20.32 ? 165 PHE B CA  1 
ATOM   1072 C C   . PHE A 1 153 ? 10.339  -1.773  -40.659 1.00 20.57 ? 165 PHE B C   1 
ATOM   1073 O O   . PHE A 1 153 ? 10.640  -1.816  -39.467 1.00 23.18 ? 165 PHE B O   1 
ATOM   1074 C CB  . PHE A 1 153 ? 12.494  -1.636  -41.872 1.00 19.71 ? 165 PHE B CB  1 
ATOM   1075 C CG  . PHE A 1 153 ? 13.414  -0.881  -42.772 1.00 20.49 ? 165 PHE B CG  1 
ATOM   1076 C CD1 . PHE A 1 153 ? 13.365  -1.054  -44.136 1.00 21.63 ? 165 PHE B CD1 1 
ATOM   1077 C CD2 . PHE A 1 153 ? 14.339  -0.003  -42.249 1.00 22.55 ? 165 PHE B CD2 1 
ATOM   1078 C CE1 . PHE A 1 153 ? 14.228  -0.365  -44.969 1.00 23.25 ? 165 PHE B CE1 1 
ATOM   1079 C CE2 . PHE A 1 153 ? 15.192  0.704   -43.073 1.00 26.64 ? 165 PHE B CE2 1 
ATOM   1080 C CZ  . PHE A 1 153 ? 15.137  0.520   -44.439 1.00 26.53 ? 165 PHE B CZ  1 
ATOM   1081 N N   . LEU A 1 154 ? 9.329   -2.428  -41.178 1.00 28.50 ? 166 LEU B N   1 
ATOM   1082 C CA  . LEU A 1 154 ? 8.549   -3.413  -40.454 1.00 28.33 ? 166 LEU B CA  1 
ATOM   1083 C C   . LEU A 1 154 ? 8.740   -4.733  -41.198 1.00 29.07 ? 166 LEU B C   1 
ATOM   1084 O O   . LEU A 1 154 ? 8.223   -4.910  -42.304 1.00 26.76 ? 166 LEU B O   1 
ATOM   1085 C CB  . LEU A 1 154 ? 7.094   -2.959  -40.401 1.00 29.55 ? 166 LEU B CB  1 
ATOM   1086 C CG  . LEU A 1 154 ? 6.288   -3.152  -39.126 1.00 30.79 ? 166 LEU B CG  1 
ATOM   1087 C CD1 . LEU A 1 154 ? 6.769   -2.205  -38.065 1.00 32.17 ? 166 LEU B CD1 1 
ATOM   1088 C CD2 . LEU A 1 154 ? 4.842   -2.890  -39.439 1.00 30.57 ? 166 LEU B CD2 1 
ATOM   1089 N N   . GLY A 1 155 ? 9.525   -5.631  -40.613 1.00 34.50 ? 167 GLY B N   1 
ATOM   1090 C CA  . GLY A 1 155 ? 9.963   -6.853  -41.275 1.00 32.76 ? 167 GLY B CA  1 
ATOM   1091 C C   . GLY A 1 155 ? 8.854   -7.882  -41.416 1.00 30.83 ? 167 GLY B C   1 
ATOM   1092 O O   . GLY A 1 155 ? 7.737   -7.720  -40.924 1.00 31.65 ? 167 GLY B O   1 
ATOM   1093 N N   . GLU A 1 156 ? 9.186   -8.977  -42.112 1.00 34.74 ? 168 GLU B N   1 
ATOM   1094 C CA  . GLU A 1 156 ? 8.181   -9.984  -42.475 1.00 38.90 ? 168 GLU B CA  1 
ATOM   1095 C C   . GLU A 1 156 ? 7.483   -10.539 -41.237 1.00 36.57 ? 168 GLU B C   1 
ATOM   1096 O O   . GLU A 1 156 ? 6.253   -10.637 -41.191 1.00 32.38 ? 168 GLU B O   1 
ATOM   1097 C CB  . GLU A 1 156 ? 8.847   -11.112 -43.278 1.00 40.46 ? 168 GLU B CB  1 
ATOM   1098 C CG  . GLU A 1 156 ? 8.213   -12.524 -43.179 1.00 49.08 ? 168 GLU B CG  1 
ATOM   1099 C CD  . GLU A 1 156 ? 7.098   -12.816 -44.208 1.00 52.89 ? 168 GLU B CD  1 
ATOM   1100 O OE1 . GLU A 1 156 ? 6.075   -13.441 -43.838 1.00 59.85 ? 168 GLU B OE1 1 
ATOM   1101 O OE2 . GLU A 1 156 ? 7.266   -12.456 -45.392 1.00 51.99 ? 168 GLU B OE2 1 
ATOM   1102 N N   . LYS A 1 157 ? 8.258   -10.869 -40.207 1.00 38.89 ? 169 LYS B N   1 
ATOM   1103 C CA  . LYS A 1 157 ? 7.734   -11.559 -39.034 1.00 40.90 ? 169 LYS B CA  1 
ATOM   1104 C C   . LYS A 1 157 ? 6.882   -10.657 -38.132 1.00 41.47 ? 169 LYS B C   1 
ATOM   1105 O O   . LYS A 1 157 ? 6.090   -11.176 -37.341 1.00 35.19 ? 169 LYS B O   1 
ATOM   1106 C CB  . LYS A 1 157 ? 8.903   -12.192 -38.255 1.00 36.84 ? 169 LYS B CB  1 
ATOM   1107 C CG  . LYS A 1 157 ? 10.103  -11.257 -38.018 1.00 41.67 ? 169 LYS B CG  1 
ATOM   1108 C CD  . LYS A 1 157 ? 10.913  -11.032 -39.294 1.00 30.16 ? 169 LYS B CD  1 
ATOM   1109 C CE  . LYS A 1 157 ? 12.281  -10.531 -38.990 1.00 29.46 ? 169 LYS B CE  1 
ATOM   1110 N NZ  . LYS A 1 157 ? 12.926  -10.289 -40.274 1.00 23.68 ? 169 LYS B NZ  1 
ATOM   1111 N N   . ALA A 1 158 ? 7.009   -9.331  -38.231 1.00 43.11 ? 170 ALA B N   1 
ATOM   1112 C CA  . ALA A 1 158 ? 6.221   -8.444  -37.382 1.00 33.29 ? 170 ALA B CA  1 
ATOM   1113 C C   . ALA A 1 158 ? 4.750   -8.452  -37.797 1.00 29.68 ? 170 ALA B C   1 
ATOM   1114 O O   . ALA A 1 158 ? 4.376   -8.961  -38.850 1.00 35.73 ? 170 ALA B O   1 
ATOM   1115 C CB  . ALA A 1 158 ? 6.776   -7.025  -37.432 1.00 33.39 ? 170 ALA B CB  1 
ATOM   1116 N N   . ALA A 1 159 ? 3.908   -7.886  -36.944 1.00 28.36 ? 171 ALA B N   1 
ATOM   1117 C CA  . ALA A 1 159 ? 2.470   -7.898  -37.180 1.00 29.50 ? 171 ALA B CA  1 
ATOM   1118 C C   . ALA A 1 159 ? 2.049   -6.694  -38.017 1.00 32.43 ? 171 ALA B C   1 
ATOM   1119 O O   . ALA A 1 159 ? 2.417   -5.555  -37.717 1.00 34.63 ? 171 ALA B O   1 
ATOM   1120 C CB  . ALA A 1 159 ? 1.718   -7.898  -35.849 1.00 28.84 ? 171 ALA B CB  1 
ATOM   1121 N N   . LYS A 1 160 ? 1.284   -6.937  -39.072 1.00 29.40 ? 172 LYS B N   1 
ATOM   1122 C CA  . LYS A 1 160 ? 0.735   -5.841  -39.851 1.00 26.47 ? 172 LYS B CA  1 
ATOM   1123 C C   . LYS A 1 160 ? -0.674  -6.219  -40.272 1.00 31.47 ? 172 LYS B C   1 
ATOM   1124 O O   . LYS A 1 160 ? -1.126  -7.353  -40.065 1.00 34.03 ? 172 LYS B O   1 
ATOM   1125 C CB  . LYS A 1 160 ? 1.599   -5.519  -41.066 1.00 23.59 ? 172 LYS B CB  1 
ATOM   1126 C CG  . LYS A 1 160 ? 2.084   -6.735  -41.796 1.00 25.87 ? 172 LYS B CG  1 
ATOM   1127 C CD  . LYS A 1 160 ? 3.419   -6.479  -42.471 1.00 32.44 ? 172 LYS B CD  1 
ATOM   1128 C CE  . LYS A 1 160 ? 4.609   -6.798  -41.549 1.00 32.84 ? 172 LYS B CE  1 
ATOM   1129 N NZ  . LYS A 1 160 ? 5.129   -8.204  -41.708 1.00 31.08 ? 172 LYS B NZ  1 
ATOM   1130 N N   . TRP A 1 161 ? -1.381  -5.243  -40.831 1.00 27.58 ? 173 TRP B N   1 
ATOM   1131 C CA  . TRP A 1 161 ? -2.743  -5.450  -41.299 1.00 28.19 ? 173 TRP B CA  1 
ATOM   1132 C C   . TRP A 1 161 ? -3.095  -4.295  -42.220 1.00 32.14 ? 173 TRP B C   1 
ATOM   1133 O O   . TRP A 1 161 ? -2.375  -3.298  -42.304 1.00 36.16 ? 173 TRP B O   1 
ATOM   1134 C CB  . TRP A 1 161 ? -3.744  -5.567  -40.132 1.00 32.60 ? 173 TRP B CB  1 
ATOM   1135 C CG  . TRP A 1 161 ? -3.602  -4.488  -39.130 1.00 29.86 ? 173 TRP B CG  1 
ATOM   1136 C CD1 . TRP A 1 161 ? -4.251  -3.293  -39.111 1.00 32.15 ? 173 TRP B CD1 1 
ATOM   1137 C CD2 . TRP A 1 161 ? -2.715  -4.480  -38.021 1.00 29.46 ? 173 TRP B CD2 1 
ATOM   1138 N NE1 . TRP A 1 161 ? -3.828  -2.538  -38.042 1.00 29.08 ? 173 TRP B NE1 1 
ATOM   1139 C CE2 . TRP A 1 161 ? -2.880  -3.249  -37.361 1.00 28.63 ? 173 TRP B CE2 1 
ATOM   1140 C CE3 . TRP A 1 161 ? -1.790  -5.398  -37.517 1.00 31.44 ? 173 TRP B CE3 1 
ATOM   1141 C CZ2 . TRP A 1 161 ? -2.159  -2.917  -36.230 1.00 28.95 ? 173 TRP B CZ2 1 
ATOM   1142 C CZ3 . TRP A 1 161 ? -1.075  -5.068  -36.396 1.00 29.03 ? 173 TRP B CZ3 1 
ATOM   1143 C CH2 . TRP A 1 161 ? -1.267  -3.839  -35.757 1.00 29.52 ? 173 TRP B CH2 1 
ATOM   1144 N N   . LYS A 1 162 ? -4.190  -4.462  -42.943 1.00 31.62 ? 174 LYS B N   1 
ATOM   1145 C CA  . LYS A 1 162 ? -4.776  -3.380  -43.705 1.00 37.74 ? 174 LYS B CA  1 
ATOM   1146 C C   . LYS A 1 162 ? -5.915  -2.816  -42.856 1.00 46.63 ? 174 LYS B C   1 
ATOM   1147 O O   . LYS A 1 162 ? -6.570  -3.568  -42.130 1.00 45.94 ? 174 LYS B O   1 
ATOM   1148 C CB  . LYS A 1 162 ? -5.258  -3.890  -45.069 1.00 38.71 ? 174 LYS B CB  1 
ATOM   1149 C CG  . LYS A 1 162 ? -4.149  -4.080  -46.117 1.00 35.05 ? 174 LYS B CG  1 
ATOM   1150 C CD  . LYS A 1 162 ? -4.142  -2.913  -47.110 1.00 42.96 ? 174 LYS B CD  1 
ATOM   1151 C CE  . LYS A 1 162 ? -4.971  -3.194  -48.373 1.00 41.24 ? 174 LYS B CE  1 
ATOM   1152 N NZ  . LYS A 1 162 ? -4.451  -2.457  -49.564 1.00 40.70 ? 174 LYS B NZ  1 
ATOM   1153 N N   . THR A 1 163 ? -6.108  -1.488  -42.892 1.00 51.57 ? 175 THR B N   1 
ATOM   1154 C CA  . THR A 1 163 ? -7.086  -0.823  -42.030 1.00 48.52 ? 175 THR B CA  1 
ATOM   1155 C C   . THR A 1 163 ? -8.475  -0.830  -42.674 1.00 56.45 ? 175 THR B C   1 
ATOM   1156 O O   . THR A 1 163 ? -8.688  -1.362  -43.769 1.00 58.58 ? 175 THR B O   1 
ATOM   1157 C CB  . THR A 1 163 ? -6.655  0.617   -41.704 1.00 50.85 ? 175 THR B CB  1 
ATOM   1158 O OG1 . THR A 1 163 ? -6.484  1.388   -42.908 1.00 50.51 ? 175 THR B OG1 1 
ATOM   1159 C CG2 . THR A 1 163 ? -5.369  0.648   -40.884 1.00 45.17 ? 175 THR B CG2 1 
ATOM   1160 N N   . SER A 1 164 ? -9.446  -0.243  -41.967 1.00 60.64 ? 176 SER B N   1 
ATOM   1161 C CA  . SER A 1 164 ? -10.737 0.059   -42.582 1.00 59.91 ? 176 SER B CA  1 
ATOM   1162 C C   . SER A 1 164 ? -10.559 0.949   -43.813 1.00 59.91 ? 176 SER B C   1 
ATOM   1163 O O   . SER A 1 164 ? -11.200 0.738   -44.849 1.00 57.22 ? 176 SER B O   1 
ATOM   1164 C CB  . SER A 1 164 ? -11.641 0.739   -41.559 1.00 56.72 ? 176 SER B CB  1 
ATOM   1165 O OG  . SER A 1 164 ? -10.908 1.725   -40.858 1.00 56.93 ? 176 SER B OG  1 
ATOM   1166 N N   . ASP A 1 165 ? -9.686  1.953   -43.711 1.00 54.50 ? 177 ASP B N   1 
ATOM   1167 C CA  . ASP A 1 165 ? -9.306  2.863   -44.789 1.00 55.16 ? 177 ASP B CA  1 
ATOM   1168 C C   . ASP A 1 165 ? -8.459  2.132   -45.837 1.00 63.27 ? 177 ASP B C   1 
ATOM   1169 O O   . ASP A 1 165 ? -8.069  2.711   -46.848 1.00 59.78 ? 177 ASP B O   1 
ATOM   1170 C CB  . ASP A 1 165 ? -8.552  4.037   -44.145 1.00 57.22 ? 177 ASP B CB  1 
ATOM   1171 C CG  . ASP A 1 165 ? -8.261  5.176   -45.112 1.00 73.51 ? 177 ASP B CG  1 
ATOM   1172 O OD1 . ASP A 1 165 ? -8.593  5.108   -46.328 1.00 74.90 ? 177 ASP B OD1 1 
ATOM   1173 O OD2 . ASP A 1 165 ? -7.674  6.176   -44.637 1.00 79.64 ? 177 ASP B OD2 1 
ATOM   1174 N N   . GLY A 1 166 ? -8.192  0.853   -45.608 1.00 61.98 ? 178 GLY B N   1 
ATOM   1175 C CA  . GLY A 1 166 ? -7.389  0.074   -46.516 1.00 55.75 ? 178 GLY B CA  1 
ATOM   1176 C C   . GLY A 1 166 ? -5.939  0.527   -46.532 1.00 54.19 ? 178 GLY B C   1 
ATOM   1177 O O   . GLY A 1 166 ? -5.276  0.542   -47.588 1.00 55.99 ? 178 GLY B O   1 
ATOM   1178 N N   . GLN A 1 167 ? -5.428  0.929   -45.376 1.00 50.71 ? 179 GLN B N   1 
ATOM   1179 C CA  . GLN A 1 167 ? -4.083  1.462   -45.263 1.00 48.97 ? 179 GLN B CA  1 
ATOM   1180 C C   . GLN A 1 167 ? -3.197  0.471   -44.523 1.00 43.86 ? 179 GLN B C   1 
ATOM   1181 O O   . GLN A 1 167 ? -3.677  -0.441  -43.853 1.00 45.55 ? 179 GLN B O   1 
ATOM   1182 C CB  . GLN A 1 167 ? -4.110  2.821   -44.551 1.00 47.52 ? 179 GLN B CB  1 
ATOM   1183 C CG  . GLN A 1 167 ? -4.021  3.940   -45.544 1.00 52.01 ? 179 GLN B CG  1 
ATOM   1184 C CD  . GLN A 1 167 ? -3.129  3.545   -46.720 1.00 60.37 ? 179 GLN B CD  1 
ATOM   1185 O OE1 . GLN A 1 167 ? -1.930  3.270   -46.542 1.00 54.26 ? 179 GLN B OE1 1 
ATOM   1186 N NE2 . GLN A 1 167 ? -3.724  3.445   -47.916 1.00 53.81 ? 179 GLN B NE2 1 
ATOM   1187 N N   . MET A 1 168 ? -1.895  0.649   -44.646 1.00 37.90 ? 180 MET B N   1 
ATOM   1188 C CA  . MET A 1 168 ? -0.997  -0.188  -43.873 1.00 35.33 ? 180 MET B CA  1 
ATOM   1189 C C   . MET A 1 168 ? -0.901  0.298   -42.423 1.00 40.87 ? 180 MET B C   1 
ATOM   1190 O O   . MET A 1 168 ? -0.976  1.499   -42.131 1.00 39.58 ? 180 MET B O   1 
ATOM   1191 C CB  . MET A 1 168 ? 0.406   -0.222  -44.502 1.00 34.98 ? 180 MET B CB  1 
ATOM   1192 C CG  . MET A 1 168 ? 0.671   -1.344  -45.527 1.00 34.50 ? 180 MET B CG  1 
ATOM   1193 S SD  . MET A 1 168 ? -0.412  -2.800  -45.477 1.00 29.72 ? 180 MET B SD  1 
ATOM   1194 C CE  . MET A 1 168 ? 0.342   -3.850  -44.221 1.00 27.13 ? 180 MET B CE  1 
ATOM   1195 N N   . ASP A 1 169 ? -0.733  -0.658  -41.509 1.00 35.52 ? 181 ASP B N   1 
ATOM   1196 C CA  . ASP A 1 169 ? -0.413  -0.360  -40.120 1.00 34.84 ? 181 ASP B CA  1 
ATOM   1197 C C   . ASP A 1 169 ? 0.234   -1.608  -39.554 1.00 28.05 ? 181 ASP B C   1 
ATOM   1198 O O   . ASP A 1 169 ? 0.087   -2.694  -40.112 1.00 28.05 ? 181 ASP B O   1 
ATOM   1199 C CB  . ASP A 1 169 ? -1.664  0.046   -39.320 1.00 41.89 ? 181 ASP B CB  1 
ATOM   1200 C CG  . ASP A 1 169 ? -1.335  0.788   -38.004 1.00 38.42 ? 181 ASP B CG  1 
ATOM   1201 O OD1 . ASP A 1 169 ? -0.138  1.035   -37.712 1.00 34.20 ? 181 ASP B OD1 1 
ATOM   1202 O OD2 . ASP A 1 169 ? -2.301  1.132   -37.275 1.00 34.51 ? 181 ASP B OD2 1 
ATOM   1203 N N   . GLY A 1 170 ? 0.957   -1.446  -38.450 1.00 27.96 ? 182 GLY B N   1 
ATOM   1204 C CA  . GLY A 1 170 ? 1.638   -2.590  -37.871 1.00 28.79 ? 182 GLY B CA  1 
ATOM   1205 C C   . GLY A 1 170 ? 2.166   -2.302  -36.483 1.00 30.61 ? 182 GLY B C   1 
ATOM   1206 O O   . GLY A 1 170 ? 2.060   -1.186  -35.967 1.00 31.14 ? 182 GLY B O   1 
ATOM   1207 N N   . LEU A 1 171 ? 2.738   -3.346  -35.881 1.00 28.03 ? 183 LEU B N   1 
ATOM   1208 C CA  . LEU A 1 171 ? 3.346   -3.288  -34.560 1.00 26.35 ? 183 LEU B CA  1 
ATOM   1209 C C   . LEU A 1 171 ? 4.839   -3.523  -34.685 1.00 27.66 ? 183 LEU B C   1 
ATOM   1210 O O   . LEU A 1 171 ? 5.289   -4.266  -35.561 1.00 32.54 ? 183 LEU B O   1 
ATOM   1211 C CB  . LEU A 1 171 ? 2.773   -4.352  -33.599 1.00 26.91 ? 183 LEU B CB  1 
ATOM   1212 C CG  . LEU A 1 171 ? 1.295   -4.262  -33.225 1.00 24.53 ? 183 LEU B CG  1 
ATOM   1213 C CD1 . LEU A 1 171 ? 0.994   -5.225  -32.124 1.00 23.63 ? 183 LEU B CD1 1 
ATOM   1214 C CD2 . LEU A 1 171 ? 0.918   -2.847  -32.831 1.00 24.94 ? 183 LEU B CD2 1 
ATOM   1215 N N   . THR A 1 172 ? 5.606   -2.902  -33.796 1.00 23.88 ? 184 THR B N   1 
ATOM   1216 C CA  . THR A 1 172 ? 7.000   -3.286  -33.675 1.00 25.39 ? 184 THR B CA  1 
ATOM   1217 C C   . THR A 1 172 ? 7.082   -4.693  -33.091 1.00 29.77 ? 184 THR B C   1 
ATOM   1218 O O   . THR A 1 172 ? 6.071   -5.333  -32.782 1.00 33.75 ? 184 THR B O   1 
ATOM   1219 C CB  . THR A 1 172 ? 7.771   -2.271  -32.830 1.00 27.85 ? 184 THR B CB  1 
ATOM   1220 O OG1 . THR A 1 172 ? 7.225   -2.200  -31.505 1.00 27.34 ? 184 THR B OG1 1 
ATOM   1221 C CG2 . THR A 1 172 ? 7.726   -0.909  -33.479 1.00 28.65 ? 184 THR B CG2 1 
ATOM   1222 N N   . THR A 1 173 ? 8.303   -5.196  -32.941 1.00 29.59 ? 185 THR B N   1 
ATOM   1223 C CA  . THR A 1 173 ? 8.452   -6.544  -32.409 1.00 33.96 ? 185 THR B CA  1 
ATOM   1224 C C   . THR A 1 173 ? 8.033   -6.601  -30.945 1.00 34.62 ? 185 THR B C   1 
ATOM   1225 O O   . THR A 1 173 ? 7.083   -7.307  -30.583 1.00 33.54 ? 185 THR B O   1 
ATOM   1226 C CB  . THR A 1 173 ? 9.890   -7.034  -32.594 1.00 38.24 ? 185 THR B CB  1 
ATOM   1227 O OG1 . THR A 1 173 ? 10.219  -7.031  -33.997 1.00 38.63 ? 185 THR B OG1 1 
ATOM   1228 C CG2 . THR A 1 173 ? 10.053  -8.437  -32.004 1.00 29.06 ? 185 THR B CG2 1 
ATOM   1229 N N   . ASN A 1 174 ? 8.729   -5.858  -30.087 1.00 35.38 ? 186 ASN B N   1 
ATOM   1230 C CA  . ASN A 1 174 ? 8.401   -5.860  -28.667 1.00 34.09 ? 186 ASN B CA  1 
ATOM   1231 C C   . ASN A 1 174 ? 7.277   -4.893  -28.318 1.00 35.47 ? 186 ASN B C   1 
ATOM   1232 O O   . ASN A 1 174 ? 6.811   -4.911  -27.172 1.00 38.05 ? 186 ASN B O   1 
ATOM   1233 C CB  . ASN A 1 174 ? 9.643   -5.518  -27.825 1.00 33.08 ? 186 ASN B CB  1 
ATOM   1234 C CG  . ASN A 1 174 ? 10.776  -6.524  -27.997 1.00 38.41 ? 186 ASN B CG  1 
ATOM   1235 O OD1 . ASN A 1 174 ? 10.556  -7.720  -28.208 1.00 38.36 ? 186 ASN B OD1 1 
ATOM   1236 N ND2 . ASN A 1 174 ? 12.002  -6.029  -27.923 1.00 37.55 ? 186 ASN B ND2 1 
ATOM   1237 N N   . GLY A 1 175 ? 6.847   -4.045  -29.258 1.00 28.30 ? 187 GLY B N   1 
ATOM   1238 C CA  . GLY A 1 175 ? 5.750   -3.120  -29.020 1.00 26.28 ? 187 GLY B CA  1 
ATOM   1239 C C   . GLY A 1 175 ? 6.083   -1.882  -28.195 1.00 30.74 ? 187 GLY B C   1 
ATOM   1240 O O   . GLY A 1 175 ? 6.981   -1.892  -27.339 1.00 28.34 ? 187 GLY B O   1 
ATOM   1241 N N   . VAL A 1 176 ? 5.357   -0.800  -28.455 1.00 28.05 ? 188 VAL B N   1 
ATOM   1242 C CA  . VAL A 1 176 ? 5.412   0.406   -27.645 1.00 23.66 ? 188 VAL B CA  1 
ATOM   1243 C C   . VAL A 1 176 ? 4.158   0.427   -26.786 1.00 25.94 ? 188 VAL B C   1 
ATOM   1244 O O   . VAL A 1 176 ? 3.037   0.309   -27.302 1.00 26.18 ? 188 VAL B O   1 
ATOM   1245 C CB  . VAL A 1 176 ? 5.529   1.668   -28.518 1.00 28.28 ? 188 VAL B CB  1 
ATOM   1246 C CG1 . VAL A 1 176 ? 5.052   2.905   -27.766 1.00 25.44 ? 188 VAL B CG1 1 
ATOM   1247 C CG2 . VAL A 1 176 ? 6.961   1.853   -28.986 1.00 28.94 ? 188 VAL B CG2 1 
ATOM   1248 N N   . LEU A 1 177 ? 4.351   0.565   -25.476 1.00 28.42 ? 189 LEU B N   1 
ATOM   1249 C CA  . LEU A 1 177 ? 3.315   0.343   -24.474 1.00 26.63 ? 189 LEU B CA  1 
ATOM   1250 C C   . LEU A 1 177 ? 3.060   1.642   -23.719 1.00 23.98 ? 189 LEU B C   1 
ATOM   1251 O O   . LEU A 1 177 ? 4.000   2.239   -23.184 1.00 26.34 ? 189 LEU B O   1 
ATOM   1252 C CB  . LEU A 1 177 ? 3.757   -0.786  -23.535 1.00 24.08 ? 189 LEU B CB  1 
ATOM   1253 C CG  . LEU A 1 177 ? 3.005   -2.099  -23.748 1.00 25.71 ? 189 LEU B CG  1 
ATOM   1254 C CD1 . LEU A 1 177 ? 2.947   -2.409  -25.224 1.00 24.93 ? 189 LEU B CD1 1 
ATOM   1255 C CD2 . LEU A 1 177 ? 3.707   -3.223  -23.021 1.00 26.23 ? 189 LEU B CD2 1 
ATOM   1256 N N   . VAL A 1 178 ? 1.799   2.082   -23.681 1.00 22.86 ? 190 VAL B N   1 
ATOM   1257 C CA  . VAL A 1 178 ? 1.425   3.359   -23.070 1.00 25.61 ? 190 VAL B CA  1 
ATOM   1258 C C   . VAL A 1 178 ? 0.213   3.160   -22.164 1.00 25.74 ? 190 VAL B C   1 
ATOM   1259 O O   . VAL A 1 178 ? -0.773  2.531   -22.561 1.00 29.45 ? 190 VAL B O   1 
ATOM   1260 C CB  . VAL A 1 178 ? 1.110   4.434   -24.128 1.00 19.27 ? 190 VAL B CB  1 
ATOM   1261 C CG1 . VAL A 1 178 ? 0.344   5.581   -23.501 1.00 18.56 ? 190 VAL B CG1 1 
ATOM   1262 C CG2 . VAL A 1 178 ? 2.372   4.937   -24.768 1.00 18.87 ? 190 VAL B CG2 1 
ATOM   1263 N N   . MET A 1 179 ? 0.260   3.735   -20.969 1.00 23.00 ? 191 MET B N   1 
ATOM   1264 C CA  . MET A 1 179 ? -0.906  3.792   -20.095 1.00 28.17 ? 191 MET B CA  1 
ATOM   1265 C C   . MET A 1 179 ? -1.163  5.244   -19.700 1.00 27.55 ? 191 MET B C   1 
ATOM   1266 O O   . MET A 1 179 ? -0.301  5.880   -19.089 1.00 27.93 ? 191 MET B O   1 
ATOM   1267 C CB  . MET A 1 179 ? -0.696  2.909   -18.858 1.00 28.63 ? 191 MET B CB  1 
ATOM   1268 C CG  . MET A 1 179 ? -1.717  3.106   -17.731 1.00 27.97 ? 191 MET B CG  1 
ATOM   1269 S SD  . MET A 1 179 ? -1.177  2.402   -16.142 1.00 24.43 ? 191 MET B SD  1 
ATOM   1270 C CE  . MET A 1 179 ? -2.337  1.027   -15.952 1.00 35.94 ? 191 MET B CE  1 
ATOM   1271 N N   . HIS A 1 180 ? -2.346  5.776   -20.060 1.00 25.28 ? 192 HIS B N   1 
ATOM   1272 C CA  . HIS A 1 180 ? -2.651  7.151   -19.702 1.00 25.68 ? 192 HIS B CA  1 
ATOM   1273 C C   . HIS A 1 180 ? -3.250  7.212   -18.314 1.00 30.41 ? 192 HIS B C   1 
ATOM   1274 O O   . HIS A 1 180 ? -3.728  6.202   -17.793 1.00 34.95 ? 192 HIS B O   1 
ATOM   1275 C CB  . HIS A 1 180 ? -3.647  7.751   -20.682 1.00 30.43 ? 192 HIS B CB  1 
ATOM   1276 C CG  . HIS A 1 180 ? -3.142  7.834   -22.078 1.00 28.74 ? 192 HIS B CG  1 
ATOM   1277 N ND1 . HIS A 1 180 ? -1.857  8.229   -22.373 1.00 25.96 ? 192 HIS B ND1 1 
ATOM   1278 C CD2 . HIS A 1 180 ? -3.746  7.587   -23.260 1.00 26.28 ? 192 HIS B CD2 1 
ATOM   1279 C CE1 . HIS A 1 180 ? -1.688  8.218   -23.680 1.00 22.38 ? 192 HIS B CE1 1 
ATOM   1280 N NE2 . HIS A 1 180 ? -2.819  7.830   -24.240 1.00 28.06 ? 192 HIS B NE2 1 
ATOM   1281 N N   . PRO A 1 181 ? -3.269  8.396   -17.687 1.00 35.18 ? 193 PRO B N   1 
ATOM   1282 C CA  . PRO A 1 181 ? -4.027  8.515   -16.425 1.00 32.32 ? 193 PRO B CA  1 
ATOM   1283 C C   . PRO A 1 181 ? -5.503  8.208   -16.609 1.00 32.83 ? 193 PRO B C   1 
ATOM   1284 O O   . PRO A 1 181 ? -6.098  7.526   -15.766 1.00 35.57 ? 193 PRO B O   1 
ATOM   1285 C CB  . PRO A 1 181 ? -3.789  9.972   -16.012 1.00 21.47 ? 193 PRO B CB  1 
ATOM   1286 C CG  . PRO A 1 181 ? -2.500  10.334  -16.670 1.00 22.38 ? 193 PRO B CG  1 
ATOM   1287 C CD  . PRO A 1 181 ? -2.512  9.627   -17.992 1.00 26.17 ? 193 PRO B CD  1 
ATOM   1288 N N   . ARG A 1 182 ? -6.105  8.678   -17.706 1.00 33.77 ? 194 ARG B N   1 
ATOM   1289 C CA  . ARG A 1 182 ? -7.530  8.522   -17.979 1.00 36.24 ? 194 ARG B CA  1 
ATOM   1290 C C   . ARG A 1 182 ? -7.720  7.880   -19.341 1.00 33.12 ? 194 ARG B C   1 
ATOM   1291 O O   . ARG A 1 182 ? -6.852  7.988   -20.208 1.00 32.01 ? 194 ARG B O   1 
ATOM   1292 C CB  . ARG A 1 182 ? -8.255  9.866   -17.966 1.00 33.39 ? 194 ARG B CB  1 
ATOM   1293 C CG  . ARG A 1 182 ? -8.105  10.627  -16.689 1.00 28.86 ? 194 ARG B CG  1 
ATOM   1294 C CD  . ARG A 1 182 ? -9.446  10.738  -16.061 1.00 35.27 ? 194 ARG B CD  1 
ATOM   1295 N NE  . ARG A 1 182 ? -9.747  9.556   -15.264 1.00 41.78 ? 194 ARG B NE  1 
ATOM   1296 C CZ  . ARG A 1 182 ? -10.940 9.298   -14.745 1.00 46.03 ? 194 ARG B CZ  1 
ATOM   1297 N NH1 . ARG A 1 182 ? -11.974 10.091  -14.973 1.00 43.02 ? 194 ARG B NH1 1 
ATOM   1298 N NH2 . ARG A 1 182 ? -11.099 8.220   -13.977 1.00 47.82 ? 194 ARG B NH2 1 
ATOM   1299 N N   . ASN A 1 183 ? -8.862  7.212   -19.532 1.00 34.58 ? 195 ASN B N   1 
ATOM   1300 C CA  . ASN A 1 183 ? -9.147  6.670   -20.862 1.00 41.74 ? 195 ASN B CA  1 
ATOM   1301 C C   . ASN A 1 183 ? -9.687  7.748   -21.800 1.00 39.11 ? 195 ASN B C   1 
ATOM   1302 O O   . ASN A 1 183 ? -9.467  7.682   -23.018 1.00 32.55 ? 195 ASN B O   1 
ATOM   1303 C CB  . ASN A 1 183 ? -10.100 5.461   -20.775 1.00 39.32 ? 195 ASN B CB  1 
ATOM   1304 C CG  . ASN A 1 183 ? -11.512 5.819   -20.313 1.00 41.65 ? 195 ASN B CG  1 
ATOM   1305 O OD1 . ASN A 1 183 ? -11.826 6.971   -20.001 1.00 41.21 ? 195 ASN B OD1 1 
ATOM   1306 N ND2 . ASN A 1 183 ? -12.373 4.804   -20.258 1.00 43.64 ? 195 ASN B ND2 1 
ATOM   1307 N N   . GLY A 1 184 ? -10.341 8.759   -21.242 1.00 41.00 ? 196 GLY B N   1 
ATOM   1308 C CA  . GLY A 1 184 ? -10.859 9.863   -22.017 1.00 37.40 ? 196 GLY B CA  1 
ATOM   1309 C C   . GLY A 1 184 ? -11.320 10.971  -21.097 1.00 41.01 ? 196 GLY B C   1 
ATOM   1310 O O   . GLY A 1 184 ? -11.010 10.985  -19.901 1.00 40.86 ? 196 GLY B O   1 
ATOM   1311 N N   . PHE A 1 185 ? -12.069 11.915  -21.675 1.00 40.11 ? 197 PHE B N   1 
ATOM   1312 C CA  . PHE A 1 185 ? -12.605 13.054  -20.933 1.00 42.00 ? 197 PHE B CA  1 
ATOM   1313 C C   . PHE A 1 185 ? -14.100 13.187  -21.242 1.00 44.36 ? 197 PHE B C   1 
ATOM   1314 O O   . PHE A 1 185 ? -14.551 14.150  -21.870 1.00 45.66 ? 197 PHE B O   1 
ATOM   1315 C CB  . PHE A 1 185 ? -11.830 14.333  -21.239 1.00 36.89 ? 197 PHE B CB  1 
ATOM   1316 C CG  . PHE A 1 185 ? -10.445 14.339  -20.667 1.00 34.81 ? 197 PHE B CG  1 
ATOM   1317 C CD1 . PHE A 1 185 ? -10.222 14.749  -19.365 1.00 32.78 ? 197 PHE B CD1 1 
ATOM   1318 C CD2 . PHE A 1 185 ? -9.370  13.911  -21.416 1.00 34.90 ? 197 PHE B CD2 1 
ATOM   1319 C CE1 . PHE A 1 185 ? -8.947  14.748  -18.832 1.00 35.65 ? 197 PHE B CE1 1 
ATOM   1320 C CE2 . PHE A 1 185 ? -8.082  13.907  -20.879 1.00 35.51 ? 197 PHE B CE2 1 
ATOM   1321 C CZ  . PHE A 1 185 ? -7.872  14.328  -19.590 1.00 31.51 ? 197 PHE B CZ  1 
ATOM   1322 N N   . THR A 1 186 ? -14.864 12.203  -20.758 1.00 48.02 ? 198 THR B N   1 
ATOM   1323 C CA  . THR A 1 186 ? -16.312 12.152  -20.905 1.00 50.70 ? 198 THR B CA  1 
ATOM   1324 C C   . THR A 1 186 ? -17.005 11.867  -19.573 1.00 55.86 ? 198 THR B C   1 
ATOM   1325 O O   . THR A 1 186 ? -16.375 11.869  -18.504 1.00 50.71 ? 198 THR B O   1 
ATOM   1326 C CB  . THR A 1 186 ? -16.692 11.084  -21.929 1.00 50.30 ? 198 THR B CB  1 
ATOM   1327 O OG1 . THR A 1 186 ? -16.026 9.859   -21.593 1.00 46.94 ? 198 THR B OG1 1 
ATOM   1328 C CG2 . THR A 1 186 ? -16.284 11.512  -23.327 1.00 46.29 ? 198 THR B CG2 1 
ATOM   1329 N N   . GLU A 1 187 ? -18.314 11.609  -19.640 1.00 59.54 ? 199 GLU B N   1 
ATOM   1330 C CA  . GLU A 1 187 ? -19.103 11.329  -18.448 1.00 60.64 ? 199 GLU B CA  1 
ATOM   1331 C C   . GLU A 1 187 ? -18.979 9.875   -17.984 1.00 60.83 ? 199 GLU B C   1 
ATOM   1332 O O   . GLU A 1 187 ? -19.289 9.586   -16.823 1.00 61.10 ? 199 GLU B O   1 
ATOM   1333 C CB  . GLU A 1 187 ? -20.574 11.692  -18.711 1.00 61.21 ? 199 GLU B CB  1 
ATOM   1334 C CG  . GLU A 1 187 ? -20.908 13.176  -18.476 1.00 59.69 ? 199 GLU B CG  1 
ATOM   1335 C CD  . GLU A 1 187 ? -21.664 13.430  -17.176 1.00 57.79 ? 199 GLU B CD  1 
ATOM   1336 O OE1 . GLU A 1 187 ? -21.011 13.759  -16.157 1.00 53.78 ? 199 GLU B OE1 1 
ATOM   1337 O OE2 . GLU A 1 187 ? -22.913 13.319  -17.188 1.00 51.26 ? 199 GLU B OE2 1 
ATOM   1338 N N   . ASP A 1 188 ? -18.536 8.963   -18.861 1.00 59.94 ? 200 ASP B N   1 
ATOM   1339 C CA  . ASP A 1 188 ? -18.180 7.590   -18.508 1.00 54.77 ? 200 ASP B CA  1 
ATOM   1340 C C   . ASP A 1 188 ? -16.670 7.394   -18.404 1.00 56.09 ? 200 ASP B C   1 
ATOM   1341 O O   . ASP A 1 188 ? -16.183 6.264   -18.539 1.00 53.09 ? 200 ASP B O   1 
ATOM   1342 C CB  . ASP A 1 188 ? -18.749 6.604   -19.534 1.00 60.59 ? 200 ASP B CB  1 
ATOM   1343 C CG  . ASP A 1 188 ? -20.141 6.100   -19.172 1.00 70.57 ? 200 ASP B CG  1 
ATOM   1344 O OD1 . ASP A 1 188 ? -20.833 6.780   -18.381 1.00 74.47 ? 200 ASP B OD1 1 
ATOM   1345 O OD2 . ASP A 1 188 ? -20.541 5.024   -19.686 1.00 70.10 ? 200 ASP B OD2 1 
ATOM   1346 N N   . SER A 1 189 ? -15.917 8.469   -18.182 1.00 55.67 ? 201 SER B N   1 
ATOM   1347 C CA  . SER A 1 189 ? -14.465 8.375   -18.219 1.00 51.77 ? 201 SER B CA  1 
ATOM   1348 C C   . SER A 1 189 ? -13.953 7.524   -17.059 1.00 45.81 ? 201 SER B C   1 
ATOM   1349 O O   . SER A 1 189 ? -14.511 7.522   -15.962 1.00 53.49 ? 201 SER B O   1 
ATOM   1350 C CB  . SER A 1 189 ? -13.836 9.780   -18.225 1.00 51.33 ? 201 SER B CB  1 
ATOM   1351 O OG  . SER A 1 189 ? -13.453 10.259  -16.945 1.00 54.10 ? 201 SER B OG  1 
ATOM   1352 N N   . LYS A 1 190 ? -12.898 6.775   -17.328 1.00 47.17 ? 202 LYS B N   1 
ATOM   1353 C CA  . LYS A 1 190 ? -12.356 5.773   -16.425 1.00 49.56 ? 202 LYS B CA  1 
ATOM   1354 C C   . LYS A 1 190 ? -10.845 5.983   -16.329 1.00 43.99 ? 202 LYS B C   1 
ATOM   1355 O O   . LYS A 1 190 ? -10.254 6.646   -17.182 1.00 40.87 ? 202 LYS B O   1 
ATOM   1356 C CB  . LYS A 1 190 ? -12.661 4.356   -16.940 1.00 50.37 ? 202 LYS B CB  1 
ATOM   1357 C CG  . LYS A 1 190 ? -14.147 3.982   -16.952 1.00 50.32 ? 202 LYS B CG  1 
ATOM   1358 C CD  . LYS A 1 190 ? -14.493 2.834   -17.943 1.00 48.70 ? 202 LYS B CD  1 
ATOM   1359 C CE  . LYS A 1 190 ? -13.661 1.547   -17.836 1.00 50.90 ? 202 LYS B CE  1 
ATOM   1360 N NZ  . LYS A 1 190 ? -13.098 1.230   -16.501 1.00 53.79 ? 202 LYS B NZ  1 
ATOM   1361 N N   . PRO A 1 191 ? -10.211 5.434   -15.294 1.00 41.81 ? 203 PRO B N   1 
ATOM   1362 C CA  . PRO A 1 191 ? -8.748  5.336   -15.323 1.00 40.43 ? 203 PRO B CA  1 
ATOM   1363 C C   . PRO A 1 191 ? -8.283  4.532   -16.535 1.00 42.38 ? 203 PRO B C   1 
ATOM   1364 O O   . PRO A 1 191 ? -9.041  3.759   -17.132 1.00 44.37 ? 203 PRO B O   1 
ATOM   1365 C CB  . PRO A 1 191 ? -8.424  4.628   -14.002 1.00 32.68 ? 203 PRO B CB  1 
ATOM   1366 C CG  . PRO A 1 191 ? -9.565  5.012   -13.108 1.00 30.73 ? 203 PRO B CG  1 
ATOM   1367 C CD  . PRO A 1 191 ? -10.753 4.962   -14.010 1.00 39.75 ? 203 PRO B CD  1 
ATOM   1368 N N   . GLY A 1 192 ? -7.025  4.751   -16.921 1.00 38.77 ? 204 GLY B N   1 
ATOM   1369 C CA  . GLY A 1 192 ? -6.456  4.135   -18.105 1.00 33.90 ? 204 GLY B CA  1 
ATOM   1370 C C   . GLY A 1 192 ? -5.598  2.929   -17.763 1.00 34.97 ? 204 GLY B C   1 
ATOM   1371 O O   . GLY A 1 192 ? -4.981  2.861   -16.695 1.00 33.85 ? 204 GLY B O   1 
ATOM   1372 N N   . ILE A 1 193 ? -5.578  1.967   -18.688 1.00 34.02 ? 205 ILE B N   1 
ATOM   1373 C CA  . ILE A 1 193 ? -4.890  0.697   -18.523 1.00 31.32 ? 205 ILE B CA  1 
ATOM   1374 C C   . ILE A 1 193 ? -3.778  0.646   -19.567 1.00 30.07 ? 205 ILE B C   1 
ATOM   1375 O O   . ILE A 1 193 ? -3.752  1.430   -20.522 1.00 26.86 ? 205 ILE B O   1 
ATOM   1376 C CB  . ILE A 1 193 ? -5.885  -0.495  -18.635 1.00 27.55 ? 205 ILE B CB  1 
ATOM   1377 C CG1 . ILE A 1 193 ? -5.219  -1.859  -18.370 1.00 36.26 ? 205 ILE B CG1 1 
ATOM   1378 C CG2 . ILE A 1 193 ? -6.643  -0.474  -19.947 1.00 24.45 ? 205 ILE B CG2 1 
ATOM   1379 C CD1 . ILE A 1 193 ? -4.324  -1.920  -17.124 1.00 38.95 ? 205 ILE B CD1 1 
ATOM   1380 N N   . TRP A 1 194 ? -2.816  -0.249  -19.344 1.00 28.84 ? 206 TRP B N   1 
ATOM   1381 C CA  . TRP A 1 194 ? -1.722  -0.409  -20.294 1.00 29.86 ? 206 TRP B CA  1 
ATOM   1382 C C   . TRP A 1 194 ? -2.245  -0.820  -21.668 1.00 30.98 ? 206 TRP B C   1 
ATOM   1383 O O   . TRP A 1 194 ? -2.991  -1.793  -21.804 1.00 34.73 ? 206 TRP B O   1 
ATOM   1384 C CB  . TRP A 1 194 ? -0.726  -1.442  -19.780 1.00 30.11 ? 206 TRP B CB  1 
ATOM   1385 C CG  . TRP A 1 194 ? 0.267   -0.909  -18.766 1.00 31.35 ? 206 TRP B CG  1 
ATOM   1386 C CD1 . TRP A 1 194 ? 0.306   -1.191  -17.433 1.00 30.36 ? 206 TRP B CD1 1 
ATOM   1387 C CD2 . TRP A 1 194 ? 1.349   0.005   -19.009 1.00 29.72 ? 206 TRP B CD2 1 
ATOM   1388 N NE1 . TRP A 1 194 ? 1.358   -0.533  -16.836 1.00 28.37 ? 206 TRP B NE1 1 
ATOM   1389 C CE2 . TRP A 1 194 ? 2.006   0.215   -17.781 1.00 26.91 ? 206 TRP B CE2 1 
ATOM   1390 C CE3 . TRP A 1 194 ? 1.813   0.674   -20.139 1.00 27.92 ? 206 TRP B CE3 1 
ATOM   1391 C CZ2 . TRP A 1 194 ? 3.109   1.054   -17.655 1.00 26.04 ? 206 TRP B CZ2 1 
ATOM   1392 C CZ3 . TRP A 1 194 ? 2.912   1.518   -20.008 1.00 28.20 ? 206 TRP B CZ3 1 
ATOM   1393 C CH2 . TRP A 1 194 ? 3.548   1.695   -18.778 1.00 25.97 ? 206 TRP B CH2 1 
ATOM   1394 N N   . ARG A 1 195 ? -1.841  -0.078  -22.696 1.00 31.48 ? 207 ARG B N   1 
ATOM   1395 C CA  . ARG A 1 195 ? -2.281  -0.317  -24.060 1.00 27.99 ? 207 ARG B CA  1 
ATOM   1396 C C   . ARG A 1 195 ? -1.086  -0.300  -25.003 1.00 31.47 ? 207 ARG B C   1 
ATOM   1397 O O   . ARG A 1 195 ? -0.006  0.190   -24.658 1.00 28.46 ? 207 ARG B O   1 
ATOM   1398 C CB  . ARG A 1 195 ? -3.304  0.726   -24.487 1.00 23.53 ? 207 ARG B CB  1 
ATOM   1399 C CG  . ARG A 1 195 ? -4.541  0.668   -23.638 1.00 25.33 ? 207 ARG B CG  1 
ATOM   1400 C CD  . ARG A 1 195 ? -5.503  -0.325  -24.226 1.00 30.53 ? 207 ARG B CD  1 
ATOM   1401 N NE  . ARG A 1 195 ? -6.882  -0.111  -23.804 1.00 32.63 ? 207 ARG B NE  1 
ATOM   1402 C CZ  . ARG A 1 195 ? -7.710  -1.073  -23.414 1.00 33.90 ? 207 ARG B CZ  1 
ATOM   1403 N NH1 . ARG A 1 195 ? -7.324  -2.343  -23.364 1.00 34.36 ? 207 ARG B NH1 1 
ATOM   1404 N NH2 . ARG A 1 195 ? -8.960  -0.756  -23.075 1.00 29.76 ? 207 ARG B NH2 1 
ATOM   1405 N N   . GLU A 1 196 ? -1.298  -0.853  -26.205 1.00 31.96 ? 208 GLU B N   1 
ATOM   1406 C CA  . GLU A 1 196 ? -0.278  -0.908  -27.246 1.00 27.71 ? 208 GLU B CA  1 
ATOM   1407 C C   . GLU A 1 196 ? -0.564  0.138   -28.312 1.00 30.59 ? 208 GLU B C   1 
ATOM   1408 O O   . GLU A 1 196 ? -1.722  0.352   -28.705 1.00 27.09 ? 208 GLU B O   1 
ATOM   1409 C CB  . GLU A 1 196 ? -0.206  -2.288  -27.902 1.00 25.59 ? 208 GLU B CB  1 
ATOM   1410 C CG  . GLU A 1 196 ? 0.863   -2.400  -28.957 1.00 23.38 ? 208 GLU B CG  1 
ATOM   1411 C CD  . GLU A 1 196 ? 1.470   -3.796  -29.026 1.00 26.99 ? 208 GLU B CD  1 
ATOM   1412 O OE1 . GLU A 1 196 ? 0.847   -4.757  -28.518 1.00 27.22 ? 208 GLU B OE1 1 
ATOM   1413 O OE2 . GLU A 1 196 ? 2.596   -3.926  -29.552 1.00 24.11 ? 208 GLU B OE2 1 
ATOM   1414 N N   . ILE A 1 197 ? 0.501   0.795   -28.761 1.00 26.44 ? 209 ILE B N   1 
ATOM   1415 C CA  . ILE A 1 197 ? 0.436   1.796   -29.813 1.00 25.68 ? 209 ILE B CA  1 
ATOM   1416 C C   . ILE A 1 197 ? 1.161   1.252   -31.035 1.00 27.08 ? 209 ILE B C   1 
ATOM   1417 O O   . ILE A 1 197 ? 2.198   0.584   -30.919 1.00 28.03 ? 209 ILE B O   1 
ATOM   1418 C CB  . ILE A 1 197 ? 1.035   3.135   -29.344 1.00 23.25 ? 209 ILE B CB  1 
ATOM   1419 C CG1 . ILE A 1 197 ? 0.339   3.592   -28.072 1.00 22.55 ? 209 ILE B CG1 1 
ATOM   1420 C CG2 . ILE A 1 197 ? 0.850   4.197   -30.392 1.00 23.02 ? 209 ILE B CG2 1 
ATOM   1421 C CD1 . ILE A 1 197 ? -1.085  4.041   -28.304 1.00 22.88 ? 209 ILE B CD1 1 
ATOM   1422 N N   . SER A 1 198 ? 0.595   1.522   -32.203 1.00 27.45 ? 210 SER B N   1 
ATOM   1423 C CA  . SER A 1 198 ? 1.083   1.020   -33.476 1.00 26.23 ? 210 SER B CA  1 
ATOM   1424 C C   . SER A 1 198 ? 2.028   2.024   -34.130 1.00 27.71 ? 210 SER B C   1 
ATOM   1425 O O   . SER A 1 198 ? 2.208   3.148   -33.661 1.00 31.57 ? 210 SER B O   1 
ATOM   1426 C CB  . SER A 1 198 ? -0.092  0.740   -34.398 1.00 28.80 ? 210 SER B CB  1 
ATOM   1427 O OG  . SER A 1 198 ? -0.995  1.828   -34.343 1.00 30.20 ? 210 SER B OG  1 
ATOM   1428 N N   . VAL A 1 199 ? 2.638   1.602   -35.240 1.00 27.17 ? 211 VAL B N   1 
ATOM   1429 C CA  . VAL A 1 199 ? 3.453   2.500   -36.045 1.00 24.42 ? 211 VAL B CA  1 
ATOM   1430 C C   . VAL A 1 199 ? 2.634   3.697   -36.506 1.00 24.42 ? 211 VAL B C   1 
ATOM   1431 O O   . VAL A 1 199 ? 3.191   4.732   -36.878 1.00 23.10 ? 211 VAL B O   1 
ATOM   1432 C CB  . VAL A 1 199 ? 4.038   1.703   -37.233 1.00 25.19 ? 211 VAL B CB  1 
ATOM   1433 C CG1 . VAL A 1 199 ? 4.782   2.606   -38.231 1.00 17.91 ? 211 VAL B CG1 1 
ATOM   1434 C CG2 . VAL A 1 199 ? 4.917   0.554   -36.717 1.00 22.42 ? 211 VAL B CG2 1 
ATOM   1435 N N   . CYS A 1 200 ? 1.311   3.596   -36.457 1.00 24.83 ? 212 CYS B N   1 
ATOM   1436 C CA  . CYS A 1 200 ? 0.453   4.683   -36.883 1.00 25.15 ? 212 CYS B CA  1 
ATOM   1437 C C   . CYS A 1 200 ? -0.351  5.291   -35.752 1.00 27.83 ? 212 CYS B C   1 
ATOM   1438 O O   . CYS A 1 200 ? -1.166  6.183   -36.002 1.00 27.30 ? 212 CYS B O   1 
ATOM   1439 C CB  . CYS A 1 200 ? -0.465  4.201   -37.991 1.00 29.78 ? 212 CYS B CB  1 
ATOM   1440 S SG  . CYS A 1 200 ? 0.472   3.969   -39.476 1.00 29.73 ? 212 CYS B SG  1 
ATOM   1441 N N   . GLY A 1 201 ? -0.131  4.852   -34.516 1.00 27.25 ? 213 GLY B N   1 
ATOM   1442 C CA  . GLY A 1 201 ? -0.720  5.518   -33.373 1.00 25.49 ? 213 GLY B CA  1 
ATOM   1443 C C   . GLY A 1 201 ? -2.097  5.043   -32.970 1.00 26.13 ? 213 GLY B C   1 
ATOM   1444 O O   . GLY A 1 201 ? -2.781  5.733   -32.203 1.00 26.21 ? 213 GLY B O   1 
ATOM   1445 N N   . ASN A 1 202 ? -2.533  3.899   -33.450 1.00 27.08 ? 214 ASN B N   1 
ATOM   1446 C CA  . ASN A 1 202 ? -3.831  3.413   -33.028 1.00 28.98 ? 214 ASN B CA  1 
ATOM   1447 C C   . ASN A 1 202 ? -3.651  2.519   -31.813 1.00 30.37 ? 214 ASN B C   1 
ATOM   1448 O O   . ASN A 1 202 ? -2.572  1.969   -31.571 1.00 29.47 ? 214 ASN B O   1 
ATOM   1449 C CB  . ASN A 1 202 ? -4.521  2.685   -34.176 1.00 26.52 ? 214 ASN B CB  1 
ATOM   1450 C CG  . ASN A 1 202 ? -4.603  3.537   -35.415 1.00 23.52 ? 214 ASN B CG  1 
ATOM   1451 O OD1 . ASN A 1 202 ? -5.262  4.564   -35.410 1.00 23.92 ? 214 ASN B OD1 1 
ATOM   1452 N ND2 . ASN A 1 202 ? -3.916  3.129   -36.482 1.00 30.43 ? 214 ASN B ND2 1 
ATOM   1453 N N   . VAL A 1 203 ? -4.701  2.410   -31.021 1.00 26.84 ? 215 VAL B N   1 
ATOM   1454 C CA  . VAL A 1 203 ? -4.588  1.748   -29.733 1.00 29.58 ? 215 VAL B CA  1 
ATOM   1455 C C   . VAL A 1 203 ? -5.061  0.310   -29.876 1.00 28.53 ? 215 VAL B C   1 
ATOM   1456 O O   . VAL A 1 203 ? -6.002  0.016   -30.626 1.00 30.77 ? 215 VAL B O   1 
ATOM   1457 C CB  . VAL A 1 203 ? -5.379  2.517   -28.660 1.00 27.64 ? 215 VAL B CB  1 
ATOM   1458 C CG1 . VAL A 1 203 ? -5.045  1.983   -27.273 1.00 27.21 ? 215 VAL B CG1 1 
ATOM   1459 C CG2 . VAL A 1 203 ? -5.072  3.996   -28.774 1.00 20.98 ? 215 VAL B CG2 1 
ATOM   1460 N N   . PHE A 1 204 ? -4.374  -0.598  -29.204 1.00 25.62 ? 216 PHE B N   1 
ATOM   1461 C CA  . PHE A 1 204 ? -4.751  -1.999  -29.226 1.00 30.42 ? 216 PHE B CA  1 
ATOM   1462 C C   . PHE A 1 204 ? -4.574  -2.545  -27.828 1.00 32.10 ? 216 PHE B C   1 
ATOM   1463 O O   . PHE A 1 204 ? -3.748  -2.041  -27.057 1.00 30.22 ? 216 PHE B O   1 
ATOM   1464 C CB  . PHE A 1 204 ? -3.912  -2.813  -30.222 1.00 30.35 ? 216 PHE B CB  1 
ATOM   1465 C CG  . PHE A 1 204 ? -4.121  -2.406  -31.647 1.00 29.50 ? 216 PHE B CG  1 
ATOM   1466 C CD1 . PHE A 1 204 ? -3.504  -1.278  -32.151 1.00 28.71 ? 216 PHE B CD1 1 
ATOM   1467 C CD2 . PHE A 1 204 ? -4.937  -3.140  -32.477 1.00 31.20 ? 216 PHE B CD2 1 
ATOM   1468 C CE1 . PHE A 1 204 ? -3.703  -0.882  -33.445 1.00 26.69 ? 216 PHE B CE1 1 
ATOM   1469 C CE2 . PHE A 1 204 ? -5.128  -2.758  -33.780 1.00 31.65 ? 216 PHE B CE2 1 
ATOM   1470 C CZ  . PHE A 1 204 ? -4.518  -1.621  -34.262 1.00 30.32 ? 216 PHE B CZ  1 
ATOM   1471 N N   . SER A 1 205 ? -5.375  -3.555  -27.497 1.00 33.37 ? 217 SER B N   1 
ATOM   1472 C CA  . SER A 1 205 ? -5.202  -4.228  -26.219 1.00 34.91 ? 217 SER B CA  1 
ATOM   1473 C C   . SER A 1 205 ? -3.890  -5.001  -26.228 1.00 32.49 ? 217 SER B C   1 
ATOM   1474 O O   . SER A 1 205 ? -3.362  -5.363  -27.286 1.00 32.08 ? 217 SER B O   1 
ATOM   1475 C CB  . SER A 1 205 ? -6.376  -5.168  -25.926 1.00 37.07 ? 217 SER B CB  1 
ATOM   1476 O OG  . SER A 1 205 ? -6.457  -6.234  -26.864 1.00 38.81 ? 217 SER B OG  1 
ATOM   1477 N N   . LEU A 1 206 ? -3.353  -5.232  -25.035 1.00 35.16 ? 218 LEU B N   1 
ATOM   1478 C CA  . LEU A 1 206 ? -2.054  -5.884  -24.923 1.00 33.99 ? 218 LEU B CA  1 
ATOM   1479 C C   . LEU A 1 206 ? -2.078  -7.278  -25.536 1.00 34.43 ? 218 LEU B C   1 
ATOM   1480 O O   . LEU A 1 206 ? -3.123  -7.933  -25.615 1.00 36.22 ? 218 LEU B O   1 
ATOM   1481 C CB  . LEU A 1 206 ? -1.631  -5.983  -23.459 1.00 34.65 ? 218 LEU B CB  1 
ATOM   1482 C CG  . LEU A 1 206 ? -0.983  -4.744  -22.837 1.00 35.37 ? 218 LEU B CG  1 
ATOM   1483 C CD1 . LEU A 1 206 ? 0.013   -5.144  -21.729 1.00 32.93 ? 218 LEU B CD1 1 
ATOM   1484 C CD2 . LEU A 1 206 ? -0.331  -3.861  -23.915 1.00 30.98 ? 218 LEU B CD2 1 
ATOM   1485 N N   . ARG A 1 207 ? -0.898  -7.737  -25.950 1.00 35.50 ? 219 ARG B N   1 
ATOM   1486 C CA  . ARG A 1 207 ? -0.754  -9.075  -26.500 1.00 32.69 ? 219 ARG B CA  1 
ATOM   1487 C C   . ARG A 1 207 ? -0.777  -10.106 -25.374 1.00 33.73 ? 219 ARG B C   1 
ATOM   1488 O O   . ARG A 1 207 ? -0.904  -9.777  -24.196 1.00 35.28 ? 219 ARG B O   1 
ATOM   1489 C CB  . ARG A 1 207 ? 0.520   -9.165  -27.336 1.00 30.60 ? 219 ARG B CB  1 
ATOM   1490 C CG  . ARG A 1 207 ? 0.404   -8.401  -28.642 1.00 31.93 ? 219 ARG B CG  1 
ATOM   1491 C CD  . ARG A 1 207 ? 1.696   -8.450  -29.428 1.00 32.49 ? 219 ARG B CD  1 
ATOM   1492 N NE  . ARG A 1 207 ? 2.290   -7.130  -29.605 1.00 29.84 ? 219 ARG B NE  1 
ATOM   1493 C CZ  . ARG A 1 207 ? 3.551   -6.924  -29.959 1.00 28.37 ? 219 ARG B CZ  1 
ATOM   1494 N NH1 . ARG A 1 207 ? 4.380   -7.928  -30.173 1.00 30.30 ? 219 ARG B NH1 1 
ATOM   1495 N NH2 . ARG A 1 207 ? 3.995   -5.681  -30.089 1.00 29.82 ? 219 ARG B NH2 1 
ATOM   1496 N N   . GLU A 1 208 ? -0.693  -11.385 -25.747 1.00 40.75 ? 220 GLU B N   1 
ATOM   1497 C CA  . GLU A 1 208 ? -0.672  -12.449 -24.742 1.00 41.63 ? 220 GLU B CA  1 
ATOM   1498 C C   . GLU A 1 208 ? 0.731   -12.663 -24.198 1.00 39.05 ? 220 GLU B C   1 
ATOM   1499 O O   . GLU A 1 208 ? 0.912   -12.927 -23.004 1.00 40.93 ? 220 GLU B O   1 
ATOM   1500 C CB  . GLU A 1 208 ? -1.212  -13.746 -25.334 1.00 37.83 ? 220 GLU B CB  1 
ATOM   1501 C CG  . GLU A 1 208 ? -2.680  -13.684 -25.658 1.00 41.50 ? 220 GLU B CG  1 
ATOM   1502 C CD  . GLU A 1 208 ? -3.519  -13.317 -24.454 1.00 47.01 ? 220 GLU B CD  1 
ATOM   1503 O OE1 . GLU A 1 208 ? -3.471  -14.066 -23.447 1.00 47.41 ? 220 GLU B OE1 1 
ATOM   1504 O OE2 . GLU A 1 208 ? -4.231  -12.282 -24.521 1.00 50.48 ? 220 GLU B OE2 1 
ATOM   1505 N N   . THR A 1 209 ? 1.726   -12.572 -25.062 1.00 38.05 ? 221 THR B N   1 
ATOM   1506 C CA  . THR A 1 209 ? 3.114   -12.437 -24.657 1.00 41.89 ? 221 THR B CA  1 
ATOM   1507 C C   . THR A 1 209 ? 3.656   -11.154 -25.276 1.00 40.30 ? 221 THR B C   1 
ATOM   1508 O O   . THR A 1 209 ? 3.026   -10.546 -26.152 1.00 36.86 ? 221 THR B O   1 
ATOM   1509 C CB  . THR A 1 209 ? 3.951   -13.662 -25.063 1.00 41.42 ? 221 THR B CB  1 
ATOM   1510 O OG1 . THR A 1 209 ? 4.682   -13.380 -26.261 1.00 43.50 ? 221 THR B OG1 1 
ATOM   1511 C CG2 . THR A 1 209 ? 3.058   -14.873 -25.302 1.00 41.61 ? 221 THR B CG2 1 
ATOM   1512 N N   . ARG A 1 210 ? 4.823   -10.726 -24.784 1.00 38.30 ? 222 ARG B N   1 
ATOM   1513 C CA  . ARG A 1 210 ? 5.343   -9.419  -25.165 1.00 37.94 ? 222 ARG B CA  1 
ATOM   1514 C C   . ARG A 1 210 ? 5.531   -9.325  -26.672 1.00 39.45 ? 222 ARG B C   1 
ATOM   1515 O O   . ARG A 1 210 ? 4.881   -8.515  -27.338 1.00 37.84 ? 222 ARG B O   1 
ATOM   1516 C CB  . ARG A 1 210 ? 6.652   -9.135  -24.443 1.00 40.27 ? 222 ARG B CB  1 
ATOM   1517 C CG  . ARG A 1 210 ? 7.283   -7.847  -24.894 1.00 42.09 ? 222 ARG B CG  1 
ATOM   1518 C CD  . ARG A 1 210 ? 7.104   -6.748  -23.861 1.00 41.48 ? 222 ARG B CD  1 
ATOM   1519 N NE  . ARG A 1 210 ? 6.997   -5.430  -24.479 1.00 38.62 ? 222 ARG B NE  1 
ATOM   1520 C CZ  . ARG A 1 210 ? 6.991   -4.292  -23.799 1.00 39.07 ? 222 ARG B CZ  1 
ATOM   1521 N NH1 . ARG A 1 210 ? 7.157   -4.276  -22.491 1.00 40.19 ? 222 ARG B NH1 1 
ATOM   1522 N NH2 . ARG A 1 210 ? 6.824   -3.142  -24.450 1.00 35.70 ? 222 ARG B NH2 1 
ATOM   1523 N N   . SER A 1 211 ? 6.386   -10.180 -27.236 1.00 41.81 ? 223 SER B N   1 
ATOM   1524 C CA  . SER A 1 211 ? 6.682   -10.176 -28.666 1.00 37.95 ? 223 SER B CA  1 
ATOM   1525 C C   . SER A 1 211 ? 5.842   -11.175 -29.466 1.00 37.81 ? 223 SER B C   1 
ATOM   1526 O O   . SER A 1 211 ? 6.278   -11.612 -30.535 1.00 43.59 ? 223 SER B O   1 
ATOM   1527 C CB  . SER A 1 211 ? 8.169   -10.452 -28.885 1.00 44.57 ? 223 SER B CB  1 
ATOM   1528 O OG  . SER A 1 211 ? 8.406   -11.828 -29.106 1.00 48.67 ? 223 SER B OG  1 
ATOM   1529 N N   . ALA A 1 212 ? 4.651   -11.533 -28.985 1.00 37.15 ? 224 ALA B N   1 
ATOM   1530 C CA  . ALA A 1 212 ? 3.794   -12.479 -29.694 1.00 35.66 ? 224 ALA B CA  1 
ATOM   1531 C C   . ALA A 1 212 ? 3.408   -11.951 -31.078 1.00 40.16 ? 224 ALA B C   1 
ATOM   1532 O O   . ALA A 1 212 ? 3.215   -10.746 -31.261 1.00 37.58 ? 224 ALA B O   1 
ATOM   1533 C CB  . ALA A 1 212 ? 2.541   -12.743 -28.858 1.00 38.81 ? 224 ALA B CB  1 
ATOM   1534 N N   . GLN A 1 213 ? 3.285   -12.859 -32.065 1.00 40.76 ? 225 GLN B N   1 
ATOM   1535 C CA  . GLN A 1 213 ? 2.953   -12.412 -33.423 1.00 39.30 ? 225 GLN B CA  1 
ATOM   1536 C C   . GLN A 1 213 ? 1.535   -11.831 -33.511 1.00 39.85 ? 225 GLN B C   1 
ATOM   1537 O O   . GLN A 1 213 ? 1.298   -10.874 -34.260 1.00 42.02 ? 225 GLN B O   1 
ATOM   1538 C CB  . GLN A 1 213 ? 3.132   -13.553 -34.439 1.00 44.27 ? 225 GLN B CB  1 
ATOM   1539 C CG  . GLN A 1 213 ? 2.209   -13.458 -35.714 1.00 54.90 ? 225 GLN B CG  1 
ATOM   1540 C CD  . GLN A 1 213 ? 2.855   -12.790 -36.959 1.00 59.92 ? 225 GLN B CD  1 
ATOM   1541 O OE1 . GLN A 1 213 ? 4.051   -12.508 -36.979 1.00 55.88 ? 225 GLN B OE1 1 
ATOM   1542 N NE2 . GLN A 1 213 ? 2.039   -12.525 -37.990 1.00 53.36 ? 225 GLN B NE2 1 
ATOM   1543 N N   . GLN A 1 214 ? 0.569   -12.388 -32.781 1.00 35.70 ? 226 GLN B N   1 
ATOM   1544 C CA  . GLN A 1 214 ? -0.800  -11.900 -32.932 1.00 35.50 ? 226 GLN B CA  1 
ATOM   1545 C C   . GLN A 1 214 ? -0.982  -10.567 -32.203 1.00 37.54 ? 226 GLN B C   1 
ATOM   1546 O O   . GLN A 1 214 ? -0.601  -10.416 -31.034 1.00 38.26 ? 226 GLN B O   1 
ATOM   1547 C CB  . GLN A 1 214 ? -1.814  -12.936 -32.433 1.00 32.01 ? 226 GLN B CB  1 
ATOM   1548 C CG  . GLN A 1 214 ? -3.291  -12.654 -32.812 1.00 32.56 ? 226 GLN B CG  1 
ATOM   1549 C CD  . GLN A 1 214 ? -3.525  -12.231 -34.283 1.00 46.87 ? 226 GLN B CD  1 
ATOM   1550 O OE1 . GLN A 1 214 ? -2.982  -12.827 -35.226 1.00 51.70 ? 226 GLN B OE1 1 
ATOM   1551 N NE2 . GLN A 1 214 ? -4.345  -11.187 -34.475 1.00 44.65 ? 226 GLN B NE2 1 
ATOM   1552 N N   . ARG A 1 215 ? -1.567  -9.601  -32.906 1.00 34.20 ? 227 ARG B N   1 
ATOM   1553 C CA  . ARG A 1 215 ? -1.897  -8.313  -32.320 1.00 32.59 ? 227 ARG B CA  1 
ATOM   1554 C C   . ARG A 1 215 ? -3.061  -8.454  -31.338 1.00 34.27 ? 227 ARG B C   1 
ATOM   1555 O O   . ARG A 1 215 ? -3.908  -9.341  -31.462 1.00 35.52 ? 227 ARG B O   1 
ATOM   1556 C CB  . ARG A 1 215 ? -2.244  -7.317  -33.435 1.00 30.71 ? 227 ARG B CB  1 
ATOM   1557 C CG  . ARG A 1 215 ? -3.468  -7.715  -34.218 1.00 32.83 ? 227 ARG B CG  1 
ATOM   1558 C CD  . ARG A 1 215 ? -4.147  -6.576  -34.950 1.00 30.82 ? 227 ARG B CD  1 
ATOM   1559 N NE  . ARG A 1 215 ? -5.586  -6.808  -34.886 1.00 38.85 ? 227 ARG B NE  1 
ATOM   1560 C CZ  . ARG A 1 215 ? -6.516  -6.129  -35.539 1.00 42.69 ? 227 ARG B CZ  1 
ATOM   1561 N NH1 . ARG A 1 215 ? -6.201  -5.281  -36.508 1.00 40.16 ? 227 ARG B NH1 1 
ATOM   1562 N NH2 . ARG A 1 215 ? -7.798  -6.309  -35.210 1.00 41.07 ? 227 ARG B NH2 1 
ATOM   1563 N N   . GLY A 1 216 ? -3.100  -7.573  -30.342 1.00 33.21 ? 228 GLY B N   1 
ATOM   1564 C CA  . GLY A 1 216 ? -4.281  -7.502  -29.504 1.00 31.53 ? 228 GLY B CA  1 
ATOM   1565 C C   . GLY A 1 216 ? -5.497  -7.063  -30.296 1.00 29.19 ? 228 GLY B C   1 
ATOM   1566 O O   . GLY A 1 216 ? -5.437  -6.925  -31.526 1.00 25.49 ? 228 GLY B O   1 
ATOM   1567 N N   . LYS A 1 217 ? -6.615  -6.852  -29.611 1.00 32.20 ? 229 LYS B N   1 
ATOM   1568 C CA  . LYS A 1 217 ? -7.814  -6.407  -30.304 1.00 37.60 ? 229 LYS B CA  1 
ATOM   1569 C C   . LYS A 1 217 ? -7.795  -4.894  -30.379 1.00 35.31 ? 229 LYS B C   1 
ATOM   1570 O O   . LYS A 1 217 ? -7.239  -4.219  -29.505 1.00 32.40 ? 229 LYS B O   1 
ATOM   1571 C CB  . LYS A 1 217 ? -9.105  -6.889  -29.621 1.00 39.96 ? 229 LYS B CB  1 
ATOM   1572 C CG  . LYS A 1 217 ? -9.158  -6.640  -28.125 1.00 45.25 ? 229 LYS B CG  1 
ATOM   1573 C CD  . LYS A 1 217 ? -10.552 -6.278  -27.621 1.00 47.83 ? 229 LYS B CD  1 
ATOM   1574 C CE  . LYS A 1 217 ? -10.494 -6.014  -26.117 1.00 52.33 ? 229 LYS B CE  1 
ATOM   1575 N NZ  . LYS A 1 217 ? -11.790 -6.232  -25.420 1.00 52.40 ? 229 LYS B NZ  1 
ATOM   1576 N N   . MET A 1 218 ? -8.372  -4.374  -31.463 1.00 36.16 ? 230 MET B N   1 
ATOM   1577 C CA  . MET A 1 218 ? -8.537  -2.939  -31.609 1.00 33.78 ? 230 MET B CA  1 
ATOM   1578 C C   . MET A 1 218 ? -9.279  -2.356  -30.412 1.00 37.15 ? 230 MET B C   1 
ATOM   1579 O O   . MET A 1 218 ? -10.243 -2.938  -29.907 1.00 32.75 ? 230 MET B O   1 
ATOM   1580 C CB  . MET A 1 218 ? -9.319  -2.631  -32.870 1.00 30.78 ? 230 MET B CB  1 
ATOM   1581 C CG  . MET A 1 218 ? -8.557  -2.735  -34.113 1.00 36.50 ? 230 MET B CG  1 
ATOM   1582 S SD  . MET A 1 218 ? -9.189  -1.491  -35.244 1.00 63.39 ? 230 MET B SD  1 
ATOM   1583 C CE  . MET A 1 218 ? -9.509  -0.110  -34.122 1.00 38.80 ? 230 MET B CE  1 
ATOM   1584 N N   . VAL A 1 219 ? -8.839  -1.183  -29.981 1.00 42.49 ? 231 VAL B N   1 
ATOM   1585 C CA  . VAL A 1 219 ? -9.461  -0.456  -28.887 1.00 39.20 ? 231 VAL B CA  1 
ATOM   1586 C C   . VAL A 1 219 ? -9.922  0.864   -29.467 1.00 40.53 ? 231 VAL B C   1 
ATOM   1587 O O   . VAL A 1 219 ? -9.099  1.735   -29.771 1.00 42.83 ? 231 VAL B O   1 
ATOM   1588 C CB  . VAL A 1 219 ? -8.494  -0.232  -27.719 1.00 34.00 ? 231 VAL B CB  1 
ATOM   1589 C CG1 . VAL A 1 219 ? -9.143  0.653   -26.704 1.00 35.10 ? 231 VAL B CG1 1 
ATOM   1590 C CG2 . VAL A 1 219 ? -8.043  -1.567  -27.103 1.00 28.00 ? 231 VAL B CG2 1 
ATOM   1591 N N   . GLU A 1 220 ? -11.222 1.016   -29.649 1.00 45.56 ? 232 GLU B N   1 
ATOM   1592 C CA  . GLU A 1 220 ? -11.682 2.274   -30.205 1.00 46.36 ? 232 GLU B CA  1 
ATOM   1593 C C   . GLU A 1 220 ? -11.677 3.339   -29.111 1.00 44.67 ? 232 GLU B C   1 
ATOM   1594 O O   . GLU A 1 220 ? -11.361 3.070   -27.951 1.00 44.47 ? 232 GLU B O   1 
ATOM   1595 C CB  . GLU A 1 220 ? -13.059 2.096   -30.836 1.00 50.48 ? 232 GLU B CB  1 
ATOM   1596 C CG  . GLU A 1 220 ? -12.976 1.910   -32.343 1.00 54.32 ? 232 GLU B CG  1 
ATOM   1597 C CD  . GLU A 1 220 ? -12.963 3.238   -33.089 1.00 67.13 ? 232 GLU B CD  1 
ATOM   1598 O OE1 . GLU A 1 220 ? -11.886 3.608   -33.619 1.00 63.27 ? 232 GLU B OE1 1 
ATOM   1599 O OE2 . GLU A 1 220 ? -14.025 3.905   -33.154 1.00 65.76 ? 232 GLU B OE2 1 
ATOM   1600 N N   . ILE A 1 221 ? -12.004 4.571   -29.492 1.00 47.87 ? 233 ILE B N   1 
ATOM   1601 C CA  . ILE A 1 221 ? -12.269 5.680   -28.570 1.00 47.69 ? 233 ILE B CA  1 
ATOM   1602 C C   . ILE A 1 221 ? -11.005 6.225   -27.910 1.00 39.41 ? 233 ILE B C   1 
ATOM   1603 O O   . ILE A 1 221 ? -10.768 7.436   -27.936 1.00 40.55 ? 233 ILE B O   1 
ATOM   1604 C CB  . ILE A 1 221 ? -13.298 5.301   -27.486 1.00 48.03 ? 233 ILE B CB  1 
ATOM   1605 C CG1 . ILE A 1 221 ? -14.520 4.617   -28.105 1.00 44.13 ? 233 ILE B CG1 1 
ATOM   1606 C CG2 . ILE A 1 221 ? -13.714 6.552   -26.714 1.00 37.82 ? 233 ILE B CG2 1 
ATOM   1607 C CD1 . ILE A 1 221 ? -15.228 5.459   -29.157 1.00 45.50 ? 233 ILE B CD1 1 
ATOM   1608 N N   . GLU A 1 222 ? -10.212 5.365   -27.278 1.00 34.81 ? 234 GLU B N   1 
ATOM   1609 C CA  . GLU A 1 222 ? -8.956  5.820   -26.692 1.00 33.64 ? 234 GLU B CA  1 
ATOM   1610 C C   . GLU A 1 222 ? -7.974  6.194   -27.799 1.00 29.47 ? 234 GLU B C   1 
ATOM   1611 O O   . GLU A 1 222 ? -7.947  5.558   -28.854 1.00 32.21 ? 234 GLU B O   1 
ATOM   1612 C CB  . GLU A 1 222 ? -8.366  4.722   -25.815 1.00 30.09 ? 234 GLU B CB  1 
ATOM   1613 C CG  . GLU A 1 222 ? -9.318  4.221   -24.770 1.00 34.12 ? 234 GLU B CG  1 
ATOM   1614 C CD  . GLU A 1 222 ? -8.782  2.989   -24.094 1.00 41.32 ? 234 GLU B CD  1 
ATOM   1615 O OE1 . GLU A 1 222 ? -7.543  2.790   -24.195 1.00 37.73 ? 234 GLU B OE1 1 
ATOM   1616 O OE2 . GLU A 1 222 ? -9.587  2.235   -23.476 1.00 38.88 ? 234 GLU B OE2 1 
ATOM   1617 N N   . THR A 1 223 ? -7.171  7.229   -27.572 1.00 23.72 ? 235 THR B N   1 
ATOM   1618 C CA  . THR A 1 223 ? -6.232  7.681   -28.589 1.00 22.49 ? 235 THR B CA  1 
ATOM   1619 C C   . THR A 1 223 ? -4.793  7.575   -28.099 1.00 20.75 ? 235 THR B C   1 
ATOM   1620 O O   . THR A 1 223 ? -4.508  7.060   -27.021 1.00 21.74 ? 235 THR B O   1 
ATOM   1621 C CB  . THR A 1 223 ? -6.535  9.116   -29.011 1.00 25.31 ? 235 THR B CB  1 
ATOM   1622 O OG1 . THR A 1 223 ? -6.213  10.010  -27.939 1.00 31.01 ? 235 THR B OG1 1 
ATOM   1623 C CG2 . THR A 1 223 ? -8.004  9.261   -29.352 1.00 26.67 ? 235 THR B CG2 1 
ATOM   1624 N N   . ASN A 1 224 ? -3.877  8.062   -28.931 1.00 21.95 ? 236 ASN B N   1 
ATOM   1625 C CA  . ASN A 1 224 ? -2.470  8.195   -28.580 1.00 24.07 ? 236 ASN B CA  1 
ATOM   1626 C C   . ASN A 1 224 ? -2.125  9.611   -28.171 1.00 21.17 ? 236 ASN B C   1 
ATOM   1627 O O   . ASN A 1 224 ? -0.986  10.049  -28.363 1.00 20.33 ? 236 ASN B O   1 
ATOM   1628 C CB  . ASN A 1 224 ? -1.583  7.788   -29.751 1.00 23.26 ? 236 ASN B CB  1 
ATOM   1629 C CG  . ASN A 1 224 ? -1.976  8.499   -31.039 1.00 23.36 ? 236 ASN B CG  1 
ATOM   1630 O OD1 . ASN A 1 224 ? -3.111  8.988   -31.186 1.00 22.32 ? 236 ASN B OD1 1 
ATOM   1631 N ND2 . ASN A 1 224 ? -1.047  8.554   -31.983 1.00 21.25 ? 236 ASN B ND2 1 
ATOM   1632 N N   . GLN A 1 225 ? -3.098  10.355  -27.670 1.00 21.44 ? 237 GLN B N   1 
ATOM   1633 C CA  . GLN A 1 225 ? -2.852  11.708  -27.202 1.00 21.53 ? 237 GLN B CA  1 
ATOM   1634 C C   . GLN A 1 225 ? -2.271  11.618  -25.801 1.00 23.01 ? 237 GLN B C   1 
ATOM   1635 O O   . GLN A 1 225 ? -2.952  11.177  -24.868 1.00 27.34 ? 237 GLN B O   1 
ATOM   1636 C CB  . GLN A 1 225 ? -4.145  12.510  -27.247 1.00 20.78 ? 237 GLN B CB  1 
ATOM   1637 C CG  . GLN A 1 225 ? -4.609  12.649  -28.665 1.00 21.29 ? 237 GLN B CG  1 
ATOM   1638 C CD  . GLN A 1 225 ? -5.891  13.386  -28.794 1.00 24.42 ? 237 GLN B CD  1 
ATOM   1639 O OE1 . GLN A 1 225 ? -6.133  14.379  -28.089 1.00 27.07 ? 237 GLN B OE1 1 
ATOM   1640 N NE2 . GLN A 1 225 ? -6.714  12.949  -29.739 1.00 22.04 ? 237 GLN B NE2 1 
ATOM   1641 N N   . LEU A 1 226 ? -1.004  11.993  -25.656 1.00 19.72 ? 238 LEU B N   1 
ATOM   1642 C CA  . LEU A 1 226 ? -0.373  11.910  -24.354 1.00 20.85 ? 238 LEU B CA  1 
ATOM   1643 C C   . LEU A 1 226 ? -1.045  12.864  -23.381 1.00 22.17 ? 238 LEU B C   1 
ATOM   1644 O O   . LEU A 1 226 ? -1.336  14.011  -23.715 1.00 23.63 ? 238 LEU B O   1 
ATOM   1645 C CB  . LEU A 1 226 ? 1.112   12.221  -24.460 1.00 20.13 ? 238 LEU B CB  1 
ATOM   1646 C CG  . LEU A 1 226 ? 1.883   11.204  -25.291 1.00 18.41 ? 238 LEU B CG  1 
ATOM   1647 C CD1 . LEU A 1 226 ? 3.151   11.849  -25.801 1.00 18.78 ? 238 LEU B CD1 1 
ATOM   1648 C CD2 . LEU A 1 226 ? 2.177   9.943   -24.492 1.00 18.62 ? 238 LEU B CD2 1 
ATOM   1649 N N   . GLN A 1 227 ? -1.311  12.378  -22.175 1.00 24.28 ? 239 GLN B N   1 
ATOM   1650 C CA  . GLN A 1 227 ? -1.799  13.216  -21.091 1.00 27.49 ? 239 GLN B CA  1 
ATOM   1651 C C   . GLN A 1 227 ? -0.685  13.447  -20.092 1.00 24.71 ? 239 GLN B C   1 
ATOM   1652 O O   . GLN A 1 227 ? 0.332   12.761  -20.093 1.00 24.55 ? 239 GLN B O   1 
ATOM   1653 C CB  . GLN A 1 227 ? -2.988  12.581  -20.365 1.00 29.75 ? 239 GLN B CB  1 
ATOM   1654 C CG  . GLN A 1 227 ? -4.193  12.276  -21.200 1.00 28.11 ? 239 GLN B CG  1 
ATOM   1655 C CD  . GLN A 1 227 ? -5.082  11.331  -20.455 1.00 29.71 ? 239 GLN B CD  1 
ATOM   1656 O OE1 . GLN A 1 227 ? -5.198  11.414  -19.236 1.00 30.92 ? 239 GLN B OE1 1 
ATOM   1657 N NE2 . GLN A 1 227 ? -5.603  10.340  -21.153 1.00 33.27 ? 239 GLN B NE2 1 
ATOM   1658 N N   . ASP A 1 228 ? -0.902  14.426  -19.226 1.00 27.26 ? 240 ASP B N   1 
ATOM   1659 C CA  . ASP A 1 228 ? 0.013   14.680  -18.122 1.00 27.07 ? 240 ASP B CA  1 
ATOM   1660 C C   . ASP A 1 228 ? -0.025  13.484  -17.182 1.00 27.39 ? 240 ASP B C   1 
ATOM   1661 O O   . ASP A 1 228 ? -1.036  13.242  -16.512 1.00 26.49 ? 240 ASP B O   1 
ATOM   1662 C CB  . ASP A 1 228 ? -0.379  15.967  -17.404 1.00 29.25 ? 240 ASP B CB  1 
ATOM   1663 C CG  . ASP A 1 228 ? 0.738   16.513  -16.510 1.00 30.30 ? 240 ASP B CG  1 
ATOM   1664 O OD1 . ASP A 1 228 ? 1.891   16.050  -16.640 1.00 32.19 ? 240 ASP B OD1 1 
ATOM   1665 O OD2 . ASP A 1 228 ? 0.451   17.382  -15.665 1.00 28.34 ? 240 ASP B OD2 1 
ATOM   1666 N N   . GLY A 1 229 ? 1.073   12.733  -17.131 1.00 26.79 ? 241 GLY B N   1 
ATOM   1667 C CA  . GLY A 1 229 ? 1.144   11.512  -16.351 1.00 27.33 ? 241 GLY B CA  1 
ATOM   1668 C C   . GLY A 1 229 ? 1.138   10.244  -17.172 1.00 27.99 ? 241 GLY B C   1 
ATOM   1669 O O   . GLY A 1 229 ? 1.166   9.155   -16.592 1.00 28.72 ? 241 GLY B O   1 
ATOM   1670 N N   . SER A 1 230 ? 1.085   10.347  -18.498 1.00 27.70 ? 242 SER B N   1 
ATOM   1671 C CA  . SER A 1 230 ? 1.187   9.179   -19.357 1.00 25.06 ? 242 SER B CA  1 
ATOM   1672 C C   . SER A 1 230 ? 2.525   8.491   -19.131 1.00 26.37 ? 242 SER B C   1 
ATOM   1673 O O   . SER A 1 230 ? 3.550   9.151   -18.957 1.00 28.40 ? 242 SER B O   1 
ATOM   1674 C CB  . SER A 1 230 ? 1.053   9.601   -20.822 1.00 21.72 ? 242 SER B CB  1 
ATOM   1675 O OG  . SER A 1 230 ? -0.263  10.036  -21.102 1.00 24.73 ? 242 SER B OG  1 
ATOM   1676 N N   . LEU A 1 231 ? 2.520   7.160   -19.141 1.00 26.65 ? 243 LEU B N   1 
ATOM   1677 C CA  . LEU A 1 231 ? 3.733   6.365   -18.982 1.00 27.48 ? 243 LEU B CA  1 
ATOM   1678 C C   . LEU A 1 231 ? 4.013   5.586   -20.265 1.00 26.48 ? 243 LEU B C   1 
ATOM   1679 O O   . LEU A 1 231 ? 3.110   4.946   -20.820 1.00 26.09 ? 243 LEU B O   1 
ATOM   1680 C CB  . LEU A 1 231 ? 3.595   5.406   -17.795 1.00 29.97 ? 243 LEU B CB  1 
ATOM   1681 C CG  . LEU A 1 231 ? 3.533   6.018   -16.388 1.00 25.61 ? 243 LEU B CG  1 
ATOM   1682 C CD1 . LEU A 1 231 ? 3.444   4.904   -15.382 1.00 27.41 ? 243 LEU B CD1 1 
ATOM   1683 C CD2 . LEU A 1 231 ? 4.722   6.899   -16.067 1.00 22.16 ? 243 LEU B CD2 1 
ATOM   1684 N N   . ILE A 1 232 ? 5.265   5.633   -20.723 1.00 27.39 ? 244 ILE B N   1 
ATOM   1685 C CA  . ILE A 1 232 ? 5.695   5.033   -21.984 1.00 24.72 ? 244 ILE B CA  1 
ATOM   1686 C C   . ILE A 1 232 ? 6.696   3.930   -21.673 1.00 25.40 ? 244 ILE B C   1 
ATOM   1687 O O   . ILE A 1 232 ? 7.829   4.218   -21.275 1.00 27.84 ? 244 ILE B O   1 
ATOM   1688 C CB  . ILE A 1 232 ? 6.322   6.075   -22.921 1.00 21.94 ? 244 ILE B CB  1 
ATOM   1689 C CG1 . ILE A 1 232 ? 5.399   7.270   -23.105 1.00 17.77 ? 244 ILE B CG1 1 
ATOM   1690 C CG2 . ILE A 1 232 ? 6.683   5.433   -24.259 1.00 24.34 ? 244 ILE B CG2 1 
ATOM   1691 C CD1 . ILE A 1 232 ? 6.101   8.474   -23.612 1.00 16.22 ? 244 ILE B CD1 1 
ATOM   1692 N N   . ASP A 1 233 ? 6.307   2.672   -21.882 1.00 24.77 ? 245 ASP B N   1 
ATOM   1693 C CA  . ASP A 1 233 ? 7.202   1.534   -21.680 1.00 28.60 ? 245 ASP B CA  1 
ATOM   1694 C C   . ASP A 1 233 ? 7.781   1.090   -23.021 1.00 30.20 ? 245 ASP B C   1 
ATOM   1695 O O   . ASP A 1 233 ? 7.030   0.730   -23.935 1.00 32.53 ? 245 ASP B O   1 
ATOM   1696 C CB  . ASP A 1 233 ? 6.471   0.382   -20.989 1.00 30.09 ? 245 ASP B CB  1 
ATOM   1697 C CG  . ASP A 1 233 ? 7.314   -0.884  -20.896 1.00 38.67 ? 245 ASP B CG  1 
ATOM   1698 O OD1 . ASP A 1 233 ? 8.474   -0.862  -20.387 1.00 40.33 ? 245 ASP B OD1 1 
ATOM   1699 O OD2 . ASP A 1 233 ? 6.785   -1.923  -21.330 1.00 42.34 ? 245 ASP B OD2 1 
ATOM   1700 N N   . LEU A 1 234 ? 9.114   1.128   -23.137 1.00 28.40 ? 246 LEU B N   1 
ATOM   1701 C CA  . LEU A 1 234 ? 9.813   0.792   -24.370 1.00 27.48 ? 246 LEU B CA  1 
ATOM   1702 C C   . LEU A 1 234 ? 10.519  -0.555  -24.279 1.00 34.62 ? 246 LEU B C   1 
ATOM   1703 O O   . LEU A 1 234 ? 11.531  -0.760  -24.952 1.00 33.42 ? 246 LEU B O   1 
ATOM   1704 C CB  . LEU A 1 234 ? 10.817  1.884   -24.728 1.00 25.38 ? 246 LEU B CB  1 
ATOM   1705 C CG  . LEU A 1 234 ? 10.261  3.302   -24.836 1.00 28.86 ? 246 LEU B CG  1 
ATOM   1706 C CD1 . LEU A 1 234 ? 11.327  4.359   -24.595 1.00 25.66 ? 246 LEU B CD1 1 
ATOM   1707 C CD2 . LEU A 1 234 ? 9.652   3.482   -26.201 1.00 27.28 ? 246 LEU B CD2 1 
ATOM   1708 N N   . CYS A 1 235 ? 9.997   -1.470  -23.447 1.00 38.07 ? 247 CYS B N   1 
ATOM   1709 C CA  . CYS A 1 235 ? 10.566  -2.807  -23.215 1.00 35.78 ? 247 CYS B CA  1 
ATOM   1710 C C   . CYS A 1 235 ? 12.015  -2.727  -22.721 1.00 35.87 ? 247 CYS B C   1 
ATOM   1711 O O   . CYS A 1 235 ? 12.966  -2.998  -23.451 1.00 31.02 ? 247 CYS B O   1 
ATOM   1712 C CB  . CYS A 1 235 ? 10.492  -3.663  -24.482 1.00 33.32 ? 247 CYS B CB  1 
ATOM   1713 S SG  . CYS A 1 235 ? 10.734  -5.432  -24.232 1.00 43.06 ? 247 CYS B SG  1 
ATOM   1714 N N   . GLY A 1 236 ? 12.157  -2.386  -21.439 1.00 36.00 ? 248 GLY B N   1 
ATOM   1715 C CA  . GLY A 1 236 ? 13.466  -2.221  -20.830 1.00 40.29 ? 248 GLY B CA  1 
ATOM   1716 C C   . GLY A 1 236 ? 13.781  -0.801  -20.424 1.00 40.39 ? 248 GLY B C   1 
ATOM   1717 O O   . GLY A 1 236 ? 14.801  -0.564  -19.755 1.00 44.69 ? 248 GLY B O   1 
ATOM   1718 N N   . ALA A 1 237 ? 12.938  0.146   -20.822 1.00 38.50 ? 249 ALA B N   1 
ATOM   1719 C CA  . ALA A 1 237 ? 12.977  1.520   -20.357 1.00 34.81 ? 249 ALA B CA  1 
ATOM   1720 C C   . ALA A 1 237 ? 11.549  2.024   -20.219 1.00 32.16 ? 249 ALA B C   1 
ATOM   1721 O O   . ALA A 1 237 ? 10.685  1.707   -21.040 1.00 30.22 ? 249 ALA B O   1 
ATOM   1722 C CB  . ALA A 1 237 ? 13.762  2.405   -21.314 1.00 25.75 ? 249 ALA B CB  1 
ATOM   1723 N N   . THR A 1 238 ? 11.308  2.804   -19.175 1.00 31.23 ? 250 THR B N   1 
ATOM   1724 C CA  . THR A 1 238 ? 9.997   3.367   -18.883 1.00 30.79 ? 250 THR B CA  1 
ATOM   1725 C C   . THR A 1 238 ? 10.126  4.873   -18.691 1.00 31.93 ? 250 THR B C   1 
ATOM   1726 O O   . THR A 1 238 ? 10.961  5.322   -17.900 1.00 35.29 ? 250 THR B O   1 
ATOM   1727 C CB  . THR A 1 238 ? 9.403   2.728   -17.628 1.00 25.82 ? 250 THR B CB  1 
ATOM   1728 O OG1 . THR A 1 238 ? 9.200   1.332   -17.854 1.00 31.14 ? 250 THR B OG1 1 
ATOM   1729 C CG2 . THR A 1 238 ? 8.108   3.391   -17.274 1.00 25.51 ? 250 THR B CG2 1 
ATOM   1730 N N   . LEU A 1 239 ? 9.294   5.653   -19.386 1.00 27.91 ? 251 LEU B N   1 
ATOM   1731 C CA  . LEU A 1 239 ? 9.340   7.108   -19.299 1.00 26.61 ? 251 LEU B CA  1 
ATOM   1732 C C   . LEU A 1 239 ? 8.056   7.669   -18.687 1.00 29.33 ? 251 LEU B C   1 
ATOM   1733 O O   . LEU A 1 239 ? 6.990   7.047   -18.737 1.00 28.86 ? 251 LEU B O   1 
ATOM   1734 C CB  . LEU A 1 239 ? 9.571   7.726   -20.683 1.00 25.56 ? 251 LEU B CB  1 
ATOM   1735 C CG  . LEU A 1 239 ? 10.737  7.117   -21.479 1.00 30.24 ? 251 LEU B CG  1 
ATOM   1736 C CD1 . LEU A 1 239 ? 10.854  7.719   -22.888 1.00 23.98 ? 251 LEU B CD1 1 
ATOM   1737 C CD2 . LEU A 1 239 ? 12.064  7.246   -20.725 1.00 27.50 ? 251 LEU B CD2 1 
ATOM   1738 N N   . LEU A 1 240 ? 8.162   8.856   -18.106 1.00 27.83 ? 252 LEU B N   1 
ATOM   1739 C CA  . LEU A 1 240 ? 7.008   9.595   -17.623 1.00 25.48 ? 252 LEU B CA  1 
ATOM   1740 C C   . LEU A 1 240 ? 6.879   10.888  -18.417 1.00 25.55 ? 252 LEU B C   1 
ATOM   1741 O O   . LEU A 1 240 ? 7.846   11.647  -18.533 1.00 26.92 ? 252 LEU B O   1 
ATOM   1742 C CB  . LEU A 1 240 ? 7.147   9.896   -16.131 1.00 29.30 ? 252 LEU B CB  1 
ATOM   1743 C CG  . LEU A 1 240 ? 6.140   10.911  -15.601 1.00 25.04 ? 252 LEU B CG  1 
ATOM   1744 C CD1 . LEU A 1 240 ? 4.861   10.224  -15.299 1.00 21.94 ? 252 LEU B CD1 1 
ATOM   1745 C CD2 . LEU A 1 240 ? 6.676   11.610  -14.374 1.00 30.77 ? 252 LEU B CD2 1 
ATOM   1746 N N   . TRP A 1 241 ? 5.699   11.131  -18.974 1.00 24.94 ? 253 TRP B N   1 
ATOM   1747 C CA  . TRP A 1 241 ? 5.429   12.355  -19.720 1.00 25.84 ? 253 TRP B CA  1 
ATOM   1748 C C   . TRP A 1 241 ? 4.747   13.344  -18.774 1.00 24.14 ? 253 TRP B C   1 
ATOM   1749 O O   . TRP A 1 241 ? 3.725   13.012  -18.165 1.00 26.01 ? 253 TRP B O   1 
ATOM   1750 C CB  . TRP A 1 241 ? 4.578   12.054  -20.964 1.00 26.42 ? 253 TRP B CB  1 
ATOM   1751 C CG  . TRP A 1 241 ? 4.230   13.251  -21.801 1.00 22.21 ? 253 TRP B CG  1 
ATOM   1752 C CD1 . TRP A 1 241 ? 3.015   13.852  -21.878 1.00 21.84 ? 253 TRP B CD1 1 
ATOM   1753 C CD2 . TRP A 1 241 ? 5.101   13.983  -22.679 1.00 21.06 ? 253 TRP B CD2 1 
ATOM   1754 N NE1 . TRP A 1 241 ? 3.071   14.927  -22.730 1.00 21.68 ? 253 TRP B NE1 1 
ATOM   1755 C CE2 . TRP A 1 241 ? 4.338   15.033  -23.238 1.00 20.70 ? 253 TRP B CE2 1 
ATOM   1756 C CE3 . TRP A 1 241 ? 6.454   13.867  -23.030 1.00 23.74 ? 253 TRP B CE3 1 
ATOM   1757 C CZ2 . TRP A 1 241 ? 4.872   15.959  -24.146 1.00 19.62 ? 253 TRP B CZ2 1 
ATOM   1758 C CZ3 . TRP A 1 241 ? 6.991   14.796  -23.933 1.00 24.14 ? 253 TRP B CZ3 1 
ATOM   1759 C CH2 . TRP A 1 241 ? 6.192   15.826  -24.479 1.00 22.04 ? 253 TRP B CH2 1 
ATOM   1760 N N   . ARG A 1 242 ? 5.354   14.531  -18.609 1.00 25.96 ? 254 ARG B N   1 
ATOM   1761 C CA  . ARG A 1 242 ? 4.877   15.618  -17.755 1.00 24.81 ? 254 ARG B CA  1 
ATOM   1762 C C   . ARG A 1 242 ? 4.642   16.826  -18.647 1.00 23.19 ? 254 ARG B C   1 
ATOM   1763 O O   . ARG A 1 242 ? 5.468   17.109  -19.520 1.00 24.77 ? 254 ARG B O   1 
ATOM   1764 C CB  . ARG A 1 242 ? 5.908   15.961  -16.659 1.00 28.01 ? 254 ARG B CB  1 
ATOM   1765 C CG  . ARG A 1 242 ? 5.768   15.205  -15.329 1.00 33.10 ? 254 ARG B CG  1 
ATOM   1766 C CD  . ARG A 1 242 ? 4.491   15.531  -14.584 1.00 38.92 ? 254 ARG B CD  1 
ATOM   1767 N NE  . ARG A 1 242 ? 4.054   14.406  -13.767 1.00 46.82 ? 254 ARG B NE  1 
ATOM   1768 C CZ  . ARG A 1 242 ? 2.773   14.108  -13.575 1.00 50.49 ? 254 ARG B CZ  1 
ATOM   1769 N NH1 . ARG A 1 242 ? 1.810   14.846  -14.116 1.00 51.64 ? 254 ARG B NH1 1 
ATOM   1770 N NH2 . ARG A 1 242 ? 2.447   13.026  -12.852 1.00 46.37 ? 254 ARG B NH2 1 
ATOM   1771 N N   . THR A 1 243 ? 3.519   17.529  -18.462 1.00 22.30 ? 255 THR B N   1 
ATOM   1772 C CA  . THR A 1 243 ? 3.164   18.548  -19.449 1.00 27.14 ? 255 THR B CA  1 
ATOM   1773 C C   . THR A 1 243 ? 2.192   19.586  -18.889 1.00 30.38 ? 255 THR B C   1 
ATOM   1774 O O   . THR A 1 243 ? 1.272   19.248  -18.137 1.00 30.22 ? 255 THR B O   1 
ATOM   1775 C CB  . THR A 1 243 ? 2.574   17.893  -20.717 1.00 30.22 ? 255 THR B CB  1 
ATOM   1776 O OG1 . THR A 1 243 ? 2.149   18.900  -21.647 1.00 35.26 ? 255 THR B OG1 1 
ATOM   1777 C CG2 . THR A 1 243 ? 1.397   16.984  -20.380 1.00 28.44 ? 255 THR B CG2 1 
ATOM   1778 N N   . ALA A 1 244 ? 2.390   20.851  -19.292 1.00 31.89 ? 256 ALA B N   1 
ATOM   1779 C CA  . ALA A 1 244 ? 1.505   21.966  -18.950 1.00 29.54 ? 256 ALA B CA  1 
ATOM   1780 C C   . ALA A 1 244 ? 0.490   22.279  -20.049 1.00 33.96 ? 256 ALA B C   1 
ATOM   1781 O O   . ALA A 1 244 ? -0.364  23.162  -19.870 1.00 34.24 ? 256 ALA B O   1 
ATOM   1782 C CB  . ALA A 1 244 ? 2.330   23.219  -18.648 1.00 23.84 ? 256 ALA B CB  1 
ATOM   1783 N N   . GLU A 1 245 ? 0.554   21.561  -21.169 1.00 33.83 ? 257 GLU B N   1 
ATOM   1784 C CA  . GLU A 1 245 ? -0.238  21.836  -22.357 1.00 36.79 ? 257 GLU B CA  1 
ATOM   1785 C C   . GLU A 1 245 ? -0.978  20.578  -22.794 1.00 36.23 ? 257 GLU B C   1 
ATOM   1786 O O   . GLU A 1 245 ? -0.766  19.480  -22.270 1.00 32.73 ? 257 GLU B O   1 
ATOM   1787 C CB  . GLU A 1 245 ? 0.645   22.319  -23.523 1.00 35.36 ? 257 GLU B CB  1 
ATOM   1788 C CG  . GLU A 1 245 ? 1.971   22.969  -23.139 1.00 32.83 ? 257 GLU B CG  1 
ATOM   1789 C CD  . GLU A 1 245 ? 1.814   24.451  -22.861 1.00 41.06 ? 257 GLU B CD  1 
ATOM   1790 O OE1 . GLU A 1 245 ? 0.718   24.984  -23.171 1.00 44.49 ? 257 GLU B OE1 1 
ATOM   1791 O OE2 . GLU A 1 245 ? 2.777   25.080  -22.351 1.00 39.94 ? 257 GLU B OE2 1 
ATOM   1792 N N   . GLY A 1 246 ? -1.852  20.759  -23.781 1.00 34.50 ? 258 GLY B N   1 
ATOM   1793 C CA  . GLY A 1 246 ? -2.372  19.645  -24.541 1.00 28.44 ? 258 GLY B CA  1 
ATOM   1794 C C   . GLY A 1 246 ? -3.728  19.128  -24.129 1.00 30.42 ? 258 GLY B C   1 
ATOM   1795 O O   . GLY A 1 246 ? -4.605  19.875  -23.679 1.00 32.82 ? 258 GLY B O   1 
ATOM   1796 N N   . LEU A 1 247 ? -3.889  17.816  -24.296 1.00 30.65 ? 259 LEU B N   1 
ATOM   1797 C CA  . LEU A 1 247 ? -5.155  17.161  -23.997 1.00 34.13 ? 259 LEU B CA  1 
ATOM   1798 C C   . LEU A 1 247 ? -5.533  17.320  -22.529 1.00 31.95 ? 259 LEU B C   1 
ATOM   1799 O O   . LEU A 1 247 ? -6.690  17.608  -22.204 1.00 31.70 ? 259 LEU B O   1 
ATOM   1800 C CB  . LEU A 1 247 ? -5.053  15.686  -24.371 1.00 29.07 ? 259 LEU B CB  1 
ATOM   1801 C CG  . LEU A 1 247 ? -6.312  14.863  -24.167 1.00 25.82 ? 259 LEU B CG  1 
ATOM   1802 C CD1 . LEU A 1 247 ? -7.391  15.335  -25.122 1.00 26.07 ? 259 LEU B CD1 1 
ATOM   1803 C CD2 . LEU A 1 247 ? -5.976  13.392  -24.359 1.00 26.96 ? 259 LEU B CD2 1 
ATOM   1804 N N   . SER A 1 248 ? -4.563  17.152  -21.630 1.00 27.75 ? 260 SER B N   1 
ATOM   1805 C CA  . SER A 1 248 ? -4.857  17.165  -20.205 1.00 32.17 ? 260 SER B CA  1 
ATOM   1806 C C   . SER A 1 248 ? -5.374  18.510  -19.708 1.00 33.59 ? 260 SER B C   1 
ATOM   1807 O O   . SER A 1 248 ? -6.052  18.547  -18.673 1.00 34.28 ? 260 SER B O   1 
ATOM   1808 C CB  . SER A 1 248 ? -3.614  16.772  -19.403 1.00 29.74 ? 260 SER B CB  1 
ATOM   1809 O OG  . SER A 1 248 ? -3.535  15.372  -19.235 1.00 25.27 ? 260 SER B OG  1 
ATOM   1810 N N   . HIS A 1 249 ? -5.089  19.601  -20.404 1.00 31.62 ? 261 HIS B N   1 
ATOM   1811 C CA  . HIS A 1 249 ? -5.351  20.918  -19.840 1.00 38.23 ? 261 HIS B CA  1 
ATOM   1812 C C   . HIS A 1 249 ? -6.375  21.747  -20.600 1.00 37.33 ? 261 HIS B C   1 
ATOM   1813 O O   . HIS A 1 249 ? -7.052  22.577  -19.979 1.00 31.67 ? 261 HIS B O   1 
ATOM   1814 C CB  . HIS A 1 249 ? -4.030  21.698  -19.708 1.00 35.46 ? 261 HIS B CB  1 
ATOM   1815 C CG  . HIS A 1 249 ? -2.996  20.942  -18.943 1.00 34.64 ? 261 HIS B CG  1 
ATOM   1816 N ND1 . HIS A 1 249 ? -3.066  20.778  -17.576 1.00 36.90 ? 261 HIS B ND1 1 
ATOM   1817 C CD2 . HIS A 1 249 ? -1.916  20.237  -19.354 1.00 36.73 ? 261 HIS B CD2 1 
ATOM   1818 C CE1 . HIS A 1 249 ? -2.049  20.038  -17.172 1.00 38.78 ? 261 HIS B CE1 1 
ATOM   1819 N NE2 . HIS A 1 249 ? -1.336  19.695  -18.231 1.00 38.90 ? 261 HIS B NE2 1 
ATOM   1820 N N   . THR A 1 250 ? -6.533  21.525  -21.892 1.00 36.60 ? 262 THR B N   1 
ATOM   1821 C CA  . THR A 1 250 ? -7.471  22.274  -22.714 1.00 29.69 ? 262 THR B CA  1 
ATOM   1822 C C   . THR A 1 250 ? -8.756  21.474  -22.893 1.00 32.66 ? 262 THR B C   1 
ATOM   1823 O O   . THR A 1 250 ? -8.689  20.261  -23.127 1.00 36.51 ? 262 THR B O   1 
ATOM   1824 C CB  . THR A 1 250 ? -6.844  22.570  -24.077 1.00 28.56 ? 262 THR B CB  1 
ATOM   1825 O OG1 . THR A 1 250 ? -5.760  23.498  -23.922 1.00 30.05 ? 262 THR B OG1 1 
ATOM   1826 C CG2 . THR A 1 250 ? -7.861  23.164  -25.026 1.00 30.78 ? 262 THR B CG2 1 
ATOM   1827 N N   . PRO A 1 251 ? -9.948  22.072  -22.763 1.00 33.52 ? 263 PRO B N   1 
ATOM   1828 C CA  . PRO A 1 251 ? -11.201 21.388  -23.131 1.00 33.33 ? 263 PRO B CA  1 
ATOM   1829 C C   . PRO A 1 251 ? -11.596 21.545  -24.616 1.00 34.91 ? 263 PRO B C   1 
ATOM   1830 O O   . PRO A 1 251 ? -11.245 20.759  -25.507 1.00 36.09 ? 263 PRO B O   1 
ATOM   1831 C CB  . PRO A 1 251 ? -12.235 22.080  -22.240 1.00 29.11 ? 263 PRO B CB  1 
ATOM   1832 C CG  . PRO A 1 251 ? -11.688 23.448  -22.062 1.00 26.67 ? 263 PRO B CG  1 
ATOM   1833 C CD  . PRO A 1 251 ? -10.202 23.265  -21.938 1.00 31.15 ? 263 PRO B CD  1 
ATOM   1834 N N   . ALA B 1 1   ? -20.537 -1.623  0.157   1.00 64.20 ? 13  ALA A N   1 
ATOM   1835 C CA  . ALA B 1 1   ? -19.093 -1.846  -0.053  1.00 59.66 ? 13  ALA A CA  1 
ATOM   1836 C C   . ALA B 1 1   ? -18.242 -0.915  0.822   1.00 63.00 ? 13  ALA A C   1 
ATOM   1837 O O   . ALA B 1 1   ? -18.704 0.152   1.206   1.00 67.03 ? 13  ALA A O   1 
ATOM   1838 C CB  . ALA B 1 1   ? -18.754 -1.679  -1.512  1.00 55.08 ? 13  ALA A CB  1 
ATOM   1839 N N   . PRO B 1 2   ? -17.005 -1.316  1.118   1.00 63.08 ? 14  PRO A N   1 
ATOM   1840 C CA  . PRO B 1 2   ? -16.096 -0.428  1.860   1.00 53.69 ? 14  PRO A CA  1 
ATOM   1841 C C   . PRO B 1 2   ? -15.587 0.690   0.965   1.00 46.56 ? 14  PRO A C   1 
ATOM   1842 O O   . PRO B 1 2   ? -15.675 0.628   -0.267  1.00 43.10 ? 14  PRO A O   1 
ATOM   1843 C CB  . PRO B 1 2   ? -14.934 -1.341  2.293   1.00 45.19 ? 14  PRO A CB  1 
ATOM   1844 C CG  . PRO B 1 2   ? -15.219 -2.669  1.711   1.00 53.74 ? 14  PRO A CG  1 
ATOM   1845 C CD  . PRO B 1 2   ? -16.462 -2.670  0.917   1.00 57.00 ? 14  PRO A CD  1 
ATOM   1846 N N   . VAL B 1 3   ? -15.015 1.710   1.607   1.00 40.65 ? 15  VAL A N   1 
ATOM   1847 C CA  . VAL B 1 3   ? -14.425 2.812   0.861   1.00 35.27 ? 15  VAL A CA  1 
ATOM   1848 C C   . VAL B 1 3   ? -13.091 2.357   0.284   1.00 35.93 ? 15  VAL A C   1 
ATOM   1849 O O   . VAL B 1 3   ? -12.260 1.788   1.006   1.00 30.01 ? 15  VAL A O   1 
ATOM   1850 C CB  . VAL B 1 3   ? -14.241 4.027   1.770   1.00 33.13 ? 15  VAL A CB  1 
ATOM   1851 C CG1 . VAL B 1 3   ? -13.417 5.091   1.074   1.00 32.62 ? 15  VAL A CG1 1 
ATOM   1852 C CG2 . VAL B 1 3   ? -15.575 4.568   2.214   1.00 32.07 ? 15  VAL A CG2 1 
ATOM   1853 N N   . LYS B 1 4   ? -12.891 2.582   -1.026  1.00 34.24 ? 16  LYS A N   1 
ATOM   1854 C CA  . LYS B 1 4   ? -11.567 2.426   -1.612  1.00 29.42 ? 16  LYS A CA  1 
ATOM   1855 C C   . LYS B 1 4   ? -10.786 3.711   -1.415  1.00 28.57 ? 16  LYS A C   1 
ATOM   1856 O O   . LYS B 1 4   ? -11.269 4.792   -1.753  1.00 32.32 ? 16  LYS A O   1 
ATOM   1857 C CB  . LYS B 1 4   ? -11.623 2.075   -3.099  1.00 26.69 ? 16  LYS A CB  1 
ATOM   1858 C CG  . LYS B 1 4   ? -10.274 1.602   -3.631  1.00 20.32 ? 16  LYS A CG  1 
ATOM   1859 C CD  . LYS B 1 4   ? -10.158 1.738   -5.120  1.00 22.04 ? 16  LYS A CD  1 
ATOM   1860 C CE  . LYS B 1 4   ? -10.321 0.395   -5.827  1.00 35.33 ? 16  LYS A CE  1 
ATOM   1861 N NZ  . LYS B 1 4   ? -9.551  0.283   -7.114  1.00 33.82 ? 16  LYS A NZ  1 
ATOM   1862 N N   . TYR B 1 5   ? -9.589  3.589   -0.838  1.00 28.50 ? 17  TYR A N   1 
ATOM   1863 C CA  . TYR B 1 5   ? -8.725  4.736   -0.616  1.00 26.41 ? 17  TYR A CA  1 
ATOM   1864 C C   . TYR B 1 5   ? -7.898  5.058   -1.850  1.00 30.54 ? 17  TYR A C   1 
ATOM   1865 O O   . TYR B 1 5   ? -7.534  6.218   -2.057  1.00 35.50 ? 17  TYR A O   1 
ATOM   1866 C CB  . TYR B 1 5   ? -7.779  4.471   0.557   1.00 27.08 ? 17  TYR A CB  1 
ATOM   1867 C CG  . TYR B 1 5   ? -8.368  4.525   1.955   1.00 28.44 ? 17  TYR A CG  1 
ATOM   1868 C CD1 . TYR B 1 5   ? -9.325  5.465   2.312   1.00 25.17 ? 17  TYR A CD1 1 
ATOM   1869 C CD2 . TYR B 1 5   ? -7.935  3.629   2.933   1.00 31.96 ? 17  TYR A CD2 1 
ATOM   1870 C CE1 . TYR B 1 5   ? -9.845  5.496   3.597   1.00 27.38 ? 17  TYR A CE1 1 
ATOM   1871 C CE2 . TYR B 1 5   ? -8.446  3.653   4.211   1.00 29.93 ? 17  TYR A CE2 1 
ATOM   1872 C CZ  . TYR B 1 5   ? -9.400  4.585   4.543   1.00 29.94 ? 17  TYR A CZ  1 
ATOM   1873 O OH  . TYR B 1 5   ? -9.883  4.592   5.839   1.00 31.54 ? 17  TYR A OH  1 
ATOM   1874 N N   . GLY B 1 6   ? -7.592  4.063   -2.662  1.00 27.08 ? 18  GLY A N   1 
ATOM   1875 C CA  . GLY B 1 6   ? -6.609  4.196   -3.720  1.00 27.07 ? 18  GLY A CA  1 
ATOM   1876 C C   . GLY B 1 6   ? -5.982  2.849   -4.019  1.00 31.94 ? 18  GLY A C   1 
ATOM   1877 O O   . GLY B 1 6   ? -6.226  1.853   -3.339  1.00 33.15 ? 18  GLY A O   1 
ATOM   1878 N N   . GLU B 1 7   ? -5.162  2.823   -5.068  1.00 31.97 ? 19  GLU A N   1 
ATOM   1879 C CA  . GLU B 1 7   ? -4.540  1.594   -5.543  1.00 30.48 ? 19  GLU A CA  1 
ATOM   1880 C C   . GLU B 1 7   ? -3.059  1.836   -5.763  1.00 30.37 ? 19  GLU A C   1 
ATOM   1881 O O   . GLU B 1 7   ? -2.661  2.896   -6.253  1.00 30.25 ? 19  GLU A O   1 
ATOM   1882 C CB  . GLU B 1 7   ? -5.164  1.117   -6.868  1.00 34.30 ? 19  GLU A CB  1 
ATOM   1883 C CG  . GLU B 1 7   ? -5.662  -0.320  -6.914  1.00 35.73 ? 19  GLU A CG  1 
ATOM   1884 C CD  . GLU B 1 7   ? -6.412  -0.611  -8.214  1.00 46.34 ? 19  GLU A CD  1 
ATOM   1885 O OE1 . GLU B 1 7   ? -6.332  0.235   -9.139  1.00 46.32 ? 19  GLU A OE1 1 
ATOM   1886 O OE2 . GLU B 1 7   ? -7.096  -1.663  -8.306  1.00 50.37 ? 19  GLU A OE2 1 
ATOM   1887 N N   . LEU B 1 8   ? -2.246  0.853   -5.420  1.00 27.56 ? 20  LEU A N   1 
ATOM   1888 C CA  . LEU B 1 8   ? -0.828  0.891   -5.726  1.00 28.26 ? 20  LEU A CA  1 
ATOM   1889 C C   . LEU B 1 8   ? -0.567  -0.056  -6.890  1.00 33.49 ? 20  LEU A C   1 
ATOM   1890 O O   . LEU B 1 8   ? -0.875  -1.248  -6.804  1.00 35.70 ? 20  LEU A O   1 
ATOM   1891 C CB  . LEU B 1 8   ? 0.013   0.493   -4.519  1.00 26.61 ? 20  LEU A CB  1 
ATOM   1892 C CG  . LEU B 1 8   ? 0.038   1.395   -3.295  1.00 23.27 ? 20  LEU A CG  1 
ATOM   1893 C CD1 . LEU B 1 8   ? 0.584   0.599   -2.100  1.00 22.47 ? 20  LEU A CD1 1 
ATOM   1894 C CD2 . LEU B 1 8   ? 0.838   2.654   -3.536  1.00 23.18 ? 20  LEU A CD2 1 
ATOM   1895 N N   . ILE B 1 9   ? -0.008  0.472   -7.970  1.00 31.86 ? 21  ILE A N   1 
ATOM   1896 C CA  . ILE B 1 9   ? 0.362   -0.312  -9.139  1.00 30.33 ? 21  ILE A CA  1 
ATOM   1897 C C   . ILE B 1 9   ? 1.879   -0.345  -9.199  1.00 33.30 ? 21  ILE A C   1 
ATOM   1898 O O   . ILE B 1 9   ? 2.526   0.710   -9.237  1.00 30.14 ? 21  ILE A O   1 
ATOM   1899 C CB  . ILE B 1 9   ? -0.221  0.285   -10.429 1.00 33.07 ? 21  ILE A CB  1 
ATOM   1900 C CG1 . ILE B 1 9   ? -1.695  0.646   -10.240 1.00 36.88 ? 21  ILE A CG1 1 
ATOM   1901 C CG2 . ILE B 1 9   ? -0.026  -0.662  -11.589 1.00 35.14 ? 21  ILE A CG2 1 
ATOM   1902 C CD1 . ILE B 1 9   ? -2.179  1.707   -11.193 1.00 33.47 ? 21  ILE A CD1 1 
ATOM   1903 N N   . VAL B 1 10  ? 2.450   -1.547  -9.225  1.00 35.66 ? 22  VAL A N   1 
ATOM   1904 C CA  . VAL B 1 10  ? 3.898   -1.686  -9.324  1.00 31.41 ? 22  VAL A CA  1 
ATOM   1905 C C   . VAL B 1 10  ? 4.330   -1.488  -10.773 1.00 32.50 ? 22  VAL A C   1 
ATOM   1906 O O   . VAL B 1 10  ? 3.766   -2.089  -11.695 1.00 33.83 ? 22  VAL A O   1 
ATOM   1907 C CB  . VAL B 1 10  ? 4.353   -3.049  -8.781  1.00 28.87 ? 22  VAL A CB  1 
ATOM   1908 C CG1 . VAL B 1 10  ? 5.843   -3.278  -9.049  1.00 27.84 ? 22  VAL A CG1 1 
ATOM   1909 C CG2 . VAL B 1 10  ? 4.053   -3.140  -7.303  1.00 31.69 ? 22  VAL A CG2 1 
ATOM   1910 N N   . LEU B 1 11  ? 5.320   -0.621  -10.978 1.00 31.71 ? 23  LEU A N   1 
ATOM   1911 C CA  . LEU B 1 11  ? 5.982   -0.474  -12.268 1.00 36.46 ? 23  LEU A CA  1 
ATOM   1912 C C   . LEU B 1 11  ? 7.118   -1.490  -12.337 1.00 42.69 ? 23  LEU A C   1 
ATOM   1913 O O   . LEU B 1 11  ? 8.067   -1.430  -11.543 1.00 41.73 ? 23  LEU A O   1 
ATOM   1914 C CB  . LEU B 1 11  ? 6.507   0.947   -12.450 1.00 28.20 ? 23  LEU A CB  1 
ATOM   1915 C CG  . LEU B 1 11  ? 5.479   2.054   -12.240 1.00 27.75 ? 23  LEU A CG  1 
ATOM   1916 C CD1 . LEU B 1 11  ? 6.100   3.425   -12.437 1.00 27.21 ? 23  LEU A CD1 1 
ATOM   1917 C CD2 . LEU B 1 11  ? 4.320   1.871   -13.175 1.00 28.99 ? 23  LEU A CD2 1 
ATOM   1918 N N   . GLY B 1 12  ? 7.027   -2.413  -13.291 1.00 42.58 ? 24  GLY A N   1 
ATOM   1919 C CA  . GLY B 1 12  ? 8.006   -3.486  -13.381 1.00 50.81 ? 24  GLY A CA  1 
ATOM   1920 C C   . GLY B 1 12  ? 9.243   -3.085  -14.175 1.00 51.41 ? 24  GLY A C   1 
ATOM   1921 O O   . GLY B 1 12  ? 9.167   -2.400  -15.198 1.00 44.59 ? 24  GLY A O   1 
ATOM   1922 N N   . TYR B 1 13  ? 10.394  -3.554  -13.697 1.00 56.16 ? 25  TYR A N   1 
ATOM   1923 C CA  . TYR B 1 13  ? 11.672  -3.300  -14.351 1.00 63.25 ? 25  TYR A CA  1 
ATOM   1924 C C   . TYR B 1 13  ? 11.978  -4.305  -15.462 1.00 60.60 ? 25  TYR A C   1 
ATOM   1925 O O   . TYR B 1 13  ? 12.950  -4.119  -16.213 1.00 56.95 ? 25  TYR A O   1 
ATOM   1926 C CB  . TYR B 1 13  ? 12.803  -3.309  -13.302 1.00 59.93 ? 25  TYR A CB  1 
ATOM   1927 C CG  . TYR B 1 13  ? 12.662  -2.268  -12.196 1.00 52.33 ? 25  TYR A CG  1 
ATOM   1928 C CD1 . TYR B 1 13  ? 11.743  -1.223  -12.298 1.00 53.74 ? 25  TYR A CD1 1 
ATOM   1929 C CD2 . TYR B 1 13  ? 13.448  -2.331  -11.052 1.00 53.89 ? 25  TYR A CD2 1 
ATOM   1930 C CE1 . TYR B 1 13  ? 11.611  -0.265  -11.290 1.00 49.98 ? 25  TYR A CE1 1 
ATOM   1931 C CE2 . TYR B 1 13  ? 13.322  -1.376  -10.033 1.00 52.94 ? 25  TYR A CE2 1 
ATOM   1932 C CZ  . TYR B 1 13  ? 12.404  -0.348  -10.157 1.00 48.69 ? 25  TYR A CZ  1 
ATOM   1933 O OH  . TYR B 1 13  ? 12.277  0.586   -9.144  1.00 42.07 ? 25  TYR A OH  1 
ATOM   1934 N N   . ASN B 1 14  ? 11.153  -5.345  -15.599 1.00 62.41 ? 26  ASN A N   1 
ATOM   1935 C CA  . ASN B 1 14  ? 11.525  -6.484  -16.429 1.00 62.92 ? 26  ASN A CA  1 
ATOM   1936 C C   . ASN B 1 14  ? 11.494  -6.141  -17.911 1.00 58.24 ? 26  ASN A C   1 
ATOM   1937 O O   . ASN B 1 14  ? 12.243  -6.730  -18.705 1.00 56.12 ? 26  ASN A O   1 
ATOM   1938 C CB  . ASN B 1 14  ? 10.590  -7.662  -16.127 1.00 57.69 ? 26  ASN A CB  1 
ATOM   1939 C CG  . ASN B 1 14  ? 11.183  -9.020  -16.536 1.00 69.00 ? 26  ASN A CG  1 
ATOM   1940 O OD1 . ASN B 1 14  ? 10.539  -10.061 -16.350 1.00 73.47 ? 26  ASN A OD1 1 
ATOM   1941 N ND2 . ASN B 1 14  ? 12.389  -9.010  -17.126 1.00 68.13 ? 26  ASN A ND2 1 
ATOM   1942 N N   . GLY B 1 15  ? 10.659  -5.184  -18.303 1.00 53.82 ? 27  GLY A N   1 
ATOM   1943 C CA  . GLY B 1 15  ? 10.325  -5.132  -19.707 1.00 49.43 ? 27  GLY A CA  1 
ATOM   1944 C C   . GLY B 1 15  ? 9.395   -6.236  -20.149 1.00 42.33 ? 27  GLY A C   1 
ATOM   1945 O O   . GLY B 1 15  ? 9.221   -6.428  -21.352 1.00 43.45 ? 27  GLY A O   1 
ATOM   1946 N N   . SER B 1 16  ? 8.801   -6.973  -19.210 1.00 45.47 ? 28  SER A N   1 
ATOM   1947 C CA  . SER B 1 16  ? 7.705   -7.878  -19.514 1.00 45.28 ? 28  SER A CA  1 
ATOM   1948 C C   . SER B 1 16  ? 6.400   -7.100  -19.674 1.00 43.08 ? 28  SER A C   1 
ATOM   1949 O O   . SER B 1 16  ? 6.302   -5.907  -19.356 1.00 42.13 ? 28  SER A O   1 
ATOM   1950 C CB  . SER B 1 16  ? 7.524   -8.919  -18.411 1.00 49.42 ? 28  SER A CB  1 
ATOM   1951 O OG  . SER B 1 16  ? 8.753   -9.363  -17.886 1.00 56.60 ? 28  SER A OG  1 
ATOM   1952 N N   . LEU B 1 17  ? 5.384   -7.799  -20.172 1.00 44.01 ? 29  LEU A N   1 
ATOM   1953 C CA  . LEU B 1 17  ? 4.065   -7.195  -20.316 1.00 45.40 ? 29  LEU A CA  1 
ATOM   1954 C C   . LEU B 1 17  ? 3.513   -6.852  -18.937 1.00 46.24 ? 29  LEU A C   1 
ATOM   1955 O O   . LEU B 1 17  ? 3.692   -7.627  -17.990 1.00 48.74 ? 29  LEU A O   1 
ATOM   1956 C CB  . LEU B 1 17  ? 3.097   -8.138  -21.040 1.00 42.47 ? 29  LEU A CB  1 
ATOM   1957 C CG  . LEU B 1 17  ? 3.256   -8.334  -22.549 1.00 37.59 ? 29  LEU A CG  1 
ATOM   1958 C CD1 . LEU B 1 17  ? 2.160   -9.231  -23.037 1.00 38.63 ? 29  LEU A CD1 1 
ATOM   1959 C CD2 . LEU B 1 17  ? 3.223   -7.016  -23.303 1.00 36.70 ? 29  LEU A CD2 1 
ATOM   1960 N N   . PRO B 1 18  ? 2.875   -5.697  -18.778 1.00 41.35 ? 30  PRO A N   1 
ATOM   1961 C CA  . PRO B 1 18  ? 2.325   -5.339  -17.468 1.00 42.41 ? 30  PRO A CA  1 
ATOM   1962 C C   . PRO B 1 18  ? 1.305   -6.364  -16.999 1.00 59.16 ? 30  PRO A C   1 
ATOM   1963 O O   . PRO B 1 18  ? 0.371   -6.714  -17.725 1.00 59.42 ? 30  PRO A O   1 
ATOM   1964 C CB  . PRO B 1 18  ? 1.686   -3.980  -17.722 1.00 37.70 ? 30  PRO A CB  1 
ATOM   1965 C CG  . PRO B 1 18  ? 2.504   -3.402  -18.812 1.00 40.86 ? 30  PRO A CG  1 
ATOM   1966 C CD  . PRO B 1 18  ? 2.935   -4.543  -19.683 1.00 38.47 ? 30  PRO A CD  1 
ATOM   1967 N N   . ASN B 1 19  ? 1.490   -6.829  -15.760 1.00 70.12 ? 31  ASN A N   1 
ATOM   1968 C CA  . ASN B 1 19  ? 0.876   -8.048  -15.240 1.00 69.14 ? 31  ASN A CA  1 
ATOM   1969 C C   . ASN B 1 19  ? -0.555  -7.791  -14.744 1.00 72.85 ? 31  ASN A C   1 
ATOM   1970 O O   . ASN B 1 19  ? -1.107  -6.690  -14.869 1.00 74.47 ? 31  ASN A O   1 
ATOM   1971 C CB  . ASN B 1 19  ? 1.757   -8.640  -14.128 1.00 76.32 ? 31  ASN A CB  1 
ATOM   1972 C CG  . ASN B 1 19  ? 3.271   -8.631  -14.480 1.00 82.57 ? 31  ASN A CG  1 
ATOM   1973 O OD1 . ASN B 1 19  ? 3.800   -7.644  -15.008 1.00 81.67 ? 31  ASN A OD1 1 
ATOM   1974 N ND2 . ASN B 1 19  ? 3.966   -9.728  -14.159 1.00 78.86 ? 31  ASN A ND2 1 
ATOM   1975 N N   . GLY B 1 20  ? -1.172  -8.832  -14.181 1.00 70.49 ? 32  GLY A N   1 
ATOM   1976 C CA  . GLY B 1 20  ? -2.514  -8.723  -13.628 1.00 65.19 ? 32  GLY A CA  1 
ATOM   1977 C C   . GLY B 1 20  ? -2.849  -9.756  -12.565 1.00 68.30 ? 32  GLY A C   1 
ATOM   1978 O O   . GLY B 1 20  ? -1.971  -10.444 -12.034 1.00 58.83 ? 32  GLY A O   1 
ATOM   1979 N N   . LYS B 1 26  ? 0.578   -9.513  -6.134  1.00 32.19 ? 38  LYS A N   1 
ATOM   1980 C CA  . LYS B 1 26  ? 0.282   -9.131  -7.522  1.00 36.54 ? 38  LYS A CA  1 
ATOM   1981 C C   . LYS B 1 26  ? 0.826   -7.717  -7.816  1.00 39.58 ? 38  LYS A C   1 
ATOM   1982 O O   . LYS B 1 26  ? 1.302   -7.021  -6.919  1.00 40.81 ? 38  LYS A O   1 
ATOM   1983 C CB  . LYS B 1 26  ? -1.241  -9.212  -7.791  1.00 39.83 ? 38  LYS A CB  1 
ATOM   1984 C CG  . LYS B 1 26  ? -1.734  -8.877  -9.249  1.00 45.94 ? 38  LYS A CG  1 
ATOM   1985 C CD  . LYS B 1 26  ? -3.278  -8.931  -9.401  1.00 50.44 ? 38  LYS A CD  1 
ATOM   1986 C CE  . LYS B 1 26  ? -3.934  -7.551  -9.465  1.00 41.14 ? 38  LYS A CE  1 
ATOM   1987 N NZ  . LYS B 1 26  ? -5.228  -7.518  -8.711  1.00 36.17 ? 38  LYS A NZ  1 
ATOM   1988 N N   . SER B 1 27  ? 0.759   -7.299  -9.079  1.00 37.57 ? 39  SER A N   1 
ATOM   1989 C CA  . SER B 1 27  ? 1.242   -5.987  -9.485  1.00 40.67 ? 39  SER A CA  1 
ATOM   1990 C C   . SER B 1 27  ? 0.343   -4.836  -9.028  1.00 36.79 ? 39  SER A C   1 
ATOM   1991 O O   . SER B 1 27  ? 0.793   -3.688  -9.045  1.00 36.38 ? 39  SER A O   1 
ATOM   1992 C CB  . SER B 1 27  ? 1.423   -5.974  -11.013 1.00 47.99 ? 39  SER A CB  1 
ATOM   1993 O OG  . SER B 1 27  ? 0.282   -5.475  -11.687 1.00 53.07 ? 39  SER A OG  1 
ATOM   1994 N N   . ARG B 1 28  ? -0.893  -5.109  -8.622  1.00 35.77 ? 40  ARG A N   1 
ATOM   1995 C CA  . ARG B 1 28  ? -1.836  -4.096  -8.170  1.00 34.83 ? 40  ARG A CA  1 
ATOM   1996 C C   . ARG B 1 28  ? -2.262  -4.417  -6.741  1.00 35.90 ? 40  ARG A C   1 
ATOM   1997 O O   . ARG B 1 28  ? -2.302  -5.588  -6.340  1.00 36.33 ? 40  ARG A O   1 
ATOM   1998 C CB  . ARG B 1 28  ? -3.072  -4.039  -9.091  1.00 37.99 ? 40  ARG A CB  1 
ATOM   1999 C CG  . ARG B 1 28  ? -3.474  -2.661  -9.555  1.00 35.28 ? 40  ARG A CG  1 
ATOM   2000 C CD  . ARG B 1 28  ? -4.327  -2.757  -10.811 1.00 40.21 ? 40  ARG A CD  1 
ATOM   2001 N NE  . ARG B 1 28  ? -4.316  -1.506  -11.566 1.00 48.00 ? 40  ARG A NE  1 
ATOM   2002 C CZ  . ARG B 1 28  ? -3.709  -1.344  -12.742 1.00 55.04 ? 40  ARG A CZ  1 
ATOM   2003 N NH1 . ARG B 1 28  ? -3.045  -2.331  -13.322 1.00 49.48 ? 40  ARG A NH1 1 
ATOM   2004 N NH2 . ARG B 1 28  ? -3.760  -0.156  -13.350 1.00 48.65 ? 40  ARG A NH2 1 
ATOM   2005 N N   . PHE B 1 29  ? -2.572  -3.372  -5.965  1.00 31.93 ? 41  PHE A N   1 
ATOM   2006 C CA  . PHE B 1 29  ? -3.136  -3.556  -4.630  1.00 29.64 ? 41  PHE A CA  1 
ATOM   2007 C C   . PHE B 1 29  ? -4.014  -2.368  -4.297  1.00 29.11 ? 41  PHE A C   1 
ATOM   2008 O O   . PHE B 1 29  ? -3.557  -1.226  -4.342  1.00 30.73 ? 41  PHE A O   1 
ATOM   2009 C CB  . PHE B 1 29  ? -2.045  -3.715  -3.575  1.00 32.51 ? 41  PHE A CB  1 
ATOM   2010 C CG  . PHE B 1 29  ? -2.579  -4.020  -2.183  1.00 36.68 ? 41  PHE A CG  1 
ATOM   2011 C CD1 . PHE B 1 29  ? -3.474  -5.071  -1.970  1.00 37.55 ? 41  PHE A CD1 1 
ATOM   2012 C CD2 . PHE B 1 29  ? -2.187  -3.251  -1.086  1.00 32.12 ? 41  PHE A CD2 1 
ATOM   2013 C CE1 . PHE B 1 29  ? -3.956  -5.349  -0.689  1.00 31.59 ? 41  PHE A CE1 1 
ATOM   2014 C CE2 . PHE B 1 29  ? -2.670  -3.528  0.184   1.00 31.45 ? 41  PHE A CE2 1 
ATOM   2015 C CZ  . PHE B 1 29  ? -3.558  -4.571  0.381   1.00 30.54 ? 41  PHE A CZ  1 
ATOM   2016 N N   . ALA B 1 30  ? -5.263  -2.633  -3.956  1.00 31.51 ? 42  ALA A N   1 
ATOM   2017 C CA  . ALA B 1 30  ? -6.158  -1.576  -3.513  1.00 33.27 ? 42  ALA A CA  1 
ATOM   2018 C C   . ALA B 1 30  ? -6.106  -1.429  -1.998  1.00 32.57 ? 42  ALA A C   1 
ATOM   2019 O O   . ALA B 1 30  ? -5.909  -2.404  -1.261  1.00 33.67 ? 42  ALA A O   1 
ATOM   2020 C CB  . ALA B 1 30  ? -7.598  -1.847  -3.958  1.00 31.47 ? 42  ALA A CB  1 
ATOM   2021 N N   . LEU B 1 31  ? -6.279  -0.192  -1.538  1.00 29.38 ? 43  LEU A N   1 
ATOM   2022 C CA  . LEU B 1 31  ? -6.371  0.106   -0.114  1.00 31.47 ? 43  LEU A CA  1 
ATOM   2023 C C   . LEU B 1 31  ? -7.832  0.383   0.213   1.00 31.21 ? 43  LEU A C   1 
ATOM   2024 O O   . LEU B 1 31  ? -8.485  1.153   -0.497  1.00 31.85 ? 43  LEU A O   1 
ATOM   2025 C CB  . LEU B 1 31  ? -5.505  1.313   0.266   1.00 30.27 ? 43  LEU A CB  1 
ATOM   2026 C CG  . LEU B 1 31  ? -3.980  1.230   0.089   1.00 29.50 ? 43  LEU A CG  1 
ATOM   2027 C CD1 . LEU B 1 31  ? -3.259  2.312   0.910   1.00 25.38 ? 43  LEU A CD1 1 
ATOM   2028 C CD2 . LEU B 1 31  ? -3.435  -0.147  0.408   1.00 27.29 ? 43  LEU A CD2 1 
ATOM   2029 N N   . PHE B 1 32  ? -8.348  -0.248  1.266   1.00 32.17 ? 44  PHE A N   1 
ATOM   2030 C CA  . PHE B 1 32  ? -9.753  -0.111  1.627   1.00 31.30 ? 44  PHE A CA  1 
ATOM   2031 C C   . PHE B 1 32  ? -9.908  0.286   3.096   1.00 30.38 ? 44  PHE A C   1 
ATOM   2032 O O   . PHE B 1 32  ? -9.134  -0.157  3.948   1.00 35.64 ? 44  PHE A O   1 
ATOM   2033 C CB  . PHE B 1 32  ? -10.511 -1.426  1.352   1.00 30.39 ? 44  PHE A CB  1 
ATOM   2034 C CG  . PHE B 1 32  ? -10.778 -1.689  -0.100  1.00 29.57 ? 44  PHE A CG  1 
ATOM   2035 C CD1 . PHE B 1 32  ? -11.755 -0.961  -0.778  1.00 33.05 ? 44  PHE A CD1 1 
ATOM   2036 C CD2 . PHE B 1 32  ? -10.072 -2.669  -0.787  1.00 28.83 ? 44  PHE A CD2 1 
ATOM   2037 C CE1 . PHE B 1 32  ? -12.021 -1.190  -2.131  1.00 28.00 ? 44  PHE A CE1 1 
ATOM   2038 C CE2 . PHE B 1 32  ? -10.328 -2.913  -2.144  1.00 32.04 ? 44  PHE A CE2 1 
ATOM   2039 C CZ  . PHE B 1 32  ? -11.302 -2.168  -2.815  1.00 32.59 ? 44  PHE A CZ  1 
ATOM   2040 N N   . LYS B 1 33  ? -10.933 1.096   3.392   1.00 29.33 ? 45  LYS A N   1 
ATOM   2041 C CA  . LYS B 1 33  ? -11.196 1.537   4.763   1.00 31.52 ? 45  LYS A CA  1 
ATOM   2042 C C   . LYS B 1 33  ? -11.453 0.361   5.692   1.00 30.10 ? 45  LYS A C   1 
ATOM   2043 O O   . LYS B 1 33  ? -12.357 -0.441  5.455   1.00 34.16 ? 45  LYS A O   1 
ATOM   2044 C CB  . LYS B 1 33  ? -12.394 2.481   4.803   1.00 30.97 ? 45  LYS A CB  1 
ATOM   2045 C CG  . LYS B 1 33  ? -12.767 2.921   6.214   1.00 30.05 ? 45  LYS A CG  1 
ATOM   2046 C CD  . LYS B 1 33  ? -13.483 4.258   6.196   1.00 31.59 ? 45  LYS A CD  1 
ATOM   2047 C CE  . LYS B 1 33  ? -14.434 4.429   7.376   1.00 34.17 ? 45  LYS A CE  1 
ATOM   2048 N NZ  . LYS B 1 33  ? -15.360 5.594   7.184   1.00 30.49 ? 45  LYS A NZ  1 
ATOM   2049 N N   . ARG B 1 34  ? -10.680 0.280   6.773   1.00 32.07 ? 46  ARG A N   1 
ATOM   2050 C CA  . ARG B 1 34  ? -10.745 -0.885  7.639   1.00 35.99 ? 46  ARG A CA  1 
ATOM   2051 C C   . ARG B 1 34  ? -11.978 -0.832  8.534   1.00 39.56 ? 46  ARG A C   1 
ATOM   2052 O O   . ARG B 1 34  ? -12.532 0.240   8.800   1.00 37.88 ? 46  ARG A O   1 
ATOM   2053 C CB  . ARG B 1 34  ? -9.485  -1.003  8.500   1.00 32.83 ? 46  ARG A CB  1 
ATOM   2054 C CG  . ARG B 1 34  ? -8.285  -1.667  7.809   1.00 36.59 ? 46  ARG A CG  1 
ATOM   2055 C CD  . ARG B 1 34  ? -7.027  -1.607  8.690   1.00 35.14 ? 46  ARG A CD  1 
ATOM   2056 N NE  . ARG B 1 34  ? -5.779  -1.356  7.967   1.00 36.80 ? 46  ARG A NE  1 
ATOM   2057 C CZ  . ARG B 1 34  ? -4.992  -2.287  7.429   1.00 38.62 ? 46  ARG A CZ  1 
ATOM   2058 N NH1 . ARG B 1 34  ? -5.344  -3.563  7.393   1.00 43.71 ? 46  ARG A NH1 1 
ATOM   2059 N NH2 . ARG B 1 34  ? -3.816  -1.928  6.917   1.00 32.90 ? 46  ARG A NH2 1 
ATOM   2060 N N   . PRO B 1 35  ? -12.449 -1.997  8.979   1.00 39.23 ? 47  PRO A N   1 
ATOM   2061 C CA  . PRO B 1 35  ? -13.609 -2.025  9.893   1.00 34.72 ? 47  PRO A CA  1 
ATOM   2062 C C   . PRO B 1 35  ? -13.404 -1.279  11.207  1.00 36.40 ? 47  PRO A C   1 
ATOM   2063 O O   . PRO B 1 35  ? -14.297 -0.536  11.635  1.00 34.49 ? 47  PRO A O   1 
ATOM   2064 C CB  . PRO B 1 35  ? -13.820 -3.530  10.087  1.00 32.38 ? 47  PRO A CB  1 
ATOM   2065 C CG  . PRO B 1 35  ? -13.461 -4.081  8.726   1.00 29.81 ? 47  PRO A CG  1 
ATOM   2066 C CD  . PRO B 1 35  ? -12.232 -3.300  8.322   1.00 32.41 ? 47  PRO A CD  1 
ATOM   2067 N N   . LYS B 1 36  ? -12.269 -1.467  11.874  1.00 37.90 ? 48  LYS A N   1 
ATOM   2068 C CA  . LYS B 1 36  ? -11.860 -0.599  12.974  1.00 36.18 ? 48  LYS A CA  1 
ATOM   2069 C C   . LYS B 1 36  ? -10.558 0.098   12.586  1.00 28.96 ? 48  LYS A C   1 
ATOM   2070 O O   . LYS B 1 36  ? -9.703  -0.488  11.917  1.00 26.46 ? 48  LYS A O   1 
ATOM   2071 C CB  . LYS B 1 36  ? -11.672 -1.380  14.309  1.00 38.40 ? 48  LYS A CB  1 
ATOM   2072 C CG  . LYS B 1 36  ? -12.789 -2.378  14.695  1.00 43.82 ? 48  LYS A CG  1 
ATOM   2073 C CD  . LYS B 1 36  ? -13.907 -1.751  15.571  1.00 48.76 ? 48  LYS A CD  1 
ATOM   2074 C CE  . LYS B 1 36  ? -15.225 -2.560  15.534  1.00 42.74 ? 48  LYS A CE  1 
ATOM   2075 N NZ  . LYS B 1 36  ? -15.568 -3.144  14.186  1.00 47.07 ? 48  LYS A NZ  1 
ATOM   2076 N N   . ALA B 1 37  ? -10.415 1.353   12.994  1.00 26.01 ? 49  ALA A N   1 
ATOM   2077 C CA  . ALA B 1 37  ? -9.176  2.082   12.758  1.00 28.56 ? 49  ALA A CA  1 
ATOM   2078 C C   . ALA B 1 37  ? -7.967  1.322   13.311  1.00 28.05 ? 49  ALA A C   1 
ATOM   2079 O O   . ALA B 1 37  ? -8.046  0.650   14.340  1.00 26.38 ? 49  ALA A O   1 
ATOM   2080 C CB  . ALA B 1 37  ? -9.253  3.467   13.401  1.00 27.75 ? 49  ALA A CB  1 
ATOM   2081 N N   . ASN B 1 38  ? -6.825  1.447   12.618  1.00 26.10 ? 50  ASN A N   1 
ATOM   2082 C CA  . ASN B 1 38  ? -5.588  0.820   13.066  1.00 24.66 ? 50  ASN A CA  1 
ATOM   2083 C C   . ASN B 1 38  ? -4.407  1.776   12.952  1.00 26.52 ? 50  ASN A C   1 
ATOM   2084 O O   . ASN B 1 38  ? -3.252  1.352   13.131  1.00 24.05 ? 50  ASN A O   1 
ATOM   2085 C CB  . ASN B 1 38  ? -5.313  -0.449  12.273  1.00 24.14 ? 50  ASN A CB  1 
ATOM   2086 C CG  . ASN B 1 38  ? -4.822  -0.159  10.885  1.00 26.53 ? 50  ASN A CG  1 
ATOM   2087 O OD1 . ASN B 1 38  ? -5.249  0.799   10.268  1.00 30.07 ? 50  ASN A OD1 1 
ATOM   2088 N ND2 . ASN B 1 38  ? -3.936  -0.994  10.375  1.00 27.27 ? 50  ASN A ND2 1 
ATOM   2089 N N   . GLY B 1 39  ? -4.664  3.048   12.655  1.00 26.06 ? 51  GLY A N   1 
ATOM   2090 C CA  . GLY B 1 39  ? -3.598  4.012   12.542  1.00 23.87 ? 51  GLY A CA  1 
ATOM   2091 C C   . GLY B 1 39  ? -3.076  4.447   13.886  1.00 22.29 ? 51  GLY A C   1 
ATOM   2092 O O   . GLY B 1 39  ? -3.761  4.373   14.903  1.00 24.80 ? 51  GLY A O   1 
ATOM   2093 N N   . VAL B 1 40  ? -1.830  4.905   13.885  1.00 23.03 ? 52  VAL A N   1 
ATOM   2094 C CA  . VAL B 1 40  ? -1.194  5.426   15.084  1.00 22.34 ? 52  VAL A CA  1 
ATOM   2095 C C   . VAL B 1 40  ? -0.730  6.848   14.807  1.00 20.36 ? 52  VAL A C   1 
ATOM   2096 O O   . VAL B 1 40  ? -0.594  7.274   13.663  1.00 21.42 ? 52  VAL A O   1 
ATOM   2097 C CB  . VAL B 1 40  ? -0.015  4.553   15.551  1.00 23.21 ? 52  VAL A CB  1 
ATOM   2098 C CG1 . VAL B 1 40  ? -0.513  3.188   16.048  1.00 23.70 ? 52  VAL A CG1 1 
ATOM   2099 C CG2 . VAL B 1 40  ? 0.991   4.402   14.443  1.00 24.46 ? 52  VAL A CG2 1 
ATOM   2100 N N   . LYS B 1 41  ? -0.489  7.580   15.883  1.00 19.66 ? 53  LYS A N   1 
ATOM   2101 C CA  . LYS B 1 41  ? -0.046  8.957   15.842  1.00 21.54 ? 53  LYS A CA  1 
ATOM   2102 C C   . LYS B 1 41  ? 1.028   9.121   16.923  1.00 23.25 ? 53  LYS A C   1 
ATOM   2103 O O   . LYS B 1 41  ? 1.033   8.365   17.893  1.00 21.77 ? 53  LYS A O   1 
ATOM   2104 C CB  . LYS B 1 41  ? -1.199  9.932   16.122  1.00 26.43 ? 53  LYS A CB  1 
ATOM   2105 C CG  . LYS B 1 41  ? -1.985  9.627   17.408  1.00 26.00 ? 53  LYS A CG  1 
ATOM   2106 C CD  . LYS B 1 41  ? -3.298  10.441  17.481  1.00 26.97 ? 53  LYS A CD  1 
ATOM   2107 C CE  . LYS B 1 41  ? -3.559  11.011  18.878  1.00 28.98 ? 53  LYS A CE  1 
ATOM   2108 N NZ  . LYS B 1 41  ? -4.385  12.265  18.844  1.00 26.99 ? 53  LYS A NZ  1 
ATOM   2109 N N   . PRO B 1 42  ? 1.899   10.115  16.765  1.00 21.89 ? 54  PRO A N   1 
ATOM   2110 C CA  . PRO B 1 42  ? 2.989   10.295  17.749  1.00 21.56 ? 54  PRO A CA  1 
ATOM   2111 C C   . PRO B 1 42  ? 2.501   10.633  19.150  1.00 20.52 ? 54  PRO A C   1 
ATOM   2112 O O   . PRO B 1 42  ? 1.461   11.267  19.347  1.00 23.16 ? 54  PRO A O   1 
ATOM   2113 C CB  . PRO B 1 42  ? 3.799   11.458  17.155  1.00 18.87 ? 54  PRO A CB  1 
ATOM   2114 C CG  . PRO B 1 42  ? 3.467   11.435  15.719  1.00 15.76 ? 54  PRO A CG  1 
ATOM   2115 C CD  . PRO B 1 42  ? 2.027   11.039  15.642  1.00 16.19 ? 54  PRO A CD  1 
ATOM   2116 N N   . SER B 1 43  ? 3.306   10.237  20.134  1.00 21.48 ? 55  SER A N   1 
ATOM   2117 C CA  . SER B 1 43  ? 2.950   10.354  21.543  1.00 24.73 ? 55  SER A CA  1 
ATOM   2118 C C   . SER B 1 43  ? 4.168   10.634  22.428  1.00 25.07 ? 55  SER A C   1 
ATOM   2119 O O   . SER B 1 43  ? 5.026   11.449  22.066  1.00 24.08 ? 55  SER A O   1 
ATOM   2120 C CB  . SER B 1 43  ? 2.250   9.074   21.997  1.00 26.74 ? 55  SER A CB  1 
ATOM   2121 O OG  . SER B 1 43  ? 1.438   9.298   23.120  1.00 28.95 ? 55  SER A OG  1 
ATOM   2122 N N   . THR B 1 44  ? 4.268   9.931   23.564  1.00 23.76 ? 56  THR A N   1 
ATOM   2123 C CA  . THR B 1 44  ? 5.252   10.256  24.598  1.00 25.47 ? 56  THR A CA  1 
ATOM   2124 C C   . THR B 1 44  ? 6.687   9.989   24.154  1.00 25.29 ? 56  THR A C   1 
ATOM   2125 O O   . THR B 1 44  ? 7.004   8.897   23.671  1.00 29.67 ? 56  THR A O   1 
ATOM   2126 C CB  . THR B 1 44  ? 4.970   9.445   25.862  1.00 24.66 ? 56  THR A CB  1 
ATOM   2127 O OG1 . THR B 1 44  ? 3.628   9.673   26.291  1.00 29.35 ? 56  THR A OG1 1 
ATOM   2128 C CG2 . THR B 1 44  ? 5.910   9.842   26.968  1.00 21.12 ? 56  THR A CG2 1 
ATOM   2129 N N   . VAL B 1 45  ? 7.575   10.959  24.379  1.00 19.69 ? 57  VAL A N   1 
ATOM   2130 C CA  . VAL B 1 45  ? 8.996   10.779  24.093  1.00 21.86 ? 57  VAL A CA  1 
ATOM   2131 C C   . VAL B 1 45  ? 9.709   10.331  25.359  1.00 20.37 ? 57  VAL A C   1 
ATOM   2132 O O   . VAL B 1 45  ? 9.455   10.852  26.442  1.00 19.57 ? 57  VAL A O   1 
ATOM   2133 C CB  . VAL B 1 45  ? 9.632   12.069  23.536  1.00 21.55 ? 57  VAL A CB  1 
ATOM   2134 C CG1 . VAL B 1 45  ? 11.104  11.837  23.225  1.00 19.96 ? 57  VAL A CG1 1 
ATOM   2135 C CG2 . VAL B 1 45  ? 8.904   12.522  22.288  1.00 23.49 ? 57  VAL A CG2 1 
ATOM   2136 N N   . HIS B 1 46  ? 10.620  9.380   25.225  1.00 23.02 ? 58  HIS A N   1 
ATOM   2137 C CA  . HIS B 1 46  ? 11.459  8.962   26.336  1.00 22.09 ? 58  HIS A CA  1 
ATOM   2138 C C   . HIS B 1 46  ? 12.936  9.155   25.988  1.00 24.14 ? 58  HIS A C   1 
ATOM   2139 O O   . HIS B 1 46  ? 13.367  8.892   24.865  1.00 23.35 ? 58  HIS A O   1 
ATOM   2140 C CB  . HIS B 1 46  ? 11.147  7.517   26.713  1.00 20.36 ? 58  HIS A CB  1 
ATOM   2141 C CG  . HIS B 1 46  ? 9.698   7.270   27.025  1.00 21.39 ? 58  HIS A CG  1 
ATOM   2142 N ND1 . HIS B 1 46  ? 9.183   7.367   28.301  1.00 24.26 ? 58  HIS A ND1 1 
ATOM   2143 C CD2 . HIS B 1 46  ? 8.657   6.925   26.227  1.00 23.89 ? 58  HIS A CD2 1 
ATOM   2144 C CE1 . HIS B 1 46  ? 7.890   7.094   28.277  1.00 25.28 ? 58  HIS A CE1 1 
ATOM   2145 N NE2 . HIS B 1 46  ? 7.545   6.821   27.030  1.00 25.34 ? 58  HIS A NE2 1 
ATOM   2146 N N   . ILE B 1 47  ? 13.711  9.631   26.957  1.00 27.02 ? 59  ILE A N   1 
ATOM   2147 C CA  . ILE B 1 47  ? 15.132  9.898   26.761  1.00 25.95 ? 59  ILE A CA  1 
ATOM   2148 C C   . ILE B 1 47  ? 16.009  8.863   27.457  1.00 30.70 ? 59  ILE A C   1 
ATOM   2149 O O   . ILE B 1 47  ? 17.214  8.764   27.139  1.00 27.00 ? 59  ILE A O   1 
ATOM   2150 C CB  . ILE B 1 47  ? 15.493  11.323  27.235  1.00 27.27 ? 59  ILE A CB  1 
ATOM   2151 C CG1 . ILE B 1 47  ? 14.603  12.294  26.496  1.00 30.30 ? 59  ILE A CG1 1 
ATOM   2152 C CG2 . ILE B 1 47  ? 16.876  11.721  26.820  1.00 31.55 ? 59  ILE A CG2 1 
ATOM   2153 C CD1 . ILE B 1 47  ? 14.645  12.064  25.012  1.00 23.66 ? 59  ILE A CD1 1 
ATOM   2154 N N   . ALA B 1 48  ? 15.440  8.068   28.367  1.00 28.85 ? 60  ALA A N   1 
ATOM   2155 C CA  . ALA B 1 48  ? 16.177  7.093   29.151  1.00 26.86 ? 60  ALA A CA  1 
ATOM   2156 C C   . ALA B 1 48  ? 15.358  5.808   29.195  1.00 27.16 ? 60  ALA A C   1 
ATOM   2157 O O   . ALA B 1 48  ? 14.222  5.764   28.720  1.00 27.00 ? 60  ALA A O   1 
ATOM   2158 C CB  . ALA B 1 48  ? 16.478  7.655   30.545  1.00 28.96 ? 60  ALA A CB  1 
ATOM   2159 N N   . CYS B 1 49  ? 15.915  4.750   29.786  1.00 30.12 ? 61  CYS A N   1 
ATOM   2160 C CA  . CYS B 1 49  ? 15.214  3.459   29.817  1.00 28.85 ? 61  CYS A CA  1 
ATOM   2161 C C   . CYS B 1 49  ? 14.325  3.326   31.055  1.00 26.72 ? 61  CYS A C   1 
ATOM   2162 O O   . CYS B 1 49  ? 14.455  2.397   31.853  1.00 25.27 ? 61  CYS A O   1 
ATOM   2163 C CB  . CYS B 1 49  ? 16.196  2.295   29.728  1.00 25.67 ? 61  CYS A CB  1 
ATOM   2164 S SG  . CYS B 1 49  ? 15.590  1.004   28.595  1.00 46.43 ? 61  CYS A SG  1 
ATOM   2165 N N   . THR B 1 50  ? 13.374  4.253   31.175  1.00 26.90 ? 62  THR A N   1 
ATOM   2166 C CA  . THR B 1 50  ? 12.401  4.171   32.254  1.00 33.19 ? 62  THR A CA  1 
ATOM   2167 C C   . THR B 1 50  ? 11.486  2.970   32.003  1.00 32.46 ? 62  THR A C   1 
ATOM   2168 O O   . THR B 1 50  ? 11.393  2.482   30.878  1.00 32.16 ? 62  THR A O   1 
ATOM   2169 C CB  . THR B 1 50  ? 11.582  5.459   32.352  1.00 31.70 ? 62  THR A CB  1 
ATOM   2170 O OG1 . THR B 1 50  ? 10.368  5.312   31.616  1.00 36.80 ? 62  THR A OG1 1 
ATOM   2171 C CG2 . THR B 1 50  ? 12.367  6.621   31.739  1.00 34.13 ? 62  THR A CG2 1 
ATOM   2172 N N   . PRO B 1 51  ? 10.819  2.450   33.036  1.00 35.40 ? 63  PRO A N   1 
ATOM   2173 C CA  . PRO B 1 51  ? 9.932   1.300   32.794  1.00 30.12 ? 63  PRO A CA  1 
ATOM   2174 C C   . PRO B 1 51  ? 8.871   1.570   31.734  1.00 30.92 ? 63  PRO A C   1 
ATOM   2175 O O   . PRO B 1 51  ? 8.430   0.635   31.057  1.00 35.11 ? 63  PRO A O   1 
ATOM   2176 C CB  . PRO B 1 51  ? 9.329   1.035   34.179  1.00 23.50 ? 63  PRO A CB  1 
ATOM   2177 C CG  . PRO B 1 51  ? 9.579   2.304   34.954  1.00 29.85 ? 63  PRO A CG  1 
ATOM   2178 C CD  . PRO B 1 51  ? 10.892  2.784   34.468  1.00 31.23 ? 63  PRO A CD  1 
ATOM   2179 N N   . GLN B 1 52  ? 8.482   2.829   31.535  1.00 32.92 ? 64  GLN A N   1 
ATOM   2180 C CA  . GLN B 1 52  ? 7.465   3.142   30.533  1.00 34.36 ? 64  GLN A CA  1 
ATOM   2181 C C   . GLN B 1 52  ? 8.024   3.027   29.113  1.00 34.74 ? 64  GLN A C   1 
ATOM   2182 O O   . GLN B 1 52  ? 7.355   2.497   28.216  1.00 35.72 ? 64  GLN A O   1 
ATOM   2183 C CB  . GLN B 1 52  ? 6.905   4.546   30.787  1.00 35.44 ? 64  GLN A CB  1 
ATOM   2184 C CG  . GLN B 1 52  ? 5.778   4.597   31.821  1.00 39.28 ? 64  GLN A CG  1 
ATOM   2185 C CD  . GLN B 1 52  ? 4.529   3.837   31.395  1.00 53.66 ? 64  GLN A CD  1 
ATOM   2186 O OE1 . GLN B 1 52  ? 4.118   3.885   30.225  1.00 58.66 ? 64  GLN A OE1 1 
ATOM   2187 N NE2 . GLN B 1 52  ? 3.923   3.115   32.346  1.00 61.10 ? 64  GLN A NE2 1 
ATOM   2188 N N   . ALA B 1 53  ? 9.231   3.550   28.877  1.00 32.05 ? 65  ALA A N   1 
ATOM   2189 C CA  . ALA B 1 53  ? 9.901   3.323   27.601  1.00 24.02 ? 65  ALA A CA  1 
ATOM   2190 C C   . ALA B 1 53  ? 10.138  1.842   27.382  1.00 28.30 ? 65  ALA A C   1 
ATOM   2191 O O   . ALA B 1 53  ? 10.018  1.341   26.260  1.00 29.96 ? 65  ALA A O   1 
ATOM   2192 C CB  . ALA B 1 53  ? 11.226  4.077   27.557  1.00 20.57 ? 65  ALA A CB  1 
ATOM   2193 N N   . ALA B 1 54  ? 10.478  1.125   28.449  1.00 30.66 ? 66  ALA A N   1 
ATOM   2194 C CA  . ALA B 1 54  ? 10.729  -0.307  28.343  1.00 32.84 ? 66  ALA A CA  1 
ATOM   2195 C C   . ALA B 1 54  ? 9.474   -1.049  27.905  1.00 29.81 ? 66  ALA A C   1 
ATOM   2196 O O   . ALA B 1 54  ? 9.542   -1.941  27.054  1.00 28.83 ? 66  ALA A O   1 
ATOM   2197 C CB  . ALA B 1 54  ? 11.244  -0.842  29.682  1.00 28.62 ? 66  ALA A CB  1 
ATOM   2198 N N   . LYS B 1 55  ? 8.321   -0.688  28.471  1.00 30.79 ? 67  LYS A N   1 
ATOM   2199 C CA  . LYS B 1 55  ? 7.056   -1.250  28.011  1.00 32.99 ? 67  LYS A CA  1 
ATOM   2200 C C   . LYS B 1 55  ? 6.865   -1.014  26.519  1.00 32.97 ? 67  LYS A C   1 
ATOM   2201 O O   . LYS B 1 55  ? 6.690   -1.964  25.747  1.00 31.02 ? 67  LYS A O   1 
ATOM   2202 C CB  . LYS B 1 55  ? 5.892   -0.643  28.793  1.00 34.67 ? 67  LYS A CB  1 
ATOM   2203 C CG  . LYS B 1 55  ? 4.546   -1.227  28.406  1.00 38.95 ? 67  LYS A CG  1 
ATOM   2204 C CD  . LYS B 1 55  ? 3.550   -1.173  29.560  1.00 43.97 ? 67  LYS A CD  1 
ATOM   2205 C CE  . LYS B 1 55  ? 2.384   -2.138  29.345  1.00 50.94 ? 67  LYS A CE  1 
ATOM   2206 N NZ  . LYS B 1 55  ? 2.828   -3.476  28.839  1.00 49.01 ? 67  LYS A NZ  1 
ATOM   2207 N N   . ALA B 1 56  ? 6.943   0.255   26.099  1.00 33.27 ? 68  ALA A N   1 
ATOM   2208 C CA  . ALA B 1 56  ? 6.686   0.644   24.714  1.00 30.77 ? 68  ALA A CA  1 
ATOM   2209 C C   . ALA B 1 56  ? 7.451   -0.213  23.708  1.00 30.86 ? 68  ALA A C   1 
ATOM   2210 O O   . ALA B 1 56  ? 6.893   -0.618  22.676  1.00 33.66 ? 68  ALA A O   1 
ATOM   2211 C CB  . ALA B 1 56  ? 7.037   2.118   24.529  1.00 29.89 ? 68  ALA A CB  1 
ATOM   2212 N N   . ILE B 1 57  ? 8.733   -0.488  23.973  1.00 26.68 ? 69  ILE A N   1 
ATOM   2213 C CA  . ILE B 1 57  ? 9.497   -1.339  23.062  1.00 26.55 ? 69  ILE A CA  1 
ATOM   2214 C C   . ILE B 1 57  ? 9.054   -2.787  23.197  1.00 27.31 ? 69  ILE A C   1 
ATOM   2215 O O   . ILE B 1 57  ? 8.817   -3.478  22.204  1.00 27.61 ? 69  ILE A O   1 
ATOM   2216 C CB  . ILE B 1 57  ? 11.011  -1.198  23.305  1.00 23.22 ? 69  ILE A CB  1 
ATOM   2217 C CG1 . ILE B 1 57  ? 11.430  0.261   23.236  1.00 23.07 ? 69  ILE A CG1 1 
ATOM   2218 C CG2 . ILE B 1 57  ? 11.804  -2.080  22.339  1.00 23.71 ? 69  ILE A CG2 1 
ATOM   2219 C CD1 . ILE B 1 57  ? 12.656  0.552   24.028  1.00 23.55 ? 69  ILE A CD1 1 
ATOM   2220 N N   . SER B 1 58  ? 8.913   -3.260  24.426  1.00 27.53 ? 70  SER A N   1 
ATOM   2221 C CA  . SER B 1 58  ? 8.746   -4.686  24.640  1.00 28.81 ? 70  SER A CA  1 
ATOM   2222 C C   . SER B 1 58  ? 7.324   -5.130  24.366  1.00 28.79 ? 70  SER A C   1 
ATOM   2223 O O   . SER B 1 58  ? 7.107   -6.186  23.771  1.00 30.88 ? 70  SER A O   1 
ATOM   2224 C CB  . SER B 1 58  ? 9.132   -5.033  26.069  1.00 33.03 ? 70  SER A CB  1 
ATOM   2225 O OG  . SER B 1 58  ? 10.516  -4.845  26.271  1.00 32.25 ? 70  SER A OG  1 
ATOM   2226 N N   . ASN B 1 59  ? 6.348   -4.343  24.791  1.00 31.10 ? 71  ASN A N   1 
ATOM   2227 C CA  . ASN B 1 59  ? 4.950   -4.725  24.644  1.00 33.43 ? 71  ASN A CA  1 
ATOM   2228 C C   . ASN B 1 59  ? 4.534   -4.719  23.180  1.00 33.39 ? 71  ASN A C   1 
ATOM   2229 O O   . ASN B 1 59  ? 4.630   -3.691  22.497  1.00 33.12 ? 71  ASN A O   1 
ATOM   2230 C CB  . ASN B 1 59  ? 4.066   -3.789  25.446  1.00 33.07 ? 71  ASN A CB  1 
ATOM   2231 C CG  . ASN B 1 59  ? 2.621   -3.993  25.146  1.00 40.14 ? 71  ASN A CG  1 
ATOM   2232 O OD1 . ASN B 1 59  ? 2.210   -5.070  24.709  1.00 41.26 ? 71  ASN A OD1 1 
ATOM   2233 N ND2 . ASN B 1 59  ? 1.829   -2.951  25.349  1.00 47.83 ? 71  ASN A ND2 1 
ATOM   2234 N N   . LYS B 1 60  ? 4.041   -5.863  22.710  1.00 32.70 ? 72  LYS A N   1 
ATOM   2235 C CA  . LYS B 1 60  ? 3.675   -6.019  21.307  1.00 39.22 ? 72  LYS A CA  1 
ATOM   2236 C C   . LYS B 1 60  ? 2.293   -5.481  20.999  1.00 37.91 ? 72  LYS A C   1 
ATOM   2237 O O   . LYS B 1 60  ? 1.810   -5.657  19.878  1.00 39.92 ? 72  LYS A O   1 
ATOM   2238 C CB  . LYS B 1 60  ? 3.777   -7.489  20.889  1.00 37.79 ? 72  LYS A CB  1 
ATOM   2239 C CG  . LYS B 1 60  ? 5.217   -7.993  20.864  1.00 39.65 ? 72  LYS A CG  1 
ATOM   2240 C CD  . LYS B 1 60  ? 5.504   -8.938  19.706  1.00 42.39 ? 72  LYS A CD  1 
ATOM   2241 C CE  . LYS B 1 60  ? 6.950   -9.429  19.786  1.00 42.77 ? 72  LYS A CE  1 
ATOM   2242 N NZ  . LYS B 1 60  ? 7.100   -10.667 20.611  1.00 45.18 ? 72  LYS A NZ  1 
ATOM   2243 N N   . ASP B 1 61  ? 1.653   -4.841  21.972  1.00 37.66 ? 73  ASP A N   1 
ATOM   2244 C CA  . ASP B 1 61  ? 0.408   -4.124  21.758  1.00 41.63 ? 73  ASP A CA  1 
ATOM   2245 C C   . ASP B 1 61  ? 0.632   -2.627  21.656  1.00 37.02 ? 73  ASP A C   1 
ATOM   2246 O O   . ASP B 1 61  ? -0.327  -1.870  21.510  1.00 36.26 ? 73  ASP A O   1 
ATOM   2247 C CB  . ASP B 1 61  ? -0.576  -4.429  22.891  1.00 42.79 ? 73  ASP A CB  1 
ATOM   2248 C CG  . ASP B 1 61  ? -1.610  -5.472  22.502  1.00 52.19 ? 73  ASP A CG  1 
ATOM   2249 O OD1 . ASP B 1 61  ? -2.248  -6.038  23.420  1.00 52.48 ? 73  ASP A OD1 1 
ATOM   2250 O OD2 . ASP B 1 61  ? -1.770  -5.733  21.284  1.00 54.35 ? 73  ASP A OD2 1 
ATOM   2251 N N   . GLN B 1 62  ? 1.874   -2.195  21.745  1.00 35.14 ? 74  GLN A N   1 
ATOM   2252 C CA  . GLN B 1 62  ? 2.240   -0.797  21.709  1.00 32.07 ? 74  GLN A CA  1 
ATOM   2253 C C   . GLN B 1 62  ? 3.141   -0.553  20.506  1.00 34.39 ? 74  GLN A C   1 
ATOM   2254 O O   . GLN B 1 62  ? 3.918   -1.428  20.106  1.00 34.72 ? 74  GLN A O   1 
ATOM   2255 C CB  . GLN B 1 62  ? 2.962   -0.431  23.002  1.00 28.62 ? 74  GLN A CB  1 
ATOM   2256 C CG  . GLN B 1 62  ? 2.482   0.802   23.693  1.00 33.87 ? 74  GLN A CG  1 
ATOM   2257 C CD  . GLN B 1 62  ? 2.808   0.746   25.171  1.00 41.76 ? 74  GLN A CD  1 
ATOM   2258 O OE1 . GLN B 1 62  ? 2.340   -0.145  25.887  1.00 42.58 ? 74  GLN A OE1 1 
ATOM   2259 N NE2 . GLN B 1 62  ? 3.654   1.663   25.630  1.00 44.33 ? 74  GLN A NE2 1 
ATOM   2260 N N   . HIS B 1 63  ? 3.049   0.638   19.931  1.00 32.51 ? 75  HIS A N   1 
ATOM   2261 C CA  . HIS B 1 63  ? 3.938   1.025   18.846  1.00 27.83 ? 75  HIS A CA  1 
ATOM   2262 C C   . HIS B 1 63  ? 5.070   1.879   19.387  1.00 24.39 ? 75  HIS A C   1 
ATOM   2263 O O   . HIS B 1 63  ? 4.861   2.711   20.272  1.00 24.68 ? 75  HIS A O   1 
ATOM   2264 C CB  . HIS B 1 63  ? 3.185   1.784   17.760  1.00 26.35 ? 75  HIS A CB  1 
ATOM   2265 C CG  . HIS B 1 63  ? 2.335   0.902   16.911  1.00 25.32 ? 75  HIS A CG  1 
ATOM   2266 N ND1 . HIS B 1 63  ? 1.057   0.537   17.274  1.00 28.47 ? 75  HIS A ND1 1 
ATOM   2267 C CD2 . HIS B 1 63  ? 2.582   0.293   15.729  1.00 23.91 ? 75  HIS A CD2 1 
ATOM   2268 C CE1 . HIS B 1 63  ? 0.550   -0.253  16.345  1.00 30.08 ? 75  HIS A CE1 1 
ATOM   2269 N NE2 . HIS B 1 63  ? 1.455   -0.416  15.397  1.00 25.57 ? 75  HIS A NE2 1 
ATOM   2270 N N   . SER B 1 64  ? 6.271   1.668   18.854  1.00 23.69 ? 76  SER A N   1 
ATOM   2271 C CA  . SER B 1 64  ? 7.415   2.479   19.239  1.00 26.89 ? 76  SER A CA  1 
ATOM   2272 C C   . SER B 1 64  ? 8.295   2.734   18.020  1.00 24.64 ? 76  SER A C   1 
ATOM   2273 O O   . SER B 1 64  ? 8.359   1.927   17.090  1.00 20.22 ? 76  SER A O   1 
ATOM   2274 C CB  . SER B 1 64  ? 8.231   1.823   20.402  1.00 23.82 ? 76  SER A CB  1 
ATOM   2275 O OG  . SER B 1 64  ? 9.462   1.226   19.983  1.00 23.89 ? 76  SER A OG  1 
ATOM   2276 N N   . ILE B 1 65  ? 8.936   3.898   18.020  1.00 23.05 ? 77  ILE A N   1 
ATOM   2277 C CA  . ILE B 1 65  ? 10.049  4.201   17.131  1.00 19.38 ? 77  ILE A CA  1 
ATOM   2278 C C   . ILE B 1 65  ? 11.220  4.585   18.015  1.00 19.67 ? 77  ILE A C   1 
ATOM   2279 O O   . ILE B 1 65  ? 11.052  5.353   18.967  1.00 22.78 ? 77  ILE A O   1 
ATOM   2280 C CB  . ILE B 1 65  ? 9.710   5.335   16.151  1.00 20.28 ? 77  ILE A CB  1 
ATOM   2281 C CG1 . ILE B 1 65  ? 8.432   5.016   15.373  1.00 21.74 ? 77  ILE A CG1 1 
ATOM   2282 C CG2 . ILE B 1 65  ? 10.846  5.549   15.205  1.00 19.73 ? 77  ILE A CG2 1 
ATOM   2283 C CD1 . ILE B 1 65  ? 8.237   5.896   14.154  1.00 21.53 ? 77  ILE A CD1 1 
ATOM   2284 N N   . SER B 1 66  ? 12.393  4.040   17.726  1.00 20.09 ? 78  SER A N   1 
ATOM   2285 C CA  . SER B 1 66  ? 13.521  4.115   18.648  1.00 21.35 ? 78  SER A CA  1 
ATOM   2286 C C   . SER B 1 66  ? 14.730  4.642   17.891  1.00 21.85 ? 78  SER A C   1 
ATOM   2287 O O   . SER B 1 66  ? 15.264  3.961   17.011  1.00 24.47 ? 78  SER A O   1 
ATOM   2288 C CB  . SER B 1 66  ? 13.794  2.748   19.278  1.00 23.79 ? 78  SER A CB  1 
ATOM   2289 O OG  . SER B 1 66  ? 12.718  1.844   18.999  1.00 26.16 ? 78  SER A OG  1 
ATOM   2290 N N   . TYR B 1 67  ? 15.146  5.855   18.230  1.00 24.24 ? 79  TYR A N   1 
ATOM   2291 C CA  . TYR B 1 67  ? 16.230  6.557   17.557  1.00 20.24 ? 79  TYR A CA  1 
ATOM   2292 C C   . TYR B 1 67  ? 17.511  6.356   18.347  1.00 23.91 ? 79  TYR A C   1 
ATOM   2293 O O   . TYR B 1 67  ? 17.602  6.794   19.498  1.00 22.16 ? 79  TYR A O   1 
ATOM   2294 C CB  . TYR B 1 67  ? 15.944  8.054   17.460  1.00 21.93 ? 79  TYR A CB  1 
ATOM   2295 C CG  . TYR B 1 67  ? 14.715  8.436   16.673  1.00 21.57 ? 79  TYR A CG  1 
ATOM   2296 C CD1 . TYR B 1 67  ? 13.441  8.352   17.234  1.00 23.02 ? 79  TYR A CD1 1 
ATOM   2297 C CD2 . TYR B 1 67  ? 14.829  8.903   15.376  1.00 19.66 ? 79  TYR A CD2 1 
ATOM   2298 C CE1 . TYR B 1 67  ? 12.313  8.709   16.510  1.00 25.23 ? 79  TYR A CE1 1 
ATOM   2299 C CE2 . TYR B 1 67  ? 13.713  9.262   14.645  1.00 21.53 ? 79  TYR A CE2 1 
ATOM   2300 C CZ  . TYR B 1 67  ? 12.459  9.164   15.210  1.00 24.39 ? 79  TYR A CZ  1 
ATOM   2301 O OH  . TYR B 1 67  ? 11.363  9.534   14.469  1.00 23.18 ? 79  TYR A OH  1 
ATOM   2302 N N   . THR B 1 68  ? 18.510  5.752   17.710  1.00 27.09 ? 80  THR A N   1 
ATOM   2303 C CA  . THR B 1 68  ? 19.807  5.478   18.329  1.00 25.61 ? 80  THR A CA  1 
ATOM   2304 C C   . THR B 1 68  ? 20.776  6.641   18.070  1.00 23.11 ? 80  THR A C   1 
ATOM   2305 O O   . THR B 1 68  ? 21.263  6.812   16.951  1.00 23.44 ? 80  THR A O   1 
ATOM   2306 C CB  . THR B 1 68  ? 20.341  4.157   17.784  1.00 21.82 ? 80  THR A CB  1 
ATOM   2307 O OG1 . THR B 1 68  ? 19.369  3.135   18.023  1.00 20.57 ? 80  THR A OG1 1 
ATOM   2308 C CG2 . THR B 1 68  ? 21.660  3.788   18.425  1.00 23.00 ? 80  THR A CG2 1 
ATOM   2309 N N   . LEU B 1 69  ? 21.073  7.428   19.111  1.00 24.63 ? 81  LEU A N   1 
ATOM   2310 C CA  . LEU B 1 69  ? 21.903  8.630   18.998  1.00 23.16 ? 81  LEU A CA  1 
ATOM   2311 C C   . LEU B 1 69  ? 23.376  8.355   19.268  1.00 26.73 ? 81  LEU A C   1 
ATOM   2312 O O   . LEU B 1 69  ? 24.247  8.950   18.625  1.00 25.98 ? 81  LEU A O   1 
ATOM   2313 C CB  . LEU B 1 69  ? 21.416  9.699   19.974  1.00 21.63 ? 81  LEU A CB  1 
ATOM   2314 C CG  . LEU B 1 69  ? 20.257  10.607  19.587  1.00 23.10 ? 81  LEU A CG  1 
ATOM   2315 C CD1 . LEU B 1 69  ? 19.078  9.823   19.052  1.00 24.63 ? 81  LEU A CD1 1 
ATOM   2316 C CD2 . LEU B 1 69  ? 19.836  11.355  20.829  1.00 30.56 ? 81  LEU A CD2 1 
ATOM   2317 N N   . SER B 1 70  ? 23.664  7.473   20.219  1.00 29.78 ? 82  SER A N   1 
ATOM   2318 C CA  . SER B 1 70  ? 25.019  7.063   20.561  1.00 27.99 ? 82  SER A CA  1 
ATOM   2319 C C   . SER B 1 70  ? 24.898  5.792   21.389  1.00 29.68 ? 82  SER A C   1 
ATOM   2320 O O   . SER B 1 70  ? 23.793  5.370   21.742  1.00 34.07 ? 82  SER A O   1 
ATOM   2321 C CB  . SER B 1 70  ? 25.757  8.169   21.319  1.00 30.35 ? 82  SER A CB  1 
ATOM   2322 O OG  . SER B 1 70  ? 25.026  8.577   22.466  1.00 33.18 ? 82  SER A OG  1 
ATOM   2323 N N   . ARG B 1 71  ? 26.044  5.185   21.710  1.00 30.72 ? 83  ARG A N   1 
ATOM   2324 C CA  . ARG B 1 71  ? 26.037  3.977   22.537  1.00 33.40 ? 83  ARG A CA  1 
ATOM   2325 C C   . ARG B 1 71  ? 25.278  4.190   23.845  1.00 32.27 ? 83  ARG A C   1 
ATOM   2326 O O   . ARG B 1 71  ? 24.656  3.253   24.367  1.00 29.96 ? 83  ARG A O   1 
ATOM   2327 C CB  . ARG B 1 71  ? 27.477  3.536   22.824  1.00 38.90 ? 83  ARG A CB  1 
ATOM   2328 C CG  . ARG B 1 71  ? 27.894  2.229   22.150  1.00 43.07 ? 83  ARG A CG  1 
ATOM   2329 C CD  . ARG B 1 71  ? 29.373  1.910   22.403  1.00 57.47 ? 83  ARG A CD  1 
ATOM   2330 N NE  . ARG B 1 71  ? 30.029  1.355   21.220  1.00 66.14 ? 83  ARG A NE  1 
ATOM   2331 C CZ  . ARG B 1 71  ? 30.967  1.973   20.510  1.00 59.43 ? 83  ARG A CZ  1 
ATOM   2332 N NH1 . ARG B 1 71  ? 31.408  3.180   20.841  1.00 51.06 ? 83  ARG A NH1 1 
ATOM   2333 N NH2 . ARG B 1 71  ? 31.481  1.361   19.443  1.00 53.20 ? 83  ARG A NH2 1 
ATOM   2334 N N   . ALA B 1 72  ? 25.316  5.414   24.375  1.00 31.67 ? 84  ALA A N   1 
ATOM   2335 C CA  . ALA B 1 72  ? 24.694  5.778   25.639  1.00 29.76 ? 84  ALA A CA  1 
ATOM   2336 C C   . ALA B 1 72  ? 23.234  6.196   25.498  1.00 30.60 ? 84  ALA A C   1 
ATOM   2337 O O   . ALA B 1 72  ? 22.446  5.989   26.433  1.00 30.23 ? 84  ALA A O   1 
ATOM   2338 C CB  . ALA B 1 72  ? 25.479  6.928   26.287  1.00 24.40 ? 84  ALA A CB  1 
ATOM   2339 N N   . GLN B 1 73  ? 22.846  6.758   24.356  1.00 28.29 ? 85  GLN A N   1 
ATOM   2340 C CA  . GLN B 1 73  ? 21.573  7.454   24.230  1.00 29.03 ? 85  GLN A CA  1 
ATOM   2341 C C   . GLN B 1 73  ? 20.685  6.791   23.186  1.00 29.85 ? 85  GLN A C   1 
ATOM   2342 O O   . GLN B 1 73  ? 21.099  6.605   22.033  1.00 25.42 ? 85  GLN A O   1 
ATOM   2343 C CB  . GLN B 1 73  ? 21.807  8.918   23.878  1.00 27.93 ? 85  GLN A CB  1 
ATOM   2344 C CG  . GLN B 1 73  ? 22.629  9.633   24.915  1.00 26.40 ? 85  GLN A CG  1 
ATOM   2345 C CD  . GLN B 1 73  ? 22.463  11.107  24.812  1.00 26.92 ? 85  GLN A CD  1 
ATOM   2346 O OE1 . GLN B 1 73  ? 21.345  11.603  24.915  1.00 29.80 ? 85  GLN A OE1 1 
ATOM   2347 N NE2 . GLN B 1 73  ? 23.569  11.834  24.625  1.00 29.99 ? 85  GLN A NE2 1 
ATOM   2348 N N   . THR B 1 74  ? 19.461  6.454   23.594  1.00 30.63 ? 86  THR A N   1 
ATOM   2349 C CA  . THR B 1 74  ? 18.389  6.060   22.687  1.00 27.37 ? 86  THR A CA  1 
ATOM   2350 C C   . THR B 1 74  ? 17.137  6.832   23.070  1.00 23.43 ? 86  THR A C   1 
ATOM   2351 O O   . THR B 1 74  ? 16.750  6.868   24.243  1.00 26.89 ? 86  THR A O   1 
ATOM   2352 C CB  . THR B 1 74  ? 18.107  4.551   22.724  1.00 27.55 ? 86  THR A CB  1 
ATOM   2353 O OG1 . THR B 1 74  ? 19.166  3.850   22.058  1.00 32.63 ? 86  THR A OG1 1 
ATOM   2354 C CG2 . THR B 1 74  ? 16.766  4.228   22.047  1.00 19.24 ? 86  THR A CG2 1 
ATOM   2355 N N   . VAL B 1 75  ? 16.535  7.477   22.087  1.00 22.59 ? 87  VAL A N   1 
ATOM   2356 C CA  . VAL B 1 75  ? 15.244  8.116   22.235  1.00 20.16 ? 87  VAL A CA  1 
ATOM   2357 C C   . VAL B 1 75  ? 14.206  7.103   21.790  1.00 20.97 ? 87  VAL A C   1 
ATOM   2358 O O   . VAL B 1 75  ? 14.330  6.508   20.714  1.00 21.80 ? 87  VAL A O   1 
ATOM   2359 C CB  . VAL B 1 75  ? 15.166  9.402   21.399  1.00 20.28 ? 87  VAL A CB  1 
ATOM   2360 C CG1 . VAL B 1 75  ? 13.777  10.046  21.515  1.00 21.16 ? 87  VAL A CG1 1 
ATOM   2361 C CG2 . VAL B 1 75  ? 16.276  10.353  21.815  1.00 20.57 ? 87  VAL A CG2 1 
ATOM   2362 N N   . VAL B 1 76  ? 13.213  6.862   22.632  1.00 22.05 ? 88  VAL A N   1 
ATOM   2363 C CA  . VAL B 1 76  ? 12.110  5.970   22.311  1.00 21.45 ? 88  VAL A CA  1 
ATOM   2364 C C   . VAL B 1 76  ? 10.863  6.831   22.293  1.00 23.75 ? 88  VAL A C   1 
ATOM   2365 O O   . VAL B 1 76  ? 10.589  7.560   23.258  1.00 21.41 ? 88  VAL A O   1 
ATOM   2366 C CB  . VAL B 1 76  ? 11.990  4.808   23.314  1.00 19.05 ? 88  VAL A CB  1 
ATOM   2367 C CG1 . VAL B 1 76  ? 10.801  3.937   22.990  1.00 17.62 ? 88  VAL A CG1 1 
ATOM   2368 C CG2 . VAL B 1 76  ? 13.252  3.979   23.292  1.00 21.76 ? 88  VAL A CG2 1 
ATOM   2369 N N   . VAL B 1 77  ? 10.141  6.786   21.180  1.00 23.88 ? 89  VAL A N   1 
ATOM   2370 C CA  . VAL B 1 77  ? 8.955   7.605   20.977  1.00 26.09 ? 89  VAL A CA  1 
ATOM   2371 C C   . VAL B 1 77  ? 7.759   6.679   20.806  1.00 23.80 ? 89  VAL A C   1 
ATOM   2372 O O   . VAL B 1 77  ? 7.786   5.764   19.971  1.00 22.50 ? 89  VAL A O   1 
ATOM   2373 C CB  . VAL B 1 77  ? 9.114   8.540   19.763  1.00 28.60 ? 89  VAL A CB  1 
ATOM   2374 C CG1 . VAL B 1 77  ? 7.850   9.369   19.577  1.00 26.07 ? 89  VAL A CG1 1 
ATOM   2375 C CG2 . VAL B 1 77  ? 10.351  9.439   19.927  1.00 23.61 ? 89  VAL A CG2 1 
ATOM   2376 N N   . GLU B 1 78  ? 6.726   6.911   21.606  1.00 23.07 ? 90  GLU A N   1 
ATOM   2377 C CA  . GLU B 1 78  ? 5.541   6.072   21.587  1.00 25.05 ? 90  GLU A CA  1 
ATOM   2378 C C   . GLU B 1 78  ? 4.617   6.519   20.470  1.00 24.06 ? 90  GLU A C   1 
ATOM   2379 O O   . GLU B 1 78  ? 4.510   7.712   20.181  1.00 25.41 ? 90  GLU A O   1 
ATOM   2380 C CB  . GLU B 1 78  ? 4.815   6.165   22.925  1.00 26.61 ? 90  GLU A CB  1 
ATOM   2381 C CG  . GLU B 1 78  ? 5.379   5.290   24.002  1.00 34.79 ? 90  GLU A CG  1 
ATOM   2382 C CD  . GLU B 1 78  ? 4.602   5.394   25.303  1.00 38.22 ? 90  GLU A CD  1 
ATOM   2383 O OE1 . GLU B 1 78  ? 3.549   4.723   25.431  1.00 41.88 ? 90  GLU A OE1 1 
ATOM   2384 O OE2 . GLU B 1 78  ? 5.054   6.151   26.195  1.00 36.19 ? 90  GLU A OE2 1 
ATOM   2385 N N   . TYR B 1 79  ? 3.946   5.562   19.837  1.00 20.40 ? 91  TYR A N   1 
ATOM   2386 C CA  . TYR B 1 79  ? 2.913   5.876   18.861  1.00 22.22 ? 91  TYR A CA  1 
ATOM   2387 C C   . TYR B 1 79  ? 1.604   5.293   19.352  1.00 21.61 ? 91  TYR A C   1 
ATOM   2388 O O   . TYR B 1 79  ? 1.434   4.072   19.388  1.00 25.94 ? 91  TYR A O   1 
ATOM   2389 C CB  . TYR B 1 79  ? 3.271   5.356   17.476  1.00 24.40 ? 91  TYR A CB  1 
ATOM   2390 C CG  . TYR B 1 79  ? 4.168   6.324   16.745  1.00 24.40 ? 91  TYR A CG  1 
ATOM   2391 C CD1 . TYR B 1 79  ? 5.501   6.468   17.106  1.00 22.68 ? 91  TYR A CD1 1 
ATOM   2392 C CD2 . TYR B 1 79  ? 3.672   7.137   15.734  1.00 21.85 ? 91  TYR A CD2 1 
ATOM   2393 C CE1 . TYR B 1 79  ? 6.321   7.355   16.463  1.00 22.02 ? 91  TYR A CE1 1 
ATOM   2394 C CE2 . TYR B 1 79  ? 4.494   8.030   15.081  1.00 21.46 ? 91  TYR A CE2 1 
ATOM   2395 C CZ  . TYR B 1 79  ? 5.821   8.132   15.444  1.00 22.48 ? 91  TYR A CZ  1 
ATOM   2396 O OH  . TYR B 1 79  ? 6.650   9.021   14.795  1.00 17.08 ? 91  TYR A OH  1 
ATOM   2397 N N   . THR B 1 80  ? 0.689   6.166   19.722  1.00 22.56 ? 92  THR A N   1 
ATOM   2398 C CA  . THR B 1 80  ? -0.571  5.739   20.295  1.00 26.94 ? 92  THR A CA  1 
ATOM   2399 C C   . THR B 1 80  ? -1.654  5.654   19.232  1.00 27.37 ? 92  THR A C   1 
ATOM   2400 O O   . THR B 1 80  ? -1.562  6.253   18.160  1.00 30.17 ? 92  THR A O   1 
ATOM   2401 C CB  . THR B 1 80  ? -1.024  6.684   21.396  1.00 26.01 ? 92  THR A CB  1 
ATOM   2402 O OG1 . THR B 1 80  ? -2.265  6.197   21.909  1.00 36.19 ? 92  THR A OG1 1 
ATOM   2403 C CG2 . THR B 1 80  ? -1.227  8.078   20.844  1.00 26.18 ? 92  THR A CG2 1 
ATOM   2404 N N   . HIS B 1 81  ? -2.706  4.918   19.571  1.00 28.07 ? 93  HIS A N   1 
ATOM   2405 C CA  . HIS B 1 81  ? -3.764  4.613   18.628  1.00 25.86 ? 93  HIS A CA  1 
ATOM   2406 C C   . HIS B 1 81  ? -4.424  5.892   18.133  1.00 28.90 ? 93  HIS A C   1 
ATOM   2407 O O   . HIS B 1 81  ? -4.672  6.822   18.905  1.00 31.61 ? 93  HIS A O   1 
ATOM   2408 C CB  . HIS B 1 81  ? -4.791  3.716   19.298  1.00 24.35 ? 93  HIS A CB  1 
ATOM   2409 C CG  . HIS B 1 81  ? -5.991  3.452   18.459  1.00 26.14 ? 93  HIS A CG  1 
ATOM   2410 N ND1 . HIS B 1 81  ? -7.187  4.112   18.642  1.00 28.49 ? 93  HIS A ND1 1 
ATOM   2411 C CD2 . HIS B 1 81  ? -6.179  2.606   17.419  1.00 26.25 ? 93  HIS A CD2 1 
ATOM   2412 C CE1 . HIS B 1 81  ? -8.068  3.674   17.759  1.00 29.77 ? 93  HIS A CE1 1 
ATOM   2413 N NE2 . HIS B 1 81  ? -7.480  2.761   17.003  1.00 29.72 ? 93  HIS A NE2 1 
ATOM   2414 N N   . ASP B 1 82  ? -4.691  5.943   16.832  1.00 23.87 ? 94  ASP A N   1 
ATOM   2415 C CA  . ASP B 1 82  ? -5.419  7.043   16.214  1.00 27.74 ? 94  ASP A CA  1 
ATOM   2416 C C   . ASP B 1 82  ? -6.699  6.504   15.588  1.00 31.20 ? 94  ASP A C   1 
ATOM   2417 O O   . ASP B 1 82  ? -6.645  5.722   14.632  1.00 34.35 ? 94  ASP A O   1 
ATOM   2418 C CB  . ASP B 1 82  ? -4.563  7.738   15.156  1.00 29.86 ? 94  ASP A CB  1 
ATOM   2419 C CG  . ASP B 1 82  ? -5.195  9.021   14.632  1.00 31.09 ? 94  ASP A CG  1 
ATOM   2420 O OD1 . ASP B 1 82  ? -6.369  9.311   14.966  1.00 32.16 ? 94  ASP A OD1 1 
ATOM   2421 O OD2 . ASP B 1 82  ? -4.509  9.734   13.864  1.00 30.14 ? 94  ASP A OD2 1 
ATOM   2422 N N   . SER B 1 83  ? -7.845  6.933   16.113  1.00 29.17 ? 95  SER A N   1 
ATOM   2423 C CA  . SER B 1 83  ? -9.125  6.445   15.629  1.00 28.44 ? 95  SER A CA  1 
ATOM   2424 C C   . SER B 1 83  ? -9.543  7.080   14.310  1.00 35.50 ? 95  SER A C   1 
ATOM   2425 O O   . SER B 1 83  ? -10.471 6.570   13.668  1.00 35.50 ? 95  SER A O   1 
ATOM   2426 C CB  . SER B 1 83  ? -10.207 6.686   16.681  1.00 34.91 ? 95  SER A CB  1 
ATOM   2427 O OG  . SER B 1 83  ? -10.366 8.072   16.956  1.00 37.72 ? 95  SER A OG  1 
ATOM   2428 N N   . ASN B 1 84  ? -8.883  8.166   13.883  1.00 35.46 ? 96  ASN A N   1 
ATOM   2429 C CA  . ASN B 1 84  ? -9.246  8.858   12.647  1.00 35.30 ? 96  ASN A CA  1 
ATOM   2430 C C   . ASN B 1 84  ? -8.637  8.258   11.386  1.00 30.77 ? 96  ASN A C   1 
ATOM   2431 O O   . ASN B 1 84  ? -9.039  8.660   10.287  1.00 32.21 ? 96  ASN A O   1 
ATOM   2432 C CB  . ASN B 1 84  ? -8.832  10.333  12.688  1.00 34.92 ? 96  ASN A CB  1 
ATOM   2433 C CG  . ASN B 1 84  ? -9.581  11.126  13.718  1.00 36.76 ? 96  ASN A CG  1 
ATOM   2434 O OD1 . ASN B 1 84  ? -10.743 10.847  14.012  1.00 40.72 ? 96  ASN A OD1 1 
ATOM   2435 N ND2 . ASN B 1 84  ? -8.935  12.164  14.239  1.00 37.14 ? 96  ASN A ND2 1 
ATOM   2436 N N   . THR B 1 85  ? -7.667  7.350   11.498  1.00 25.23 ? 97  THR A N   1 
ATOM   2437 C CA  . THR B 1 85  ? -6.839  7.001   10.353  1.00 26.57 ? 97  THR A CA  1 
ATOM   2438 C C   . THR B 1 85  ? -6.615  5.501   10.282  1.00 23.89 ? 97  THR A C   1 
ATOM   2439 O O   . THR B 1 85  ? -6.571  4.814   11.302  1.00 26.64 ? 97  THR A O   1 
ATOM   2440 C CB  . THR B 1 85  ? -5.463  7.702   10.399  1.00 24.54 ? 97  THR A CB  1 
ATOM   2441 O OG1 . THR B 1 85  ? -4.760  7.278   11.566  1.00 24.67 ? 97  THR A OG1 1 
ATOM   2442 C CG2 . THR B 1 85  ? -5.583  9.222   10.424  1.00 22.00 ? 97  THR A CG2 1 
ATOM   2443 N N   . ASP B 1 86  ? -6.437  5.007   9.062   1.00 24.61 ? 98  ASP A N   1 
ATOM   2444 C CA  . ASP B 1 86  ? -6.021  3.635   8.806   1.00 28.33 ? 98  ASP A CA  1 
ATOM   2445 C C   . ASP B 1 86  ? -4.570  3.594   8.343   1.00 24.21 ? 98  ASP A C   1 
ATOM   2446 O O   . ASP B 1 86  ? -4.107  4.489   7.632   1.00 27.00 ? 98  ASP A O   1 
ATOM   2447 C CB  . ASP B 1 86  ? -6.909  2.980   7.748   1.00 28.51 ? 98  ASP A CB  1 
ATOM   2448 C CG  . ASP B 1 86  ? -8.249  2.591   8.299   1.00 32.16 ? 98  ASP A CG  1 
ATOM   2449 O OD1 . ASP B 1 86  ? -8.378  2.554   9.545   1.00 30.17 ? 98  ASP A OD1 1 
ATOM   2450 O OD2 . ASP B 1 86  ? -9.161  2.308   7.500   1.00 34.87 ? 98  ASP A OD2 1 
ATOM   2451 N N   . MET B 1 87  ? -3.849  2.547   8.725   1.00 21.43 ? 99  MET A N   1 
ATOM   2452 C CA  . MET B 1 87  ? -2.432  2.462   8.403   1.00 26.28 ? 99  MET A CA  1 
ATOM   2453 C C   . MET B 1 87  ? -2.167  1.234   7.548   1.00 23.76 ? 99  MET A C   1 
ATOM   2454 O O   . MET B 1 87  ? -2.616  0.135   7.883   1.00 25.17 ? 99  MET A O   1 
ATOM   2455 C CB  . MET B 1 87  ? -1.577  2.452   9.681   1.00 26.03 ? 99  MET A CB  1 
ATOM   2456 C CG  . MET B 1 87  ? -0.099  2.595   9.395   1.00 24.83 ? 99  MET A CG  1 
ATOM   2457 S SD  . MET B 1 87  ? 0.907   2.692   10.879  1.00 34.00 ? 99  MET A SD  1 
ATOM   2458 C CE  . MET B 1 87  ? 0.144   1.480   11.967  1.00 26.80 ? 99  MET A CE  1 
ATOM   2459 N N   . PHE B 1 88  ? -1.471  1.436   6.429   1.00 22.51 ? 100 PHE A N   1 
ATOM   2460 C CA  . PHE B 1 88  ? -1.061  0.363   5.534   1.00 26.06 ? 100 PHE A CA  1 
ATOM   2461 C C   . PHE B 1 88  ? 0.443   0.443   5.354   1.00 22.84 ? 100 PHE A C   1 
ATOM   2462 O O   . PHE B 1 88  ? 0.995   1.539   5.267   1.00 22.09 ? 100 PHE A O   1 
ATOM   2463 C CB  . PHE B 1 88  ? -1.767  0.460   4.168   1.00 27.41 ? 100 PHE A CB  1 
ATOM   2464 C CG  . PHE B 1 88  ? -3.243  0.588   4.277   1.00 26.95 ? 100 PHE A CG  1 
ATOM   2465 C CD1 . PHE B 1 88  ? -3.823  1.814   4.546   1.00 27.17 ? 100 PHE A CD1 1 
ATOM   2466 C CD2 . PHE B 1 88  ? -4.057  -0.516  4.128   1.00 28.76 ? 100 PHE A CD2 1 
ATOM   2467 C CE1 . PHE B 1 88  ? -5.199  1.942   4.664   1.00 27.28 ? 100 PHE A CE1 1 
ATOM   2468 C CE2 . PHE B 1 88  ? -5.438  -0.400  4.244   1.00 30.10 ? 100 PHE A CE2 1 
ATOM   2469 C CZ  . PHE B 1 88  ? -6.006  0.831   4.513   1.00 28.60 ? 100 PHE A CZ  1 
ATOM   2470 N N   . GLN B 1 89  ? 1.104   -0.709  5.303   1.00 24.26 ? 101 GLN A N   1 
ATOM   2471 C CA  . GLN B 1 89  ? 2.555   -0.762  5.186   1.00 25.57 ? 101 GLN A CA  1 
ATOM   2472 C C   . GLN B 1 89  ? 2.988   -1.560  3.954   1.00 23.54 ? 101 GLN A C   1 
ATOM   2473 O O   . GLN B 1 89  ? 2.302   -2.478  3.506   1.00 23.51 ? 101 GLN A O   1 
ATOM   2474 C CB  . GLN B 1 89  ? 3.169   -1.348  6.462   1.00 23.69 ? 101 GLN A CB  1 
ATOM   2475 C CG  . GLN B 1 89  ? 2.794   -0.545  7.714   1.00 23.35 ? 101 GLN A CG  1 
ATOM   2476 C CD  . GLN B 1 89  ? 3.648   -0.879  8.932   1.00 24.80 ? 101 GLN A CD  1 
ATOM   2477 O OE1 . GLN B 1 89  ? 3.981   0.003   9.706   1.00 26.90 ? 101 GLN A OE1 1 
ATOM   2478 N NE2 . GLN B 1 89  ? 3.991   -2.154  9.110   1.00 24.59 ? 101 GLN A NE2 1 
ATOM   2479 N N   . ILE B 1 90  ? 4.139   -1.202  3.405   1.00 23.02 ? 102 ILE A N   1 
ATOM   2480 C CA  . ILE B 1 90  ? 4.668   -1.833  2.204   1.00 26.20 ? 102 ILE A CA  1 
ATOM   2481 C C   . ILE B 1 90  ? 6.101   -2.280  2.478   1.00 27.75 ? 102 ILE A C   1 
ATOM   2482 O O   . ILE B 1 90  ? 6.867   -1.561  3.129   1.00 26.83 ? 102 ILE A O   1 
ATOM   2483 C CB  . ILE B 1 90  ? 4.606   -0.860  1.005   1.00 25.04 ? 102 ILE A CB  1 
ATOM   2484 C CG1 . ILE B 1 90  ? 3.151   -0.569  0.647   1.00 26.47 ? 102 ILE A CG1 1 
ATOM   2485 C CG2 . ILE B 1 90  ? 5.342   -1.423  -0.207  1.00 21.01 ? 102 ILE A CG2 1 
ATOM   2486 C CD1 . ILE B 1 90  ? 2.703   0.816   1.003   1.00 25.86 ? 102 ILE A CD1 1 
ATOM   2487 N N   . GLY B 1 91  ? 6.475   -3.457  1.988   1.00 25.33 ? 103 GLY A N   1 
ATOM   2488 C CA  . GLY B 1 91  ? 7.864   -3.857  2.143   1.00 27.99 ? 103 GLY A CA  1 
ATOM   2489 C C   . GLY B 1 91  ? 8.155   -5.222  1.547   1.00 30.39 ? 103 GLY A C   1 
ATOM   2490 O O   . GLY B 1 91  ? 7.271   -5.914  1.035   1.00 27.92 ? 103 GLY A O   1 
ATOM   2491 N N   . ARG B 1 92  ? 9.436   -5.595  1.634   1.00 31.34 ? 104 ARG A N   1 
ATOM   2492 C CA  . ARG B 1 92  ? 9.922   -6.855  1.082   1.00 31.43 ? 104 ARG A CA  1 
ATOM   2493 C C   . ARG B 1 92  ? 9.462   -8.055  1.909   1.00 34.57 ? 104 ARG A C   1 
ATOM   2494 O O   . ARG B 1 92  ? 9.239   -9.140  1.349   1.00 38.04 ? 104 ARG A O   1 
ATOM   2495 C CB  . ARG B 1 92  ? 11.452  -6.802  1.006   1.00 34.58 ? 104 ARG A CB  1 
ATOM   2496 C CG  . ARG B 1 92  ? 12.139  -7.988  0.344   1.00 40.26 ? 104 ARG A CG  1 
ATOM   2497 C CD  . ARG B 1 92  ? 13.507  -8.287  0.961   1.00 36.91 ? 104 ARG A CD  1 
ATOM   2498 N NE  . ARG B 1 92  ? 14.121  -7.142  1.627   1.00 33.47 ? 104 ARG A NE  1 
ATOM   2499 C CZ  . ARG B 1 92  ? 15.084  -7.236  2.540   1.00 37.98 ? 104 ARG A CZ  1 
ATOM   2500 N NH1 . ARG B 1 92  ? 15.595  -8.402  2.892   1.00 39.97 ? 104 ARG A NH1 1 
ATOM   2501 N NH2 . ARG B 1 92  ? 15.545  -6.130  3.118   1.00 38.15 ? 104 ARG A NH2 1 
ATOM   2502 N N   . SER B 1 93  ? 9.314   -7.885  3.227   1.00 32.07 ? 105 SER A N   1 
ATOM   2503 C CA  . SER B 1 93  ? 8.902   -8.979  4.101   1.00 33.17 ? 105 SER A CA  1 
ATOM   2504 C C   . SER B 1 93  ? 7.502   -9.451  3.744   1.00 32.38 ? 105 SER A C   1 
ATOM   2505 O O   . SER B 1 93  ? 6.721   -8.733  3.118   1.00 33.43 ? 105 SER A O   1 
ATOM   2506 C CB  . SER B 1 93  ? 8.928   -8.552  5.569   1.00 29.22 ? 105 SER A CB  1 
ATOM   2507 O OG  . SER B 1 93  ? 9.232   -9.665  6.400   1.00 31.70 ? 105 SER A OG  1 
ATOM   2508 N N   . THR B 1 94  ? 7.186   -10.681 4.151   1.00 33.20 ? 106 THR A N   1 
ATOM   2509 C CA  . THR B 1 94  ? 5.860   -11.248 3.931   1.00 33.52 ? 106 THR A CA  1 
ATOM   2510 C C   . THR B 1 94  ? 5.084   -11.388 5.239   1.00 33.97 ? 106 THR A C   1 
ATOM   2511 O O   . THR B 1 94  ? 3.997   -11.981 5.252   1.00 36.08 ? 106 THR A O   1 
ATOM   2512 C CB  . THR B 1 94  ? 5.947   -12.602 3.210   1.00 33.07 ? 106 THR A CB  1 
ATOM   2513 O OG1 . THR B 1 94  ? 6.823   -13.487 3.916   1.00 36.06 ? 106 THR A OG1 1 
ATOM   2514 C CG2 . THR B 1 94  ? 6.460   -12.439 1.774   1.00 30.53 ? 106 THR A CG2 1 
ATOM   2515 N N   . GLU B 1 95  ? 5.617   -10.828 6.331   1.00 29.04 ? 107 GLU A N   1 
ATOM   2516 C CA  . GLU B 1 95  ? 5.060   -10.966 7.671   1.00 30.13 ? 107 GLU A CA  1 
ATOM   2517 C C   . GLU B 1 95  ? 3.741   -10.204 7.812   1.00 31.24 ? 107 GLU A C   1 
ATOM   2518 O O   . GLU B 1 95  ? 3.408   -9.331  7.006   1.00 34.85 ? 107 GLU A O   1 
ATOM   2519 C CB  . GLU B 1 95  ? 6.070   -10.472 8.711   1.00 25.98 ? 107 GLU A CB  1 
ATOM   2520 C CG  . GLU B 1 95  ? 7.351   -11.279 8.714   1.00 28.64 ? 107 GLU A CG  1 
ATOM   2521 C CD  . GLU B 1 95  ? 8.375   -10.794 9.728   1.00 34.51 ? 107 GLU A CD  1 
ATOM   2522 O OE1 . GLU B 1 95  ? 7.982   -10.190 10.743  1.00 32.38 ? 107 GLU A OE1 1 
ATOM   2523 O OE2 . GLU B 1 95  ? 9.585   -11.004 9.492   1.00 47.10 ? 107 GLU A OE2 1 
ATOM   2524 N N   . SER B 1 96  ? 2.986   -10.551 8.870   1.00 26.50 ? 108 SER A N   1 
ATOM   2525 C CA  . SER B 1 96  ? 1.710   -9.936  9.233   1.00 28.05 ? 108 SER A CA  1 
ATOM   2526 C C   . SER B 1 96  ? 1.641   -8.413  9.032   1.00 29.52 ? 108 SER A C   1 
ATOM   2527 O O   . SER B 1 96  ? 0.630   -7.919  8.513   1.00 30.63 ? 108 SER A O   1 
ATOM   2528 C CB  . SER B 1 96  ? 1.378   -10.302 10.683  1.00 28.55 ? 108 SER A CB  1 
ATOM   2529 O OG  . SER B 1 96  ? 0.699   -9.247  11.347  1.00 33.74 ? 108 SER A OG  1 
ATOM   2530 N N   . PRO B 1 97  ? 2.661   -7.628  9.407   1.00 25.98 ? 109 PRO A N   1 
ATOM   2531 C CA  . PRO B 1 97  ? 2.532   -6.167  9.266   1.00 26.70 ? 109 PRO A CA  1 
ATOM   2532 C C   . PRO B 1 97  ? 2.440   -5.654  7.831   1.00 30.44 ? 109 PRO A C   1 
ATOM   2533 O O   . PRO B 1 97  ? 1.986   -4.514  7.635   1.00 28.37 ? 109 PRO A O   1 
ATOM   2534 C CB  . PRO B 1 97  ? 3.800   -5.647  9.956   1.00 28.47 ? 109 PRO A CB  1 
ATOM   2535 C CG  . PRO B 1 97  ? 4.079   -6.681  10.990  1.00 26.63 ? 109 PRO A CG  1 
ATOM   2536 C CD  . PRO B 1 97  ? 3.834   -7.955  10.241  1.00 28.60 ? 109 PRO A CD  1 
ATOM   2537 N N   . ILE B 1 98  ? 2.837   -6.432  6.827   1.00 28.60 ? 110 ILE A N   1 
ATOM   2538 C CA  . ILE B 1 98  ? 3.047   -5.909  5.480   1.00 26.64 ? 110 ILE A CA  1 
ATOM   2539 C C   . ILE B 1 98  ? 1.797   -6.160  4.641   1.00 27.53 ? 110 ILE A C   1 
ATOM   2540 O O   . ILE B 1 98  ? 1.576   -7.255  4.123   1.00 30.66 ? 110 ILE A O   1 
ATOM   2541 C CB  . ILE B 1 98  ? 4.298   -6.499  4.834   1.00 25.18 ? 110 ILE A CB  1 
ATOM   2542 C CG1 . ILE B 1 98  ? 5.538   -5.973  5.549   1.00 26.33 ? 110 ILE A CG1 1 
ATOM   2543 C CG2 . ILE B 1 98  ? 4.383   -6.065  3.402   1.00 25.81 ? 110 ILE A CG2 1 
ATOM   2544 C CD1 . ILE B 1 98  ? 5.734   -4.471  5.398   1.00 24.68 ? 110 ILE A CD1 1 
ATOM   2545 N N   . ASP B 1 99  ? 1.005   -5.106  4.465   1.00 26.70 ? 111 ASP A N   1 
ATOM   2546 C CA  . ASP B 1 99  ? -0.203  -5.166  3.653   1.00 25.29 ? 111 ASP A CA  1 
ATOM   2547 C C   . ASP B 1 99  ? 0.107   -5.447  2.190   1.00 29.89 ? 111 ASP A C   1 
ATOM   2548 O O   . ASP B 1 99  ? -0.719  -6.035  1.478   1.00 33.66 ? 111 ASP A O   1 
ATOM   2549 C CB  . ASP B 1 99  ? -0.950  -3.841  3.773   1.00 25.58 ? 111 ASP A CB  1 
ATOM   2550 C CG  . ASP B 1 99  ? -1.515  -3.633  5.146   1.00 32.53 ? 111 ASP A CG  1 
ATOM   2551 O OD1 . ASP B 1 99  ? -2.643  -4.120  5.403   1.00 34.20 ? 111 ASP A OD1 1 
ATOM   2552 O OD2 . ASP B 1 99  ? -0.809  -3.012  5.973   1.00 32.91 ? 111 ASP A OD2 1 
ATOM   2553 N N   . PHE B 1 100 ? 1.270   -5.026  1.710   1.00 27.62 ? 112 PHE A N   1 
ATOM   2554 C CA  . PHE B 1 100 ? 1.595   -5.161  0.291   1.00 26.39 ? 112 PHE A CA  1 
ATOM   2555 C C   . PHE B 1 100 ? 3.068   -5.526  0.178   1.00 27.85 ? 112 PHE A C   1 
ATOM   2556 O O   . PHE B 1 100 ? 3.937   -4.668  0.365   1.00 27.12 ? 112 PHE A O   1 
ATOM   2557 C CB  . PHE B 1 100 ? 1.291   -3.890  -0.478  1.00 26.60 ? 112 PHE A CB  1 
ATOM   2558 C CG  . PHE B 1 100 ? 1.380   -4.064  -1.973  1.00 36.04 ? 112 PHE A CG  1 
ATOM   2559 C CD1 . PHE B 1 100 ? 1.061   -5.284  -2.572  1.00 37.38 ? 112 PHE A CD1 1 
ATOM   2560 C CD2 . PHE B 1 100 ? 1.832   -3.030  -2.780  1.00 35.15 ? 112 PHE A CD2 1 
ATOM   2561 C CE1 . PHE B 1 100 ? 1.147   -5.445  -3.951  1.00 33.86 ? 112 PHE A CE1 1 
ATOM   2562 C CE2 . PHE B 1 100 ? 1.926   -3.191  -4.162  1.00 33.93 ? 112 PHE A CE2 1 
ATOM   2563 C CZ  . PHE B 1 100 ? 1.586   -4.400  -4.741  1.00 35.33 ? 112 PHE A CZ  1 
ATOM   2564 N N   . VAL B 1 101 ? 3.334   -6.792  -0.139  1.00 28.72 ? 113 VAL A N   1 
ATOM   2565 C CA  . VAL B 1 101 ? 4.698   -7.274  -0.291  1.00 25.13 ? 113 VAL A CA  1 
ATOM   2566 C C   . VAL B 1 101 ? 5.201   -6.858  -1.664  1.00 29.62 ? 113 VAL A C   1 
ATOM   2567 O O   . VAL B 1 101 ? 4.528   -7.092  -2.677  1.00 31.11 ? 113 VAL A O   1 
ATOM   2568 C CB  . VAL B 1 101 ? 4.754   -8.798  -0.121  1.00 24.04 ? 113 VAL A CB  1 
ATOM   2569 C CG1 . VAL B 1 101 ? 6.194   -9.282  -0.161  1.00 26.55 ? 113 VAL A CG1 1 
ATOM   2570 C CG2 . VAL B 1 101 ? 4.085   -9.215  1.150   1.00 22.95 ? 113 VAL A CG2 1 
ATOM   2571 N N   . VAL B 1 102 ? 6.368   -6.216  -1.705  1.00 26.60 ? 114 VAL A N   1 
ATOM   2572 C CA  . VAL B 1 102 ? 7.003   -5.857  -2.967  1.00 28.26 ? 114 VAL A CA  1 
ATOM   2573 C C   . VAL B 1 102 ? 8.295   -6.652  -3.090  1.00 33.24 ? 114 VAL A C   1 
ATOM   2574 O O   . VAL B 1 102 ? 8.848   -7.158  -2.103  1.00 34.84 ? 114 VAL A O   1 
ATOM   2575 C CB  . VAL B 1 102 ? 7.276   -4.340  -3.122  1.00 27.37 ? 114 VAL A CB  1 
ATOM   2576 C CG1 . VAL B 1 102 ? 5.975   -3.537  -3.084  1.00 28.85 ? 114 VAL A CG1 1 
ATOM   2577 C CG2 . VAL B 1 102 ? 8.268   -3.838  -2.089  1.00 32.62 ? 114 VAL A CG2 1 
ATOM   2578 N N   . THR B 1 103 ? 8.775   -6.763  -4.335  1.00 37.86 ? 115 THR A N   1 
ATOM   2579 C CA  . THR B 1 103 ? 9.919   -7.596  -4.688  1.00 36.08 ? 115 THR A CA  1 
ATOM   2580 C C   . THR B 1 103 ? 10.806  -6.898  -5.707  1.00 37.06 ? 115 THR A C   1 
ATOM   2581 O O   . THR B 1 103 ? 10.334  -6.127  -6.550  1.00 37.74 ? 115 THR A O   1 
ATOM   2582 C CB  . THR B 1 103 ? 9.493   -8.962  -5.272  1.00 39.18 ? 115 THR A CB  1 
ATOM   2583 O OG1 . THR B 1 103 ? 10.655  -9.781  -5.457  1.00 45.60 ? 115 THR A OG1 1 
ATOM   2584 C CG2 . THR B 1 103 ? 8.768   -8.814  -6.621  1.00 30.43 ? 115 THR A CG2 1 
ATOM   2585 N N   . ASP B 1 104 ? 12.099  -7.205  -5.636  1.00 41.07 ? 116 ASP A N   1 
ATOM   2586 C CA  . ASP B 1 104 ? 13.020  -6.803  -6.691  1.00 44.43 ? 116 ASP A CA  1 
ATOM   2587 C C   . ASP B 1 104 ? 12.579  -7.353  -8.047  1.00 45.77 ? 116 ASP A C   1 
ATOM   2588 O O   . ASP B 1 104 ? 12.178  -8.516  -8.166  1.00 41.55 ? 116 ASP A O   1 
ATOM   2589 C CB  . ASP B 1 104 ? 14.430  -7.281  -6.369  1.00 38.03 ? 116 ASP A CB  1 
ATOM   2590 C CG  . ASP B 1 104 ? 15.159  -6.334  -5.456  1.00 40.99 ? 116 ASP A CG  1 
ATOM   2591 O OD1 . ASP B 1 104 ? 15.293  -5.171  -5.882  1.00 40.63 ? 116 ASP A OD1 1 
ATOM   2592 O OD2 . ASP B 1 104 ? 15.637  -6.742  -4.362  1.00 38.51 ? 116 ASP A OD2 1 
ATOM   2593 N N   . THR B 1 105 ? 12.668  -6.504  -9.073  1.00 52.11 ? 117 THR A N   1 
ATOM   2594 C CA  . THR B 1 105 ? 12.312  -6.860  -10.449 1.00 51.89 ? 117 THR A CA  1 
ATOM   2595 C C   . THR B 1 105 ? 13.530  -6.772  -11.394 1.00 47.74 ? 117 THR A C   1 
ATOM   2596 O O   . THR B 1 105 ? 14.342  -7.704  -11.505 1.00 37.44 ? 117 THR A O   1 
ATOM   2597 C CB  . THR B 1 105 ? 11.176  -5.932  -10.988 1.00 56.81 ? 117 THR A CB  1 
ATOM   2598 O OG1 . THR B 1 105 ? 11.474  -4.571  -10.647 1.00 57.45 ? 117 THR A OG1 1 
ATOM   2599 C CG2 . THR B 1 105 ? 9.826   -6.309  -10.361 1.00 49.84 ? 117 THR A CG2 1 
ATOM   2600 N N   . VAL B 1 118 ? 20.663  -13.443 -3.007  1.00 57.00 ? 130 VAL A N   1 
ATOM   2601 C CA  . VAL B 1 118 ? 19.301  -13.046 -2.660  1.00 63.76 ? 130 VAL A CA  1 
ATOM   2602 C C   . VAL B 1 118 ? 19.353  -11.793 -1.759  1.00 67.38 ? 130 VAL A C   1 
ATOM   2603 O O   . VAL B 1 118 ? 18.651  -11.680 -0.729  1.00 63.39 ? 130 VAL A O   1 
ATOM   2604 C CB  . VAL B 1 118 ? 18.495  -14.253 -2.032  1.00 60.88 ? 130 VAL A CB  1 
ATOM   2605 C CG1 . VAL B 1 118 ? 18.625  -15.488 -2.923  1.00 54.07 ? 130 VAL A CG1 1 
ATOM   2606 C CG2 . VAL B 1 118 ? 18.948  -14.599 -0.604  1.00 51.70 ? 130 VAL A CG2 1 
ATOM   2607 N N   . GLN B 1 119 ? 20.178  -10.832 -2.191  1.00 61.33 ? 131 GLN A N   1 
ATOM   2608 C CA  . GLN B 1 119 ? 20.345  -9.570  -1.476  1.00 61.39 ? 131 GLN A CA  1 
ATOM   2609 C C   . GLN B 1 119 ? 19.398  -8.511  -2.014  1.00 57.84 ? 131 GLN A C   1 
ATOM   2610 O O   . GLN B 1 119 ? 19.194  -8.390  -3.231  1.00 54.17 ? 131 GLN A O   1 
ATOM   2611 C CB  . GLN B 1 119 ? 21.782  -9.064  -1.576  1.00 59.11 ? 131 GLN A CB  1 
ATOM   2612 C CG  . GLN B 1 119 ? 22.799  -10.099 -1.162  1.00 64.82 ? 131 GLN A CG  1 
ATOM   2613 C CD  . GLN B 1 119 ? 23.061  -10.096 0.334   1.00 64.35 ? 131 GLN A CD  1 
ATOM   2614 O OE1 . GLN B 1 119 ? 22.145  -10.306 1.148   1.00 56.78 ? 131 GLN A OE1 1 
ATOM   2615 N NE2 . GLN B 1 119 ? 24.320  -9.860  0.708   1.00 61.34 ? 131 GLN A NE2 1 
ATOM   2616 N N   . SER B 1 120 ? 18.831  -7.734  -1.094  1.00 54.54 ? 132 SER A N   1 
ATOM   2617 C CA  . SER B 1 120 ? 17.792  -6.782  -1.437  1.00 45.75 ? 132 SER A CA  1 
ATOM   2618 C C   . SER B 1 120 ? 18.121  -5.445  -0.804  1.00 42.57 ? 132 SER A C   1 
ATOM   2619 O O   . SER B 1 120 ? 18.505  -5.387  0.370   1.00 42.71 ? 132 SER A O   1 
ATOM   2620 C CB  . SER B 1 120 ? 16.425  -7.274  -0.974  1.00 40.71 ? 132 SER A CB  1 
ATOM   2621 O OG  . SER B 1 120 ? 15.414  -6.534  -1.614  1.00 38.10 ? 132 SER A OG  1 
ATOM   2622 N N   . THR B 1 121 ? 18.005  -4.385  -1.604  1.00 37.92 ? 133 THR A N   1 
ATOM   2623 C CA  . THR B 1 121 ? 18.053  -3.016  -1.110  1.00 37.59 ? 133 THR A CA  1 
ATOM   2624 C C   . THR B 1 121 ? 16.703  -2.550  -0.589  1.00 36.28 ? 133 THR A C   1 
ATOM   2625 O O   . THR B 1 121 ? 16.615  -1.471  0.012   1.00 36.38 ? 133 THR A O   1 
ATOM   2626 C CB  . THR B 1 121 ? 18.524  -2.044  -2.211  1.00 35.10 ? 133 THR A CB  1 
ATOM   2627 O OG1 . THR B 1 121 ? 17.902  -2.367  -3.462  1.00 33.98 ? 133 THR A OG1 1 
ATOM   2628 C CG2 . THR B 1 121 ? 20.027  -2.088  -2.376  1.00 34.14 ? 133 THR A CG2 1 
ATOM   2629 N N   . ILE B 1 122 ? 15.655  -3.322  -0.817  1.00 35.92 ? 134 ILE A N   1 
ATOM   2630 C CA  . ILE B 1 122 ? 14.323  -2.925  -0.390  1.00 31.71 ? 134 ILE A CA  1 
ATOM   2631 C C   . ILE B 1 122 ? 14.157  -3.264  1.076   1.00 30.17 ? 134 ILE A C   1 
ATOM   2632 O O   . ILE B 1 122 ? 14.619  -4.307  1.544   1.00 35.44 ? 134 ILE A O   1 
ATOM   2633 C CB  . ILE B 1 122 ? 13.258  -3.615  -1.248  1.00 26.99 ? 134 ILE A CB  1 
ATOM   2634 C CG1 . ILE B 1 122 ? 13.591  -3.405  -2.731  1.00 29.68 ? 134 ILE A CG1 1 
ATOM   2635 C CG2 . ILE B 1 122 ? 11.903  -3.082  -0.867  1.00 31.95 ? 134 ILE A CG2 1 
ATOM   2636 C CD1 . ILE B 1 122 ? 12.588  -3.974  -3.716  1.00 30.82 ? 134 ILE A CD1 1 
ATOM   2637 N N   . SER B 1 123 ? 13.509  -2.389  1.819   1.00 25.82 ? 135 SER A N   1 
ATOM   2638 C CA  . SER B 1 123 ? 13.330  -2.693  3.222   1.00 31.32 ? 135 SER A CA  1 
ATOM   2639 C C   . SER B 1 123 ? 12.272  -3.767  3.413   1.00 29.43 ? 135 SER A C   1 
ATOM   2640 O O   . SER B 1 123 ? 11.361  -3.930  2.600   1.00 29.11 ? 135 SER A O   1 
ATOM   2641 C CB  . SER B 1 123 ? 12.954  -1.444  4.002   1.00 32.04 ? 135 SER A CB  1 
ATOM   2642 O OG  . SER B 1 123 ? 14.127  -0.867  4.543   1.00 48.86 ? 135 SER A OG  1 
ATOM   2643 N N   . ARG B 1 124 ? 12.406  -4.515  4.503   1.00 31.04 ? 136 ARG A N   1 
ATOM   2644 C CA  . ARG B 1 124 ? 11.339  -5.431  4.881   1.00 29.23 ? 136 ARG A CA  1 
ATOM   2645 C C   . ARG B 1 124 ? 10.078  -4.655  5.197   1.00 25.79 ? 136 ARG A C   1 
ATOM   2646 O O   . ARG B 1 124 ? 8.993   -4.973  4.701   1.00 25.97 ? 136 ARG A O   1 
ATOM   2647 C CB  . ARG B 1 124 ? 11.773  -6.285  6.065   1.00 26.61 ? 136 ARG A CB  1 
ATOM   2648 C CG  . ARG B 1 124 ? 12.735  -7.368  5.646   1.00 31.76 ? 136 ARG A CG  1 
ATOM   2649 C CD  . ARG B 1 124 ? 13.482  -7.967  6.817   1.00 37.88 ? 136 ARG A CD  1 
ATOM   2650 N NE  . ARG B 1 124 ? 14.764  -7.311  7.022   1.00 37.10 ? 136 ARG A NE  1 
ATOM   2651 C CZ  . ARG B 1 124 ? 15.331  -7.153  8.208   1.00 39.55 ? 136 ARG A CZ  1 
ATOM   2652 N NH1 . ARG B 1 124 ? 14.757  -7.605  9.312   1.00 33.05 ? 136 ARG A NH1 1 
ATOM   2653 N NH2 . ARG B 1 124 ? 16.497  -6.517  8.290   1.00 42.33 ? 136 ARG A NH2 1 
ATOM   2654 N N   . PHE B 1 125 ? 10.213  -3.602  5.988   1.00 24.28 ? 137 PHE A N   1 
ATOM   2655 C CA  . PHE B 1 125 ? 9.108   -2.715  6.313   1.00 23.63 ? 137 PHE A CA  1 
ATOM   2656 C C   . PHE B 1 125 ? 9.543   -1.334  5.834   1.00 24.97 ? 137 PHE A C   1 
ATOM   2657 O O   . PHE B 1 125 ? 10.218  -0.588  6.550   1.00 27.10 ? 137 PHE A O   1 
ATOM   2658 C CB  . PHE B 1 125 ? 8.802   -2.785  7.798   1.00 21.54 ? 137 PHE A CB  1 
ATOM   2659 C CG  . PHE B 1 125 ? 8.712   -4.195  8.314   1.00 23.95 ? 137 PHE A CG  1 
ATOM   2660 C CD1 . PHE B 1 125 ? 9.858   -4.892  8.670   1.00 25.12 ? 137 PHE A CD1 1 
ATOM   2661 C CD2 . PHE B 1 125 ? 7.490   -4.838  8.421   1.00 24.84 ? 137 PHE A CD2 1 
ATOM   2662 C CE1 . PHE B 1 125 ? 9.784   -6.188  9.129   1.00 24.19 ? 137 PHE A CE1 1 
ATOM   2663 C CE2 . PHE B 1 125 ? 7.414   -6.140  8.879   1.00 24.77 ? 137 PHE A CE2 1 
ATOM   2664 C CZ  . PHE B 1 125 ? 8.563   -6.811  9.235   1.00 26.71 ? 137 PHE A CZ  1 
ATOM   2665 N N   . ALA B 1 126 ? 9.172   -1.005  4.597   1.00 22.47 ? 138 ALA A N   1 
ATOM   2666 C CA  . ALA B 1 126 ? 9.756   0.136   3.906   1.00 22.62 ? 138 ALA A CA  1 
ATOM   2667 C C   . ALA B 1 126 ? 9.047   1.461   4.180   1.00 22.44 ? 138 ALA A C   1 
ATOM   2668 O O   . ALA B 1 126 ? 9.695   2.513   4.190   1.00 18.34 ? 138 ALA A O   1 
ATOM   2669 C CB  . ALA B 1 126 ? 9.770   -0.137  2.406   1.00 23.60 ? 138 ALA A CB  1 
ATOM   2670 N N   . CYS B 1 127 ? 7.743   1.441   4.416   1.00 22.69 ? 139 CYS A N   1 
ATOM   2671 C CA  . CYS B 1 127 ? 6.995   2.678   4.535   1.00 20.59 ? 139 CYS A CA  1 
ATOM   2672 C C   . CYS B 1 127 ? 5.580   2.348   4.986   1.00 23.77 ? 139 CYS A C   1 
ATOM   2673 O O   . CYS B 1 127 ? 5.147   1.196   4.919   1.00 25.63 ? 139 CYS A O   1 
ATOM   2674 C CB  . CYS B 1 127 ? 6.976   3.432   3.202   1.00 23.71 ? 139 CYS A CB  1 
ATOM   2675 S SG  . CYS B 1 127 ? 5.929   2.666   1.933   1.00 25.68 ? 139 CYS A SG  1 
ATOM   2676 N N   . ARG B 1 128 ? 4.862   3.373   5.451   1.00 25.16 ? 140 ARG A N   1 
ATOM   2677 C CA  . ARG B 1 128 ? 3.450   3.253   5.782   1.00 22.62 ? 140 ARG A CA  1 
ATOM   2678 C C   . ARG B 1 128 ? 2.689   4.361   5.079   1.00 21.94 ? 140 ARG A C   1 
ATOM   2679 O O   . ARG B 1 128 ? 3.180   5.487   4.950   1.00 23.41 ? 140 ARG A O   1 
ATOM   2680 C CB  . ARG B 1 128 ? 3.188   3.303   7.323   1.00 28.60 ? 140 ARG A CB  1 
ATOM   2681 C CG  . ARG B 1 128 ? 4.048   4.310   8.049   1.00 26.10 ? 140 ARG A CG  1 
ATOM   2682 C CD  . ARG B 1 128 ? 4.784   3.728   9.246   1.00 24.41 ? 140 ARG A CD  1 
ATOM   2683 N NE  . ARG B 1 128 ? 5.901   4.595   9.630   1.00 26.41 ? 140 ARG A NE  1 
ATOM   2684 C CZ  . ARG B 1 128 ? 5.797   5.657   10.427  1.00 30.64 ? 140 ARG A CZ  1 
ATOM   2685 N NH1 . ARG B 1 128 ? 4.672   5.931   11.081  1.00 28.88 ? 140 ARG A NH1 1 
ATOM   2686 N NH2 . ARG B 1 128 ? 6.855   6.447   10.601  1.00 25.12 ? 140 ARG A NH2 1 
ATOM   2687 N N   . ILE B 1 129 ? 1.523   4.009   4.564   1.00 23.94 ? 141 ILE A N   1 
ATOM   2688 C CA  . ILE B 1 129 ? 0.539   4.976   4.106   1.00 22.76 ? 141 ILE A CA  1 
ATOM   2689 C C   . ILE B 1 129 ? -0.507  5.113   5.198   1.00 24.63 ? 141 ILE A C   1 
ATOM   2690 O O   . ILE B 1 129 ? -1.075  4.108   5.656   1.00 25.76 ? 141 ILE A O   1 
ATOM   2691 C CB  . ILE B 1 129 ? -0.125  4.540   2.791   1.00 24.26 ? 141 ILE A CB  1 
ATOM   2692 C CG1 . ILE B 1 129 ? 0.876   3.821   1.871   1.00 23.31 ? 141 ILE A CG1 1 
ATOM   2693 C CG2 . ILE B 1 129 ? -0.766  5.737   2.143   1.00 22.04 ? 141 ILE A CG2 1 
ATOM   2694 C CD1 . ILE B 1 129 ? 1.795   4.729   1.160   1.00 21.65 ? 141 ILE A CD1 1 
ATOM   2695 N N   . ILE B 1 130 ? -0.757  6.343   5.627   1.00 21.91 ? 142 ILE A N   1 
ATOM   2696 C CA  . ILE B 1 130 ? -1.821  6.635   6.577   1.00 21.95 ? 142 ILE A CA  1 
ATOM   2697 C C   . ILE B 1 130 ? -2.934  7.365   5.846   1.00 26.43 ? 142 ILE A C   1 
ATOM   2698 O O   . ILE B 1 130 ? -2.692  8.401   5.210   1.00 24.46 ? 142 ILE A O   1 
ATOM   2699 C CB  . ILE B 1 130 ? -1.321  7.467   7.757   1.00 19.96 ? 142 ILE A CB  1 
ATOM   2700 C CG1 . ILE B 1 130 ? -0.152  6.764   8.446   1.00 19.95 ? 142 ILE A CG1 1 
ATOM   2701 C CG2 . ILE B 1 130 ? -2.477  7.714   8.675   1.00 21.40 ? 142 ILE A CG2 1 
ATOM   2702 C CD1 . ILE B 1 130 ? -0.152  6.944   9.920   1.00 18.16 ? 142 ILE A CD1 1 
ATOM   2703 N N   . CYS B 1 131 ? -4.156  6.838   5.960   1.00 25.42 ? 143 CYS A N   1 
ATOM   2704 C CA  . CYS B 1 131 ? -5.327  7.374   5.279   1.00 21.52 ? 143 CYS A CA  1 
ATOM   2705 C C   . CYS B 1 131 ? -6.350  7.857   6.287   1.00 25.50 ? 143 CYS A C   1 
ATOM   2706 O O   . CYS B 1 131 ? -6.751  7.105   7.176   1.00 28.22 ? 143 CYS A O   1 
ATOM   2707 C CB  . CYS B 1 131 ? -5.974  6.330   4.380   1.00 23.89 ? 143 CYS A CB  1 
ATOM   2708 S SG  . CYS B 1 131 ? -4.863  5.642   3.153   1.00 25.15 ? 143 CYS A SG  1 
ATOM   2709 N N   . GLU B 1 132 ? -6.772  9.108   6.136   1.00 30.52 ? 144 GLU A N   1 
ATOM   2710 C CA  . GLU B 1 132 ? -7.855  9.647   6.939   1.00 26.19 ? 144 GLU A CA  1 
ATOM   2711 C C   . GLU B 1 132 ? -9.117  8.841   6.662   1.00 33.11 ? 144 GLU A C   1 
ATOM   2712 O O   . GLU B 1 132 ? -9.426  8.553   5.504   1.00 36.04 ? 144 GLU A O   1 
ATOM   2713 C CB  . GLU B 1 132 ? -8.046  11.113  6.587   1.00 24.53 ? 144 GLU A CB  1 
ATOM   2714 C CG  . GLU B 1 132 ? -6.831  11.942  6.874   1.00 30.86 ? 144 GLU A CG  1 
ATOM   2715 C CD  . GLU B 1 132 ? -6.789  12.378  8.319   1.00 47.78 ? 144 GLU A CD  1 
ATOM   2716 O OE1 . GLU B 1 132 ? -5.673  12.594  8.855   1.00 51.96 ? 144 GLU A OE1 1 
ATOM   2717 O OE2 . GLU B 1 132 ? -7.888  12.484  8.925   1.00 56.76 ? 144 GLU A OE2 1 
ATOM   2718 N N   . ARG B 1 133 ? -9.823  8.431   7.723   1.00 33.46 ? 145 ARG A N   1 
ATOM   2719 C CA  . ARG B 1 133 ? -11.007 7.582   7.576   1.00 31.34 ? 145 ARG A CA  1 
ATOM   2720 C C   . ARG B 1 133 ? -12.273 8.355   7.199   1.00 35.04 ? 145 ARG A C   1 
ATOM   2721 O O   . ARG B 1 133 ? -13.310 7.726   6.962   1.00 31.08 ? 145 ARG A O   1 
ATOM   2722 C CB  . ARG B 1 133 ? -11.250 6.795   8.871   1.00 31.47 ? 145 ARG A CB  1 
ATOM   2723 C CG  . ARG B 1 133 ? -10.144 5.803   9.201   1.00 30.98 ? 145 ARG A CG  1 
ATOM   2724 C CD  . ARG B 1 133 ? -10.435 4.964   10.440  1.00 29.21 ? 145 ARG A CD  1 
ATOM   2725 N NE  . ARG B 1 133 ? -11.783 4.406   10.453  1.00 29.67 ? 145 ARG A NE  1 
ATOM   2726 C CZ  . ARG B 1 133 ? -12.111 3.195   10.015  1.00 34.56 ? 145 ARG A CZ  1 
ATOM   2727 N NH1 . ARG B 1 133 ? -11.215 2.390   9.463   1.00 35.03 ? 145 ARG A NH1 1 
ATOM   2728 N NH2 . ARG B 1 133 ? -13.374 2.783   10.122  1.00 37.05 ? 145 ARG A NH2 1 
ATOM   2729 N N   . ASN B 1 134 ? -12.216 9.683   7.133   1.00 35.67 ? 146 ASN A N   1 
ATOM   2730 C CA  . ASN B 1 134 ? -13.329 10.548  6.778   1.00 34.79 ? 146 ASN A CA  1 
ATOM   2731 C C   . ASN B 1 134 ? -13.036 11.282  5.478   1.00 37.13 ? 146 ASN A C   1 
ATOM   2732 O O   . ASN B 1 134 ? -11.870 11.471  5.115   1.00 37.41 ? 146 ASN A O   1 
ATOM   2733 C CB  . ASN B 1 134 ? -13.588 11.570  7.891   1.00 42.70 ? 146 ASN A CB  1 
ATOM   2734 C CG  . ASN B 1 134 ? -14.009 10.909  9.204   1.00 51.78 ? 146 ASN A CG  1 
ATOM   2735 O OD1 . ASN B 1 134 ? -15.194 10.602  9.417   1.00 48.78 ? 146 ASN A OD1 1 
ATOM   2736 N ND2 . ASN B 1 134 ? -13.036 10.694  10.097  1.00 46.54 ? 146 ASN A ND2 1 
ATOM   2737 N N   . PRO B 1 135 ? -14.065 11.702  4.744   1.00 36.69 ? 147 PRO A N   1 
ATOM   2738 C CA  . PRO B 1 135 ? -13.839 12.430  3.497   1.00 30.86 ? 147 PRO A CA  1 
ATOM   2739 C C   . PRO B 1 135 ? -12.931 13.621  3.721   1.00 28.65 ? 147 PRO A C   1 
ATOM   2740 O O   . PRO B 1 135 ? -13.029 14.294  4.760   1.00 28.30 ? 147 PRO A O   1 
ATOM   2741 C CB  . PRO B 1 135 ? -15.250 12.870  3.093   1.00 28.28 ? 147 PRO A CB  1 
ATOM   2742 C CG  . PRO B 1 135 ? -16.105 11.770  3.613   1.00 32.25 ? 147 PRO A CG  1 
ATOM   2743 C CD  . PRO B 1 135 ? -15.493 11.420  4.948   1.00 38.10 ? 147 PRO A CD  1 
ATOM   2744 N N   . PRO B 1 136 ? -12.019 13.908  2.767   1.00 27.00 ? 148 PRO A N   1 
ATOM   2745 C CA  . PRO B 1 136 ? -11.834 13.228  1.489   1.00 26.60 ? 148 PRO A CA  1 
ATOM   2746 C C   . PRO B 1 136 ? -10.833 12.067  1.517   1.00 29.36 ? 148 PRO A C   1 
ATOM   2747 O O   . PRO B 1 136 ? -10.338 11.703  0.460   1.00 28.48 ? 148 PRO A O   1 
ATOM   2748 C CB  . PRO B 1 136 ? -11.322 14.351  0.573   1.00 27.23 ? 148 PRO A CB  1 
ATOM   2749 C CG  . PRO B 1 136 ? -10.799 15.446  1.470   1.00 22.00 ? 148 PRO A CG  1 
ATOM   2750 C CD  . PRO B 1 136 ? -11.148 15.091  2.886   1.00 26.28 ? 148 PRO A CD  1 
ATOM   2751 N N   . PHE B 1 137 ? -10.506 11.474  2.670   1.00 27.92 ? 149 PHE A N   1 
ATOM   2752 C CA  . PHE B 1 137 ? -9.688  10.249  2.742   1.00 27.08 ? 149 PHE A CA  1 
ATOM   2753 C C   . PHE B 1 137 ? -8.250  10.491  2.286   1.00 25.79 ? 149 PHE A C   1 
ATOM   2754 O O   . PHE B 1 137 ? -7.665  9.659   1.592   1.00 23.49 ? 149 PHE A O   1 
ATOM   2755 C CB  . PHE B 1 137 ? -10.314 9.099   1.943   1.00 29.58 ? 149 PHE A CB  1 
ATOM   2756 C CG  . PHE B 1 137 ? -11.802 8.953   2.164   1.00 34.36 ? 149 PHE A CG  1 
ATOM   2757 C CD1 . PHE B 1 137 ? -12.304 8.691   3.427   1.00 35.19 ? 149 PHE A CD1 1 
ATOM   2758 C CD2 . PHE B 1 137 ? -12.699 9.090   1.111   1.00 32.72 ? 149 PHE A CD2 1 
ATOM   2759 C CE1 . PHE B 1 137 ? -13.666 8.571   3.638   1.00 35.10 ? 149 PHE A CE1 1 
ATOM   2760 C CE2 . PHE B 1 137 ? -14.060 8.964   1.321   1.00 30.36 ? 149 PHE A CE2 1 
ATOM   2761 C CZ  . PHE B 1 137 ? -14.541 8.709   2.586   1.00 33.02 ? 149 PHE A CZ  1 
ATOM   2762 N N   . THR B 1 138 ? -7.679  11.627  2.697   1.00 27.83 ? 150 THR A N   1 
ATOM   2763 C CA  . THR B 1 138 ? -6.319  11.998  2.317   1.00 23.83 ? 150 THR A CA  1 
ATOM   2764 C C   . THR B 1 138 ? -5.303  10.952  2.766   1.00 21.31 ? 150 THR A C   1 
ATOM   2765 O O   . THR B 1 138 ? -5.350  10.465  3.895   1.00 23.77 ? 150 THR A O   1 
ATOM   2766 C CB  . THR B 1 138 ? -5.961  13.349  2.933   1.00 25.08 ? 150 THR A CB  1 
ATOM   2767 O OG1 . THR B 1 138 ? -7.019  14.278  2.697   1.00 26.27 ? 150 THR A OG1 1 
ATOM   2768 C CG2 . THR B 1 138 ? -4.686  13.888  2.333   1.00 27.57 ? 150 THR A CG2 1 
ATOM   2769 N N   . ALA B 1 139 ? -4.354  10.641  1.886   1.00 19.54 ? 151 ALA A N   1 
ATOM   2770 C CA  . ALA B 1 139 ? -3.321  9.642   2.125   1.00 17.57 ? 151 ALA A CA  1 
ATOM   2771 C C   . ALA B 1 139 ? -1.959  10.299  2.252   1.00 17.95 ? 151 ALA A C   1 
ATOM   2772 O O   . ALA B 1 139 ? -1.587  11.115  1.408   1.00 20.23 ? 151 ALA A O   1 
ATOM   2773 C CB  . ALA B 1 139 ? -3.282  8.625   0.988   1.00 18.12 ? 151 ALA A CB  1 
ATOM   2774 N N   . ARG B 1 140 ? -1.202  9.919   3.285   1.00 20.43 ? 152 ARG A N   1 
ATOM   2775 C CA  . ARG B 1 140 ? 0.120   10.483  3.540   1.00 17.99 ? 152 ARG A CA  1 
ATOM   2776 C C   . ARG B 1 140 ? 1.140   9.362   3.687   1.00 20.47 ? 152 ARG A C   1 
ATOM   2777 O O   . ARG B 1 140 ? 0.824   8.303   4.234   1.00 23.83 ? 152 ARG A O   1 
ATOM   2778 C CB  . ARG B 1 140 ? 0.110   11.347  4.795   1.00 15.73 ? 152 ARG A CB  1 
ATOM   2779 C CG  . ARG B 1 140 ? -0.465  12.698  4.535   1.00 16.68 ? 152 ARG A CG  1 
ATOM   2780 C CD  . ARG B 1 140 ? -0.535  13.527  5.764   1.00 18.83 ? 152 ARG A CD  1 
ATOM   2781 N NE  . ARG B 1 140 ? -1.380  14.695  5.552   1.00 25.38 ? 152 ARG A NE  1 
ATOM   2782 C CZ  . ARG B 1 140 ? -2.655  14.755  5.905   1.00 28.29 ? 152 ARG A CZ  1 
ATOM   2783 N NH1 . ARG B 1 140 ? -3.242  13.751  6.533   1.00 31.47 ? 152 ARG A NH1 1 
ATOM   2784 N NH2 . ARG B 1 140 ? -3.359  15.848  5.620   1.00 26.59 ? 152 ARG A NH2 1 
ATOM   2785 N N   . ILE B 1 141 ? 2.362   9.582   3.204   1.00 19.58 ? 153 ILE A N   1 
ATOM   2786 C CA  . ILE B 1 141 ? 3.410   8.561   3.260   1.00 18.91 ? 153 ILE A CA  1 
ATOM   2787 C C   . ILE B 1 141 ? 4.461   8.919   4.312   1.00 18.81 ? 153 ILE A C   1 
ATOM   2788 O O   . ILE B 1 141 ? 4.841   10.088  4.463   1.00 21.44 ? 153 ILE A O   1 
ATOM   2789 C CB  . ILE B 1 141 ? 4.057   8.353   1.875   1.00 18.62 ? 153 ILE A CB  1 
ATOM   2790 C CG1 . ILE B 1 141 ? 4.945   7.126   1.905   1.00 18.79 ? 153 ILE A CG1 1 
ATOM   2791 C CG2 . ILE B 1 141 ? 4.854   9.559   1.418   1.00 15.77 ? 153 ILE A CG2 1 
ATOM   2792 C CD1 . ILE B 1 141 ? 5.020   6.457   0.595   1.00 18.36 ? 153 ILE A CD1 1 
ATOM   2793 N N   . TYR B 1 142 ? 4.918   7.910   5.059   1.00 19.57 ? 154 TYR A N   1 
ATOM   2794 C CA  . TYR B 1 142 ? 6.003   8.061   6.032   1.00 22.98 ? 154 TYR A CA  1 
ATOM   2795 C C   . TYR B 1 142 ? 7.045   6.986   5.747   1.00 22.35 ? 154 TYR A C   1 
ATOM   2796 O O   . TYR B 1 142 ? 6.684   5.850   5.422   1.00 21.25 ? 154 TYR A O   1 
ATOM   2797 C CB  . TYR B 1 142 ? 5.507   7.957   7.528   1.00 20.38 ? 154 TYR A CB  1 
ATOM   2798 C CG  . TYR B 1 142 ? 4.383   8.909   7.837   1.00 17.60 ? 154 TYR A CG  1 
ATOM   2799 C CD1 . TYR B 1 142 ? 3.083   8.623   7.435   1.00 17.73 ? 154 TYR A CD1 1 
ATOM   2800 C CD2 . TYR B 1 142 ? 4.627   10.132  8.463   1.00 19.13 ? 154 TYR A CD2 1 
ATOM   2801 C CE1 . TYR B 1 142 ? 2.048   9.515   7.665   1.00 19.83 ? 154 TYR A CE1 1 
ATOM   2802 C CE2 . TYR B 1 142 ? 3.590   11.041  8.708   1.00 15.27 ? 154 TYR A CE2 1 
ATOM   2803 C CZ  . TYR B 1 142 ? 2.300   10.717  8.302   1.00 17.48 ? 154 TYR A CZ  1 
ATOM   2804 O OH  . TYR B 1 142 ? 1.247   11.576  8.517   1.00 19.17 ? 154 TYR A OH  1 
ATOM   2805 N N   . ALA B 1 143 ? 8.328   7.349   5.837   1.00 19.88 ? 155 ALA A N   1 
ATOM   2806 C CA  . ALA B 1 143 ? 9.379   6.353   5.702   1.00 18.93 ? 155 ALA A CA  1 
ATOM   2807 C C   . ALA B 1 143 ? 9.322   5.370   6.873   1.00 21.36 ? 155 ALA A C   1 
ATOM   2808 O O   . ALA B 1 143 ? 8.832   5.695   7.965   1.00 22.26 ? 155 ALA A O   1 
ATOM   2809 C CB  . ALA B 1 143 ? 10.752  7.021   5.638   1.00 17.45 ? 155 ALA A CB  1 
ATOM   2810 N N   . ALA B 1 144 ? 9.813   4.149   6.618   1.00 18.80 ? 156 ALA A N   1 
ATOM   2811 C CA  . ALA B 1 144 ? 9.897   3.033   7.572   1.00 21.44 ? 156 ALA A CA  1 
ATOM   2812 C C   . ALA B 1 144 ? 8.535   2.440   7.942   1.00 23.28 ? 156 ALA A C   1 
ATOM   2813 O O   . ALA B 1 144 ? 7.524   3.150   7.972   1.00 26.77 ? 156 ALA A O   1 
ATOM   2814 C CB  . ALA B 1 144 ? 10.643  3.451   8.846   1.00 14.59 ? 156 ALA A CB  1 
ATOM   2815 N N   . GLY B 1 145 ? 8.494   1.142   8.236   1.00 21.53 ? 157 GLY A N   1 
ATOM   2816 C CA  . GLY B 1 145 ? 7.276   0.483   8.677   1.00 21.40 ? 157 GLY A CA  1 
ATOM   2817 C C   . GLY B 1 145 ? 7.483   -0.247  9.993   1.00 25.28 ? 157 GLY A C   1 
ATOM   2818 O O   . GLY B 1 145 ? 8.578   -0.745  10.283  1.00 24.74 ? 157 GLY A O   1 
ATOM   2819 N N   . PHE B 1 146 ? 6.422   -0.299  10.801  1.00 25.47 ? 158 PHE A N   1 
ATOM   2820 C CA  . PHE B 1 146 ? 6.493   -0.993  12.081  1.00 22.24 ? 158 PHE A CA  1 
ATOM   2821 C C   . PHE B 1 146 ? 6.577   -2.491  11.850  1.00 27.50 ? 158 PHE A C   1 
ATOM   2822 O O   . PHE B 1 146 ? 5.736   -3.063  11.148  1.00 28.51 ? 158 PHE A O   1 
ATOM   2823 C CB  . PHE B 1 146 ? 5.264   -0.697  12.918  1.00 20.86 ? 158 PHE A CB  1 
ATOM   2824 C CG  . PHE B 1 146 ? 5.200   0.693   13.428  1.00 22.79 ? 158 PHE A CG  1 
ATOM   2825 C CD1 . PHE B 1 146 ? 5.921   1.068   14.537  1.00 22.06 ? 158 PHE A CD1 1 
ATOM   2826 C CD2 . PHE B 1 146 ? 4.393   1.630   12.810  1.00 25.08 ? 158 PHE A CD2 1 
ATOM   2827 C CE1 . PHE B 1 146 ? 5.850   2.363   15.017  1.00 22.92 ? 158 PHE A CE1 1 
ATOM   2828 C CE2 . PHE B 1 146 ? 4.319   2.920   13.287  1.00 23.91 ? 158 PHE A CE2 1 
ATOM   2829 C CZ  . PHE B 1 146 ? 5.050   3.286   14.392  1.00 20.97 ? 158 PHE A CZ  1 
ATOM   2830 N N   . ASP B 1 147 ? 7.577   -3.134  12.461  1.00 27.69 ? 159 ASP A N   1 
ATOM   2831 C CA  . ASP B 1 147 ? 7.738   -4.579  12.337  1.00 24.22 ? 159 ASP A CA  1 
ATOM   2832 C C   . ASP B 1 147 ? 6.676   -5.322  13.139  1.00 26.36 ? 159 ASP A C   1 
ATOM   2833 O O   . ASP B 1 147 ? 5.662   -4.737  13.540  1.00 23.39 ? 159 ASP A O   1 
ATOM   2834 C CB  . ASP B 1 147 ? 9.144   -5.008  12.771  1.00 21.60 ? 159 ASP A CB  1 
ATOM   2835 C CG  . ASP B 1 147 ? 9.383   -4.877  14.280  1.00 29.49 ? 159 ASP A CG  1 
ATOM   2836 O OD1 . ASP B 1 147 ? 8.441   -4.730  15.096  1.00 31.36 ? 159 ASP A OD1 1 
ATOM   2837 O OD2 . ASP B 1 147 ? 10.565  -4.924  14.662  1.00 32.49 ? 159 ASP A OD2 1 
ATOM   2838 N N   . SER B 1 148 ? 6.926   -6.606  13.410  1.00 29.51 ? 160 SER A N   1 
ATOM   2839 C CA  . SER B 1 148 ? 5.955   -7.439  14.109  1.00 27.68 ? 160 SER A CA  1 
ATOM   2840 C C   . SER B 1 148 ? 5.932   -7.196  15.605  1.00 31.62 ? 160 SER A C   1 
ATOM   2841 O O   . SER B 1 148 ? 4.963   -7.589  16.267  1.00 32.70 ? 160 SER A O   1 
ATOM   2842 C CB  . SER B 1 148 ? 6.233   -8.908  13.835  1.00 25.23 ? 160 SER A CB  1 
ATOM   2843 O OG  . SER B 1 148 ? 6.730   -9.072  12.528  1.00 31.01 ? 160 SER A OG  1 
ATOM   2844 N N   . SER B 1 149 ? 6.975   -6.578  16.150  1.00 32.73 ? 161 SER A N   1 
ATOM   2845 C CA  . SER B 1 149 ? 6.965   -6.097  17.520  1.00 29.35 ? 161 SER A CA  1 
ATOM   2846 C C   . SER B 1 149 ? 6.370   -4.702  17.620  1.00 31.87 ? 161 SER A C   1 
ATOM   2847 O O   . SER B 1 149 ? 6.499   -4.053  18.666  1.00 34.31 ? 161 SER A O   1 
ATOM   2848 C CB  . SER B 1 149 ? 8.385   -6.121  18.078  1.00 32.95 ? 161 SER A CB  1 
ATOM   2849 O OG  . SER B 1 149 ? 9.081   -7.267  17.618  1.00 36.93 ? 161 SER A OG  1 
ATOM   2850 N N   . LYS B 1 150 ? 5.719   -4.236  16.549  1.00 31.60 ? 162 LYS A N   1 
ATOM   2851 C CA  . LYS B 1 150 ? 5.196   -2.878  16.462  1.00 26.32 ? 162 LYS A CA  1 
ATOM   2852 C C   . LYS B 1 150 ? 6.295   -1.856  16.762  1.00 25.63 ? 162 LYS A C   1 
ATOM   2853 O O   . LYS B 1 150 ? 6.048   -0.800  17.350  1.00 25.96 ? 162 LYS A O   1 
ATOM   2854 C CB  . LYS B 1 150 ? 3.979   -2.723  17.373  1.00 24.96 ? 162 LYS A CB  1 
ATOM   2855 C CG  . LYS B 1 150 ? 2.903   -3.778  17.096  1.00 27.06 ? 162 LYS A CG  1 
ATOM   2856 C CD  . LYS B 1 150 ? 1.555   -3.401  17.712  1.00 38.43 ? 162 LYS A CD  1 
ATOM   2857 C CE  . LYS B 1 150 ? 0.434   -4.359  17.315  1.00 39.06 ? 162 LYS A CE  1 
ATOM   2858 N NZ  . LYS B 1 150 ? -0.152  -4.035  15.982  1.00 45.61 ? 162 LYS A NZ  1 
ATOM   2859 N N   . ASN B 1 151 ? 7.519   -2.174  16.322  1.00 25.40 ? 163 ASN A N   1 
ATOM   2860 C CA  . ASN B 1 151 ? 8.714   -1.374  16.554  1.00 25.24 ? 163 ASN A CA  1 
ATOM   2861 C C   . ASN B 1 151 ? 9.343   -0.899  15.249  1.00 23.28 ? 163 ASN A C   1 
ATOM   2862 O O   . ASN B 1 151 ? 9.343   -1.621  14.249  1.00 22.10 ? 163 ASN A O   1 
ATOM   2863 C CB  . ASN B 1 151 ? 9.758   -2.159  17.324  1.00 23.91 ? 163 ASN A CB  1 
ATOM   2864 C CG  . ASN B 1 151 ? 9.446   -2.238  18.777  1.00 24.77 ? 163 ASN A CG  1 
ATOM   2865 O OD1 . ASN B 1 151 ? 8.913   -1.302  19.348  1.00 26.66 ? 163 ASN A OD1 1 
ATOM   2866 N ND2 . ASN B 1 151 ? 9.818   -3.338  19.405  1.00 28.28 ? 163 ASN A ND2 1 
ATOM   2867 N N   . ILE B 1 152 ? 9.866   0.330   15.282  1.00 24.10 ? 164 ILE A N   1 
ATOM   2868 C CA  . ILE B 1 152 ? 10.760  0.894   14.274  1.00 20.68 ? 164 ILE A CA  1 
ATOM   2869 C C   . ILE B 1 152 ? 12.062  1.265   14.988  1.00 23.13 ? 164 ILE A C   1 
ATOM   2870 O O   . ILE B 1 152 ? 12.037  1.788   16.114  1.00 22.97 ? 164 ILE A O   1 
ATOM   2871 C CB  . ILE B 1 152 ? 10.126  2.116   13.567  1.00 17.52 ? 164 ILE A CB  1 
ATOM   2872 C CG1 . ILE B 1 152 ? 9.000   1.697   12.649  1.00 17.43 ? 164 ILE A CG1 1 
ATOM   2873 C CG2 . ILE B 1 152 ? 11.119  2.867   12.733  1.00 18.94 ? 164 ILE A CG2 1 
ATOM   2874 C CD1 . ILE B 1 152 ? 8.355   2.861   12.001  1.00 17.60 ? 164 ILE A CD1 1 
ATOM   2875 N N   . PHE B 1 153 ? 13.199  0.933   14.361  1.00 20.26 ? 165 PHE A N   1 
ATOM   2876 C CA  . PHE B 1 153 ? 14.531  1.203   14.903  1.00 20.34 ? 165 PHE A CA  1 
ATOM   2877 C C   . PHE B 1 153 ? 15.358  1.950   13.862  1.00 19.03 ? 165 PHE A C   1 
ATOM   2878 O O   . PHE B 1 153 ? 15.464  1.507   12.722  1.00 20.71 ? 165 PHE A O   1 
ATOM   2879 C CB  . PHE B 1 153 ? 15.284  -0.088  15.295  1.00 20.36 ? 165 PHE A CB  1 
ATOM   2880 C CG  . PHE B 1 153 ? 14.573  -0.962  16.292  1.00 21.28 ? 165 PHE A CG  1 
ATOM   2881 C CD1 . PHE B 1 153 ? 14.817  -0.834  17.647  1.00 22.71 ? 165 PHE A CD1 1 
ATOM   2882 C CD2 . PHE B 1 153 ? 13.688  -1.934  15.865  1.00 21.30 ? 165 PHE A CD2 1 
ATOM   2883 C CE1 . PHE B 1 153 ? 14.170  -1.637  18.554  1.00 25.75 ? 165 PHE A CE1 1 
ATOM   2884 C CE2 . PHE B 1 153 ? 13.035  -2.748  16.764  1.00 23.93 ? 165 PHE A CE2 1 
ATOM   2885 C CZ  . PHE B 1 153 ? 13.277  -2.603  18.113  1.00 28.80 ? 165 PHE A CZ  1 
ATOM   2886 N N   . LEU B 1 154 ? 15.955  3.065   14.250  1.00 20.38 ? 166 LEU A N   1 
ATOM   2887 C CA  . LEU B 1 154 ? 16.961  3.738   13.440  1.00 20.01 ? 166 LEU A CA  1 
ATOM   2888 C C   . LEU B 1 154 ? 18.294  3.654   14.162  1.00 19.76 ? 166 LEU A C   1 
ATOM   2889 O O   . LEU B 1 154 ? 18.440  4.188   15.266  1.00 22.97 ? 166 LEU A O   1 
ATOM   2890 C CB  . LEU B 1 154 ? 16.589  5.190   13.157  1.00 22.78 ? 166 LEU A CB  1 
ATOM   2891 C CG  . LEU B 1 154 ? 15.426  5.434   12.208  1.00 25.36 ? 166 LEU A CG  1 
ATOM   2892 C CD1 . LEU B 1 154 ? 14.144  5.321   12.978  1.00 26.05 ? 166 LEU A CD1 1 
ATOM   2893 C CD2 . LEU B 1 154 ? 15.555  6.827   11.611  1.00 21.18 ? 166 LEU A CD2 1 
ATOM   2894 N N   . GLY B 1 155 ? 19.254  2.982   13.538  1.00 20.25 ? 167 GLY A N   1 
ATOM   2895 C CA  . GLY B 1 155 ? 20.519  2.711   14.176  1.00 23.61 ? 167 GLY A CA  1 
ATOM   2896 C C   . GLY B 1 155 ? 21.396  3.928   14.252  1.00 26.19 ? 167 GLY A C   1 
ATOM   2897 O O   . GLY B 1 155 ? 21.093  4.975   13.678  1.00 28.19 ? 167 GLY A O   1 
ATOM   2898 N N   . GLU B 1 156 ? 22.510  3.772   14.973  1.00 27.40 ? 168 GLU A N   1 
ATOM   2899 C CA  . GLU B 1 156 ? 23.416  4.895   15.172  1.00 26.58 ? 168 GLU A CA  1 
ATOM   2900 C C   . GLU B 1 156 ? 23.851  5.506   13.843  1.00 27.75 ? 168 GLU A C   1 
ATOM   2901 O O   . GLU B 1 156 ? 23.922  6.735   13.712  1.00 30.13 ? 168 GLU A O   1 
ATOM   2902 C CB  . GLU B 1 156 ? 24.634  4.459   15.988  1.00 26.23 ? 168 GLU A CB  1 
ATOM   2903 C CG  . GLU B 1 156 ? 25.710  5.527   16.032  1.00 27.50 ? 168 GLU A CG  1 
ATOM   2904 C CD  . GLU B 1 156 ? 26.466  5.569   17.341  1.00 38.35 ? 168 GLU A CD  1 
ATOM   2905 O OE1 . GLU B 1 156 ? 26.513  4.523   18.033  1.00 42.68 ? 168 GLU A OE1 1 
ATOM   2906 O OE2 . GLU B 1 156 ? 27.006  6.657   17.676  1.00 45.16 ? 168 GLU A OE2 1 
ATOM   2907 N N   . LYS B 1 157 ? 24.117  4.669   12.834  1.00 29.31 ? 169 LYS A N   1 
ATOM   2908 C CA  . LYS B 1 157 ? 24.657  5.189   11.582  1.00 30.69 ? 169 LYS A CA  1 
ATOM   2909 C C   . LYS B 1 157 ? 23.617  5.937   10.755  1.00 29.41 ? 169 LYS A C   1 
ATOM   2910 O O   . LYS B 1 157 ? 23.998  6.686   9.849   1.00 28.87 ? 169 LYS A O   1 
ATOM   2911 C CB  . LYS B 1 157 ? 25.277  4.057   10.758  1.00 31.50 ? 169 LYS A CB  1 
ATOM   2912 C CG  . LYS B 1 157 ? 26.787  3.910   10.987  1.00 37.45 ? 169 LYS A CG  1 
ATOM   2913 C CD  . LYS B 1 157 ? 27.528  3.485   9.728   1.00 45.02 ? 169 LYS A CD  1 
ATOM   2914 C CE  . LYS B 1 157 ? 27.405  4.551   8.632   1.00 50.07 ? 169 LYS A CE  1 
ATOM   2915 N NZ  . LYS B 1 157 ? 27.694  4.046   7.248   1.00 39.13 ? 169 LYS A NZ  1 
ATOM   2916 N N   . ALA B 1 158 ? 22.329  5.762   11.049  1.00 27.08 ? 170 ALA A N   1 
ATOM   2917 C CA  . ALA B 1 158 ? 21.278  6.410   10.280  1.00 24.80 ? 170 ALA A CA  1 
ATOM   2918 C C   . ALA B 1 158 ? 21.331  7.929   10.453  1.00 23.32 ? 170 ALA A C   1 
ATOM   2919 O O   . ALA B 1 158 ? 21.879  8.459   11.423  1.00 21.76 ? 170 ALA A O   1 
ATOM   2920 C CB  . ALA B 1 158 ? 19.903  5.881   10.695  1.00 22.11 ? 170 ALA A CB  1 
ATOM   2921 N N   . ALA B 1 159 ? 20.757  8.630   9.482   1.00 20.28 ? 171 ALA A N   1 
ATOM   2922 C CA  . ALA B 1 159 ? 20.717  10.082  9.521   1.00 18.08 ? 171 ALA A CA  1 
ATOM   2923 C C   . ALA B 1 159 ? 19.545  10.505  10.375  1.00 18.45 ? 171 ALA A C   1 
ATOM   2924 O O   . ALA B 1 159 ? 18.395  10.205  10.049  1.00 21.29 ? 171 ALA A O   1 
ATOM   2925 C CB  . ALA B 1 159 ? 20.584  10.671  8.120   1.00 19.20 ? 171 ALA A CB  1 
ATOM   2926 N N   . LYS B 1 160 ? 19.824  11.207  11.457  1.00 17.04 ? 172 LYS A N   1 
ATOM   2927 C CA  . LYS B 1 160 ? 18.759  11.685  12.314  1.00 21.01 ? 172 LYS A CA  1 
ATOM   2928 C C   . LYS B 1 160 ? 19.124  13.081  12.787  1.00 21.71 ? 172 LYS A C   1 
ATOM   2929 O O   . LYS B 1 160 ? 20.262  13.528  12.629  1.00 22.09 ? 172 LYS A O   1 
ATOM   2930 C CB  . LYS B 1 160 ? 18.518  10.732  13.490  1.00 20.35 ? 172 LYS A CB  1 
ATOM   2931 C CG  . LYS B 1 160 ? 19.726  10.543  14.380  1.00 20.03 ? 172 LYS A CG  1 
ATOM   2932 C CD  . LYS B 1 160 ? 19.604  9.293   15.218  1.00 20.91 ? 172 LYS A CD  1 
ATOM   2933 C CE  . LYS B 1 160 ? 19.612  8.039   14.382  1.00 19.69 ? 172 LYS A CE  1 
ATOM   2934 N NZ  . LYS B 1 160 ? 20.987  7.747   13.917  1.00 22.27 ? 172 LYS A NZ  1 
ATOM   2935 N N   . TRP B 1 161 ? 18.136  13.778  13.338  1.00 17.90 ? 173 TRP A N   1 
ATOM   2936 C CA  . TRP B 1 161 ? 18.331  15.160  13.741  1.00 21.73 ? 173 TRP A CA  1 
ATOM   2937 C C   . TRP B 1 161 ? 17.222  15.509  14.718  1.00 26.19 ? 173 TRP A C   1 
ATOM   2938 O O   . TRP B 1 161 ? 16.233  14.780  14.853  1.00 26.79 ? 173 TRP A O   1 
ATOM   2939 C CB  . TRP B 1 161 ? 18.338  16.133  12.538  1.00 23.41 ? 173 TRP A CB  1 
ATOM   2940 C CG  . TRP B 1 161 ? 17.097  16.045  11.693  1.00 21.80 ? 173 TRP A CG  1 
ATOM   2941 C CD1 . TRP B 1 161 ? 15.941  16.775  11.837  1.00 22.60 ? 173 TRP A CD1 1 
ATOM   2942 C CD2 . TRP B 1 161 ? 16.885  15.172  10.588  1.00 17.98 ? 173 TRP A CD2 1 
ATOM   2943 N NE1 . TRP B 1 161 ? 15.020  16.389  10.890  1.00 22.76 ? 173 TRP A NE1 1 
ATOM   2944 C CE2 . TRP B 1 161 ? 15.580  15.404  10.115  1.00 20.29 ? 173 TRP A CE2 1 
ATOM   2945 C CE3 . TRP B 1 161 ? 17.670  14.207  9.955   1.00 18.65 ? 173 TRP A CE3 1 
ATOM   2946 C CZ2 . TRP B 1 161 ? 15.048  14.704  9.043   1.00 21.20 ? 173 TRP A CZ2 1 
ATOM   2947 C CZ3 . TRP B 1 161 ? 17.141  13.522  8.892   1.00 19.33 ? 173 TRP A CZ3 1 
ATOM   2948 C CH2 . TRP B 1 161 ? 15.844  13.773  8.444   1.00 20.60 ? 173 TRP A CH2 1 
ATOM   2949 N N   . LYS B 1 162 ? 17.425  16.623  15.423  1.00 28.87 ? 174 LYS A N   1 
ATOM   2950 C CA  . LYS B 1 162 ? 16.436  17.239  16.297  1.00 26.77 ? 174 LYS A CA  1 
ATOM   2951 C C   . LYS B 1 162 ? 15.864  18.455  15.583  1.00 30.35 ? 174 LYS A C   1 
ATOM   2952 O O   . LYS B 1 162 ? 16.612  19.316  15.106  1.00 33.61 ? 174 LYS A O   1 
ATOM   2953 C CB  . LYS B 1 162 ? 17.056  17.656  17.634  1.00 28.19 ? 174 LYS A CB  1 
ATOM   2954 C CG  . LYS B 1 162 ? 16.029  18.075  18.663  1.00 31.71 ? 174 LYS A CG  1 
ATOM   2955 C CD  . LYS B 1 162 ? 16.591  18.106  20.076  1.00 37.54 ? 174 LYS A CD  1 
ATOM   2956 C CE  . LYS B 1 162 ? 16.824  19.532  20.595  1.00 36.05 ? 174 LYS A CE  1 
ATOM   2957 N NZ  . LYS B 1 162 ? 16.720  19.610  22.095  1.00 32.35 ? 174 LYS A NZ  1 
ATOM   2958 N N   . THR B 1 163 ? 14.545  18.525  15.504  1.00 34.20 ? 175 THR A N   1 
ATOM   2959 C CA  . THR B 1 163 ? 13.892  19.578  14.743  1.00 32.73 ? 175 THR A CA  1 
ATOM   2960 C C   . THR B 1 163 ? 13.894  20.896  15.530  1.00 35.04 ? 175 THR A C   1 
ATOM   2961 O O   . THR B 1 163 ? 14.435  20.999  16.637  1.00 35.99 ? 175 THR A O   1 
ATOM   2962 C CB  . THR B 1 163 ? 12.479  19.134  14.377  1.00 33.72 ? 175 THR A CB  1 
ATOM   2963 O OG1 . THR B 1 163 ? 11.723  18.914  15.579  1.00 37.84 ? 175 THR A OG1 1 
ATOM   2964 C CG2 . THR B 1 163 ? 12.534  17.829  13.582  1.00 32.78 ? 175 THR A CG2 1 
ATOM   2965 N N   . SER B 1 164 ? 13.276  21.922  14.946  1.00 34.35 ? 176 SER A N   1 
ATOM   2966 C CA  . SER B 1 164 ? 13.249  23.226  15.587  1.00 34.24 ? 176 SER A CA  1 
ATOM   2967 C C   . SER B 1 164 ? 12.350  23.240  16.822  1.00 40.87 ? 176 SER A C   1 
ATOM   2968 O O   . SER B 1 164 ? 12.577  24.041  17.737  1.00 41.85 ? 176 SER A O   1 
ATOM   2969 C CB  . SER B 1 164 ? 12.815  24.280  14.577  1.00 33.35 ? 176 SER A CB  1 
ATOM   2970 O OG  . SER B 1 164 ? 11.812  23.769  13.721  1.00 43.84 ? 176 SER A OG  1 
ATOM   2971 N N   . ASP B 1 165 ? 11.335  22.373  16.887  1.00 38.64 ? 177 ASP A N   1 
ATOM   2972 C CA  . ASP B 1 165 ? 10.534  22.276  18.102  1.00 41.23 ? 177 ASP A CA  1 
ATOM   2973 C C   . ASP B 1 165 ? 11.004  21.157  19.014  1.00 40.06 ? 177 ASP A C   1 
ATOM   2974 O O   . ASP B 1 165 ? 10.271  20.759  19.931  1.00 39.65 ? 177 ASP A O   1 
ATOM   2975 C CB  . ASP B 1 165 ? 9.044   22.097  17.784  1.00 43.19 ? 177 ASP A CB  1 
ATOM   2976 C CG  . ASP B 1 165 ? 8.785   21.043  16.733  1.00 43.81 ? 177 ASP A CG  1 
ATOM   2977 O OD1 . ASP B 1 165 ? 9.703   20.247  16.443  1.00 42.61 ? 177 ASP A OD1 1 
ATOM   2978 O OD2 . ASP B 1 165 ? 7.642   20.987  16.223  1.00 46.52 ? 177 ASP A OD2 1 
ATOM   2979 N N   . GLY B 1 166 ? 12.199  20.626  18.764  1.00 40.88 ? 178 GLY A N   1 
ATOM   2980 C CA  . GLY B 1 166 ? 12.832  19.700  19.682  1.00 40.35 ? 178 GLY A CA  1 
ATOM   2981 C C   . GLY B 1 166 ? 12.392  18.267  19.562  1.00 33.34 ? 178 GLY A C   1 
ATOM   2982 O O   . GLY B 1 166 ? 12.492  17.521  20.538  1.00 38.63 ? 178 GLY A O   1 
ATOM   2983 N N   . GLN B 1 167 ? 11.905  17.861  18.401  1.00 32.27 ? 179 GLN A N   1 
ATOM   2984 C CA  . GLN B 1 167 ? 11.441  16.507  18.173  1.00 32.93 ? 179 GLN A CA  1 
ATOM   2985 C C   . GLN B 1 167 ? 12.470  15.708  17.376  1.00 33.69 ? 179 GLN A C   1 
ATOM   2986 O O   . GLN B 1 167 ? 13.322  16.258  16.676  1.00 34.22 ? 179 GLN A O   1 
ATOM   2987 C CB  . GLN B 1 167 ? 10.089  16.534  17.446  1.00 34.66 ? 179 GLN A CB  1 
ATOM   2988 C CG  . GLN B 1 167 ? 8.898   17.065  18.249  1.00 35.33 ? 179 GLN A CG  1 
ATOM   2989 C CD  . GLN B 1 167 ? 8.938   16.714  19.748  1.00 49.04 ? 179 GLN A CD  1 
ATOM   2990 O OE1 . GLN B 1 167 ? 9.872   17.077  20.476  1.00 48.01 ? 179 GLN A OE1 1 
ATOM   2991 N NE2 . GLN B 1 167 ? 7.931   15.960  20.203  1.00 50.06 ? 179 GLN A NE2 1 
ATOM   2992 N N   . MET B 1 168 ? 12.392  14.390  17.486  1.00 32.58 ? 180 MET A N   1 
ATOM   2993 C CA  . MET B 1 168 ? 13.251  13.540  16.679  1.00 29.18 ? 180 MET A CA  1 
ATOM   2994 C C   . MET B 1 168 ? 12.654  13.336  15.282  1.00 26.50 ? 180 MET A C   1 
ATOM   2995 O O   . MET B 1 168 ? 11.431  13.348  15.093  1.00 26.75 ? 180 MET A O   1 
ATOM   2996 C CB  . MET B 1 168 ? 13.452  12.199  17.382  1.00 24.53 ? 180 MET A CB  1 
ATOM   2997 C CG  . MET B 1 168 ? 14.886  11.763  17.437  1.00 25.91 ? 180 MET A CG  1 
ATOM   2998 S SD  . MET B 1 168 ? 15.867  12.992  18.306  1.00 33.17 ? 180 MET A SD  1 
ATOM   2999 C CE  . MET B 1 168 ? 17.364  12.988  17.323  1.00 28.14 ? 180 MET A CE  1 
ATOM   3000 N N   . ASP B 1 169 ? 13.540  13.172  14.295  1.00 24.11 ? 181 ASP A N   1 
ATOM   3001 C CA  . ASP B 1 169 ? 13.180  12.834  12.918  1.00 22.64 ? 181 ASP A CA  1 
ATOM   3002 C C   . ASP B 1 169 ? 14.398  12.179  12.280  1.00 20.98 ? 181 ASP A C   1 
ATOM   3003 O O   . ASP B 1 169 ? 15.534  12.422  12.698  1.00 20.28 ? 181 ASP A O   1 
ATOM   3004 C CB  . ASP B 1 169 ? 12.754  14.078  12.112  1.00 23.23 ? 181 ASP A CB  1 
ATOM   3005 C CG  . ASP B 1 169 ? 11.879  13.738  10.893  1.00 24.63 ? 181 ASP A CG  1 
ATOM   3006 O OD1 . ASP B 1 169 ? 11.431  12.561  10.787  1.00 22.01 ? 181 ASP A OD1 1 
ATOM   3007 O OD2 . ASP B 1 169 ? 11.683  14.651  10.033  1.00 22.10 ? 181 ASP A OD2 1 
ATOM   3008 N N   . GLY B 1 170 ? 14.164  11.356  11.262  1.00 17.48 ? 182 GLY A N   1 
ATOM   3009 C CA  . GLY B 1 170 ? 15.316  10.796  10.582  1.00 16.02 ? 182 GLY A CA  1 
ATOM   3010 C C   . GLY B 1 170 ? 14.921  10.107  9.300   1.00 15.55 ? 182 GLY A C   1 
ATOM   3011 O O   . GLY B 1 170 ? 13.752  10.086  8.913   1.00 17.85 ? 182 GLY A O   1 
ATOM   3012 N N   . LEU B 1 171 ? 15.921  9.532   8.645   1.00 16.81 ? 183 LEU A N   1 
ATOM   3013 C CA  . LEU B 1 171 ? 15.749  8.885   7.354   1.00 19.82 ? 183 LEU A CA  1 
ATOM   3014 C C   . LEU B 1 171 ? 16.196  7.436   7.423   1.00 20.36 ? 183 LEU A C   1 
ATOM   3015 O O   . LEU B 1 171 ? 17.174  7.107   8.102   1.00 22.29 ? 183 LEU A O   1 
ATOM   3016 C CB  . LEU B 1 171 ? 16.556  9.585   6.259   1.00 19.18 ? 183 LEU A CB  1 
ATOM   3017 C CG  . LEU B 1 171 ? 16.401  11.086  6.178   1.00 16.47 ? 183 LEU A CG  1 
ATOM   3018 C CD1 . LEU B 1 171 ? 17.450  11.633  5.260   1.00 17.36 ? 183 LEU A CD1 1 
ATOM   3019 C CD2 . LEU B 1 171 ? 15.010  11.394  5.678   1.00 15.69 ? 183 LEU A CD2 1 
ATOM   3020 N N   . THR B 1 172 ? 15.495  6.572   6.693   1.00 17.62 ? 184 THR A N   1 
ATOM   3021 C CA  . THR B 1 172 ? 15.992  5.219   6.596   1.00 17.96 ? 184 THR A CA  1 
ATOM   3022 C C   . THR B 1 172 ? 17.247  5.203   5.754   1.00 21.23 ? 184 THR A C   1 
ATOM   3023 O O   . THR B 1 172 ? 17.609  6.185   5.102   1.00 21.50 ? 184 THR A O   1 
ATOM   3024 C CB  . THR B 1 172 ? 14.988  4.273   5.956   1.00 19.68 ? 184 THR A CB  1 
ATOM   3025 O OG1 . THR B 1 172 ? 14.557  4.829   4.716   1.00 25.94 ? 184 THR A OG1 1 
ATOM   3026 C CG2 . THR B 1 172 ? 13.807  4.053   6.846   1.00 17.67 ? 184 THR A CG2 1 
ATOM   3027 N N   . THR B 1 173 ? 17.863  4.023   5.722   1.00 26.46 ? 185 THR A N   1 
ATOM   3028 C CA  . THR B 1 173 ? 19.173  3.839   5.108   1.00 28.28 ? 185 THR A CA  1 
ATOM   3029 C C   . THR B 1 173 ? 19.179  4.263   3.648   1.00 29.87 ? 185 THR A C   1 
ATOM   3030 O O   . THR B 1 173 ? 19.923  5.170   3.250   1.00 27.56 ? 185 THR A O   1 
ATOM   3031 C CB  . THR B 1 173 ? 19.572  2.379   5.247   1.00 27.30 ? 185 THR A CB  1 
ATOM   3032 O OG1 . THR B 1 173 ? 19.348  1.978   6.607   1.00 27.93 ? 185 THR A OG1 1 
ATOM   3033 C CG2 . THR B 1 173 ? 21.032  2.187   4.848   1.00 25.85 ? 185 THR A CG2 1 
ATOM   3034 N N   . ASN B 1 174 ? 18.376  3.593   2.826   1.00 29.52 ? 186 ASN A N   1 
ATOM   3035 C CA  . ASN B 1 174 ? 18.265  3.957   1.424   1.00 25.33 ? 186 ASN A CA  1 
ATOM   3036 C C   . ASN B 1 174 ? 17.153  4.961   1.165   1.00 24.65 ? 186 ASN A C   1 
ATOM   3037 O O   . ASN B 1 174 ? 17.083  5.500   0.056   1.00 23.34 ? 186 ASN A O   1 
ATOM   3038 C CB  . ASN B 1 174 ? 18.062  2.695   0.607   1.00 27.16 ? 186 ASN A CB  1 
ATOM   3039 C CG  . ASN B 1 174 ? 19.166  1.700   0.836   1.00 33.85 ? 186 ASN A CG  1 
ATOM   3040 O OD1 . ASN B 1 174 ? 20.331  2.077   0.952   1.00 37.15 ? 186 ASN A OD1 1 
ATOM   3041 N ND2 . ASN B 1 174 ? 18.813  0.423   0.928   1.00 34.33 ? 186 ASN A ND2 1 
ATOM   3042 N N   . GLY B 1 175 ? 16.309  5.230   2.169   1.00 22.04 ? 187 GLY A N   1 
ATOM   3043 C CA  . GLY B 1 175 ? 15.314  6.280   2.100   1.00 22.50 ? 187 GLY A CA  1 
ATOM   3044 C C   . GLY B 1 175 ? 14.066  5.875   1.326   1.00 29.16 ? 187 GLY A C   1 
ATOM   3045 O O   . GLY B 1 175 ? 14.006  4.840   0.648   1.00 29.45 ? 187 GLY A O   1 
ATOM   3046 N N   . VAL B 1 176 ? 13.041  6.724   1.426   1.00 24.67 ? 188 VAL A N   1 
ATOM   3047 C CA  . VAL B 1 176 ? 11.835  6.600   0.616   1.00 22.87 ? 188 VAL A CA  1 
ATOM   3048 C C   . VAL B 1 176 ? 11.686  7.875   -0.201  1.00 23.40 ? 188 VAL A C   1 
ATOM   3049 O O   . VAL B 1 176 ? 11.745  8.983   0.349   1.00 21.64 ? 188 VAL A O   1 
ATOM   3050 C CB  . VAL B 1 176 ? 10.585  6.345   1.474   1.00 20.37 ? 188 VAL A CB  1 
ATOM   3051 C CG1 . VAL B 1 176 ? 9.335   6.226   0.580   1.00 16.97 ? 188 VAL A CG1 1 
ATOM   3052 C CG2 . VAL B 1 176 ? 10.789  5.117   2.316   1.00 19.18 ? 188 VAL A CG2 1 
ATOM   3053 N N   . LEU B 1 177 ? 11.480  7.712   -1.508  1.00 24.53 ? 189 LEU A N   1 
ATOM   3054 C CA  . LEU B 1 177 ? 11.478  8.796   -2.478  1.00 21.42 ? 189 LEU A CA  1 
ATOM   3055 C C   . LEU B 1 177 ? 10.104  8.899   -3.119  1.00 19.17 ? 189 LEU A C   1 
ATOM   3056 O O   . LEU B 1 177 ? 9.458   7.881   -3.389  1.00 17.73 ? 189 LEU A O   1 
ATOM   3057 C CB  . LEU B 1 177 ? 12.543  8.549   -3.542  1.00 23.67 ? 189 LEU A CB  1 
ATOM   3058 C CG  . LEU B 1 177 ? 13.892  9.254   -3.383  1.00 25.84 ? 189 LEU A CG  1 
ATOM   3059 C CD1 . LEU B 1 177 ? 14.523  8.976   -2.037  1.00 23.57 ? 189 LEU A CD1 1 
ATOM   3060 C CD2 . LEU B 1 177 ? 14.823  8.805   -4.496  1.00 27.82 ? 189 LEU A CD2 1 
ATOM   3061 N N   . VAL B 1 178 ? 9.653   10.127  -3.347  1.00 21.26 ? 190 VAL A N   1 
ATOM   3062 C CA  . VAL B 1 178 ? 8.298   10.388  -3.834  1.00 23.95 ? 190 VAL A CA  1 
ATOM   3063 C C   . VAL B 1 178 ? 8.338   11.492  -4.887  1.00 23.25 ? 190 VAL A C   1 
ATOM   3064 O O   . VAL B 1 178 ? 9.033   12.503  -4.730  1.00 22.01 ? 190 VAL A O   1 
ATOM   3065 C CB  . VAL B 1 178 ? 7.333   10.773  -2.684  1.00 21.60 ? 190 VAL A CB  1 
ATOM   3066 C CG1 . VAL B 1 178 ? 6.081   11.423  -3.220  1.00 19.44 ? 190 VAL A CG1 1 
ATOM   3067 C CG2 . VAL B 1 178 ? 6.959   9.556   -1.863  1.00 24.99 ? 190 VAL A CG2 1 
ATOM   3068 N N   . MET B 1 179 ? 7.585   11.301  -5.960  1.00 24.17 ? 191 MET A N   1 
ATOM   3069 C CA  . MET B 1 179 ? 7.416   12.318  -6.980  1.00 25.12 ? 191 MET A CA  1 
ATOM   3070 C C   . MET B 1 179 ? 5.947   12.669  -7.041  1.00 24.54 ? 191 MET A C   1 
ATOM   3071 O O   . MET B 1 179 ? 5.106   11.776  -7.145  1.00 24.35 ? 191 MET A O   1 
ATOM   3072 C CB  . MET B 1 179 ? 7.909   11.827  -8.334  1.00 26.64 ? 191 MET A CB  1 
ATOM   3073 C CG  . MET B 1 179 ? 8.489   12.911  -9.200  1.00 30.73 ? 191 MET A CG  1 
ATOM   3074 S SD  . MET B 1 179 ? 8.273   12.540  -10.940 1.00 34.78 ? 191 MET A SD  1 
ATOM   3075 C CE  . MET B 1 179 ? 9.815   11.693  -11.291 1.00 29.02 ? 191 MET A CE  1 
ATOM   3076 N N   . HIS B 1 180 ? 5.654   13.926  -6.954  1.00 28.75 ? 192 HIS A N   1 
ATOM   3077 C CA  . HIS B 1 180 ? 4.305   14.439  -7.065  1.00 30.59 ? 192 HIS A CA  1 
ATOM   3078 C C   . HIS B 1 180 ? 4.055   14.961  -8.472  1.00 36.50 ? 192 HIS A C   1 
ATOM   3079 O O   . HIS B 1 180 ? 4.993   15.376  -9.161  1.00 38.06 ? 192 HIS A O   1 
ATOM   3080 C CB  . HIS B 1 180 ? 4.080   15.565  -6.065  1.00 29.34 ? 192 HIS A CB  1 
ATOM   3081 C CG  . HIS B 1 180 ? 3.960   15.099  -4.657  1.00 29.72 ? 192 HIS A CG  1 
ATOM   3082 N ND1 . HIS B 1 180 ? 4.931   15.344  -3.709  1.00 32.66 ? 192 HIS A ND1 1 
ATOM   3083 C CD2 . HIS B 1 180 ? 2.980   14.413  -4.027  1.00 29.83 ? 192 HIS A CD2 1 
ATOM   3084 C CE1 . HIS B 1 180 ? 4.553   14.828  -2.553  1.00 26.66 ? 192 HIS A CE1 1 
ATOM   3085 N NE2 . HIS B 1 180 ? 3.370   14.263  -2.716  1.00 28.12 ? 192 HIS A NE2 1 
ATOM   3086 N N   . PRO B 1 181 ? 2.789   14.943  -8.917  1.00 40.48 ? 193 PRO A N   1 
ATOM   3087 C CA  . PRO B 1 181 ? 2.457   15.421  -10.272 1.00 45.96 ? 193 PRO A CA  1 
ATOM   3088 C C   . PRO B 1 181 ? 2.294   16.937  -10.362 1.00 49.60 ? 193 PRO A C   1 
ATOM   3089 O O   . PRO B 1 181 ? 2.425   17.532  -11.441 1.00 44.66 ? 193 PRO A O   1 
ATOM   3090 C CB  . PRO B 1 181 ? 1.139   14.697  -10.583 1.00 41.67 ? 193 PRO A CB  1 
ATOM   3091 C CG  . PRO B 1 181 ? 0.552   14.342  -9.258  1.00 38.47 ? 193 PRO A CG  1 
ATOM   3092 C CD  . PRO B 1 181 ? 1.618   14.404  -8.205  1.00 37.94 ? 193 PRO A CD  1 
ATOM   3093 N N   . ARG B 1 182 ? 1.990   17.556  -9.222  1.00 51.31 ? 194 ARG A N   1 
ATOM   3094 C CA  . ARG B 1 182 ? 1.816   18.996  -9.086  1.00 58.61 ? 194 ARG A CA  1 
ATOM   3095 C C   . ARG B 1 182 ? 2.532   19.443  -7.813  1.00 68.63 ? 194 ARG A C   1 
ATOM   3096 O O   . ARG B 1 182 ? 2.676   18.656  -6.871  1.00 69.27 ? 194 ARG A O   1 
ATOM   3097 C CB  . ARG B 1 182 ? 0.290   19.356  -9.039  1.00 55.36 ? 194 ARG A CB  1 
ATOM   3098 C CG  . ARG B 1 182 ? -0.625  18.145  -9.323  1.00 51.42 ? 194 ARG A CG  1 
ATOM   3099 C CD  . ARG B 1 182 ? -2.120  18.354  -9.040  1.00 50.48 ? 194 ARG A CD  1 
ATOM   3100 N NE  . ARG B 1 182 ? -2.454  18.660  -7.649  1.00 52.81 ? 194 ARG A NE  1 
ATOM   3101 C CZ  . ARG B 1 182 ? -3.515  18.181  -7.008  1.00 47.12 ? 194 ARG A CZ  1 
ATOM   3102 N NH1 . ARG B 1 182 ? -4.305  17.274  -7.561  1.00 43.51 ? 194 ARG A NH1 1 
ATOM   3103 N NH2 . ARG B 1 182 ? -3.782  18.613  -5.777  1.00 44.12 ? 194 ARG A NH2 1 
ATOM   3104 N N   . ASN B 1 183 ? 3.011   20.698  -7.793  1.00 80.11 ? 195 ASN A N   1 
ATOM   3105 C CA  . ASN B 1 183 ? 3.727   21.233  -6.625  1.00 78.38 ? 195 ASN A CA  1 
ATOM   3106 C C   . ASN B 1 183 ? 2.755   21.770  -5.564  1.00 78.97 ? 195 ASN A C   1 
ATOM   3107 O O   . ASN B 1 183 ? 1.898   21.023  -5.072  1.00 73.42 ? 195 ASN A O   1 
ATOM   3108 C CB  . ASN B 1 183 ? 4.740   22.319  -7.039  1.00 72.53 ? 195 ASN A CB  1 
ATOM   3109 C CG  . ASN B 1 183 ? 4.270   23.159  -8.231  1.00 82.84 ? 195 ASN A CG  1 
ATOM   3110 O OD1 . ASN B 1 183 ? 4.093   22.643  -9.348  1.00 77.14 ? 195 ASN A OD1 1 
ATOM   3111 N ND2 . ASN B 1 183 ? 4.074   24.459  -7.999  1.00 83.19 ? 195 ASN A ND2 1 
ATOM   3112 N N   . GLY B 1 184 ? 2.872   23.047  -5.189  1.00 77.26 ? 196 GLY A N   1 
ATOM   3113 C CA  . GLY B 1 184 ? 1.968   23.617  -4.202  1.00 62.04 ? 196 GLY A CA  1 
ATOM   3114 C C   . GLY B 1 184 ? 2.259   25.049  -3.809  1.00 61.14 ? 196 GLY A C   1 
ATOM   3115 O O   . GLY B 1 184 ? 1.341   25.861  -3.665  1.00 52.98 ? 196 GLY A O   1 
ATOM   3116 N N   . PRO B 1 191 ? 7.950   20.031  -14.251 1.00 76.87 ? 203 PRO A N   1 
ATOM   3117 C CA  . PRO B 1 191 ? 9.133   19.696  -13.442 1.00 75.61 ? 203 PRO A CA  1 
ATOM   3118 C C   . PRO B 1 191 ? 8.889   18.528  -12.478 1.00 64.53 ? 203 PRO A C   1 
ATOM   3119 O O   . PRO B 1 191 ? 8.470   18.743  -11.346 1.00 61.15 ? 203 PRO A O   1 
ATOM   3120 C CB  . PRO B 1 191 ? 9.415   20.996  -12.671 1.00 75.42 ? 203 PRO A CB  1 
ATOM   3121 C CG  . PRO B 1 191 ? 8.734   22.083  -13.481 1.00 84.87 ? 203 PRO A CG  1 
ATOM   3122 C CD  . PRO B 1 191 ? 7.513   21.425  -14.054 1.00 81.44 ? 203 PRO A CD  1 
ATOM   3123 N N   . GLY B 1 192 ? 9.151   17.308  -12.941 1.00 92.87 ? 204 GLY A N   1 
ATOM   3124 C CA  . GLY B 1 192 ? 8.994   16.116  -12.129 1.00 57.38 ? 204 GLY A CA  1 
ATOM   3125 C C   . GLY B 1 192 ? 10.256  15.771  -11.363 1.00 52.56 ? 204 GLY A C   1 
ATOM   3126 O O   . GLY B 1 192 ? 11.206  15.198  -11.923 1.00 49.42 ? 204 GLY A O   1 
ATOM   3127 N N   . ILE B 1 193 ? 10.260  16.117  -10.071 1.00 48.99 ? 205 ILE A N   1 
ATOM   3128 C CA  . ILE B 1 193 ? 11.460  16.141  -9.243  1.00 37.73 ? 205 ILE A CA  1 
ATOM   3129 C C   . ILE B 1 193 ? 11.247  15.258  -8.029  1.00 30.71 ? 205 ILE A C   1 
ATOM   3130 O O   . ILE B 1 193 ? 10.238  15.389  -7.327  1.00 28.40 ? 205 ILE A O   1 
ATOM   3131 C CB  . ILE B 1 193 ? 11.814  17.575  -8.817  1.00 36.71 ? 205 ILE A CB  1 
ATOM   3132 C CG1 . ILE B 1 193 ? 12.196  18.385  -10.049 1.00 49.32 ? 205 ILE A CG1 1 
ATOM   3133 C CG2 . ILE B 1 193 ? 12.946  17.575  -7.812  1.00 30.78 ? 205 ILE A CG2 1 
ATOM   3134 C CD1 . ILE B 1 193 ? 13.534  17.977  -10.658 1.00 43.87 ? 205 ILE A CD1 1 
ATOM   3135 N N   . TRP B 1 194 ? 12.206  14.377  -7.774  1.00 29.44 ? 206 TRP A N   1 
ATOM   3136 C CA  . TRP B 1 194 ? 12.105  13.446  -6.666  1.00 23.62 ? 206 TRP A CA  1 
ATOM   3137 C C   . TRP B 1 194 ? 12.461  14.139  -5.365  1.00 19.28 ? 206 TRP A C   1 
ATOM   3138 O O   . TRP B 1 194 ? 13.389  14.951  -5.304  1.00 18.32 ? 206 TRP A O   1 
ATOM   3139 C CB  . TRP B 1 194 ? 13.027  12.249  -6.882  1.00 24.15 ? 206 TRP A CB  1 
ATOM   3140 C CG  . TRP B 1 194 ? 12.592  11.319  -7.988  1.00 24.71 ? 206 TRP A CG  1 
ATOM   3141 C CD1 . TRP B 1 194 ? 13.078  11.279  -9.260  1.00 25.15 ? 206 TRP A CD1 1 
ATOM   3142 C CD2 . TRP B 1 194 ? 11.599  10.294  -7.907  1.00 21.32 ? 206 TRP A CD2 1 
ATOM   3143 N NE1 . TRP B 1 194 ? 12.453  10.290  -9.971  1.00 26.56 ? 206 TRP A NE1 1 
ATOM   3144 C CE2 . TRP B 1 194 ? 11.544  9.665   -9.155  1.00 24.09 ? 206 TRP A CE2 1 
ATOM   3145 C CE3 . TRP B 1 194 ? 10.753  9.846   -6.897  1.00 21.85 ? 206 TRP A CE3 1 
ATOM   3146 C CZ2 . TRP B 1 194 ? 10.674  8.604   -9.418  1.00 24.94 ? 206 TRP A CZ2 1 
ATOM   3147 C CZ3 . TRP B 1 194 ? 9.893   8.792   -7.162  1.00 21.89 ? 206 TRP A CZ3 1 
ATOM   3148 C CH2 . TRP B 1 194 ? 9.862   8.186   -8.406  1.00 23.20 ? 206 TRP A CH2 1 
ATOM   3149 N N   . ARG B 1 195 ? 11.694  13.828  -4.332  1.00 22.01 ? 207 ARG A N   1 
ATOM   3150 C CA  . ARG B 1 195 ? 11.921  14.304  -2.980  1.00 20.72 ? 207 ARG A CA  1 
ATOM   3151 C C   . ARG B 1 195 ? 12.032  13.105  -2.037  1.00 22.56 ? 207 ARG A C   1 
ATOM   3152 O O   . ARG B 1 195 ? 11.598  11.987  -2.358  1.00 22.65 ? 207 ARG A O   1 
ATOM   3153 C CB  . ARG B 1 195 ? 10.801  15.251  -2.541  1.00 16.27 ? 207 ARG A CB  1 
ATOM   3154 C CG  . ARG B 1 195 ? 11.240  16.666  -2.512  1.00 17.50 ? 207 ARG A CG  1 
ATOM   3155 C CD  . ARG B 1 195 ? 11.228  17.232  -3.874  1.00 19.70 ? 207 ARG A CD  1 
ATOM   3156 N NE  . ARG B 1 195 ? 11.300  18.689  -3.891  1.00 25.38 ? 207 ARG A NE  1 
ATOM   3157 C CZ  . ARG B 1 195 ? 12.398  19.376  -4.184  1.00 28.51 ? 207 ARG A CZ  1 
ATOM   3158 N NH1 . ARG B 1 195 ? 13.557  18.768  -4.389  1.00 30.86 ? 207 ARG A NH1 1 
ATOM   3159 N NH2 . ARG B 1 195 ? 12.332  20.703  -4.281  1.00 25.07 ? 207 ARG A NH2 1 
ATOM   3160 N N   . GLU B 1 196 ? 12.670  13.329  -0.886  1.00 21.79 ? 208 GLU A N   1 
ATOM   3161 C CA  . GLU B 1 196 ? 12.787  12.299  0.135   1.00 20.15 ? 208 GLU A CA  1 
ATOM   3162 C C   . GLU B 1 196 ? 11.787  12.524  1.260   1.00 19.74 ? 208 GLU A C   1 
ATOM   3163 O O   . GLU B 1 196 ? 11.487  13.662  1.636   1.00 15.07 ? 208 GLU A O   1 
ATOM   3164 C CB  . GLU B 1 196 ? 14.181  12.229  0.723   1.00 15.74 ? 208 GLU A CB  1 
ATOM   3165 C CG  . GLU B 1 196 ? 14.371  10.908  1.372   1.00 20.72 ? 208 GLU A CG  1 
ATOM   3166 C CD  . GLU B 1 196 ? 15.723  10.772  1.965   1.00 22.64 ? 208 GLU A CD  1 
ATOM   3167 O OE1 . GLU B 1 196 ? 16.557  11.645  1.646   1.00 26.01 ? 208 GLU A OE1 1 
ATOM   3168 O OE2 . GLU B 1 196 ? 15.946  9.783   2.704   1.00 19.49 ? 208 GLU A OE2 1 
ATOM   3169 N N   . ILE B 1 197 ? 11.281  11.421  1.794   1.00 19.06 ? 209 ILE A N   1 
ATOM   3170 C CA  . ILE B 1 197 ? 10.279  11.433  2.842   1.00 18.33 ? 209 ILE A CA  1 
ATOM   3171 C C   . ILE B 1 197 ? 10.902  10.837  4.094   1.00 21.41 ? 209 ILE A C   1 
ATOM   3172 O O   . ILE B 1 197 ? 11.562  9.785   4.037   1.00 20.79 ? 209 ILE A O   1 
ATOM   3173 C CB  . ILE B 1 197 ? 9.018   10.681  2.407   1.00 14.74 ? 209 ILE A CB  1 
ATOM   3174 C CG1 . ILE B 1 197 ? 8.477   11.341  1.146   1.00 18.04 ? 209 ILE A CG1 1 
ATOM   3175 C CG2 . ILE B 1 197 ? 8.002   10.724  3.503   1.00 18.78 ? 209 ILE A CG2 1 
ATOM   3176 C CD1 . ILE B 1 197 ? 8.225   12.829  1.308   1.00 15.74 ? 209 ILE A CD1 1 
ATOM   3177 N N   . SER B 1 198 ? 10.737  11.543  5.213   1.00 17.70 ? 210 SER A N   1 
ATOM   3178 C CA  . SER B 1 198 ? 11.358  11.138  6.458   1.00 19.11 ? 210 SER A CA  1 
ATOM   3179 C C   . SER B 1 198 ? 10.404  10.269  7.266   1.00 19.43 ? 210 SER A C   1 
ATOM   3180 O O   . SER B 1 198 ? 9.239   10.093  6.927   1.00 22.65 ? 210 SER A O   1 
ATOM   3181 C CB  . SER B 1 198 ? 11.781  12.356  7.264   1.00 18.01 ? 210 SER A CB  1 
ATOM   3182 O OG  . SER B 1 198 ? 10.661  12.927  7.889   1.00 19.34 ? 210 SER A OG  1 
ATOM   3183 N N   . VAL B 1 199 ? 10.921  9.708   8.355   1.00 19.77 ? 211 VAL A N   1 
ATOM   3184 C CA  . VAL B 1 199 ? 10.108  8.828   9.179   1.00 22.01 ? 211 VAL A CA  1 
ATOM   3185 C C   . VAL B 1 199 ? 8.949   9.597   9.811   1.00 24.05 ? 211 VAL A C   1 
ATOM   3186 O O   . VAL B 1 199 ? 7.926   9.005   10.167  1.00 28.55 ? 211 VAL A O   1 
ATOM   3187 C CB  . VAL B 1 199 ? 11.036  8.135   10.204  1.00 19.54 ? 211 VAL A CB  1 
ATOM   3188 C CG1 . VAL B 1 199 ? 10.267  7.434   11.329  1.00 16.20 ? 211 VAL A CG1 1 
ATOM   3189 C CG2 . VAL B 1 199 ? 11.949  7.181   9.476   1.00 16.68 ? 211 VAL A CG2 1 
ATOM   3190 N N   . CYS B 1 200 ? 9.044   10.915  9.894   1.00 20.23 ? 212 CYS A N   1 
ATOM   3191 C CA  . CYS B 1 200 ? 7.936   11.704  10.399  1.00 19.12 ? 212 CYS A CA  1 
ATOM   3192 C C   . CYS B 1 200 ? 7.116   12.388  9.305   1.00 21.31 ? 212 CYS A C   1 
ATOM   3193 O O   . CYS B 1 200 ? 6.295   13.247  9.618   1.00 25.58 ? 212 CYS A O   1 
ATOM   3194 C CB  . CYS B 1 200 ? 8.465   12.740  11.376  1.00 20.88 ? 212 CYS A CB  1 
ATOM   3195 S SG  . CYS B 1 200 ? 9.072   11.949  12.854  1.00 24.56 ? 212 CYS A SG  1 
ATOM   3196 N N   . GLY B 1 201 ? 7.322   12.054  8.039   1.00 19.08 ? 213 GLY A N   1 
ATOM   3197 C CA  . GLY B 1 201 ? 6.516   12.627  6.984   1.00 17.12 ? 213 GLY A CA  1 
ATOM   3198 C C   . GLY B 1 201 ? 6.972   13.966  6.451   1.00 18.55 ? 213 GLY A C   1 
ATOM   3199 O O   . GLY B 1 201 ? 6.199   14.626  5.742   1.00 18.27 ? 213 GLY A O   1 
ATOM   3200 N N   . ASN B 1 202 ? 8.189   14.399  6.762   1.00 18.23 ? 214 ASN A N   1 
ATOM   3201 C CA  . ASN B 1 202 ? 8.693   15.646  6.213   1.00 16.25 ? 214 ASN A CA  1 
ATOM   3202 C C   . ASN B 1 202 ? 9.399   15.387  4.895   1.00 16.75 ? 214 ASN A C   1 
ATOM   3203 O O   . ASN B 1 202 ? 9.778   14.255  4.577   1.00 16.66 ? 214 ASN A O   1 
ATOM   3204 C CB  . ASN B 1 202 ? 9.641   16.315  7.183   1.00 17.66 ? 214 ASN A CB  1 
ATOM   3205 C CG  . ASN B 1 202 ? 8.935   16.820  8.407   1.00 20.26 ? 214 ASN A CG  1 
ATOM   3206 O OD1 . ASN B 1 202 ? 8.240   17.843  8.358   1.00 17.66 ? 214 ASN A OD1 1 
ATOM   3207 N ND2 . ASN B 1 202 ? 9.085   16.099  9.520   1.00 21.63 ? 214 ASN A ND2 1 
ATOM   3208 N N   . VAL B 1 203 ? 9.581   16.459  4.129   1.00 14.04 ? 215 VAL A N   1 
ATOM   3209 C CA  . VAL B 1 203 ? 9.996   16.372  2.738   1.00 17.12 ? 215 VAL A CA  1 
ATOM   3210 C C   . VAL B 1 203 ? 11.354  17.043  2.595   1.00 19.80 ? 215 VAL A C   1 
ATOM   3211 O O   . VAL B 1 203 ? 11.529  18.195  3.007   1.00 22.35 ? 215 VAL A O   1 
ATOM   3212 C CB  . VAL B 1 203 ? 8.949   17.015  1.805   1.00 18.57 ? 215 VAL A CB  1 
ATOM   3213 C CG1 . VAL B 1 203 ? 9.395   16.953  0.367   1.00 18.79 ? 215 VAL A CG1 1 
ATOM   3214 C CG2 . VAL B 1 203 ? 7.632   16.314  1.934   1.00 17.05 ? 215 VAL A CG2 1 
ATOM   3215 N N   . PHE B 1 204 ? 12.311  16.328  2.011   1.00 17.91 ? 216 PHE A N   1 
ATOM   3216 C CA  . PHE B 1 204 ? 13.652  16.851  1.812   1.00 19.69 ? 216 PHE A CA  1 
ATOM   3217 C C   . PHE B 1 204 ? 14.106  16.643  0.377   1.00 19.75 ? 216 PHE A C   1 
ATOM   3218 O O   . PHE B 1 204 ? 13.655  15.730  -0.317  1.00 19.09 ? 216 PHE A O   1 
ATOM   3219 C CB  . PHE B 1 204 ? 14.648  16.189  2.764   1.00 20.29 ? 216 PHE A CB  1 
ATOM   3220 C CG  . PHE B 1 204 ? 14.313  16.401  4.194   1.00 20.03 ? 216 PHE A CG  1 
ATOM   3221 C CD1 . PHE B 1 204 ? 13.289  15.687  4.785   1.00 21.10 ? 216 PHE A CD1 1 
ATOM   3222 C CD2 . PHE B 1 204 ? 15.005  17.321  4.953   1.00 25.04 ? 216 PHE A CD2 1 
ATOM   3223 C CE1 . PHE B 1 204 ? 12.955  15.890  6.093   1.00 20.12 ? 216 PHE A CE1 1 
ATOM   3224 C CE2 . PHE B 1 204 ? 14.681  17.523  6.267   1.00 23.46 ? 216 PHE A CE2 1 
ATOM   3225 C CZ  . PHE B 1 204 ? 13.648  16.806  6.833   1.00 23.15 ? 216 PHE A CZ  1 
ATOM   3226 N N   . SER B 1 205 ? 15.016  17.502  -0.058  1.00 24.08 ? 217 SER A N   1 
ATOM   3227 C CA  . SER B 1 205 ? 15.701  17.272  -1.318  1.00 25.37 ? 217 SER A CA  1 
ATOM   3228 C C   . SER B 1 205 ? 16.559  16.011  -1.227  1.00 22.76 ? 217 SER A C   1 
ATOM   3229 O O   . SER B 1 205 ? 16.823  15.467  -0.150  1.00 23.63 ? 217 SER A O   1 
ATOM   3230 C CB  . SER B 1 205 ? 16.551  18.486  -1.698  1.00 23.88 ? 217 SER A CB  1 
ATOM   3231 O OG  . SER B 1 205 ? 17.660  18.625  -0.828  1.00 25.62 ? 217 SER A OG  1 
ATOM   3232 N N   . LEU B 1 206 ? 16.978  15.537  -2.384  1.00 20.98 ? 218 LEU A N   1 
ATOM   3233 C CA  . LEU B 1 206 ? 17.662  14.264  -2.450  1.00 23.14 ? 218 LEU A CA  1 
ATOM   3234 C C   . LEU B 1 206 ? 19.020  14.356  -1.767  1.00 24.91 ? 218 LEU A C   1 
ATOM   3235 O O   . LEU B 1 206 ? 19.604  15.435  -1.642  1.00 22.55 ? 218 LEU A O   1 
ATOM   3236 C CB  . LEU B 1 206 ? 17.810  13.841  -3.914  1.00 24.14 ? 218 LEU A CB  1 
ATOM   3237 C CG  . LEU B 1 206 ? 16.518  13.356  -4.556  1.00 18.92 ? 218 LEU A CG  1 
ATOM   3238 C CD1 . LEU B 1 206 ? 16.784  12.729  -5.882  1.00 22.96 ? 218 LEU A CD1 1 
ATOM   3239 C CD2 . LEU B 1 206 ? 15.933  12.319  -3.657  1.00 23.87 ? 218 LEU A CD2 1 
ATOM   3240 N N   . ARG B 1 207 ? 19.515  13.207  -1.308  1.00 28.26 ? 219 ARG A N   1 
ATOM   3241 C CA  . ARG B 1 207 ? 20.879  13.143  -0.806  1.00 27.60 ? 219 ARG A CA  1 
ATOM   3242 C C   . ARG B 1 207 ? 21.884  13.229  -1.951  1.00 30.93 ? 219 ARG A C   1 
ATOM   3243 O O   . ARG B 1 207 ? 21.529  13.223  -3.134  1.00 30.84 ? 219 ARG A O   1 
ATOM   3244 C CB  . ARG B 1 207 ? 21.100  11.868  -0.008  1.00 25.23 ? 219 ARG A CB  1 
ATOM   3245 C CG  . ARG B 1 207 ? 20.411  11.891  1.325   1.00 25.27 ? 219 ARG A CG  1 
ATOM   3246 C CD  . ARG B 1 207 ? 20.577  10.575  2.013   1.00 24.00 ? 219 ARG A CD  1 
ATOM   3247 N NE  . ARG B 1 207 ? 19.300  9.913   2.233   1.00 22.73 ? 219 ARG A NE  1 
ATOM   3248 C CZ  . ARG B 1 207 ? 19.173  8.745   2.839   1.00 22.21 ? 219 ARG A CZ  1 
ATOM   3249 N NH1 . ARG B 1 207 ? 20.230  8.032   3.169   1.00 25.75 ? 219 ARG A NH1 1 
ATOM   3250 N NH2 . ARG B 1 207 ? 17.956  8.296   3.143   1.00 22.19 ? 219 ARG A NH2 1 
ATOM   3251 N N   . GLU B 1 208 ? 23.169  13.327  -1.581  1.00 38.40 ? 220 GLU A N   1 
ATOM   3252 C CA  . GLU B 1 208 ? 24.233  13.348  -2.588  1.00 37.22 ? 220 GLU A CA  1 
ATOM   3253 C C   . GLU B 1 208 ? 24.492  11.963  -3.171  1.00 35.91 ? 220 GLU A C   1 
ATOM   3254 O O   . GLU B 1 208 ? 24.909  11.847  -4.330  1.00 36.34 ? 220 GLU A O   1 
ATOM   3255 C CB  . GLU B 1 208 ? 25.520  13.919  -1.994  1.00 34.22 ? 220 GLU A CB  1 
ATOM   3256 C CG  . GLU B 1 208 ? 25.551  15.448  -1.904  1.00 41.73 ? 220 GLU A CG  1 
ATOM   3257 C CD  . GLU B 1 208 ? 25.110  16.150  -3.193  1.00 40.71 ? 220 GLU A CD  1 
ATOM   3258 O OE1 . GLU B 1 208 ? 25.893  16.172  -4.186  1.00 36.96 ? 220 GLU A OE1 1 
ATOM   3259 O OE2 . GLU B 1 208 ? 23.973  16.676  -3.195  1.00 35.54 ? 220 GLU A OE2 1 
ATOM   3260 N N   . THR B 1 209 ? 24.273  10.919  -2.379  1.00 34.03 ? 221 THR A N   1 
ATOM   3261 C CA  . THR B 1 209 ? 24.228  9.553   -2.856  1.00 34.45 ? 221 THR A CA  1 
ATOM   3262 C C   . THR B 1 209 ? 23.123  8.848   -2.096  1.00 34.99 ? 221 THR A C   1 
ATOM   3263 O O   . THR B 1 209 ? 22.755  9.260   -0.995  1.00 32.43 ? 221 THR A O   1 
ATOM   3264 C CB  . THR B 1 209 ? 25.557  8.831   -2.652  1.00 38.84 ? 221 THR A CB  1 
ATOM   3265 O OG1 . THR B 1 209 ? 26.156  9.276   -1.425  1.00 36.93 ? 221 THR A OG1 1 
ATOM   3266 C CG2 . THR B 1 209 ? 26.486  9.107   -3.816  1.00 37.49 ? 221 THR A CG2 1 
ATOM   3267 N N   . ARG B 1 210 ? 22.612  7.766   -2.695  1.00 37.80 ? 222 ARG A N   1 
ATOM   3268 C CA  . ARG B 1 210 ? 21.403  7.111   -2.192  1.00 37.08 ? 222 ARG A CA  1 
ATOM   3269 C C   . ARG B 1 210 ? 21.482  6.762   -0.704  1.00 33.66 ? 222 ARG A C   1 
ATOM   3270 O O   . ARG B 1 210 ? 20.514  6.988   0.034   1.00 28.28 ? 222 ARG A O   1 
ATOM   3271 C CB  . ARG B 1 210 ? 21.105  5.859   -3.019  1.00 38.26 ? 222 ARG A CB  1 
ATOM   3272 C CG  . ARG B 1 210 ? 19.828  5.141   -2.590  1.00 35.24 ? 222 ARG A CG  1 
ATOM   3273 C CD  . ARG B 1 210 ? 18.613  5.621   -3.379  1.00 36.71 ? 222 ARG A CD  1 
ATOM   3274 N NE  . ARG B 1 210 ? 17.364  5.448   -2.644  1.00 29.54 ? 222 ARG A NE  1 
ATOM   3275 C CZ  . ARG B 1 210 ? 16.185  5.282   -3.225  1.00 29.21 ? 222 ARG A CZ  1 
ATOM   3276 N NH1 . ARG B 1 210 ? 16.060  5.316   -4.540  1.00 32.98 ? 222 ARG A NH1 1 
ATOM   3277 N NH2 . ARG B 1 210 ? 15.109  5.058   -2.470  1.00 23.25 ? 222 ARG A NH2 1 
ATOM   3278 N N   . SER B 1 211 ? 22.623  6.220   -0.246  1.00 38.68 ? 223 SER A N   1 
ATOM   3279 C CA  . SER B 1 211 ? 22.826  5.778   1.141   1.00 36.85 ? 223 SER A CA  1 
ATOM   3280 C C   . SER B 1 211 ? 23.611  6.770   2.004   1.00 37.46 ? 223 SER A C   1 
ATOM   3281 O O   . SER B 1 211 ? 24.020  6.406   3.113   1.00 37.36 ? 223 SER A O   1 
ATOM   3282 C CB  . SER B 1 211 ? 23.539  4.417   1.187   1.00 37.60 ? 223 SER A CB  1 
ATOM   3283 O OG  . SER B 1 211 ? 22.836  3.409   0.474   1.00 41.71 ? 223 SER A OG  1 
ATOM   3284 N N   . ALA B 1 212 ? 23.819  8.006   1.537   1.00 34.09 ? 224 ALA A N   1 
ATOM   3285 C CA  . ALA B 1 212 ? 24.644  8.970   2.263   1.00 32.19 ? 224 ALA A CA  1 
ATOM   3286 C C   . ALA B 1 212 ? 24.103  9.237   3.670   1.00 32.73 ? 224 ALA A C   1 
ATOM   3287 O O   . ALA B 1 212 ? 22.892  9.281   3.894   1.00 31.70 ? 224 ALA A O   1 
ATOM   3288 C CB  . ALA B 1 212 ? 24.741  10.274  1.467   1.00 30.66 ? 224 ALA A CB  1 
ATOM   3289 N N   . GLN B 1 213 ? 24.977  9.451   4.653   1.00 32.85 ? 225 GLN A N   1 
ATOM   3290 C CA  . GLN B 1 213 ? 24.527  9.611   6.063   1.00 29.73 ? 225 GLN A CA  1 
ATOM   3291 C C   . GLN B 1 213 ? 24.199  11.074  6.334   1.00 32.98 ? 225 GLN A C   1 
ATOM   3292 O O   . GLN B 1 213 ? 24.162  11.457  7.505   1.00 38.31 ? 225 GLN A O   1 
ATOM   3293 C CB  . GLN B 1 213 ? 25.620  9.097   6.992   1.00 30.00 ? 225 GLN A CB  1 
ATOM   3294 C CG  . GLN B 1 213 ? 25.763  7.579   7.002   1.00 30.00 ? 225 GLN A CG  1 
ATOM   3295 C CD  . GLN B 1 213 ? 26.788  7.057   6.019   1.00 30.00 ? 225 GLN A CD  1 
ATOM   3296 O OE1 . GLN B 1 213 ? 28.001  7.186   6.219   1.00 30.00 ? 225 GLN A OE1 1 
ATOM   3297 N NE2 . GLN B 1 213 ? 26.307  6.447   4.946   1.00 30.00 ? 225 GLN A NE2 1 
ATOM   3298 N N   . GLN B 1 214 ? 23.952  11.840  5.287   1.00 40.17 ? 226 GLN A N   1 
ATOM   3299 C CA  . GLN B 1 214 ? 23.668  13.269  5.364   1.00 39.19 ? 226 GLN A CA  1 
ATOM   3300 C C   . GLN B 1 214 ? 22.365  13.562  4.623   1.00 37.03 ? 226 GLN A C   1 
ATOM   3301 O O   . GLN B 1 214 ? 22.186  13.128  3.482   1.00 37.71 ? 226 GLN A O   1 
ATOM   3302 C CB  . GLN B 1 214 ? 24.855  14.053  4.763   1.00 36.68 ? 226 GLN A CB  1 
ATOM   3303 C CG  . GLN B 1 214 ? 24.511  15.338  3.983   1.00 46.15 ? 226 GLN A CG  1 
ATOM   3304 C CD  . GLN B 1 214 ? 24.122  15.097  2.498   1.00 52.71 ? 226 GLN A CD  1 
ATOM   3305 O OE1 . GLN B 1 214 ? 24.628  14.182  1.825   1.00 49.57 ? 226 GLN A OE1 1 
ATOM   3306 N NE2 . GLN B 1 214 ? 23.216  15.932  1.994   1.00 47.07 ? 226 GLN A NE2 1 
ATOM   3307 N N   . ARG B 1 215 ? 21.458  14.284  5.266   1.00 32.22 ? 227 ARG A N   1 
ATOM   3308 C CA  . ARG B 1 215 ? 20.165  14.576  4.672   1.00 29.07 ? 227 ARG A CA  1 
ATOM   3309 C C   . ARG B 1 215 ? 20.248  15.768  3.717   1.00 34.99 ? 227 ARG A C   1 
ATOM   3310 O O   . ARG B 1 215 ? 21.093  16.656  3.865   1.00 39.21 ? 227 ARG A O   1 
ATOM   3311 C CB  . ARG B 1 215 ? 19.150  14.871  5.770   1.00 25.74 ? 227 ARG A CB  1 
ATOM   3312 C CG  . ARG B 1 215 ? 19.380  16.209  6.425   1.00 26.23 ? 227 ARG A CG  1 
ATOM   3313 C CD  . ARG B 1 215 ? 18.175  16.683  7.210   1.00 28.55 ? 227 ARG A CD  1 
ATOM   3314 N NE  . ARG B 1 215 ? 18.556  17.712  8.174   1.00 35.95 ? 227 ARG A NE  1 
ATOM   3315 C CZ  . ARG B 1 215 ? 18.864  18.963  7.853   1.00 36.25 ? 227 ARG A CZ  1 
ATOM   3316 N NH1 . ARG B 1 215 ? 18.790  19.395  6.603   1.00 34.54 ? 227 ARG A NH1 1 
ATOM   3317 N NH2 . ARG B 1 215 ? 19.249  19.803  8.811   1.00 33.66 ? 227 ARG A NH2 1 
ATOM   3318 N N   . GLY B 1 216 ? 19.353  15.777  2.728   1.00 27.58 ? 228 GLY A N   1 
ATOM   3319 C CA  . GLY B 1 216 ? 19.132  16.934  1.888   1.00 20.90 ? 228 GLY A CA  1 
ATOM   3320 C C   . GLY B 1 216 ? 18.523  18.089  2.667   1.00 24.53 ? 228 GLY A C   1 
ATOM   3321 O O   . GLY B 1 216 ? 18.293  18.040  3.879   1.00 25.44 ? 228 GLY A O   1 
ATOM   3322 N N   . LYS B 1 217 ? 18.279  19.169  1.934   1.00 25.47 ? 229 LYS A N   1 
ATOM   3323 C CA  . LYS B 1 217 ? 17.751  20.391  2.520   1.00 21.96 ? 229 LYS A CA  1 
ATOM   3324 C C   . LYS B 1 217 ? 16.236  20.289  2.650   1.00 23.38 ? 229 LYS A C   1 
ATOM   3325 O O   . LYS B 1 217 ? 15.556  19.809  1.743   1.00 25.78 ? 229 LYS A O   1 
ATOM   3326 C CB  . LYS B 1 217 ? 18.161  21.582  1.656   1.00 16.87 ? 229 LYS A CB  1 
ATOM   3327 C CG  . LYS B 1 217 ? 17.851  22.930  2.257   1.00 22.46 ? 229 LYS A CG  1 
ATOM   3328 C CD  . LYS B 1 217 ? 18.594  24.072  1.547   1.00 26.31 ? 229 LYS A CD  1 
ATOM   3329 C CE  . LYS B 1 217 ? 17.939  25.443  1.815   1.00 28.75 ? 229 LYS A CE  1 
ATOM   3330 N NZ  . LYS B 1 217 ? 16.860  25.437  2.880   1.00 36.97 ? 229 LYS A NZ  1 
ATOM   3331 N N   . MET B 1 218 ? 15.702  20.712  3.792   1.00 25.65 ? 230 MET A N   1 
ATOM   3332 C CA  . MET B 1 218 ? 14.254  20.647  3.961   1.00 23.97 ? 230 MET A CA  1 
ATOM   3333 C C   . MET B 1 218 ? 13.538  21.430  2.881   1.00 28.05 ? 230 MET A C   1 
ATOM   3334 O O   . MET B 1 218 ? 13.851  22.595  2.625   1.00 31.11 ? 230 MET A O   1 
ATOM   3335 C CB  . MET B 1 218 ? 13.818  21.193  5.309   1.00 27.77 ? 230 MET A CB  1 
ATOM   3336 C CG  . MET B 1 218 ? 12.394  20.767  5.610   1.00 33.15 ? 230 MET A CG  1 
ATOM   3337 S SD  . MET B 1 218 ? 11.697  21.404  7.136   1.00 50.04 ? 230 MET A SD  1 
ATOM   3338 C CE  . MET B 1 218 ? 10.602  22.674  6.461   1.00 43.81 ? 230 MET A CE  1 
ATOM   3339 N N   . VAL B 1 219 ? 12.553  20.795  2.273   1.00 28.49 ? 231 VAL A N   1 
ATOM   3340 C CA  . VAL B 1 219 ? 11.650  21.458  1.347   1.00 30.80 ? 231 VAL A CA  1 
ATOM   3341 C C   . VAL B 1 219 ? 10.385  21.793  2.110   1.00 35.03 ? 231 VAL A C   1 
ATOM   3342 O O   . VAL B 1 219 ? 9.768   20.915  2.716   1.00 36.52 ? 231 VAL A O   1 
ATOM   3343 C CB  . VAL B 1 219 ? 11.350  20.583  0.123   1.00 29.72 ? 231 VAL A CB  1 
ATOM   3344 C CG1 . VAL B 1 219 ? 10.589  21.373  -0.909  1.00 30.47 ? 231 VAL A CG1 1 
ATOM   3345 C CG2 . VAL B 1 219 ? 12.659  20.027  -0.470  1.00 26.55 ? 231 VAL A CG2 1 
ATOM   3346 N N   . GLU B 1 220 ? 9.996   23.061  2.067   1.00 46.78 ? 232 GLU A N   1 
ATOM   3347 C CA  . GLU B 1 220 ? 9.006   23.669  2.954   1.00 51.98 ? 232 GLU A CA  1 
ATOM   3348 C C   . GLU B 1 220 ? 7.573   23.557  2.429   1.00 48.02 ? 232 GLU A C   1 
ATOM   3349 O O   . GLU B 1 220 ? 6.684   23.110  3.162   1.00 48.35 ? 232 GLU A O   1 
ATOM   3350 C CB  . GLU B 1 220 ? 9.383   25.145  3.197   1.00 59.77 ? 232 GLU A CB  1 
ATOM   3351 C CG  . GLU B 1 220 ? 10.928  25.419  3.326   1.00 67.06 ? 232 GLU A CG  1 
ATOM   3352 C CD  . GLU B 1 220 ? 11.714  25.488  1.975   1.00 55.61 ? 232 GLU A CD  1 
ATOM   3353 O OE1 . GLU B 1 220 ? 11.191  24.994  0.939   1.00 50.34 ? 232 GLU A OE1 1 
ATOM   3354 O OE2 . GLU B 1 220 ? 12.873  25.997  1.966   1.00 44.22 ? 232 GLU A OE2 1 
ATOM   3355 N N   . ILE B 1 221 ? 7.332   23.939  1.168   1.00 46.55 ? 233 ILE A N   1 
ATOM   3356 C CA  . ILE B 1 221 ? 5.956   23.998  0.673   1.00 46.38 ? 233 ILE A CA  1 
ATOM   3357 C C   . ILE B 1 221 ? 5.371   22.602  0.454   1.00 44.23 ? 233 ILE A C   1 
ATOM   3358 O O   . ILE B 1 221 ? 4.210   22.353  0.808   1.00 44.39 ? 233 ILE A O   1 
ATOM   3359 C CB  . ILE B 1 221 ? 5.865   24.854  -0.602  1.00 49.99 ? 233 ILE A CB  1 
ATOM   3360 C CG1 . ILE B 1 221 ? 6.612   24.209  -1.775  1.00 47.99 ? 233 ILE A CG1 1 
ATOM   3361 C CG2 . ILE B 1 221 ? 6.395   26.245  -0.314  1.00 56.03 ? 233 ILE A CG2 1 
ATOM   3362 C CD1 . ILE B 1 221 ? 6.152   24.697  -3.150  1.00 49.60 ? 233 ILE A CD1 1 
ATOM   3363 N N   . GLU B 1 222 ? 6.142   21.677  -0.130  1.00 38.62 ? 234 GLU A N   1 
ATOM   3364 C CA  . GLU B 1 222 ? 5.606   20.356  -0.451  1.00 32.94 ? 234 GLU A CA  1 
ATOM   3365 C C   . GLU B 1 222 ? 5.302   19.549  0.812   1.00 26.21 ? 234 GLU A C   1 
ATOM   3366 O O   . GLU B 1 222 ? 5.829   19.810  1.895   1.00 30.72 ? 234 GLU A O   1 
ATOM   3367 C CB  . GLU B 1 222 ? 6.577   19.579  -1.335  1.00 30.42 ? 234 GLU A CB  1 
ATOM   3368 C CG  . GLU B 1 222 ? 7.445   20.443  -2.219  1.00 37.67 ? 234 GLU A CG  1 
ATOM   3369 C CD  . GLU B 1 222 ? 8.187   19.639  -3.301  1.00 43.03 ? 234 GLU A CD  1 
ATOM   3370 O OE1 . GLU B 1 222 ? 7.731   18.505  -3.638  1.00 37.75 ? 234 GLU A OE1 1 
ATOM   3371 O OE2 . GLU B 1 222 ? 9.199   20.175  -3.842  1.00 36.52 ? 234 GLU A OE2 1 
ATOM   3372 N N   . THR B 1 223 ? 4.430   18.555  0.660   1.00 21.63 ? 235 THR A N   1 
ATOM   3373 C CA  . THR B 1 223 ? 4.051   17.685  1.760   1.00 20.97 ? 235 THR A CA  1 
ATOM   3374 C C   . THR B 1 223 ? 4.159   16.229  1.333   1.00 20.10 ? 235 THR A C   1 
ATOM   3375 O O   . THR B 1 223 ? 4.416   15.913  0.171   1.00 20.04 ? 235 THR A O   1 
ATOM   3376 C CB  . THR B 1 223 ? 2.622   17.944  2.247   1.00 20.22 ? 235 THR A CB  1 
ATOM   3377 O OG1 . THR B 1 223 ? 1.697   17.388  1.310   1.00 19.04 ? 235 THR A OG1 1 
ATOM   3378 C CG2 . THR B 1 223 ? 2.357   19.419  2.408   1.00 21.24 ? 235 THR A CG2 1 
ATOM   3379 N N   . ASN B 1 224 ? 3.953   15.341  2.306   1.00 19.36 ? 236 ASN A N   1 
ATOM   3380 C CA  . ASN B 1 224 ? 3.956   13.901  2.107   1.00 17.56 ? 236 ASN A CA  1 
ATOM   3381 C C   . ASN B 1 224 ? 2.577   13.353  1.788   1.00 18.09 ? 236 ASN A C   1 
ATOM   3382 O O   . ASN B 1 224 ? 2.367   12.136  1.892   1.00 18.74 ? 236 ASN A O   1 
ATOM   3383 C CB  . ASN B 1 224 ? 4.513   13.198  3.344   1.00 16.90 ? 236 ASN A CB  1 
ATOM   3384 C CG  . ASN B 1 224 ? 3.582   13.288  4.536   1.00 17.80 ? 236 ASN A CG  1 
ATOM   3385 O OD1 . ASN B 1 224 ? 2.895   14.304  4.745   1.00 16.28 ? 236 ASN A OD1 1 
ATOM   3386 N ND2 . ASN B 1 224 ? 3.573   12.234  5.342   1.00 15.93 ? 236 ASN A ND2 1 
ATOM   3387 N N   . GLN B 1 225 ? 1.630   14.223  1.442   1.00 17.20 ? 237 GLN A N   1 
ATOM   3388 C CA  . GLN B 1 225 ? 0.356   13.778  0.900   1.00 19.40 ? 237 GLN A CA  1 
ATOM   3389 C C   . GLN B 1 225 ? 0.560   13.159  -0.464  1.00 22.35 ? 237 GLN A C   1 
ATOM   3390 O O   . GLN B 1 225 ? 1.223   13.746  -1.322  1.00 26.20 ? 237 GLN A O   1 
ATOM   3391 C CB  . GLN B 1 225 ? -0.611  14.940  0.760   1.00 23.66 ? 237 GLN A CB  1 
ATOM   3392 C CG  . GLN B 1 225 ? -0.865  15.692  2.023   1.00 30.26 ? 237 GLN A CG  1 
ATOM   3393 C CD  . GLN B 1 225 ? -1.800  16.849  1.798   1.00 32.10 ? 237 GLN A CD  1 
ATOM   3394 O OE1 . GLN B 1 225 ? -2.833  16.721  1.121   1.00 32.63 ? 237 GLN A OE1 1 
ATOM   3395 N NE2 . GLN B 1 225 ? -1.435  18.001  2.349   1.00 38.08 ? 237 GLN A NE2 1 
ATOM   3396 N N   . LEU B 1 226 ? -0.055  12.000  -0.678  1.00 20.73 ? 238 LEU A N   1 
ATOM   3397 C CA  . LEU B 1 226 ? 0.013   11.295  -1.955  1.00 24.28 ? 238 LEU A CA  1 
ATOM   3398 C C   . LEU B 1 226 ? -1.118  11.801  -2.846  1.00 26.86 ? 238 LEU A C   1 
ATOM   3399 O O   . LEU B 1 226 ? -2.282  11.436  -2.660  1.00 27.37 ? 238 LEU A O   1 
ATOM   3400 C CB  . LEU B 1 226 ? -0.070  9.786   -1.746  1.00 23.10 ? 238 LEU A CB  1 
ATOM   3401 C CG  . LEU B 1 226 ? 1.101   9.091   -1.058  1.00 19.79 ? 238 LEU A CG  1 
ATOM   3402 C CD1 . LEU B 1 226 ? 0.709   7.704   -0.615  1.00 16.90 ? 238 LEU A CD1 1 
ATOM   3403 C CD2 . LEU B 1 226 ? 2.270   9.023   -2.016  1.00 22.43 ? 238 LEU A CD2 1 
ATOM   3404 N N   . GLN B 1 227 ? -0.779  12.652  -3.815  1.00 27.40 ? 239 GLN A N   1 
ATOM   3405 C CA  . GLN B 1 227 ? -1.739  13.039  -4.835  1.00 25.80 ? 239 GLN A CA  1 
ATOM   3406 C C   . GLN B 1 227 ? -1.940  11.905  -5.826  1.00 26.99 ? 239 GLN A C   1 
ATOM   3407 O O   . GLN B 1 227 ? -1.052  11.079  -6.041  1.00 26.85 ? 239 GLN A O   1 
ATOM   3408 C CB  . GLN B 1 227 ? -1.271  14.287  -5.575  1.00 25.56 ? 239 GLN A CB  1 
ATOM   3409 C CG  . GLN B 1 227 ? -1.572  15.554  -4.848  1.00 29.52 ? 239 GLN A CG  1 
ATOM   3410 C CD  . GLN B 1 227 ? -0.319  16.305  -4.485  1.00 40.40 ? 239 GLN A CD  1 
ATOM   3411 O OE1 . GLN B 1 227 ? 0.641   16.362  -5.273  1.00 41.09 ? 239 GLN A OE1 1 
ATOM   3412 N NE2 . GLN B 1 227 ? -0.296  16.863  -3.266  1.00 39.37 ? 239 GLN A NE2 1 
ATOM   3413 N N   . ASP B 1 228 ? -3.130  11.864  -6.414  1.00 27.58 ? 240 ASP A N   1 
ATOM   3414 C CA  . ASP B 1 228 ? -3.396  11.024  -7.571  1.00 22.83 ? 240 ASP A CA  1 
ATOM   3415 C C   . ASP B 1 228 ? -2.227  11.082  -8.542  1.00 27.31 ? 240 ASP A C   1 
ATOM   3416 O O   . ASP B 1 228 ? -1.802  12.165  -8.959  1.00 28.52 ? 240 ASP A O   1 
ATOM   3417 C CB  . ASP B 1 228 ? -4.671  11.506  -8.258  1.00 23.49 ? 240 ASP A CB  1 
ATOM   3418 C CG  . ASP B 1 228 ? -5.268  10.475  -9.181  1.00 29.92 ? 240 ASP A CG  1 
ATOM   3419 O OD1 . ASP B 1 228 ? -4.832  9.312   -9.135  1.00 33.26 ? 240 ASP A OD1 1 
ATOM   3420 O OD2 . ASP B 1 228 ? -6.164  10.827  -9.981  1.00 35.16 ? 240 ASP A OD2 1 
ATOM   3421 N N   . GLY B 1 229 ? -1.673  9.919   -8.874  1.00 28.91 ? 241 GLY A N   1 
ATOM   3422 C CA  . GLY B 1 229 ? -0.564  9.880   -9.801  1.00 25.72 ? 241 GLY A CA  1 
ATOM   3423 C C   . GLY B 1 229 ? 0.782   10.155  -9.184  1.00 29.24 ? 241 GLY A C   1 
ATOM   3424 O O   . GLY B 1 229 ? 1.719   10.523  -9.900  1.00 34.72 ? 241 GLY A O   1 
ATOM   3425 N N   . SER B 1 230 ? 0.907   10.009  -7.873  1.00 26.81 ? 242 SER A N   1 
ATOM   3426 C CA  . SER B 1 230 ? 2.195   10.157  -7.225  1.00 25.54 ? 242 SER A CA  1 
ATOM   3427 C C   . SER B 1 230 ? 3.038   8.916   -7.498  1.00 26.11 ? 242 SER A C   1 
ATOM   3428 O O   . SER B 1 230 ? 2.507   7.827   -7.720  1.00 27.47 ? 242 SER A O   1 
ATOM   3429 C CB  . SER B 1 230 ? 2.005   10.366  -5.724  1.00 22.71 ? 242 SER A CB  1 
ATOM   3430 O OG  . SER B 1 230 ? 1.648   11.698  -5.448  1.00 19.28 ? 242 SER A OG  1 
ATOM   3431 N N   . LEU B 1 231 ? 4.365   9.082   -7.486  1.00 27.20 ? 243 LEU A N   1 
ATOM   3432 C CA  . LEU B 1 231 ? 5.292   7.973   -7.708  1.00 24.82 ? 243 LEU A CA  1 
ATOM   3433 C C   . LEU B 1 231 ? 6.082   7.691   -6.437  1.00 21.88 ? 243 LEU A C   1 
ATOM   3434 O O   . LEU B 1 231 ? 6.536   8.620   -5.765  1.00 21.69 ? 243 LEU A O   1 
ATOM   3435 C CB  . LEU B 1 231 ? 6.249   8.270   -8.861  1.00 21.48 ? 243 LEU A CB  1 
ATOM   3436 C CG  . LEU B 1 231 ? 5.702   8.118   -10.283 1.00 18.44 ? 243 LEU A CG  1 
ATOM   3437 C CD1 . LEU B 1 231 ? 6.832   8.227   -11.285 1.00 22.21 ? 243 LEU A CD1 1 
ATOM   3438 C CD2 . LEU B 1 231 ? 4.903   6.840   -10.485 1.00 17.37 ? 243 LEU A CD2 1 
ATOM   3439 N N   . ILE B 1 232 ? 6.243   6.414   -6.107  1.00 21.86 ? 244 ILE A N   1 
ATOM   3440 C CA  . ILE B 1 232 ? 6.917   5.993   -4.885  1.00 22.97 ? 244 ILE A CA  1 
ATOM   3441 C C   . ILE B 1 232 ? 8.107   5.131   -5.264  1.00 26.13 ? 244 ILE A C   1 
ATOM   3442 O O   . ILE B 1 232 ? 7.975   4.223   -6.090  1.00 28.29 ? 244 ILE A O   1 
ATOM   3443 C CB  . ILE B 1 232 ? 5.979   5.217   -3.950  1.00 19.12 ? 244 ILE A CB  1 
ATOM   3444 C CG1 . ILE B 1 232 ? 4.860   6.125   -3.437  1.00 20.21 ? 244 ILE A CG1 1 
ATOM   3445 C CG2 . ILE B 1 232 ? 6.771   4.613   -2.811  1.00 19.01 ? 244 ILE A CG2 1 
ATOM   3446 C CD1 . ILE B 1 232 ? 3.646   5.371   -2.942  1.00 17.51 ? 244 ILE A CD1 1 
ATOM   3447 N N   . ASP B 1 233 ? 9.260   5.411   -4.663  1.00 24.79 ? 245 ASP A N   1 
ATOM   3448 C CA  . ASP B 1 233 ? 10.487  4.681   -4.941  1.00 25.43 ? 245 ASP A CA  1 
ATOM   3449 C C   . ASP B 1 233 ? 10.999  4.081   -3.648  1.00 26.32 ? 245 ASP A C   1 
ATOM   3450 O O   . ASP B 1 233 ? 11.183  4.801   -2.663  1.00 26.68 ? 245 ASP A O   1 
ATOM   3451 C CB  . ASP B 1 233 ? 11.550  5.593   -5.543  1.00 28.37 ? 245 ASP A CB  1 
ATOM   3452 C CG  . ASP B 1 233 ? 12.798  4.839   -5.960  1.00 33.74 ? 245 ASP A CG  1 
ATOM   3453 O OD1 . ASP B 1 233 ? 13.455  4.253   -5.067  1.00 33.74 ? 245 ASP A OD1 1 
ATOM   3454 O OD2 . ASP B 1 233 ? 13.141  4.858   -7.171  1.00 40.12 ? 245 ASP A OD2 1 
ATOM   3455 N N   . LEU B 1 234 ? 11.257  2.778   -3.658  1.00 25.53 ? 246 LEU A N   1 
ATOM   3456 C CA  . LEU B 1 234 ? 11.642  2.084   -2.439  1.00 25.11 ? 246 LEU A CA  1 
ATOM   3457 C C   . LEU B 1 234 ? 12.980  1.361   -2.578  1.00 30.29 ? 246 LEU A C   1 
ATOM   3458 O O   . LEU B 1 234 ? 13.266  0.433   -1.808  1.00 32.93 ? 246 LEU A O   1 
ATOM   3459 C CB  . LEU B 1 234 ? 10.540  1.108   -2.016  1.00 24.42 ? 246 LEU A CB  1 
ATOM   3460 C CG  . LEU B 1 234 ? 9.159   1.676   -1.694  1.00 24.53 ? 246 LEU A CG  1 
ATOM   3461 C CD1 . LEU B 1 234 ? 8.158   0.545   -1.508  1.00 19.84 ? 246 LEU A CD1 1 
ATOM   3462 C CD2 . LEU B 1 234 ? 9.193   2.587   -0.456  1.00 22.76 ? 246 LEU A CD2 1 
ATOM   3463 N N   . CYS B 1 235 ? 13.811  1.778   -3.541  1.00 27.12 ? 247 CYS A N   1 
ATOM   3464 C CA  . CYS B 1 235 ? 15.142  1.201   -3.774  1.00 30.52 ? 247 CYS A CA  1 
ATOM   3465 C C   . CYS B 1 235 ? 15.051  -0.229  -4.322  1.00 31.86 ? 247 CYS A C   1 
ATOM   3466 O O   . CYS B 1 235 ? 15.457  -1.210  -3.695  1.00 27.16 ? 247 CYS A O   1 
ATOM   3467 C CB  . CYS B 1 235 ? 16.007  1.223   -2.515  1.00 28.00 ? 247 CYS A CB  1 
ATOM   3468 S SG  . CYS B 1 235 ? 17.678  1.643   -2.897  1.00 30.17 ? 247 CYS A SG  1 
ATOM   3469 N N   . GLY B 1 236 ? 14.566  -0.302  -5.552  1.00 28.17 ? 248 GLY A N   1 
ATOM   3470 C CA  . GLY B 1 236 ? 14.391  -1.554  -6.248  1.00 31.17 ? 248 GLY A CA  1 
ATOM   3471 C C   . GLY B 1 236 ? 12.970  -1.787  -6.677  1.00 33.35 ? 248 GLY A C   1 
ATOM   3472 O O   . GLY B 1 236 ? 12.712  -2.691  -7.487  1.00 36.87 ? 248 GLY A O   1 
ATOM   3473 N N   . ALA B 1 237 ? 12.039  -0.995  -6.147  1.00 31.19 ? 249 ALA A N   1 
ATOM   3474 C CA  . ALA B 1 237 ? 10.640  -1.016  -6.541  1.00 28.03 ? 249 ALA A CA  1 
ATOM   3475 C C   . ALA B 1 237 ? 10.163  0.418   -6.706  1.00 28.81 ? 249 ALA A C   1 
ATOM   3476 O O   . ALA B 1 237 ? 10.406  1.263   -5.835  1.00 26.89 ? 249 ALA A O   1 
ATOM   3477 C CB  . ALA B 1 237 ? 9.783   -1.747  -5.505  1.00 22.11 ? 249 ALA A CB  1 
ATOM   3478 N N   . THR B 1 238 ? 9.502   0.686   -7.829  1.00 29.72 ? 250 THR A N   1 
ATOM   3479 C CA  . THR B 1 238 ? 8.815   1.947   -8.070  1.00 29.73 ? 250 THR A CA  1 
ATOM   3480 C C   . THR B 1 238 ? 7.315   1.669   -8.153  1.00 30.03 ? 250 THR A C   1 
ATOM   3481 O O   . THR B 1 238 ? 6.894   0.669   -8.745  1.00 30.77 ? 250 THR A O   1 
ATOM   3482 C CB  . THR B 1 238 ? 9.328   2.614   -9.355  1.00 27.09 ? 250 THR A CB  1 
ATOM   3483 O OG1 . THR B 1 238 ? 10.669  3.073   -9.155  1.00 26.64 ? 250 THR A OG1 1 
ATOM   3484 C CG2 . THR B 1 238 ? 8.471   3.801   -9.735  1.00 20.14 ? 250 THR A CG2 1 
ATOM   3485 N N   . LEU B 1 239 ? 6.508   2.538   -7.539  1.00 26.81 ? 251 LEU A N   1 
ATOM   3486 C CA  . LEU B 1 239 ? 5.079   2.308   -7.381  1.00 24.87 ? 251 LEU A CA  1 
ATOM   3487 C C   . LEU B 1 239 ? 4.281   3.538   -7.787  1.00 25.62 ? 251 LEU A C   1 
ATOM   3488 O O   . LEU B 1 239 ? 4.655   4.667   -7.458  1.00 27.41 ? 251 LEU A O   1 
ATOM   3489 C CB  . LEU B 1 239 ? 4.749   1.966   -5.941  1.00 22.82 ? 251 LEU A CB  1 
ATOM   3490 C CG  . LEU B 1 239 ? 4.934   0.511   -5.562  1.00 24.82 ? 251 LEU A CG  1 
ATOM   3491 C CD1 . LEU B 1 239 ? 6.363   0.242   -5.197  1.00 27.85 ? 251 LEU A CD1 1 
ATOM   3492 C CD2 . LEU B 1 239 ? 4.012   0.191   -4.411  1.00 27.02 ? 251 LEU A CD2 1 
ATOM   3493 N N   . LEU B 1 240 ? 3.157   3.314   -8.462  1.00 27.68 ? 252 LEU A N   1 
ATOM   3494 C CA  . LEU B 1 240 ? 2.235   4.381   -8.841  1.00 25.83 ? 252 LEU A CA  1 
ATOM   3495 C C   . LEU B 1 240 ? 1.010   4.353   -7.928  1.00 27.55 ? 252 LEU A C   1 
ATOM   3496 O O   . LEU B 1 240 ? 0.434   3.287   -7.680  1.00 27.81 ? 252 LEU A O   1 
ATOM   3497 C CB  . LEU B 1 240 ? 1.817   4.239   -10.306 1.00 25.69 ? 252 LEU A CB  1 
ATOM   3498 C CG  . LEU B 1 240 ? 0.725   5.150   -10.878 1.00 24.31 ? 252 LEU A CG  1 
ATOM   3499 C CD1 . LEU B 1 240 ? 1.134   6.612   -10.853 1.00 21.70 ? 252 LEU A CD1 1 
ATOM   3500 C CD2 . LEU B 1 240 ? 0.431   4.713   -12.282 1.00 22.78 ? 252 LEU A CD2 1 
ATOM   3501 N N   . TRP B 1 241 ? 0.628   5.524   -7.424  1.00 25.17 ? 253 TRP A N   1 
ATOM   3502 C CA  . TRP B 1 241 ? -0.516  5.687   -6.541  1.00 25.11 ? 253 TRP A CA  1 
ATOM   3503 C C   . TRP B 1 241 ? -1.627  6.401   -7.296  1.00 29.63 ? 253 TRP A C   1 
ATOM   3504 O O   . TRP B 1 241 ? -1.422  7.521   -7.777  1.00 27.99 ? 253 TRP A O   1 
ATOM   3505 C CB  . TRP B 1 241 ? -0.132  6.495   -5.310  1.00 25.33 ? 253 TRP A CB  1 
ATOM   3506 C CG  . TRP B 1 241 ? -1.304  6.925   -4.518  1.00 24.12 ? 253 TRP A CG  1 
ATOM   3507 C CD1 . TRP B 1 241 ? -1.891  8.155   -4.524  1.00 24.95 ? 253 TRP A CD1 1 
ATOM   3508 C CD2 . TRP B 1 241 ? -2.023  6.142   -3.563  1.00 28.00 ? 253 TRP A CD2 1 
ATOM   3509 N NE1 . TRP B 1 241 ? -2.951  8.180   -3.652  1.00 26.55 ? 253 TRP A NE1 1 
ATOM   3510 C CE2 . TRP B 1 241 ? -3.051  6.953   -3.047  1.00 29.85 ? 253 TRP A CE2 1 
ATOM   3511 C CE3 . TRP B 1 241 ? -1.901  4.835   -3.095  1.00 29.42 ? 253 TRP A CE3 1 
ATOM   3512 C CZ2 . TRP B 1 241 ? -3.953  6.493   -2.087  1.00 28.52 ? 253 TRP A CZ2 1 
ATOM   3513 C CZ3 . TRP B 1 241 ? -2.803  4.386   -2.145  1.00 28.22 ? 253 TRP A CZ3 1 
ATOM   3514 C CH2 . TRP B 1 241 ? -3.810  5.212   -1.653  1.00 24.79 ? 253 TRP A CH2 1 
ATOM   3515 N N   . ARG B 1 242 ? -2.797  5.760   -7.386  1.00 32.48 ? 254 ARG A N   1 
ATOM   3516 C CA  . ARG B 1 242 ? -3.992  6.333   -7.991  1.00 28.84 ? 254 ARG A CA  1 
ATOM   3517 C C   . ARG B 1 242 ? -5.050  6.551   -6.913  1.00 29.82 ? 254 ARG A C   1 
ATOM   3518 O O   . ARG B 1 242 ? -5.164  5.769   -5.969  1.00 31.72 ? 254 ARG A O   1 
ATOM   3519 C CB  . ARG B 1 242 ? -4.558  5.426   -9.093  1.00 29.06 ? 254 ARG A CB  1 
ATOM   3520 C CG  . ARG B 1 242 ? -3.709  5.313   -10.343 1.00 28.30 ? 254 ARG A CG  1 
ATOM   3521 C CD  . ARG B 1 242 ? -3.386  6.673   -10.891 1.00 35.84 ? 254 ARG A CD  1 
ATOM   3522 N NE  . ARG B 1 242 ? -4.563  7.406   -11.344 1.00 35.86 ? 254 ARG A NE  1 
ATOM   3523 C CZ  . ARG B 1 242 ? -5.133  7.220   -12.528 1.00 39.77 ? 254 ARG A CZ  1 
ATOM   3524 N NH1 . ARG B 1 242 ? -4.691  6.286   -13.369 1.00 44.93 ? 254 ARG A NH1 1 
ATOM   3525 N NH2 . ARG B 1 242 ? -6.165  7.991   -12.880 1.00 30.37 ? 254 ARG A NH2 1 
ATOM   3526 N N   . THR B 1 243 ? -5.831  7.612   -7.075  1.00 30.03 ? 255 THR A N   1 
ATOM   3527 C CA  . THR B 1 243 ? -6.800  8.054   -6.088  1.00 26.06 ? 255 THR A CA  1 
ATOM   3528 C C   . THR B 1 243 ? -8.230  7.732   -6.522  1.00 32.58 ? 255 THR A C   1 
ATOM   3529 O O   . THR B 1 243 ? -8.899  6.865   -5.945  1.00 33.04 ? 255 THR A O   1 
ATOM   3530 C CB  . THR B 1 243 ? -6.641  9.565   -5.860  1.00 30.07 ? 255 THR A CB  1 
ATOM   3531 O OG1 . THR B 1 243 ? -5.922  9.783   -4.645  1.00 32.66 ? 255 THR A OG1 1 
ATOM   3532 C CG2 . THR B 1 243 ? -7.974  10.284  -5.811  1.00 33.94 ? 255 THR A CG2 1 
ATOM   3533 N N   . ALA C 2 1   ? 16.165  -16.503 4.107   1.00 46.38 ? 1   ALA C N   1 
ATOM   3534 C CA  . ALA C 2 1   ? 15.372  -16.330 2.887   1.00 53.00 ? 1   ALA C CA  1 
ATOM   3535 C C   . ALA C 2 1   ? 15.588  -14.947 2.271   1.00 54.96 ? 1   ALA C C   1 
ATOM   3536 O O   . ALA C 2 1   ? 16.332  -14.131 2.815   1.00 55.89 ? 1   ALA C O   1 
ATOM   3537 C CB  . ALA C 2 1   ? 13.884  -16.551 3.173   1.00 49.73 ? 1   ALA C CB  1 
ATOM   3538 N N   . TYR C 2 2   ? 14.928  -14.695 1.135   1.00 50.33 ? 2   TYR C N   1 
ATOM   3539 C CA  . TYR C 2 2   ? 15.029  -13.388 0.494   1.00 48.76 ? 2   TYR C CA  1 
ATOM   3540 C C   . TYR C 2 2   ? 14.291  -12.321 1.297   1.00 51.23 ? 2   TYR C C   1 
ATOM   3541 O O   . TYR C 2 2   ? 14.795  -11.204 1.461   1.00 49.91 ? 2   TYR C O   1 
ATOM   3542 C CB  . TYR C 2 2   ? 14.483  -13.466 -0.930  1.00 49.30 ? 2   TYR C CB  1 
ATOM   3543 C CG  . TYR C 2 2   ? 14.199  -12.122 -1.590  1.00 49.71 ? 2   TYR C CG  1 
ATOM   3544 C CD1 . TYR C 2 2   ? 15.227  -11.329 -2.101  1.00 48.02 ? 2   TYR C CD1 1 
ATOM   3545 C CD2 . TYR C 2 2   ? 12.899  -11.650 -1.702  1.00 45.15 ? 2   TYR C CD2 1 
ATOM   3546 C CE1 . TYR C 2 2   ? 14.956  -10.108 -2.706  1.00 48.49 ? 2   TYR C CE1 1 
ATOM   3547 C CE2 . TYR C 2 2   ? 12.621  -10.440 -2.301  1.00 43.38 ? 2   TYR C CE2 1 
ATOM   3548 C CZ  . TYR C 2 2   ? 13.644  -9.669  -2.798  1.00 46.75 ? 2   TYR C CZ  1 
ATOM   3549 O OH  . TYR C 2 2   ? 13.344  -8.458  -3.392  1.00 43.87 ? 2   TYR C OH  1 
ATOM   3550 N N   . GLU C 2 3   ? 13.102  -12.649 1.816   1.00 54.85 ? 3   GLU C N   1 
ATOM   3551 C CA  . GLU C 2 3   ? 12.259  -11.706 2.550   1.00 48.57 ? 3   GLU C CA  1 
ATOM   3552 C C   . GLU C 2 3   ? 12.737  -11.450 3.972   1.00 47.34 ? 3   GLU C C   1 
ATOM   3553 O O   . GLU C 2 3   ? 12.180  -10.578 4.647   1.00 45.42 ? 3   GLU C O   1 
ATOM   3554 C CB  . GLU C 2 3   ? 10.804  -12.205 2.643   1.00 46.66 ? 3   GLU C CB  1 
ATOM   3555 C CG  . GLU C 2 3   ? 10.033  -12.423 1.323   1.00 50.61 ? 3   GLU C CG  1 
ATOM   3556 C CD  . GLU C 2 3   ? 10.290  -13.792 0.677   1.00 50.74 ? 3   GLU C CD  1 
ATOM   3557 O OE1 . GLU C 2 3   ? 9.796   -14.023 -0.452  1.00 42.64 ? 3   GLU C OE1 1 
ATOM   3558 O OE2 . GLU C 2 3   ? 10.995  -14.624 1.292   1.00 54.23 ? 3   GLU C OE2 1 
ATOM   3559 N N   . ASP C 2 4   ? 13.698  -12.219 4.467   1.00 48.63 ? 4   ASP C N   1 
ATOM   3560 C CA  . ASP C 2 4   ? 14.171  -12.049 5.829   1.00 50.86 ? 4   ASP C CA  1 
ATOM   3561 C C   . ASP C 2 4   ? 15.568  -11.470 5.897   1.00 45.03 ? 4   ASP C C   1 
ATOM   3562 O O   . ASP C 2 4   ? 15.957  -10.960 6.956   1.00 43.25 ? 4   ASP C O   1 
ATOM   3563 C CB  . ASP C 2 4   ? 14.123  -13.389 6.578   1.00 52.27 ? 4   ASP C CB  1 
ATOM   3564 C CG  . ASP C 2 4   ? 12.706  -13.786 6.959   1.00 54.94 ? 4   ASP C CG  1 
ATOM   3565 O OD1 . ASP C 2 4   ? 11.767  -12.989 6.701   1.00 60.57 ? 4   ASP C OD1 1 
ATOM   3566 O OD2 . ASP C 2 4   ? 12.525  -14.904 7.483   1.00 56.70 ? 4   ASP C OD2 1 
ATOM   3567 N N   . SER C 2 5   ? 16.309  -11.503 4.791   1.00 43.43 ? 5   SER C N   1 
ATOM   3568 C CA  . SER C 2 5   ? 17.625  -10.900 4.746   1.00 44.46 ? 5   SER C CA  1 
ATOM   3569 C C   . SER C 2 5   ? 17.552  -9.437  5.194   1.00 49.09 ? 5   SER C C   1 
ATOM   3570 O O   . SER C 2 5   ? 16.489  -8.814  5.249   1.00 48.97 ? 5   SER C O   1 
ATOM   3571 C CB  . SER C 2 5   ? 18.227  -11.025 3.339   1.00 50.52 ? 5   SER C CB  1 
ATOM   3572 O OG  . SER C 2 5   ? 17.758  -10.030 2.430   1.00 51.67 ? 5   SER C OG  1 
ATOM   3573 N N   . GLU C 2 6   ? 18.712  -8.899  5.534   1.00 51.16 ? 6   GLU C N   1 
ATOM   3574 C CA  . GLU C 2 6   ? 18.825  -7.532  6.008   1.00 46.44 ? 6   GLU C CA  1 
ATOM   3575 C C   . GLU C 2 6   ? 18.906  -6.550  4.841   1.00 41.81 ? 6   GLU C C   1 
ATOM   3576 O O   . GLU C 2 6   ? 19.397  -6.892  3.768   1.00 42.08 ? 6   GLU C O   1 
ATOM   3577 C CB  . GLU C 2 6   ? 20.048  -7.428  6.909   1.00 48.66 ? 6   GLU C CB  1 
ATOM   3578 C CG  . GLU C 2 6   ? 20.728  -6.085  6.930   1.00 55.79 ? 6   GLU C CG  1 
ATOM   3579 C CD  . GLU C 2 6   ? 21.375  -5.815  8.266   1.00 57.42 ? 6   GLU C CD  1 
ATOM   3580 O OE1 . GLU C 2 6   ? 21.607  -6.798  9.008   1.00 59.56 ? 6   GLU C OE1 1 
ATOM   3581 O OE2 . GLU C 2 6   ? 21.650  -4.633  8.565   1.00 55.96 ? 6   GLU C OE2 1 
HETATM 3582 N N   . TPO C 2 7   ? 18.409  -5.337  5.049   1.00 42.10 ? 7   TPO C N   1 
HETATM 3583 C CA  . TPO C 2 7   ? 18.415  -4.347  3.988   1.00 41.27 ? 7   TPO C CA  1 
HETATM 3584 C CB  . TPO C 2 7   ? 17.460  -3.231  4.308   1.00 39.49 ? 7   TPO C CB  1 
HETATM 3585 C CG2 . TPO C 2 7   ? 17.329  -2.335  3.077   1.00 38.10 ? 7   TPO C CG2 1 
HETATM 3586 O OG1 . TPO C 2 7   ? 16.194  -3.825  4.589   1.00 38.20 ? 7   TPO C OG1 1 
HETATM 3587 P P   . TPO C 2 7   ? 15.853  -3.492  6.125   1.00 37.32 ? 7   TPO C P   1 
HETATM 3588 O O1P . TPO C 2 7   ? 16.090  -2.051  6.371   1.00 38.19 ? 7   TPO C O1P 1 
HETATM 3589 O O2P . TPO C 2 7   ? 14.307  -3.835  6.407   1.00 34.80 ? 7   TPO C O2P 1 
HETATM 3590 O O3P . TPO C 2 7   ? 16.787  -4.367  7.100   1.00 40.31 ? 7   TPO C O3P 1 
HETATM 3591 C C   . TPO C 2 7   ? 19.819  -3.809  3.736   1.00 42.77 ? 7   TPO C C   1 
HETATM 3592 O O   . TPO C 2 7   ? 20.438  -3.177  4.590   1.00 43.48 ? 7   TPO C O   1 
ATOM   3593 N N   . GLN C 2 8   ? 20.303  -4.116  2.542   1.00 38.97 ? 8   GLN C N   1 
ATOM   3594 C CA  . GLN C 2 8   ? 21.602  -3.703  2.028   1.00 41.61 ? 8   GLN C CA  1 
ATOM   3595 C C   . GLN C 2 8   ? 21.646  -2.216  1.723   1.00 47.73 ? 8   GLN C C   1 
ATOM   3596 O O   . GLN C 2 8   ? 20.681  -1.671  1.174   1.00 47.38 ? 8   GLN C O   1 
ATOM   3597 C CB  . GLN C 2 8   ? 21.925  -4.466  0.735   1.00 48.72 ? 8   GLN C CB  1 
ATOM   3598 C CG  . GLN C 2 8   ? 23.296  -5.152  0.685   1.00 56.78 ? 8   GLN C CG  1 
ATOM   3599 C CD  . GLN C 2 8   ? 23.400  -6.391  1.591   1.00 62.18 ? 8   GLN C CD  1 
ATOM   3600 O OE1 . GLN C 2 8   ? 22.587  -7.311  1.511   1.00 67.56 ? 8   GLN C OE1 1 
ATOM   3601 N NE2 . GLN C 2 8   ? 24.399  -6.403  2.467   1.00 58.55 ? 8   GLN C NE2 1 
ATOM   3602 N N   . PRO C 2 9   ? 22.752  -1.554  2.075   1.00 50.71 ? 9   PRO C N   1 
ATOM   3603 C CA  . PRO C 2 9   ? 22.940  -0.150  1.667   1.00 44.88 ? 9   PRO C CA  1 
ATOM   3604 C C   . PRO C 2 9   ? 23.310  -0.069  0.192   1.00 42.57 ? 9   PRO C C   1 
ATOM   3605 O O   . PRO C 2 9   ? 24.165  -0.822  -0.287  1.00 40.45 ? 9   PRO C O   1 
ATOM   3606 C CB  . PRO C 2 9   ? 24.088  0.333   2.563   1.00 43.68 ? 9   PRO C CB  1 
ATOM   3607 C CG  . PRO C 2 9   ? 24.093  -0.644  3.721   1.00 39.13 ? 9   PRO C CG  1 
ATOM   3608 C CD  . PRO C 2 9   ? 23.735  -1.957  3.092   1.00 47.11 ? 9   PRO C CD  1 
ATOM   3609 N N   . PHE C 2 10  ? 22.650  0.849   -0.527  1.00 38.72 ? 10  PHE C N   1 
ATOM   3610 C CA  . PHE C 2 10  ? 22.855  0.953   -1.969  1.00 41.97 ? 10  PHE C CA  1 
ATOM   3611 C C   . PHE C 2 10  ? 24.292  1.342   -2.322  1.00 46.51 ? 10  PHE C C   1 
ATOM   3612 O O   . PHE C 2 10  ? 24.798  0.950   -3.383  1.00 42.38 ? 10  PHE C O   1 
ATOM   3613 C CB  . PHE C 2 10  ? 21.878  1.963   -2.569  1.00 38.90 ? 10  PHE C CB  1 
ATOM   3614 C CG  . PHE C 2 10  ? 22.055  2.158   -4.045  1.00 41.96 ? 10  PHE C CG  1 
ATOM   3615 C CD1 . PHE C 2 10  ? 21.504  1.270   -4.948  1.00 44.83 ? 10  PHE C CD1 1 
ATOM   3616 C CD2 . PHE C 2 10  ? 22.840  3.196   -4.527  1.00 50.25 ? 10  PHE C CD2 1 
ATOM   3617 C CE1 . PHE C 2 10  ? 21.692  1.434   -6.315  1.00 49.57 ? 10  PHE C CE1 1 
ATOM   3618 C CE2 . PHE C 2 10  ? 23.034  3.365   -5.887  1.00 53.51 ? 10  PHE C CE2 1 
ATOM   3619 C CZ  . PHE C 2 10  ? 22.465  2.471   -6.780  1.00 51.40 ? 10  PHE C CZ  1 
ATOM   3620 N N   . ASP C 2 11  ? 24.955  2.125   -1.468  1.00 54.00 ? 11  ASP C N   1 
ATOM   3621 C CA  . ASP C 2 11  ? 26.335  2.563   -1.721  1.00 55.34 ? 11  ASP C CA  1 
ATOM   3622 C C   . ASP C 2 11  ? 27.354  1.697   -0.976  1.00 53.90 ? 11  ASP C C   1 
ATOM   3623 O O   . ASP C 2 11  ? 27.153  0.498   -0.788  1.00 50.30 ? 11  ASP C O   1 
ATOM   3624 C CB  . ASP C 2 11  ? 26.539  4.035   -1.316  1.00 50.22 ? 11  ASP C CB  1 
ATOM   3625 C CG  . ASP C 2 11  ? 25.556  4.999   -1.998  1.00 50.79 ? 11  ASP C CG  1 
ATOM   3626 O OD1 . ASP C 2 11  ? 25.364  4.953   -3.258  1.00 46.44 ? 11  ASP C OD1 1 
ATOM   3627 O OD2 . ASP C 2 11  ? 25.008  5.843   -1.247  1.00 46.18 ? 11  ASP C OD2 1 
ATOM   3628 N N   . ALA D 2 1   ? 29.108  -2.887  -30.085 1.00 45.96 ? 1   ALA D N   1 
ATOM   3629 C CA  . ALA D 2 1   ? 28.409  -1.613  -29.917 1.00 56.87 ? 1   ALA D CA  1 
ATOM   3630 C C   . ALA D 2 1   ? 26.963  -1.808  -29.410 1.00 56.34 ? 1   ALA D C   1 
ATOM   3631 O O   . ALA D 2 1   ? 26.063  -2.168  -30.180 1.00 54.50 ? 1   ALA D O   1 
ATOM   3632 C CB  . ALA D 2 1   ? 28.420  -0.842  -31.242 1.00 51.74 ? 1   ALA D CB  1 
ATOM   3633 N N   . TYR D 2 2   ? 26.745  -1.568  -28.111 1.00 49.11 ? 2   TYR D N   1 
ATOM   3634 C CA  . TYR D 2 2   ? 25.410  -1.745  -27.537 1.00 54.44 ? 2   TYR D CA  1 
ATOM   3635 C C   . TYR D 2 2   ? 24.368  -0.892  -28.261 1.00 51.11 ? 2   TYR D C   1 
ATOM   3636 O O   . TYR D 2 2   ? 23.212  -1.307  -28.399 1.00 49.65 ? 2   TYR D O   1 
ATOM   3637 C CB  . TYR D 2 2   ? 25.464  -1.435  -26.031 1.00 53.51 ? 2   TYR D CB  1 
ATOM   3638 C CG  . TYR D 2 2   ? 24.143  -1.170  -25.321 1.00 48.61 ? 2   TYR D CG  1 
ATOM   3639 C CD1 . TYR D 2 2   ? 23.306  -2.215  -24.939 1.00 51.05 ? 2   TYR D CD1 1 
ATOM   3640 C CD2 . TYR D 2 2   ? 23.759  0.128   -24.996 1.00 45.92 ? 2   TYR D CD2 1 
ATOM   3641 C CE1 . TYR D 2 2   ? 22.099  -1.972  -24.278 1.00 52.39 ? 2   TYR D CE1 1 
ATOM   3642 C CE2 . TYR D 2 2   ? 22.557  0.386   -24.335 1.00 47.34 ? 2   TYR D CE2 1 
ATOM   3643 C CZ  . TYR D 2 2   ? 21.727  -0.667  -23.981 1.00 50.12 ? 2   TYR D CZ  1 
ATOM   3644 O OH  . TYR D 2 2   ? 20.532  -0.425  -23.320 1.00 49.57 ? 2   TYR D OH  1 
ATOM   3645 N N   . GLU D 2 3   ? 24.769  0.280   -28.762 1.00 49.06 ? 3   GLU D N   1 
ATOM   3646 C CA  . GLU D 2 3   ? 23.855  1.147   -29.501 1.00 46.12 ? 3   GLU D CA  1 
ATOM   3647 C C   . GLU D 2 3   ? 23.543  0.579   -30.878 1.00 51.46 ? 3   GLU D C   1 
ATOM   3648 O O   . GLU D 2 3   ? 22.417  0.719   -31.371 1.00 48.76 ? 3   GLU D O   1 
ATOM   3649 C CB  . GLU D 2 3   ? 24.452  2.553   -29.645 1.00 42.83 ? 3   GLU D CB  1 
ATOM   3650 C CG  . GLU D 2 3   ? 24.740  3.285   -28.341 1.00 47.82 ? 3   GLU D CG  1 
ATOM   3651 C CD  . GLU D 2 3   ? 25.922  2.685   -27.572 1.00 55.37 ? 3   GLU D CD  1 
ATOM   3652 O OE1 . GLU D 2 3   ? 25.736  1.620   -26.927 1.00 54.48 ? 3   GLU D OE1 1 
ATOM   3653 O OE2 . GLU D 2 3   ? 27.032  3.254   -27.618 1.00 53.41 ? 3   GLU D OE2 1 
ATOM   3654 N N   . ASP D 2 4   ? 24.533  -0.046  -31.522 1.00 52.01 ? 4   ASP D N   1 
ATOM   3655 C CA  . ASP D 2 4   ? 24.392  -0.559  -32.880 1.00 51.93 ? 4   ASP D CA  1 
ATOM   3656 C C   . ASP D 2 4   ? 23.924  -2.019  -32.920 1.00 51.23 ? 4   ASP D C   1 
ATOM   3657 O O   . ASP D 2 4   ? 23.866  -2.616  -34.002 1.00 50.43 ? 4   ASP D O   1 
ATOM   3658 C CB  . ASP D 2 4   ? 25.712  -0.402  -33.650 1.00 61.08 ? 4   ASP D CB  1 
ATOM   3659 C CG  . ASP D 2 4   ? 26.234  1.028   -33.642 1.00 63.04 ? 4   ASP D CG  1 
ATOM   3660 O OD1 . ASP D 2 4   ? 25.394  1.954   -33.638 1.00 67.28 ? 4   ASP D OD1 1 
ATOM   3661 O OD2 . ASP D 2 4   ? 27.472  1.230   -33.663 1.00 60.84 ? 4   ASP D OD2 1 
ATOM   3662 N N   . SER D 2 5   ? 23.584  -2.601  -31.775 1.00 51.07 ? 5   SER D N   1 
ATOM   3663 C CA  . SER D 2 5   ? 23.059  -3.956  -31.757 1.00 48.35 ? 5   SER D CA  1 
ATOM   3664 C C   . SER D 2 5   ? 21.689  -3.979  -32.440 1.00 46.59 ? 5   SER D C   1 
ATOM   3665 O O   . SER D 2 5   ? 21.116  -2.935  -32.741 1.00 50.22 ? 5   SER D O   1 
ATOM   3666 C CB  . SER D 2 5   ? 23.018  -4.467  -30.302 1.00 52.84 ? 5   SER D CB  1 
ATOM   3667 O OG  . SER D 2 5   ? 21.730  -4.908  -29.876 1.00 49.64 ? 5   SER D OG  1 
ATOM   3668 N N   . GLU D 2 6   ? 21.179  -5.180  -32.721 1.00 48.02 ? 6   GLU D N   1 
ATOM   3669 C CA  . GLU D 2 6   ? 19.812  -5.329  -33.260 1.00 47.57 ? 6   GLU D CA  1 
ATOM   3670 C C   . GLU D 2 6   ? 18.789  -5.654  -32.154 1.00 44.48 ? 6   GLU D C   1 
ATOM   3671 O O   . GLU D 2 6   ? 19.086  -6.384  -31.209 1.00 48.13 ? 6   GLU D O   1 
ATOM   3672 C CB  . GLU D 2 6   ? 19.773  -6.411  -34.350 1.00 51.39 ? 6   GLU D CB  1 
ATOM   3673 C CG  . GLU D 2 6   ? 20.893  -6.300  -35.411 1.00 62.49 ? 6   GLU D CG  1 
ATOM   3674 C CD  . GLU D 2 6   ? 20.435  -5.740  -36.774 1.00 69.33 ? 6   GLU D CD  1 
ATOM   3675 O OE1 . GLU D 2 6   ? 19.471  -6.296  -37.361 1.00 69.53 ? 6   GLU D OE1 1 
ATOM   3676 O OE2 . GLU D 2 6   ? 21.045  -4.747  -37.253 1.00 64.84 ? 6   GLU D OE2 1 
HETATM 3677 N N   . TPO D 2 7   ? 17.594  -5.099  -32.264 1.00 44.37 ? 7   TPO D N   1 
HETATM 3678 C CA  . TPO D 2 7   ? 16.607  -5.304  -31.218 1.00 43.36 ? 7   TPO D CA  1 
HETATM 3679 C CB  . TPO D 2 7   ? 15.437  -4.392  -31.416 1.00 41.93 ? 7   TPO D CB  1 
HETATM 3680 C CG2 . TPO D 2 7   ? 14.619  -4.392  -30.125 1.00 41.35 ? 7   TPO D CG2 1 
HETATM 3681 O OG1 . TPO D 2 7   ? 15.951  -3.083  -31.645 1.00 40.55 ? 7   TPO D OG1 1 
HETATM 3682 P P   . TPO D 2 7   ? 15.763  -2.755  -33.208 1.00 40.79 ? 7   TPO D P   1 
HETATM 3683 O O1P . TPO D 2 7   ? 16.341  -3.853  -34.020 1.00 42.47 ? 7   TPO D O1P 1 
HETATM 3684 O O2P . TPO D 2 7   ? 14.193  -2.631  -33.534 1.00 39.90 ? 7   TPO D O2P 1 
HETATM 3685 O O3P . TPO D 2 7   ? 16.508  -1.375  -33.562 1.00 39.99 ? 7   TPO D O3P 1 
HETATM 3686 C C   . TPO D 2 7   ? 16.159  -6.758  -31.169 1.00 42.65 ? 7   TPO D C   1 
HETATM 3687 O O   . TPO D 2 7   ? 15.471  -7.253  -32.062 1.00 42.17 ? 7   TPO D O   1 
ATOM   3688 N N   . GLN D 2 8   ? 16.613  -7.434  -30.123 1.00 38.72 ? 8   GLN D N   1 
ATOM   3689 C CA  . GLN D 2 8   ? 16.239  -8.827  -29.847 1.00 43.75 ? 8   GLN D CA  1 
ATOM   3690 C C   . GLN D 2 8   ? 14.821  -8.932  -29.278 1.00 43.95 ? 8   GLN D C   1 
ATOM   3691 O O   . GLN D 2 8   ? 14.364  -8.043  -28.555 1.00 47.65 ? 8   GLN D O   1 
ATOM   3692 C CB  . GLN D 2 8   ? 17.231  -9.482  -28.866 1.00 41.97 ? 8   GLN D CB  1 
ATOM   3693 C CG  . GLN D 2 8   ? 16.871  -9.249  -27.382 1.00 48.30 ? 8   GLN D CG  1 
ATOM   3694 C CD  . GLN D 2 8   ? 17.453  -10.278 -26.399 1.00 53.45 ? 8   GLN D CD  1 
ATOM   3695 O OE1 . GLN D 2 8   ? 18.668  -10.513 -26.364 1.00 56.68 ? 8   GLN D OE1 1 
ATOM   3696 N NE2 . GLN D 2 8   ? 16.583  -10.859 -25.561 1.00 45.66 ? 8   GLN D NE2 1 
ATOM   3697 N N   . PRO D 2 9   ? 14.118  -10.014 -29.609 1.00 42.16 ? 9   PRO D N   1 
ATOM   3698 C CA  . PRO D 2 9   ? 12.769  -10.217 -29.057 1.00 41.66 ? 9   PRO D CA  1 
ATOM   3699 C C   . PRO D 2 9   ? 12.803  -10.510 -27.566 1.00 40.81 ? 9   PRO D C   1 
ATOM   3700 O O   . PRO D 2 9   ? 13.648  -11.266 -27.082 1.00 41.33 ? 9   PRO D O   1 
ATOM   3701 C CB  . PRO D 2 9   ? 12.240  -11.419 -29.849 1.00 39.05 ? 9   PRO D CB  1 
ATOM   3702 C CG  . PRO D 2 9   ? 12.990  -11.338 -31.159 1.00 39.88 ? 9   PRO D CG  1 
ATOM   3703 C CD  . PRO D 2 9   ? 14.383  -10.901 -30.752 1.00 42.26 ? 9   PRO D CD  1 
ATOM   3704 N N   . PHE D 2 10  ? 11.869  -9.900  -26.832 1.00 43.23 ? 10  PHE D N   1 
ATOM   3705 C CA  . PHE D 2 10  ? 11.761  -10.204 -25.409 1.00 44.24 ? 10  PHE D CA  1 
ATOM   3706 C C   . PHE D 2 10  ? 11.362  -11.660 -25.189 1.00 40.31 ? 10  PHE D C   1 
ATOM   3707 O O   . PHE D 2 10  ? 11.905  -12.332 -24.305 1.00 43.06 ? 10  PHE D O   1 
ATOM   3708 C CB  . PHE D 2 10  ? 10.764  -9.266  -24.719 1.00 42.00 ? 10  PHE D CB  1 
ATOM   3709 C CG  . PHE D 2 10  ? 10.500  -9.633  -23.280 1.00 41.13 ? 10  PHE D CG  1 
ATOM   3710 C CD1 . PHE D 2 10  ? 11.406  -9.310  -22.292 1.00 41.49 ? 10  PHE D CD1 1 
ATOM   3711 C CD2 . PHE D 2 10  ? 9.364   -10.334 -22.921 1.00 36.97 ? 10  PHE D CD2 1 
ATOM   3712 C CE1 . PHE D 2 10  ? 11.165  -9.660  -20.964 1.00 44.69 ? 10  PHE D CE1 1 
ATOM   3713 C CE2 . PHE D 2 10  ? 9.127   -10.684 -21.607 1.00 38.91 ? 10  PHE D CE2 1 
ATOM   3714 C CZ  . PHE D 2 10  ? 10.029  -10.349 -20.629 1.00 40.80 ? 10  PHE D CZ  1 
ATOM   3715 N N   . ASP D 2 11  ? 10.418  -12.162 -25.980 1.00 39.94 ? 11  ASP D N   1 
ATOM   3716 C CA  . ASP D 2 11  ? 9.997   -13.551 -25.864 1.00 41.89 ? 11  ASP D CA  1 
ATOM   3717 C C   . ASP D 2 11  ? 11.180  -14.497 -26.030 1.00 45.78 ? 11  ASP D C   1 
ATOM   3718 O O   . ASP D 2 11  ? 11.959  -14.357 -26.971 1.00 50.13 ? 11  ASP D O   1 
ATOM   3719 C CB  . ASP D 2 11  ? 8.919   -13.886 -26.899 1.00 42.91 ? 11  ASP D CB  1 
ATOM   3720 C CG  . ASP D 2 11  ? 7.561   -13.273 -26.565 1.00 44.10 ? 11  ASP D CG  1 
ATOM   3721 O OD1 . ASP D 2 11  ? 7.357   -12.829 -25.413 1.00 43.38 ? 11  ASP D OD1 1 
ATOM   3722 O OD2 . ASP D 2 11  ? 6.675   -13.273 -27.447 1.00 41.25 ? 11  ASP D OD2 1 
HETATM 3723 S S   . SO4 E 3 .   ? -10.590 -4.305  -22.697 1.00 82.30 ? 301 SO4 B S   1 
HETATM 3724 O O1  . SO4 E 3 .   ? -9.265  -4.209  -23.302 1.00 60.07 ? 301 SO4 B O1  1 
HETATM 3725 O O2  . SO4 E 3 .   ? -11.608 -4.114  -23.726 1.00 71.87 ? 301 SO4 B O2  1 
HETATM 3726 O O3  . SO4 E 3 .   ? -10.755 -5.622  -22.089 1.00 80.04 ? 301 SO4 B O3  1 
HETATM 3727 O O4  . SO4 E 3 .   ? -10.734 -3.276  -21.673 1.00 69.12 ? 301 SO4 B O4  1 
HETATM 3728 S S   . SO4 F 3 .   ? 24.805  10.336  -37.053 1.00 60.09 ? 302 SO4 B S   1 
HETATM 3729 O O1  . SO4 F 3 .   ? 26.051  9.687   -36.658 1.00 53.81 ? 302 SO4 B O1  1 
HETATM 3730 O O2  . SO4 F 3 .   ? 23.903  9.354   -37.649 1.00 45.51 ? 302 SO4 B O2  1 
HETATM 3731 O O3  . SO4 F 3 .   ? 24.195  10.917  -35.866 1.00 43.97 ? 302 SO4 B O3  1 
HETATM 3732 O O4  . SO4 F 3 .   ? 25.080  11.397  -38.016 1.00 59.02 ? 302 SO4 B O4  1 
HETATM 3733 S S   . SO4 G 3 .   ? 5.513   -18.797 -50.968 1.00 27.87 ? 303 SO4 B S   1 
HETATM 3734 O O1  . SO4 G 3 .   ? 5.756   -20.204 -51.272 1.00 26.26 ? 303 SO4 B O1  1 
HETATM 3735 O O2  . SO4 G 3 .   ? 4.129   -18.619 -50.541 1.00 27.89 ? 303 SO4 B O2  1 
HETATM 3736 O O3  . SO4 G 3 .   ? 6.406   -18.370 -49.895 1.00 29.26 ? 303 SO4 B O3  1 
HETATM 3737 O O4  . SO4 G 3 .   ? 5.761   -17.995 -52.163 1.00 28.93 ? 303 SO4 B O4  1 
HETATM 3738 S S   . SO4 H 3 .   ? 23.901  0.874   12.601  1.00 58.97 ? 301 SO4 A S   1 
HETATM 3739 O O1  . SO4 H 3 .   ? 24.782  0.191   11.658  1.00 53.65 ? 301 SO4 A O1  1 
HETATM 3740 O O2  . SO4 H 3 .   ? 23.062  1.828   11.882  1.00 37.19 ? 301 SO4 A O2  1 
HETATM 3741 O O3  . SO4 H 3 .   ? 23.055  -0.107  13.275  1.00 41.52 ? 301 SO4 A O3  1 
HETATM 3742 O O4  . SO4 H 3 .   ? 24.707  1.584   13.591  1.00 38.16 ? 301 SO4 A O4  1 
HETATM 3743 S S   . SO4 I 3 .   ? -1.884  2.640   22.714  1.00 52.07 ? 302 SO4 A S   1 
HETATM 3744 O O1  . SO4 I 3 .   ? -0.504  3.064   22.495  1.00 37.17 ? 302 SO4 A O1  1 
HETATM 3745 O O2  . SO4 I 3 .   ? -2.569  2.534   21.429  1.00 37.50 ? 302 SO4 A O2  1 
HETATM 3746 O O3  . SO4 I 3 .   ? -1.897  1.341   23.380  1.00 45.32 ? 302 SO4 A O3  1 
HETATM 3747 O O4  . SO4 I 3 .   ? -2.567  3.622   23.552  1.00 41.23 ? 302 SO4 A O4  1 
HETATM 3748 O O   . HOH J 4 .   ? 9.962   33.364  -28.003 1.00 32.99 ? 401 HOH B O   1 
HETATM 3749 O O   . HOH J 4 .   ? 1.324   -5.763  -26.513 1.00 22.10 ? 402 HOH B O   1 
HETATM 3750 O O   . HOH J 4 .   ? 21.817  3.962   -26.095 1.00 34.54 ? 403 HOH B O   1 
HETATM 3751 O O   . HOH J 4 .   ? 4.271   -6.418  -26.516 1.00 31.84 ? 404 HOH B O   1 
HETATM 3752 O O   . HOH J 4 .   ? -4.577  10.745  -31.876 1.00 21.16 ? 405 HOH B O   1 
HETATM 3753 O O   . HOH J 4 .   ? -2.219  -1.526  -49.392 1.00 39.77 ? 406 HOH B O   1 
HETATM 3754 O O   . HOH J 4 .   ? 24.841  -7.527  -22.755 1.00 46.82 ? 407 HOH B O   1 
HETATM 3755 O O   . HOH J 4 .   ? -14.991 16.211  -23.145 1.00 30.15 ? 408 HOH B O   1 
HETATM 3756 O O   . HOH J 4 .   ? 9.865   13.178  -45.977 1.00 29.55 ? 409 HOH B O   1 
HETATM 3757 O O   . HOH J 4 .   ? -7.443  8.060   -24.549 1.00 32.41 ? 410 HOH B O   1 
HETATM 3758 O O   . HOH J 4 .   ? -1.482  -11.836 -28.168 1.00 35.04 ? 411 HOH B O   1 
HETATM 3759 O O   . HOH J 4 .   ? 12.185  -0.423  -27.584 1.00 35.58 ? 412 HOH B O   1 
HETATM 3760 O O   . HOH J 4 .   ? 6.213   26.559  -22.454 1.00 27.37 ? 413 HOH B O   1 
HETATM 3761 O O   . HOH J 4 .   ? 6.643   -6.442  -55.311 1.00 45.40 ? 414 HOH B O   1 
HETATM 3762 O O   . HOH J 4 .   ? -4.595  -12.110 -37.360 1.00 32.86 ? 415 HOH B O   1 
HETATM 3763 O O   . HOH J 4 .   ? 4.517   21.880  -20.756 1.00 29.04 ? 416 HOH B O   1 
HETATM 3764 O O   . HOH J 4 .   ? 5.471   30.557  -31.258 1.00 28.51 ? 417 HOH B O   1 
HETATM 3765 O O   . HOH J 4 .   ? 7.027   -14.709 -47.119 1.00 41.54 ? 418 HOH B O   1 
HETATM 3766 O O   . HOH J 4 .   ? 11.162  -0.416  -61.403 1.00 21.29 ? 419 HOH B O   1 
HETATM 3767 O O   . HOH J 4 .   ? 12.807  0.824   -38.597 1.00 22.90 ? 420 HOH B O   1 
HETATM 3768 O O   . HOH J 4 .   ? -6.150  0.210   -50.452 1.00 35.13 ? 421 HOH B O   1 
HETATM 3769 O O   . HOH J 4 .   ? 2.293   21.039  -44.536 1.00 27.13 ? 422 HOH B O   1 
HETATM 3770 O O   . HOH J 4 .   ? -5.644  -8.992  -37.014 1.00 28.71 ? 423 HOH B O   1 
HETATM 3771 O O   . HOH J 4 .   ? 11.323  -2.193  -28.637 1.00 33.98 ? 424 HOH B O   1 
HETATM 3772 O O   . HOH J 4 .   ? 9.071   16.272  -48.048 1.00 12.11 ? 425 HOH B O   1 
HETATM 3773 O O   . HOH J 4 .   ? 12.177  -3.812  -46.524 1.00 24.31 ? 426 HOH B O   1 
HETATM 3774 O O   . HOH J 4 .   ? 8.247   34.337  -29.122 1.00 48.67 ? 427 HOH B O   1 
HETATM 3775 O O   . HOH J 4 .   ? 8.062   15.163  -49.425 1.00 21.64 ? 428 HOH B O   1 
HETATM 3776 O O   . HOH J 4 .   ? 15.331  16.408  -39.578 1.00 31.14 ? 429 HOH B O   1 
HETATM 3777 O O   . HOH J 4 .   ? 13.712  17.125  -42.005 1.00 14.82 ? 430 HOH B O   1 
HETATM 3778 O O   . HOH K 4 .   ? 17.314  13.641  2.042   1.00 33.08 ? 401 HOH A O   1 
HETATM 3779 O O   . HOH K 4 .   ? 7.337   -4.126  -18.625 1.00 38.56 ? 402 HOH A O   1 
HETATM 3780 O O   . HOH K 4 .   ? -11.044 7.290   -6.591  1.00 31.23 ? 403 HOH A O   1 
HETATM 3781 O O   . HOH K 4 .   ? -7.301  -2.266  1.490   1.00 29.74 ? 404 HOH A O   1 
HETATM 3782 O O   . HOH K 4 .   ? 11.104  13.507  19.341  1.00 30.71 ? 405 HOH A O   1 
HETATM 3783 O O   . HOH K 4 .   ? -0.032  16.656  5.001   1.00 17.82 ? 406 HOH A O   1 
HETATM 3784 O O   . HOH K 4 .   ? -2.600  8.408   12.221  1.00 24.36 ? 407 HOH A O   1 
HETATM 3785 O O   . HOH K 4 .   ? -4.493  -8.485  -6.468  1.00 22.90 ? 408 HOH A O   1 
HETATM 3786 O O   . HOH K 4 .   ? -1.216  10.881  8.804   1.00 21.17 ? 409 HOH A O   1 
HETATM 3787 O O   . HOH K 4 .   ? 23.073  1.328   15.581  1.00 26.70 ? 410 HOH A O   1 
HETATM 3788 O O   . HOH K 4 .   ? 0.003   2.023   20.131  1.00 30.16 ? 411 HOH A O   1 
HETATM 3789 O O   . HOH K 4 .   ? 8.809   10.012  15.902  1.00 21.84 ? 412 HOH A O   1 
HETATM 3790 O O   . HOH K 4 .   ? 1.721   -10.132 -3.840  1.00 29.49 ? 413 HOH A O   1 
HETATM 3791 O O   . HOH K 4 .   ? 12.801  18.705  22.937  1.00 26.71 ? 414 HOH A O   1 
HETATM 3792 O O   . HOH K 4 .   ? 9.723   -8.473  11.986  1.00 21.36 ? 415 HOH A O   1 
HETATM 3793 O O   . HOH K 4 .   ? 14.181  1.284   34.365  1.00 21.65 ? 416 HOH A O   1 
HETATM 3794 O O   . HOH K 4 .   ? 8.242   19.718  21.560  1.00 23.14 ? 417 HOH A O   1 
HETATM 3795 O O   . HOH K 4 .   ? 18.889  2.040   10.847  1.00 19.54 ? 418 HOH A O   1 
HETATM 3796 O O   . HOH K 4 .   ? 18.926  9.975   25.098  1.00 26.44 ? 419 HOH A O   1 
HETATM 3797 O O   . HOH K 4 .   ? -3.419  13.210  10.623  1.00 33.17 ? 420 HOH A O   1 
HETATM 3798 O O   . HOH K 4 .   ? 12.774  2.728   3.669   1.00 20.67 ? 421 HOH A O   1 
HETATM 3799 O O   . HOH K 4 .   ? 9.428   11.813  16.805  1.00 19.96 ? 422 HOH A O   1 
HETATM 3800 O O   . HOH K 4 .   ? 7.902   -16.096 2.736   1.00 33.60 ? 423 HOH A O   1 
HETATM 3801 O O   . HOH K 4 .   ? 16.443  20.161  9.985   1.00 17.28 ? 424 HOH A O   1 
HETATM 3802 O O   . HOH K 4 .   ? 0.499   -3.089  -13.680 1.00 42.36 ? 425 HOH A O   1 
HETATM 3803 O O   . HOH K 4 .   ? 15.721  4.849   -8.956  1.00 41.30 ? 426 HOH A O   1 
HETATM 3804 O O   . HOH K 4 .   ? 28.801  7.447   20.126  1.00 27.56 ? 427 HOH A O   1 
HETATM 3805 O O   . HOH K 4 .   ? -2.646  -8.141  -4.371  1.00 30.62 ? 428 HOH A O   1 
HETATM 3806 O O   . HOH K 4 .   ? 17.906  20.737  12.220  1.00 19.31 ? 429 HOH A O   1 
HETATM 3807 O O   . HOH K 4 .   ? 0.790   20.808  -11.840 1.00 45.95 ? 430 HOH A O   1 
HETATM 3808 O O   . HOH K 4 .   ? 21.437  0.102   17.165  1.00 27.28 ? 431 HOH A O   1 
HETATM 3809 O O   . HOH K 4 .   ? 2.524   18.005  5.926   1.00 15.76 ? 432 HOH A O   1 
HETATM 3810 O O   . HOH K 4 .   ? -0.763  -8.769  -2.421  1.00 32.73 ? 433 HOH A O   1 
HETATM 3811 O O   . HOH K 4 .   ? -10.191 9.552   -8.853  1.00 27.17 ? 434 HOH A O   1 
HETATM 3812 O O   . HOH K 4 .   ? -12.744 6.114   -7.754  1.00 51.14 ? 435 HOH A O   1 
HETATM 3813 O O   . HOH K 4 .   ? 15.502  26.727  6.959   1.00 27.05 ? 436 HOH A O   1 
HETATM 3814 O O   . HOH K 4 .   ? -1.173  21.597  -11.309 1.00 36.41 ? 437 HOH A O   1 
HETATM 3815 O O   . HOH K 4 .   ? 4.584   -14.294 -0.687  1.00 20.20 ? 438 HOH A O   1 
HETATM 3816 O O   . HOH K 4 .   ? 2.714   -12.444 -0.723  1.00 28.91 ? 439 HOH A O   1 
HETATM 3817 O O   . HOH L 4 .   ? 17.370  -4.917  -38.443 1.00 35.25 ? 101 HOH D O   1 
# 
