data_8P3I
# 
_entry.id   8P3I 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8P3I         pdb_00008p3i 10.2210/pdb8p3i/pdb 
WWPDB D_1292129005 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8P3I 
_pdbx_database_status.recvd_initial_deposition_date   2023-05-17 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              e.tate@imperial.ac.uk 
_pdbx_contact_author.name_first         Edward 
_pdbx_contact_author.name_last          Tate 
_pdbx_contact_author.name_mi            W 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2213-5814 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'De Vita, E.'     1 0000-0003-4707-8342 
'Brustur, D.'     2 ?                   
'Tersa, M.'       3 0000-0002-2370-7776 
'Petracca, R.'    4 ?                   
'Morgan, R.M.L.'  5 0000-0002-9760-3638 
'Lanyon-Hogg, T.' 6 0000-0002-7092-8096 
'Norman, J.C.'    7 ?                   
'Cota, E.'        8 ?                   
'Tate, E.W.'      9 0000-0003-2213-5814 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Targeted covalent inhibitors of the small GTPase Rab27A' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'De Vita, E.'     1 0000-0003-4707-8342 
primary 'Brustur, D.'     2 ?                   
primary 'Tersa, M.'       3 0000-0002-2370-7776 
primary 'Petracca, R.'    4 ?                   
primary 'Morgan, R.M.L.'  5 0000-0002-9760-3638 
primary 'Lanyon-Hogg, T.' 6 0000-0002-7092-8096 
primary 'Norman, J.C.'    7 ?                   
primary 'Cota, E.'        8 ?                   
primary 'Tate, E.W.'      9 0000-0003-2213-5814 
# 
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 'Synaptotagmin-like protein 2,Ras-related protein Rab-27A'     25914.211 2  3.6.5.2 Q78L,C188S ? ? 
2 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'                  522.196   2  ?       ?          ? ? 
3 non-polymer syn GLYCEROL                                                       92.094    12 ?       ?          ? ? 
4 non-polymer syn '~{N}-(3-methoxy-4-pyrrolidin-1-ylsulfonyl-phenyl)propanamide' 312.385   2  ?       ?          ? ? 
5 non-polymer syn 'MAGNESIUM ION'                                                24.305    2  ?       ?          ? ? 
6 water       nat water                                                          18.015    57 ?       ?          ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Breast cancer-associated antigen SGA-72M,Exophilin-4,Rab-27,GTP-binding protein Ram' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GHMSFLTEEEQEAIMKVLQRDAALKRAEEERGSGSGSGMSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTV
GIDFREKRVVYRASGPDGATGRGQRIHLQLWDTAGLERFRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMHAY
CENPDIVLCGNKSDLEDQRVVKEEEAIALAEKYGIPYFETSAANGTNISQAIEMLLDLIMKRMERSVDKS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GHMSFLTEEEQEAIMKVLQRDAALKRAEEERGSGSGSGMSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTV
GIDFREKRVVYRASGPDGATGRGQRIHLQLWDTAGLERFRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMHAY
CENPDIVLCGNKSDLEDQRVVKEEEAIALAEKYGIPYFETSAANGTNISQAIEMLLDLIMKRMERSVDKS
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'                  GNP 
3 GLYCEROL                                                       GOL 
4 '~{N}-(3-methoxy-4-pyrrolidin-1-ylsulfonyl-phenyl)propanamide' WTK 
5 'MAGNESIUM ION'                                                MG  
6 water                                                          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   HIS n 
1 3   MET n 
1 4   SER n 
1 5   PHE n 
1 6   LEU n 
1 7   THR n 
1 8   GLU n 
1 9   GLU n 
1 10  GLU n 
1 11  GLN n 
1 12  GLU n 
1 13  ALA n 
1 14  ILE n 
1 15  MET n 
1 16  LYS n 
1 17  VAL n 
1 18  LEU n 
1 19  GLN n 
1 20  ARG n 
1 21  ASP n 
1 22  ALA n 
1 23  ALA n 
1 24  LEU n 
1 25  LYS n 
1 26  ARG n 
1 27  ALA n 
1 28  GLU n 
1 29  GLU n 
1 30  GLU n 
1 31  ARG n 
1 32  GLY n 
1 33  SER n 
1 34  GLY n 
1 35  SER n 
1 36  GLY n 
1 37  SER n 
1 38  GLY n 
1 39  MET n 
1 40  SER n 
1 41  ASP n 
1 42  GLY n 
1 43  ASP n 
1 44  TYR n 
1 45  ASP n 
1 46  TYR n 
1 47  LEU n 
1 48  ILE n 
1 49  LYS n 
1 50  PHE n 
1 51  LEU n 
1 52  ALA n 
1 53  LEU n 
1 54  GLY n 
1 55  ASP n 
1 56  SER n 
1 57  GLY n 
1 58  VAL n 
1 59  GLY n 
1 60  LYS n 
1 61  THR n 
1 62  SER n 
1 63  VAL n 
1 64  LEU n 
1 65  TYR n 
1 66  GLN n 
1 67  TYR n 
1 68  THR n 
1 69  ASP n 
1 70  GLY n 
1 71  LYS n 
1 72  PHE n 
1 73  ASN n 
1 74  SER n 
1 75  LYS n 
1 76  PHE n 
1 77  ILE n 
1 78  THR n 
1 79  THR n 
1 80  VAL n 
1 81  GLY n 
1 82  ILE n 
1 83  ASP n 
1 84  PHE n 
1 85  ARG n 
1 86  GLU n 
1 87  LYS n 
1 88  ARG n 
1 89  VAL n 
1 90  VAL n 
1 91  TYR n 
1 92  ARG n 
1 93  ALA n 
1 94  SER n 
1 95  GLY n 
1 96  PRO n 
1 97  ASP n 
1 98  GLY n 
1 99  ALA n 
1 100 THR n 
1 101 GLY n 
1 102 ARG n 
1 103 GLY n 
1 104 GLN n 
1 105 ARG n 
1 106 ILE n 
1 107 HIS n 
1 108 LEU n 
1 109 GLN n 
1 110 LEU n 
1 111 TRP n 
1 112 ASP n 
1 113 THR n 
1 114 ALA n 
1 115 GLY n 
1 116 LEU n 
1 117 GLU n 
1 118 ARG n 
1 119 PHE n 
1 120 ARG n 
1 121 SER n 
1 122 LEU n 
1 123 THR n 
1 124 THR n 
1 125 ALA n 
1 126 PHE n 
1 127 PHE n 
1 128 ARG n 
1 129 ASP n 
1 130 ALA n 
1 131 MET n 
1 132 GLY n 
1 133 PHE n 
1 134 LEU n 
1 135 LEU n 
1 136 LEU n 
1 137 PHE n 
1 138 ASP n 
1 139 LEU n 
1 140 THR n 
1 141 ASN n 
1 142 GLU n 
1 143 GLN n 
1 144 SER n 
1 145 PHE n 
1 146 LEU n 
1 147 ASN n 
1 148 VAL n 
1 149 ARG n 
1 150 ASN n 
1 151 TRP n 
1 152 ILE n 
1 153 SER n 
1 154 GLN n 
1 155 LEU n 
1 156 GLN n 
1 157 MET n 
1 158 HIS n 
1 159 ALA n 
1 160 TYR n 
1 161 CYS n 
1 162 GLU n 
1 163 ASN n 
1 164 PRO n 
1 165 ASP n 
1 166 ILE n 
1 167 VAL n 
1 168 LEU n 
1 169 CYS n 
1 170 GLY n 
1 171 ASN n 
1 172 LYS n 
1 173 SER n 
1 174 ASP n 
1 175 LEU n 
1 176 GLU n 
1 177 ASP n 
1 178 GLN n 
1 179 ARG n 
1 180 VAL n 
1 181 VAL n 
1 182 LYS n 
1 183 GLU n 
1 184 GLU n 
1 185 GLU n 
1 186 ALA n 
1 187 ILE n 
1 188 ALA n 
1 189 LEU n 
1 190 ALA n 
1 191 GLU n 
1 192 LYS n 
1 193 TYR n 
1 194 GLY n 
1 195 ILE n 
1 196 PRO n 
1 197 TYR n 
1 198 PHE n 
1 199 GLU n 
1 200 THR n 
1 201 SER n 
1 202 ALA n 
1 203 ALA n 
1 204 ASN n 
1 205 GLY n 
1 206 THR n 
1 207 ASN n 
1 208 ILE n 
1 209 SER n 
1 210 GLN n 
1 211 ALA n 
1 212 ILE n 
1 213 GLU n 
1 214 MET n 
1 215 LEU n 
1 216 LEU n 
1 217 ASP n 
1 218 LEU n 
1 219 ILE n 
1 220 MET n 
1 221 LYS n 
1 222 ARG n 
1 223 MET n 
1 224 GLU n 
1 225 ARG n 
1 226 SER n 
1 227 VAL n 
1 228 ASP n 
1 229 LYS n 
1 230 SER n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1  31  human ? 'SYTL2, KIAA1597, SGA72M, SLP2, SLP2A' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? 
? ? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 32 230 ?     ? 'RAB27A, RAB27'                        ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? 
? ? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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  
GNP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'                  ?                               
'C10 H17 N6 O13 P3' 522.196 
GOL non-polymer         . GLYCEROL                                                       'GLYCERIN; PROPANE-1,2,3-TRIOL' 
'C3 H8 O3'          92.094  
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 
MG  non-polymer         . 'MAGNESIUM ION'                                                ?                               'Mg 2' 
24.305  
PHE 'L-peptide linking' y PHENYLALANINE                                                  ?                               
'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                                        ?                               
'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                                                         ?                               
'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                                                      ?                               
'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                     ?                               
'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                                       ?                               
'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                                         ?                               
'C5 H11 N O2'       117.146 
WTK non-polymer         . '~{N}-(3-methoxy-4-pyrrolidin-1-ylsulfonyl-phenyl)propanamide' WT6                             
'C14 H20 N2 O4 S'   312.385 
# 
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   GLY 1   -38 -38 GLY GLY A . n 
A 1 2   HIS 2   -37 -37 HIS HIS A . n 
A 1 3   MET 3   -36 -36 MET MET A . n 
A 1 4   SER 4   -35 -35 SER SER A . n 
A 1 5   PHE 5   -34 -34 PHE PHE A . n 
A 1 6   LEU 6   -33 -33 LEU LEU A . n 
A 1 7   THR 7   -32 -32 THR THR A . n 
A 1 8   GLU 8   -31 -31 GLU GLU A . n 
A 1 9   GLU 9   -30 -30 GLU GLU A . n 
A 1 10  GLU 10  -29 -29 GLU GLU A . n 
A 1 11  GLN 11  -28 -28 GLN GLN A . n 
A 1 12  GLU 12  -27 -27 GLU GLU A . n 
A 1 13  ALA 13  -26 -26 ALA ALA A . n 
A 1 14  ILE 14  -25 -25 ILE ILE A . n 
A 1 15  MET 15  -24 -24 MET MET A . n 
A 1 16  LYS 16  -23 -23 LYS LYS A . n 
A 1 17  VAL 17  -22 -22 VAL VAL A . n 
A 1 18  LEU 18  -21 -21 LEU LEU A . n 
A 1 19  GLN 19  -20 -20 GLN GLN A . n 
A 1 20  ARG 20  -19 -19 ARG ARG A . n 
A 1 21  ASP 21  -18 -18 ASP ASP A . n 
A 1 22  ALA 22  -17 -17 ALA ALA A . n 
A 1 23  ALA 23  -16 -16 ALA ALA A . n 
A 1 24  LEU 24  -15 -15 LEU LEU A . n 
A 1 25  LYS 25  -14 -14 LYS LYS A . n 
A 1 26  ARG 26  -13 -13 ARG ARG A . n 
A 1 27  ALA 27  -12 -12 ALA ALA A . n 
A 1 28  GLU 28  -11 -11 GLU GLU A . n 
A 1 29  GLU 29  -10 -10 GLU GLU A . n 
A 1 30  GLU 30  -9  -9  GLU GLU A . n 
A 1 31  ARG 31  -9  ?   ?   ?   A A n 
A 1 32  GLY 32  -9  ?   ?   ?   A B n 
A 1 33  SER 33  -9  ?   ?   ?   A C n 
A 1 34  GLY 34  -9  ?   ?   ?   A D n 
A 1 35  SER 35  -9  ?   ?   ?   A E n 
A 1 36  GLY 36  -9  ?   ?   ?   A F n 
A 1 37  SER 37  -9  ?   ?   ?   A G n 
A 1 38  GLY 38  -9  ?   ?   ?   A H n 
A 1 39  MET 39  -9  ?   ?   ?   A I n 
A 1 40  SER 40  -9  ?   ?   ?   A J n 
A 1 41  ASP 41  -9  ?   ?   ?   A K n 
A 1 42  GLY 42  -9  ?   ?   ?   A L n 
A 1 43  ASP 43  -8  5   ASP ASP A . n 
A 1 44  TYR 44  -7  6   TYR TYR A . n 
A 1 45  ASP 45  -6  7   ASP ASP A . n 
A 1 46  TYR 46  -5  8   TYR TYR A . n 
A 1 47  LEU 47  -4  9   LEU LEU A . n 
A 1 48  ILE 48  -3  10  ILE ILE A . n 
A 1 49  LYS 49  -2  11  LYS LYS A . n 
A 1 50  PHE 50  -1  12  PHE PHE A . n 
A 1 51  LEU 51  0   13  LEU LEU A . n 
A 1 52  ALA 52  1   14  ALA ALA A . n 
A 1 53  LEU 53  2   15  LEU LEU A . n 
A 1 54  GLY 54  3   16  GLY GLY A . n 
A 1 55  ASP 55  4   17  ASP ASP A . n 
A 1 56  SER 56  5   18  SER SER A . n 
A 1 57  GLY 57  6   19  GLY GLY A . n 
A 1 58  VAL 58  7   20  VAL VAL A . n 
A 1 59  GLY 59  8   21  GLY GLY A . n 
A 1 60  LYS 60  9   22  LYS LYS A . n 
A 1 61  THR 61  10  23  THR THR A . n 
A 1 62  SER 62  11  24  SER SER A . n 
A 1 63  VAL 63  12  25  VAL VAL A . n 
A 1 64  LEU 64  13  26  LEU LEU A . n 
A 1 65  TYR 65  14  27  TYR TYR A . n 
A 1 66  GLN 66  15  28  GLN GLN A . n 
A 1 67  TYR 67  16  29  TYR TYR A . n 
A 1 68  THR 68  17  30  THR THR A . n 
A 1 69  ASP 69  18  31  ASP ASP A . n 
A 1 70  GLY 70  19  32  GLY GLY A . n 
A 1 71  LYS 71  20  33  LYS LYS A . n 
A 1 72  PHE 72  21  34  PHE PHE A . n 
A 1 73  ASN 73  22  35  ASN ASN A . n 
A 1 74  SER 74  23  36  SER SER A . n 
A 1 75  LYS 75  24  37  LYS LYS A . n 
A 1 76  PHE 76  25  38  PHE PHE A . n 
A 1 77  ILE 77  26  39  ILE ILE A . n 
A 1 78  THR 78  27  40  THR THR A . n 
A 1 79  THR 79  28  41  THR THR A . n 
A 1 80  VAL 80  29  42  VAL VAL A . n 
A 1 81  GLY 81  30  43  GLY GLY A . n 
A 1 82  ILE 82  31  44  ILE ILE A . n 
A 1 83  ASP 83  32  45  ASP ASP A . n 
A 1 84  PHE 84  33  46  PHE PHE A . n 
A 1 85  ARG 85  34  47  ARG ARG A . n 
A 1 86  GLU 86  35  48  GLU GLU A . n 
A 1 87  LYS 87  36  49  LYS LYS A . n 
A 1 88  ARG 88  37  50  ARG ARG A . n 
A 1 89  VAL 89  38  51  VAL VAL A . n 
A 1 90  VAL 90  39  52  VAL VAL A . n 
A 1 91  TYR 91  40  53  TYR TYR A . n 
A 1 92  ARG 92  41  54  ARG ARG A . n 
A 1 93  ALA 93  42  55  ALA ALA A . n 
A 1 94  SER 94  43  56  SER SER A . n 
A 1 95  GLY 95  44  57  GLY GLY A . n 
A 1 96  PRO 96  45  58  PRO PRO A . n 
A 1 97  ASP 97  46  59  ASP ASP A . n 
A 1 98  GLY 98  47  60  GLY GLY A . n 
A 1 99  ALA 99  48  61  ALA ALA A . n 
A 1 100 THR 100 49  62  THR THR A . n 
A 1 101 GLY 101 50  63  GLY GLY A . n 
A 1 102 ARG 102 51  64  ARG ARG A . n 
A 1 103 GLY 103 52  65  GLY GLY A . n 
A 1 104 GLN 104 53  66  GLN GLN A . n 
A 1 105 ARG 105 54  67  ARG ARG A . n 
A 1 106 ILE 106 55  68  ILE ILE A . n 
A 1 107 HIS 107 56  69  HIS HIS A . n 
A 1 108 LEU 108 57  70  LEU LEU A . n 
A 1 109 GLN 109 58  71  GLN GLN A . n 
A 1 110 LEU 110 59  72  LEU LEU A . n 
A 1 111 TRP 111 60  73  TRP TRP A . n 
A 1 112 ASP 112 61  74  ASP ASP A . n 
A 1 113 THR 113 62  75  THR THR A . n 
A 1 114 ALA 114 63  76  ALA ALA A . n 
A 1 115 GLY 115 64  77  GLY GLY A . n 
A 1 116 LEU 116 65  78  LEU LEU A . n 
A 1 117 GLU 117 66  79  GLU GLU A . n 
A 1 118 ARG 118 67  80  ARG ARG A . n 
A 1 119 PHE 119 68  81  PHE PHE A . n 
A 1 120 ARG 120 69  82  ARG ARG A . n 
A 1 121 SER 121 70  83  SER SER A . n 
A 1 122 LEU 122 71  84  LEU LEU A . n 
A 1 123 THR 123 72  85  THR THR A . n 
A 1 124 THR 124 73  86  THR THR A . n 
A 1 125 ALA 125 74  87  ALA ALA A . n 
A 1 126 PHE 126 75  88  PHE PHE A . n 
A 1 127 PHE 127 76  89  PHE PHE A . n 
A 1 128 ARG 128 77  90  ARG ARG A . n 
A 1 129 ASP 129 78  91  ASP ASP A . n 
A 1 130 ALA 130 79  92  ALA ALA A . n 
A 1 131 MET 131 80  93  MET MET A . n 
A 1 132 GLY 132 81  94  GLY GLY A . n 
A 1 133 PHE 133 82  95  PHE PHE A . n 
A 1 134 LEU 134 83  96  LEU LEU A . n 
A 1 135 LEU 135 84  97  LEU LEU A . n 
A 1 136 LEU 136 85  98  LEU LEU A . n 
A 1 137 PHE 137 86  99  PHE PHE A . n 
A 1 138 ASP 138 87  100 ASP ASP A . n 
A 1 139 LEU 139 88  101 LEU LEU A . n 
A 1 140 THR 140 89  102 THR THR A . n 
A 1 141 ASN 141 90  103 ASN ASN A . n 
A 1 142 GLU 142 91  104 GLU GLU A . n 
A 1 143 GLN 143 92  105 GLN GLN A . n 
A 1 144 SER 144 93  106 SER SER A . n 
A 1 145 PHE 145 94  107 PHE PHE A . n 
A 1 146 LEU 146 95  108 LEU LEU A . n 
A 1 147 ASN 147 96  109 ASN ASN A . n 
A 1 148 VAL 148 97  110 VAL VAL A . n 
A 1 149 ARG 149 98  111 ARG ARG A . n 
A 1 150 ASN 150 99  112 ASN ASN A . n 
A 1 151 TRP 151 100 113 TRP TRP A . n 
A 1 152 ILE 152 101 114 ILE ILE A . n 
A 1 153 SER 153 102 115 SER SER A . n 
A 1 154 GLN 154 103 116 GLN GLN A . n 
A 1 155 LEU 155 104 117 LEU LEU A . n 
A 1 156 GLN 156 105 118 GLN GLN A . n 
A 1 157 MET 157 106 119 MET MET A . n 
A 1 158 HIS 158 107 120 HIS HIS A . n 
A 1 159 ALA 159 108 121 ALA ALA A . n 
A 1 160 TYR 160 109 122 TYR TYR A . n 
A 1 161 CYS 161 110 123 CYS C13 A . n 
A 1 162 GLU 162 111 124 GLU GLU A . n 
A 1 163 ASN 163 112 125 ASN ASN A . n 
A 1 164 PRO 164 113 126 PRO PRO A . n 
A 1 165 ASP 165 114 127 ASP ASP A . n 
A 1 166 ILE 166 115 128 ILE ILE A . n 
A 1 167 VAL 167 116 129 VAL VAL A . n 
A 1 168 LEU 168 117 130 LEU LEU A . n 
A 1 169 CYS 169 118 131 CYS CYS A . n 
A 1 170 GLY 170 119 132 GLY GLY A . n 
A 1 171 ASN 171 120 133 ASN ASN A . n 
A 1 172 LYS 172 121 134 LYS LYS A . n 
A 1 173 SER 173 122 135 SER SER A . n 
A 1 174 ASP 174 123 136 ASP ASP A . n 
A 1 175 LEU 175 124 137 LEU LEU A . n 
A 1 176 GLU 176 125 138 GLU GLU A . n 
A 1 177 ASP 177 126 139 ASP ASP A . n 
A 1 178 GLN 178 127 140 GLN GLN A . n 
A 1 179 ARG 179 128 141 ARG ARG A . n 
A 1 180 VAL 180 129 142 VAL VAL A . n 
A 1 181 VAL 181 130 143 VAL VAL A . n 
A 1 182 LYS 182 131 144 LYS LYS A . n 
A 1 183 GLU 183 132 145 GLU GLU A . n 
A 1 184 GLU 184 133 146 GLU GLU A . n 
A 1 185 GLU 185 134 147 GLU GLU A . n 
A 1 186 ALA 186 135 148 ALA ALA A . n 
A 1 187 ILE 187 136 149 ILE ILE A . n 
A 1 188 ALA 188 137 150 ALA ALA A . n 
A 1 189 LEU 189 138 151 LEU LEU A . n 
A 1 190 ALA 190 139 152 ALA ALA A . n 
A 1 191 GLU 191 140 153 GLU GLU A . n 
A 1 192 LYS 192 141 154 LYS LYS A . n 
A 1 193 TYR 193 142 155 TYR TYR A . n 
A 1 194 GLY 194 143 156 GLY GLY A . n 
A 1 195 ILE 195 144 157 ILE ILE A . n 
A 1 196 PRO 196 145 158 PRO PRO A . n 
A 1 197 TYR 197 146 159 TYR TYR A . n 
A 1 198 PHE 198 147 160 PHE PHE A . n 
A 1 199 GLU 199 148 161 GLU GLU A . n 
A 1 200 THR 200 149 162 THR THR A . n 
A 1 201 SER 201 150 163 SER SER A . n 
A 1 202 ALA 202 151 164 ALA ALA A . n 
A 1 203 ALA 203 152 165 ALA ALA A . n 
A 1 204 ASN 204 153 166 ASN ASN A . n 
A 1 205 GLY 205 154 167 GLY GLY A . n 
A 1 206 THR 206 155 168 THR THR A . n 
A 1 207 ASN 207 156 169 ASN ASN A . n 
A 1 208 ILE 208 157 170 ILE ILE A . n 
A 1 209 SER 209 158 171 SER SER A . n 
A 1 210 GLN 210 159 172 GLN GLN A . n 
A 1 211 ALA 211 160 173 ALA ALA A . n 
A 1 212 ILE 212 161 174 ILE ILE A . n 
A 1 213 GLU 213 162 175 GLU GLU A . n 
A 1 214 MET 214 163 176 MET MET A . n 
A 1 215 LEU 215 164 177 LEU LEU A . n 
A 1 216 LEU 216 165 178 LEU LEU A . n 
A 1 217 ASP 217 166 179 ASP ASP A . n 
A 1 218 LEU 218 167 180 LEU LEU A . n 
A 1 219 ILE 219 168 181 ILE ILE A . n 
A 1 220 MET 220 169 182 MET MET A . n 
A 1 221 LYS 221 170 183 LYS LYS A . n 
A 1 222 ARG 222 171 184 ARG ARG A . n 
A 1 223 MET 223 172 185 MET MET A . n 
A 1 224 GLU 224 173 186 GLU GLU A . n 
A 1 225 ARG 225 174 187 ARG ARG A . n 
A 1 226 SER 226 175 188 SER SER A . n 
A 1 227 VAL 227 176 ?   ?   ?   A . n 
A 1 228 ASP 228 177 ?   ?   ?   A . n 
A 1 229 LYS 229 178 ?   ?   ?   A . n 
A 1 230 SER 230 179 ?   ?   ?   A . n 
B 1 1   GLY 1   -38 ?   ?   ?   B . n 
B 1 2   HIS 2   -37 -37 HIS HIS B . n 
B 1 3   MET 3   -36 -36 MET MET B . n 
B 1 4   SER 4   -35 -35 SER SER B . n 
B 1 5   PHE 5   -34 -34 PHE PHE B . n 
B 1 6   LEU 6   -33 -33 LEU LEU B . n 
B 1 7   THR 7   -32 -32 THR THR B . n 
B 1 8   GLU 8   -31 -31 GLU GLU B . n 
B 1 9   GLU 9   -30 -30 GLU GLU B . n 
B 1 10  GLU 10  -29 -29 GLU GLU B . n 
B 1 11  GLN 11  -28 -28 GLN GLN B . n 
B 1 12  GLU 12  -27 -27 GLU GLU B . n 
B 1 13  ALA 13  -26 -26 ALA ALA B . n 
B 1 14  ILE 14  -25 -25 ILE ILE B . n 
B 1 15  MET 15  -24 -24 MET MET B . n 
B 1 16  LYS 16  -23 -23 LYS LYS B . n 
B 1 17  VAL 17  -22 -22 VAL VAL B . n 
B 1 18  LEU 18  -21 -21 LEU LEU B . n 
B 1 19  GLN 19  -20 -20 GLN GLN B . n 
B 1 20  ARG 20  -19 -19 ARG ARG B . n 
B 1 21  ASP 21  -18 -18 ASP ASP B . n 
B 1 22  ALA 22  -17 -17 ALA ALA B . n 
B 1 23  ALA 23  -16 -16 ALA ALA B . n 
B 1 24  LEU 24  -15 -15 LEU LEU B . n 
B 1 25  LYS 25  -14 -14 LYS LYS B . n 
B 1 26  ARG 26  -13 -13 ARG ARG B . n 
B 1 27  ALA 27  -12 -12 ALA ALA B . n 
B 1 28  GLU 28  -11 -11 GLU GLU B . n 
B 1 29  GLU 29  -10 -10 GLU GLU B . n 
B 1 30  GLU 30  -9  -9  GLU GLU B . n 
B 1 31  ARG 31  -9  ?   ?   ?   B A n 
B 1 32  GLY 32  -9  ?   ?   ?   B B n 
B 1 33  SER 33  -9  ?   ?   ?   B C n 
B 1 34  GLY 34  -9  ?   ?   ?   B D n 
B 1 35  SER 35  -9  ?   ?   ?   B E n 
B 1 36  GLY 36  -9  ?   ?   ?   B F n 
B 1 37  SER 37  -9  ?   ?   ?   B G n 
B 1 38  GLY 38  -9  ?   ?   ?   B H n 
B 1 39  MET 39  -9  ?   ?   ?   B I n 
B 1 40  SER 40  -9  ?   ?   ?   B J n 
B 1 41  ASP 41  -9  ?   ?   ?   B K n 
B 1 42  GLY 42  -9  ?   ?   ?   B L n 
B 1 43  ASP 43  -9  ?   ?   ?   B M n 
B 1 44  TYR 44  -8  6   TYR TYR B . n 
B 1 45  ASP 45  -7  7   ASP ASP B . n 
B 1 46  TYR 46  -6  8   TYR TYR B . n 
B 1 47  LEU 47  -5  9   LEU LEU B . n 
B 1 48  ILE 48  -4  10  ILE ILE B . n 
B 1 49  LYS 49  -3  11  LYS LYS B . n 
B 1 50  PHE 50  -2  12  PHE PHE B . n 
B 1 51  LEU 51  -1  13  LEU LEU B . n 
B 1 52  ALA 52  0   14  ALA ALA B . n 
B 1 53  LEU 53  1   15  LEU LEU B . n 
B 1 54  GLY 54  2   16  GLY GLY B . n 
B 1 55  ASP 55  3   17  ASP ASP B . n 
B 1 56  SER 56  4   18  SER SER B . n 
B 1 57  GLY 57  5   19  GLY GLY B . n 
B 1 58  VAL 58  6   20  VAL VAL B . n 
B 1 59  GLY 59  7   21  GLY GLY B . n 
B 1 60  LYS 60  8   22  LYS LYS B . n 
B 1 61  THR 61  9   23  THR THR B . n 
B 1 62  SER 62  10  24  SER SER B . n 
B 1 63  VAL 63  11  25  VAL VAL B . n 
B 1 64  LEU 64  12  26  LEU LEU B . n 
B 1 65  TYR 65  13  27  TYR TYR B . n 
B 1 66  GLN 66  14  28  GLN GLN B . n 
B 1 67  TYR 67  15  29  TYR TYR B . n 
B 1 68  THR 68  16  30  THR THR B . n 
B 1 69  ASP 69  17  31  ASP ASP B . n 
B 1 70  GLY 70  18  32  GLY GLY B . n 
B 1 71  LYS 71  19  33  LYS LYS B . n 
B 1 72  PHE 72  20  34  PHE PHE B . n 
B 1 73  ASN 73  21  35  ASN ASN B . n 
B 1 74  SER 74  22  36  SER SER B . n 
B 1 75  LYS 75  23  37  LYS LYS B . n 
B 1 76  PHE 76  24  38  PHE PHE B . n 
B 1 77  ILE 77  25  39  ILE ILE B . n 
B 1 78  THR 78  26  40  THR THR B . n 
B 1 79  THR 79  27  41  THR THR B . n 
B 1 80  VAL 80  28  42  VAL VAL B . n 
B 1 81  GLY 81  29  43  GLY GLY B . n 
B 1 82  ILE 82  30  44  ILE ILE B . n 
B 1 83  ASP 83  31  45  ASP ASP B . n 
B 1 84  PHE 84  32  46  PHE PHE B . n 
B 1 85  ARG 85  33  47  ARG ARG B . n 
B 1 86  GLU 86  34  48  GLU GLU B . n 
B 1 87  LYS 87  35  49  LYS LYS B . n 
B 1 88  ARG 88  36  50  ARG ARG B . n 
B 1 89  VAL 89  37  51  VAL VAL B . n 
B 1 90  VAL 90  38  52  VAL VAL B . n 
B 1 91  TYR 91  39  53  TYR TYR B . n 
B 1 92  ARG 92  40  54  ARG ARG B . n 
B 1 93  ALA 93  41  55  ALA ALA B . n 
B 1 94  SER 94  42  56  SER SER B . n 
B 1 95  GLY 95  43  57  GLY GLY B . n 
B 1 96  PRO 96  44  58  PRO PRO B . n 
B 1 97  ASP 97  45  59  ASP ASP B . n 
B 1 98  GLY 98  46  60  GLY GLY B . n 
B 1 99  ALA 99  47  61  ALA ALA B . n 
B 1 100 THR 100 48  62  THR THR B . n 
B 1 101 GLY 101 49  63  GLY GLY B . n 
B 1 102 ARG 102 50  64  ARG ARG B . n 
B 1 103 GLY 103 51  65  GLY GLY B . n 
B 1 104 GLN 104 52  66  GLN GLN B . n 
B 1 105 ARG 105 53  67  ARG ARG B . n 
B 1 106 ILE 106 54  68  ILE ILE B . n 
B 1 107 HIS 107 55  69  HIS HIS B . n 
B 1 108 LEU 108 56  70  LEU LEU B . n 
B 1 109 GLN 109 57  71  GLN GLN B . n 
B 1 110 LEU 110 58  72  LEU LEU B . n 
B 1 111 TRP 111 59  73  TRP TRP B . n 
B 1 112 ASP 112 60  74  ASP ASP B . n 
B 1 113 THR 113 61  75  THR THR B . n 
B 1 114 ALA 114 62  76  ALA ALA B . n 
B 1 115 GLY 115 63  77  GLY GLY B . n 
B 1 116 LEU 116 64  78  LEU LEU B . n 
B 1 117 GLU 117 65  79  GLU GLU B . n 
B 1 118 ARG 118 66  80  ARG ARG B . n 
B 1 119 PHE 119 67  81  PHE PHE B . n 
B 1 120 ARG 120 68  82  ARG ARG B . n 
B 1 121 SER 121 69  83  SER SER B . n 
B 1 122 LEU 122 70  84  LEU LEU B . n 
B 1 123 THR 123 71  85  THR THR B . n 
B 1 124 THR 124 72  86  THR THR B . n 
B 1 125 ALA 125 73  87  ALA ALA B . n 
B 1 126 PHE 126 74  88  PHE PHE B . n 
B 1 127 PHE 127 75  89  PHE PHE B . n 
B 1 128 ARG 128 76  90  ARG ARG B . n 
B 1 129 ASP 129 77  91  ASP ASP B . n 
B 1 130 ALA 130 78  92  ALA ALA B . n 
B 1 131 MET 131 79  93  MET MET B . n 
B 1 132 GLY 132 80  94  GLY GLY B . n 
B 1 133 PHE 133 81  95  PHE PHE B . n 
B 1 134 LEU 134 82  96  LEU LEU B . n 
B 1 135 LEU 135 83  97  LEU LEU B . n 
B 1 136 LEU 136 84  98  LEU LEU B . n 
B 1 137 PHE 137 85  99  PHE PHE B . n 
B 1 138 ASP 138 86  100 ASP ASP B . n 
B 1 139 LEU 139 87  101 LEU LEU B . n 
B 1 140 THR 140 88  102 THR THR B . n 
B 1 141 ASN 141 89  103 ASN ASN B . n 
B 1 142 GLU 142 90  104 GLU GLU B . n 
B 1 143 GLN 143 91  105 GLN GLN B . n 
B 1 144 SER 144 92  106 SER SER B . n 
B 1 145 PHE 145 93  107 PHE PHE B . n 
B 1 146 LEU 146 94  108 LEU LEU B . n 
B 1 147 ASN 147 95  109 ASN ASN B . n 
B 1 148 VAL 148 96  110 VAL VAL B . n 
B 1 149 ARG 149 97  111 ARG ARG B . n 
B 1 150 ASN 150 98  112 ASN ASN B . n 
B 1 151 TRP 151 99  113 TRP TRP B . n 
B 1 152 ILE 152 100 114 ILE ILE B . n 
B 1 153 SER 153 101 115 SER SER B . n 
B 1 154 GLN 154 102 116 GLN GLN B . n 
B 1 155 LEU 155 103 117 LEU LEU B . n 
B 1 156 GLN 156 104 118 GLN GLN B . n 
B 1 157 MET 157 105 119 MET MET B . n 
B 1 158 HIS 158 106 120 HIS HIS B . n 
B 1 159 ALA 159 107 121 ALA ALA B . n 
B 1 160 TYR 160 108 122 TYR TYR B . n 
B 1 161 CYS 161 109 123 CYS C13 B . n 
B 1 162 GLU 162 110 124 GLU GLU B . n 
B 1 163 ASN 163 111 125 ASN ASN B . n 
B 1 164 PRO 164 112 126 PRO PRO B . n 
B 1 165 ASP 165 113 127 ASP ASP B . n 
B 1 166 ILE 166 114 128 ILE ILE B . n 
B 1 167 VAL 167 115 129 VAL VAL B . n 
B 1 168 LEU 168 116 130 LEU LEU B . n 
B 1 169 CYS 169 117 131 CYS CYS B . n 
B 1 170 GLY 170 118 132 GLY GLY B . n 
B 1 171 ASN 171 119 133 ASN ASN B . n 
B 1 172 LYS 172 120 134 LYS LYS B . n 
B 1 173 SER 173 121 135 SER SER B . n 
B 1 174 ASP 174 122 136 ASP ASP B . n 
B 1 175 LEU 175 123 137 LEU LEU B . n 
B 1 176 GLU 176 124 138 GLU GLU B . n 
B 1 177 ASP 177 125 139 ASP ASP B . n 
B 1 178 GLN 178 126 140 GLN GLN B . n 
B 1 179 ARG 179 127 141 ARG ARG B . n 
B 1 180 VAL 180 128 142 VAL VAL B . n 
B 1 181 VAL 181 129 143 VAL VAL B . n 
B 1 182 LYS 182 130 144 LYS LYS B . n 
B 1 183 GLU 183 131 145 GLU GLU B . n 
B 1 184 GLU 184 132 146 GLU GLU B . n 
B 1 185 GLU 185 133 147 GLU GLU B . n 
B 1 186 ALA 186 134 148 ALA ALA B . n 
B 1 187 ILE 187 135 149 ILE ILE B . n 
B 1 188 ALA 188 136 150 ALA ALA B . n 
B 1 189 LEU 189 137 151 LEU LEU B . n 
B 1 190 ALA 190 138 152 ALA ALA B . n 
B 1 191 GLU 191 139 153 GLU GLU B . n 
B 1 192 LYS 192 140 154 LYS LYS B . n 
B 1 193 TYR 193 141 155 TYR TYR B . n 
B 1 194 GLY 194 142 156 GLY GLY B . n 
B 1 195 ILE 195 143 157 ILE ILE B . n 
B 1 196 PRO 196 144 158 PRO PRO B . n 
B 1 197 TYR 197 145 159 TYR TYR B . n 
B 1 198 PHE 198 146 160 PHE PHE B . n 
B 1 199 GLU 199 147 161 GLU GLU B . n 
B 1 200 THR 200 148 162 THR THR B . n 
B 1 201 SER 201 149 163 SER SER B . n 
B 1 202 ALA 202 150 164 ALA ALA B . n 
B 1 203 ALA 203 151 165 ALA ALA B . n 
B 1 204 ASN 204 152 166 ASN ASN B . n 
B 1 205 GLY 205 153 167 GLY GLY B . n 
B 1 206 THR 206 154 168 THR THR B . n 
B 1 207 ASN 207 155 169 ASN ASN B . n 
B 1 208 ILE 208 156 170 ILE ILE B . n 
B 1 209 SER 209 157 171 SER SER B . n 
B 1 210 GLN 210 158 172 GLN GLN B . n 
B 1 211 ALA 211 159 173 ALA ALA B . n 
B 1 212 ILE 212 160 174 ILE ILE B . n 
B 1 213 GLU 213 161 175 GLU GLU B . n 
B 1 214 MET 214 162 176 MET MET B . n 
B 1 215 LEU 215 163 177 LEU LEU B . n 
B 1 216 LEU 216 164 178 LEU LEU B . n 
B 1 217 ASP 217 165 179 ASP ASP B . n 
B 1 218 LEU 218 166 180 LEU LEU B . n 
B 1 219 ILE 219 167 181 ILE ILE B . n 
B 1 220 MET 220 168 182 MET MET B . n 
B 1 221 LYS 221 169 183 LYS LYS B . n 
B 1 222 ARG 222 170 184 ARG ARG B . n 
B 1 223 MET 223 171 185 MET MET B . n 
B 1 224 GLU 224 172 186 GLU GLU B . n 
B 1 225 ARG 225 173 187 ARG ARG B . n 
B 1 226 SER 226 174 188 SER SER B . n 
B 1 227 VAL 227 175 ?   ?   ?   B . n 
B 1 228 ASP 228 176 ?   ?   ?   B . n 
B 1 229 LYS 229 177 ?   ?   ?   B . n 
B 1 230 SER 230 178 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WTK 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WTK 
_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 
C 2 GNP 1  201 201 GNP GNP A . 
D 3 GOL 1  202 301 GOL GOL A . 
E 3 GOL 1  203 401 GOL GOL A . 
F 3 GOL 1  204 501 GOL GOL A . 
G 3 GOL 1  205 601 GOL GOL A . 
H 3 GOL 1  206 701 GOL GOL A . 
I 3 GOL 1  207 801 GOL GOL A . 
J 4 WTK 1  208 123 WTK C13 A . 
K 5 MG  1  209 3   MG  MG  A . 
L 2 GNP 1  201 201 GNP GNP B . 
M 3 GOL 1  202 301 GOL GOL B . 
N 3 GOL 1  203 401 GOL GOL B . 
O 3 GOL 1  204 501 GOL GOL B . 
P 3 GOL 1  205 601 GOL GOL B . 
Q 3 GOL 1  206 701 GOL GOL B . 
R 3 GOL 1  207 801 GOL GOL B . 
S 4 WTK 1  208 123 WTK C13 B . 
T 5 MG  1  209 4   MG  MG  B . 
U 6 HOH 1  301 59  HOH HOH A . 
U 6 HOH 2  302 2   HOH HOH A . 
U 6 HOH 3  303 12  HOH HOH A . 
U 6 HOH 4  304 1   HOH HOH A . 
U 6 HOH 5  305 30  HOH HOH A . 
U 6 HOH 6  306 32  HOH HOH A . 
U 6 HOH 7  307 33  HOH HOH A . 
U 6 HOH 8  308 11  HOH HOH A . 
U 6 HOH 9  309 7   HOH HOH A . 
U 6 HOH 10 310 5   HOH HOH A . 
U 6 HOH 11 311 14  HOH HOH A . 
U 6 HOH 12 312 13  HOH HOH A . 
U 6 HOH 13 313 55  HOH HOH A . 
U 6 HOH 14 314 56  HOH HOH A . 
U 6 HOH 15 315 48  HOH HOH A . 
U 6 HOH 16 316 31  HOH HOH A . 
U 6 HOH 17 317 60  HOH HOH A . 
U 6 HOH 18 318 17  HOH HOH A . 
U 6 HOH 19 319 6   HOH HOH A . 
U 6 HOH 20 320 58  HOH HOH A . 
U 6 HOH 21 321 16  HOH HOH A . 
U 6 HOH 22 322 38  HOH HOH A . 
U 6 HOH 23 323 49  HOH HOH A . 
U 6 HOH 24 324 15  HOH HOH A . 
U 6 HOH 25 325 8   HOH HOH A . 
U 6 HOH 26 326 9   HOH HOH A . 
U 6 HOH 27 327 10  HOH HOH A . 
U 6 HOH 28 328 22  HOH HOH A . 
V 6 HOH 1  301 47  HOH HOH B . 
V 6 HOH 2  302 50  HOH HOH B . 
V 6 HOH 3  303 46  HOH HOH B . 
V 6 HOH 4  304 3   HOH HOH B . 
V 6 HOH 5  305 54  HOH HOH B . 
V 6 HOH 6  306 35  HOH HOH B . 
V 6 HOH 7  307 4   HOH HOH B . 
V 6 HOH 8  308 23  HOH HOH B . 
V 6 HOH 9  309 41  HOH HOH B . 
V 6 HOH 10 310 36  HOH HOH B . 
V 6 HOH 11 311 43  HOH HOH B . 
V 6 HOH 12 312 42  HOH HOH B . 
V 6 HOH 13 313 52  HOH HOH B . 
V 6 HOH 14 314 53  HOH HOH B . 
V 6 HOH 15 315 27  HOH HOH B . 
V 6 HOH 16 316 19  HOH HOH B . 
V 6 HOH 17 317 21  HOH HOH B . 
V 6 HOH 18 318 45  HOH HOH B . 
V 6 HOH 19 319 44  HOH HOH B . 
V 6 HOH 20 320 20  HOH HOH B . 
V 6 HOH 21 321 40  HOH HOH B . 
V 6 HOH 22 322 57  HOH HOH B . 
V 6 HOH 23 323 34  HOH HOH B . 
V 6 HOH 24 324 18  HOH HOH B . 
V 6 HOH 25 325 29  HOH HOH B . 
V 6 HOH 26 326 37  HOH HOH B . 
V 6 HOH 27 327 28  HOH HOH B . 
V 6 HOH 28 328 39  HOH HOH B . 
V 6 HOH 29 329 51  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU -30 ? CG  ? A GLU 9   CG  
2  1 Y 1 A GLU -30 ? CD  ? A GLU 9   CD  
3  1 Y 1 A GLU -30 ? OE1 ? A GLU 9   OE1 
4  1 Y 1 A GLU -30 ? OE2 ? A GLU 9   OE2 
5  1 Y 1 A GLU -27 ? CG  ? A GLU 12  CG  
6  1 Y 1 A GLU -27 ? CD  ? A GLU 12  CD  
7  1 Y 1 A GLU -27 ? OE1 ? A GLU 12  OE1 
8  1 Y 1 A GLU -27 ? OE2 ? A GLU 12  OE2 
9  1 Y 1 A ASP -8  ? CG  ? A ASP 43  CG  
10 1 Y 1 A ASP -8  ? OD1 ? A ASP 43  OD1 
11 1 Y 1 A ASP -8  ? OD2 ? A ASP 43  OD2 
12 1 Y 1 A ASP 46  ? CG  ? A ASP 97  CG  
13 1 Y 1 A ASP 46  ? OD1 ? A ASP 97  OD1 
14 1 Y 1 A ASP 46  ? OD2 ? A ASP 97  OD2 
15 1 Y 1 A GLU 66  ? CG  ? A GLU 117 CG  
16 1 Y 1 A GLU 66  ? CD  ? A GLU 117 CD  
17 1 Y 1 A GLU 66  ? OE1 ? A GLU 117 OE1 
18 1 Y 1 A GLU 66  ? OE2 ? A GLU 117 OE2 
19 1 Y 1 A ARG 98  ? CG  ? A ARG 149 CG  
20 1 Y 1 A ARG 98  ? CD  ? A ARG 149 CD  
21 1 Y 1 A ARG 98  ? NE  ? A ARG 149 NE  
22 1 Y 1 A ARG 98  ? CZ  ? A ARG 149 CZ  
23 1 Y 1 A ARG 98  ? NH1 ? A ARG 149 NH1 
24 1 Y 1 A ARG 98  ? NH2 ? A ARG 149 NH2 
25 1 Y 1 A GLU 125 ? CG  ? A GLU 176 CG  
26 1 Y 1 A GLU 125 ? CD  ? A GLU 176 CD  
27 1 Y 1 A GLU 125 ? OE1 ? A GLU 176 OE1 
28 1 Y 1 A GLU 125 ? OE2 ? A GLU 176 OE2 
29 1 Y 1 A LYS 131 ? CG  ? A LYS 182 CG  
30 1 Y 1 A LYS 131 ? CD  ? A LYS 182 CD  
31 1 Y 1 A LYS 131 ? CE  ? A LYS 182 CE  
32 1 Y 1 A LYS 131 ? NZ  ? A LYS 182 NZ  
33 1 Y 1 A GLU 173 ? CG  ? A GLU 224 CG  
34 1 Y 1 A GLU 173 ? CD  ? A GLU 224 CD  
35 1 Y 1 A GLU 173 ? OE1 ? A GLU 224 OE1 
36 1 Y 1 A GLU 173 ? OE2 ? A GLU 224 OE2 
37 1 Y 1 B MET -36 ? CG  ? B MET 3   CG  
38 1 Y 1 B MET -36 ? SD  ? B MET 3   SD  
39 1 Y 1 B MET -36 ? CE  ? B MET 3   CE  
40 1 Y 1 B GLU -31 ? CG  ? B GLU 8   CG  
41 1 Y 1 B GLU -31 ? CD  ? B GLU 8   CD  
42 1 Y 1 B GLU -31 ? OE1 ? B GLU 8   OE1 
43 1 Y 1 B GLU -31 ? OE2 ? B GLU 8   OE2 
44 1 Y 1 B GLU -30 ? CG  ? B GLU 9   CG  
45 1 Y 1 B GLU -30 ? CD  ? B GLU 9   CD  
46 1 Y 1 B GLU -30 ? OE1 ? B GLU 9   OE1 
47 1 Y 1 B GLU -30 ? OE2 ? B GLU 9   OE2 
48 1 Y 1 B GLU -29 ? CG  ? B GLU 10  CG  
49 1 Y 1 B GLU -29 ? CD  ? B GLU 10  CD  
50 1 Y 1 B GLU -29 ? OE1 ? B GLU 10  OE1 
51 1 Y 1 B GLU -29 ? OE2 ? B GLU 10  OE2 
52 1 Y 1 B GLU -27 ? CG  ? B GLU 12  CG  
53 1 Y 1 B GLU -27 ? CD  ? B GLU 12  CD  
54 1 Y 1 B GLU -27 ? OE1 ? B GLU 12  OE1 
55 1 Y 1 B GLU -27 ? OE2 ? B GLU 12  OE2 
56 1 Y 1 B GLU -11 ? CG  ? B GLU 28  CG  
57 1 Y 1 B GLU -11 ? CD  ? B GLU 28  CD  
58 1 Y 1 B GLU -11 ? OE1 ? B GLU 28  OE1 
59 1 Y 1 B GLU -11 ? OE2 ? B GLU 28  OE2 
60 1 Y 1 B GLU 110 ? CG  ? B GLU 162 CG  
61 1 Y 1 B GLU 110 ? CD  ? B GLU 162 CD  
62 1 Y 1 B GLU 110 ? OE1 ? B GLU 162 OE1 
63 1 Y 1 B GLU 110 ? OE2 ? B GLU 162 OE2 
64 1 Y 1 B LYS 130 ? CG  ? B LYS 182 CG  
65 1 Y 1 B LYS 130 ? CD  ? B LYS 182 CD  
66 1 Y 1 B LYS 130 ? CE  ? B LYS 182 CE  
67 1 Y 1 B LYS 130 ? NZ  ? B LYS 182 NZ  
68 1 Y 1 B GLU 139 ? CG  ? B GLU 191 CG  
69 1 Y 1 B GLU 139 ? CD  ? B GLU 191 CD  
70 1 Y 1 B GLU 139 ? OE1 ? B GLU 191 OE1 
71 1 Y 1 B GLU 139 ? OE2 ? B GLU 191 OE2 
72 1 N 0 A WTK 208 ? C13 ? J WTK ?   C13 
# 
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 ? ? ? '(1.17_3644: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                  4 
# 
_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                     8P3I 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.367 
_cell.length_a_esd                 ? 
_cell.length_b                     76.601 
_cell.length_b_esd                 ? 
_cell.length_c                     118.674 
_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                         8P3I 
_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                   8P3I 
_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             2.82 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.35 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.15 M NH4SO4, 0.1 M MES, pH 6.0, 15% PEG 4K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2020-02-06 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9763 
_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 I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9763 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8P3I 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.0 
_reflns.d_resolution_low                               64.36 
_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                                     38565 
_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                           87.99 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.39 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_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                              ? 
_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                        ? 
# 
_reflns_shell.d_res_high                                    2.0 
_reflns_shell.d_res_low                                     2.071 
_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                             3800 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.331 
_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               ? 
# 
_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                                 8P3I 
_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                            2.00 
_refine.ls_d_res_low                             64.36 
_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                     33930 
_refine.ls_number_reflns_R_free                  1757 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    87.98 
_refine.ls_percent_reflns_R_free                 5.18 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2319 
_refine.ls_R_factor_R_free                       0.2801 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2293 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_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                 39.81 
_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                            0.42 
_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                       2.00 
_refine_hist.d_res_low                        64.36 
_refine_hist.number_atoms_solvent             57 
_refine_hist.number_atoms_total               3586 
_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        3391 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         138 
_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' ? 0.008  ? 3575 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.028  ? 4810 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 27.741 ? 515  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.049  ? 519  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 594  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.00 2.05  . . 34  452  17.00  . . . . 0.4726 . . . . . . . . . . . 0.5134 
'X-RAY DIFFRACTION' 2.05 2.11  . . 62  1403 51.00  . . . . 0.4426 . . . . . . . . . . . 0.4742 
'X-RAY DIFFRACTION' 2.11 2.18  . . 135 2238 81.00  . . . . 0.4193 . . . . . . . . . . . 0.4274 
'X-RAY DIFFRACTION' 2.18 2.26  . . 129 2663 95.00  . . . . 0.4097 . . . . . . . . . . . 0.4524 
'X-RAY DIFFRACTION' 2.26 2.35  . . 145 2757 100.00 . . . . 0.3799 . . . . . . . . . . . 0.3741 
'X-RAY DIFFRACTION' 2.35 2.46  . . 150 2787 100.00 . . . . 0.3512 . . . . . . . . . . . 0.3955 
'X-RAY DIFFRACTION' 2.46 2.59  . . 143 2778 100.00 . . . . 0.3160 . . . . . . . . . . . 0.3622 
'X-RAY DIFFRACTION' 2.59 2.75  . . 155 2799 100.00 . . . . 0.2791 . . . . . . . . . . . 0.3445 
'X-RAY DIFFRACTION' 2.75 2.96  . . 146 2811 100.00 . . . . 0.2653 . . . . . . . . . . . 0.3207 
'X-RAY DIFFRACTION' 2.96 3.26  . . 166 2794 100.00 . . . . 0.2281 . . . . . . . . . . . 0.3200 
'X-RAY DIFFRACTION' 3.26 3.73  . . 161 2829 100.00 . . . . 0.1990 . . . . . . . . . . . 0.2786 
'X-RAY DIFFRACTION' 3.73 4.70  . . 156 2876 100.00 . . . . 0.1601 . . . . . . . . . . . 0.2056 
'X-RAY DIFFRACTION' 4.70 64.36 . . 175 2986 100.00 . . . . 0.1887 . . . . . . . . . . . 0.2300 
# 
_struct.entry_id                     8P3I 
_struct.title                        'Fusion hSlp2-a_Rab27A bound to covalent hit fragment IMP-1721' 
_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        8P3I 
_struct_keywords.text            
;Small GTPase, Targeted Covalent Inhibitors, High Throughput screening, Drug Discovery, Vesicle trafficking, Breast Cancer, CYTOSOLIC PROTEIN
;
_struct_keywords.pdbx_keywords   'CYTOSOLIC 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 3 ? 
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 5 ? 
L N N 2 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 3 ? 
S N N 4 ? 
T N N 5 ? 
U N N 6 ? 
V N N 6 ? 
# 
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 SYTL2_HUMAN Q9HCH5 ? 1 SFLTEEEQEAIMKVLQRDAALKRAEEER 5 
2 UNP RB27A_HUMAN P51159 ? 1 
;MSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTVGIDFREKRVVYRASGPDGATGRGQRIHLQLWDTAGQER
FRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMHAYCENPDIVLCGNKSDLEDQRVVKEEEAIALAEKYGIPYF
ETSAANGTNISQAIEMLLDLIMKRMERCVDKS
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8P3I A 4  ? 31  A Q9HCH5 5 ? 32  ? -35 -9  
2 2 8P3I A 39 I 230 ? P51159 1 ? 192 ? -9  179 
3 1 8P3I B 4  ? 31  A Q9HCH5 5 ? 32  ? -35 -9  
4 2 8P3I B 39 I 230 ? P51159 1 ? 192 ? -9  178 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8P3I GLY A 1   ? UNP Q9HCH5 ?   ?   'expression tag'      -38 1  
1 8P3I HIS A 2   ? UNP Q9HCH5 ?   ?   'expression tag'      -37 2  
1 8P3I MET A 3   ? UNP Q9HCH5 ?   ?   'expression tag'      -36 3  
1 8P3I GLY A 32  B UNP Q9HCH5 ?   ?   linker                -9  4  
1 8P3I SER A 33  C UNP Q9HCH5 ?   ?   linker                -9  5  
1 8P3I GLY A 34  D UNP Q9HCH5 ?   ?   linker                -9  6  
1 8P3I SER A 35  E UNP Q9HCH5 ?   ?   linker                -9  7  
1 8P3I GLY A 36  F UNP Q9HCH5 ?   ?   linker                -9  8  
1 8P3I SER A 37  G UNP Q9HCH5 ?   ?   linker                -9  9  
1 8P3I GLY A 38  H UNP Q9HCH5 ?   ?   linker                -9  10 
2 8P3I LEU A 116 ? UNP P51159 GLN 78  'engineered mutation' 65  11 
2 8P3I SER A 226 ? UNP P51159 CYS 188 'engineered mutation' 175 12 
3 8P3I GLY B 1   ? UNP Q9HCH5 ?   ?   'expression tag'      -38 13 
3 8P3I HIS B 2   ? UNP Q9HCH5 ?   ?   'expression tag'      -37 14 
3 8P3I MET B 3   ? UNP Q9HCH5 ?   ?   'expression tag'      -36 15 
3 8P3I GLY B 32  B UNP Q9HCH5 ?   ?   linker                -9  16 
3 8P3I SER B 33  C UNP Q9HCH5 ?   ?   linker                -9  17 
3 8P3I GLY B 34  D UNP Q9HCH5 ?   ?   linker                -9  18 
3 8P3I SER B 35  E UNP Q9HCH5 ?   ?   linker                -9  19 
3 8P3I GLY B 36  F UNP Q9HCH5 ?   ?   linker                -9  20 
3 8P3I SER B 37  G UNP Q9HCH5 ?   ?   linker                -9  21 
3 8P3I GLY B 38  H UNP Q9HCH5 ?   ?   linker                -9  22 
4 8P3I LEU B 116 ? UNP P51159 GLN 78  'engineered mutation' 64  23 
4 8P3I SER B 226 ? UNP P51159 CYS 188 'engineered mutation' 174 24 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 7880  ? 
1 MORE         -52   ? 
1 'SSA (A^2)'  19790 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 7   ? GLU A 29  ? THR A -32 GLU A -10 1 ? 23 
HELX_P HELX_P2  AA2 GLY A 59  ? GLY A 70  ? GLY A 8   GLY A 19  1 ? 12 
HELX_P HELX_P3  AA3 LEU A 116 ? ARG A 118 ? LEU A 65  ARG A 67  5 ? 3  
HELX_P HELX_P4  AA4 PHE A 119 ? ALA A 125 ? PHE A 68  ALA A 74  1 ? 7  
HELX_P HELX_P5  AA5 PHE A 126 ? ASP A 129 ? PHE A 75  ASP A 78  5 ? 4  
HELX_P HELX_P6  AA6 ASN A 141 ? ASN A 147 ? ASN A 90  ASN A 96  1 ? 7  
HELX_P HELX_P7  AA7 ASN A 147 ? ALA A 159 ? ASN A 96  ALA A 108 1 ? 13 
HELX_P HELX_P8  AA8 LEU A 175 ? ARG A 179 ? LEU A 124 ARG A 128 5 ? 5  
HELX_P HELX_P9  AA9 LYS A 182 ? GLY A 194 ? LYS A 131 GLY A 143 1 ? 13 
HELX_P HELX_P10 AB1 ASN A 207 ? SER A 226 ? ASN A 156 SER A 175 1 ? 20 
HELX_P HELX_P11 AB2 THR B 7   ? GLU B 29  ? THR B -32 GLU B -10 1 ? 23 
HELX_P HELX_P12 AB3 GLY B 59  ? GLY B 70  ? GLY B 7   GLY B 18  1 ? 12 
HELX_P HELX_P13 AB4 LEU B 116 ? ARG B 118 ? LEU B 64  ARG B 66  5 ? 3  
HELX_P HELX_P14 AB5 PHE B 119 ? ALA B 125 ? PHE B 67  ALA B 73  1 ? 7  
HELX_P HELX_P15 AB6 PHE B 126 ? ALA B 130 ? PHE B 74  ALA B 78  5 ? 5  
HELX_P HELX_P16 AB7 ASN B 141 ? ASN B 147 ? ASN B 89  ASN B 95  1 ? 7  
HELX_P HELX_P17 AB8 ASN B 147 ? ALA B 159 ? ASN B 95  ALA B 107 1 ? 13 
HELX_P HELX_P18 AB9 LEU B 175 ? ARG B 179 ? LEU B 123 ARG B 127 5 ? 5  
HELX_P HELX_P19 AC1 LYS B 182 ? GLY B 194 ? LYS B 130 GLY B 142 1 ? 13 
HELX_P HELX_P20 AC2 ASN B 207 ? MET B 223 ? ASN B 155 MET B 171 1 ? 17 
# 
_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 
covale1  covale none ? A CYS 161 SG  ? ? ? 1_555 J WTK . C05 ? ? A CYS 110 A WTK 208 1_555 ? ? ? ? ? ? ? 1.904 ? ? 
covale2  covale none ? B CYS 161 SG  ? ? ? 1_555 S WTK . C05 ? ? B CYS 109 B WTK 208 1_555 ? ? ? ? ? ? ? 1.905 ? ? 
metalc1  metalc ?    ? A THR 61  OG1 ? ? ? 1_555 K MG  . MG  ? ? A THR 10  A MG  209 1_555 ? ? ? ? ? ? ? 2.108 ? ? 
metalc2  metalc ?    ? A THR 79  OG1 ? ? ? 1_555 K MG  . MG  ? ? A THR 28  A MG  209 1_555 ? ? ? ? ? ? ? 2.165 ? ? 
metalc3  metalc ?    ? C GNP .   O3G ? ? ? 1_555 K MG  . MG  ? ? A GNP 201 A MG  209 1_555 ? ? ? ? ? ? ? 2.088 ? ? 
metalc4  metalc ?    ? C GNP .   O1B ? ? ? 1_555 K MG  . MG  ? ? A GNP 201 A MG  209 1_555 ? ? ? ? ? ? ? 1.976 ? ? 
metalc5  metalc ?    ? K MG  .   MG  ? ? ? 1_555 U HOH . O   ? ? A MG  209 A HOH 302 1_555 ? ? ? ? ? ? ? 2.376 ? ? 
metalc6  metalc ?    ? K MG  .   MG  ? ? ? 1_555 U HOH . O   ? ? A MG  209 A HOH 304 1_555 ? ? ? ? ? ? ? 2.174 ? ? 
metalc7  metalc ?    ? B THR 61  OG1 ? ? ? 1_555 T MG  . MG  ? ? B THR 9   B MG  209 1_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc8  metalc ?    ? B THR 79  OG1 ? ? ? 1_555 T MG  . MG  ? ? B THR 27  B MG  209 1_555 ? ? ? ? ? ? ? 2.133 ? ? 
metalc9  metalc ?    ? L GNP .   O3G ? ? ? 1_555 T MG  . MG  ? ? B GNP 201 B MG  209 1_555 ? ? ? ? ? ? ? 1.871 ? ? 
metalc10 metalc ?    ? L GNP .   O1B ? ? ? 1_555 T MG  . MG  ? ? B GNP 201 B MG  209 1_555 ? ? ? ? ? ? ? 1.926 ? ? 
metalc11 metalc ?    ? T MG  .   MG  ? ? ? 1_555 V HOH . O   ? ? B MG  209 B HOH 304 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc12 metalc ?    ? T MG  .   MG  ? ? ? 1_555 V HOH . O   ? ? B MG  209 B HOH 307 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG1 ? A THR 61 ? A THR 10  ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 OG1 ? A THR 79 ? A THR 28  ? 1_555 79.5  ? 
2  OG1 ? A THR 61 ? A THR 10  ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 O3G ? C GNP .  ? A GNP 201 ? 1_555 157.4 ? 
3  OG1 ? A THR 79 ? A THR 28  ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 O3G ? C GNP .  ? A GNP 201 ? 1_555 77.9  ? 
4  OG1 ? A THR 61 ? A THR 10  ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 O1B ? C GNP .  ? A GNP 201 ? 1_555 91.4  ? 
5  OG1 ? A THR 79 ? A THR 28  ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 O1B ? C GNP .  ? A GNP 201 ? 1_555 159.2 ? 
6  O3G ? C GNP .  ? A GNP 201 ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 O1B ? C GNP .  ? A GNP 201 ? 1_555 110.3 ? 
7  OG1 ? A THR 61 ? A THR 10  ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 O   ? U HOH .  ? A HOH 302 ? 1_555 82.3  ? 
8  OG1 ? A THR 79 ? A THR 28  ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 O   ? U HOH .  ? A HOH 302 ? 1_555 83.7  ? 
9  O3G ? C GNP .  ? A GNP 201 ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 O   ? U HOH .  ? A HOH 302 ? 1_555 93.8  ? 
10 O1B ? C GNP .  ? A GNP 201 ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 O   ? U HOH .  ? A HOH 302 ? 1_555 113.8 ? 
11 OG1 ? A THR 61 ? A THR 10  ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 O   ? U HOH .  ? A HOH 304 ? 1_555 89.8  ? 
12 OG1 ? A THR 79 ? A THR 28  ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 O   ? U HOH .  ? A HOH 304 ? 1_555 72.7  ? 
13 O3G ? C GNP .  ? A GNP 201 ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 O   ? U HOH .  ? A HOH 304 ? 1_555 84.9  ? 
14 O1B ? C GNP .  ? A GNP 201 ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 O   ? U HOH .  ? A HOH 304 ? 1_555 88.7  ? 
15 O   ? U HOH .  ? A HOH 302 ? 1_555 MG ? K MG . ? A MG 209 ? 1_555 O   ? U HOH .  ? A HOH 304 ? 1_555 156.2 ? 
16 OG1 ? B THR 61 ? B THR 9   ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 OG1 ? B THR 79 ? B THR 27  ? 1_555 83.6  ? 
17 OG1 ? B THR 61 ? B THR 9   ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 O3G ? L GNP .  ? B GNP 201 ? 1_555 158.3 ? 
18 OG1 ? B THR 79 ? B THR 27  ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 O3G ? L GNP .  ? B GNP 201 ? 1_555 81.1  ? 
19 OG1 ? B THR 61 ? B THR 9   ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 O1B ? L GNP .  ? B GNP 201 ? 1_555 93.3  ? 
20 OG1 ? B THR 79 ? B THR 27  ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 O1B ? L GNP .  ? B GNP 201 ? 1_555 158.0 ? 
21 O3G ? L GNP .  ? B GNP 201 ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 O1B ? L GNP .  ? B GNP 201 ? 1_555 95.1  ? 
22 OG1 ? B THR 61 ? B THR 9   ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 O   ? V HOH .  ? B HOH 304 ? 1_555 75.1  ? 
23 OG1 ? B THR 79 ? B THR 27  ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 O   ? V HOH .  ? B HOH 304 ? 1_555 71.9  ? 
24 O3G ? L GNP .  ? B GNP 201 ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 O   ? V HOH .  ? B HOH 304 ? 1_555 85.6  ? 
25 O1B ? L GNP .  ? B GNP 201 ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 O   ? V HOH .  ? B HOH 304 ? 1_555 86.2  ? 
26 OG1 ? B THR 61 ? B THR 9   ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 O   ? V HOH .  ? B HOH 307 ? 1_555 96.5  ? 
27 OG1 ? B THR 79 ? B THR 27  ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 O   ? V HOH .  ? B HOH 307 ? 1_555 96.5  ? 
28 O3G ? L GNP .  ? B GNP 201 ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 O   ? V HOH .  ? B HOH 307 ? 1_555 100.4 ? 
29 O1B ? L GNP .  ? B GNP 201 ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 O   ? V HOH .  ? B HOH 307 ? 1_555 105.5 ? 
30 O   ? V HOH .  ? B HOH 304 ? 1_555 MG ? T MG . ? B MG 209 ? 1_555 O   ? V HOH .  ? B HOH 307 ? 1_555 166.2 ? 
# 
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 WTK J . ? CYS A 161 ? WTK A 208 ? 1_555 CYS A 110 ? 1_555 C05 SG CYS 1 WTK None 'Covalent chemical modification' 
2 WTK S . ? CYS B 161 ? WTK B 208 ? 1_555 CYS B 109 ? 1_555 C05 SG CYS 1 WTK None 'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 82  ? ARG A 92  ? ILE A 31  ARG A 41  
AA1 2 GLY A 103 ? THR A 113 ? GLY A 52  THR A 62  
AA1 3 TYR A 46  ? GLY A 54  ? TYR A -5  GLY A 3   
AA1 4 PHE A 133 ? ASP A 138 ? PHE A 82  ASP A 87  
AA1 5 ILE A 166 ? ASN A 171 ? ILE A 115 ASN A 120 
AA1 6 TYR A 197 ? GLU A 199 ? TYR A 146 GLU A 148 
AA2 1 ILE B 82  ? ARG B 92  ? ILE B 30  ARG B 40  
AA2 2 GLY B 103 ? THR B 113 ? GLY B 51  THR B 61  
AA2 3 LEU B 47  ? LEU B 53  ? LEU B -5  LEU B 1   
AA2 4 PHE B 133 ? ASP B 138 ? PHE B 81  ASP B 86  
AA2 5 ILE B 166 ? ASN B 171 ? ILE B 114 ASN B 119 
AA2 6 TYR B 197 ? GLU B 199 ? TYR B 145 GLU B 147 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ASP A 83  ? N ASP A 32  O ASP A 112 ? O ASP A 61  
AA1 2 3 O GLN A 109 ? O GLN A 58  N ILE A 48  ? N ILE A -3  
AA1 3 4 N LEU A 51  ? N LEU A 0   O LEU A 134 ? O LEU A 83  
AA1 4 5 N LEU A 135 ? N LEU A 84  O CYS A 169 ? O CYS A 118 
AA1 5 6 N GLY A 170 ? N GLY A 119 O PHE A 198 ? O PHE A 147 
AA2 1 2 N ASP B 83  ? N ASP B 31  O ASP B 112 ? O ASP B 60  
AA2 2 3 O TRP B 111 ? O TRP B 59  N PHE B 50  ? N PHE B -2  
AA2 3 4 N LEU B 51  ? N LEU B -1  O LEU B 134 ? O LEU B 82  
AA2 4 5 N LEU B 135 ? N LEU B 83  O CYS B 169 ? O CYS B 117 
AA2 5 6 N GLY B 170 ? N GLY B 118 O PHE B 198 ? O PHE B 146 
# 
_pdbx_entry_details.entry_id                   8P3I 
_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 A TYR 109 ? ? N A CYS 110 ? ? 1.77 
2 1 O A HOH 314 ? ? O A HOH 325 ? ? 2.16 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NZ 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    LYS 
_pdbx_validate_symm_contact.auth_seq_id_1     -23 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    THR 
_pdbx_validate_symm_contact.auth_seq_id_2     48 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_545 
_pdbx_validate_symm_contact.dist              2.17 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA A TYR 109 ? ? C A TYR 109 ? ? N  A CYS 110 ? ? 139.35 117.20 22.15  2.20 Y 
2 1 O  A TYR 109 ? ? C A TYR 109 ? ? N  A CYS 110 ? ? 83.14  122.70 -39.56 1.60 Y 
3 1 C  A TYR 109 ? ? N A CYS 110 ? ? CA A CYS 110 ? ? 166.69 121.70 44.99  2.50 Y 
4 1 CA A CYS 110 ? ? C A CYS 110 ? ? N  A GLU 111 ? ? 84.90  117.20 -32.30 2.20 Y 
5 1 O  A CYS 110 ? ? C A CYS 110 ? ? N  A GLU 111 ? ? 103.61 122.70 -19.09 1.60 Y 
6 1 CA B TYR 108 ? ? C B TYR 108 ? ? N  B CYS 109 ? ? 96.80  117.20 -20.40 2.20 Y 
7 1 O  B TYR 108 ? ? C B TYR 108 ? ? N  B CYS 109 ? ? 138.48 122.70 15.78  1.60 Y 
8 1 O  B CYS 109 ? ? C B CYS 109 ? ? N  B GLU 110 ? ? 111.98 122.70 -10.72 1.60 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 TYR A 109 ? ? -100.39 46.28  
2 1 CYS A 110 ? ? 89.85   113.67 
3 1 ASN A 156 ? ? 67.95   -1.48  
4 1 ARG B 66  ? ? -56.71  -8.39  
5 1 LEU B 123 ? ? -100.75 62.15  
6 1 ASN B 155 ? ? 69.93   -8.51  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 TYR A 109 ? ? CYS A 110 ? ? -85.30  
2 1 CYS A 110 ? ? GLU A 111 ? ? 149.23  
3 1 TYR B 108 ? ? CYS B 109 ? ? -143.56 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 TYR A 109 ? ? -38.02 
2 1 CYS A 110 ? ? 33.50  
3 1 CYS B 109 ? ? 19.63  
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       329 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.94 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ARG -9  A A ARG 31  
2  1 Y 1 A GLY -9  B A GLY 32  
3  1 Y 1 A SER -9  C A SER 33  
4  1 Y 1 A GLY -9  D A GLY 34  
5  1 Y 1 A SER -9  E A SER 35  
6  1 Y 1 A GLY -9  F A GLY 36  
7  1 Y 1 A SER -9  G A SER 37  
8  1 Y 1 A GLY -9  H A GLY 38  
9  1 Y 1 A MET -9  I A MET 39  
10 1 Y 1 A SER -9  J A SER 40  
11 1 Y 1 A ASP -9  K A ASP 41  
12 1 Y 1 A GLY -9  L A GLY 42  
13 1 Y 1 A VAL 176 ? A VAL 227 
14 1 Y 1 A ASP 177 ? A ASP 228 
15 1 Y 1 A LYS 178 ? A LYS 229 
16 1 Y 1 A SER 179 ? A SER 230 
17 1 Y 1 B GLY -38 ? B GLY 1   
18 1 Y 1 B ARG -9  A B ARG 31  
19 1 Y 1 B GLY -9  B B GLY 32  
20 1 Y 1 B SER -9  C B SER 33  
21 1 Y 1 B GLY -9  D B GLY 34  
22 1 Y 1 B SER -9  E B SER 35  
23 1 Y 1 B GLY -9  F B GLY 36  
24 1 Y 1 B SER -9  G B SER 37  
25 1 Y 1 B GLY -9  H B GLY 38  
26 1 Y 1 B MET -9  I B MET 39  
27 1 Y 1 B SER -9  J B SER 40  
28 1 Y 1 B ASP -9  K B ASP 41  
29 1 Y 1 B GLY -9  L B GLY 42  
30 1 Y 1 B ASP -9  M B ASP 43  
31 1 Y 1 B VAL 175 ? B VAL 227 
32 1 Y 1 B ASP 176 ? B ASP 228 
33 1 Y 1 B LYS 177 ? B LYS 229 
34 1 Y 1 B SER 178 ? B SER 230 
# 
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 
GNP PG     P  N N 137 
GNP O1G    O  N N 138 
GNP O2G    O  N N 139 
GNP O3G    O  N N 140 
GNP N3B    N  N N 141 
GNP PB     P  N R 142 
GNP O1B    O  N N 143 
GNP O2B    O  N N 144 
GNP O3A    O  N N 145 
GNP PA     P  N S 146 
GNP O1A    O  N N 147 
GNP O2A    O  N N 148 
GNP "O5'"  O  N N 149 
GNP "C5'"  C  N N 150 
GNP "C4'"  C  N R 151 
GNP "O4'"  O  N N 152 
GNP "C3'"  C  N S 153 
GNP "O3'"  O  N N 154 
GNP "C2'"  C  N R 155 
GNP "O2'"  O  N N 156 
GNP "C1'"  C  N R 157 
GNP N9     N  Y N 158 
GNP C8     C  Y N 159 
GNP N7     N  Y N 160 
GNP C5     C  Y N 161 
GNP C6     C  Y N 162 
GNP O6     O  N N 163 
GNP N1     N  Y N 164 
GNP C2     C  Y N 165 
GNP N2     N  N N 166 
GNP N3     N  Y N 167 
GNP C4     C  Y N 168 
GNP HOG2   H  N N 169 
GNP HOG3   H  N N 170 
GNP HNB3   H  N N 171 
GNP HOB2   H  N N 172 
GNP HOA2   H  N N 173 
GNP "H5'2" H  N N 174 
GNP "H5'1" H  N N 175 
GNP "H4'"  H  N N 176 
GNP "H3'"  H  N N 177 
GNP "HO3'" H  N N 178 
GNP "H2'"  H  N N 179 
GNP "HO2'" H  N N 180 
GNP "H1'"  H  N N 181 
GNP H8     H  N N 182 
GNP HN1    H  N N 183 
GNP HN21   H  N N 184 
GNP HN22   H  N N 185 
GOL C1     C  N N 186 
GOL O1     O  N N 187 
GOL C2     C  N N 188 
GOL O2     O  N N 189 
GOL C3     C  N N 190 
GOL O3     O  N N 191 
GOL H11    H  N N 192 
GOL H12    H  N N 193 
GOL HO1    H  N N 194 
GOL H2     H  N N 195 
GOL HO2    H  N N 196 
GOL H31    H  N N 197 
GOL H32    H  N N 198 
GOL HO3    H  N N 199 
HIS N      N  N N 200 
HIS CA     C  N S 201 
HIS C      C  N N 202 
HIS O      O  N N 203 
HIS CB     C  N N 204 
HIS CG     C  Y N 205 
HIS ND1    N  Y N 206 
HIS CD2    C  Y N 207 
HIS CE1    C  Y N 208 
HIS NE2    N  Y N 209 
HIS OXT    O  N N 210 
HIS H      H  N N 211 
HIS H2     H  N N 212 
HIS HA     H  N N 213 
HIS HB2    H  N N 214 
HIS HB3    H  N N 215 
HIS HD1    H  N N 216 
HIS HD2    H  N N 217 
HIS HE1    H  N N 218 
HIS HE2    H  N N 219 
HIS HXT    H  N N 220 
HOH O      O  N N 221 
HOH H1     H  N N 222 
HOH H2     H  N N 223 
ILE N      N  N N 224 
ILE CA     C  N S 225 
ILE C      C  N N 226 
ILE O      O  N N 227 
ILE CB     C  N S 228 
ILE CG1    C  N N 229 
ILE CG2    C  N N 230 
ILE CD1    C  N N 231 
ILE OXT    O  N N 232 
ILE H      H  N N 233 
ILE H2     H  N N 234 
ILE HA     H  N N 235 
ILE HB     H  N N 236 
ILE HG12   H  N N 237 
ILE HG13   H  N N 238 
ILE HG21   H  N N 239 
ILE HG22   H  N N 240 
ILE HG23   H  N N 241 
ILE HD11   H  N N 242 
ILE HD12   H  N N 243 
ILE HD13   H  N N 244 
ILE HXT    H  N N 245 
LEU N      N  N N 246 
LEU CA     C  N S 247 
LEU C      C  N N 248 
LEU O      O  N N 249 
LEU CB     C  N N 250 
LEU CG     C  N N 251 
LEU CD1    C  N N 252 
LEU CD2    C  N N 253 
LEU OXT    O  N N 254 
LEU H      H  N N 255 
LEU H2     H  N N 256 
LEU HA     H  N N 257 
LEU HB2    H  N N 258 
LEU HB3    H  N N 259 
LEU HG     H  N N 260 
LEU HD11   H  N N 261 
LEU HD12   H  N N 262 
LEU HD13   H  N N 263 
LEU HD21   H  N N 264 
LEU HD22   H  N N 265 
LEU HD23   H  N N 266 
LEU HXT    H  N N 267 
LYS N      N  N N 268 
LYS CA     C  N S 269 
LYS C      C  N N 270 
LYS O      O  N N 271 
LYS CB     C  N N 272 
LYS CG     C  N N 273 
LYS CD     C  N N 274 
LYS CE     C  N N 275 
LYS NZ     N  N N 276 
LYS OXT    O  N N 277 
LYS H      H  N N 278 
LYS H2     H  N N 279 
LYS HA     H  N N 280 
LYS HB2    H  N N 281 
LYS HB3    H  N N 282 
LYS HG2    H  N N 283 
LYS HG3    H  N N 284 
LYS HD2    H  N N 285 
LYS HD3    H  N N 286 
LYS HE2    H  N N 287 
LYS HE3    H  N N 288 
LYS HZ1    H  N N 289 
LYS HZ2    H  N N 290 
LYS HZ3    H  N N 291 
LYS HXT    H  N N 292 
MET N      N  N N 293 
MET CA     C  N S 294 
MET C      C  N N 295 
MET O      O  N N 296 
MET CB     C  N N 297 
MET CG     C  N N 298 
MET SD     S  N N 299 
MET CE     C  N N 300 
MET OXT    O  N N 301 
MET H      H  N N 302 
MET H2     H  N N 303 
MET HA     H  N N 304 
MET HB2    H  N N 305 
MET HB3    H  N N 306 
MET HG2    H  N N 307 
MET HG3    H  N N 308 
MET HE1    H  N N 309 
MET HE2    H  N N 310 
MET HE3    H  N N 311 
MET HXT    H  N N 312 
MG  MG     MG N N 313 
PHE N      N  N N 314 
PHE CA     C  N S 315 
PHE C      C  N N 316 
PHE O      O  N N 317 
PHE CB     C  N N 318 
PHE CG     C  Y N 319 
PHE CD1    C  Y N 320 
PHE CD2    C  Y N 321 
PHE CE1    C  Y N 322 
PHE CE2    C  Y N 323 
PHE CZ     C  Y N 324 
PHE OXT    O  N N 325 
PHE H      H  N N 326 
PHE H2     H  N N 327 
PHE HA     H  N N 328 
PHE HB2    H  N N 329 
PHE HB3    H  N N 330 
PHE HD1    H  N N 331 
PHE HD2    H  N N 332 
PHE HE1    H  N N 333 
PHE HE2    H  N N 334 
PHE HZ     H  N N 335 
PHE HXT    H  N N 336 
PRO N      N  N N 337 
PRO CA     C  N S 338 
PRO C      C  N N 339 
PRO O      O  N N 340 
PRO CB     C  N N 341 
PRO CG     C  N N 342 
PRO CD     C  N N 343 
PRO OXT    O  N N 344 
PRO H      H  N N 345 
PRO HA     H  N N 346 
PRO HB2    H  N N 347 
PRO HB3    H  N N 348 
PRO HG2    H  N N 349 
PRO HG3    H  N N 350 
PRO HD2    H  N N 351 
PRO HD3    H  N N 352 
PRO HXT    H  N N 353 
SER N      N  N N 354 
SER CA     C  N S 355 
SER C      C  N N 356 
SER O      O  N N 357 
SER CB     C  N N 358 
SER OG     O  N N 359 
SER OXT    O  N N 360 
SER H      H  N N 361 
SER H2     H  N N 362 
SER HA     H  N N 363 
SER HB2    H  N N 364 
SER HB3    H  N N 365 
SER HG     H  N N 366 
SER HXT    H  N N 367 
THR N      N  N N 368 
THR CA     C  N S 369 
THR C      C  N N 370 
THR O      O  N N 371 
THR CB     C  N R 372 
THR OG1    O  N N 373 
THR CG2    C  N N 374 
THR OXT    O  N N 375 
THR H      H  N N 376 
THR H2     H  N N 377 
THR HA     H  N N 378 
THR HB     H  N N 379 
THR HG1    H  N N 380 
THR HG21   H  N N 381 
THR HG22   H  N N 382 
THR HG23   H  N N 383 
THR HXT    H  N N 384 
TRP N      N  N N 385 
TRP CA     C  N S 386 
TRP C      C  N N 387 
TRP O      O  N N 388 
TRP CB     C  N N 389 
TRP CG     C  Y N 390 
TRP CD1    C  Y N 391 
TRP CD2    C  Y N 392 
TRP NE1    N  Y N 393 
TRP CE2    C  Y N 394 
TRP CE3    C  Y N 395 
TRP CZ2    C  Y N 396 
TRP CZ3    C  Y N 397 
TRP CH2    C  Y N 398 
TRP OXT    O  N N 399 
TRP H      H  N N 400 
TRP H2     H  N N 401 
TRP HA     H  N N 402 
TRP HB2    H  N N 403 
TRP HB3    H  N N 404 
TRP HD1    H  N N 405 
TRP HE1    H  N N 406 
TRP HE3    H  N N 407 
TRP HZ2    H  N N 408 
TRP HZ3    H  N N 409 
TRP HH2    H  N N 410 
TRP HXT    H  N N 411 
TYR N      N  N N 412 
TYR CA     C  N S 413 
TYR C      C  N N 414 
TYR O      O  N N 415 
TYR CB     C  N N 416 
TYR CG     C  Y N 417 
TYR CD1    C  Y N 418 
TYR CD2    C  Y N 419 
TYR CE1    C  Y N 420 
TYR CE2    C  Y N 421 
TYR CZ     C  Y N 422 
TYR OH     O  N N 423 
TYR OXT    O  N N 424 
TYR H      H  N N 425 
TYR H2     H  N N 426 
TYR HA     H  N N 427 
TYR HB2    H  N N 428 
TYR HB3    H  N N 429 
TYR HD1    H  N N 430 
TYR HD2    H  N N 431 
TYR HE1    H  N N 432 
TYR HE2    H  N N 433 
TYR HH     H  N N 434 
TYR HXT    H  N N 435 
VAL N      N  N N 436 
VAL CA     C  N S 437 
VAL C      C  N N 438 
VAL O      O  N N 439 
VAL CB     C  N N 440 
VAL CG1    C  N N 441 
VAL CG2    C  N N 442 
VAL OXT    O  N N 443 
VAL H      H  N N 444 
VAL H2     H  N N 445 
VAL HA     H  N N 446 
VAL HB     H  N N 447 
VAL HG11   H  N N 448 
VAL HG12   H  N N 449 
VAL HG13   H  N N 450 
VAL HG21   H  N N 451 
VAL HG22   H  N N 452 
VAL HG23   H  N N 453 
VAL HXT    H  N N 454 
WTK C05    C  N N 455 
WTK C06    C  N N 456 
WTK C07    C  N N 457 
WTK C09    C  Y N 458 
WTK C10    C  Y N 459 
WTK C11    C  Y N 460 
WTK C12    C  Y N 461 
WTK C13    C  Y N 462 
WTK C15    C  N N 463 
WTK C16    C  Y N 464 
WTK C20    C  N N 465 
WTK C21    C  N N 466 
WTK C22    C  N N 467 
WTK C23    C  N N 468 
WTK N08    N  N N 469 
WTK N19    N  N N 470 
WTK O14    O  N N 471 
WTK O18    O  N N 472 
WTK O24    O  N N 473 
WTK O25    O  N N 474 
WTK S17    S  N N 475 
WTK H1     H  N N 476 
WTK H2     H  N N 477 
WTK H3     H  N N 478 
WTK H4     H  N N 479 
WTK H5     H  N N 480 
WTK H6     H  N N 481 
WTK H7     H  N N 482 
WTK H8     H  N N 483 
WTK H9     H  N N 484 
WTK H10    H  N N 485 
WTK H11    H  N N 486 
WTK H12    H  N N 487 
WTK H13    H  N N 488 
WTK H14    H  N N 489 
WTK H15    H  N N 490 
WTK H16    H  N N 491 
WTK H17    H  N N 492 
WTK H18    H  N N 493 
WTK H19    H  N N 494 
WTK H20    H  N N 495 
# 
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 
GNP PG    O1G    doub N N 129 
GNP PG    O2G    sing N N 130 
GNP PG    O3G    sing N N 131 
GNP PG    N3B    sing N N 132 
GNP O2G   HOG2   sing N N 133 
GNP O3G   HOG3   sing N N 134 
GNP N3B   PB     sing N N 135 
GNP N3B   HNB3   sing N N 136 
GNP PB    O1B    doub N N 137 
GNP PB    O2B    sing N N 138 
GNP PB    O3A    sing N N 139 
GNP O2B   HOB2   sing N N 140 
GNP O3A   PA     sing N N 141 
GNP PA    O1A    doub N N 142 
GNP PA    O2A    sing N N 143 
GNP PA    "O5'"  sing N N 144 
GNP O2A   HOA2   sing N N 145 
GNP "O5'" "C5'"  sing N N 146 
GNP "C5'" "C4'"  sing N N 147 
GNP "C5'" "H5'2" sing N N 148 
GNP "C5'" "H5'1" sing N N 149 
GNP "C4'" "O4'"  sing N N 150 
GNP "C4'" "C3'"  sing N N 151 
GNP "C4'" "H4'"  sing N N 152 
GNP "O4'" "C1'"  sing N N 153 
GNP "C3'" "O3'"  sing N N 154 
GNP "C3'" "C2'"  sing N N 155 
GNP "C3'" "H3'"  sing N N 156 
GNP "O3'" "HO3'" sing N N 157 
GNP "C2'" "O2'"  sing N N 158 
GNP "C2'" "C1'"  sing N N 159 
GNP "C2'" "H2'"  sing N N 160 
GNP "O2'" "HO2'" sing N N 161 
GNP "C1'" N9     sing N N 162 
GNP "C1'" "H1'"  sing N N 163 
GNP N9    C8     sing Y N 164 
GNP N9    C4     sing Y N 165 
GNP C8    N7     doub Y N 166 
GNP C8    H8     sing N N 167 
GNP N7    C5     sing Y N 168 
GNP C5    C6     sing Y N 169 
GNP C5    C4     doub Y N 170 
GNP C6    O6     doub N N 171 
GNP C6    N1     sing Y N 172 
GNP N1    C2     sing Y N 173 
GNP N1    HN1    sing N N 174 
GNP C2    N2     sing N N 175 
GNP C2    N3     doub Y N 176 
GNP N2    HN21   sing N N 177 
GNP N2    HN22   sing N N 178 
GNP N3    C4     sing Y N 179 
GOL C1    O1     sing N N 180 
GOL C1    C2     sing N N 181 
GOL C1    H11    sing N N 182 
GOL C1    H12    sing N N 183 
GOL O1    HO1    sing N N 184 
GOL C2    O2     sing N N 185 
GOL C2    C3     sing N N 186 
GOL C2    H2     sing N N 187 
GOL O2    HO2    sing N N 188 
GOL C3    O3     sing N N 189 
GOL C3    H31    sing N N 190 
GOL C3    H32    sing N N 191 
GOL O3    HO3    sing N N 192 
HIS N     CA     sing N N 193 
HIS N     H      sing N N 194 
HIS N     H2     sing N N 195 
HIS CA    C      sing N N 196 
HIS CA    CB     sing N N 197 
HIS CA    HA     sing N N 198 
HIS C     O      doub N N 199 
HIS C     OXT    sing N N 200 
HIS CB    CG     sing N N 201 
HIS CB    HB2    sing N N 202 
HIS CB    HB3    sing N N 203 
HIS CG    ND1    sing Y N 204 
HIS CG    CD2    doub Y N 205 
HIS ND1   CE1    doub Y N 206 
HIS ND1   HD1    sing N N 207 
HIS CD2   NE2    sing Y N 208 
HIS CD2   HD2    sing N N 209 
HIS CE1   NE2    sing Y N 210 
HIS CE1   HE1    sing N N 211 
HIS NE2   HE2    sing N N 212 
HIS OXT   HXT    sing N N 213 
HOH O     H1     sing N N 214 
HOH O     H2     sing N N 215 
ILE N     CA     sing N N 216 
ILE N     H      sing N N 217 
ILE N     H2     sing N N 218 
ILE CA    C      sing N N 219 
ILE CA    CB     sing N N 220 
ILE CA    HA     sing N N 221 
ILE C     O      doub N N 222 
ILE C     OXT    sing N N 223 
ILE CB    CG1    sing N N 224 
ILE CB    CG2    sing N N 225 
ILE CB    HB     sing N N 226 
ILE CG1   CD1    sing N N 227 
ILE CG1   HG12   sing N N 228 
ILE CG1   HG13   sing N N 229 
ILE CG2   HG21   sing N N 230 
ILE CG2   HG22   sing N N 231 
ILE CG2   HG23   sing N N 232 
ILE CD1   HD11   sing N N 233 
ILE CD1   HD12   sing N N 234 
ILE CD1   HD13   sing N N 235 
ILE OXT   HXT    sing N N 236 
LEU N     CA     sing N N 237 
LEU N     H      sing N N 238 
LEU N     H2     sing N N 239 
LEU CA    C      sing N N 240 
LEU CA    CB     sing N N 241 
LEU CA    HA     sing N N 242 
LEU C     O      doub N N 243 
LEU C     OXT    sing N N 244 
LEU CB    CG     sing N N 245 
LEU CB    HB2    sing N N 246 
LEU CB    HB3    sing N N 247 
LEU CG    CD1    sing N N 248 
LEU CG    CD2    sing N N 249 
LEU CG    HG     sing N N 250 
LEU CD1   HD11   sing N N 251 
LEU CD1   HD12   sing N N 252 
LEU CD1   HD13   sing N N 253 
LEU CD2   HD21   sing N N 254 
LEU CD2   HD22   sing N N 255 
LEU CD2   HD23   sing N N 256 
LEU OXT   HXT    sing N N 257 
LYS N     CA     sing N N 258 
LYS N     H      sing N N 259 
LYS N     H2     sing N N 260 
LYS CA    C      sing N N 261 
LYS CA    CB     sing N N 262 
LYS CA    HA     sing N N 263 
LYS C     O      doub N N 264 
LYS C     OXT    sing N N 265 
LYS CB    CG     sing N N 266 
LYS CB    HB2    sing N N 267 
LYS CB    HB3    sing N N 268 
LYS CG    CD     sing N N 269 
LYS CG    HG2    sing N N 270 
LYS CG    HG3    sing N N 271 
LYS CD    CE     sing N N 272 
LYS CD    HD2    sing N N 273 
LYS CD    HD3    sing N N 274 
LYS CE    NZ     sing N N 275 
LYS CE    HE2    sing N N 276 
LYS CE    HE3    sing N N 277 
LYS NZ    HZ1    sing N N 278 
LYS NZ    HZ2    sing N N 279 
LYS NZ    HZ3    sing N N 280 
LYS OXT   HXT    sing N N 281 
MET N     CA     sing N N 282 
MET N     H      sing N N 283 
MET N     H2     sing N N 284 
MET CA    C      sing N N 285 
MET CA    CB     sing N N 286 
MET CA    HA     sing N N 287 
MET C     O      doub N N 288 
MET C     OXT    sing N N 289 
MET CB    CG     sing N N 290 
MET CB    HB2    sing N N 291 
MET CB    HB3    sing N N 292 
MET CG    SD     sing N N 293 
MET CG    HG2    sing N N 294 
MET CG    HG3    sing N N 295 
MET SD    CE     sing N N 296 
MET CE    HE1    sing N N 297 
MET CE    HE2    sing N N 298 
MET CE    HE3    sing N N 299 
MET OXT   HXT    sing N N 300 
PHE N     CA     sing N N 301 
PHE N     H      sing N N 302 
PHE N     H2     sing N N 303 
PHE CA    C      sing N N 304 
PHE CA    CB     sing N N 305 
PHE CA    HA     sing N N 306 
PHE C     O      doub N N 307 
PHE C     OXT    sing N N 308 
PHE CB    CG     sing N N 309 
PHE CB    HB2    sing N N 310 
PHE CB    HB3    sing N N 311 
PHE CG    CD1    doub Y N 312 
PHE CG    CD2    sing Y N 313 
PHE CD1   CE1    sing Y N 314 
PHE CD1   HD1    sing N N 315 
PHE CD2   CE2    doub Y N 316 
PHE CD2   HD2    sing N N 317 
PHE CE1   CZ     doub Y N 318 
PHE CE1   HE1    sing N N 319 
PHE CE2   CZ     sing Y N 320 
PHE CE2   HE2    sing N N 321 
PHE CZ    HZ     sing N N 322 
PHE OXT   HXT    sing N N 323 
PRO N     CA     sing N N 324 
PRO N     CD     sing N N 325 
PRO N     H      sing N N 326 
PRO CA    C      sing N N 327 
PRO CA    CB     sing N N 328 
PRO CA    HA     sing N N 329 
PRO C     O      doub N N 330 
PRO C     OXT    sing N N 331 
PRO CB    CG     sing N N 332 
PRO CB    HB2    sing N N 333 
PRO CB    HB3    sing N N 334 
PRO CG    CD     sing N N 335 
PRO CG    HG2    sing N N 336 
PRO CG    HG3    sing N N 337 
PRO CD    HD2    sing N N 338 
PRO CD    HD3    sing N N 339 
PRO OXT   HXT    sing N N 340 
SER N     CA     sing N N 341 
SER N     H      sing N N 342 
SER N     H2     sing N N 343 
SER CA    C      sing N N 344 
SER CA    CB     sing N N 345 
SER CA    HA     sing N N 346 
SER C     O      doub N N 347 
SER C     OXT    sing N N 348 
SER CB    OG     sing N N 349 
SER CB    HB2    sing N N 350 
SER CB    HB3    sing N N 351 
SER OG    HG     sing N N 352 
SER OXT   HXT    sing N N 353 
THR N     CA     sing N N 354 
THR N     H      sing N N 355 
THR N     H2     sing N N 356 
THR CA    C      sing N N 357 
THR CA    CB     sing N N 358 
THR CA    HA     sing N N 359 
THR C     O      doub N N 360 
THR C     OXT    sing N N 361 
THR CB    OG1    sing N N 362 
THR CB    CG2    sing N N 363 
THR CB    HB     sing N N 364 
THR OG1   HG1    sing N N 365 
THR CG2   HG21   sing N N 366 
THR CG2   HG22   sing N N 367 
THR CG2   HG23   sing N N 368 
THR OXT   HXT    sing N N 369 
TRP N     CA     sing N N 370 
TRP N     H      sing N N 371 
TRP N     H2     sing N N 372 
TRP CA    C      sing N N 373 
TRP CA    CB     sing N N 374 
TRP CA    HA     sing N N 375 
TRP C     O      doub N N 376 
TRP C     OXT    sing N N 377 
TRP CB    CG     sing N N 378 
TRP CB    HB2    sing N N 379 
TRP CB    HB3    sing N N 380 
TRP CG    CD1    doub Y N 381 
TRP CG    CD2    sing Y N 382 
TRP CD1   NE1    sing Y N 383 
TRP CD1   HD1    sing N N 384 
TRP CD2   CE2    doub Y N 385 
TRP CD2   CE3    sing Y N 386 
TRP NE1   CE2    sing Y N 387 
TRP NE1   HE1    sing N N 388 
TRP CE2   CZ2    sing Y N 389 
TRP CE3   CZ3    doub Y N 390 
TRP CE3   HE3    sing N N 391 
TRP CZ2   CH2    doub Y N 392 
TRP CZ2   HZ2    sing N N 393 
TRP CZ3   CH2    sing Y N 394 
TRP CZ3   HZ3    sing N N 395 
TRP CH2   HH2    sing N N 396 
TRP OXT   HXT    sing N N 397 
TYR N     CA     sing N N 398 
TYR N     H      sing N N 399 
TYR N     H2     sing N N 400 
TYR CA    C      sing N N 401 
TYR CA    CB     sing N N 402 
TYR CA    HA     sing N N 403 
TYR C     O      doub N N 404 
TYR C     OXT    sing N N 405 
TYR CB    CG     sing N N 406 
TYR CB    HB2    sing N N 407 
TYR CB    HB3    sing N N 408 
TYR CG    CD1    doub Y N 409 
TYR CG    CD2    sing Y N 410 
TYR CD1   CE1    sing Y N 411 
TYR CD1   HD1    sing N N 412 
TYR CD2   CE2    doub Y N 413 
TYR CD2   HD2    sing N N 414 
TYR CE1   CZ     doub Y N 415 
TYR CE1   HE1    sing N N 416 
TYR CE2   CZ     sing Y N 417 
TYR CE2   HE2    sing N N 418 
TYR CZ    OH     sing N N 419 
TYR OH    HH     sing N N 420 
TYR OXT   HXT    sing N N 421 
VAL N     CA     sing N N 422 
VAL N     H      sing N N 423 
VAL N     H2     sing N N 424 
VAL CA    C      sing N N 425 
VAL CA    CB     sing N N 426 
VAL CA    HA     sing N N 427 
VAL C     O      doub N N 428 
VAL C     OXT    sing N N 429 
VAL CB    CG1    sing N N 430 
VAL CB    CG2    sing N N 431 
VAL CB    HB     sing N N 432 
VAL CG1   HG11   sing N N 433 
VAL CG1   HG12   sing N N 434 
VAL CG1   HG13   sing N N 435 
VAL CG2   HG21   sing N N 436 
VAL CG2   HG22   sing N N 437 
VAL CG2   HG23   sing N N 438 
VAL OXT   HXT    sing N N 439 
WTK O18   S17    doub N N 440 
WTK O24   S17    doub N N 441 
WTK C11   C10    doub Y N 442 
WTK C11   C16    sing Y N 443 
WTK C10   C09    sing Y N 444 
WTK S17   C16    sing N N 445 
WTK S17   N19    sing N N 446 
WTK C16   C13    doub Y N 447 
WTK C09   N08    sing N N 448 
WTK C09   C12    doub Y N 449 
WTK N08   C07    sing N N 450 
WTK C07   C06    sing N N 451 
WTK C07   O25    doub N N 452 
WTK C06   C05    sing N N 453 
WTK C15   O14    sing N N 454 
WTK C13   C12    sing Y N 455 
WTK C13   O14    sing N N 456 
WTK N19   C20    sing N N 457 
WTK N19   C23    sing N N 458 
WTK C20   C21    sing N N 459 
WTK C23   C22    sing N N 460 
WTK C21   C22    sing N N 461 
WTK C05   H1     sing N N 462 
WTK C05   H2     sing N N 463 
WTK C05   H3     sing N N 464 
WTK C06   H4     sing N N 465 
WTK C06   H5     sing N N 466 
WTK C10   H6     sing N N 467 
WTK C11   H7     sing N N 468 
WTK C12   H8     sing N N 469 
WTK C15   H9     sing N N 470 
WTK C15   H10    sing N N 471 
WTK C15   H11    sing N N 472 
WTK C20   H12    sing N N 473 
WTK C20   H13    sing N N 474 
WTK C21   H14    sing N N 475 
WTK C21   H15    sing N N 476 
WTK C22   H16    sing N N 477 
WTK C22   H17    sing N N 478 
WTK C23   H18    sing N N 479 
WTK C23   H19    sing N N 480 
WTK N08   H20    sing N N 481 
# 
_pdbx_audit_support.funding_organization   'Cancer Research UK' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           C29637/A20781 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7OPP 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8P3I 
_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]   0.016295 
_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]   0.013055 
_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]   0.008426 
_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  
MG 
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     . GLY A 1 1   ? 23.710  -18.173 12.740  1.00 80.20  ?  -38 GLY A N     1 
ATOM   2    C  CA    . GLY A 1 1   ? 22.925  -17.036 13.184  1.00 71.24  ?  -38 GLY A CA    1 
ATOM   3    C  C     . GLY A 1 1   ? 23.797  -15.841 13.505  1.00 74.93  ?  -38 GLY A C     1 
ATOM   4    O  O     . GLY A 1 1   ? 24.055  -15.546 14.679  1.00 78.70  ?  -38 GLY A O     1 
ATOM   5    N  N     . HIS A 1 2   ? 24.255  -15.138 12.452  1.00 70.89  ?  -37 HIS A N     1 
ATOM   6    C  CA    . HIS A 1 2   ? 25.181  -14.019 12.599  1.00 71.12  ?  -37 HIS A CA    1 
ATOM   7    C  C     . HIS A 1 2   ? 24.831  -12.912 11.599  1.00 70.38  ?  -37 HIS A C     1 
ATOM   8    O  O     . HIS A 1 2   ? 25.551  -12.640 10.637  1.00 71.45  ?  -37 HIS A O     1 
ATOM   9    C  CB    . HIS A 1 2   ? 26.624  -14.492 12.441  1.00 70.22  ?  -37 HIS A CB    1 
ATOM   10   C  CG    . HIS A 1 2   ? 27.013  -15.529 13.445  1.00 74.65  ?  -37 HIS A CG    1 
ATOM   11   N  ND1   . HIS A 1 2   ? 27.115  -15.255 14.792  1.00 77.26  ?  -37 HIS A ND1   1 
ATOM   12   C  CD2   . HIS A 1 2   ? 27.282  -16.849 13.308  1.00 77.80  ?  -37 HIS A CD2   1 
ATOM   13   C  CE1   . HIS A 1 2   ? 27.451  -16.356 15.439  1.00 79.96  ?  -37 HIS A CE1   1 
ATOM   14   N  NE2   . HIS A 1 2   ? 27.558  -17.339 14.562  1.00 77.86  ?  -37 HIS A NE2   1 
ATOM   15   N  N     . MET A 1 3   ? 23.712  -12.238 11.857  1.00 68.36  ?  -36 MET A N     1 
ATOM   16   C  CA    . MET A 1 3   ? 23.238  -11.156 11.004  1.00 63.45  ?  -36 MET A CA    1 
ATOM   17   C  C     . MET A 1 3   ? 24.162  -9.955  11.126  1.00 66.39  ?  -36 MET A C     1 
ATOM   18   O  O     . MET A 1 3   ? 24.268  -9.346  12.191  1.00 65.94  ?  -36 MET A O     1 
ATOM   19   C  CB    . MET A 1 3   ? 21.814  -10.780 11.387  1.00 60.89  ?  -36 MET A CB    1 
ATOM   20   C  CG    . MET A 1 3   ? 20.819  -11.879 11.132  1.00 54.57  ?  -36 MET A CG    1 
ATOM   21   S  SD    . MET A 1 3   ? 19.212  -11.443 11.823  1.00 63.16  ?  -36 MET A SD    1 
ATOM   22   C  CE    . MET A 1 3   ? 19.530  -11.596 13.588  1.00 61.60  ?  -36 MET A CE    1 
ATOM   23   N  N     . SER A 1 4   ? 24.811  -9.595  10.026  1.00 68.72  ?  -35 SER A N     1 
ATOM   24   C  CA    . SER A 1 4   ? 25.664  -8.419  10.019  1.00 67.76  ?  -35 SER A CA    1 
ATOM   25   C  C     . SER A 1 4   ? 24.836  -7.164  10.250  1.00 66.81  ?  -35 SER A C     1 
ATOM   26   O  O     . SER A 1 4   ? 23.715  -7.040  9.748   1.00 63.81  ?  -35 SER A O     1 
ATOM   27   C  CB    . SER A 1 4   ? 26.395  -8.306  8.679   1.00 65.24  ?  -35 SER A CB    1 
ATOM   28   O  OG    . SER A 1 4   ? 26.739  -9.580  8.160   1.00 67.13  ?  -35 SER A OG    1 
ATOM   29   N  N     . PHE A 1 5   ? 25.398  -6.225  11.009  1.00 64.71  ?  -34 PHE A N     1 
ATOM   30   C  CA    . PHE A 1 5   ? 24.852  -4.877  11.011  1.00 62.51  ?  -34 PHE A CA    1 
ATOM   31   C  C     . PHE A 1 5   ? 24.965  -4.259  9.617   1.00 61.36  ?  -34 PHE A C     1 
ATOM   32   O  O     . PHE A 1 5   ? 25.724  -4.721  8.765   1.00 59.96  ?  -34 PHE A O     1 
ATOM   33   C  CB    . PHE A 1 5   ? 25.579  -4.008  12.032  1.00 61.50  ?  -34 PHE A CB    1 
ATOM   34   C  CG    . PHE A 1 5   ? 25.058  -4.172  13.417  1.00 66.86  ?  -34 PHE A CG    1 
ATOM   35   C  CD1   . PHE A 1 5   ? 23.839  -3.619  13.765  1.00 67.67  ?  -34 PHE A CD1   1 
ATOM   36   C  CD2   . PHE A 1 5   ? 25.772  -4.888  14.370  1.00 67.58  ?  -34 PHE A CD2   1 
ATOM   37   C  CE1   . PHE A 1 5   ? 23.329  -3.770  15.039  1.00 68.73  ?  -34 PHE A CE1   1 
ATOM   38   C  CE2   . PHE A 1 5   ? 25.274  -5.047  15.662  1.00 71.65  ?  -34 PHE A CE2   1 
ATOM   39   C  CZ    . PHE A 1 5   ? 24.050  -4.483  15.999  1.00 68.78  ?  -34 PHE A CZ    1 
ATOM   40   N  N     . LEU A 1 6   ? 24.197  -3.199  9.385   1.00 56.61  ?  -33 LEU A N     1 
ATOM   41   C  CA    . LEU A 1 6   ? 24.286  -2.515  8.111   1.00 52.59  ?  -33 LEU A CA    1 
ATOM   42   C  C     . LEU A 1 6   ? 25.698  -1.998  7.917   1.00 55.54  ?  -33 LEU A C     1 
ATOM   43   O  O     . LEU A 1 6   ? 26.368  -1.610  8.875   1.00 62.91  ?  -33 LEU A O     1 
ATOM   44   C  CB    . LEU A 1 6   ? 23.294  -1.360  8.041   1.00 53.06  ?  -33 LEU A CB    1 
ATOM   45   C  CG    . LEU A 1 6   ? 21.824  -1.700  8.280   1.00 56.53  ?  -33 LEU A CG    1 
ATOM   46   C  CD1   . LEU A 1 6   ? 20.972  -0.434  8.253   1.00 57.15  ?  -33 LEU A CD1   1 
ATOM   47   C  CD2   . LEU A 1 6   ? 21.324  -2.704  7.267   1.00 56.16  ?  -33 LEU A CD2   1 
ATOM   48   N  N     . THR A 1 7   ? 26.171  -2.058  6.679   1.00 56.24  ?  -32 THR A N     1 
ATOM   49   C  CA    . THR A 1 7   ? 27.417  -1.412  6.324   1.00 54.88  ?  -32 THR A CA    1 
ATOM   50   C  C     . THR A 1 7   ? 27.174  0.078   6.155   1.00 54.87  ?  -32 THR A C     1 
ATOM   51   O  O     . THR A 1 7   ? 26.036  0.542   6.041   1.00 54.14  ?  -32 THR A O     1 
ATOM   52   C  CB    . THR A 1 7   ? 27.991  -1.996  5.034   1.00 55.02  ?  -32 THR A CB    1 
ATOM   53   O  OG1   . THR A 1 7   ? 27.133  -1.649  3.946   1.00 53.51  ?  -32 THR A OG1   1 
ATOM   54   C  CG2   . THR A 1 7   ? 28.071  -3.498  5.116   1.00 59.39  ?  -32 THR A CG2   1 
ATOM   55   N  N     . GLU A 1 8   ? 28.265  0.836   6.127   1.00 57.22  ?  -31 GLU A N     1 
ATOM   56   C  CA    . GLU A 1 8   ? 28.139  2.266   5.873   1.00 61.16  ?  -31 GLU A CA    1 
ATOM   57   C  C     . GLU A 1 8   ? 27.396  2.527   4.561   1.00 60.46  ?  -31 GLU A C     1 
ATOM   58   O  O     . GLU A 1 8   ? 26.574  3.450   4.473   1.00 60.84  ?  -31 GLU A O     1 
ATOM   59   C  CB    . GLU A 1 8   ? 29.532  2.901   5.867   1.00 66.23  ?  -31 GLU A CB    1 
ATOM   60   C  CG    . GLU A 1 8   ? 29.594  4.348   6.313   1.00 72.65  ?  -31 GLU A CG    1 
ATOM   61   C  CD    . GLU A 1 8   ? 30.889  5.021   5.870   1.00 84.06  ?  -31 GLU A CD    1 
ATOM   62   O  OE1   . GLU A 1 8   ? 31.974  4.475   6.181   1.00 82.98  ?  -31 GLU A OE1   1 
ATOM   63   O  OE2   . GLU A 1 8   ? 30.820  6.081   5.196   1.00 87.21  ?  -31 GLU A OE2   1 
ATOM   64   N  N     . GLU A 1 9   ? 27.640  1.694   3.540   1.00 56.13  ?  -30 GLU A N     1 
ATOM   65   C  CA    . GLU A 1 9   ? 26.986  1.884   2.245   1.00 56.28  ?  -30 GLU A CA    1 
ATOM   66   C  C     . GLU A 1 9   ? 25.511  1.489   2.293   1.00 52.75  ?  -30 GLU A C     1 
ATOM   67   O  O     . GLU A 1 9   ? 24.659  2.188   1.731   1.00 54.74  ?  -30 GLU A O     1 
ATOM   68   C  CB    . GLU A 1 9   ? 27.722  1.094   1.161   1.00 58.03  ?  -30 GLU A CB    1 
ATOM   69   N  N     . GLU A 1 10  ? 25.186  0.375   2.953   1.00 52.08  ?  -29 GLU A N     1 
ATOM   70   C  CA    . GLU A 1 10  ? 23.785  0.036   3.186   1.00 50.12  ?  -29 GLU A CA    1 
ATOM   71   C  C     . GLU A 1 10  ? 23.056  1.173   3.894   1.00 55.19  ?  -29 GLU A C     1 
ATOM   72   O  O     . GLU A 1 10  ? 21.922  1.515   3.536   1.00 53.66  ?  -29 GLU A O     1 
ATOM   73   C  CB    . GLU A 1 10  ? 23.683  -1.255  4.007   1.00 50.90  ?  -29 GLU A CB    1 
ATOM   74   C  CG    . GLU A 1 10  ? 24.141  -2.528  3.269   1.00 54.78  ?  -29 GLU A CG    1 
ATOM   75   C  CD    . GLU A 1 10  ? 23.886  -3.824  4.046   1.00 58.49  ?  -29 GLU A CD    1 
ATOM   76   O  OE1   . GLU A 1 10  ? 24.101  -3.846  5.282   1.00 57.80  ?  -29 GLU A OE1   1 
ATOM   77   O  OE2   . GLU A 1 10  ? 23.478  -4.833  3.418   1.00 56.56  ?  -29 GLU A OE2   1 
ATOM   78   N  N     . GLN A 1 11  ? 23.698  1.788   4.898   1.00 56.84  ?  -28 GLN A N     1 
ATOM   79   C  CA    . GLN A 1 11  ? 22.999  2.790   5.694   1.00 54.42  ?  -28 GLN A CA    1 
ATOM   80   C  C     . GLN A 1 11  ? 22.807  4.098   4.938   1.00 52.69  ?  -28 GLN A C     1 
ATOM   81   O  O     . GLN A 1 11  ? 21.774  4.749   5.119   1.00 51.58  ?  -28 GLN A O     1 
ATOM   82   C  CB    . GLN A 1 11  ? 23.730  3.018   7.023   1.00 58.12  ?  -28 GLN A CB    1 
ATOM   83   C  CG    . GLN A 1 11  ? 22.851  3.659   8.099   1.00 60.56  ?  -28 GLN A CG    1 
ATOM   84   C  CD    . GLN A 1 11  ? 23.041  3.053   9.477   1.00 59.55  ?  -28 GLN A CD    1 
ATOM   85   O  OE1   . GLN A 1 11  ? 22.123  3.074   10.300  1.00 58.08  ?  -28 GLN A OE1   1 
ATOM   86   N  NE2   . GLN A 1 11  ? 24.231  2.511   9.740   1.00 62.57  ?  -28 GLN A NE2   1 
ATOM   87   N  N     . GLU A 1 12  ? 23.758  4.487   4.075   1.00 52.75  ?  -27 GLU A N     1 
ATOM   88   C  CA    . GLU A 1 12  ? 23.556  5.668   3.233   1.00 56.09  ?  -27 GLU A CA    1 
ATOM   89   C  C     . GLU A 1 12  ? 22.371  5.473   2.297   1.00 54.53  ?  -27 GLU A C     1 
ATOM   90   O  O     . GLU A 1 12  ? 21.572  6.398   2.085   1.00 52.17  ?  -27 GLU A O     1 
ATOM   91   C  CB    . GLU A 1 12  ? 24.819  5.977   2.422   1.00 55.18  ?  -27 GLU A CB    1 
ATOM   92   N  N     . ALA A 1 13  ? 22.262  4.277   1.716   1.00 51.71  ?  -26 ALA A N     1 
ATOM   93   C  CA    . ALA A 1 13  ? 21.095  3.904   0.921   1.00 51.58  ?  -26 ALA A CA    1 
ATOM   94   C  C     . ALA A 1 13  ? 19.786  4.149   1.670   1.00 53.26  ?  -26 ALA A C     1 
ATOM   95   O  O     . ALA A 1 13  ? 18.873  4.810   1.159   1.00 51.57  ?  -26 ALA A O     1 
ATOM   96   C  CB    . ALA A 1 13  ? 21.211  2.435   0.533   1.00 46.17  ?  -26 ALA A CB    1 
ATOM   97   N  N     . ILE A 1 14  ? 19.672  3.614   2.888   1.00 51.27  ?  -25 ILE A N     1 
ATOM   98   C  CA    . ILE A 1 14  ? 18.402  3.694   3.601   1.00 51.07  ?  -25 ILE A CA    1 
ATOM   99   C  C     . ILE A 1 14  ? 18.100  5.133   4.002   1.00 50.79  ?  -25 ILE A C     1 
ATOM   100  O  O     . ILE A 1 14  ? 16.942  5.569   3.981   1.00 50.17  ?  -25 ILE A O     1 
ATOM   101  C  CB    . ILE A 1 14  ? 18.416  2.739   4.811   1.00 55.39  ?  -25 ILE A CB    1 
ATOM   102  C  CG1   . ILE A 1 14  ? 18.537  1.287   4.333   1.00 50.77  ?  -25 ILE A CG1   1 
ATOM   103  C  CG2   . ILE A 1 14  ? 17.172  2.903   5.657   1.00 52.13  ?  -25 ILE A CG2   1 
ATOM   104  C  CD1   . ILE A 1 14  ? 18.874  0.315   5.436   1.00 55.31  ?  -25 ILE A CD1   1 
ATOM   105  N  N     . MET A 1 15  ? 19.128  5.903   4.362   1.00 56.33  ?  -24 MET A N     1 
ATOM   106  C  CA    . MET A 1 15  ? 18.882  7.290   4.744   1.00 54.69  ?  -24 MET A CA    1 
ATOM   107  C  C     . MET A 1 15  ? 18.411  8.120   3.555   1.00 54.31  ?  -24 MET A C     1 
ATOM   108  O  O     . MET A 1 15  ? 17.639  9.071   3.737   1.00 55.51  ?  -24 MET A O     1 
ATOM   109  C  CB    . MET A 1 15  ? 20.133  7.903   5.370   1.00 48.46  ?  -24 MET A CB    1 
ATOM   110  C  CG    . MET A 1 15  ? 20.649  7.160   6.589   1.00 56.04  ?  -24 MET A CG    1 
ATOM   111  S  SD    . MET A 1 15  ? 19.796  7.551   8.125   1.00 61.93  ?  -24 MET A SD    1 
ATOM   112  C  CE    . MET A 1 15  ? 19.724  9.347   8.023   1.00 55.27  ?  -24 MET A CE    1 
ATOM   113  N  N     . LYS A 1 16  ? 18.852  7.781   2.336   1.00 51.92  ?  -23 LYS A N     1 
ATOM   114  C  CA    . LYS A 1 16  ? 18.343  8.484   1.159   1.00 52.77  ?  -23 LYS A CA    1 
ATOM   115  C  C     . LYS A 1 16  ? 16.853  8.221   0.958   1.00 53.69  ?  -23 LYS A C     1 
ATOM   116  O  O     . LYS A 1 16  ? 16.084  9.154   0.693   1.00 55.42  ?  -23 LYS A O     1 
ATOM   117  C  CB    . LYS A 1 16  ? 19.127  8.089   -0.088  1.00 53.91  ?  -23 LYS A CB    1 
ATOM   118  C  CG    . LYS A 1 16  ? 20.547  8.626   -0.117  1.00 59.48  ?  -23 LYS A CG    1 
ATOM   119  C  CD    . LYS A 1 16  ? 21.216  8.410   -1.465  1.00 60.90  ?  -23 LYS A CD    1 
ATOM   120  C  CE    . LYS A 1 16  ? 22.596  7.750   -1.320  1.00 62.76  ?  -23 LYS A CE    1 
ATOM   121  N  NZ    . LYS A 1 16  ? 22.538  6.257   -1.530  1.00 64.19  ?  -23 LYS A NZ    1 
ATOM   122  N  N     . VAL A 1 17  ? 16.423  6.961   1.085   1.00 50.10  ?  -22 VAL A N     1 
ATOM   123  C  CA    . VAL A 1 17  ? 14.993  6.657   1.064   1.00 47.00  ?  -22 VAL A CA    1 
ATOM   124  C  C     . VAL A 1 17  ? 14.253  7.449   2.139   1.00 50.98  ?  -22 VAL A C     1 
ATOM   125  O  O     . VAL A 1 17  ? 13.149  7.958   1.913   1.00 50.24  ?  -22 VAL A O     1 
ATOM   126  C  CB    . VAL A 1 17  ? 14.780  5.141   1.228   1.00 48.39  ?  -22 VAL A CB    1 
ATOM   127  C  CG1   . VAL A 1 17  ? 13.299  4.795   1.188   1.00 43.57  ?  -22 VAL A CG1   1 
ATOM   128  C  CG2   . VAL A 1 17  ? 15.553  4.385   0.160   1.00 49.60  ?  -22 VAL A CG2   1 
ATOM   129  N  N     . LEU A 1 18  ? 14.837  7.554   3.335   1.00 52.34  ?  -21 LEU A N     1 
ATOM   130  C  CA    . LEU A 1 18  ? 14.181  8.318   4.394   1.00 56.03  ?  -21 LEU A CA    1 
ATOM   131  C  C     . LEU A 1 18  ? 14.154  9.799   4.052   1.00 56.48  ?  -21 LEU A C     1 
ATOM   132  O  O     . LEU A 1 18  ? 13.169  10.498  4.336   1.00 56.99  ?  -21 LEU A O     1 
ATOM   133  C  CB    . LEU A 1 18  ? 14.890  8.087   5.730   1.00 50.16  ?  -21 LEU A CB    1 
ATOM   134  C  CG    . LEU A 1 18  ? 14.514  6.725   6.278   1.00 49.67  ?  -21 LEU A CG    1 
ATOM   135  C  CD1   . LEU A 1 18  ? 15.334  6.358   7.517   1.00 52.32  ?  -21 LEU A CD1   1 
ATOM   136  C  CD2   . LEU A 1 18  ? 13.024  6.740   6.570   1.00 53.95  ?  -21 LEU A CD2   1 
ATOM   137  N  N     . GLN A 1 19  ? 15.234  10.293  3.452   1.00 53.84  ?  -20 GLN A N     1 
ATOM   138  C  CA    . GLN A 1 19  ? 15.238  11.665  2.971   1.00 57.24  ?  -20 GLN A CA    1 
ATOM   139  C  C     . GLN A 1 19  ? 14.171  11.872  1.895   1.00 58.78  ?  -20 GLN A C     1 
ATOM   140  O  O     . GLN A 1 19  ? 13.413  12.848  1.948   1.00 60.09  ?  -20 GLN A O     1 
ATOM   141  C  CB    . GLN A 1 19  ? 16.638  12.013  2.466   1.00 60.72  ?  -20 GLN A CB    1 
ATOM   142  C  CG    . GLN A 1 19  ? 16.789  13.376  1.828   1.00 70.26  ?  -20 GLN A CG    1 
ATOM   143  C  CD    . GLN A 1 19  ? 18.217  13.623  1.335   1.00 77.58  ?  -20 GLN A CD    1 
ATOM   144  O  OE1   . GLN A 1 19  ? 18.870  12.714  0.804   1.00 78.34  ?  -20 GLN A OE1   1 
ATOM   145  N  NE2   . GLN A 1 19  ? 18.703  14.857  1.503   1.00 78.67  ?  -20 GLN A NE2   1 
ATOM   146  N  N     . ARG A 1 20  ? 14.058  10.941  0.936   1.00 57.49  ?  -19 ARG A N     1 
ATOM   147  C  CA    . ARG A 1 20  ? 13.034  11.079  -0.105  1.00 55.56  ?  -19 ARG A CA    1 
ATOM   148  C  C     . ARG A 1 20  ? 11.628  11.003  0.479   1.00 58.12  ?  -19 ARG A C     1 
ATOM   149  O  O     . ARG A 1 20  ? 10.728  11.722  0.030   1.00 62.80  ?  -19 ARG A O     1 
ATOM   150  C  CB    . ARG A 1 20  ? 13.200  10.011  -1.194  1.00 49.45  ?  -19 ARG A CB    1 
ATOM   151  C  CG    . ARG A 1 20  ? 14.309  10.278  -2.161  1.00 44.89  ?  -19 ARG A CG    1 
ATOM   152  C  CD    . ARG A 1 20  ? 14.671  9.042   -2.957  1.00 51.31  ?  -19 ARG A CD    1 
ATOM   153  N  NE    . ARG A 1 20  ? 13.500  8.383   -3.534  1.00 54.46  ?  -19 ARG A NE    1 
ATOM   154  C  CZ    . ARG A 1 20  ? 13.308  7.062   -3.529  1.00 52.22  ?  -19 ARG A CZ    1 
ATOM   155  N  NH1   . ARG A 1 20  ? 14.207  6.254   -2.965  1.00 51.65  ?  -19 ARG A NH1   1 
ATOM   156  N  NH2   . ARG A 1 20  ? 12.209  6.546   -4.068  1.00 50.63  ?  -19 ARG A NH2   1 
ATOM   157  N  N     . ASP A 1 21  ? 11.411  10.125  1.465   1.00 58.39  ?  -18 ASP A N     1 
ATOM   158  C  CA    . ASP A 1 21  ? 10.080  9.976   2.051   1.00 58.77  ?  -18 ASP A CA    1 
ATOM   159  C  C     . ASP A 1 21  ? 9.651   11.261  2.750   1.00 60.60  ?  -18 ASP A C     1 
ATOM   160  O  O     . ASP A 1 21  ? 8.520   11.731  2.577   1.00 60.83  ?  -18 ASP A O     1 
ATOM   161  C  CB    . ASP A 1 21  ? 10.068  8.791   3.022   1.00 53.88  ?  -18 ASP A CB    1 
ATOM   162  C  CG    . ASP A 1 21  ? 8.750   8.653   3.759   1.00 56.68  ?  -18 ASP A CG    1 
ATOM   163  O  OD1   . ASP A 1 21  ? 7.711   8.540   3.075   1.00 53.90  ?  -18 ASP A OD1   1 
ATOM   164  O  OD2   . ASP A 1 21  ? 8.749   8.651   5.020   1.00 62.96  ?  -18 ASP A OD2   1 
ATOM   165  N  N     . ALA A 1 22  ? 10.558  11.858  3.527   1.00 61.25  ?  -17 ALA A N     1 
ATOM   166  C  CA    . ALA A 1 22  ? 10.216  13.065  4.269   1.00 63.47  ?  -17 ALA A CA    1 
ATOM   167  C  C     . ALA A 1 22  ? 9.926   14.235  3.341   1.00 64.29  ?  -17 ALA A C     1 
ATOM   168  O  O     . ALA A 1 22  ? 9.039   15.046  3.636   1.00 65.97  ?  -17 ALA A O     1 
ATOM   169  C  CB    . ALA A 1 22  ? 11.337  13.409  5.246   1.00 62.96  ?  -17 ALA A CB    1 
ATOM   170  N  N     . ALA A 1 23  ? 10.647  14.337  2.220   1.00 61.50  ?  -16 ALA A N     1 
ATOM   171  C  CA    . ALA A 1 23  ? 10.327  15.359  1.228   1.00 60.58  ?  -16 ALA A CA    1 
ATOM   172  C  C     . ALA A 1 23  ? 8.954   15.119  0.628   1.00 65.90  ?  -16 ALA A C     1 
ATOM   173  O  O     . ALA A 1 23  ? 8.180   16.058  0.430   1.00 71.21  ?  -16 ALA A O     1 
ATOM   174  C  CB    . ALA A 1 23  ? 11.376  15.382  0.120   1.00 58.42  ?  -16 ALA A CB    1 
ATOM   175  N  N     . LEU A 1 24  ? 8.636   13.868  0.316   1.00 66.18  ?  -15 LEU A N     1 
ATOM   176  C  CA    . LEU A 1 24  ? 7.314   13.580  -0.213  1.00 62.90  ?  -15 LEU A CA    1 
ATOM   177  C  C     . LEU A 1 24  ? 6.246   13.870  0.827   1.00 65.67  ?  -15 LEU A C     1 
ATOM   178  O  O     . LEU A 1 24  ? 5.225   14.489  0.512   1.00 72.13  ?  -15 LEU A O     1 
ATOM   179  C  CB    . LEU A 1 24  ? 7.245   12.128  -0.692  1.00 58.36  ?  -15 LEU A CB    1 
ATOM   180  C  CG    . LEU A 1 24  ? 5.870   11.549  -1.024  1.00 55.86  ?  -15 LEU A CG    1 
ATOM   181  C  CD1   . LEU A 1 24  ? 5.020   12.498  -1.868  1.00 62.86  ?  -15 LEU A CD1   1 
ATOM   182  C  CD2   . LEU A 1 24  ? 6.052   10.235  -1.731  1.00 52.88  ?  -15 LEU A CD2   1 
ATOM   183  N  N     . LYS A 1 25  ? 6.465   13.449  2.078   1.00 66.07  ?  -14 LYS A N     1 
ATOM   184  C  CA    . LYS A 1 25  ? 5.435   13.638  3.096   1.00 62.96  ?  -14 LYS A CA    1 
ATOM   185  C  C     . LYS A 1 25  ? 5.225   15.115  3.395   1.00 69.21  ?  -14 LYS A C     1 
ATOM   186  O  O     . LYS A 1 25  ? 4.084   15.566  3.556   1.00 72.81  ?  -14 LYS A O     1 
ATOM   187  C  CB    . LYS A 1 25  ? 5.797   12.886  4.376   1.00 61.95  ?  -14 LYS A CB    1 
ATOM   188  C  CG    . LYS A 1 25  ? 5.757   11.379  4.259   1.00 58.98  ?  -14 LYS A CG    1 
ATOM   189  C  CD    . LYS A 1 25  ? 4.343   10.869  4.099   1.00 57.51  ?  -14 LYS A CD    1 
ATOM   190  C  CE    . LYS A 1 25  ? 4.221   9.427   4.580   1.00 56.26  ?  -14 LYS A CE    1 
ATOM   191  N  NZ    . LYS A 1 25  ? 5.198   8.486   3.920   1.00 51.11  ?  -14 LYS A NZ    1 
ATOM   192  N  N     . ARG A 1 26  ? 6.311   15.890  3.467   1.00 68.75  ?  -13 ARG A N     1 
ATOM   193  C  CA    . ARG A 1 26  ? 6.157   17.298  3.814   1.00 71.88  ?  -13 ARG A CA    1 
ATOM   194  C  C     . ARG A 1 26  ? 5.391   18.056  2.746   1.00 74.37  ?  -13 ARG A C     1 
ATOM   195  O  O     . ARG A 1 26  ? 4.696   19.026  3.062   1.00 78.72  ?  -13 ARG A O     1 
ATOM   196  C  CB    . ARG A 1 26  ? 7.518   17.955  4.054   1.00 70.83  ?  -13 ARG A CB    1 
ATOM   197  C  CG    . ARG A 1 26  ? 7.792   18.285  5.528   1.00 67.72  ?  -13 ARG A CG    1 
ATOM   198  C  CD    . ARG A 1 26  ? 9.140   18.942  5.695   1.00 66.80  ?  -13 ARG A CD    1 
ATOM   199  N  NE    . ARG A 1 26  ? 9.947   18.252  6.685   1.00 68.53  ?  -13 ARG A NE    1 
ATOM   200  C  CZ    . ARG A 1 26  ? 11.038  17.549  6.391   1.00 68.85  ?  -13 ARG A CZ    1 
ATOM   201  N  NH1   . ARG A 1 26  ? 11.447  17.456  5.127   1.00 65.73  ?  -13 ARG A NH1   1 
ATOM   202  N  NH2   . ARG A 1 26  ? 11.719  16.936  7.360   1.00 66.52  ?  -13 ARG A NH2   1 
ATOM   203  N  N     . ALA A 1 27  ? 5.488   17.622  1.487   1.00 75.73  ?  -12 ALA A N     1 
ATOM   204  C  CA    . ALA A 1 27  ? 4.779   18.304  0.409   1.00 76.83  ?  -12 ALA A CA    1 
ATOM   205  C  C     . ALA A 1 27  ? 3.281   18.031  0.447   1.00 81.32  ?  -12 ALA A C     1 
ATOM   206  O  O     . ALA A 1 27  ? 2.493   18.851  -0.038  1.00 86.97  ?  -12 ALA A O     1 
ATOM   207  C  CB    . ALA A 1 27  ? 5.354   17.895  -0.942  1.00 63.60  ?  -12 ALA A CB    1 
ATOM   208  N  N     . GLU A 1 28  ? 2.864   16.900  1.013   1.00 80.99  ?  -11 GLU A N     1 
ATOM   209  C  CA    . GLU A 1 28  ? 1.438   16.600  1.060   1.00 83.87  ?  -11 GLU A CA    1 
ATOM   210  C  C     . GLU A 1 28  ? 0.766   17.304  2.237   1.00 87.92  ?  -11 GLU A C     1 
ATOM   211  O  O     . GLU A 1 28  ? -0.341  17.843  2.092   1.00 89.52  ?  -11 GLU A O     1 
ATOM   212  C  CB    . GLU A 1 28  ? 1.238   15.080  1.102   1.00 80.27  ?  -11 GLU A CB    1 
ATOM   213  C  CG    . GLU A 1 28  ? 1.174   14.388  2.460   1.00 81.68  ?  -11 GLU A CG    1 
ATOM   214  C  CD    . GLU A 1 28  ? -0.249  14.260  2.968   1.00 87.39  ?  -11 GLU A CD    1 
ATOM   215  O  OE1   . GLU A 1 28  ? -1.170  14.363  2.126   1.00 86.37  ?  -11 GLU A OE1   1 
ATOM   216  O  OE2   . GLU A 1 28  ? -0.443  14.034  4.186   1.00 95.04  ?  -11 GLU A OE2   1 
ATOM   217  N  N     . GLU A 1 29  ? 1.431   17.323  3.402   1.00 87.76  ?  -10 GLU A N     1 
ATOM   218  C  CA    . GLU A 1 29  ? 1.005   18.133  4.540   1.00 89.75  ?  -10 GLU A CA    1 
ATOM   219  C  C     . GLU A 1 29  ? 0.950   19.619  4.201   1.00 94.31  ?  -10 GLU A C     1 
ATOM   220  O  O     . GLU A 1 29  ? 0.419   20.399  5.000   1.00 93.36  ?  -10 GLU A O     1 
ATOM   221  C  CB    . GLU A 1 29  ? 1.960   17.907  5.721   1.00 87.77  ?  -10 GLU A CB    1 
ATOM   222  C  CG    . GLU A 1 29  ? 1.640   18.716  6.980   1.00 89.42  ?  -10 GLU A CG    1 
ATOM   223  C  CD    . GLU A 1 29  ? 2.890   19.138  7.748   1.00 87.18  ?  -10 GLU A CD    1 
ATOM   224  O  OE1   . GLU A 1 29  ? 2.847   20.203  8.399   1.00 86.30  ?  -10 GLU A OE1   1 
ATOM   225  O  OE2   . GLU A 1 29  ? 3.908   18.410  7.707   1.00 87.62  ?  -10 GLU A OE2   1 
ATOM   226  N  N     . GLU A 1 30  ? 1.482   20.013  3.039   1.00 93.38  ?  -9  GLU A N     1 
ATOM   227  C  CA    . GLU A 1 30  ? 1.511   21.391  2.552   1.00 91.32  ?  -9  GLU A CA    1 
ATOM   228  C  C     . GLU A 1 30  ? 2.002   22.365  3.629   1.00 97.44  ?  -9  GLU A C     1 
ATOM   229  O  O     . GLU A 1 30  ? 3.099   22.197  4.183   1.00 96.47  ?  -9  GLU A O     1 
ATOM   230  C  CB    . GLU A 1 30  ? 0.128   21.797  2.024   1.00 91.70  ?  -9  GLU A CB    1 
ATOM   231  C  CG    . GLU A 1 30  ? -0.276  21.050  0.740   1.00 91.94  ?  -9  GLU A CG    1 
ATOM   232  C  CD    . GLU A 1 30  ? -1.701  21.337  0.288   1.00 87.98  ?  -9  GLU A CD    1 
ATOM   233  O  OE1   . GLU A 1 30  ? -2.248  22.401  0.652   1.00 88.71  ?  -9  GLU A OE1   1 
ATOM   234  O  OE2   . GLU A 1 30  ? -2.274  20.493  -0.435  1.00 88.33  ?  -9  GLU A OE2   1 
ATOM   235  N  N     . ASP A 1 43  ? -3.608  20.051  -5.228  1.00 77.26  ?  -8  ASP A N     1 
ATOM   236  C  CA    . ASP A 1 43  ? -3.230  19.171  -6.360  1.00 76.63  ?  -8  ASP A CA    1 
ATOM   237  C  C     . ASP A 1 43  ? -3.969  17.843  -6.207  1.00 82.67  ?  -8  ASP A C     1 
ATOM   238  O  O     . ASP A 1 43  ? -5.183  17.878  -5.977  1.00 83.44  ?  -8  ASP A O     1 
ATOM   239  C  CB    . ASP A 1 43  ? -1.717  19.023  -6.496  1.00 74.82  ?  -8  ASP A CB    1 
ATOM   240  N  N     . TYR A 1 44  ? -3.245  16.723  -6.144  1.00 81.19  ?  -7  TYR A N     1 
ATOM   241  C  CA    . TYR A 1 44  ? -3.882  15.383  -6.090  1.00 75.14  ?  -7  TYR A CA    1 
ATOM   242  C  C     . TYR A 1 44  ? -4.787  15.261  -4.880  1.00 71.62  ?  -7  TYR A C     1 
ATOM   243  O  O     . TYR A 1 44  ? -4.535  15.804  -3.832  1.00 75.80  ?  -7  TYR A O     1 
ATOM   244  C  CB    . TYR A 1 44  ? -2.867  14.251  -6.119  1.00 71.44  ?  -7  TYR A CB    1 
ATOM   245  C  CG    . TYR A 1 44  ? -1.985  14.263  -4.912  1.00 74.77  ?  -7  TYR A CG    1 
ATOM   246  C  CD1   . TYR A 1 44  ? -0.647  14.553  -5.030  1.00 76.98  ?  -7  TYR A CD1   1 
ATOM   247  C  CD2   . TYR A 1 44  ? -2.494  14.041  -3.655  1.00 70.87  ?  -7  TYR A CD2   1 
ATOM   248  C  CE1   . TYR A 1 44  ? 0.184   14.584  -3.930  1.00 72.31  ?  -7  TYR A CE1   1 
ATOM   249  C  CE2   . TYR A 1 44  ? -1.678  14.074  -2.543  1.00 71.64  ?  -7  TYR A CE2   1 
ATOM   250  C  CZ    . TYR A 1 44  ? -0.333  14.334  -2.682  1.00 72.38  ?  -7  TYR A CZ    1 
ATOM   251  O  OH    . TYR A 1 44  ? 0.497   14.381  -1.611  1.00 77.03  ?  -7  TYR A OH    1 
ATOM   252  N  N     . ASP A 1 45  ? -5.847  14.505  -5.077  1.00 71.72  ?  -6  ASP A N     1 
ATOM   253  C  CA    . ASP A 1 45  ? -6.935  14.403  -4.082  1.00 74.74  ?  -6  ASP A CA    1 
ATOM   254  C  C     . ASP A 1 45  ? -6.577  13.598  -2.835  1.00 71.04  ?  -6  ASP A C     1 
ATOM   255  O  O     . ASP A 1 45  ? -7.044  14.022  -1.831  1.00 71.94  ?  -6  ASP A O     1 
ATOM   256  C  CB    . ASP A 1 45  ? -8.286  14.180  -4.757  1.00 73.65  ?  -6  ASP A CB    1 
ATOM   257  C  CG    . ASP A 1 45  ? -8.643  15.381  -5.606  1.00 77.53  ?  -6  ASP A CG    1 
ATOM   258  O  OD1   . ASP A 1 45  ? -8.051  16.428  -5.370  1.00 80.72  ?  -6  ASP A OD1   1 
ATOM   259  O  OD2   . ASP A 1 45  ? -9.471  15.247  -6.500  1.00 75.76  ?  -6  ASP A OD2   1 
ATOM   260  N  N     . TYR A 1 46  ? -5.801  12.519  -2.904  1.00 66.27  ?  -5  TYR A N     1 
ATOM   261  C  CA    . TYR A 1 46  ? -5.454  11.751  -1.708  1.00 68.81  ?  -5  TYR A CA    1 
ATOM   262  C  C     . TYR A 1 46  ? -4.063  11.168  -1.899  1.00 65.37  ?  -5  TYR A C     1 
ATOM   263  O  O     . TYR A 1 46  ? -3.700  10.786  -3.018  1.00 64.22  ?  -5  TYR A O     1 
ATOM   264  C  CB    . TYR A 1 46  ? -6.439  10.607  -1.416  1.00 64.53  ?  -5  TYR A CB    1 
ATOM   265  C  CG    . TYR A 1 46  ? -7.819  11.049  -0.975  1.00 72.19  ?  -5  TYR A CG    1 
ATOM   266  C  CD1   . TYR A 1 46  ? -8.941  10.749  -1.742  1.00 74.00  ?  -5  TYR A CD1   1 
ATOM   267  C  CD2   . TYR A 1 46  ? -8.007  11.769  0.204   1.00 74.40  ?  -5  TYR A CD2   1 
ATOM   268  C  CE1   . TYR A 1 46  ? -10.215 11.152  -1.352  1.00 73.89  ?  -5  TYR A CE1   1 
ATOM   269  C  CE2   . TYR A 1 46  ? -9.280  12.186  0.601   1.00 76.44  ?  -5  TYR A CE2   1 
ATOM   270  C  CZ    . TYR A 1 46  ? -10.381 11.869  -0.183  1.00 75.78  ?  -5  TYR A CZ    1 
ATOM   271  O  OH    . TYR A 1 46  ? -11.650 12.270  0.195   1.00 77.22  ?  -5  TYR A OH    1 
ATOM   272  N  N     . LEU A 1 47  ? -3.284  11.122  -0.820  1.00 56.21  ?  -4  LEU A N     1 
ATOM   273  C  CA    . LEU A 1 47  ? -2.096  10.280  -0.772  1.00 56.06  ?  -4  LEU A CA    1 
ATOM   274  C  C     . LEU A 1 47  ? -2.505  8.911   -0.256  1.00 54.22  ?  -4  LEU A C     1 
ATOM   275  O  O     . LEU A 1 47  ? -3.200  8.811   0.754   1.00 56.07  ?  -4  LEU A O     1 
ATOM   276  C  CB    . LEU A 1 47  ? -1.016  10.875  0.125   1.00 54.43  ?  -4  LEU A CB    1 
ATOM   277  C  CG    . LEU A 1 47  ? 0.266   10.050  0.207   1.00 54.35  ?  -4  LEU A CG    1 
ATOM   278  C  CD1   . LEU A 1 47  ? 0.904   9.922   -1.150  1.00 55.87  ?  -4  LEU A CD1   1 
ATOM   279  C  CD2   . LEU A 1 47  ? 1.248   10.690  1.154   1.00 58.94  ?  -4  LEU A CD2   1 
ATOM   280  N  N     . ILE A 1 48  ? -2.110  7.860   -0.960  1.00 52.66  ?  -3  ILE A N     1 
ATOM   281  C  CA    . ILE A 1 48  ? -2.434  6.497   -0.560  1.00 53.24  ?  -3  ILE A CA    1 
ATOM   282  C  C     . ILE A 1 48  ? -1.137  5.718   -0.485  1.00 54.00  ?  -3  ILE A C     1 
ATOM   283  O  O     . ILE A 1 48  ? -0.309  5.809   -1.398  1.00 53.08  ?  -3  ILE A O     1 
ATOM   284  C  CB    . ILE A 1 48  ? -3.410  5.821   -1.539  1.00 52.31  ?  -3  ILE A CB    1 
ATOM   285  C  CG1   . ILE A 1 48  ? -4.715  6.601   -1.611  1.00 55.79  ?  -3  ILE A CG1   1 
ATOM   286  C  CG2   . ILE A 1 48  ? -3.704  4.408   -1.108  1.00 50.66  ?  -3  ILE A CG2   1 
ATOM   287  C  CD1   . ILE A 1 48  ? -5.408  6.749   -0.280  1.00 54.37  ?  -3  ILE A CD1   1 
ATOM   288  N  N     . LYS A 1 49  ? -0.967  4.943   0.588   1.00 51.45  ?  -2  LYS A N     1 
ATOM   289  C  CA    . LYS A 1 49  ? 0.258   4.191   0.826   1.00 51.13  ?  -2  LYS A CA    1 
ATOM   290  C  C     . LYS A 1 49  ? -0.048  2.703   0.969   1.00 52.11  ?  -2  LYS A C     1 
ATOM   291  O  O     . LYS A 1 49  ? -0.920  2.311   1.755   1.00 53.49  ?  -2  LYS A O     1 
ATOM   292  C  CB    . LYS A 1 49  ? 0.972   4.733   2.067   1.00 52.02  ?  -2  LYS A CB    1 
ATOM   293  C  CG    . LYS A 1 49  ? 1.268   6.224   1.949   1.00 53.55  ?  -2  LYS A CG    1 
ATOM   294  C  CD    . LYS A 1 49  ? 1.617   6.863   3.280   1.00 55.17  ?  -2  LYS A CD    1 
ATOM   295  C  CE    . LYS A 1 49  ? 0.376   7.181   4.126   1.00 55.11  ?  -2  LYS A CE    1 
ATOM   296  N  NZ    . LYS A 1 49  ? 0.715   7.713   5.496   1.00 55.84  ?  -2  LYS A NZ    1 
ATOM   297  N  N     . PHE A 1 50  ? 0.657   1.885   0.189   1.00 49.61  ?  -1  PHE A N     1 
ATOM   298  C  CA    . PHE A 1 50  ? 0.709   0.440   0.340   1.00 46.23  ?  -1  PHE A CA    1 
ATOM   299  C  C     . PHE A 1 50  ? 2.099   0.019   0.768   1.00 46.65  ?  -1  PHE A C     1 
ATOM   300  O  O     . PHE A 1 50  ? 3.079   0.744   0.585   1.00 46.31  ?  -1  PHE A O     1 
ATOM   301  C  CB    . PHE A 1 50  ? 0.438   -0.308  -0.964  1.00 50.95  ?  -1  PHE A CB    1 
ATOM   302  C  CG    . PHE A 1 50  ? -0.794  0.103   -1.671  1.00 53.19  ?  -1  PHE A CG    1 
ATOM   303  C  CD1   . PHE A 1 50  ? -0.846  0.027   -3.061  1.00 54.71  ?  -1  PHE A CD1   1 
ATOM   304  C  CD2   . PHE A 1 50  ? -1.911  0.523   -0.971  1.00 54.34  ?  -1  PHE A CD2   1 
ATOM   305  C  CE1   . PHE A 1 50  ? -1.980  0.385   -3.742  1.00 55.89  ?  -1  PHE A CE1   1 
ATOM   306  C  CE2   . PHE A 1 50  ? -3.059  0.888   -1.652  1.00 58.87  ?  -1  PHE A CE2   1 
ATOM   307  C  CZ    . PHE A 1 50  ? -3.102  0.819   -3.037  1.00 55.32  ?  -1  PHE A CZ    1 
ATOM   308  N  N     . LEU A 1 51  ? 2.195   -1.217  1.241   1.00 46.86  ?  0   LEU A N     1 
ATOM   309  C  CA    . LEU A 1 51  ? 3.489   -1.780  1.575   1.00 44.32  ?  0   LEU A CA    1 
ATOM   310  C  C     . LEU A 1 51  ? 3.512   -3.207  1.069   1.00 46.61  ?  0   LEU A C     1 
ATOM   311  O  O     . LEU A 1 51  ? 2.539   -3.942  1.265   1.00 48.67  ?  0   LEU A O     1 
ATOM   312  C  CB    . LEU A 1 51  ? 3.732   -1.712  3.085   1.00 46.57  ?  0   LEU A CB    1 
ATOM   313  C  CG    . LEU A 1 51  ? 5.120   -2.091  3.582   1.00 45.93  ?  0   LEU A CG    1 
ATOM   314  C  CD1   . LEU A 1 51  ? 5.509   -1.196  4.754   1.00 42.83  ?  0   LEU A CD1   1 
ATOM   315  C  CD2   . LEU A 1 51  ? 5.108   -3.554  3.991   1.00 46.31  ?  0   LEU A CD2   1 
ATOM   316  N  N     . ALA A 1 52  ? 4.593   -3.583  0.377   1.00 46.07  ?  1   ALA A N     1 
ATOM   317  C  CA    . ALA A 1 52  ? 4.770   -4.944  -0.103  1.00 41.27  ?  1   ALA A CA    1 
ATOM   318  C  C     . ALA A 1 52  ? 5.682   -5.699  0.851   1.00 43.34  ?  1   ALA A C     1 
ATOM   319  O  O     . ALA A 1 52  ? 6.737   -5.189  1.249   1.00 47.10  ?  1   ALA A O     1 
ATOM   320  C  CB    . ALA A 1 52  ? 5.347   -4.960  -1.520  1.00 44.47  ?  1   ALA A CB    1 
ATOM   321  N  N     . LEU A 1 53  ? 5.279   -6.911  1.219   1.00 41.45  ?  2   LEU A N     1 
ATOM   322  C  CA    . LEU A 1 53  ? 6.046   -7.722  2.149   1.00 43.11  ?  2   LEU A CA    1 
ATOM   323  C  C     . LEU A 1 53  ? 5.922   -9.175  1.721   1.00 40.18  ?  2   LEU A C     1 
ATOM   324  O  O     . LEU A 1 53  ? 5.115   -9.525  0.854   1.00 43.97  ?  2   LEU A O     1 
ATOM   325  C  CB    . LEU A 1 53  ? 5.588   -7.493  3.604   1.00 39.96  ?  2   LEU A CB    1 
ATOM   326  C  CG    . LEU A 1 53  ? 4.277   -8.081  4.133   1.00 40.31  ?  2   LEU A CG    1 
ATOM   327  C  CD1   . LEU A 1 53  ? 4.132   -7.767  5.626   1.00 43.72  ?  2   LEU A CD1   1 
ATOM   328  C  CD2   . LEU A 1 53  ? 3.062   -7.583  3.386   1.00 41.39  ?  2   LEU A CD2   1 
ATOM   329  N  N     . GLY A 1 54  ? 6.769   -10.014 2.294   1.00 38.42  ?  3   GLY A N     1 
ATOM   330  C  CA    . GLY A 1 54  ? 6.873   -11.390 1.858   1.00 37.81  ?  3   GLY A CA    1 
ATOM   331  C  C     . GLY A 1 54  ? 8.321   -11.818 1.886   1.00 38.89  ?  3   GLY A C     1 
ATOM   332  O  O     . GLY A 1 54  ? 9.207   -10.987 2.118   1.00 40.28  ?  3   GLY A O     1 
ATOM   333  N  N     . ASP A 1 55  ? 8.578   -13.101 1.660   1.00 41.04  ?  4   ASP A N     1 
ATOM   334  C  CA    . ASP A 1 55  ? 9.927   -13.633 1.802   1.00 44.51  ?  4   ASP A CA    1 
ATOM   335  C  C     . ASP A 1 55  ? 10.850  -13.011 0.766   1.00 44.58  ?  4   ASP A C     1 
ATOM   336  O  O     . ASP A 1 55  ? 10.411  -12.509 -0.267  1.00 46.82  ?  4   ASP A O     1 
ATOM   337  C  CB    . ASP A 1 55  ? 9.924   -15.156 1.630   1.00 46.05  ?  4   ASP A CB    1 
ATOM   338  C  CG    . ASP A 1 55  ? 9.457   -15.897 2.878   1.00 50.51  ?  4   ASP A CG    1 
ATOM   339  O  OD1   . ASP A 1 55  ? 9.265   -15.258 3.933   1.00 51.27  ?  4   ASP A OD1   1 
ATOM   340  O  OD2   . ASP A 1 55  ? 9.296   -17.139 2.803   1.00 54.78  ?  4   ASP A OD2   1 
ATOM   341  N  N     . SER A 1 56  ? 12.149  -13.075 1.026   1.00 42.25  ?  5   SER A N     1 
ATOM   342  C  CA    . SER A 1 56  ? 13.095  -12.591 0.037   1.00 38.99  ?  5   SER A CA    1 
ATOM   343  C  C     . SER A 1 56  ? 13.048  -13.486 -1.209  1.00 46.54  ?  5   SER A C     1 
ATOM   344  O  O     . SER A 1 56  ? 13.007  -14.726 -1.122  1.00 47.11  ?  5   SER A O     1 
ATOM   345  C  CB    . SER A 1 56  ? 14.508  -12.540 0.615   1.00 40.19  ?  5   SER A CB    1 
ATOM   346  O  OG    . SER A 1 56  ? 15.490  -12.584 -0.431  1.00 43.90  ?  5   SER A OG    1 
ATOM   347  N  N     . GLY A 1 57  ? 12.987  -12.848 -2.372  1.00 45.56  ?  6   GLY A N     1 
ATOM   348  C  CA    . GLY A 1 57  ? 13.045  -13.532 -3.645  1.00 47.10  ?  6   GLY A CA    1 
ATOM   349  C  C     . GLY A 1 57  ? 11.703  -13.806 -4.291  1.00 47.55  ?  6   GLY A C     1 
ATOM   350  O  O     . GLY A 1 57  ? 11.675  -14.316 -5.412  1.00 49.03  ?  6   GLY A O     1 
ATOM   351  N  N     . VAL A 1 58  ? 10.588  -13.479 -3.632  1.00 47.93  ?  7   VAL A N     1 
ATOM   352  C  CA    . VAL A 1 58  ? 9.282   -13.773 -4.220  1.00 48.38  ?  7   VAL A CA    1 
ATOM   353  C  C     . VAL A 1 58  ? 8.892   -12.824 -5.346  1.00 42.10  ?  7   VAL A C     1 
ATOM   354  O  O     . VAL A 1 58  ? 7.926   -13.101 -6.055  1.00 45.46  ?  7   VAL A O     1 
ATOM   355  C  CB    . VAL A 1 58  ? 8.206   -13.744 -3.116  1.00 46.97  ?  7   VAL A CB    1 
ATOM   356  C  CG1   . VAL A 1 58  ? 8.534   -14.766 -2.046  1.00 42.70  ?  7   VAL A CG1   1 
ATOM   357  C  CG2   . VAL A 1 58  ? 8.089   -12.346 -2.528  1.00 42.95  ?  7   VAL A CG2   1 
ATOM   358  N  N     . GLY A 1 59  ? 9.584   -11.695 -5.506  1.00 42.23  ?  8   GLY A N     1 
ATOM   359  C  CA    . GLY A 1 59  ? 9.296   -10.750 -6.565  1.00 40.47  ?  8   GLY A CA    1 
ATOM   360  C  C     . GLY A 1 59  ? 8.620   -9.454  -6.146  1.00 45.06  ?  8   GLY A C     1 
ATOM   361  O  O     . GLY A 1 59  ? 7.854   -8.898  -6.931  1.00 42.40  ?  8   GLY A O     1 
ATOM   362  N  N     . LYS A 1 60  ? 8.897   -8.944  -4.935  1.00 46.26  ?  9   LYS A N     1 
ATOM   363  C  CA    . LYS A 1 60  ? 8.225   -7.730  -4.475  1.00 43.11  ?  9   LYS A CA    1 
ATOM   364  C  C     . LYS A 1 60  ? 8.687   -6.512  -5.264  1.00 42.22  ?  9   LYS A C     1 
ATOM   365  O  O     . LYS A 1 60  ? 7.871   -5.701  -5.718  1.00 43.69  ?  9   LYS A O     1 
ATOM   366  C  CB    . LYS A 1 60  ? 8.478   -7.514  -2.974  1.00 42.73  ?  9   LYS A CB    1 
ATOM   367  C  CG    . LYS A 1 60  ? 7.926   -8.604  -2.075  1.00 43.46  ?  9   LYS A CG    1 
ATOM   368  C  CD    . LYS A 1 60  ? 8.305   -8.405  -0.645  1.00 40.04  ?  9   LYS A CD    1 
ATOM   369  C  CE    . LYS A 1 60  ? 9.822   -8.452  -0.439  1.00 41.78  ?  9   LYS A CE    1 
ATOM   370  N  NZ    . LYS A 1 60  ? 10.353  -9.848  -0.552  1.00 36.06  ?  9   LYS A NZ    1 
ATOM   371  N  N     . THR A 1 61  ? 9.997   -6.331  -5.386  1.00 40.38  ?  10  THR A N     1 
ATOM   372  C  CA    . THR A 1 61  ? 10.516  -5.224  -6.179  1.00 42.40  ?  10  THR A CA    1 
ATOM   373  C  C     . THR A 1 61  ? 10.046  -5.313  -7.635  1.00 46.06  ?  10  THR A C     1 
ATOM   374  O  O     . THR A 1 61  ? 9.599   -4.316  -8.225  1.00 44.53  ?  10  THR A O     1 
ATOM   375  C  CB    . THR A 1 61  ? 12.039  -5.238  -6.100  1.00 45.48  ?  10  THR A CB    1 
ATOM   376  O  OG1   . THR A 1 61  ? 12.435  -5.196  -4.720  1.00 48.03  ?  10  THR A OG1   1 
ATOM   377  C  CG2   . THR A 1 61  ? 12.624  -4.078  -6.868  1.00 44.06  ?  10  THR A CG2   1 
ATOM   378  N  N     . SER A 1 62  ? 10.132  -6.510  -8.227  1.00 43.50  ?  11  SER A N     1 
ATOM   379  C  CA    . SER A 1 62  ? 9.732   -6.690  -9.618  1.00 40.34  ?  11  SER A CA    1 
ATOM   380  C  C     . SER A 1 62  ? 8.254   -6.397  -9.821  1.00 43.03  ?  11  SER A C     1 
ATOM   381  O  O     . SER A 1 62  ? 7.854   -5.861  -10.860 1.00 45.98  ?  11  SER A O     1 
ATOM   382  C  CB    . SER A 1 62  ? 10.056  -8.105  -10.071 1.00 39.30  ?  11  SER A CB    1 
ATOM   383  O  OG    . SER A 1 62  ? 11.435  -8.372  -9.901  1.00 41.96  ?  11  SER A OG    1 
ATOM   384  N  N     . VAL A 1 63  ? 7.421   -6.737  -8.847  1.00 45.24  ?  12  VAL A N     1 
ATOM   385  C  CA    . VAL A 1 63  ? 5.995   -6.498  -9.025  1.00 46.40  ?  12  VAL A CA    1 
ATOM   386  C  C     . VAL A 1 63  ? 5.722   -5.004  -9.074  1.00 47.97  ?  12  VAL A C     1 
ATOM   387  O  O     . VAL A 1 63  ? 5.014   -4.514  -9.962  1.00 50.58  ?  12  VAL A O     1 
ATOM   388  C  CB    . VAL A 1 63  ? 5.185   -7.195  -7.918  1.00 43.28  ?  12  VAL A CB    1 
ATOM   389  C  CG1   . VAL A 1 63  ? 3.841   -6.508  -7.734  1.00 39.21  ?  12  VAL A CG1   1 
ATOM   390  C  CG2   . VAL A 1 63  ? 4.979   -8.658  -8.280  1.00 39.98  ?  12  VAL A CG2   1 
ATOM   391  N  N     . LEU A 1 64  ? 6.321   -4.246  -8.157  1.00 44.47  ?  13  LEU A N     1 
ATOM   392  C  CA    . LEU A 1 64  ? 6.071   -2.810  -8.183  1.00 47.52  ?  13  LEU A CA    1 
ATOM   393  C  C     . LEU A 1 64  ? 6.691   -2.153  -9.416  1.00 45.44  ?  13  LEU A C     1 
ATOM   394  O  O     . LEU A 1 64  ? 6.128   -1.196  -9.954  1.00 44.88  ?  13  LEU A O     1 
ATOM   395  C  CB    . LEU A 1 64  ? 6.580   -2.173  -6.893  1.00 41.92  ?  13  LEU A CB    1 
ATOM   396  C  CG    . LEU A 1 64  ? 5.991   -2.850  -5.656  1.00 43.24  ?  13  LEU A CG    1 
ATOM   397  C  CD1   . LEU A 1 64  ? 6.790   -2.452  -4.428  1.00 44.96  ?  13  LEU A CD1   1 
ATOM   398  C  CD2   . LEU A 1 64  ? 4.521   -2.501  -5.473  1.00 39.90  ?  13  LEU A CD2   1 
ATOM   399  N  N     . TYR A 1 65  ? 7.832   -2.659  -9.876  1.00 43.11  ?  14  TYR A N     1 
ATOM   400  C  CA    . TYR A 1 65  ? 8.485   -2.124  -11.063 1.00 48.13  ?  14  TYR A CA    1 
ATOM   401  C  C     . TYR A 1 65  ? 7.659   -2.376  -12.319 1.00 46.84  ?  14  TYR A C     1 
ATOM   402  O  O     . TYR A 1 65  ? 7.541   -1.501  -13.182 1.00 48.51  ?  14  TYR A O     1 
ATOM   403  C  CB    . TYR A 1 65  ? 9.863   -2.764  -11.197 1.00 48.41  ?  14  TYR A CB    1 
ATOM   404  C  CG    . TYR A 1 65  ? 10.760  -2.083  -12.176 1.00 50.55  ?  14  TYR A CG    1 
ATOM   405  C  CD1   . TYR A 1 65  ? 10.829  -0.700  -12.231 1.00 50.10  ?  14  TYR A CD1   1 
ATOM   406  C  CD2   . TYR A 1 65  ? 11.558  -2.825  -13.047 1.00 53.47  ?  14  TYR A CD2   1 
ATOM   407  C  CE1   . TYR A 1 65  ? 11.655  -0.077  -13.128 1.00 52.75  ?  14  TYR A CE1   1 
ATOM   408  C  CE2   . TYR A 1 65  ? 12.388  -2.209  -13.944 1.00 49.60  ?  14  TYR A CE2   1 
ATOM   409  C  CZ    . TYR A 1 65  ? 12.425  -0.836  -13.987 1.00 51.06  ?  14  TYR A CZ    1 
ATOM   410  O  OH    . TYR A 1 65  ? 13.259  -0.211  -14.874 1.00 50.51  ?  14  TYR A OH    1 
ATOM   411  N  N     . GLN A 1 66  ? 7.121   -3.584  -12.464 1.00 48.69  ?  15  GLN A N     1 
ATOM   412  C  CA    . GLN A 1 66  ? 6.208   -3.857  -13.566 1.00 46.38  ?  15  GLN A CA    1 
ATOM   413  C  C     . GLN A 1 66  ? 5.032   -2.886  -13.532 1.00 47.37  ?  15  GLN A C     1 
ATOM   414  O  O     . GLN A 1 66  ? 4.631   -2.345  -14.569 1.00 47.48  ?  15  GLN A O     1 
ATOM   415  C  CB    . GLN A 1 66  ? 5.751   -5.321  -13.481 1.00 44.12  ?  15  GLN A CB    1 
ATOM   416  C  CG    . GLN A 1 66  ? 4.921   -5.868  -14.647 1.00 44.63  ?  15  GLN A CG    1 
ATOM   417  C  CD    . GLN A 1 66  ? 5.614   -5.762  -15.993 1.00 47.07  ?  15  GLN A CD    1 
ATOM   418  O  OE1   . GLN A 1 66  ? 5.103   -5.112  -16.907 1.00 48.44  ?  15  GLN A OE1   1 
ATOM   419  N  NE2   . GLN A 1 66  ? 6.780   -6.394  -16.127 1.00 45.24  ?  15  GLN A NE2   1 
ATOM   420  N  N     . TYR A 1 67  ? 4.525   -2.586  -12.333 1.00 47.19  ?  16  TYR A N     1 
ATOM   421  C  CA    . TYR A 1 67  ? 3.316   -1.772  -12.212 1.00 47.17  ?  16  TYR A CA    1 
ATOM   422  C  C     . TYR A 1 67  ? 3.580   -0.304  -12.516 1.00 48.05  ?  16  TYR A C     1 
ATOM   423  O  O     . TYR A 1 67  ? 2.763   0.353   -13.170 1.00 50.25  ?  16  TYR A O     1 
ATOM   424  C  CB    . TYR A 1 67  ? 2.716   -1.902  -10.813 1.00 47.04  ?  16  TYR A CB    1 
ATOM   425  C  CG    . TYR A 1 67  ? 1.505   -1.017  -10.594 1.00 44.75  ?  16  TYR A CG    1 
ATOM   426  C  CD1   . TYR A 1 67  ? 0.298   -1.300  -11.210 1.00 44.99  ?  16  TYR A CD1   1 
ATOM   427  C  CD2   . TYR A 1 67  ? 1.572   0.090   -9.773  1.00 45.37  ?  16  TYR A CD2   1 
ATOM   428  C  CE1   . TYR A 1 67  ? -0.804  -0.504  -11.023 1.00 43.75  ?  16  TYR A CE1   1 
ATOM   429  C  CE2   . TYR A 1 67  ? 0.471   0.892   -9.565  1.00 47.01  ?  16  TYR A CE2   1 
ATOM   430  C  CZ    . TYR A 1 67  ? -0.716  0.591   -10.199 1.00 49.30  ?  16  TYR A CZ    1 
ATOM   431  O  OH    . TYR A 1 67  ? -1.823  1.393   -10.004 1.00 51.96  ?  16  TYR A OH    1 
ATOM   432  N  N     . THR A 1 68  ? 4.690   0.247   -12.040 1.00 46.38  ?  17  THR A N     1 
ATOM   433  C  CA    . THR A 1 68  ? 4.903   1.659   -12.313 1.00 46.76  ?  17  THR A CA    1 
ATOM   434  C  C     . THR A 1 68  ? 5.468   1.904   -13.713 1.00 49.57  ?  17  THR A C     1 
ATOM   435  O  O     . THR A 1 68  ? 5.141   2.921   -14.330 1.00 50.89  ?  17  THR A O     1 
ATOM   436  C  CB    . THR A 1 68  ? 5.823   2.283   -11.263 1.00 43.37  ?  17  THR A CB    1 
ATOM   437  O  OG1   . THR A 1 68  ? 7.105   1.656   -11.319 1.00 45.47  ?  17  THR A OG1   1 
ATOM   438  C  CG2   . THR A 1 68  ? 5.278   2.109   -9.884  1.00 47.10  ?  17  THR A CG2   1 
ATOM   439  N  N     . ASP A 1 69  ? 6.319   1.015   -14.233 1.00 49.33  ?  18  ASP A N     1 
ATOM   440  C  CA    . ASP A 1 69  ? 7.037   1.287   -15.472 1.00 47.06  ?  18  ASP A CA    1 
ATOM   441  C  C     . ASP A 1 69  ? 6.898   0.220   -16.541 1.00 48.78  ?  18  ASP A C     1 
ATOM   442  O  O     . ASP A 1 69  ? 7.625   0.291   -17.529 1.00 54.85  ?  18  ASP A O     1 
ATOM   443  C  CB    . ASP A 1 69  ? 8.542   1.455   -15.214 1.00 49.34  ?  18  ASP A CB    1 
ATOM   444  C  CG    . ASP A 1 69  ? 8.854   2.532   -14.200 1.00 52.35  ?  18  ASP A CG    1 
ATOM   445  O  OD1   . ASP A 1 69  ? 8.137   2.643   -13.191 1.00 54.39  ?  18  ASP A OD1   1 
ATOM   446  O  OD2   . ASP A 1 69  ? 9.859   3.249   -14.380 1.00 56.38  ?  18  ASP A OD2   1 
ATOM   447  N  N     . GLY A 1 70  ? 6.052   -0.789  -16.359 1.00 48.57  ?  19  GLY A N     1 
ATOM   448  C  CA    . GLY A 1 70  ? 5.902   -1.818  -17.375 1.00 47.82  ?  19  GLY A CA    1 
ATOM   449  C  C     . GLY A 1 70  ? 7.185   -2.497  -17.809 1.00 49.56  ?  19  GLY A C     1 
ATOM   450  O  O     . GLY A 1 70  ? 7.273   -2.958  -18.951 1.00 47.18  ?  19  GLY A O     1 
ATOM   451  N  N     . LYS A 1 71  ? 8.180   -2.590  -16.932 1.00 48.89  ?  20  LYS A N     1 
ATOM   452  C  CA    . LYS A 1 71  ? 9.460   -3.190  -17.281 1.00 45.09  ?  20  LYS A CA    1 
ATOM   453  C  C     . LYS A 1 71  ? 9.799   -4.310  -16.310 1.00 43.99  ?  20  LYS A C     1 
ATOM   454  O  O     . LYS A 1 71  ? 9.232   -4.401  -15.226 1.00 46.93  ?  20  LYS A O     1 
ATOM   455  C  CB    . LYS A 1 71  ? 10.562  -2.129  -17.286 1.00 48.23  ?  20  LYS A CB    1 
ATOM   456  C  CG    . LYS A 1 71  ? 10.365  -1.073  -18.373 1.00 47.81  ?  20  LYS A CG    1 
ATOM   457  C  CD    . LYS A 1 71  ? 11.317  0.097   -18.205 1.00 49.92  ?  20  LYS A CD    1 
ATOM   458  C  CE    . LYS A 1 71  ? 11.531  0.821   -19.530 1.00 52.22  ?  20  LYS A CE    1 
ATOM   459  N  NZ    . LYS A 1 71  ? 12.723  1.727   -19.465 1.00 56.02  ?  20  LYS A NZ    1 
ATOM   460  N  N     . PHE A 1 72  ? 10.727  -5.176  -16.706 1.00 44.06  ?  21  PHE A N     1 
ATOM   461  C  CA    . PHE A 1 72  ? 11.089  -6.323  -15.884 1.00 40.68  ?  21  PHE A CA    1 
ATOM   462  C  C     . PHE A 1 72  ? 12.552  -6.647  -16.113 1.00 42.08  ?  21  PHE A C     1 
ATOM   463  O  O     . PHE A 1 72  ? 13.033  -6.595  -17.244 1.00 45.53  ?  21  PHE A O     1 
ATOM   464  C  CB    . PHE A 1 72  ? 10.231  -7.557  -16.204 1.00 40.22  ?  21  PHE A CB    1 
ATOM   465  C  CG    . PHE A 1 72  ? 10.712  -8.834  -15.535 1.00 43.08  ?  21  PHE A CG    1 
ATOM   466  C  CD1   . PHE A 1 72  ? 10.533  -9.038  -14.176 1.00 44.24  ?  21  PHE A CD1   1 
ATOM   467  C  CD2   . PHE A 1 72  ? 11.320  -9.834  -16.269 1.00 44.47  ?  21  PHE A CD2   1 
ATOM   468  C  CE1   . PHE A 1 72  ? 10.984  -10.216 -13.569 1.00 43.44  ?  21  PHE A CE1   1 
ATOM   469  C  CE2   . PHE A 1 72  ? 11.768  -11.019 -15.671 1.00 41.62  ?  21  PHE A CE2   1 
ATOM   470  C  CZ    . PHE A 1 72  ? 11.599  -11.208 -14.331 1.00 44.67  ?  21  PHE A CZ    1 
ATOM   471  N  N     . ASN A 1 73  ? 13.255  -6.991  -15.047 1.00 43.15  ?  22  ASN A N     1 
ATOM   472  C  CA    . ASN A 1 73  ? 14.691  -7.218  -15.107 1.00 45.23  ?  22  ASN A CA    1 
ATOM   473  C  C     . ASN A 1 73  ? 15.014  -8.557  -14.469 1.00 44.57  ?  22  ASN A C     1 
ATOM   474  O  O     . ASN A 1 73  ? 14.606  -8.830  -13.339 1.00 51.42  ?  22  ASN A O     1 
ATOM   475  C  CB    . ASN A 1 73  ? 15.452  -6.079  -14.414 1.00 50.66  ?  22  ASN A CB    1 
ATOM   476  C  CG    . ASN A 1 73  ? 16.962  -6.223  -14.539 1.00 54.65  ?  22  ASN A CG    1 
ATOM   477  O  OD1   . ASN A 1 73  ? 17.486  -7.319  -14.802 1.00 50.86  ?  22  ASN A OD1   1 
ATOM   478  N  ND2   . ASN A 1 73  ? 17.673  -5.112  -14.362 1.00 58.41  ?  22  ASN A ND2   1 
ATOM   479  N  N     . SER A 1 74  ? 15.753  -9.385  -15.190 1.00 46.51  ?  23  SER A N     1 
ATOM   480  C  CA    . SER A 1 74  ? 15.985  -10.760 -14.772 1.00 48.58  ?  23  SER A CA    1 
ATOM   481  C  C     . SER A 1 74  ? 17.004  -10.898 -13.651 1.00 45.75  ?  23  SER A C     1 
ATOM   482  O  O     . SER A 1 74  ? 16.997  -11.919 -12.953 1.00 46.17  ?  23  SER A O     1 
ATOM   483  C  CB    . SER A 1 74  ? 16.456  -11.575 -15.970 1.00 46.48  ?  23  SER A CB    1 
ATOM   484  O  OG    . SER A 1 74  ? 15.338  -11.974 -16.741 1.00 59.87  ?  23  SER A OG    1 
ATOM   485  N  N     . LYS A 1 75  ? 17.909  -9.936  -13.506 1.00 43.95  ?  24  LYS A N     1 
ATOM   486  C  CA    . LYS A 1 75  ? 18.978  -10.043 -12.527 1.00 47.29  ?  24  LYS A CA    1 
ATOM   487  C  C     . LYS A 1 75  ? 18.429  -9.761  -11.129 1.00 47.74  ?  24  LYS A C     1 
ATOM   488  O  O     . LYS A 1 75  ? 17.719  -8.770  -10.925 1.00 49.76  ?  24  LYS A O     1 
ATOM   489  C  CB    . LYS A 1 75  ? 20.097  -9.060  -12.882 1.00 43.63  ?  24  LYS A CB    1 
ATOM   490  C  CG    . LYS A 1 75  ? 21.219  -9.046  -11.865 1.00 53.73  ?  24  LYS A CG    1 
ATOM   491  C  CD    . LYS A 1 75  ? 22.577  -8.848  -12.521 1.00 65.22  ?  24  LYS A CD    1 
ATOM   492  C  CE    . LYS A 1 75  ? 23.650  -9.744  -11.864 1.00 72.17  ?  24  LYS A CE    1 
ATOM   493  N  NZ    . LYS A 1 75  ? 24.599  -10.312 -12.879 1.00 78.23  ?  24  LYS A NZ    1 
ATOM   494  N  N     . PHE A 1 76  ? 18.737  -10.632 -10.169 1.00 46.86  ?  25  PHE A N     1 
ATOM   495  C  CA    . PHE A 1 76  ? 18.239  -10.476 -8.796  1.00 51.61  ?  25  PHE A CA    1 
ATOM   496  C  C     . PHE A 1 76  ? 19.056  -9.406  -8.084  1.00 48.09  ?  25  PHE A C     1 
ATOM   497  O  O     . PHE A 1 76  ? 20.224  -9.628  -7.766  1.00 51.96  ?  25  PHE A O     1 
ATOM   498  C  CB    . PHE A 1 76  ? 18.313  -11.805 -8.049  1.00 51.03  ?  25  PHE A CB    1 
ATOM   499  C  CG    . PHE A 1 76  ? 17.878  -11.744 -6.598  1.00 46.09  ?  25  PHE A CG    1 
ATOM   500  C  CD1   . PHE A 1 76  ? 16.797  -10.974 -6.202  1.00 47.78  ?  25  PHE A CD1   1 
ATOM   501  C  CD2   . PHE A 1 76  ? 18.518  -12.512 -5.644  1.00 43.08  ?  25  PHE A CD2   1 
ATOM   502  C  CE1   . PHE A 1 76  ? 16.400  -10.927 -4.855  1.00 47.44  ?  25  PHE A CE1   1 
ATOM   503  C  CE2   . PHE A 1 76  ? 18.121  -12.479 -4.296  1.00 46.47  ?  25  PHE A CE2   1 
ATOM   504  C  CZ    . PHE A 1 76  ? 17.056  -11.702 -3.906  1.00 43.31  ?  25  PHE A CZ    1 
ATOM   505  N  N     . ILE A 1 77  ? 18.460  -8.234  -7.863  1.00 46.58  ?  26  ILE A N     1 
ATOM   506  C  CA    . ILE A 1 77  ? 19.099  -7.187  -7.071  1.00 48.68  ?  26  ILE A CA    1 
ATOM   507  C  C     . ILE A 1 77  ? 18.336  -7.027  -5.769  1.00 47.15  ?  26  ILE A C     1 
ATOM   508  O  O     . ILE A 1 77  ? 17.338  -6.294  -5.712  1.00 46.11  ?  26  ILE A O     1 
ATOM   509  C  CB    . ILE A 1 77  ? 19.146  -5.844  -7.814  1.00 53.46  ?  26  ILE A CB    1 
ATOM   510  C  CG1   . ILE A 1 77  ? 19.843  -5.997  -9.173  1.00 54.58  ?  26  ILE A CG1   1 
ATOM   511  C  CG2   . ILE A 1 77  ? 19.840  -4.808  -6.932  1.00 41.78  ?  26  ILE A CG2   1 
ATOM   512  C  CD1   . ILE A 1 77  ? 19.098  -5.315  -10.329 1.00 57.23  ?  26  ILE A CD1   1 
ATOM   513  N  N     . THR A 1 78  ? 18.798  -7.696  -4.716  1.00 44.81  ?  27  THR A N     1 
ATOM   514  C  CA    . THR A 1 78  ? 18.034  -7.730  -3.478  1.00 44.86  ?  27  THR A CA    1 
ATOM   515  C  C     . THR A 1 78  ? 17.941  -6.345  -2.850  1.00 41.81  ?  27  THR A C     1 
ATOM   516  O  O     . THR A 1 78  ? 18.897  -5.559  -2.876  1.00 41.80  ?  27  THR A O     1 
ATOM   517  C  CB    . THR A 1 78  ? 18.638  -8.753  -2.509  1.00 42.07  ?  27  THR A CB    1 
ATOM   518  O  OG1   . THR A 1 78  ? 17.667  -9.088  -1.514  1.00 39.93  ?  27  THR A OG1   1 
ATOM   519  C  CG2   . THR A 1 78  ? 19.919  -8.253  -1.861  1.00 36.54  ?  27  THR A CG2   1 
ATOM   520  N  N     . THR A 1 79  ? 16.750  -6.043  -2.323  1.00 39.92  ?  28  THR A N     1 
ATOM   521  C  CA    . THR A 1 79  ? 16.438  -4.736  -1.755  1.00 42.83  ?  28  THR A CA    1 
ATOM   522  C  C     . THR A 1 79  ? 17.203  -4.455  -0.468  1.00 42.08  ?  28  THR A C     1 
ATOM   523  O  O     . THR A 1 79  ? 17.177  -5.254  0.478   1.00 44.48  ?  28  THR A O     1 
ATOM   524  C  CB    . THR A 1 79  ? 14.951  -4.652  -1.458  1.00 45.30  ?  28  THR A CB    1 
ATOM   525  O  OG1   . THR A 1 79  ? 14.211  -4.951  -2.657  1.00 47.48  ?  28  THR A OG1   1 
ATOM   526  C  CG2   . THR A 1 79  ? 14.608  -3.268  -0.909  1.00 45.29  ?  28  THR A CG2   1 
ATOM   527  N  N     . VAL A 1 80  ? 17.835  -3.285  -0.408  1.00 42.99  ?  29  VAL A N     1 
ATOM   528  C  CA    . VAL A 1 80  ? 18.621  -2.892  0.758   1.00 44.79  ?  29  VAL A CA    1 
ATOM   529  C  C     . VAL A 1 80  ? 17.706  -2.325  1.831   1.00 44.43  ?  29  VAL A C     1 
ATOM   530  O  O     . VAL A 1 80  ? 17.547  -1.110  1.940   1.00 46.85  ?  29  VAL A O     1 
ATOM   531  C  CB    . VAL A 1 80  ? 19.691  -1.866  0.364   1.00 46.25  ?  29  VAL A CB    1 
ATOM   532  C  CG1   . VAL A 1 80  ? 20.644  -1.631  1.491   1.00 45.37  ?  29  VAL A CG1   1 
ATOM   533  C  CG2   . VAL A 1 80  ? 20.411  -2.334  -0.907  1.00 46.52  ?  29  VAL A CG2   1 
ATOM   534  N  N     . GLY A 1 81  ? 17.077  -3.194  2.609   1.00 43.84  ?  30  GLY A N     1 
ATOM   535  C  CA    . GLY A 1 81  ? 16.224  -2.755  3.689   1.00 45.80  ?  30  GLY A CA    1 
ATOM   536  C  C     . GLY A 1 81  ? 14.850  -2.289  3.268   1.00 45.09  ?  30  GLY A C     1 
ATOM   537  O  O     . GLY A 1 81  ? 13.841  -2.907  3.612   1.00 45.13  ?  30  GLY A O     1 
ATOM   538  N  N     . ILE A 1 82  ? 14.796  -1.189  2.526   1.00 44.44  ?  31  ILE A N     1 
ATOM   539  C  CA    . ILE A 1 82  ? 13.544  -0.479  2.313   1.00 46.27  ?  31  ILE A CA    1 
ATOM   540  C  C     . ILE A 1 82  ? 13.721  0.409   1.088   1.00 48.90  ?  31  ILE A C     1 
ATOM   541  O  O     . ILE A 1 82  ? 14.834  0.859   0.778   1.00 45.93  ?  31  ILE A O     1 
ATOM   542  C  CB    . ILE A 1 82  ? 13.162  0.329   3.579   1.00 46.39  ?  31  ILE A CB    1 
ATOM   543  C  CG1   . ILE A 1 82  ? 11.754  0.935   3.472   1.00 48.30  ?  31  ILE A CG1   1 
ATOM   544  C  CG2   . ILE A 1 82  ? 14.174  1.432   3.799   1.00 47.23  ?  31  ILE A CG2   1 
ATOM   545  C  CD1   . ILE A 1 82  ? 10.615  -0.056  3.649   1.00 46.72  ?  31  ILE A CD1   1 
ATOM   546  N  N     . ASP A 1 83  ? 12.622  0.640   0.378   1.00 46.28  ?  32  ASP A N     1 
ATOM   547  C  CA    . ASP A 1 83  ? 12.557  1.553   -0.757  1.00 46.64  ?  32  ASP A CA    1 
ATOM   548  C  C     . ASP A 1 83  ? 11.080  1.807   -1.028  1.00 47.60  ?  32  ASP A C     1 
ATOM   549  O  O     . ASP A 1 83  ? 10.207  1.220   -0.380  1.00 44.86  ?  32  ASP A O     1 
ATOM   550  C  CB    . ASP A 1 83  ? 13.262  0.985   -1.991  1.00 48.90  ?  32  ASP A CB    1 
ATOM   551  C  CG    . ASP A 1 83  ? 13.727  2.069   -2.947  1.00 55.31  ?  32  ASP A CG    1 
ATOM   552  O  OD1   . ASP A 1 83  ? 13.164  3.191   -2.897  1.00 52.47  ?  32  ASP A OD1   1 
ATOM   553  O  OD2   . ASP A 1 83  ? 14.653  1.796   -3.751  1.00 62.00  ?  32  ASP A OD2   1 
ATOM   554  N  N     . PHE A 1 84  ? 10.801  2.682   -1.993  1.00 48.42  ?  33  PHE A N     1 
ATOM   555  C  CA    . PHE A 1 84  ? 9.424   2.920   -2.405  1.00 48.41  ?  33  PHE A CA    1 
ATOM   556  C  C     . PHE A 1 84  ? 9.419   3.491   -3.819  1.00 49.31  ?  33  PHE A C     1 
ATOM   557  O  O     . PHE A 1 84  ? 10.407  4.064   -4.283  1.00 49.85  ?  33  PHE A O     1 
ATOM   558  C  CB    . PHE A 1 84  ? 8.671   3.839   -1.419  1.00 45.00  ?  33  PHE A CB    1 
ATOM   559  C  CG    . PHE A 1 84  ? 9.137   5.283   -1.411  1.00 48.04  ?  33  PHE A CG    1 
ATOM   560  C  CD1   . PHE A 1 84  ? 8.535   6.236   -2.234  1.00 51.98  ?  33  PHE A CD1   1 
ATOM   561  C  CD2   . PHE A 1 84  ? 10.156  5.695   -0.560  1.00 46.27  ?  33  PHE A CD2   1 
ATOM   562  C  CE1   . PHE A 1 84  ? 8.961   7.565   -2.215  1.00 51.50  ?  33  PHE A CE1   1 
ATOM   563  C  CE2   . PHE A 1 84  ? 10.579  7.013   -0.531  1.00 47.88  ?  33  PHE A CE2   1 
ATOM   564  C  CZ    . PHE A 1 84  ? 9.983   7.953   -1.354  1.00 51.29  ?  33  PHE A CZ    1 
ATOM   565  N  N     . ARG A 1 85  ? 8.291   3.292   -4.501  1.00 47.91  ?  34  ARG A N     1 
ATOM   566  C  CA    . ARG A 1 85  ? 8.008   3.836   -5.822  1.00 52.53  ?  34  ARG A CA    1 
ATOM   567  C  C     . ARG A 1 85  ? 6.718   4.639   -5.734  1.00 50.23  ?  34  ARG A C     1 
ATOM   568  O  O     . ARG A 1 85  ? 5.974   4.536   -4.760  1.00 52.77  ?  34  ARG A O     1 
ATOM   569  C  CB    . ARG A 1 85  ? 7.883   2.726   -6.883  1.00 45.30  ?  34  ARG A CB    1 
ATOM   570  C  CG    . ARG A 1 85  ? 9.102   1.797   -7.013  1.00 43.75  ?  34  ARG A CG    1 
ATOM   571  C  CD    . ARG A 1 85  ? 9.051   0.962   -8.288  1.00 49.27  ?  34  ARG A CD    1 
ATOM   572  N  NE    . ARG A 1 85  ? 9.349   1.781   -9.465  1.00 50.02  ?  34  ARG A NE    1 
ATOM   573  C  CZ    . ARG A 1 85  ? 10.577  2.021   -9.918  1.00 49.53  ?  34  ARG A CZ    1 
ATOM   574  N  NH1   . ARG A 1 85  ? 11.627  1.488   -9.313  1.00 45.44  ?  34  ARG A NH1   1 
ATOM   575  N  NH2   . ARG A 1 85  ? 10.757  2.793   -10.980 1.00 50.24  ?  34  ARG A NH2   1 
ATOM   576  N  N     . GLU A 1 86  ? 6.451   5.445   -6.757  1.00 51.91  ?  35  GLU A N     1 
ATOM   577  C  CA    . GLU A 1 86  ? 5.255   6.277   -6.810  1.00 51.14  ?  35  GLU A CA    1 
ATOM   578  C  C     . GLU A 1 86  ? 4.532   6.082   -8.133  1.00 51.72  ?  35  GLU A C     1 
ATOM   579  O  O     . GLU A 1 86  ? 5.124   5.675   -9.133  1.00 50.63  ?  35  GLU A O     1 
ATOM   580  C  CB    . GLU A 1 86  ? 5.583   7.764   -6.654  1.00 53.82  ?  35  GLU A CB    1 
ATOM   581  C  CG    . GLU A 1 86  ? 6.701   8.070   -5.671  1.00 58.08  ?  35  GLU A CG    1 
ATOM   582  C  CD    . GLU A 1 86  ? 6.837   9.565   -5.389  1.00 59.82  ?  35  GLU A CD    1 
ATOM   583  O  OE1   . GLU A 1 86  ? 5.799   10.257  -5.270  1.00 59.77  ?  35  GLU A OE1   1 
ATOM   584  O  OE2   . GLU A 1 86  ? 7.986   10.050  -5.306  1.00 61.15  ?  35  GLU A OE2   1 
ATOM   585  N  N     . LYS A 1 87  ? 3.237   6.388   -8.130  1.00 49.20  ?  36  LYS A N     1 
ATOM   586  C  CA    . LYS A 1 87  ? 2.471   6.399   -9.368  1.00 51.37  ?  36  LYS A CA    1 
ATOM   587  C  C     . LYS A 1 87  ? 1.245   7.281   -9.193  1.00 54.22  ?  36  LYS A C     1 
ATOM   588  O  O     . LYS A 1 87  ? 0.545   7.178   -8.177  1.00 51.93  ?  36  LYS A O     1 
ATOM   589  C  CB    . LYS A 1 87  ? 2.042   4.991   -9.788  1.00 51.62  ?  36  LYS A CB    1 
ATOM   590  C  CG    . LYS A 1 87  ? 1.848   4.896   -11.322 1.00 49.86  ?  36  LYS A CG    1 
ATOM   591  C  CD    . LYS A 1 87  ? 1.170   3.609   -11.760 1.00 46.55  ?  36  LYS A CD    1 
ATOM   592  C  CE    . LYS A 1 87  ? 1.461   3.334   -13.233 1.00 52.49  ?  36  LYS A CE    1 
ATOM   593  N  NZ    . LYS A 1 87  ? 0.538   2.277   -13.743 1.00 52.88  ?  36  LYS A NZ    1 
ATOM   594  N  N     . ARG A 1 88  ? 0.992   8.144   -10.175 1.00 51.87  ?  37  ARG A N     1 
ATOM   595  C  CA    . ARG A 1 88  ? -0.255  8.895   -10.247 1.00 50.68  ?  37  ARG A CA    1 
ATOM   596  C  C     . ARG A 1 88  ? -1.280  8.056   -10.992 1.00 50.06  ?  37  ARG A C     1 
ATOM   597  O  O     . ARG A 1 88  ? -0.954  7.448   -12.012 1.00 52.52  ?  37  ARG A O     1 
ATOM   598  C  CB    . ARG A 1 88  ? -0.050  10.222  -10.966 1.00 53.76  ?  37  ARG A CB    1 
ATOM   599  C  CG    . ARG A 1 88  ? 0.911   11.150  -10.282 1.00 58.44  ?  37  ARG A CG    1 
ATOM   600  C  CD    . ARG A 1 88  ? 0.333   11.625  -8.977  1.00 61.24  ?  37  ARG A CD    1 
ATOM   601  N  NE    . ARG A 1 88  ? 1.235   12.546  -8.295  1.00 66.62  ?  37  ARG A NE    1 
ATOM   602  C  CZ    . ARG A 1 88  ? 0.923   13.797  -7.977  1.00 72.28  ?  37  ARG A CZ    1 
ATOM   603  N  NH1   . ARG A 1 88  ? 1.812   14.560  -7.349  1.00 74.40  ?  37  ARG A NH1   1 
ATOM   604  N  NH2   . ARG A 1 88  ? -0.277  14.284  -8.277  1.00 76.49  ?  37  ARG A NH2   1 
ATOM   605  N  N     . VAL A 1 89  ? -2.508  8.002   -10.480 1.00 48.00  ?  38  VAL A N     1 
ATOM   606  C  CA    . VAL A 1 89  ? -3.563  7.187   -11.067 1.00 43.50  ?  38  VAL A CA    1 
ATOM   607  C  C     . VAL A 1 89  ? -4.897  7.890   -10.856 1.00 43.97  ?  38  VAL A C     1 
ATOM   608  O  O     . VAL A 1 89  ? -4.989  8.882   -10.143 1.00 50.92  ?  38  VAL A O     1 
ATOM   609  C  CB    . VAL A 1 89  ? -3.612  5.761   -10.467 1.00 51.25  ?  38  VAL A CB    1 
ATOM   610  C  CG1   . VAL A 1 89  ? -2.258  5.057   -10.563 1.00 52.29  ?  38  VAL A CG1   1 
ATOM   611  C  CG2   . VAL A 1 89  ? -4.094  5.789   -9.035  1.00 49.98  ?  38  VAL A CG2   1 
ATOM   612  N  N     . VAL A 1 90  ? -5.947  7.361   -11.480 1.00 46.07  ?  39  VAL A N     1 
ATOM   613  C  CA    . VAL A 1 90  ? -7.305  7.876   -11.328 1.00 50.25  ?  39  VAL A CA    1 
ATOM   614  C  C     . VAL A 1 90  ? -8.175  6.733   -10.842 1.00 53.10  ?  39  VAL A C     1 
ATOM   615  O  O     . VAL A 1 90  ? -8.433  5.787   -11.595 1.00 51.47  ?  39  VAL A O     1 
ATOM   616  C  CB    . VAL A 1 90  ? -7.876  8.447   -12.631 1.00 52.71  ?  39  VAL A CB    1 
ATOM   617  C  CG1   . VAL A 1 90  ? -9.317  8.925   -12.413 1.00 48.05  ?  39  VAL A CG1   1 
ATOM   618  C  CG2   . VAL A 1 90  ? -6.992  9.558   -13.182 1.00 51.31  ?  39  VAL A CG2   1 
ATOM   619  N  N     . TYR A 1 91  ? -8.634  6.825   -9.596  1.00 51.14  ?  40  TYR A N     1 
ATOM   620  C  CA    . TYR A 1 91  ? -9.586  5.884   -9.037  1.00 51.86  ?  40  TYR A CA    1 
ATOM   621  C  C     . TYR A 1 91  ? -11.013 6.373   -9.264  1.00 52.30  ?  40  TYR A C     1 
ATOM   622  O  O     . TYR A 1 91  ? -11.304 7.562   -9.135  1.00 54.39  ?  40  TYR A O     1 
ATOM   623  C  CB    . TYR A 1 91  ? -9.326  5.720   -7.538  1.00 56.38  ?  40  TYR A CB    1 
ATOM   624  C  CG    . TYR A 1 91  ? -10.417 4.974   -6.811  1.00 56.01  ?  40  TYR A CG    1 
ATOM   625  C  CD1   . TYR A 1 91  ? -10.405 3.589   -6.750  1.00 56.29  ?  40  TYR A CD1   1 
ATOM   626  C  CD2   . TYR A 1 91  ? -11.459 5.652   -6.192  1.00 52.05  ?  40  TYR A CD2   1 
ATOM   627  C  CE1   . TYR A 1 91  ? -11.393 2.907   -6.108  1.00 56.77  ?  40  TYR A CE1   1 
ATOM   628  C  CE2   . TYR A 1 91  ? -12.455 4.976   -5.564  1.00 53.19  ?  40  TYR A CE2   1 
ATOM   629  C  CZ    . TYR A 1 91  ? -12.415 3.604   -5.515  1.00 56.49  ?  40  TYR A CZ    1 
ATOM   630  O  OH    . TYR A 1 91  ? -13.405 2.909   -4.863  1.00 63.28  ?  40  TYR A OH    1 
ATOM   631  N  N     . ARG A 1 92  ? -11.913 5.450   -9.569  1.00 54.45  ?  41  ARG A N     1 
ATOM   632  C  CA    . ARG A 1 92  ? -13.331 5.770   -9.693  1.00 59.23  ?  41  ARG A CA    1 
ATOM   633  C  C     . ARG A 1 92  ? -14.106 4.811   -8.811  1.00 59.94  ?  41  ARG A C     1 
ATOM   634  O  O     . ARG A 1 92  ? -13.944 3.595   -8.926  1.00 65.94  ?  41  ARG A O     1 
ATOM   635  C  CB    . ARG A 1 92  ? -13.832 5.663   -11.146 1.00 57.06  ?  41  ARG A CB    1 
ATOM   636  C  CG    . ARG A 1 92  ? -13.146 6.604   -12.134 1.00 60.02  ?  41  ARG A CG    1 
ATOM   637  C  CD    . ARG A 1 92  ? -13.731 6.481   -13.556 1.00 60.46  ?  41  ARG A CD    1 
ATOM   638  N  NE    . ARG A 1 92  ? -15.145 6.846   -13.602 1.00 61.07  ?  41  ARG A NE    1 
ATOM   639  C  CZ    . ARG A 1 92  ? -15.960 6.511   -14.590 1.00 58.07  ?  41  ARG A CZ    1 
ATOM   640  N  NH1   . ARG A 1 92  ? -15.489 5.805   -15.609 1.00 57.44  ?  41  ARG A NH1   1 
ATOM   641  N  NH2   . ARG A 1 92  ? -17.233 6.883   -14.559 1.00 61.67  ?  41  ARG A NH2   1 
ATOM   642  N  N     . ALA A 1 93  ? -14.933 5.347   -7.926  1.00 67.54  ?  42  ALA A N     1 
ATOM   643  C  CA    . ALA A 1 93  ? -15.698 4.482   -7.046  1.00 70.30  ?  42  ALA A CA    1 
ATOM   644  C  C     . ALA A 1 93  ? -16.594 3.568   -7.872  1.00 76.69  ?  42  ALA A C     1 
ATOM   645  O  O     . ALA A 1 93  ? -16.871 3.820   -9.048  1.00 79.03  ?  42  ALA A O     1 
ATOM   646  C  CB    . ALA A 1 93  ? -16.534 5.307   -6.069  1.00 68.24  ?  42  ALA A CB    1 
ATOM   647  N  N     . SER A 1 94  ? -17.028 2.477   -7.243  1.00 84.99  ?  43  SER A N     1 
ATOM   648  C  CA    . SER A 1 94  ? -17.960 1.526   -7.841  1.00 87.93  ?  43  SER A CA    1 
ATOM   649  C  C     . SER A 1 94  ? -19.248 1.595   -7.034  1.00 91.69  ?  43  SER A C     1 
ATOM   650  O  O     . SER A 1 94  ? -19.268 1.222   -5.856  1.00 90.67  ?  43  SER A O     1 
ATOM   651  C  CB    . SER A 1 94  ? -17.378 0.113   -7.851  1.00 86.41  ?  43  SER A CB    1 
ATOM   652  O  OG    . SER A 1 94  ? -16.012 0.127   -8.234  1.00 81.46  ?  43  SER A OG    1 
ATOM   653  N  N     . GLY A 1 95  ? -20.314 2.086   -7.660  1.00 97.67  ?  44  GLY A N     1 
ATOM   654  C  CA    . GLY A 1 95  ? -21.564 2.297   -6.974  1.00 104.30 ?  44  GLY A CA    1 
ATOM   655  C  C     . GLY A 1 95  ? -22.522 1.139   -7.156  1.00 110.77 ?  44  GLY A C     1 
ATOM   656  O  O     . GLY A 1 95  ? -22.137 0.042   -7.579  1.00 109.05 ?  44  GLY A O     1 
ATOM   657  N  N     . PRO A 1 96  ? -23.798 1.366   -6.833  1.00 116.67 ?  45  PRO A N     1 
ATOM   658  C  CA    . PRO A 1 96  ? -24.799 0.292   -6.970  1.00 117.67 ?  45  PRO A CA    1 
ATOM   659  C  C     . PRO A 1 96  ? -25.099 -0.006  -8.436  1.00 112.04 ?  45  PRO A C     1 
ATOM   660  O  O     . PRO A 1 96  ? -25.488 0.883   -9.199  1.00 111.77 ?  45  PRO A O     1 
ATOM   661  C  CB    . PRO A 1 96  ? -26.030 0.852   -6.237  1.00 114.87 ?  45  PRO A CB    1 
ATOM   662  C  CG    . PRO A 1 96  ? -25.538 2.054   -5.464  1.00 114.51 ?  45  PRO A CG    1 
ATOM   663  C  CD    . PRO A 1 96  ? -24.365 2.585   -6.230  1.00 114.41 ?  45  PRO A CD    1 
ATOM   664  N  N     . ASP A 1 97  ? -24.916 -1.275  -8.821  1.00 110.22 ?  46  ASP A N     1 
ATOM   665  C  CA    . ASP A 1 97  ? -25.115 -1.734  -10.198 1.00 108.77 ?  46  ASP A CA    1 
ATOM   666  C  C     . ASP A 1 97  ? -24.240 -0.945  -11.173 1.00 106.84 ?  46  ASP A C     1 
ATOM   667  O  O     . ASP A 1 97  ? -24.717 -0.390  -12.167 1.00 105.06 ?  46  ASP A O     1 
ATOM   668  C  CB    . ASP A 1 97  ? -26.593 -1.664  -10.597 1.00 111.91 ?  46  ASP A CB    1 
ATOM   669  N  N     . GLY A 1 98  ? -22.945 -0.894  -10.870 1.00 105.40 ?  47  GLY A N     1 
ATOM   670  C  CA    . GLY A 1 98  ? -21.984 -0.255  -11.757 1.00 104.34 ?  47  GLY A CA    1 
ATOM   671  C  C     . GLY A 1 98  ? -22.161 1.240   -11.916 1.00 103.58 ?  47  GLY A C     1 
ATOM   672  O  O     . GLY A 1 98  ? -22.053 1.755   -13.036 1.00 105.46 ?  47  GLY A O     1 
ATOM   673  N  N     . ALA A 1 99  ? -22.422 1.954   -10.816 1.00 103.77 ?  48  ALA A N     1 
ATOM   674  C  CA    . ALA A 1 99  ? -22.650 3.405   -10.847 1.00 99.93  ?  48  ALA A CA    1 
ATOM   675  C  C     . ALA A 1 99  ? -21.336 4.145   -10.577 1.00 94.25  ?  48  ALA A C     1 
ATOM   676  O  O     . ALA A 1 99  ? -21.119 4.751   -9.522  1.00 89.39  ?  48  ALA A O     1 
ATOM   677  C  CB    . ALA A 1 99  ? -23.730 3.797   -9.845  1.00 99.27  ?  48  ALA A CB    1 
ATOM   678  N  N     . THR A 1 100 ? -20.465 4.114   -11.590 1.00 89.58  ?  49  THR A N     1 
ATOM   679  C  CA    . THR A 1 100 ? -19.086 4.569   -11.431 1.00 84.46  ?  49  THR A CA    1 
ATOM   680  C  C     . THR A 1 100 ? -19.010 6.090   -11.306 1.00 80.78  ?  49  THR A C     1 
ATOM   681  O  O     . THR A 1 100 ? -19.321 6.822   -12.255 1.00 78.32  ?  49  THR A O     1 
ATOM   682  C  CB    . THR A 1 100 ? -18.250 4.085   -12.605 1.00 75.52  ?  49  THR A CB    1 
ATOM   683  O  OG1   . THR A 1 100 ? -19.055 4.144   -13.780 1.00 79.51  ?  49  THR A OG1   1 
ATOM   684  C  CG2   . THR A 1 100 ? -17.791 2.653   -12.377 1.00 78.35  ?  49  THR A CG2   1 
ATOM   685  N  N     . GLY A 1 101 ? -18.551 6.555   -10.147 1.00 74.05  ?  50  GLY A N     1 
ATOM   686  C  CA    . GLY A 1 101 ? -18.538 7.963   -9.826  1.00 72.56  ?  50  GLY A CA    1 
ATOM   687  C  C     . GLY A 1 101 ? -17.398 8.723   -10.477 1.00 70.03  ?  50  GLY A C     1 
ATOM   688  O  O     . GLY A 1 101 ? -16.709 8.251   -11.386 1.00 67.19  ?  50  GLY A O     1 
ATOM   689  N  N     . ARG A 1 102 ? -17.212 9.946   -9.982  1.00 69.42  ?  51  ARG A N     1 
ATOM   690  C  CA    . ARG A 1 102 ? -16.229 10.870  -10.529 1.00 64.64  ?  51  ARG A CA    1 
ATOM   691  C  C     . ARG A 1 102 ? -14.821 10.294  -10.435 1.00 62.67  ?  51  ARG A C     1 
ATOM   692  O  O     . ARG A 1 102 ? -14.490 9.535   -9.519  1.00 67.63  ?  51  ARG A O     1 
ATOM   693  C  CB    . ARG A 1 102 ? -16.290 12.202  -9.776  1.00 67.17  ?  51  ARG A CB    1 
ATOM   694  C  CG    . ARG A 1 102 ? -15.636 12.148  -8.402  1.00 68.28  ?  51  ARG A CG    1 
ATOM   695  C  CD    . ARG A 1 102 ? -15.415 13.528  -7.804  1.00 69.26  ?  51  ARG A CD    1 
ATOM   696  N  NE    . ARG A 1 102 ? -16.678 14.120  -7.376  1.00 78.32  ?  51  ARG A NE    1 
ATOM   697  C  CZ    . ARG A 1 102 ? -17.345 13.753  -6.284  1.00 82.87  ?  51  ARG A CZ    1 
ATOM   698  N  NH1   . ARG A 1 102 ? -18.493 14.345  -5.976  1.00 81.81  ?  51  ARG A NH1   1 
ATOM   699  N  NH2   . ARG A 1 102 ? -16.866 12.792  -5.500  1.00 84.04  ?  51  ARG A NH2   1 
ATOM   700  N  N     . GLY A 1 103 ? -13.980 10.670  -11.395 1.00 58.37  ?  52  GLY A N     1 
ATOM   701  C  CA    . GLY A 1 103 ? -12.588 10.276  -11.358 1.00 56.88  ?  52  GLY A CA    1 
ATOM   702  C  C     . GLY A 1 103 ? -11.860 11.072  -10.299 1.00 56.51  ?  52  GLY A C     1 
ATOM   703  O  O     . GLY A 1 103 ? -11.896 12.310  -10.318 1.00 62.47  ?  52  GLY A O     1 
ATOM   704  N  N     . GLN A 1 104 ? -11.199 10.384  -9.375  1.00 55.48  ?  53  GLN A N     1 
ATOM   705  C  CA    . GLN A 1 104 ? -10.472 10.993  -8.268  1.00 54.28  ?  53  GLN A CA    1 
ATOM   706  C  C     . GLN A 1 104 ? -8.968  10.878  -8.493  1.00 54.77  ?  53  GLN A C     1 
ATOM   707  O  O     . GLN A 1 104 ? -8.471  9.817   -8.882  1.00 55.35  ?  53  GLN A O     1 
ATOM   708  C  CB    . GLN A 1 104 ? -10.841 10.298  -6.954  1.00 56.54  ?  53  GLN A CB    1 
ATOM   709  C  CG    . GLN A 1 104 ? -12.329 10.298  -6.605  1.00 55.96  ?  53  GLN A CG    1 
ATOM   710  C  CD    . GLN A 1 104 ? -12.581 9.927   -5.141  1.00 61.78  ?  53  GLN A CD    1 
ATOM   711  O  OE1   . GLN A 1 104 ? -12.124 10.615  -4.215  1.00 60.69  ?  53  GLN A OE1   1 
ATOM   712  N  NE2   . GLN A 1 104 ? -13.312 8.840   -4.930  1.00 59.77  ?  53  GLN A NE2   1 
ATOM   713  N  N     . ARG A 1 105 ? -8.235  11.959  -8.231  1.00 57.10  ?  54  ARG A N     1 
ATOM   714  C  CA    . ARG A 1 105 ? -6.783  11.926  -8.372  1.00 56.26  ?  54  ARG A CA    1 
ATOM   715  C  C     . ARG A 1 105 ? -6.172  11.222  -7.176  1.00 59.41  ?  54  ARG A C     1 
ATOM   716  O  O     . ARG A 1 105 ? -6.346  11.672  -6.041  1.00 64.64  ?  54  ARG A O     1 
ATOM   717  C  CB    . ARG A 1 105 ? -6.206  13.329  -8.468  1.00 63.15  ?  54  ARG A CB    1 
ATOM   718  C  CG    . ARG A 1 105 ? -6.332  13.957  -9.817  1.00 63.18  ?  54  ARG A CG    1 
ATOM   719  C  CD    . ARG A 1 105 ? -6.469  15.445  -9.652  1.00 63.98  ?  54  ARG A CD    1 
ATOM   720  N  NE    . ARG A 1 105 ? -5.239  16.145  -9.970  1.00 64.14  ?  54  ARG A NE    1 
ATOM   721  C  CZ    . ARG A 1 105 ? -4.988  17.380  -9.572  1.00 66.21  ?  54  ARG A CZ    1 
ATOM   722  N  NH1   . ARG A 1 105 ? -3.854  17.983  -9.908  1.00 67.50  ?  54  ARG A NH1   1 
ATOM   723  N  NH2   . ARG A 1 105 ? -5.891  18.004  -8.834  1.00 71.16  ?  54  ARG A NH2   1 
ATOM   724  N  N     . ILE A 1 106 ? -5.439  10.144  -7.424  1.00 56.84  ?  55  ILE A N     1 
ATOM   725  C  CA    . ILE A 1 106 ? -4.763  9.392   -6.377  1.00 53.12  ?  55  ILE A CA    1 
ATOM   726  C  C     . ILE A 1 106 ? -3.268  9.442   -6.633  1.00 53.45  ?  55  ILE A C     1 
ATOM   727  O  O     . ILE A 1 106 ? -2.814  9.176   -7.752  1.00 52.88  ?  55  ILE A O     1 
ATOM   728  C  CB    . ILE A 1 106 ? -5.234  7.931   -6.327  1.00 55.13  ?  55  ILE A CB    1 
ATOM   729  C  CG1   . ILE A 1 106 ? -6.722  7.856   -5.974  1.00 57.00  ?  55  ILE A CG1   1 
ATOM   730  C  CG2   . ILE A 1 106 ? -4.377  7.136   -5.350  1.00 54.82  ?  55  ILE A CG2   1 
ATOM   731  C  CD1   . ILE A 1 106 ? -7.051  8.423   -4.643  1.00 59.11  ?  55  ILE A CD1   1 
ATOM   732  N  N     . HIS A 1 107 ? -2.510  9.774   -5.597  1.00 56.59  ?  56  HIS A N     1 
ATOM   733  C  CA    . HIS A 1 107 ? -1.061  9.637   -5.594  1.00 58.32  ?  56  HIS A CA    1 
ATOM   734  C  C     . HIS A 1 107 ? -0.705  8.451   -4.707  1.00 53.96  ?  56  HIS A C     1 
ATOM   735  O  O     . HIS A 1 107 ? -1.001  8.462   -3.511  1.00 55.20  ?  56  HIS A O     1 
ATOM   736  C  CB    . HIS A 1 107 ? -0.387  10.912  -5.092  1.00 59.53  ?  56  HIS A CB    1 
ATOM   737  C  CG    . HIS A 1 107 ? 1.111   10.857  -5.112  1.00 58.04  ?  56  HIS A CG    1 
ATOM   738  N  ND1   . HIS A 1 107 ? 1.897   11.819  -4.515  1.00 60.36  ?  56  HIS A ND1   1 
ATOM   739  C  CD2   . HIS A 1 107 ? 1.966   9.961   -5.660  1.00 57.84  ?  56  HIS A CD2   1 
ATOM   740  C  CE1   . HIS A 1 107 ? 3.171   11.518  -4.693  1.00 59.93  ?  56  HIS A CE1   1 
ATOM   741  N  NE2   . HIS A 1 107 ? 3.241   10.395  -5.384  1.00 58.79  ?  56  HIS A NE2   1 
ATOM   742  N  N     . LEU A 1 108 ? -0.077  7.439   -5.291  1.00 51.65  ?  57  LEU A N     1 
ATOM   743  C  CA    . LEU A 1 108 ? 0.237   6.199   -4.603  1.00 50.65  ?  57  LEU A CA    1 
ATOM   744  C  C     . LEU A 1 108 ? 1.702   6.177   -4.210  1.00 52.54  ?  57  LEU A C     1 
ATOM   745  O  O     . LEU A 1 108 ? 2.573   6.384   -5.057  1.00 50.23  ?  57  LEU A O     1 
ATOM   746  C  CB    . LEU A 1 108 ? -0.054  4.994   -5.492  1.00 47.44  ?  57  LEU A CB    1 
ATOM   747  C  CG    . LEU A 1 108 ? -1.516  4.667   -5.747  1.00 51.37  ?  57  LEU A CG    1 
ATOM   748  C  CD1   . LEU A 1 108 ? -1.607  3.697   -6.894  1.00 48.48  ?  57  LEU A CD1   1 
ATOM   749  C  CD2   . LEU A 1 108 ? -2.128  4.064   -4.497  1.00 54.88  ?  57  LEU A CD2   1 
ATOM   750  N  N     . GLN A 1 109 ? 1.974   5.892   -2.937  1.00 51.78  ?  58  GLN A N     1 
ATOM   751  C  CA    . GLN A 1 109 ? 3.325   5.592   -2.483  1.00 48.13  ?  58  GLN A CA    1 
ATOM   752  C  C     . GLN A 1 109 ? 3.380   4.104   -2.195  1.00 49.18  ?  58  GLN A C     1 
ATOM   753  O  O     . GLN A 1 109 ? 2.587   3.593   -1.395  1.00 50.02  ?  58  GLN A O     1 
ATOM   754  C  CB    . GLN A 1 109 ? 3.699   6.406   -1.244  1.00 50.92  ?  58  GLN A CB    1 
ATOM   755  C  CG    . GLN A 1 109 ? 5.142   6.201   -0.792  1.00 48.76  ?  58  GLN A CG    1 
ATOM   756  C  CD    . GLN A 1 109 ? 5.496   7.016   0.435   1.00 49.66  ?  58  GLN A CD    1 
ATOM   757  O  OE1   . GLN A 1 109 ? 4.617   7.392   1.228   1.00 47.48  ?  58  GLN A OE1   1 
ATOM   758  N  NE2   . GLN A 1 109 ? 6.790   7.307   0.599   1.00 46.40  ?  58  GLN A NE2   1 
ATOM   759  N  N     . LEU A 1 110 ? 4.293   3.411   -2.848  1.00 49.74  ?  59  LEU A N     1 
ATOM   760  C  CA    . LEU A 1 110 ? 4.334   1.951   -2.814  1.00 50.18  ?  59  LEU A CA    1 
ATOM   761  C  C     . LEU A 1 110 ? 5.614   1.541   -2.110  1.00 50.41  ?  59  LEU A C     1 
ATOM   762  O  O     . LEU A 1 110 ? 6.687   1.521   -2.726  1.00 49.88  ?  59  LEU A O     1 
ATOM   763  C  CB    . LEU A 1 110 ? 4.260   1.375   -4.226  1.00 45.44  ?  59  LEU A CB    1 
ATOM   764  C  CG    . LEU A 1 110 ? 3.111   1.995   -5.015  1.00 47.38  ?  59  LEU A CG    1 
ATOM   765  C  CD1   . LEU A 1 110 ? 3.390   1.954   -6.507  1.00 51.28  ?  59  LEU A CD1   1 
ATOM   766  C  CD2   . LEU A 1 110 ? 1.819   1.275   -4.682  1.00 46.40  ?  59  LEU A CD2   1 
ATOM   767  N  N     . TRP A 1 111 ? 5.494   1.212   -0.824  1.00 44.13  ?  60  TRP A N     1 
ATOM   768  C  CA    . TRP A 1 111 ? 6.652   0.817   -0.042  1.00 45.48  ?  60  TRP A CA    1 
ATOM   769  C  C     . TRP A 1 111 ? 7.093   -0.587  -0.429  1.00 43.12  ?  60  TRP A C     1 
ATOM   770  O  O     . TRP A 1 111 ? 6.267   -1.479  -0.644  1.00 43.93  ?  60  TRP A O     1 
ATOM   771  C  CB    . TRP A 1 111 ? 6.331   0.865   1.460   1.00 46.12  ?  60  TRP A CB    1 
ATOM   772  C  CG    . TRP A 1 111 ? 6.294   2.236   2.082   1.00 44.87  ?  60  TRP A CG    1 
ATOM   773  C  CD1   . TRP A 1 111 ? 5.181   2.919   2.504   1.00 44.82  ?  60  TRP A CD1   1 
ATOM   774  C  CD2   . TRP A 1 111 ? 7.420   3.076   2.389   1.00 45.55  ?  60  TRP A CD2   1 
ATOM   775  N  NE1   . TRP A 1 111 ? 5.547   4.136   3.034   1.00 45.96  ?  60  TRP A NE1   1 
ATOM   776  C  CE2   . TRP A 1 111 ? 6.913   4.253   2.983   1.00 44.40  ?  60  TRP A CE2   1 
ATOM   777  C  CE3   . TRP A 1 111 ? 8.802   2.944   2.221   1.00 42.95  ?  60  TRP A CE3   1 
ATOM   778  C  CZ2   . TRP A 1 111 ? 7.738   5.292   3.401   1.00 44.51  ?  60  TRP A CZ2   1 
ATOM   779  C  CZ3   . TRP A 1 111 ? 9.617   3.969   2.629   1.00 46.40  ?  60  TRP A CZ3   1 
ATOM   780  C  CH2   . TRP A 1 111 ? 9.083   5.134   3.221   1.00 48.69  ?  60  TRP A CH2   1 
ATOM   781  N  N     . ASP A 1 112 ? 8.405   -0.793  -0.458  1.00 42.36  ?  61  ASP A N     1 
ATOM   782  C  CA    . ASP A 1 112 ? 9.018   -2.053  -0.869  1.00 44.98  ?  61  ASP A CA    1 
ATOM   783  C  C     . ASP A 1 112 ? 9.961   -2.468  0.256   1.00 44.80  ?  61  ASP A C     1 
ATOM   784  O  O     . ASP A 1 112 ? 10.953  -1.781  0.523   1.00 48.21  ?  61  ASP A O     1 
ATOM   785  C  CB    . ASP A 1 112 ? 9.766   -1.866  -2.199  1.00 43.64  ?  61  ASP A CB    1 
ATOM   786  C  CG    . ASP A 1 112 ? 10.381  -3.155  -2.731  1.00 46.77  ?  61  ASP A CG    1 
ATOM   787  O  OD1   . ASP A 1 112 ? 9.972   -4.242  -2.260  1.00 45.20  ?  61  ASP A OD1   1 
ATOM   788  O  OD2   . ASP A 1 112 ? 11.275  -3.079  -3.624  1.00 47.64  ?  61  ASP A OD2   1 
ATOM   789  N  N     . THR A 1 113 ? 9.656   -3.567  0.939   1.00 44.17  ?  62  THR A N     1 
ATOM   790  C  CA    . THR A 1 113 ? 10.445  -3.990  2.086   1.00 46.33  ?  62  THR A CA    1 
ATOM   791  C  C     . THR A 1 113 ? 11.326  -5.164  1.700   1.00 45.72  ?  62  THR A C     1 
ATOM   792  O  O     . THR A 1 113 ? 10.934  -6.006  0.887   1.00 48.71  ?  62  THR A O     1 
ATOM   793  C  CB    . THR A 1 113 ? 9.550   -4.372  3.261   1.00 43.35  ?  62  THR A CB    1 
ATOM   794  O  OG1   . THR A 1 113 ? 8.826   -5.558  2.939   1.00 48.10  ?  62  THR A OG1   1 
ATOM   795  C  CG2   . THR A 1 113 ? 8.551   -3.286  3.514   1.00 45.76  ?  62  THR A CG2   1 
ATOM   796  N  N     . ALA A 1 114 ? 12.526  -5.203  2.257   1.00 43.25  ?  63  ALA A N     1 
ATOM   797  C  CA    . ALA A 1 114 ? 13.362  -6.371  2.077   1.00 43.33  ?  63  ALA A CA    1 
ATOM   798  C  C     . ALA A 1 114 ? 12.794  -7.523  2.889   1.00 48.03  ?  63  ALA A C     1 
ATOM   799  O  O     . ALA A 1 114 ? 12.222  -7.322  3.963   1.00 46.01  ?  63  ALA A O     1 
ATOM   800  C  CB    . ALA A 1 114 ? 14.791  -6.072  2.513   1.00 45.77  ?  63  ALA A CB    1 
ATOM   801  N  N     . GLY A 1 115 ? 12.950  -8.745  2.366   1.00 46.28  ?  64  GLY A N     1 
ATOM   802  C  CA    . GLY A 1 115 ? 12.400  -9.902  3.051   1.00 44.58  ?  64  GLY A CA    1 
ATOM   803  C  C     . GLY A 1 115 ? 13.347  -10.684 3.943   1.00 44.53  ?  64  GLY A C     1 
ATOM   804  O  O     . GLY A 1 115 ? 12.902  -11.578 4.673   1.00 47.55  ?  64  GLY A O     1 
ATOM   805  N  N     . LEU A 1 116 ? 14.646  -10.396 3.901   1.00 42.35  ?  65  LEU A N     1 
ATOM   806  C  CA    . LEU A 1 116 ? 15.587  -11.098 4.762   1.00 44.66  ?  65  LEU A CA    1 
ATOM   807  C  C     . LEU A 1 116 ? 15.407  -10.675 6.221   1.00 48.38  ?  65  LEU A C     1 
ATOM   808  O  O     . LEU A 1 116 ? 15.021  -9.537  6.526   1.00 44.11  ?  65  LEU A O     1 
ATOM   809  C  CB    . LEU A 1 116 ? 17.023  -10.831 4.304   1.00 44.34  ?  65  LEU A CB    1 
ATOM   810  C  CG    . LEU A 1 116 ? 17.418  -11.515 2.995   1.00 42.10  ?  65  LEU A CG    1 
ATOM   811  C  CD1   . LEU A 1 116 ? 18.730  -10.992 2.469   1.00 40.75  ?  65  LEU A CD1   1 
ATOM   812  C  CD2   . LEU A 1 116 ? 17.512  -13.001 3.209   1.00 38.52  ?  65  LEU A CD2   1 
ATOM   813  N  N     . GLU A 1 117 ? 15.688  -11.617 7.129   1.00 51.30  ?  66  GLU A N     1 
ATOM   814  C  CA    . GLU A 1 117 ? 15.447  -11.382 8.556   1.00 50.50  ?  66  GLU A CA    1 
ATOM   815  C  C     . GLU A 1 117 ? 16.265  -10.205 9.074   1.00 48.33  ?  66  GLU A C     1 
ATOM   816  O  O     . GLU A 1 117 ? 15.748  -9.370  9.826   1.00 47.44  ?  66  GLU A O     1 
ATOM   817  C  CB    . GLU A 1 117 ? 15.756  -12.646 9.361   1.00 44.55  ?  66  GLU A CB    1 
ATOM   818  N  N     . ARG A 1 118 ? 17.500  -10.090 8.625   1.00 44.68  ?  67  ARG A N     1 
ATOM   819  C  CA    . ARG A 1 118 ? 18.411  -9.031  9.101   1.00 45.86  ?  67  ARG A CA    1 
ATOM   820  C  C     . ARG A 1 118 ? 17.826  -7.628  8.970   1.00 49.91  ?  67  ARG A C     1 
ATOM   821  O  O     . ARG A 1 118 ? 18.421  -6.735  9.512   1.00 55.07  ?  67  ARG A O     1 
ATOM   822  C  CB    . ARG A 1 118 ? 19.782  -9.143  8.438   1.00 48.11  ?  67  ARG A CB    1 
ATOM   823  C  CG    . ARG A 1 118 ? 19.994  -8.217  7.263   1.00 54.20  ?  67  ARG A CG    1 
ATOM   824  C  CD    . ARG A 1 118 ? 21.261  -8.492  6.510   1.00 58.50  ?  67  ARG A CD    1 
ATOM   825  N  NE    . ARG A 1 118 ? 22.338  -7.610  6.866   1.00 57.72  ?  67  ARG A NE    1 
ATOM   826  C  CZ    . ARG A 1 118 ? 22.980  -6.860  6.011   1.00 60.13  ?  67  ARG A CZ    1 
ATOM   827  N  NH1   . ARG A 1 118 ? 22.649  -6.894  4.743   1.00 62.87  ?  67  ARG A NH1   1 
ATOM   828  N  NH2   . ARG A 1 118 ? 23.967  -6.094  6.405   1.00 57.02  ?  67  ARG A NH2   1 
ATOM   829  N  N     . PHE A 1 119 ? 16.732  -7.460  8.246   1.00 49.88  ?  68  PHE A N     1 
ATOM   830  C  CA    . PHE A 1 119 ? 16.067  -6.179  8.023   1.00 43.84  ?  68  PHE A CA    1 
ATOM   831  C  C     . PHE A 1 119 ? 14.704  -6.137  8.691   1.00 44.85  ?  68  PHE A C     1 
ATOM   832  O  O     . PHE A 1 119 ? 13.939  -5.195  8.460   1.00 45.58  ?  68  PHE A O     1 
ATOM   833  C  CB    . PHE A 1 119 ? 15.862  -5.917  6.521   1.00 49.28  ?  68  PHE A CB    1 
ATOM   834  C  CG    . PHE A 1 119 ? 17.129  -5.779  5.727   1.00 48.62  ?  68  PHE A CG    1 
ATOM   835  C  CD1   . PHE A 1 119 ? 18.020  -4.741  5.980   1.00 46.62  ?  68  PHE A CD1   1 
ATOM   836  C  CD2   . PHE A 1 119 ? 17.410  -6.672  4.697   1.00 48.98  ?  68  PHE A CD2   1 
ATOM   837  C  CE1   . PHE A 1 119 ? 19.184  -4.607  5.243   1.00 51.04  ?  68  PHE A CE1   1 
ATOM   838  C  CE2   . PHE A 1 119 ? 18.572  -6.552  3.943   1.00 45.17  ?  68  PHE A CE2   1 
ATOM   839  C  CZ    . PHE A 1 119 ? 19.466  -5.511  4.216   1.00 48.18  ?  68  PHE A CZ    1 
ATOM   840  N  N     . ARG A 1 120 ? 14.368  -7.158  9.485   1.00 48.47  ?  69  ARG A N     1 
ATOM   841  C  CA    . ARG A 1 120 ? 12.984  -7.352  9.909   1.00 48.96  ?  69  ARG A CA    1 
ATOM   842  C  C     . ARG A 1 120 ? 12.489  -6.206  10.791  1.00 50.15  ?  69  ARG A C     1 
ATOM   843  O  O     . ARG A 1 120 ? 11.362  -5.721  10.619  1.00 50.03  ?  69  ARG A O     1 
ATOM   844  C  CB    . ARG A 1 120 ? 12.853  -8.700  10.622  1.00 51.16  ?  69  ARG A CB    1 
ATOM   845  C  CG    . ARG A 1 120 ? 11.428  -9.173  10.839  1.00 51.64  ?  69  ARG A CG    1 
ATOM   846  C  CD    . ARG A 1 120 ? 10.627  -9.276  9.524   1.00 58.41  ?  69  ARG A CD    1 
ATOM   847  N  NE    . ARG A 1 120 ? 11.249  -10.098 8.476   1.00 55.29  ?  69  ARG A NE    1 
ATOM   848  C  CZ    . ARG A 1 120 ? 11.137  -11.426 8.375   1.00 57.34  ?  69  ARG A CZ    1 
ATOM   849  N  NH1   . ARG A 1 120 ? 10.434  -12.124 9.269   1.00 53.52  ?  69  ARG A NH1   1 
ATOM   850  N  NH2   . ARG A 1 120 ? 11.727  -12.056 7.364   1.00 56.66  ?  69  ARG A NH2   1 
ATOM   851  N  N     . SER A 1 121 ? 13.301  -5.742  11.736  1.00 50.16  ?  70  SER A N     1 
ATOM   852  C  CA    . SER A 1 121 ? 12.761  -4.679  12.574  1.00 53.34  ?  70  SER A CA    1 
ATOM   853  C  C     . SER A 1 121 ? 12.770  -3.349  11.837  1.00 49.98  ?  70  SER A C     1 
ATOM   854  O  O     . SER A 1 121 ? 11.889  -2.509  12.063  1.00 50.86  ?  70  SER A O     1 
ATOM   855  C  CB    . SER A 1 121 ? 13.506  -4.584  13.918  1.00 48.73  ?  70  SER A CB    1 
ATOM   856  O  OG    . SER A 1 121 ? 14.875  -4.254  13.757  1.00 48.95  ?  70  SER A OG    1 
ATOM   857  N  N     . LEU A 1 122 ? 13.718  -3.150  10.923  1.00 50.78  ?  71  LEU A N     1 
ATOM   858  C  CA    . LEU A 1 122 ? 13.691  -1.939  10.110  1.00 48.93  ?  71  LEU A CA    1 
ATOM   859  C  C     . LEU A 1 122 ? 12.419  -1.863  9.276   1.00 47.24  ?  71  LEU A C     1 
ATOM   860  O  O     . LEU A 1 122 ? 11.748  -0.826  9.239   1.00 49.53  ?  71  LEU A O     1 
ATOM   861  C  CB    . LEU A 1 122 ? 14.914  -1.880  9.206   1.00 51.48  ?  71  LEU A CB    1 
ATOM   862  C  CG    . LEU A 1 122 ? 14.815  -0.651  8.322   1.00 51.66  ?  71  LEU A CG    1 
ATOM   863  C  CD1   . LEU A 1 122 ? 14.993  0.579   9.183   1.00 48.48  ?  71  LEU A CD1   1 
ATOM   864  C  CD2   . LEU A 1 122 ? 15.847  -0.694  7.230   1.00 52.28  ?  71  LEU A CD2   1 
ATOM   865  N  N     . THR A 1 123 ? 12.069  -2.955  8.592   1.00 48.60  ?  72  THR A N     1 
ATOM   866  C  CA    . THR A 1 123 ? 10.902  -2.908  7.717   1.00 48.64  ?  72  THR A CA    1 
ATOM   867  C  C     . THR A 1 123 ? 9.613   -2.876  8.527   1.00 49.33  ?  72  THR A C     1 
ATOM   868  O  O     . THR A 1 123 ? 8.640   -2.231  8.123   1.00 50.48  ?  72  THR A O     1 
ATOM   869  C  CB    . THR A 1 123 ? 10.914  -4.089  6.735   1.00 46.30  ?  72  THR A CB    1 
ATOM   870  O  OG1   . THR A 1 123 ? 10.900  -5.332  7.441   1.00 50.36  ?  72  THR A OG1   1 
ATOM   871  C  CG2   . THR A 1 123 ? 12.169  -4.066  5.913   1.00 46.94  ?  72  THR A CG2   1 
ATOM   872  N  N     . THR A 1 124 ? 9.587   -3.562  9.678   1.00 52.57  ?  73  THR A N     1 
ATOM   873  C  CA    . THR A 1 124 ? 8.406   -3.531  10.540  1.00 49.24  ?  73  THR A CA    1 
ATOM   874  C  C     . THR A 1 124 ? 8.099   -2.121  11.022  1.00 46.74  ?  73  THR A C     1 
ATOM   875  O  O     . THR A 1 124 ? 6.931   -1.758  11.209  1.00 45.81  ?  73  THR A O     1 
ATOM   876  C  CB    . THR A 1 124 ? 8.622   -4.455  11.723  1.00 49.40  ?  73  THR A CB    1 
ATOM   877  O  OG1   . THR A 1 124 ? 8.915   -5.765  11.235  1.00 49.71  ?  73  THR A OG1   1 
ATOM   878  C  CG2   . THR A 1 124 ? 7.380   -4.510  12.597  1.00 54.20  ?  73  THR A CG2   1 
ATOM   879  N  N     . ALA A 1 125 ? 9.136   -1.312  11.221  1.00 46.15  ?  74  ALA A N     1 
ATOM   880  C  CA    . ALA A 1 125 ? 8.930   0.089   11.539  1.00 45.69  ?  74  ALA A CA    1 
ATOM   881  C  C     . ALA A 1 125 ? 7.934   0.756   10.600  1.00 51.51  ?  74  ALA A C     1 
ATOM   882  O  O     . ALA A 1 125 ? 7.165   1.620   11.033  1.00 54.61  ?  74  ALA A O     1 
ATOM   883  C  CB    . ALA A 1 125 ? 10.267  0.827   11.492  1.00 50.73  ?  74  ALA A CB    1 
ATOM   884  N  N     . PHE A 1 126 ? 7.913   0.367   9.322   1.00 54.22  ?  75  PHE A N     1 
ATOM   885  C  CA    . PHE A 1 126 ? 7.131   1.090   8.321   1.00 51.50  ?  75  PHE A CA    1 
ATOM   886  C  C     . PHE A 1 126 ? 5.696   0.596   8.179   1.00 52.69  ?  75  PHE A C     1 
ATOM   887  O  O     . PHE A 1 126 ? 4.939   1.196   7.402   1.00 53.24  ?  75  PHE A O     1 
ATOM   888  C  CB    . PHE A 1 126 ? 7.821   1.039   6.957   1.00 47.29  ?  75  PHE A CB    1 
ATOM   889  C  CG    . PHE A 1 126 ? 9.115   1.774   6.923   1.00 49.46  ?  75  PHE A CG    1 
ATOM   890  C  CD1   . PHE A 1 126 ? 10.293  1.135   7.284   1.00 50.60  ?  75  PHE A CD1   1 
ATOM   891  C  CD2   . PHE A 1 126 ? 9.152   3.118   6.592   1.00 51.71  ?  75  PHE A CD2   1 
ATOM   892  C  CE1   . PHE A 1 126 ? 11.503  1.808   7.291   1.00 50.93  ?  75  PHE A CE1   1 
ATOM   893  C  CE2   . PHE A 1 126 ? 10.360  3.812   6.600   1.00 56.43  ?  75  PHE A CE2   1 
ATOM   894  C  CZ    . PHE A 1 126 ? 11.540  3.154   6.941   1.00 55.18  ?  75  PHE A CZ    1 
ATOM   895  N  N     . PHE A 1 127 ? 5.291   -0.458  8.911   1.00 49.90  ?  76  PHE A N     1 
ATOM   896  C  CA    . PHE A 1 127 ? 3.884   -0.855  8.874   1.00 49.48  ?  76  PHE A CA    1 
ATOM   897  C  C     . PHE A 1 127 ? 2.979   0.253   9.392   1.00 55.80  ?  76  PHE A C     1 
ATOM   898  O  O     . PHE A 1 127 ? 1.771   0.213   9.154   1.00 60.22  ?  76  PHE A O     1 
ATOM   899  C  CB    . PHE A 1 127 ? 3.599   -2.103  9.706   1.00 50.57  ?  76  PHE A CB    1 
ATOM   900  C  CG    . PHE A 1 127 ? 4.278   -3.362  9.231   1.00 48.72  ?  76  PHE A CG    1 
ATOM   901  C  CD1   . PHE A 1 127 ? 5.379   -3.329  8.394   1.00 52.29  ?  76  PHE A CD1   1 
ATOM   902  C  CD2   . PHE A 1 127 ? 3.834   -4.589  9.677   1.00 44.56  ?  76  PHE A CD2   1 
ATOM   903  C  CE1   . PHE A 1 127 ? 5.998   -4.501  7.992   1.00 53.03  ?  76  PHE A CE1   1 
ATOM   904  C  CE2   . PHE A 1 127 ? 4.453   -5.755  9.293   1.00 45.29  ?  76  PHE A CE2   1 
ATOM   905  C  CZ    . PHE A 1 127 ? 5.538   -5.715  8.452   1.00 49.37  ?  76  PHE A CZ    1 
ATOM   906  N  N     . ARG A 1 128 ? 3.522   1.218   10.136  1.00 59.43  ?  77  ARG A N     1 
ATOM   907  C  CA    . ARG A 1 128 ? 2.724   2.368   10.564  1.00 63.96  ?  77  ARG A CA    1 
ATOM   908  C  C     . ARG A 1 128 ? 2.198   3.142   9.365   1.00 63.63  ?  77  ARG A C     1 
ATOM   909  O  O     . ARG A 1 128 ? 1.029   3.565   9.344   1.00 64.97  ?  77  ARG A O     1 
ATOM   910  C  CB    . ARG A 1 128 ? 3.558   3.299   11.464  1.00 66.26  ?  77  ARG A CB    1 
ATOM   911  C  CG    . ARG A 1 128 ? 4.735   4.020   10.759  1.00 68.84  ?  77  ARG A CG    1 
ATOM   912  C  CD    . ARG A 1 128 ? 5.515   5.033   11.601  1.00 73.43  ?  77  ARG A CD    1 
ATOM   913  N  NE    . ARG A 1 128 ? 6.206   4.436   12.749  1.00 73.64  ?  77  ARG A NE    1 
ATOM   914  C  CZ    . ARG A 1 128 ? 5.759   4.530   13.999  1.00 77.12  ?  77  ARG A CZ    1 
ATOM   915  N  NH1   . ARG A 1 128 ? 4.634   5.218   14.264  1.00 73.54  ?  77  ARG A NH1   1 
ATOM   916  N  NH2   . ARG A 1 128 ? 6.437   3.949   14.985  1.00 72.88  ?  77  ARG A NH2   1 
ATOM   917  N  N     . ASP A 1 129 ? 3.038   3.292   8.336   1.00 61.88  ?  78  ASP A N     1 
ATOM   918  C  CA    . ASP A 1 129 ? 2.741   4.217   7.264   1.00 57.14  ?  78  ASP A CA    1 
ATOM   919  C  C     . ASP A 1 129 ? 1.725   3.653   6.295   1.00 55.93  ?  78  ASP A C     1 
ATOM   920  O  O     . ASP A 1 129 ? 1.150   4.415   5.519   1.00 63.84  ?  78  ASP A O     1 
ATOM   921  C  CB    . ASP A 1 129 ? 4.024   4.598   6.529   1.00 52.71  ?  78  ASP A CB    1 
ATOM   922  C  CG    . ASP A 1 129 ? 3.988   6.018   5.997   1.00 55.15  ?  78  ASP A CG    1 
ATOM   923  O  OD1   . ASP A 1 129 ? 3.335   6.854   6.638   1.00 57.13  ?  78  ASP A OD1   1 
ATOM   924  O  OD2   . ASP A 1 129 ? 4.593   6.298   4.929   1.00 56.19  ?  78  ASP A OD2   1 
ATOM   925  N  N     . ALA A 1 130 ? 1.482   2.352   6.311   1.00 54.42  ?  79  ALA A N     1 
ATOM   926  C  CA    . ALA A 1 130 ? 0.654   1.759   5.275   1.00 53.87  ?  79  ALA A CA    1 
ATOM   927  C  C     . ALA A 1 130 ? -0.822  1.836   5.632   1.00 53.89  ?  79  ALA A C     1 
ATOM   928  O  O     . ALA A 1 130 ? -1.204  1.784   6.799   1.00 59.27  ?  79  ALA A O     1 
ATOM   929  C  CB    . ALA A 1 130 ? 1.053   0.308   5.034   1.00 51.07  ?  79  ALA A CB    1 
ATOM   930  N  N     . MET A 1 131 ? -1.652  1.970   4.604   1.00 55.65  ?  80  MET A N     1 
ATOM   931  C  CA    . MET A 1 131 ? -3.090  1.782   4.729   1.00 56.14  ?  80  MET A CA    1 
ATOM   932  C  C     . MET A 1 131 ? -3.545  0.458   4.126   1.00 54.64  ?  80  MET A C     1 
ATOM   933  O  O     . MET A 1 131 ? -4.754  0.187   4.068   1.00 52.91  ?  80  MET A O     1 
ATOM   934  C  CB    . MET A 1 131 ? -3.833  2.943   4.057   1.00 52.31  ?  80  MET A CB    1 
ATOM   935  C  CG    . MET A 1 131 ? -3.184  4.282   4.264   1.00 48.54  ?  80  MET A CG    1 
ATOM   936  S  SD    . MET A 1 131 ? -3.847  5.437   3.061   1.00 57.31  ?  80  MET A SD    1 
ATOM   937  C  CE    . MET A 1 131 ? -3.024  6.931   3.559   1.00 55.39  ?  80  MET A CE    1 
ATOM   938  N  N     . GLY A 1 132 ? -2.610  -0.362  3.666   1.00 49.47  ?  81  GLY A N     1 
ATOM   939  C  CA    . GLY A 1 132 ? -2.944  -1.625  3.044   1.00 46.72  ?  81  GLY A CA    1 
ATOM   940  C  C     . GLY A 1 132 ? -1.663  -2.341  2.699   1.00 48.16  ?  81  GLY A C     1 
ATOM   941  O  O     . GLY A 1 132 ? -0.577  -1.752  2.710   1.00 48.48  ?  81  GLY A O     1 
ATOM   942  N  N     . PHE A 1 133 ? -1.805  -3.630  2.391   1.00 48.03  ?  82  PHE A N     1 
ATOM   943  C  CA    . PHE A 1 133 ? -0.660  -4.513  2.252   1.00 48.33  ?  82  PHE A CA    1 
ATOM   944  C  C     . PHE A 1 133 ? -0.821  -5.426  1.042   1.00 49.24  ?  82  PHE A C     1 
ATOM   945  O  O     . PHE A 1 133 ? -1.909  -5.948  0.766   1.00 48.24  ?  82  PHE A O     1 
ATOM   946  C  CB    . PHE A 1 133 ? -0.456  -5.360  3.526   1.00 48.59  ?  82  PHE A CB    1 
ATOM   947  C  CG    . PHE A 1 133 ? -0.149  -4.545  4.751   1.00 48.81  ?  82  PHE A CG    1 
ATOM   948  C  CD1   . PHE A 1 133 ? 1.153   -4.180  5.046   1.00 46.24  ?  82  PHE A CD1   1 
ATOM   949  C  CD2   . PHE A 1 133 ? -1.172  -4.125  5.596   1.00 49.27  ?  82  PHE A CD2   1 
ATOM   950  C  CE1   . PHE A 1 133 ? 1.433   -3.423  6.177   1.00 49.32  ?  82  PHE A CE1   1 
ATOM   951  C  CE2   . PHE A 1 133 ? -0.903  -3.368  6.727   1.00 50.18  ?  82  PHE A CE2   1 
ATOM   952  C  CZ    . PHE A 1 133 ? 0.403   -3.015  7.021   1.00 47.91  ?  82  PHE A CZ    1 
ATOM   953  N  N     . LEU A 1 134 ? 0.281   -5.603  0.325   1.00 47.79  ?  83  LEU A N     1 
ATOM   954  C  CA    . LEU A 1 134 ? 0.392   -6.566  -0.758  1.00 49.69  ?  83  LEU A CA    1 
ATOM   955  C  C     . LEU A 1 134 ? 1.304   -7.674  -0.251  1.00 47.41  ?  83  LEU A C     1 
ATOM   956  O  O     . LEU A 1 134 ? 2.506   -7.455  -0.048  1.00 49.35  ?  83  LEU A O     1 
ATOM   957  C  CB    . LEU A 1 134 ? 0.940   -5.903  -2.019  1.00 48.33  ?  83  LEU A CB    1 
ATOM   958  C  CG    . LEU A 1 134 ? 0.304   -6.298  -3.352  1.00 49.00  ?  83  LEU A CG    1 
ATOM   959  C  CD1   . LEU A 1 134 ? -1.198  -6.099  -3.333  1.00 50.85  ?  83  LEU A CD1   1 
ATOM   960  C  CD2   . LEU A 1 134 ? 0.904   -5.491  -4.475  1.00 50.70  ?  83  LEU A CD2   1 
ATOM   961  N  N     . LEU A 1 135 ? 0.734   -8.849  -0.009  1.00 45.59  ?  84  LEU A N     1 
ATOM   962  C  CA    . LEU A 1 135 ? 1.467   -9.945  0.612   1.00 40.89  ?  84  LEU A CA    1 
ATOM   963  C  C     . LEU A 1 135 ? 1.792   -10.967 -0.462  1.00 43.91  ?  84  LEU A C     1 
ATOM   964  O  O     . LEU A 1 135 ? 0.884   -11.537 -1.082  1.00 49.59  ?  84  LEU A O     1 
ATOM   965  C  CB    . LEU A 1 135 ? 0.646   -10.561 1.746   1.00 47.19  ?  84  LEU A CB    1 
ATOM   966  C  CG    . LEU A 1 135 ? 1.175   -11.806 2.466   1.00 44.63  ?  84  LEU A CG    1 
ATOM   967  C  CD1   . LEU A 1 135 ? 2.691   -11.748 2.707   1.00 38.16  ?  84  LEU A CD1   1 
ATOM   968  C  CD2   . LEU A 1 135 ? 0.417   -11.982 3.769   1.00 45.79  ?  84  LEU A CD2   1 
ATOM   969  N  N     . LEU A 1 136 ? 3.076   -11.173 -0.717  1.00 41.37  ?  85  LEU A N     1 
ATOM   970  C  CA    . LEU A 1 136 ? 3.497   -11.989 -1.839  1.00 43.09  ?  85  LEU A CA    1 
ATOM   971  C  C     . LEU A 1 136 ? 4.096   -13.291 -1.357  1.00 46.30  ?  85  LEU A C     1 
ATOM   972  O  O     . LEU A 1 136 ? 4.879   -13.300 -0.403  1.00 42.58  ?  85  LEU A O     1 
ATOM   973  C  CB    . LEU A 1 136 ? 4.534   -11.268 -2.696  1.00 43.84  ?  85  LEU A CB    1 
ATOM   974  C  CG    . LEU A 1 136 ? 3.943   -10.559 -3.897  1.00 42.19  ?  85  LEU A CG    1 
ATOM   975  C  CD1   . LEU A 1 136 ? 3.188   -9.344  -3.402  1.00 41.83  ?  85  LEU A CD1   1 
ATOM   976  C  CD2   . LEU A 1 136 ? 5.045   -10.183 -4.884  1.00 39.84  ?  85  LEU A CD2   1 
ATOM   977  N  N     . PHE A 1 137 ? 3.745   -14.384 -2.035  1.00 46.14  ?  86  PHE A N     1 
ATOM   978  C  CA    . PHE A 1 137 ? 4.597   -15.559 -2.046  1.00 44.65  ?  86  PHE A CA    1 
ATOM   979  C  C     . PHE A 1 137 ? 4.971   -15.878 -3.487  1.00 48.20  ?  86  PHE A C     1 
ATOM   980  O  O     . PHE A 1 137 ? 4.495   -15.249 -4.431  1.00 48.18  ?  86  PHE A O     1 
ATOM   981  C  CB    . PHE A 1 137 ? 3.945   -16.763 -1.352  1.00 39.58  ?  86  PHE A CB    1 
ATOM   982  C  CG    . PHE A 1 137 ? 2.754   -17.322 -2.064  1.00 41.34  ?  86  PHE A CG    1 
ATOM   983  C  CD1   . PHE A 1 137 ? 1.505   -16.758 -1.895  1.00 42.42  ?  86  PHE A CD1   1 
ATOM   984  C  CD2   . PHE A 1 137 ? 2.874   -18.438 -2.863  1.00 42.80  ?  86  PHE A CD2   1 
ATOM   985  C  CE1   . PHE A 1 137 ? 0.398   -17.277 -2.531  1.00 41.22  ?  86  PHE A CE1   1 
ATOM   986  C  CE2   . PHE A 1 137 ? 1.767   -18.962 -3.517  1.00 43.36  ?  86  PHE A CE2   1 
ATOM   987  C  CZ    . PHE A 1 137 ? 0.525   -18.381 -3.345  1.00 38.72  ?  86  PHE A CZ    1 
ATOM   988  N  N     . ASP A 1 138 ? 5.850   -16.865 -3.630  1.00 48.51  ?  87  ASP A N     1 
ATOM   989  C  CA    . ASP A 1 138 ? 6.356   -17.341 -4.904  1.00 46.25  ?  87  ASP A CA    1 
ATOM   990  C  C     . ASP A 1 138 ? 5.696   -18.681 -5.218  1.00 50.24  ?  87  ASP A C     1 
ATOM   991  O  O     . ASP A 1 138 ? 5.733   -19.600 -4.387  1.00 49.29  ?  87  ASP A O     1 
ATOM   992  C  CB    . ASP A 1 138 ? 7.878   -17.473 -4.813  1.00 44.56  ?  87  ASP A CB    1 
ATOM   993  C  CG    . ASP A 1 138 ? 8.510   -17.971 -6.087  1.00 48.51  ?  87  ASP A CG    1 
ATOM   994  O  OD1   . ASP A 1 138 ? 7.784   -18.385 -7.031  1.00 52.58  ?  87  ASP A OD1   1 
ATOM   995  O  OD2   . ASP A 1 138 ? 9.765   -17.959 -6.148  1.00 49.36  ?  87  ASP A OD2   1 
ATOM   996  N  N     . LEU A 1 139 ? 5.111   -18.796 -6.422  1.00 46.60  ?  88  LEU A N     1 
ATOM   997  C  CA    . LEU A 1 139 ? 4.460   -20.031 -6.862  1.00 46.17  ?  88  LEU A CA    1 
ATOM   998  C  C     . LEU A 1 139 ? 5.450   -21.166 -7.091  1.00 47.47  ?  88  LEU A C     1 
ATOM   999  O  O     . LEU A 1 139 ? 5.047   -22.336 -7.079  1.00 46.25  ?  88  LEU A O     1 
ATOM   1000 C  CB    . LEU A 1 139 ? 3.664   -19.794 -8.154  1.00 43.71  ?  88  LEU A CB    1 
ATOM   1001 C  CG    . LEU A 1 139 ? 2.341   -19.017 -8.026  1.00 48.88  ?  88  LEU A CG    1 
ATOM   1002 C  CD1   . LEU A 1 139 ? 1.764   -18.635 -9.379  1.00 47.01  ?  88  LEU A CD1   1 
ATOM   1003 C  CD2   . LEU A 1 139 ? 1.304   -19.763 -7.187  1.00 44.39  ?  88  LEU A CD2   1 
ATOM   1004 N  N     . THR A 1 140 ? 6.725   -20.858 -7.320  1.00 45.43  ?  89  THR A N     1 
ATOM   1005 C  CA    . THR A 1 140 ? 7.745   -21.881 -7.485  1.00 45.54  ?  89  THR A CA    1 
ATOM   1006 C  C     . THR A 1 140 ? 8.458   -22.237 -6.179  1.00 49.71  ?  89  THR A C     1 
ATOM   1007 O  O     . THR A 1 140 ? 9.548   -22.819 -6.226  1.00 50.38  ?  89  THR A O     1 
ATOM   1008 C  CB    . THR A 1 140 ? 8.764   -21.436 -8.541  1.00 50.21  ?  89  THR A CB    1 
ATOM   1009 O  OG1   . THR A 1 140 ? 9.517   -20.301 -8.081  1.00 47.08  ?  89  THR A OG1   1 
ATOM   1010 C  CG2   . THR A 1 140 ? 8.053   -21.058 -9.828  1.00 50.69  ?  89  THR A CG2   1 
ATOM   1011 N  N     . ASN A 1 141 ? 7.875   -21.916 -5.014  1.00 50.77  ?  90  ASN A N     1 
ATOM   1012 C  CA    . ASN A 1 141 ? 8.615   -22.054 -3.748  1.00 52.47  ?  90  ASN A CA    1 
ATOM   1013 C  C     . ASN A 1 141 ? 7.633   -22.313 -2.602  1.00 48.63  ?  90  ASN A C     1 
ATOM   1014 O  O     . ASN A 1 141 ? 7.128   -21.376 -1.984  1.00 47.70  ?  90  ASN A O     1 
ATOM   1015 C  CB    . ASN A 1 141 ? 9.454   -20.819 -3.480  1.00 51.53  ?  90  ASN A CB    1 
ATOM   1016 C  CG    . ASN A 1 141 ? 10.425  -21.025 -2.360  1.00 53.47  ?  90  ASN A CG    1 
ATOM   1017 O  OD1   . ASN A 1 141 ? 10.056  -21.484 -1.283  1.00 54.49  ?  90  ASN A OD1   1 
ATOM   1018 N  ND2   . ASN A 1 141 ? 11.687  -20.700 -2.607  1.00 60.86  ?  90  ASN A ND2   1 
ATOM   1019 N  N     . GLU A 1 142 ? 7.412   -23.595 -2.298  1.00 48.09  ?  91  GLU A N     1 
ATOM   1020 C  CA    . GLU A 1 142 ? 6.414   -23.963 -1.298  1.00 53.08  ?  91  GLU A CA    1 
ATOM   1021 C  C     . GLU A 1 142 ? 6.726   -23.342 0.068   1.00 51.24  ?  91  GLU A C     1 
ATOM   1022 O  O     . GLU A 1 142 ? 5.816   -22.906 0.789   1.00 52.99  ?  91  GLU A O     1 
ATOM   1023 C  CB    . GLU A 1 142 ? 6.323   -25.495 -1.212  1.00 53.01  ?  91  GLU A CB    1 
ATOM   1024 C  CG    . GLU A 1 142 ? 5.318   -26.021 -0.176  1.00 54.27  ?  91  GLU A CG    1 
ATOM   1025 C  CD    . GLU A 1 142 ? 3.886   -26.148 -0.703  1.00 64.03  ?  91  GLU A CD    1 
ATOM   1026 O  OE1   . GLU A 1 142 ? 3.692   -26.406 -1.920  1.00 63.67  ?  91  GLU A OE1   1 
ATOM   1027 O  OE2   . GLU A 1 142 ? 2.943   -25.988 0.113   1.00 67.53  ?  91  GLU A OE2   1 
ATOM   1028 N  N     . GLN A 1 143 ? 8.003   -23.267 0.440   1.00 47.17  ?  92  GLN A N     1 
ATOM   1029 C  CA    . GLN A 1 143 ? 8.332   -22.677 1.737   1.00 52.34  ?  92  GLN A CA    1 
ATOM   1030 C  C     . GLN A 1 143 ? 7.841   -21.235 1.838   1.00 50.41  ?  92  GLN A C     1 
ATOM   1031 O  O     . GLN A 1 143 ? 7.396   -20.798 2.904   1.00 49.45  ?  92  GLN A O     1 
ATOM   1032 C  CB    . GLN A 1 143 ? 9.841   -22.750 1.991   1.00 50.11  ?  92  GLN A CB    1 
ATOM   1033 C  CG    . GLN A 1 143 ? 10.248  -22.233 3.354   1.00 56.76  ?  92  GLN A CG    1 
ATOM   1034 C  CD    . GLN A 1 143 ? 9.789   -23.139 4.495   1.00 58.41  ?  92  GLN A CD    1 
ATOM   1035 O  OE1   . GLN A 1 143 ? 8.727   -22.930 5.100   1.00 56.04  ?  92  GLN A OE1   1 
ATOM   1036 N  NE2   . GLN A 1 143 ? 10.599  -24.148 4.800   1.00 57.09  ?  92  GLN A NE2   1 
ATOM   1037 N  N     . SER A 1 144 ? 7.916   -20.475 0.741   1.00 50.18  ?  93  SER A N     1 
ATOM   1038 C  CA    . SER A 1 144 ? 7.449   -19.094 0.782   1.00 43.55  ?  93  SER A CA    1 
ATOM   1039 C  C     . SER A 1 144 ? 5.944   -19.013 0.931   1.00 42.71  ?  93  SER A C     1 
ATOM   1040 O  O     . SER A 1 144 ? 5.428   -18.007 1.431   1.00 47.27  ?  93  SER A O     1 
ATOM   1041 C  CB    . SER A 1 144 ? 7.889   -18.345 -0.469  1.00 45.86  ?  93  SER A CB    1 
ATOM   1042 O  OG    . SER A 1 144 ? 6.974   -18.572 -1.529  1.00 46.30  ?  93  SER A OG    1 
ATOM   1043 N  N     . PHE A 1 145 ? 5.228   -20.046 0.526   1.00 43.86  ?  94  PHE A N     1 
ATOM   1044 C  CA    . PHE A 1 145 ? 3.792   -20.035 0.733   1.00 44.93  ?  94  PHE A CA    1 
ATOM   1045 C  C     . PHE A 1 145 ? 3.439   -20.483 2.145   1.00 51.01  ?  94  PHE A C     1 
ATOM   1046 O  O     . PHE A 1 145 ? 2.479   -19.980 2.743   1.00 50.71  ?  94  PHE A O     1 
ATOM   1047 C  CB    . PHE A 1 145 ? 3.115   -20.930 -0.302  1.00 42.88  ?  94  PHE A CB    1 
ATOM   1048 C  CG    . PHE A 1 145 ? 1.682   -21.179 -0.005  1.00 46.77  ?  94  PHE A CG    1 
ATOM   1049 C  CD1   . PHE A 1 145 ? 0.756   -20.150 -0.109  1.00 45.18  ?  94  PHE A CD1   1 
ATOM   1050 C  CD2   . PHE A 1 145 ? 1.258   -22.422 0.429   1.00 47.77  ?  94  PHE A CD2   1 
ATOM   1051 C  CE1   . PHE A 1 145 ? -0.584  -20.366 0.188   1.00 46.42  ?  94  PHE A CE1   1 
ATOM   1052 C  CE2   . PHE A 1 145 ? -0.070  -22.641 0.726   1.00 49.72  ?  94  PHE A CE2   1 
ATOM   1053 C  CZ    . PHE A 1 145 ? -0.993  -21.614 0.609   1.00 46.94  ?  94  PHE A CZ    1 
ATOM   1054 N  N     . LEU A 1 146 ? 4.209   -21.406 2.707   1.00 49.45  ?  95  LEU A N     1 
ATOM   1055 C  CA    . LEU A 1 146 ? 3.915   -21.818 4.066   1.00 51.15  ?  95  LEU A CA    1 
ATOM   1056 C  C     . LEU A 1 146 ? 4.138   -20.700 5.070   1.00 51.25  ?  95  LEU A C     1 
ATOM   1057 O  O     . LEU A 1 146 ? 3.543   -20.740 6.149   1.00 54.50  ?  95  LEU A O     1 
ATOM   1058 C  CB    . LEU A 1 146 ? 4.762   -23.033 4.427   1.00 49.80  ?  95  LEU A CB    1 
ATOM   1059 C  CG    . LEU A 1 146 ? 4.396   -24.252 3.592   1.00 50.30  ?  95  LEU A CG    1 
ATOM   1060 C  CD1   . LEU A 1 146 ? 5.277   -25.411 3.978   1.00 44.13  ?  95  LEU A CD1   1 
ATOM   1061 C  CD2   . LEU A 1 146 ? 2.916   -24.578 3.768   1.00 45.48  ?  95  LEU A CD2   1 
ATOM   1062 N  N     . ASN A 1 147 ? 4.984   -19.717 4.754   1.00 52.72  ?  96  ASN A N     1 
ATOM   1063 C  CA    . ASN A 1 147 ? 5.256   -18.637 5.696   1.00 48.05  ?  96  ASN A CA    1 
ATOM   1064 C  C     . ASN A 1 147 ? 4.188   -17.566 5.671   1.00 47.53  ?  96  ASN A C     1 
ATOM   1065 O  O     . ASN A 1 147 ? 4.237   -16.642 6.487   1.00 45.48  ?  96  ASN A O     1 
ATOM   1066 C  CB    . ASN A 1 147 ? 6.599   -17.988 5.397   1.00 45.16  ?  96  ASN A CB    1 
ATOM   1067 C  CG    . ASN A 1 147 ? 7.746   -18.893 5.691   1.00 47.93  ?  96  ASN A CG    1 
ATOM   1068 O  OD1   . ASN A 1 147 ? 7.674   -19.693 6.602   1.00 55.83  ?  96  ASN A OD1   1 
ATOM   1069 N  ND2   . ASN A 1 147 ? 8.824   -18.766 4.938   1.00 51.88  ?  96  ASN A ND2   1 
ATOM   1070 N  N     . VAL A 1 148 ? 3.244   -17.661 4.738   1.00 51.72  ?  97  VAL A N     1 
ATOM   1071 C  CA    . VAL A 1 148 ? 2.212   -16.641 4.600   1.00 49.03  ?  97  VAL A CA    1 
ATOM   1072 C  C     . VAL A 1 148 ? 1.413   -16.506 5.883   1.00 45.28  ?  97  VAL A C     1 
ATOM   1073 O  O     . VAL A 1 148 ? 0.931   -15.414 6.212   1.00 47.08  ?  97  VAL A O     1 
ATOM   1074 C  CB    . VAL A 1 148 ? 1.322   -16.986 3.393   1.00 45.66  ?  97  VAL A CB    1 
ATOM   1075 C  CG1   . VAL A 1 148 ? 0.065   -16.123 3.384   1.00 47.80  ?  97  VAL A CG1   1 
ATOM   1076 C  CG2   . VAL A 1 148 ? 2.116   -16.798 2.100   1.00 48.36  ?  97  VAL A CG2   1 
ATOM   1077 N  N     . ARG A 1 149 ? 1.269   -17.602 6.636   1.00 49.60  ?  98  ARG A N     1 
ATOM   1078 C  CA    . ARG A 1 149 ? 0.510   -17.560 7.888   1.00 49.45  ?  98  ARG A CA    1 
ATOM   1079 C  C     . ARG A 1 149 ? 1.196   -16.656 8.904   1.00 46.10  ?  98  ARG A C     1 
ATOM   1080 O  O     . ARG A 1 149 ? 0.562   -15.783 9.509   1.00 44.68  ?  98  ARG A O     1 
ATOM   1081 C  CB    . ARG A 1 149 ? 0.333   -18.977 8.450   1.00 39.49  ?  98  ARG A CB    1 
ATOM   1082 N  N     . ASN A 1 150 ? 2.504   -16.839 9.087   1.00 45.55  ?  99  ASN A N     1 
ATOM   1083 C  CA    . ASN A 1 150 ? 3.254   -15.967 9.977   1.00 44.10  ?  99  ASN A CA    1 
ATOM   1084 C  C     . ASN A 1 150 ? 3.113   -14.509 9.565   1.00 48.10  ?  99  ASN A C     1 
ATOM   1085 O  O     . ASN A 1 150 ? 2.850   -13.645 10.410  1.00 54.16  ?  99  ASN A O     1 
ATOM   1086 C  CB    . ASN A 1 150 ? 4.724   -16.387 9.996   1.00 53.98  ?  99  ASN A CB    1 
ATOM   1087 C  CG    . ASN A 1 150 ? 4.923   -17.812 10.509  1.00 64.07  ?  99  ASN A CG    1 
ATOM   1088 O  OD1   . ASN A 1 150 ? 4.197   -18.283 11.402  1.00 63.87  ?  99  ASN A OD1   1 
ATOM   1089 N  ND2   . ASN A 1 150 ? 5.913   -18.509 9.944   1.00 66.77  ?  99  ASN A ND2   1 
ATOM   1090 N  N     . TRP A 1 151 ? 3.280   -14.222 8.263   1.00 47.76  ?  100 TRP A N     1 
ATOM   1091 C  CA    . TRP A 1 151 ? 3.221   -12.851 7.754   1.00 41.93  ?  100 TRP A CA    1 
ATOM   1092 C  C     . TRP A 1 151 ? 1.901   -12.196 8.110   1.00 43.90  ?  100 TRP A C     1 
ATOM   1093 O  O     . TRP A 1 151 ? 1.866   -11.036 8.537   1.00 48.02  ?  100 TRP A O     1 
ATOM   1094 C  CB    . TRP A 1 151 ? 3.406   -12.820 6.225   1.00 42.48  ?  100 TRP A CB    1 
ATOM   1095 C  CG    . TRP A 1 151 ? 4.813   -12.969 5.754   1.00 39.79  ?  100 TRP A CG    1 
ATOM   1096 C  CD1   . TRP A 1 151 ? 5.338   -14.015 5.056   1.00 40.63  ?  100 TRP A CD1   1 
ATOM   1097 C  CD2   . TRP A 1 151 ? 5.879   -12.035 5.938   1.00 38.48  ?  100 TRP A CD2   1 
ATOM   1098 N  NE1   . TRP A 1 151 ? 6.673   -13.801 4.814   1.00 39.09  ?  100 TRP A NE1   1 
ATOM   1099 C  CE2   . TRP A 1 151 ? 7.029   -12.593 5.355   1.00 39.01  ?  100 TRP A CE2   1 
ATOM   1100 C  CE3   . TRP A 1 151 ? 5.977   -10.791 6.562   1.00 41.00  ?  100 TRP A CE3   1 
ATOM   1101 C  CZ2   . TRP A 1 151 ? 8.258   -11.942 5.358   1.00 41.04  ?  100 TRP A CZ2   1 
ATOM   1102 C  CZ3   . TRP A 1 151 ? 7.201   -10.148 6.560   1.00 43.28  ?  100 TRP A CZ3   1 
ATOM   1103 C  CH2   . TRP A 1 151 ? 8.319   -10.721 5.951   1.00 38.16  ?  100 TRP A CH2   1 
ATOM   1104 N  N     . ILE A 1 152 ? 0.789   -12.894 7.874   1.00 44.24  ?  101 ILE A N     1 
ATOM   1105 C  CA    . ILE A 1 152 ? -0.500  -12.327 8.255   1.00 46.16  ?  101 ILE A CA    1 
ATOM   1106 C  C     . ILE A 1 152 ? -0.527  -12.075 9.757   1.00 50.18  ?  101 ILE A C     1 
ATOM   1107 O  O     . ILE A 1 152 ? -0.958  -11.014 10.223  1.00 50.15  ?  101 ILE A O     1 
ATOM   1108 C  CB    . ILE A 1 152 ? -1.639  -13.262 7.823   1.00 46.63  ?  101 ILE A CB    1 
ATOM   1109 C  CG1   . ILE A 1 152 ? -1.662  -13.395 6.305   1.00 49.38  ?  101 ILE A CG1   1 
ATOM   1110 C  CG2   . ILE A 1 152 ? -2.975  -12.753 8.353   1.00 48.69  ?  101 ILE A CG2   1 
ATOM   1111 C  CD1   . ILE A 1 152 ? -2.503  -14.539 5.804   1.00 48.62  ?  101 ILE A CD1   1 
ATOM   1112 N  N     . SER A 1 153 ? -0.049  -13.045 10.534  1.00 50.13  ?  102 SER A N     1 
ATOM   1113 C  CA    . SER A 1 153 ? -0.009  -12.886 11.978  1.00 49.73  ?  102 SER A CA    1 
ATOM   1114 C  C     . SER A 1 153 ? 0.795   -11.648 12.360  1.00 53.55  ?  102 SER A C     1 
ATOM   1115 O  O     . SER A 1 153 ? 0.341   -10.819 13.157  1.00 53.73  ?  102 SER A O     1 
ATOM   1116 C  CB    . SER A 1 153 ? 0.575   -14.138 12.598  1.00 46.23  ?  102 SER A CB    1 
ATOM   1117 O  OG    . SER A 1 153 ? 1.275   -13.779 13.768  1.00 60.97  ?  102 SER A OG    1 
ATOM   1118 N  N     . GLN A 1 154 ? 1.977   -11.484 11.759  1.00 51.22  ?  103 GLN A N     1 
ATOM   1119 C  CA    . GLN A 1 154 ? 2.750   -10.257 11.928  1.00 48.53  ?  103 GLN A CA    1 
ATOM   1120 C  C     . GLN A 1 154 ? 1.937   -9.015  11.577  1.00 52.57  ?  103 GLN A C     1 
ATOM   1121 O  O     . GLN A 1 154 ? 1.971   -8.012  12.297  1.00 54.75  ?  103 GLN A O     1 
ATOM   1122 C  CB    . GLN A 1 154 ? 4.001   -10.322 11.066  1.00 46.88  ?  103 GLN A CB    1 
ATOM   1123 C  CG    . GLN A 1 154 ? 5.030   -11.241 11.613  1.00 55.30  ?  103 GLN A CG    1 
ATOM   1124 C  CD    . GLN A 1 154 ? 6.112   -10.490 12.356  1.00 67.80  ?  103 GLN A CD    1 
ATOM   1125 O  OE1   . GLN A 1 154 ? 6.082   -10.370 13.604  1.00 58.51  ?  103 GLN A OE1   1 
ATOM   1126 N  NE2   . GLN A 1 154 ? 7.091   -9.970  11.589  1.00 64.32  ?  103 GLN A NE2   1 
ATOM   1127 N  N     . LEU A 1 155 ? 1.215   -9.053  10.456  1.00 52.05  ?  104 LEU A N     1 
ATOM   1128 C  CA    . LEU A 1 155 ? 0.464   -7.876  10.027  1.00 53.55  ?  104 LEU A CA    1 
ATOM   1129 C  C     . LEU A 1 155 ? -0.631  -7.531  11.027  1.00 53.93  ?  104 LEU A C     1 
ATOM   1130 O  O     . LEU A 1 155 ? -0.832  -6.358  11.356  1.00 55.38  ?  104 LEU A O     1 
ATOM   1131 C  CB    . LEU A 1 155 ? -0.129  -8.103  8.632   1.00 52.69  ?  104 LEU A CB    1 
ATOM   1132 C  CG    . LEU A 1 155 ? 0.884   -7.960  7.509   1.00 52.00  ?  104 LEU A CG    1 
ATOM   1133 C  CD1   . LEU A 1 155 ? 0.258   -8.242  6.150   1.00 49.13  ?  104 LEU A CD1   1 
ATOM   1134 C  CD2   . LEU A 1 155 ? 1.418   -6.553  7.588   1.00 49.57  ?  104 LEU A CD2   1 
ATOM   1135 N  N     . GLN A 1 156 ? -1.372  -8.537  11.491  1.00 52.43  ?  105 GLN A N     1 
ATOM   1136 C  CA    . GLN A 1 156 ? -2.333  -8.332  12.573  1.00 61.06  ?  105 GLN A CA    1 
ATOM   1137 C  C     . GLN A 1 156 ? -1.716  -7.566  13.745  1.00 58.61  ?  105 GLN A C     1 
ATOM   1138 O  O     . GLN A 1 156 ? -2.303  -6.606  14.260  1.00 59.46  ?  105 GLN A O     1 
ATOM   1139 C  CB    . GLN A 1 156 ? -2.858  -9.690  13.048  1.00 59.05  ?  105 GLN A CB    1 
ATOM   1140 C  CG    . GLN A 1 156 ? -3.473  -10.522 11.958  1.00 59.01  ?  105 GLN A CG    1 
ATOM   1141 C  CD    . GLN A 1 156 ? -4.781  -9.943  11.484  1.00 63.45  ?  105 GLN A CD    1 
ATOM   1142 O  OE1   . GLN A 1 156 ? -5.223  -8.894  11.969  1.00 64.67  ?  105 GLN A OE1   1 
ATOM   1143 N  NE2   . GLN A 1 156 ? -5.423  -10.625 10.538  1.00 64.61  ?  105 GLN A NE2   1 
ATOM   1144 N  N     . MET A 1 157 ? -0.512  -7.969  14.158  1.00 58.58  ?  106 MET A N     1 
ATOM   1145 C  CA    . MET A 1 157 ? 0.111   -7.409  15.354  1.00 56.50  ?  106 MET A CA    1 
ATOM   1146 C  C     . MET A 1 157 ? 0.650   -5.998  15.124  1.00 57.87  ?  106 MET A C     1 
ATOM   1147 O  O     . MET A 1 157 ? 0.552   -5.145  16.011  1.00 59.18  ?  106 MET A O     1 
ATOM   1148 C  CB    . MET A 1 157 ? 1.228   -8.339  15.828  1.00 58.37  ?  106 MET A CB    1 
ATOM   1149 C  CG    . MET A 1 157 ? 1.943   -7.870  17.083  1.00 62.03  ?  106 MET A CG    1 
ATOM   1150 S  SD    . MET A 1 157 ? 3.298   -8.954  17.591  1.00 66.12  ?  106 MET A SD    1 
ATOM   1151 C  CE    . MET A 1 157 ? 2.573   -10.579 17.313  1.00 66.23  ?  106 MET A CE    1 
ATOM   1152 N  N     . HIS A 1 158 ? 1.223   -5.718  13.950  1.00 59.60  ?  107 HIS A N     1 
ATOM   1153 C  CA    . HIS A 1 158 ? 1.915   -4.448  13.740  1.00 53.95  ?  107 HIS A CA    1 
ATOM   1154 C  C     . HIS A 1 158 ? 1.183   -3.465  12.847  1.00 55.25  ?  107 HIS A C     1 
ATOM   1155 O  O     . HIS A 1 158 ? 1.592   -2.307  12.778  1.00 58.84  ?  107 HIS A O     1 
ATOM   1156 C  CB    . HIS A 1 158 ? 3.306   -4.682  13.156  1.00 52.39  ?  107 HIS A CB    1 
ATOM   1157 C  CG    . HIS A 1 158 ? 4.240   -5.363  14.098  1.00 56.65  ?  107 HIS A CG    1 
ATOM   1158 N  ND1   . HIS A 1 158 ? 5.050   -4.668  14.969  1.00 59.43  ?  107 HIS A ND1   1 
ATOM   1159 C  CD2   . HIS A 1 158 ? 4.491   -6.676  14.312  1.00 56.68  ?  107 HIS A CD2   1 
ATOM   1160 C  CE1   . HIS A 1 158 ? 5.759   -5.526  15.684  1.00 56.40  ?  107 HIS A CE1   1 
ATOM   1161 N  NE2   . HIS A 1 158 ? 5.437   -6.750  15.305  1.00 58.04  ?  107 HIS A NE2   1 
ATOM   1162 N  N     . ALA A 1 159 ? 0.137   -3.877  12.151  1.00 56.99  ?  108 ALA A N     1 
ATOM   1163 C  CA    . ALA A 1 159 ? -0.643  -2.902  11.415  1.00 58.07  ?  108 ALA A CA    1 
ATOM   1164 C  C     . ALA A 1 159 ? -1.241  -1.917  12.399  1.00 59.10  ?  108 ALA A C     1 
ATOM   1165 O  O     . ALA A 1 159 ? -1.578  -2.277  13.525  1.00 61.68  ?  108 ALA A O     1 
ATOM   1166 C  CB    . ALA A 1 159 ? -1.748  -3.582  10.606  1.00 59.72  ?  108 ALA A CB    1 
ATOM   1167 N  N     . TYR A 1 160 ? -1.370  -0.671  11.970  1.00 63.78  ?  109 TYR A N     1 
ATOM   1168 C  CA    . TYR A 1 160 ? -1.863  0.374   12.849  1.00 63.18  ?  109 TYR A CA    1 
ATOM   1169 C  C     . TYR A 1 160 ? -3.336  0.648   12.568  1.00 63.82  ?  109 TYR A C     1 
ATOM   1170 O  O     . TYR A 1 160 ? -4.019  1.282   13.374  1.00 65.37  ?  109 TYR A O     1 
ATOM   1171 C  CB    . TYR A 1 160 ? -1.028  1.655   12.690  1.00 66.74  ?  109 TYR A CB    1 
ATOM   1172 C  CG    . TYR A 1 160 ? 0.365   1.589   13.311  1.00 67.83  ?  109 TYR A CG    1 
ATOM   1173 C  CD1   . TYR A 1 160 ? 1.275   0.591   12.949  1.00 65.30  ?  109 TYR A CD1   1 
ATOM   1174 C  CD2   . TYR A 1 160 ? 0.764   2.519   14.265  1.00 64.22  ?  109 TYR A CD2   1 
ATOM   1175 C  CE1   . TYR A 1 160 ? 2.548   0.524   13.522  1.00 67.88  ?  109 TYR A CE1   1 
ATOM   1176 C  CE2   . TYR A 1 160 ? 2.030   2.462   14.843  1.00 67.05  ?  109 TYR A CE2   1 
ATOM   1177 C  CZ    . TYR A 1 160 ? 2.919   1.462   14.480  1.00 70.15  ?  109 TYR A CZ    1 
ATOM   1178 O  OH    . TYR A 1 160 ? 4.179   1.421   15.069  1.00 68.01  ?  109 TYR A OH    1 
ATOM   1179 N  N     . CYS A 1 161 ? -4.554  -0.073  12.364  1.00 62.33  ?  110 CYS A N     1 
ATOM   1180 C  CA    . CYS A 1 161 ? -5.673  -0.812  11.843  1.00 67.06  ?  110 CYS A CA    1 
ATOM   1181 C  C     . CYS A 1 161 ? -5.337  -2.302  11.960  1.00 65.43  ?  110 CYS A C     1 
ATOM   1182 O  O     . CYS A 1 161 ? -4.300  -2.624  12.659  0.76 64.10  -1 110 CYS A O     1 
ATOM   1183 C  CB    . CYS A 1 161 ? -5.966  -0.446  10.357  1.00 61.01  ?  110 CYS A CB    1 
ATOM   1184 S  SG    . CYS A 1 161 ? -6.864  1.167   10.314  0.69 65.51  ?  110 CYS A SG    1 
ATOM   1185 N  N     . GLU A 1 162 ? -6.406  -2.338  12.908  1.00 64.80  ?  111 GLU A N     1 
ATOM   1186 C  CA    . GLU A 1 162 ? -7.292  -3.459  13.187  1.00 67.04  ?  111 GLU A CA    1 
ATOM   1187 C  C     . GLU A 1 162 ? -7.940  -4.010  11.925  1.00 62.45  ?  111 GLU A C     1 
ATOM   1188 O  O     . GLU A 1 162 ? -8.683  -3.306  11.267  1.00 62.94  ?  111 GLU A O     1 
ATOM   1189 C  CB    . GLU A 1 162 ? -8.373  -3.041  14.186  1.00 30.00  ?  111 GLU A CB    1 
ATOM   1190 C  CG    . GLU A 1 162 ? -7.845  -2.717  15.574  1.00 30.00  ?  111 GLU A CG    1 
ATOM   1191 C  CD    . GLU A 1 162 ? -8.935  -2.238  16.514  1.00 30.00  ?  111 GLU A CD    1 
ATOM   1192 O  OE1   . GLU A 1 162 ? -10.059 -1.977  16.038  1.00 30.00  ?  111 GLU A OE1   1 
ATOM   1193 O  OE2   . GLU A 1 162 ? -8.666  -2.120  17.728  1.00 30.00  ?  111 GLU A OE2   1 
ATOM   1194 N  N     . ASN A 1 163 ? -7.670  -5.283  11.613  1.00 67.18  ?  112 ASN A N     1 
ATOM   1195 C  CA    . ASN A 1 163 ? -8.170  -5.978  10.421  1.00 65.64  ?  112 ASN A CA    1 
ATOM   1196 C  C     . ASN A 1 163 ? -7.679  -5.342  9.125   1.00 63.70  ?  112 ASN A C     1 
ATOM   1197 O  O     . ASN A 1 163 ? -8.493  -4.979  8.263   1.00 66.01  ?  112 ASN A O     1 
ATOM   1198 C  CB    . ASN A 1 163 ? -9.696  -6.015  10.421  1.00 65.41  ?  112 ASN A CB    1 
ATOM   1199 C  CG    . ASN A 1 163 ? -10.226 -7.269  11.038  1.00 72.78  ?  112 ASN A CG    1 
ATOM   1200 O  OD1   . ASN A 1 163 ? -10.469 -7.321  12.244  1.00 73.73  ?  112 ASN A OD1   1 
ATOM   1201 N  ND2   . ASN A 1 163 ? -10.394 -8.306  10.222  1.00 73.97  ?  112 ASN A ND2   1 
ATOM   1202 N  N     . PRO A 1 164 ? -6.371  -5.218  8.930   1.00 60.76  ?  113 PRO A N     1 
ATOM   1203 C  CA    . PRO A 1 164 ? -5.875  -4.438  7.791   1.00 57.12  ?  113 PRO A CA    1 
ATOM   1204 C  C     . PRO A 1 164 ? -6.228  -5.095  6.472   1.00 56.04  ?  113 PRO A C     1 
ATOM   1205 O  O     . PRO A 1 164 ? -6.224  -6.321  6.355   1.00 58.15  ?  113 PRO A O     1 
ATOM   1206 C  CB    . PRO A 1 164 ? -4.360  -4.411  8.013   1.00 60.11  ?  113 PRO A CB    1 
ATOM   1207 C  CG    . PRO A 1 164 ? -4.079  -5.617  8.855   1.00 61.06  ?  113 PRO A CG    1 
ATOM   1208 C  CD    . PRO A 1 164 ? -5.281  -5.830  9.711   1.00 58.80  ?  113 PRO A CD    1 
ATOM   1209 N  N     . ASP A 1 165 ? -6.538  -4.266  5.472   1.00 59.10  ?  114 ASP A N     1 
ATOM   1210 C  CA    . ASP A 1 165 ? -6.784  -4.792  4.132   1.00 57.22  ?  114 ASP A CA    1 
ATOM   1211 C  C     . ASP A 1 165 ? -5.510  -5.397  3.571   1.00 52.05  ?  114 ASP A C     1 
ATOM   1212 O  O     . ASP A 1 165 ? -4.446  -4.769  3.599   1.00 51.12  ?  114 ASP A O     1 
ATOM   1213 C  CB    . ASP A 1 165 ? -7.290  -3.702  3.190   1.00 49.56  ?  114 ASP A CB    1 
ATOM   1214 C  CG    . ASP A 1 165 ? -8.518  -3.007  3.716   1.00 58.46  ?  114 ASP A CG    1 
ATOM   1215 O  OD1   . ASP A 1 165 ? -8.439  -1.777  3.957   1.00 64.84  ?  114 ASP A OD1   1 
ATOM   1216 O  OD2   . ASP A 1 165 ? -9.556  -3.683  3.899   1.00 58.78  ?  114 ASP A OD2   1 
ATOM   1217 N  N     . ILE A 1 166 ? -5.629  -6.624  3.067   1.00 52.71  ?  115 ILE A N     1 
ATOM   1218 C  CA    . ILE A 1 166 ? -4.530  -7.366  2.467   1.00 50.87  ?  115 ILE A CA    1 
ATOM   1219 C  C     . ILE A 1 166 ? -5.021  -7.914  1.139   1.00 50.60  ?  115 ILE A C     1 
ATOM   1220 O  O     . ILE A 1 166 ? -6.185  -8.314  1.025   1.00 51.81  ?  115 ILE A O     1 
ATOM   1221 C  CB    . ILE A 1 166 ? -4.052  -8.519  3.378   1.00 51.15  ?  115 ILE A CB    1 
ATOM   1222 C  CG1   . ILE A 1 166 ? -3.789  -8.010  4.801   1.00 55.16  ?  115 ILE A CG1   1 
ATOM   1223 C  CG2   . ILE A 1 166 ? -2.809  -9.208  2.804   1.00 46.98  ?  115 ILE A CG2   1 
ATOM   1224 C  CD1   . ILE A 1 166 ? -3.667  -9.124  5.835   1.00 48.28  ?  115 ILE A CD1   1 
ATOM   1225 N  N     . VAL A 1 167 ? -4.150  -7.899  0.128   1.00 48.03  ?  116 VAL A N     1 
ATOM   1226 C  CA    . VAL A 1 167 ? -4.352  -8.662  -1.099  1.00 47.06  ?  116 VAL A CA    1 
ATOM   1227 C  C     . VAL A 1 167 ? -3.195  -9.640  -1.213  1.00 46.08  ?  116 VAL A C     1 
ATOM   1228 O  O     . VAL A 1 167 ? -2.021  -9.245  -1.144  1.00 45.75  ?  116 VAL A O     1 
ATOM   1229 C  CB    . VAL A 1 167 ? -4.454  -7.773  -2.350  1.00 47.76  ?  116 VAL A CB    1 
ATOM   1230 C  CG1   . VAL A 1 167 ? -4.237  -8.602  -3.613  1.00 44.75  ?  116 VAL A CG1   1 
ATOM   1231 C  CG2   . VAL A 1 167 ? -5.831  -7.107  -2.417  1.00 44.61  ?  116 VAL A CG2   1 
ATOM   1232 N  N     . LEU A 1 168 ? -3.528  -10.916 -1.341  1.00 42.55  ?  117 LEU A N     1 
ATOM   1233 C  CA    . LEU A 1 168 ? -2.531  -11.962 -1.468  1.00 46.44  ?  117 LEU A CA    1 
ATOM   1234 C  C     . LEU A 1 168 ? -2.142  -12.152 -2.930  1.00 50.20  ?  117 LEU A C     1 
ATOM   1235 O  O     . LEU A 1 168 ? -3.007  -12.217 -3.816  1.00 46.56  ?  117 LEU A O     1 
ATOM   1236 C  CB    . LEU A 1 168 ? -3.081  -13.260 -0.887  1.00 46.71  ?  117 LEU A CB    1 
ATOM   1237 C  CG    . LEU A 1 168 ? -2.088  -14.409 -0.752  1.00 50.44  ?  117 LEU A CG    1 
ATOM   1238 C  CD1   . LEU A 1 168 ? -1.011  -14.115 0.305   1.00 46.21  ?  117 LEU A CD1   1 
ATOM   1239 C  CD2   . LEU A 1 168 ? -2.842  -15.692 -0.430  1.00 47.54  ?  117 LEU A CD2   1 
ATOM   1240 N  N     . CYS A 1 169 ? -0.837  -12.256 -3.180  1.00 46.90  ?  118 CYS A N     1 
ATOM   1241 C  CA    . CYS A 1 169 ? -0.319  -12.388 -4.541  1.00 44.24  ?  118 CYS A CA    1 
ATOM   1242 C  C     . CYS A 1 169 ? 0.566   -13.617 -4.618  1.00 46.23  ?  118 CYS A C     1 
ATOM   1243 O  O     . CYS A 1 169 ? 1.624   -13.655 -3.980  1.00 47.65  ?  118 CYS A O     1 
ATOM   1244 C  CB    . CYS A 1 169 ? 0.494   -11.169 -4.941  1.00 42.66  ?  118 CYS A CB    1 
ATOM   1245 S  SG    . CYS A 1 169 ? -0.496  -9.763  -5.334  1.00 49.23  ?  118 CYS A SG    1 
ATOM   1246 N  N     . GLY A 1 170 ? 0.165   -14.600 -5.422  1.00 45.45  ?  119 GLY A N     1 
ATOM   1247 C  CA    . GLY A 1 170 ? 1.061   -15.690 -5.758  1.00 44.52  ?  119 GLY A CA    1 
ATOM   1248 C  C     . GLY A 1 170 ? 1.767   -15.379 -7.058  1.00 46.40  ?  119 GLY A C     1 
ATOM   1249 O  O     . GLY A 1 170 ? 1.156   -15.444 -8.120  1.00 49.01  ?  119 GLY A O     1 
ATOM   1250 N  N     . ASN A 1 171 ? 3.046   -15.045 -6.984  1.00 44.66  ?  120 ASN A N     1 
ATOM   1251 C  CA    . ASN A 1 171 ? 3.770   -14.456 -8.090  1.00 45.53  ?  120 ASN A CA    1 
ATOM   1252 C  C     . ASN A 1 171 ? 4.502   -15.530 -8.904  1.00 47.26  ?  120 ASN A C     1 
ATOM   1253 O  O     . ASN A 1 171 ? 4.587   -16.693 -8.518  1.00 48.11  ?  120 ASN A O     1 
ATOM   1254 C  CB    . ASN A 1 171 ? 4.746   -13.407 -7.555  1.00 45.05  ?  120 ASN A CB    1 
ATOM   1255 C  CG    . ASN A 1 171 ? 5.225   -12.477 -8.632  1.00 43.66  ?  120 ASN A CG    1 
ATOM   1256 O  OD1   . ASN A 1 171 ? 4.425   -11.910 -9.371  1.00 43.46  ?  120 ASN A OD1   1 
ATOM   1257 N  ND2   . ASN A 1 171 ? 6.537   -12.342 -8.759  1.00 42.76  ?  120 ASN A ND2   1 
ATOM   1258 N  N     . LYS A 1 172 ? 5.032   -15.117 -10.059 1.00 47.49  ?  121 LYS A N     1 
ATOM   1259 C  CA    . LYS A 1 172 ? 5.773   -15.984 -10.991 1.00 44.28  ?  121 LYS A CA    1 
ATOM   1260 C  C     . LYS A 1 172 ? 4.863   -17.019 -11.656 1.00 46.71  ?  121 LYS A C     1 
ATOM   1261 O  O     . LYS A 1 172 ? 5.274   -18.155 -11.916 1.00 44.34  ?  121 LYS A O     1 
ATOM   1262 C  CB    . LYS A 1 172 ? 6.977   -16.658 -10.321 1.00 42.46  ?  121 LYS A CB    1 
ATOM   1263 C  CG    . LYS A 1 172 ? 7.744   -15.724 -9.411  1.00 43.52  ?  121 LYS A CG    1 
ATOM   1264 C  CD    . LYS A 1 172 ? 9.197   -16.132 -9.269  1.00 41.76  ?  121 LYS A CD    1 
ATOM   1265 C  CE    . LYS A 1 172 ? 9.822   -15.321 -8.163  1.00 42.03  ?  121 LYS A CE    1 
ATOM   1266 N  NZ    . LYS A 1 172 ? 11.233  -15.682 -7.903  1.00 43.24  ?  121 LYS A NZ    1 
ATOM   1267 N  N     . SER A 1 173 ? 3.631   -16.611 -11.986 1.00 46.43  ?  122 SER A N     1 
ATOM   1268 C  CA    . SER A 1 173 ? 2.722   -17.514 -12.678 1.00 46.65  ?  122 SER A CA    1 
ATOM   1269 C  C     . SER A 1 173 ? 3.184   -17.833 -14.096 1.00 52.75  ?  122 SER A C     1 
ATOM   1270 O  O     . SER A 1 173 ? 2.669   -18.775 -14.709 1.00 52.55  ?  122 SER A O     1 
ATOM   1271 C  CB    . SER A 1 173 ? 1.316   -16.918 -12.694 1.00 47.30  ?  122 SER A CB    1 
ATOM   1272 O  OG    . SER A 1 173 ? 1.238   -15.734 -13.479 1.00 48.52  ?  122 SER A OG    1 
ATOM   1273 N  N     . ASP A 1 174 ? 4.158   -17.095 -14.619 1.00 51.07  ?  123 ASP A N     1 
ATOM   1274 C  CA    . ASP A 1 174 ? 4.691   -17.373 -15.943 1.00 50.57  ?  123 ASP A CA    1 
ATOM   1275 C  C     . ASP A 1 174 ? 5.655   -18.554 -15.958 1.00 53.06  ?  123 ASP A C     1 
ATOM   1276 O  O     . ASP A 1 174 ? 5.959   -19.071 -17.035 1.00 54.46  ?  123 ASP A O     1 
ATOM   1277 C  CB    . ASP A 1 174 ? 5.398   -16.128 -16.470 1.00 48.90  ?  123 ASP A CB    1 
ATOM   1278 C  CG    . ASP A 1 174 ? 6.569   -15.716 -15.599 1.00 50.25  ?  123 ASP A CG    1 
ATOM   1279 O  OD1   . ASP A 1 174 ? 6.345   -15.135 -14.508 1.00 48.15  ?  123 ASP A OD1   1 
ATOM   1280 O  OD2   . ASP A 1 174 ? 7.720   -15.992 -16.002 1.00 50.42  ?  123 ASP A OD2   1 
ATOM   1281 N  N     . LEU A 1 175 ? 6.170   -18.972 -14.803 1.00 51.55  ?  124 LEU A N     1 
ATOM   1282 C  CA    . LEU A 1 175 ? 7.031   -20.152 -14.728 1.00 53.13  ?  124 LEU A CA    1 
ATOM   1283 C  C     . LEU A 1 175 ? 6.161   -21.377 -14.435 1.00 53.73  ?  124 LEU A C     1 
ATOM   1284 O  O     . LEU A 1 175 ? 6.148   -21.923 -13.337 1.00 54.98  ?  124 LEU A O     1 
ATOM   1285 C  CB    . LEU A 1 175 ? 8.112   -19.961 -13.667 1.00 51.15  ?  124 LEU A CB    1 
ATOM   1286 C  CG    . LEU A 1 175 ? 9.073   -18.763 -13.759 1.00 52.15  ?  124 LEU A CG    1 
ATOM   1287 C  CD1   . LEU A 1 175 ? 10.103  -18.751 -12.627 1.00 45.96  ?  124 LEU A CD1   1 
ATOM   1288 C  CD2   . LEU A 1 175 ? 9.773   -18.681 -15.104 1.00 49.77  ?  124 LEU A CD2   1 
ATOM   1289 N  N     . GLU A 1 176 ? 5.402   -21.803 -15.447 1.00 56.15  ?  125 GLU A N     1 
ATOM   1290 C  CA    . GLU A 1 176 ? 4.432   -22.869 -15.202 1.00 55.65  ?  125 GLU A CA    1 
ATOM   1291 C  C     . GLU A 1 176 ? 5.115   -24.220 -15.030 1.00 56.09  ?  125 GLU A C     1 
ATOM   1292 O  O     . GLU A 1 176 ? 4.609   -25.087 -14.311 1.00 53.92  ?  125 GLU A O     1 
ATOM   1293 C  CB    . GLU A 1 176 ? 3.394   -22.920 -16.329 1.00 52.36  ?  125 GLU A CB    1 
ATOM   1294 N  N     . ASP A 1 177 ? 6.262   -24.419 -15.669 1.00 61.16  ?  126 ASP A N     1 
ATOM   1295 C  CA    . ASP A 1 177 ? 6.979   -25.672 -15.489 1.00 61.19  ?  126 ASP A CA    1 
ATOM   1296 C  C     . ASP A 1 177 ? 7.529   -25.813 -14.088 1.00 58.60  ?  126 ASP A C     1 
ATOM   1297 O  O     . ASP A 1 177 ? 7.794   -26.935 -13.653 1.00 63.43  ?  126 ASP A O     1 
ATOM   1298 C  CB    . ASP A 1 177 ? 8.130   -25.779 -16.495 1.00 68.23  ?  126 ASP A CB    1 
ATOM   1299 C  CG    . ASP A 1 177 ? 7.645   -25.878 -17.923 1.00 73.60  ?  126 ASP A CG    1 
ATOM   1300 O  OD1   . ASP A 1 177 ? 6.556   -26.453 -18.129 1.00 77.04  ?  126 ASP A OD1   1 
ATOM   1301 O  OD2   . ASP A 1 177 ? 8.336   -25.366 -18.837 1.00 79.50  ?  126 ASP A OD2   1 
ATOM   1302 N  N     . GLN A 1 178 ? 7.724   -24.700 -13.383 1.00 57.78  ?  127 GLN A N     1 
ATOM   1303 C  CA    . GLN A 1 178 ? 8.360   -24.693 -12.076 1.00 53.58  ?  127 GLN A CA    1 
ATOM   1304 C  C     . GLN A 1 178 ? 7.376   -24.451 -10.954 1.00 51.56  ?  127 GLN A C     1 
ATOM   1305 O  O     . GLN A 1 178 ? 7.794   -24.256 -9.811  1.00 53.11  ?  127 GLN A O     1 
ATOM   1306 C  CB    . GLN A 1 178 ? 9.468   -23.643 -12.037 1.00 56.83  ?  127 GLN A CB    1 
ATOM   1307 C  CG    . GLN A 1 178 ? 10.556  -23.898 -13.076 1.00 61.20  ?  127 GLN A CG    1 
ATOM   1308 C  CD    . GLN A 1 178 ? 10.735  -22.741 -14.031 1.00 63.81  ?  127 GLN A CD    1 
ATOM   1309 O  OE1   . GLN A 1 178 ? 11.321  -21.722 -13.660 1.00 65.05  ?  127 GLN A OE1   1 
ATOM   1310 N  NE2   . GLN A 1 178 ? 10.226  -22.883 -15.272 1.00 61.93  ?  127 GLN A NE2   1 
ATOM   1311 N  N     . ARG A 1 179 ? 6.080   -24.475 -11.248 1.00 52.87  ?  128 ARG A N     1 
ATOM   1312 C  CA    . ARG A 1 179 ? 5.071   -24.225 -10.229 1.00 50.87  ?  128 ARG A CA    1 
ATOM   1313 C  C     . ARG A 1 179 ? 5.018   -25.406 -9.260  1.00 53.90  ?  128 ARG A C     1 
ATOM   1314 O  O     . ARG A 1 179 ? 5.001   -26.563 -9.689  1.00 50.60  ?  128 ARG A O     1 
ATOM   1315 C  CB    . ARG A 1 179 ? 3.723   -23.991 -10.908 1.00 42.36  ?  128 ARG A CB    1 
ATOM   1316 C  CG    . ARG A 1 179 ? 2.547   -24.159 -10.029 1.00 44.40  ?  128 ARG A CG    1 
ATOM   1317 C  CD    . ARG A 1 179 ? 1.352   -23.439 -10.568 1.00 46.30  ?  128 ARG A CD    1 
ATOM   1318 N  NE    . ARG A 1 179 ? 0.402   -23.201 -9.493  1.00 47.00  ?  128 ARG A NE    1 
ATOM   1319 C  CZ    . ARG A 1 179 ? -0.626  -22.364 -9.567  1.00 52.67  ?  128 ARG A CZ    1 
ATOM   1320 N  NH1   . ARG A 1 179 ? -0.841  -21.679 -10.673 1.00 49.96  ?  128 ARG A NH1   1 
ATOM   1321 N  NH2   . ARG A 1 179 ? -1.432  -22.201 -8.520  1.00 51.99  ?  128 ARG A NH2   1 
ATOM   1322 N  N     . VAL A 1 180 ? 5.038   -25.125 -7.952  1.00 52.76  ?  129 VAL A N     1 
ATOM   1323 C  CA    . VAL A 1 180 ? 4.878   -26.169 -6.940  1.00 51.54  ?  129 VAL A CA    1 
ATOM   1324 C  C     . VAL A 1 180 ? 3.752   -25.894 -5.957  1.00 53.22  ?  129 VAL A C     1 
ATOM   1325 O  O     . VAL A 1 180 ? 3.252   -26.833 -5.321  1.00 58.25  ?  129 VAL A O     1 
ATOM   1326 C  CB    . VAL A 1 180 ? 6.193   -26.414 -6.165  1.00 51.60  ?  129 VAL A CB    1 
ATOM   1327 C  CG1   . VAL A 1 180 ? 7.352   -26.699 -7.122  1.00 52.24  ?  129 VAL A CG1   1 
ATOM   1328 C  CG2   . VAL A 1 180 ? 6.501   -25.230 -5.279  1.00 53.96  ?  129 VAL A CG2   1 
ATOM   1329 N  N     . VAL A 1 181 ? 3.320   -24.659 -5.755  1.00 54.46  ?  130 VAL A N     1 
ATOM   1330 C  CA    . VAL A 1 181 ? 2.184   -24.391 -4.882  1.00 51.23  ?  130 VAL A CA    1 
ATOM   1331 C  C     . VAL A 1 181 ? 0.918   -24.795 -5.628  1.00 53.18  ?  130 VAL A C     1 
ATOM   1332 O  O     . VAL A 1 181 ? 0.601   -24.235 -6.680  1.00 53.06  ?  130 VAL A O     1 
ATOM   1333 C  CB    . VAL A 1 181 ? 2.141   -22.913 -4.469  1.00 44.57  ?  130 VAL A CB    1 
ATOM   1334 C  CG1   . VAL A 1 181 ? 0.966   -22.649 -3.562  1.00 44.77  ?  130 VAL A CG1   1 
ATOM   1335 C  CG2   . VAL A 1 181 ? 3.451   -22.499 -3.829  1.00 40.03  ?  130 VAL A CG2   1 
ATOM   1336 N  N     . LYS A 1 182 ? 0.207   -25.782 -5.102  1.00 58.04  ?  131 LYS A N     1 
ATOM   1337 C  CA    . LYS A 1 182 ? -1.082  -26.143 -5.672  1.00 57.05  ?  131 LYS A CA    1 
ATOM   1338 C  C     . LYS A 1 182 ? -2.036  -24.963 -5.579  1.00 53.84  ?  131 LYS A C     1 
ATOM   1339 O  O     . LYS A 1 182 ? -1.987  -24.176 -4.635  1.00 54.81  ?  131 LYS A O     1 
ATOM   1340 C  CB    . LYS A 1 182 ? -1.659  -27.356 -4.937  1.00 62.21  ?  131 LYS A CB    1 
ATOM   1341 N  N     . GLU A 1 183 ? -2.916  -24.840 -6.563  1.00 57.39  ?  132 GLU A N     1 
ATOM   1342 C  CA    . GLU A 1 183 ? -3.842  -23.711 -6.565  1.00 59.35  ?  132 GLU A CA    1 
ATOM   1343 C  C     . GLU A 1 183 ? -4.860  -23.812 -5.437  1.00 56.90  ?  132 GLU A C     1 
ATOM   1344 O  O     . GLU A 1 183 ? -5.220  -22.797 -4.829  1.00 56.53  ?  132 GLU A O     1 
ATOM   1345 C  CB    . GLU A 1 183 ? -4.558  -23.626 -7.908  1.00 59.52  ?  132 GLU A CB    1 
ATOM   1346 C  CG    . GLU A 1 183 ? -5.674  -22.633 -7.919  1.00 59.15  ?  132 GLU A CG    1 
ATOM   1347 C  CD    . GLU A 1 183 ? -6.529  -22.759 -9.153  1.00 67.74  ?  132 GLU A CD    1 
ATOM   1348 O  OE1   . GLU A 1 183 ? -7.298  -23.744 -9.234  1.00 68.18  ?  132 GLU A OE1   1 
ATOM   1349 O  OE2   . GLU A 1 183 ? -6.422  -21.878 -10.042 1.00 71.37  ?  132 GLU A OE2   1 
ATOM   1350 N  N     . GLU A 1 184 ? -5.351  -25.023 -5.157  1.00 59.44  ?  133 GLU A N     1 
ATOM   1351 C  CA    . GLU A 1 184 ? -6.411  -25.183 -4.166  1.00 58.10  ?  133 GLU A CA    1 
ATOM   1352 C  C     . GLU A 1 184 ? -5.945  -24.787 -2.785  1.00 52.68  ?  133 GLU A C     1 
ATOM   1353 O  O     . GLU A 1 184 ? -6.742  -24.267 -1.992  1.00 54.15  ?  133 GLU A O     1 
ATOM   1354 C  CB    . GLU A 1 184 ? -6.909  -26.625 -4.132  1.00 60.30  ?  133 GLU A CB    1 
ATOM   1355 C  CG    . GLU A 1 184 ? -7.575  -27.063 -5.412  1.00 68.60  ?  133 GLU A CG    1 
ATOM   1356 C  CD    . GLU A 1 184 ? -6.579  -27.373 -6.513  1.00 67.11  ?  133 GLU A CD    1 
ATOM   1357 O  OE1   . GLU A 1 184 ? -6.928  -27.155 -7.695  1.00 65.51  ?  133 GLU A OE1   1 
ATOM   1358 O  OE2   . GLU A 1 184 ? -5.446  -27.814 -6.188  1.00 67.04  ?  133 GLU A OE2   1 
ATOM   1359 N  N     . GLU A 1 185 ? -4.669  -25.025 -2.472  1.00 51.82  ?  134 GLU A N     1 
ATOM   1360 C  CA    . GLU A 1 185 ? -4.173  -24.681 -1.144  1.00 56.30  ?  134 GLU A CA    1 
ATOM   1361 C  C     . GLU A 1 185 ? -4.257  -23.183 -0.905  1.00 54.90  ?  134 GLU A C     1 
ATOM   1362 O  O     . GLU A 1 185 ? -4.770  -22.729 0.129   1.00 53.59  ?  134 GLU A O     1 
ATOM   1363 C  CB    . GLU A 1 185 ? -2.736  -25.167 -0.963  1.00 58.64  ?  134 GLU A CB    1 
ATOM   1364 C  CG    . GLU A 1 185 ? -2.663  -26.563 -0.398  1.00 62.33  ?  134 GLU A CG    1 
ATOM   1365 C  CD    . GLU A 1 185 ? -1.367  -27.263 -0.738  1.00 78.18  ?  134 GLU A CD    1 
ATOM   1366 O  OE1   . GLU A 1 185 ? -1.397  -28.514 -0.871  1.00 81.52  ?  134 GLU A OE1   1 
ATOM   1367 O  OE2   . GLU A 1 185 ? -0.323  -26.562 -0.859  1.00 76.25  ?  134 GLU A OE2   1 
ATOM   1368 N  N     . ALA A 1 186 ? -3.754  -22.399 -1.862  1.00 53.47  ?  135 ALA A N     1 
ATOM   1369 C  CA    . ALA A 1 186 ? -3.706  -20.951 -1.699  1.00 49.78  ?  135 ALA A CA    1 
ATOM   1370 C  C     . ALA A 1 186 ? -5.100  -20.343 -1.734  1.00 49.85  ?  135 ALA A C     1 
ATOM   1371 O  O     . ALA A 1 186 ? -5.371  -19.353 -1.045  1.00 48.07  ?  135 ALA A O     1 
ATOM   1372 C  CB    . ALA A 1 186 ? -2.829  -20.340 -2.788  1.00 49.14  ?  135 ALA A CB    1 
ATOM   1373 N  N     . ILE A 1 187 ? -5.988  -20.899 -2.558  1.00 53.61  ?  136 ILE A N     1 
ATOM   1374 C  CA    . ILE A 1 187 ? -7.370  -20.439 -2.540  1.00 51.81  ?  136 ILE A CA    1 
ATOM   1375 C  C     . ILE A 1 187 ? -7.980  -20.722 -1.181  1.00 51.44  ?  136 ILE A C     1 
ATOM   1376 O  O     . ILE A 1 187 ? -8.742  -19.910 -0.639  1.00 54.14  ?  136 ILE A O     1 
ATOM   1377 C  CB    . ILE A 1 187 ? -8.168  -21.097 -3.682  1.00 48.45  ?  136 ILE A CB    1 
ATOM   1378 C  CG1   . ILE A 1 187 ? -7.573  -20.691 -5.038  1.00 54.99  ?  136 ILE A CG1   1 
ATOM   1379 C  CG2   . ILE A 1 187 ? -9.647  -20.727 -3.590  1.00 41.45  ?  136 ILE A CG2   1 
ATOM   1380 C  CD1   . ILE A 1 187 ? -8.389  -21.151 -6.269  1.00 51.19  ?  136 ILE A CD1   1 
ATOM   1381 N  N     . ALA A 1 188 ? -7.623  -21.863 -0.589  1.00 53.10  ?  137 ALA A N     1 
ATOM   1382 C  CA    . ALA A 1 188 ? -8.053  -22.164 0.775   1.00 49.25  ?  137 ALA A CA    1 
ATOM   1383 C  C     . ALA A 1 188 ? -7.507  -21.145 1.768   1.00 50.91  ?  137 ALA A C     1 
ATOM   1384 O  O     . ALA A 1 188 ? -8.265  -20.562 2.562   1.00 52.65  ?  137 ALA A O     1 
ATOM   1385 C  CB    . ALA A 1 188 ? -7.615  -23.575 1.152   1.00 43.14  ?  137 ALA A CB    1 
ATOM   1386 N  N     . LEU A 1 189 ? -6.191  -20.912 1.749   1.00 48.83  ?  138 LEU A N     1 
ATOM   1387 C  CA    . LEU A 1 189 ? -5.629  -19.944 2.691   1.00 49.35  ?  138 LEU A CA    1 
ATOM   1388 C  C     . LEU A 1 189 ? -6.301  -18.586 2.554   1.00 47.40  ?  138 LEU A C     1 
ATOM   1389 O  O     . LEU A 1 189 ? -6.592  -17.930 3.552   1.00 51.02  ?  138 LEU A O     1 
ATOM   1390 C  CB    . LEU A 1 189 ? -4.115  -19.822 2.503   1.00 48.60  ?  138 LEU A CB    1 
ATOM   1391 C  CG    . LEU A 1 189 ? -3.330  -19.255 3.691   1.00 46.60  ?  138 LEU A CG    1 
ATOM   1392 C  CD1   . LEU A 1 189 ? -1.863  -19.645 3.621   1.00 50.02  ?  138 LEU A CD1   1 
ATOM   1393 C  CD2   . LEU A 1 189 ? -3.436  -17.743 3.726   1.00 55.44  ?  138 LEU A CD2   1 
ATOM   1394 N  N     . ALA A 1 190 ? -6.562  -18.141 1.332   1.00 53.76  ?  139 ALA A N     1 
ATOM   1395 C  CA    . ALA A 1 190 ? -7.133  -16.809 1.168   1.00 52.52  ?  139 ALA A CA    1 
ATOM   1396 C  C     . ALA A 1 190 ? -8.572  -16.763 1.658   1.00 50.23  ?  139 ALA A C     1 
ATOM   1397 O  O     . ALA A 1 190 ? -8.997  -15.772 2.261   1.00 53.01  ?  139 ALA A O     1 
ATOM   1398 C  CB    . ALA A 1 190 ? -7.044  -16.370 -0.294  1.00 55.43  ?  139 ALA A CB    1 
ATOM   1399 N  N     . GLU A 1 191 ? -9.339  -17.820 1.405   1.00 51.23  ?  140 GLU A N     1 
ATOM   1400 C  CA    . GLU A 1 191 ? -10.709 -17.860 1.897   1.00 53.58  ?  140 GLU A CA    1 
ATOM   1401 C  C     . GLU A 1 191 ? -10.739 -17.927 3.421   1.00 57.03  ?  140 GLU A C     1 
ATOM   1402 O  O     . GLU A 1 191 ? -11.560 -17.255 4.063   1.00 54.16  ?  140 GLU A O     1 
ATOM   1403 C  CB    . GLU A 1 191 ? -11.441 -19.047 1.274   1.00 55.98  ?  140 GLU A CB    1 
ATOM   1404 C  CG    . GLU A 1 191 ? -12.777 -19.358 1.914   1.00 61.49  ?  140 GLU A CG    1 
ATOM   1405 C  CD    . GLU A 1 191 ? -13.913 -18.515 1.351   1.00 69.89  ?  140 GLU A CD    1 
ATOM   1406 O  OE1   . GLU A 1 191 ? -13.857 -18.151 0.147   1.00 71.05  ?  140 GLU A OE1   1 
ATOM   1407 O  OE2   . GLU A 1 191 ? -14.861 -18.219 2.123   1.00 74.10  ?  140 GLU A OE2   1 
ATOM   1408 N  N     . LYS A 1 192 ? -9.825  -18.702 4.021   1.00 56.48  ?  141 LYS A N     1 
ATOM   1409 C  CA    . LYS A 1 192 ? -9.785  -18.801 5.479   1.00 53.45  ?  141 LYS A CA    1 
ATOM   1410 C  C     . LYS A 1 192 ? -9.626  -17.432 6.114   1.00 54.49  ?  141 LYS A C     1 
ATOM   1411 O  O     . LYS A 1 192 ? -10.240 -17.144 7.149   1.00 56.98  ?  141 LYS A O     1 
ATOM   1412 C  CB    . LYS A 1 192 ? -8.652  -19.724 5.922   1.00 51.81  ?  141 LYS A CB    1 
ATOM   1413 C  CG    . LYS A 1 192 ? -8.530  -19.856 7.428   1.00 55.78  ?  141 LYS A CG    1 
ATOM   1414 C  CD    . LYS A 1 192 ? -7.219  -20.526 7.822   1.00 56.11  ?  141 LYS A CD    1 
ATOM   1415 C  CE    . LYS A 1 192 ? -7.414  -21.990 8.159   1.00 62.62  ?  141 LYS A CE    1 
ATOM   1416 N  NZ    . LYS A 1 192 ? -7.580  -22.202 9.624   1.00 62.34  ?  141 LYS A NZ    1 
ATOM   1417 N  N     . TYR A 1 193 ? -8.834  -16.560 5.497   1.00 53.28  ?  142 TYR A N     1 
ATOM   1418 C  CA    . TYR A 1 193 ? -8.581  -15.244 6.064   1.00 50.33  ?  142 TYR A CA    1 
ATOM   1419 C  C     . TYR A 1 193 ? -9.437  -14.139 5.452   1.00 52.22  ?  142 TYR A C     1 
ATOM   1420 O  O     . TYR A 1 193 ? -9.273  -12.972 5.827   1.00 50.39  ?  142 TYR A O     1 
ATOM   1421 C  CB    . TYR A 1 193 ? -7.102  -14.897 5.921   1.00 50.12  ?  142 TYR A CB    1 
ATOM   1422 C  CG    . TYR A 1 193 ? -6.209  -15.662 6.878   1.00 51.71  ?  142 TYR A CG    1 
ATOM   1423 C  CD1   . TYR A 1 193 ? -5.994  -15.211 8.166   1.00 49.27  ?  142 TYR A CD1   1 
ATOM   1424 C  CD2   . TYR A 1 193 ? -5.573  -16.823 6.483   1.00 53.66  ?  142 TYR A CD2   1 
ATOM   1425 C  CE1   . TYR A 1 193 ? -5.169  -15.903 9.038   1.00 55.09  ?  142 TYR A CE1   1 
ATOM   1426 C  CE2   . TYR A 1 193 ? -4.740  -17.520 7.345   1.00 55.14  ?  142 TYR A CE2   1 
ATOM   1427 C  CZ    . TYR A 1 193 ? -4.544  -17.058 8.620   1.00 54.06  ?  142 TYR A CZ    1 
ATOM   1428 O  OH    . TYR A 1 193 ? -3.726  -17.758 9.484   1.00 59.58  ?  142 TYR A OH    1 
ATOM   1429 N  N     . GLY A 1 194 ? -10.341 -14.463 4.529   1.00 51.12  ?  143 GLY A N     1 
ATOM   1430 C  CA    . GLY A 1 194 ? -11.178 -13.431 3.929   1.00 51.32  ?  143 GLY A CA    1 
ATOM   1431 C  C     . GLY A 1 194 ? -10.441 -12.382 3.112   1.00 55.10  ?  143 GLY A C     1 
ATOM   1432 O  O     . GLY A 1 194 ? -10.846 -11.210 3.100   1.00 55.23  ?  143 GLY A O     1 
ATOM   1433 N  N     . ILE A 1 195 ? -9.376  -12.761 2.415   1.00 49.32  ?  144 ILE A N     1 
ATOM   1434 C  CA    . ILE A 1 195 ? -8.628  -11.735 1.695   1.00 54.52  ?  144 ILE A CA    1 
ATOM   1435 C  C     . ILE A 1 195 ? -8.511  -12.079 0.213   1.00 54.51  ?  144 ILE A C     1 
ATOM   1436 O  O     . ILE A 1 195 ? -8.320  -13.255 -0.147  1.00 51.94  ?  144 ILE A O     1 
ATOM   1437 C  CB    . ILE A 1 195 ? -7.246  -11.526 2.323   1.00 54.43  ?  144 ILE A CB    1 
ATOM   1438 C  CG1   . ILE A 1 195 ? -6.531  -12.862 2.473   1.00 53.49  ?  144 ILE A CG1   1 
ATOM   1439 C  CG2   . ILE A 1 195 ? -7.379  -10.869 3.684   1.00 54.54  ?  144 ILE A CG2   1 
ATOM   1440 C  CD1   . ILE A 1 195 ? -5.092  -12.796 2.016   1.00 53.80  ?  144 ILE A CD1   1 
ATOM   1441 N  N     . PRO A 1 196 ? -8.598  -11.085 -0.675  1.00 51.52  ?  145 PRO A N     1 
ATOM   1442 C  CA    . PRO A 1 196 ? -8.537  -11.369 -2.110  1.00 48.04  ?  145 PRO A CA    1 
ATOM   1443 C  C     . PRO A 1 196 ? -7.211  -12.010 -2.491  1.00 48.60  ?  145 PRO A C     1 
ATOM   1444 O  O     . PRO A 1 196 ? -6.180  -11.794 -1.846  1.00 51.03  ?  145 PRO A O     1 
ATOM   1445 C  CB    . PRO A 1 196 ? -8.699  -9.987  -2.753  1.00 48.02  ?  145 PRO A CB    1 
ATOM   1446 C  CG    . PRO A 1 196 ? -9.350  -9.141  -1.704  1.00 46.47  ?  145 PRO A CG    1 
ATOM   1447 C  CD    . PRO A 1 196 ? -8.807  -9.652  -0.399  1.00 49.36  ?  145 PRO A CD    1 
ATOM   1448 N  N     . TYR A 1 197 ? -7.247  -12.804 -3.557  1.00 47.92  ?  146 TYR A N     1 
ATOM   1449 C  CA    . TYR A 1 197 ? -6.082  -13.552 -3.996  1.00 46.06  ?  146 TYR A CA    1 
ATOM   1450 C  C     . TYR A 1 197 ? -5.947  -13.471 -5.511  1.00 50.21  ?  146 TYR A C     1 
ATOM   1451 O  O     . TYR A 1 197 ? -6.928  -13.668 -6.235  1.00 50.41  ?  146 TYR A O     1 
ATOM   1452 C  CB    . TYR A 1 197 ? -6.201  -15.008 -3.567  1.00 45.75  ?  146 TYR A CB    1 
ATOM   1453 C  CG    . TYR A 1 197 ? -5.164  -15.915 -4.181  1.00 44.71  ?  146 TYR A CG    1 
ATOM   1454 C  CD1   . TYR A 1 197 ? -3.811  -15.679 -3.987  1.00 43.18  ?  146 TYR A CD1   1 
ATOM   1455 C  CD2   . TYR A 1 197 ? -5.538  -17.018 -4.930  1.00 44.44  ?  146 TYR A CD2   1 
ATOM   1456 C  CE1   . TYR A 1 197 ? -2.864  -16.510 -4.533  1.00 43.56  ?  146 TYR A CE1   1 
ATOM   1457 C  CE2   . TYR A 1 197 ? -4.594  -17.850 -5.480  1.00 42.68  ?  146 TYR A CE2   1 
ATOM   1458 C  CZ    . TYR A 1 197 ? -3.264  -17.583 -5.275  1.00 41.41  ?  146 TYR A CZ    1 
ATOM   1459 O  OH    . TYR A 1 197 ? -2.327  -18.407 -5.809  1.00 46.90  ?  146 TYR A OH    1 
ATOM   1460 N  N     . PHE A 1 198 ? -4.727  -13.205 -5.980  1.00 45.94  ?  147 PHE A N     1 
ATOM   1461 C  CA    . PHE A 1 198 ? -4.405  -13.134 -7.394  1.00 46.61  ?  147 PHE A CA    1 
ATOM   1462 C  C     . PHE A 1 198 ? -3.126  -13.907 -7.647  1.00 46.01  ?  147 PHE A C     1 
ATOM   1463 O  O     . PHE A 1 198 ? -2.141  -13.719 -6.931  1.00 46.35  ?  147 PHE A O     1 
ATOM   1464 C  CB    . PHE A 1 198 ? -4.186  -11.689 -7.859  1.00 48.17  ?  147 PHE A CB    1 
ATOM   1465 C  CG    . PHE A 1 198 ? -5.400  -10.825 -7.779  1.00 44.42  ?  147 PHE A CG    1 
ATOM   1466 C  CD1   . PHE A 1 198 ? -5.698  -10.147 -6.637  1.00 45.66  ?  147 PHE A CD1   1 
ATOM   1467 C  CD2   . PHE A 1 198 ? -6.223  -10.676 -8.867  1.00 46.64  ?  147 PHE A CD2   1 
ATOM   1468 C  CE1   . PHE A 1 198 ? -6.810  -9.342  -6.560  1.00 49.03  ?  147 PHE A CE1   1 
ATOM   1469 C  CE2   . PHE A 1 198 ? -7.334  -9.869  -8.801  1.00 48.04  ?  147 PHE A CE2   1 
ATOM   1470 C  CZ    . PHE A 1 198 ? -7.624  -9.196  -7.648  1.00 47.76  ?  147 PHE A CZ    1 
ATOM   1471 N  N     . GLU A 1 199 ? -3.115  -14.741 -8.673  1.00 47.01  ?  148 GLU A N     1 
ATOM   1472 C  CA    . GLU A 1 199 ? -1.846  -15.219 -9.180  1.00 48.10  ?  148 GLU A CA    1 
ATOM   1473 C  C     . GLU A 1 199 ? -1.358  -14.186 -10.190 1.00 47.96  ?  148 GLU A C     1 
ATOM   1474 O  O     . GLU A 1 199 ? -2.146  -13.637 -10.965 1.00 52.16  ?  148 GLU A O     1 
ATOM   1475 C  CB    . GLU A 1 199 ? -1.980  -16.628 -9.769  1.00 48.47  ?  148 GLU A CB    1 
ATOM   1476 C  CG    . GLU A 1 199 ? -2.739  -17.573 -8.809  1.00 49.99  ?  148 GLU A CG    1 
ATOM   1477 C  CD    . GLU A 1 199 ? -2.476  -19.070 -9.028  1.00 55.57  ?  148 GLU A CD    1 
ATOM   1478 O  OE1   . GLU A 1 199 ? -2.326  -19.803 -8.026  1.00 55.12  ?  148 GLU A OE1   1 
ATOM   1479 O  OE2   . GLU A 1 199 ? -2.438  -19.528 -10.189 1.00 59.11  ?  148 GLU A OE2   1 
ATOM   1480 N  N     . THR A 1 200 ? -0.070  -13.862 -10.124 1.00 46.07  ?  149 THR A N     1 
ATOM   1481 C  CA    . THR A 1 200 ? 0.490   -12.699 -10.794 1.00 43.19  ?  149 THR A CA    1 
ATOM   1482 C  C     . THR A 1 200 ? 1.757   -13.100 -11.525 1.00 44.38  ?  149 THR A C     1 
ATOM   1483 O  O     . THR A 1 200 ? 2.313   -14.182 -11.312 1.00 45.62  ?  149 THR A O     1 
ATOM   1484 C  CB    . THR A 1 200 ? 0.824   -11.575 -9.794  1.00 48.63  ?  149 THR A CB    1 
ATOM   1485 O  OG1   . THR A 1 200 ? 1.764   -12.056 -8.824  1.00 47.75  ?  149 THR A OG1   1 
ATOM   1486 C  CG2   . THR A 1 200 ? -0.423  -11.076 -9.069  1.00 45.89  ?  149 THR A CG2   1 
ATOM   1487 N  N     . SER A 1 201 ? 2.231   -12.205 -12.390 1.00 45.87  ?  150 SER A N     1 
ATOM   1488 C  CA    . SER A 1 201 ? 3.539   -12.372 -13.009 1.00 42.52  ?  150 SER A CA    1 
ATOM   1489 C  C     . SER A 1 201 ? 4.180   -11.003 -13.103 1.00 42.45  ?  150 SER A C     1 
ATOM   1490 O  O     . SER A 1 201 ? 3.599   -10.083 -13.675 1.00 46.17  ?  150 SER A O     1 
ATOM   1491 C  CB    . SER A 1 201 ? 3.431   -13.021 -14.392 1.00 47.17  ?  150 SER A CB    1 
ATOM   1492 O  OG    . SER A 1 201 ? 4.698   -13.060 -15.042 1.00 47.21  ?  150 SER A OG    1 
ATOM   1493 N  N     . ALA A 1 202 ? 5.339   -10.836 -12.485 1.00 45.41  ?  151 ALA A N     1 
ATOM   1494 C  CA    . ALA A 1 202 ? 6.025   -9.578  -12.692 1.00 43.89  ?  151 ALA A CA    1 
ATOM   1495 C  C     . ALA A 1 202 ? 6.687   -9.543  -14.050 1.00 43.86  ?  151 ALA A C     1 
ATOM   1496 O  O     . ALA A 1 202 ? 7.040   -8.455  -14.526 1.00 47.35  ?  151 ALA A O     1 
ATOM   1497 C  CB    . ALA A 1 202 ? 7.058   -9.334  -11.596 1.00 38.59  ?  151 ALA A CB    1 
ATOM   1498 N  N     . ALA A 1 203 ? 6.866   -10.699 -14.687 1.00 42.19  ?  152 ALA A N     1 
ATOM   1499 C  CA    . ALA A 1 203 ? 7.590   -10.728 -15.957 1.00 47.19  ?  152 ALA A CA    1 
ATOM   1500 C  C     . ALA A 1 203 ? 6.723   -10.207 -17.094 1.00 44.39  ?  152 ALA A C     1 
ATOM   1501 O  O     . ALA A 1 203 ? 7.080   -9.235  -17.775 1.00 44.23  ?  152 ALA A O     1 
ATOM   1502 C  CB    . ALA A 1 203 ? 8.081   -12.146 -16.255 1.00 44.72  ?  152 ALA A CB    1 
ATOM   1503 N  N     . ASN A 1 204 ? 5.578   -10.844 -17.319 1.00 46.23  ?  153 ASN A N     1 
ATOM   1504 C  CA    . ASN A 1 204 ? 4.696   -10.455 -18.412 1.00 47.89  ?  153 ASN A CA    1 
ATOM   1505 C  C     . ASN A 1 204 ? 3.564   -9.555  -17.958 1.00 48.59  ?  153 ASN A C     1 
ATOM   1506 O  O     . ASN A 1 204 ? 2.744   -9.151  -18.791 1.00 50.01  ?  153 ASN A O     1 
ATOM   1507 C  CB    . ASN A 1 204 ? 4.120   -11.696 -19.111 1.00 48.94  ?  153 ASN A CB    1 
ATOM   1508 C  CG    . ASN A 1 204 ? 3.262   -12.554 -18.188 1.00 47.61  ?  153 ASN A CG    1 
ATOM   1509 O  OD1   . ASN A 1 204 ? 2.508   -12.043 -17.364 1.00 51.88  ?  153 ASN A OD1   1 
ATOM   1510 N  ND2   . ASN A 1 204 ? 3.374   -13.870 -18.330 1.00 47.96  ?  153 ASN A ND2   1 
ATOM   1511 N  N     . GLY A 1 205 ? 3.465   -9.282  -16.655 1.00 43.42  ?  154 GLY A N     1 
ATOM   1512 C  CA    . GLY A 1 205 ? 2.528   -8.304  -16.152 1.00 42.93  ?  154 GLY A CA    1 
ATOM   1513 C  C     . GLY A 1 205 ? 1.148   -8.826  -15.825 1.00 45.78  ?  154 GLY A C     1 
ATOM   1514 O  O     . GLY A 1 205 ? 0.298   -8.041  -15.377 1.00 46.29  ?  154 GLY A O     1 
ATOM   1515 N  N     . THR A 1 206 ? 0.897   -10.119 -16.009 1.00 42.93  ?  155 THR A N     1 
ATOM   1516 C  CA    . THR A 1 206 ? -0.423  -10.672 -15.724 1.00 49.14  ?  155 THR A CA    1 
ATOM   1517 C  C     . THR A 1 206 ? -0.876  -10.371 -14.298 1.00 46.46  ?  155 THR A C     1 
ATOM   1518 O  O     . THR A 1 206 ? -0.167  -10.663 -13.337 1.00 47.85  ?  155 THR A O     1 
ATOM   1519 C  CB    . THR A 1 206 ? -0.410  -12.186 -15.941 1.00 48.22  ?  155 THR A CB    1 
ATOM   1520 O  OG1   . THR A 1 206 ? 0.086   -12.481 -17.254 1.00 54.15  ?  155 THR A OG1   1 
ATOM   1521 C  CG2   . THR A 1 206 ? -1.811  -12.730 -15.801 1.00 44.32  ?  155 THR A CG2   1 
ATOM   1522 N  N     . ASN A 1 207 ? -2.066  -9.783  -14.170 1.00 49.28  ?  156 ASN A N     1 
ATOM   1523 C  CA    . ASN A 1 207 ? -2.807  -9.529  -12.931 1.00 50.07  ?  156 ASN A CA    1 
ATOM   1524 C  C     . ASN A 1 207 ? -2.180  -8.495  -11.994 1.00 48.36  ?  156 ASN A C     1 
ATOM   1525 O  O     . ASN A 1 207 ? -2.769  -8.208  -10.950 1.00 47.40  ?  156 ASN A O     1 
ATOM   1526 C  CB    . ASN A 1 207 ? -3.035  -10.813 -12.131 1.00 50.09  ?  156 ASN A CB    1 
ATOM   1527 C  CG    . ASN A 1 207 ? -4.314  -11.512 -12.512 1.00 50.28  ?  156 ASN A CG    1 
ATOM   1528 O  OD1   . ASN A 1 207 ? -5.267  -10.897 -13.007 1.00 48.73  ?  156 ASN A OD1   1 
ATOM   1529 N  ND2   . ASN A 1 207 ? -4.343  -12.814 -12.284 1.00 47.00  ?  156 ASN A ND2   1 
ATOM   1530 N  N     . ILE A 1 208 ? -1.021  -7.928  -12.333 1.00 46.23  ?  157 ILE A N     1 
ATOM   1531 C  CA    . ILE A 1 208 ? -0.360  -6.940  -11.480 1.00 44.63  ?  157 ILE A CA    1 
ATOM   1532 C  C     . ILE A 1 208 ? -1.275  -5.757  -11.195 1.00 49.36  ?  157 ILE A C     1 
ATOM   1533 O  O     . ILE A 1 208 ? -1.444  -5.334  -10.043 1.00 51.25  ?  157 ILE A O     1 
ATOM   1534 C  CB    . ILE A 1 208 ? 0.949   -6.472  -12.134 1.00 39.39  ?  157 ILE A CB    1 
ATOM   1535 C  CG1   . ILE A 1 208 ? 1.932   -7.632  -12.198 1.00 44.20  ?  157 ILE A CG1   1 
ATOM   1536 C  CG2   . ILE A 1 208 ? 1.525   -5.295  -11.380 1.00 42.08  ?  157 ILE A CG2   1 
ATOM   1537 C  CD1   . ILE A 1 208 ? 2.346   -8.106  -10.855 1.00 42.37  ?  157 ILE A CD1   1 
ATOM   1538 N  N     . SER A 1 209 ? -1.847  -5.175  -12.237 1.00 46.77  ?  158 SER A N     1 
ATOM   1539 C  CA    . SER A 1 209 ? -2.650  -3.986  -12.008 1.00 48.32  ?  158 SER A CA    1 
ATOM   1540 C  C     . SER A 1 209 ? -3.986  -4.340  -11.384 1.00 46.35  ?  158 SER A C     1 
ATOM   1541 O  O     . SER A 1 209 ? -4.540  -3.537  -10.632 1.00 48.91  ?  158 SER A O     1 
ATOM   1542 C  CB    . SER A 1 209 ? -2.838  -3.215  -13.322 1.00 46.83  ?  158 SER A CB    1 
ATOM   1543 O  OG    . SER A 1 209 ? -4.097  -3.500  -13.908 1.00 54.19  ?  158 SER A OG    1 
ATOM   1544 N  N     . GLN A 1 210 ? -4.513  -5.532  -11.669 1.00 51.16  ?  159 GLN A N     1 
ATOM   1545 C  CA    . GLN A 1 210 ? -5.771  -5.950  -11.054 1.00 48.48  ?  159 GLN A CA    1 
ATOM   1546 C  C     . GLN A 1 210 ? -5.616  -6.125  -9.552  1.00 49.12  ?  159 GLN A C     1 
ATOM   1547 O  O     . GLN A 1 210 ? -6.496  -5.719  -8.781  1.00 48.77  ?  159 GLN A O     1 
ATOM   1548 C  CB    . GLN A 1 210 ? -6.263  -7.245  -11.690 1.00 48.55  ?  159 GLN A CB    1 
ATOM   1549 C  CG    . GLN A 1 210 ? -6.845  -7.079  -13.091 1.00 52.30  ?  159 GLN A CG    1 
ATOM   1550 C  CD    . GLN A 1 210 ? -5.826  -7.317  -14.221 1.00 54.96  ?  159 GLN A CD    1 
ATOM   1551 O  OE1   . GLN A 1 210 ? -4.630  -7.005  -14.098 1.00 52.66  ?  159 GLN A OE1   1 
ATOM   1552 N  NE2   . GLN A 1 210 ? -6.311  -7.852  -15.342 1.00 58.19  ?  159 GLN A NE2   1 
ATOM   1553 N  N     . ALA A 1 211 ? -4.504  -6.721  -9.110  1.00 47.45  ?  160 ALA A N     1 
ATOM   1554 C  CA    . ALA A 1 211 ? -4.317  -6.918  -7.672  1.00 51.69  ?  160 ALA A CA    1 
ATOM   1555 C  C     . ALA A 1 211 ? -4.133  -5.587  -6.959  1.00 49.33  ?  160 ALA A C     1 
ATOM   1556 O  O     . ALA A 1 211 ? -4.753  -5.346  -5.918  1.00 51.82  ?  160 ALA A O     1 
ATOM   1557 C  CB    . ALA A 1 211 ? -3.127  -7.839  -7.399  1.00 46.13  ?  160 ALA A CB    1 
ATOM   1558 N  N     . ILE A 1 212 ? -3.315  -4.697  -7.530  1.00 49.22  ?  161 ILE A N     1 
ATOM   1559 C  CA    . ILE A 1 212 ? -3.061  -3.396  -6.923  1.00 47.31  ?  161 ILE A CA    1 
ATOM   1560 C  C     . ILE A 1 212 ? -4.311  -2.530  -6.953  1.00 46.51  ?  161 ILE A C     1 
ATOM   1561 O  O     . ILE A 1 212 ? -4.552  -1.735  -6.036  1.00 50.39  ?  161 ILE A O     1 
ATOM   1562 C  CB    . ILE A 1 212 ? -1.866  -2.728  -7.629  1.00 47.20  ?  161 ILE A CB    1 
ATOM   1563 C  CG1   . ILE A 1 212 ? -0.565  -3.408  -7.185  1.00 44.42  ?  161 ILE A CG1   1 
ATOM   1564 C  CG2   . ILE A 1 212 ? -1.853  -1.223  -7.390  1.00 45.22  ?  161 ILE A CG2   1 
ATOM   1565 C  CD1   . ILE A 1 212 ? 0.673   -2.597  -7.402  1.00 41.82  ?  161 ILE A CD1   1 
ATOM   1566 N  N     . GLU A 1 213 ? -5.137  -2.679  -7.975  1.00 48.22  ?  162 GLU A N     1 
ATOM   1567 C  CA    . GLU A 1 213 ? -6.366  -1.904  -8.024  1.00 49.77  ?  162 GLU A CA    1 
ATOM   1568 C  C     . GLU A 1 213 ? -7.383  -2.447  -7.050  1.00 47.84  ?  162 GLU A C     1 
ATOM   1569 O  O     . GLU A 1 213 ? -8.204  -1.682  -6.528  1.00 52.77  ?  162 GLU A O     1 
ATOM   1570 C  CB    . GLU A 1 213 ? -6.956  -1.913  -9.436  1.00 47.98  ?  162 GLU A CB    1 
ATOM   1571 C  CG    . GLU A 1 213 ? -6.263  -1.015  -10.407 1.00 50.39  ?  162 GLU A CG    1 
ATOM   1572 C  CD    . GLU A 1 213 ? -6.576  -1.398  -11.836 1.00 60.66  ?  162 GLU A CD    1 
ATOM   1573 O  OE1   . GLU A 1 213 ? -7.603  -2.094  -12.067 1.00 62.82  ?  162 GLU A OE1   1 
ATOM   1574 O  OE2   . GLU A 1 213 ? -5.776  -1.034  -12.728 1.00 62.40  ?  162 GLU A OE2   1 
ATOM   1575 N  N     . MET A 1 214 ? -7.370  -3.763  -6.822  1.00 48.34  ?  163 MET A N     1 
ATOM   1576 C  CA    . MET A 1 214 ? -8.235  -4.329  -5.793  1.00 53.12  ?  163 MET A CA    1 
ATOM   1577 C  C     . MET A 1 214 ? -7.892  -3.759  -4.431  1.00 49.40  ?  163 MET A C     1 
ATOM   1578 O  O     . MET A 1 214 ? -8.784  -3.410  -3.648  1.00 54.36  ?  163 MET A O     1 
ATOM   1579 C  CB    . MET A 1 214 ? -8.123  -5.855  -5.771  1.00 55.84  ?  163 MET A CB    1 
ATOM   1580 C  CG    . MET A 1 214 ? -8.961  -6.520  -4.654  1.00 53.94  ?  163 MET A CG    1 
ATOM   1581 S  SD    . MET A 1 214 ? -10.760 -6.263  -4.802  1.00 62.79  ?  163 MET A SD    1 
ATOM   1582 C  CE    . MET A 1 214 ? -11.330 -7.885  -5.278  1.00 52.46  ?  163 MET A CE    1 
ATOM   1583 N  N     . LEU A 1 215 ? -6.602  -3.637  -4.135  1.00 46.61  ?  164 LEU A N     1 
ATOM   1584 C  CA    . LEU A 1 215 ? -6.217  -3.091  -2.845  1.00 47.77  ?  164 LEU A CA    1 
ATOM   1585 C  C     . LEU A 1 215 ? -6.631  -1.636  -2.719  1.00 52.06  ?  164 LEU A C     1 
ATOM   1586 O  O     . LEU A 1 215 ? -7.104  -1.213  -1.662  1.00 53.34  ?  164 LEU A O     1 
ATOM   1587 C  CB    . LEU A 1 215 ? -4.716  -3.247  -2.643  1.00 49.00  ?  164 LEU A CB    1 
ATOM   1588 C  CG    . LEU A 1 215 ? -4.153  -2.853  -1.285  1.00 50.22  ?  164 LEU A CG    1 
ATOM   1589 C  CD1   . LEU A 1 215 ? -4.836  -3.580  -0.097  1.00 46.75  ?  164 LEU A CD1   1 
ATOM   1590 C  CD2   . LEU A 1 215 ? -2.672  -3.128  -1.334  1.00 49.78  ?  164 LEU A CD2   1 
ATOM   1591 N  N     . LEU A 1 216 ? -6.454  -0.853  -3.781  1.00 53.29  ?  165 LEU A N     1 
ATOM   1592 C  CA    . LEU A 1 216 ? -6.884  0.541   -3.751  1.00 52.18  ?  165 LEU A CA    1 
ATOM   1593 C  C     . LEU A 1 216 ? -8.371  0.646   -3.445  1.00 51.79  ?  165 LEU A C     1 
ATOM   1594 O  O     . LEU A 1 216 ? -8.799  1.472   -2.633  1.00 55.19  ?  165 LEU A O     1 
ATOM   1595 C  CB    . LEU A 1 216 ? -6.559  1.198   -5.090  1.00 54.51  ?  165 LEU A CB    1 
ATOM   1596 C  CG    . LEU A 1 216 ? -6.875  2.679   -5.292  1.00 55.35  ?  165 LEU A CG    1 
ATOM   1597 C  CD1   . LEU A 1 216 ? -6.337  3.522   -4.138  1.00 53.89  ?  165 LEU A CD1   1 
ATOM   1598 C  CD2   . LEU A 1 216 ? -6.270  3.128   -6.598  1.00 48.13  ?  165 LEU A CD2   1 
ATOM   1599 N  N     . ASP A 1 217 ? -9.176  -0.194  -4.085  1.00 52.09  ?  166 ASP A N     1 
ATOM   1600 C  CA    . ASP A 1 217 ? -10.616 -0.170  -3.855  1.00 55.60  ?  166 ASP A CA    1 
ATOM   1601 C  C     . ASP A 1 217 ? -10.946 -0.454  -2.392  1.00 55.12  ?  166 ASP A C     1 
ATOM   1602 O  O     . ASP A 1 217 ? -11.744 0.258   -1.775  1.00 57.88  ?  166 ASP A O     1 
ATOM   1603 C  CB    . ASP A 1 217 ? -11.297 -1.181  -4.782  1.00 57.53  ?  166 ASP A CB    1 
ATOM   1604 C  CG    . ASP A 1 217 ? -12.750 -0.842  -5.057  1.00 61.19  ?  166 ASP A CG    1 
ATOM   1605 O  OD1   . ASP A 1 217 ? -13.139 0.339   -4.928  1.00 62.66  ?  166 ASP A OD1   1 
ATOM   1606 O  OD2   . ASP A 1 217 ? -13.508 -1.764  -5.411  1.00 63.29  ?  166 ASP A OD2   1 
ATOM   1607 N  N     . LEU A 1 218 ? -10.331 -1.487  -1.817  1.00 56.57  ?  167 LEU A N     1 
ATOM   1608 C  CA    . LEU A 1 218 ? -10.599 -1.839  -0.424  1.00 52.57  ?  167 LEU A CA    1 
ATOM   1609 C  C     . LEU A 1 218 ? -10.374 -0.645  0.484   1.00 53.47  ?  167 LEU A C     1 
ATOM   1610 O  O     . LEU A 1 218 ? -11.188 -0.346  1.366   1.00 53.66  ?  167 LEU A O     1 
ATOM   1611 C  CB    . LEU A 1 218 ? -9.704  -2.999  -0.000  1.00 51.27  ?  167 LEU A CB    1 
ATOM   1612 C  CG    . LEU A 1 218 ? -10.098 -4.398  -0.457  1.00 51.17  ?  167 LEU A CG    1 
ATOM   1613 C  CD1   . LEU A 1 218 ? -8.894  -5.320  -0.361  1.00 49.50  ?  167 LEU A CD1   1 
ATOM   1614 C  CD2   . LEU A 1 218 ? -11.226 -4.903  0.408   1.00 47.47  ?  167 LEU A CD2   1 
ATOM   1615 N  N     . ILE A 1 219 ? -9.277  0.071   0.247   1.00 55.09  ?  168 ILE A N     1 
ATOM   1616 C  CA    . ILE A 1 219 ? -8.919  1.209   1.083   1.00 53.57  ?  168 ILE A CA    1 
ATOM   1617 C  C     . ILE A 1 219 ? -9.867  2.373   0.849   1.00 57.73  ?  168 ILE A C     1 
ATOM   1618 O  O     . ILE A 1 219 ? -10.315 3.026   1.801   1.00 61.69  ?  168 ILE A O     1 
ATOM   1619 C  CB    . ILE A 1 219 ? -7.461  1.598   0.814   1.00 47.63  ?  168 ILE A CB    1 
ATOM   1620 C  CG1   . ILE A 1 219 ? -6.569  0.483   1.335   1.00 52.89  ?  168 ILE A CG1   1 
ATOM   1621 C  CG2   . ILE A 1 219 ? -7.136  2.903   1.477   1.00 48.71  ?  168 ILE A CG2   1 
ATOM   1622 C  CD1   . ILE A 1 219 ? -5.201  0.514   0.763   1.00 55.39  ?  168 ILE A CD1   1 
ATOM   1623 N  N     . MET A 1 220 ? -10.182 2.664   -0.417  1.00 56.18  ?  169 MET A N     1 
ATOM   1624 C  CA    . MET A 1 220 ? -11.116 3.745   -0.703  1.00 56.13  ?  169 MET A CA    1 
ATOM   1625 C  C     . MET A 1 220 ? -12.481 3.443   -0.105  1.00 58.41  ?  169 MET A C     1 
ATOM   1626 O  O     . MET A 1 220 ? -13.079 4.295   0.566   1.00 59.75  ?  169 MET A O     1 
ATOM   1627 C  CB    . MET A 1 220 ? -11.226 3.977   -2.211  1.00 55.20  ?  169 MET A CB    1 
ATOM   1628 C  CG    . MET A 1 220 ? -9.961  4.537   -2.861  1.00 55.02  ?  169 MET A CG    1 
ATOM   1629 S  SD    . MET A 1 220 ? -9.370  6.075   -2.127  1.00 58.91  ?  169 MET A SD    1 
ATOM   1630 C  CE    . MET A 1 220 ? -10.586 7.236   -2.747  1.00 59.48  ?  169 MET A CE    1 
ATOM   1631 N  N     . LYS A 1 221 ? -12.990 2.227   -0.331  1.00 59.16  ?  170 LYS A N     1 
ATOM   1632 C  CA    . LYS A 1 221 ? -14.274 1.859   0.258   1.00 60.94  ?  170 LYS A CA    1 
ATOM   1633 C  C     . LYS A 1 221 ? -14.187 1.867   1.774   1.00 62.51  ?  170 LYS A C     1 
ATOM   1634 O  O     . LYS A 1 221 ? -15.105 2.338   2.457   1.00 63.36  ?  170 LYS A O     1 
ATOM   1635 C  CB    . LYS A 1 221 ? -14.726 0.491   -0.253  1.00 59.33  ?  170 LYS A CB    1 
ATOM   1636 C  CG    . LYS A 1 221 ? -14.898 0.421   -1.760  1.00 64.16  ?  170 LYS A CG    1 
ATOM   1637 C  CD    . LYS A 1 221 ? -16.050 -0.484  -2.169  1.00 68.29  ?  170 LYS A CD    1 
ATOM   1638 C  CE    . LYS A 1 221 ? -16.147 -0.627  -3.701  1.00 75.09  ?  170 LYS A CE    1 
ATOM   1639 N  NZ    . LYS A 1 221 ? -16.057 0.663   -4.469  1.00 76.75  ?  170 LYS A NZ    1 
ATOM   1640 N  N     . ARG A 1 222 ? -13.074 1.370   2.317   1.00 60.96  ?  171 ARG A N     1 
ATOM   1641 C  CA    . ARG A 1 222 ? -12.850 1.477   3.752   1.00 65.22  ?  171 ARG A CA    1 
ATOM   1642 C  C     . ARG A 1 222 ? -12.864 2.932   4.204   1.00 68.04  ?  171 ARG A C     1 
ATOM   1643 O  O     . ARG A 1 222 ? -13.370 3.249   5.289   1.00 72.10  ?  171 ARG A O     1 
ATOM   1644 C  CB    . ARG A 1 222 ? -11.526 0.814   4.132   1.00 64.16  ?  171 ARG A CB    1 
ATOM   1645 C  CG    . ARG A 1 222 ? -11.226 0.845   5.615   1.00 66.15  ?  171 ARG A CG    1 
ATOM   1646 C  CD    . ARG A 1 222 ? -10.381 -0.342  6.042   1.00 64.78  ?  171 ARG A CD    1 
ATOM   1647 N  NE    . ARG A 1 222 ? -10.443 -0.490  7.486   1.00 68.34  ?  171 ARG A NE    1 
ATOM   1648 C  CZ    . ARG A 1 222 ? -9.883  -1.473  8.186   1.00 69.28  ?  171 ARG A CZ    1 
ATOM   1649 N  NH1   . ARG A 1 222 ? -9.189  -2.431  7.577   1.00 63.53  ?  171 ARG A NH1   1 
ATOM   1650 N  NH2   . ARG A 1 222 ? -10.019 -1.485  9.511   1.00 65.48  ?  171 ARG A NH2   1 
ATOM   1651 N  N     . MET A 1 223 ? -12.323 3.837   3.383   1.00 65.01  ?  172 MET A N     1 
ATOM   1652 C  CA    . MET A 1 223 ? -12.255 5.234   3.803   1.00 66.96  ?  172 MET A CA    1 
ATOM   1653 C  C     . MET A 1 223 ? -13.621 5.904   3.788   1.00 69.64  ?  172 MET A C     1 
ATOM   1654 O  O     . MET A 1 223 ? -13.913 6.728   4.666   1.00 72.93  ?  172 MET A O     1 
ATOM   1655 C  CB    . MET A 1 223 ? -11.279 6.009   2.928   1.00 64.57  ?  172 MET A CB    1 
ATOM   1656 C  CG    . MET A 1 223 ? -10.008 6.354   3.670   1.00 68.66  ?  172 MET A CG    1 
ATOM   1657 S  SD    . MET A 1 223 ? -8.872  7.245   2.614   1.00 82.35  ?  172 MET A SD    1 
ATOM   1658 C  CE    . MET A 1 223 ? -9.994  8.472   1.928   1.00 77.23  ?  172 MET A CE    1 
ATOM   1659 N  N     . GLU A 1 224 ? -14.476 5.548   2.828   1.00 67.51  ?  173 GLU A N     1 
ATOM   1660 C  CA    . GLU A 1 224 ? -15.752 6.237   2.697   1.00 70.96  ?  173 GLU A CA    1 
ATOM   1661 C  C     . GLU A 1 224 ? -16.631 6.007   3.919   1.00 75.50  ?  173 GLU A C     1 
ATOM   1662 O  O     . GLU A 1 224 ? -17.282 6.943   4.398   1.00 81.63  ?  173 GLU A O     1 
ATOM   1663 C  CB    . GLU A 1 224 ? -16.461 5.796   1.414   1.00 68.83  ?  173 GLU A CB    1 
ATOM   1664 N  N     . ARG A 1 225 ? -16.642 4.782   4.455   1.00 73.45  ?  174 ARG A N     1 
ATOM   1665 C  CA    . ARG A 1 225 ? -17.462 4.476   5.625   1.00 73.97  ?  174 ARG A CA    1 
ATOM   1666 C  C     . ARG A 1 225 ? -17.247 5.479   6.758   1.00 76.79  ?  174 ARG A C     1 
ATOM   1667 O  O     . ARG A 1 225 ? -18.208 6.065   7.269   1.00 79.79  ?  174 ARG A O     1 
ATOM   1668 C  CB    . ARG A 1 225 ? -17.164 3.057   6.106   1.00 77.26  ?  174 ARG A CB    1 
ATOM   1669 C  CG    . ARG A 1 225 ? -17.371 2.013   5.033   1.00 71.73  ?  174 ARG A CG    1 
ATOM   1670 C  CD    . ARG A 1 225 ? -17.318 0.594   5.588   1.00 67.60  ?  174 ARG A CD    1 
ATOM   1671 N  NE    . ARG A 1 225 ? -16.770 -0.289  4.569   1.00 73.79  ?  174 ARG A NE    1 
ATOM   1672 C  CZ    . ARG A 1 225 ? -15.669 -1.014  4.724   1.00 73.55  ?  174 ARG A CZ    1 
ATOM   1673 N  NH1   . ARG A 1 225 ? -15.015 -0.990  5.885   1.00 75.03  ?  174 ARG A NH1   1 
ATOM   1674 N  NH2   . ARG A 1 225 ? -15.234 -1.770  3.723   1.00 63.73  ?  174 ARG A NH2   1 
ATOM   1675 N  N     . SER A 1 226 ? -15.993 5.702   7.149   1.00 73.46  ?  175 SER A N     1 
ATOM   1676 C  CA    . SER A 1 226 ? -15.670 6.563   8.293   1.00 73.74  ?  175 SER A CA    1 
ATOM   1677 C  C     . SER A 1 226 ? -16.331 7.948   8.266   1.00 74.91  ?  175 SER A C     1 
ATOM   1678 O  O     . SER A 1 226 ? -16.681 8.474   7.208   1.00 74.72  ?  175 SER A O     1 
ATOM   1679 C  CB    . SER A 1 226 ? -14.158 6.732   8.382   1.00 75.74  ?  175 SER A CB    1 
ATOM   1680 O  OG    . SER A 1 226 ? -13.513 5.535   7.985   1.00 77.52  ?  175 SER A OG    1 
ATOM   1681 N  N     . HIS B 1 2   ? 34.838  -8.625  19.894  1.00 95.16  ?  -37 HIS B N     1 
ATOM   1682 C  CA    . HIS B 1 2   ? 35.679  -8.011  18.874  1.00 96.65  ?  -37 HIS B CA    1 
ATOM   1683 C  C     . HIS B 1 2   ? 34.898  -7.695  17.582  1.00 99.75  ?  -37 HIS B C     1 
ATOM   1684 O  O     . HIS B 1 2   ? 35.026  -6.598  17.030  1.00 101.46 ?  -37 HIS B O     1 
ATOM   1685 C  CB    . HIS B 1 2   ? 36.882  -8.915  18.580  1.00 90.37  ?  -37 HIS B CB    1 
ATOM   1686 C  CG    . HIS B 1 2   ? 37.697  -8.489  17.396  1.00 92.23  ?  -37 HIS B CG    1 
ATOM   1687 N  ND1   . HIS B 1 2   ? 37.271  -8.654  16.093  1.00 94.23  ?  -37 HIS B ND1   1 
ATOM   1688 C  CD2   . HIS B 1 2   ? 38.924  -7.920  17.319  1.00 94.32  ?  -37 HIS B CD2   1 
ATOM   1689 C  CE1   . HIS B 1 2   ? 38.192  -8.192  15.266  1.00 92.56  ?  -37 HIS B CE1   1 
ATOM   1690 N  NE2   . HIS B 1 2   ? 39.205  -7.741  15.984  1.00 97.80  ?  -37 HIS B NE2   1 
ATOM   1691 N  N     . MET B 1 3   ? 34.103  -8.649  17.092  1.00 98.78  ?  -36 MET B N     1 
ATOM   1692 C  CA    . MET B 1 3   ? 33.258  -8.446  15.914  1.00 93.91  ?  -36 MET B CA    1 
ATOM   1693 C  C     . MET B 1 3   ? 31.827  -8.795  16.298  1.00 94.73  ?  -36 MET B C     1 
ATOM   1694 O  O     . MET B 1 3   ? 31.516  -9.970  16.520  1.00 97.45  ?  -36 MET B O     1 
ATOM   1695 C  CB    . MET B 1 3   ? 33.730  -9.298  14.735  1.00 93.76  ?  -36 MET B CB    1 
ATOM   1696 N  N     . SER B 1 4   ? 30.958  -7.788  16.382  1.00 88.62  ?  -35 SER B N     1 
ATOM   1697 C  CA    . SER B 1 4   ? 29.604  -7.985  16.881  1.00 86.22  ?  -35 SER B CA    1 
ATOM   1698 C  C     . SER B 1 4   ? 28.590  -7.848  15.753  1.00 81.48  ?  -35 SER B C     1 
ATOM   1699 O  O     . SER B 1 4   ? 28.778  -7.090  14.797  1.00 78.27  ?  -35 SER B O     1 
ATOM   1700 C  CB    . SER B 1 4   ? 29.265  -7.005  18.015  1.00 87.52  ?  -35 SER B CB    1 
ATOM   1701 O  OG    . SER B 1 4   ? 28.017  -7.335  18.622  1.00 78.94  ?  -35 SER B OG    1 
ATOM   1702 N  N     . PHE B 1 5   ? 27.511  -8.606  15.889  1.00 80.65  ?  -34 PHE B N     1 
ATOM   1703 C  CA    . PHE B 1 5   ? 26.488  -8.746  14.873  1.00 72.51  ?  -34 PHE B CA    1 
ATOM   1704 C  C     . PHE B 1 5   ? 25.130  -8.512  15.522  1.00 70.10  ?  -34 PHE B C     1 
ATOM   1705 O  O     . PHE B 1 5   ? 24.984  -8.596  16.744  1.00 73.62  ?  -34 PHE B O     1 
ATOM   1706 C  CB    . PHE B 1 5   ? 26.567  -10.141 14.244  1.00 73.47  ?  -34 PHE B CB    1 
ATOM   1707 C  CG    . PHE B 1 5   ? 27.735  -10.326 13.293  1.00 82.96  ?  -34 PHE B CG    1 
ATOM   1708 C  CD1   . PHE B 1 5   ? 28.461  -11.519 13.289  1.00 82.14  ?  -34 PHE B CD1   1 
ATOM   1709 C  CD2   . PHE B 1 5   ? 28.106  -9.314  12.397  1.00 84.05  ?  -34 PHE B CD2   1 
ATOM   1710 C  CE1   . PHE B 1 5   ? 29.535  -11.703 12.409  1.00 79.58  ?  -34 PHE B CE1   1 
ATOM   1711 C  CE2   . PHE B 1 5   ? 29.184  -9.490  11.512  1.00 85.56  ?  -34 PHE B CE2   1 
ATOM   1712 C  CZ    . PHE B 1 5   ? 29.897  -10.694 11.523  1.00 84.63  ?  -34 PHE B CZ    1 
ATOM   1713 N  N     . LEU B 1 6   ? 24.132  -8.198  14.709  1.00 66.11  ?  -33 LEU B N     1 
ATOM   1714 C  CA    . LEU B 1 6   ? 22.798  -7.969  15.255  1.00 62.50  ?  -33 LEU B CA    1 
ATOM   1715 C  C     . LEU B 1 6   ? 22.249  -9.308  15.715  1.00 63.66  ?  -33 LEU B C     1 
ATOM   1716 O  O     . LEU B 1 6   ? 21.806  -10.121 14.905  1.00 68.56  ?  -33 LEU B O     1 
ATOM   1717 C  CB    . LEU B 1 6   ? 21.892  -7.312  14.219  1.00 70.06  ?  -33 LEU B CB    1 
ATOM   1718 C  CG    . LEU B 1 6   ? 20.383  -7.312  14.484  1.00 69.12  ?  -33 LEU B CG    1 
ATOM   1719 C  CD1   . LEU B 1 6   ? 20.078  -6.188  15.448  1.00 69.38  ?  -33 LEU B CD1   1 
ATOM   1720 C  CD2   . LEU B 1 6   ? 19.590  -7.144  13.180  1.00 62.68  ?  -33 LEU B CD2   1 
ATOM   1721 N  N     . THR B 1 7   ? 22.311  -9.553  17.019  1.00 64.04  ?  -32 THR B N     1 
ATOM   1722 C  CA    . THR B 1 7   ? 21.886  -10.812 17.596  1.00 63.18  ?  -32 THR B CA    1 
ATOM   1723 C  C     . THR B 1 7   ? 20.372  -10.970 17.511  1.00 61.80  ?  -32 THR B C     1 
ATOM   1724 O  O     . THR B 1 7   ? 19.623  -10.016 17.279  1.00 65.92  ?  -32 THR B O     1 
ATOM   1725 C  CB    . THR B 1 7   ? 22.302  -10.888 19.053  1.00 61.67  ?  -32 THR B CB    1 
ATOM   1726 O  OG1   . THR B 1 7   ? 21.263  -10.307 19.845  1.00 64.06  ?  -32 THR B OG1   1 
ATOM   1727 C  CG2   . THR B 1 7   ? 23.583  -10.110 19.268  1.00 61.36  ?  -32 THR B CG2   1 
ATOM   1728 N  N     . GLU B 1 8   ? 19.919  -12.202 17.722  1.00 60.96  ?  -31 GLU B N     1 
ATOM   1729 C  CA    . GLU B 1 8   ? 18.487  -12.455 17.653  1.00 62.27  ?  -31 GLU B CA    1 
ATOM   1730 C  C     . GLU B 1 8   ? 17.763  -11.843 18.850  1.00 65.82  ?  -31 GLU B C     1 
ATOM   1731 O  O     . GLU B 1 8   ? 16.699  -11.233 18.685  1.00 67.80  ?  -31 GLU B O     1 
ATOM   1732 C  CB    . GLU B 1 8   ? 18.227  -13.957 17.552  1.00 65.85  ?  -31 GLU B CB    1 
ATOM   1733 N  N     . GLU B 1 9   ? 18.328  -11.980 20.061  1.00 67.04  ?  -30 GLU B N     1 
ATOM   1734 C  CA    . GLU B 1 9   ? 17.746  -11.328 21.236  1.00 62.30  ?  -30 GLU B CA    1 
ATOM   1735 C  C     . GLU B 1 9   ? 17.579  -9.827  21.010  1.00 62.60  ?  -30 GLU B C     1 
ATOM   1736 O  O     . GLU B 1 9   ? 16.513  -9.261  21.286  1.00 62.10  ?  -30 GLU B O     1 
ATOM   1737 C  CB    . GLU B 1 9   ? 18.614  -11.587 22.466  1.00 56.48  ?  -30 GLU B CB    1 
ATOM   1738 N  N     . GLU B 1 10  ? 18.614  -9.172  20.476  1.00 59.50  ?  -29 GLU B N     1 
ATOM   1739 C  CA    . GLU B 1 10  ? 18.529  -7.744  20.207  1.00 54.99  ?  -29 GLU B CA    1 
ATOM   1740 C  C     . GLU B 1 10  ? 17.378  -7.419  19.259  1.00 60.38  ?  -29 GLU B C     1 
ATOM   1741 O  O     . GLU B 1 10  ? 16.722  -6.381  19.405  1.00 60.56  ?  -29 GLU B O     1 
ATOM   1742 C  CB    . GLU B 1 10  ? 19.853  -7.239  19.633  1.00 62.82  ?  -29 GLU B CB    1 
ATOM   1743 N  N     . GLN B 1 11  ? 17.114  -8.280  18.270  1.00 62.37  ?  -28 GLN B N     1 
ATOM   1744 C  CA    . GLN B 1 11  ? 16.003  -7.967  17.375  1.00 59.47  ?  -28 GLN B CA    1 
ATOM   1745 C  C     . GLN B 1 11  ? 14.661  -8.290  18.017  1.00 54.59  ?  -28 GLN B C     1 
ATOM   1746 O  O     . GLN B 1 11  ? 13.681  -7.578  17.773  1.00 56.11  ?  -28 GLN B O     1 
ATOM   1747 C  CB    . GLN B 1 11  ? 16.140  -8.695  16.028  1.00 63.81  ?  -28 GLN B CB    1 
ATOM   1748 C  CG    . GLN B 1 11  ? 15.216  -8.135  14.925  1.00 52.69  ?  -28 GLN B CG    1 
ATOM   1749 C  CD    . GLN B 1 11  ? 15.725  -8.417  13.524  1.00 64.29  ?  -28 GLN B CD    1 
ATOM   1750 O  OE1   . GLN B 1 11  ? 15.670  -7.554  12.628  1.00 63.27  ?  -28 GLN B OE1   1 
ATOM   1751 N  NE2   . GLN B 1 11  ? 16.221  -9.637  13.315  1.00 66.35  ?  -28 GLN B NE2   1 
ATOM   1752 N  N     . GLU B 1 12  ? 14.599  -9.341  18.833  1.00 55.77  ?  -27 GLU B N     1 
ATOM   1753 C  CA    . GLU B 1 12  ? 13.393  -9.608  19.616  1.00 59.65  ?  -27 GLU B CA    1 
ATOM   1754 C  C     . GLU B 1 12  ? 13.015  -8.394  20.462  1.00 56.20  ?  -27 GLU B C     1 
ATOM   1755 O  O     . GLU B 1 12  ? 11.861  -7.947  20.445  1.00 52.90  ?  -27 GLU B O     1 
ATOM   1756 C  CB    . GLU B 1 12  ? 13.597  -10.847 20.497  1.00 57.54  ?  -27 GLU B CB    1 
ATOM   1757 N  N     . ALA B 1 13  ? 13.988  -7.839  21.196  1.00 54.94  ?  -26 ALA B N     1 
ATOM   1758 C  CA    . ALA B 1 13  ? 13.768  -6.612  21.962  1.00 52.53  ?  -26 ALA B CA    1 
ATOM   1759 C  C     . ALA B 1 13  ? 13.095  -5.540  21.124  1.00 53.20  ?  -26 ALA B C     1 
ATOM   1760 O  O     . ALA B 1 13  ? 12.066  -4.971  21.517  1.00 50.85  ?  -26 ALA B O     1 
ATOM   1761 C  CB    . ALA B 1 13  ? 15.098  -6.082  22.493  1.00 47.60  ?  -26 ALA B CB    1 
ATOM   1762 N  N     . ILE B 1 14  ? 13.672  -5.245  19.957  1.00 54.41  ?  -25 ILE B N     1 
ATOM   1763 C  CA    . ILE B 1 14  ? 13.165  -4.153  19.141  1.00 50.11  ?  -25 ILE B CA    1 
ATOM   1764 C  C     . ILE B 1 14  ? 11.770  -4.465  18.629  1.00 49.58  ?  -25 ILE B C     1 
ATOM   1765 O  O     . ILE B 1 14  ? 10.931  -3.565  18.518  1.00 52.24  ?  -25 ILE B O     1 
ATOM   1766 C  CB    . ILE B 1 14  ? 14.141  -3.859  17.992  1.00 53.72  ?  -25 ILE B CB    1 
ATOM   1767 C  CG1   . ILE B 1 14  ? 15.517  -3.494  18.549  1.00 51.53  ?  -25 ILE B CG1   1 
ATOM   1768 C  CG2   . ILE B 1 14  ? 13.615  -2.750  17.126  1.00 50.50  ?  -25 ILE B CG2   1 
ATOM   1769 C  CD1   . ILE B 1 14  ? 16.545  -3.269  17.471  1.00 53.39  ?  -25 ILE B CD1   1 
ATOM   1770 N  N     . MET B 1 15  ? 11.481  -5.729  18.321  1.00 50.72  ?  -24 MET B N     1 
ATOM   1771 C  CA    . MET B 1 15  ? 10.137  -6.046  17.852  1.00 54.75  ?  -24 MET B CA    1 
ATOM   1772 C  C     . MET B 1 15  ? 9.105   -5.855  18.958  1.00 54.34  ?  -24 MET B C     1 
ATOM   1773 O  O     . MET B 1 15  ? 7.966   -5.466  18.668  1.00 56.48  ?  -24 MET B O     1 
ATOM   1774 C  CB    . MET B 1 15  ? 10.074  -7.470  17.291  1.00 55.20  ?  -24 MET B CB    1 
ATOM   1775 C  CG    . MET B 1 15  ? 11.085  -7.758  16.210  1.00 55.41  ?  -24 MET B CG    1 
ATOM   1776 S  SD    . MET B 1 15  ? 10.764  -6.838  14.702  1.00 57.89  ?  -24 MET B SD    1 
ATOM   1777 C  CE    . MET B 1 15  ? 9.428   -7.789  13.955  1.00 46.17  ?  -24 MET B CE    1 
ATOM   1778 N  N     . LYS B 1 16  ? 9.477   -6.077  20.227  1.00 55.31  ?  -23 LYS B N     1 
ATOM   1779 C  CA    . LYS B 1 16  ? 8.499   -5.866  21.300  1.00 58.72  ?  -23 LYS B CA    1 
ATOM   1780 C  C     . LYS B 1 16  ? 8.223   -4.375  21.534  1.00 57.27  ?  -23 LYS B C     1 
ATOM   1781 O  O     . LYS B 1 16  ? 7.075   -3.985  21.810  1.00 56.51  ?  -23 LYS B O     1 
ATOM   1782 C  CB    . LYS B 1 16  ? 8.938   -6.547  22.596  1.00 54.49  ?  -23 LYS B CB    1 
ATOM   1783 C  CG    . LYS B 1 16  ? 7.827   -6.457  23.661  1.00 65.48  ?  -23 LYS B CG    1 
ATOM   1784 C  CD    . LYS B 1 16  ? 8.151   -7.101  25.010  1.00 72.30  ?  -23 LYS B CD    1 
ATOM   1785 C  CE    . LYS B 1 16  ? 7.644   -6.221  26.184  1.00 76.47  ?  -23 LYS B CE    1 
ATOM   1786 N  NZ    . LYS B 1 16  ? 6.383   -6.661  26.864  1.00 81.66  ?  -23 LYS B NZ    1 
ATOM   1787 N  N     . VAL B 1 17  ? 9.248   -3.520  21.427  1.00 49.31  ?  -22 VAL B N     1 
ATOM   1788 C  CA    . VAL B 1 17  ? 8.967   -2.088  21.420  1.00 50.79  ?  -22 VAL B CA    1 
ATOM   1789 C  C     . VAL B 1 17  ? 7.949   -1.754  20.334  1.00 56.97  ?  -22 VAL B C     1 
ATOM   1790 O  O     . VAL B 1 17  ? 7.045   -0.933  20.543  1.00 60.35  ?  -22 VAL B O     1 
ATOM   1791 C  CB    . VAL B 1 17  ? 10.260  -1.275  21.237  1.00 52.79  ?  -22 VAL B CB    1 
ATOM   1792 C  CG1   . VAL B 1 17  ? 9.943   0.192   21.232  1.00 47.24  ?  -22 VAL B CG1   1 
ATOM   1793 C  CG2   . VAL B 1 17  ? 11.256  -1.609  22.320  1.00 48.46  ?  -22 VAL B CG2   1 
ATOM   1794 N  N     . LEU B 1 18  ? 8.068   -2.394  19.161  1.00 55.36  ?  -21 LEU B N     1 
ATOM   1795 C  CA    . LEU B 1 18  ? 7.188   -2.072  18.037  1.00 55.20  ?  -21 LEU B CA    1 
ATOM   1796 C  C     . LEU B 1 18  ? 5.780   -2.610  18.265  1.00 53.36  ?  -21 LEU B C     1 
ATOM   1797 O  O     . LEU B 1 18  ? 4.792   -1.907  18.026  1.00 53.20  ?  -21 LEU B O     1 
ATOM   1798 C  CB    . LEU B 1 18  ? 7.779   -2.624  16.729  1.00 53.34  ?  -21 LEU B CB    1 
ATOM   1799 C  CG    . LEU B 1 18  ? 8.919   -1.793  16.127  1.00 50.84  ?  -21 LEU B CG    1 
ATOM   1800 C  CD1   . LEU B 1 18  ? 9.810   -2.617  15.205  1.00 48.40  ?  -21 LEU B CD1   1 
ATOM   1801 C  CD2   . LEU B 1 18  ? 8.353   -0.576  15.391  1.00 52.36  ?  -21 LEU B CD2   1 
ATOM   1802 N  N     . GLN B 1 19  ? 5.670   -3.864  18.706  1.00 52.59  ?  -20 GLN B N     1 
ATOM   1803 C  CA    . GLN B 1 19  ? 4.372   -4.412  19.087  1.00 57.01  ?  -20 GLN B CA    1 
ATOM   1804 C  C     . GLN B 1 19  ? 3.666   -3.509  20.088  1.00 59.62  ?  -20 GLN B C     1 
ATOM   1805 O  O     . GLN B 1 19  ? 2.497   -3.152  19.900  1.00 61.01  ?  -20 GLN B O     1 
ATOM   1806 C  CB    . GLN B 1 19  ? 4.547   -5.811  19.672  1.00 58.30  ?  -20 GLN B CB    1 
ATOM   1807 C  CG    . GLN B 1 19  ? 3.259   -6.442  20.171  1.00 63.16  ?  -20 GLN B CG    1 
ATOM   1808 C  CD    . GLN B 1 19  ? 3.508   -7.773  20.869  1.00 68.12  ?  -20 GLN B CD    1 
ATOM   1809 O  OE1   . GLN B 1 19  ? 4.661   -8.150  21.121  1.00 62.61  ?  -20 GLN B OE1   1 
ATOM   1810 N  NE2   . GLN B 1 19  ? 2.428   -8.499  21.172  1.00 71.45  ?  -20 GLN B NE2   1 
ATOM   1811 N  N     . ARG B 1 20  ? 4.373   -3.121  21.160  1.00 58.39  ?  -19 ARG B N     1 
ATOM   1812 C  CA    . ARG B 1 20  ? 3.792   -2.221  22.152  1.00 59.29  ?  -19 ARG B CA    1 
ATOM   1813 C  C     . ARG B 1 20  ? 3.344   -0.917  21.512  1.00 59.73  ?  -19 ARG B C     1 
ATOM   1814 O  O     . ARG B 1 20  ? 2.314   -0.345  21.893  1.00 59.83  ?  -19 ARG B O     1 
ATOM   1815 C  CB    . ARG B 1 20  ? 4.798   -1.934  23.269  1.00 57.82  ?  -19 ARG B CB    1 
ATOM   1816 C  CG    . ARG B 1 20  ? 5.148   -3.125  24.120  1.00 61.79  ?  -19 ARG B CG    1 
ATOM   1817 C  CD    . ARG B 1 20  ? 6.433   -2.868  24.880  1.00 59.76  ?  -19 ARG B CD    1 
ATOM   1818 N  NE    . ARG B 1 20  ? 6.512   -1.476  25.319  1.00 60.72  ?  -19 ARG B NE    1 
ATOM   1819 C  CZ    . ARG B 1 20  ? 7.642   -0.866  25.656  1.00 53.16  ?  -19 ARG B CZ    1 
ATOM   1820 N  NH1   . ARG B 1 20  ? 8.788   -1.522  25.600  1.00 54.99  ?  -19 ARG B NH1   1 
ATOM   1821 N  NH2   . ARG B 1 20  ? 7.625   0.401   26.036  1.00 52.87  ?  -19 ARG B NH2   1 
ATOM   1822 N  N     . ASP B 1 21  ? 4.114   -0.416  20.549  1.00 60.18  ?  -18 ASP B N     1 
ATOM   1823 C  CA    . ASP B 1 21  ? 3.734   0.842   19.921  1.00 61.46  ?  -18 ASP B CA    1 
ATOM   1824 C  C     . ASP B 1 21  ? 2.455   0.674   19.110  1.00 62.85  ?  -18 ASP B C     1 
ATOM   1825 O  O     . ASP B 1 21  ? 1.525   1.484   19.225  1.00 62.78  ?  -18 ASP B O     1 
ATOM   1826 C  CB    . ASP B 1 21  ? 4.872   1.374   19.050  1.00 59.70  ?  -18 ASP B CB    1 
ATOM   1827 C  CG    . ASP B 1 21  ? 4.483   2.651   18.314  1.00 64.18  ?  -18 ASP B CG    1 
ATOM   1828 O  OD1   . ASP B 1 21  ? 3.832   3.499   18.970  1.00 63.16  ?  -18 ASP B OD1   1 
ATOM   1829 O  OD2   . ASP B 1 21  ? 4.804   2.798   17.098  1.00 64.65  ?  -18 ASP B OD2   1 
ATOM   1830 N  N     . ALA B 1 22  ? 2.381   -0.379  18.290  1.00 60.97  ?  -17 ALA B N     1 
ATOM   1831 C  CA    . ALA B 1 22  ? 1.164   -0.591  17.517  1.00 62.90  ?  -17 ALA B CA    1 
ATOM   1832 C  C     . ALA B 1 22  ? -0.022  -0.784  18.444  1.00 64.37  ?  -17 ALA B C     1 
ATOM   1833 O  O     . ALA B 1 22  ? -1.131  -0.319  18.146  1.00 64.86  ?  -17 ALA B O     1 
ATOM   1834 C  CB    . ALA B 1 22  ? 1.327   -1.785  16.577  1.00 63.01  ?  -17 ALA B CB    1 
ATOM   1835 N  N     . ALA B 1 23  ? 0.207   -1.434  19.588  1.00 64.79  ?  -16 ALA B N     1 
ATOM   1836 C  CA    . ALA B 1 23  ? -0.824  -1.541  20.615  1.00 68.20  ?  -16 ALA B CA    1 
ATOM   1837 C  C     . ALA B 1 23  ? -1.283  -0.164  21.071  1.00 67.65  ?  -16 ALA B C     1 
ATOM   1838 O  O     . ALA B 1 23  ? -2.483  0.139   21.052  1.00 68.68  ?  -16 ALA B O     1 
ATOM   1839 C  CB    . ALA B 1 23  ? -0.302  -2.351  21.803  1.00 68.40  ?  -16 ALA B CB    1 
ATOM   1840 N  N     . LEU B 1 24  ? -0.335  0.687   21.481  1.00 67.77  ?  -15 LEU B N     1 
ATOM   1841 C  CA    . LEU B 1 24  ? -0.689  2.013   21.982  1.00 63.40  ?  -15 LEU B CA    1 
ATOM   1842 C  C     . LEU B 1 24  ? -1.469  2.798   20.940  1.00 66.06  ?  -15 LEU B C     1 
ATOM   1843 O  O     . LEU B 1 24  ? -2.513  3.384   21.247  1.00 66.41  ?  -15 LEU B O     1 
ATOM   1844 C  CB    . LEU B 1 24  ? 0.573   2.772   22.397  1.00 60.02  ?  -15 LEU B CB    1 
ATOM   1845 C  CG    . LEU B 1 24  ? 0.401   4.098   23.150  1.00 62.97  ?  -15 LEU B CG    1 
ATOM   1846 C  CD1   . LEU B 1 24  ? 1.501   4.260   24.172  1.00 61.34  ?  -15 LEU B CD1   1 
ATOM   1847 C  CD2   . LEU B 1 24  ? 0.393   5.291   22.212  1.00 62.41  ?  -15 LEU B CD2   1 
ATOM   1848 N  N     . LYS B 1 25  ? -0.991  2.795   19.691  1.00 68.18  ?  -14 LYS B N     1 
ATOM   1849 C  CA    . LYS B 1 25  ? -1.643  3.586   18.653  1.00 65.56  ?  -14 LYS B CA    1 
ATOM   1850 C  C     . LYS B 1 25  ? -3.025  3.033   18.327  1.00 66.51  ?  -14 LYS B C     1 
ATOM   1851 O  O     . LYS B 1 25  ? -3.976  3.803   18.144  1.00 70.22  ?  -14 LYS B O     1 
ATOM   1852 C  CB    . LYS B 1 25  ? -0.768  3.643   17.394  1.00 62.14  ?  -14 LYS B CB    1 
ATOM   1853 C  CG    . LYS B 1 25  ? 0.672   4.132   17.615  1.00 61.62  ?  -14 LYS B CG    1 
ATOM   1854 C  CD    . LYS B 1 25  ? 0.700   5.586   18.043  1.00 61.94  ?  -14 LYS B CD    1 
ATOM   1855 C  CE    . LYS B 1 25  ? 1.943   6.327   17.563  1.00 57.08  ?  -14 LYS B CE    1 
ATOM   1856 N  NZ    . LYS B 1 25  ? 3.214   5.673   17.955  1.00 56.48  ?  -14 LYS B NZ    1 
ATOM   1857 N  N     . ARG B 1 26  ? -3.163  1.706   18.251  1.00 63.31  ?  -13 ARG B N     1 
ATOM   1858 C  CA    . ARG B 1 26  ? -4.468  1.137   17.924  1.00 68.66  ?  -13 ARG B CA    1 
ATOM   1859 C  C     . ARG B 1 26  ? -5.525  1.584   18.931  1.00 72.72  ?  -13 ARG B C     1 
ATOM   1860 O  O     . ARG B 1 26  ? -6.615  2.023   18.544  1.00 74.83  ?  -13 ARG B O     1 
ATOM   1861 C  CB    . ARG B 1 26  ? -4.377  -0.392  17.844  1.00 67.72  ?  -13 ARG B CB    1 
ATOM   1862 C  CG    . ARG B 1 26  ? -5.046  -1.002  16.596  1.00 67.39  ?  -13 ARG B CG    1 
ATOM   1863 C  CD    . ARG B 1 26  ? -4.224  -2.135  15.996  1.00 63.04  ?  -13 ARG B CD    1 
ATOM   1864 N  NE    . ARG B 1 26  ? -3.689  -2.989  17.054  1.00 71.38  ?  -13 ARG B NE    1 
ATOM   1865 C  CZ    . ARG B 1 26  ? -2.501  -3.588  17.009  1.00 68.49  ?  -13 ARG B CZ    1 
ATOM   1866 N  NH1   . ARG B 1 26  ? -2.082  -4.343  18.031  1.00 58.50  ?  -13 ARG B NH1   1 
ATOM   1867 N  NH2   . ARG B 1 26  ? -1.729  -3.430  15.934  1.00 66.75  ?  -13 ARG B NH2   1 
ATOM   1868 N  N     . ALA B 1 27  ? -5.190  1.541   20.226  1.00 72.37  ?  -12 ALA B N     1 
ATOM   1869 C  CA    . ALA B 1 27  ? -6.123  1.963   21.269  1.00 73.32  ?  -12 ALA B CA    1 
ATOM   1870 C  C     . ALA B 1 27  ? -6.493  3.438   21.147  1.00 79.49  ?  -12 ALA B C     1 
ATOM   1871 O  O     . ALA B 1 27  ? -7.654  3.809   21.360  1.00 83.43  ?  -12 ALA B O     1 
ATOM   1872 C  CB    . ALA B 1 27  ? -5.522  1.684   22.642  1.00 71.02  ?  -12 ALA B CB    1 
ATOM   1873 N  N     . GLU B 1 28  ? -5.524  4.299   20.819  1.00 76.58  ?  -11 GLU B N     1 
ATOM   1874 C  CA    . GLU B 1 28  ? -5.813  5.727   20.756  1.00 77.20  ?  -11 GLU B CA    1 
ATOM   1875 C  C     . GLU B 1 28  ? -6.802  6.080   19.649  1.00 85.24  ?  -11 GLU B C     1 
ATOM   1876 O  O     . GLU B 1 28  ? -7.412  7.153   19.717  1.00 89.36  ?  -11 GLU B O     1 
ATOM   1877 C  CB    . GLU B 1 28  ? -4.522  6.530   20.574  1.00 73.01  ?  -11 GLU B CB    1 
ATOM   1878 N  N     . GLU B 1 29  ? -6.984  5.212   18.639  1.00 87.46  ?  -10 GLU B N     1 
ATOM   1879 C  CA    . GLU B 1 29  ? -7.938  5.510   17.569  1.00 90.49  ?  -10 GLU B CA    1 
ATOM   1880 C  C     . GLU B 1 29  ? -9.319  5.816   18.141  1.00 95.54  ?  -10 GLU B C     1 
ATOM   1881 O  O     . GLU B 1 29  ? -10.051 6.664   17.612  1.00 97.53  ?  -10 GLU B O     1 
ATOM   1882 C  CB    . GLU B 1 29  ? -8.024  4.347   16.572  1.00 86.67  ?  -10 GLU B CB    1 
ATOM   1883 C  CG    . GLU B 1 29  ? -9.331  4.346   15.756  1.00 93.48  ?  -10 GLU B CG    1 
ATOM   1884 C  CD    . GLU B 1 29  ? -9.323  3.409   14.546  1.00 98.30  ?  -10 GLU B CD    1 
ATOM   1885 O  OE1   . GLU B 1 29  ? -10.426 3.028   14.095  1.00 97.97  ?  -10 GLU B OE1   1 
ATOM   1886 O  OE2   . GLU B 1 29  ? -8.232  3.065   14.035  1.00 94.47  ?  -10 GLU B OE2   1 
ATOM   1887 N  N     . GLU B 1 30  ? -9.678  5.145   19.231  1.00 94.59  ?  -9  GLU B N     1 
ATOM   1888 C  CA    . GLU B 1 30  ? -10.894 5.436   19.982  1.00 96.49  ?  -9  GLU B CA    1 
ATOM   1889 C  C     . GLU B 1 30  ? -11.097 6.935   20.221  1.00 94.67  ?  -9  GLU B C     1 
ATOM   1890 O  O     . GLU B 1 30  ? -11.850 7.332   21.109  1.00 90.40  ?  -9  GLU B O     1 
ATOM   1891 C  CB    . GLU B 1 30  ? -10.842 4.715   21.316  1.00 96.37  ?  -9  GLU B CB    1 
ATOM   1892 C  CG    . GLU B 1 30  ? -11.741 3.506   21.418  1.00 101.82 ?  -9  GLU B CG    1 
ATOM   1893 C  CD    . GLU B 1 30  ? -11.687 2.925   22.815  1.00 101.31 ?  -9  GLU B CD    1 
ATOM   1894 O  OE1   . GLU B 1 30  ? -10.582 2.502   23.227  1.00 95.23  ?  -9  GLU B OE1   1 
ATOM   1895 O  OE2   . GLU B 1 30  ? -12.733 2.913   23.502  1.00 100.13 ?  -9  GLU B OE2   1 
ATOM   1896 N  N     . TYR B 1 44  ? -4.991  9.861   27.250  1.00 89.82  ?  -8  TYR B N     1 
ATOM   1897 C  CA    . TYR B 1 44  ? -6.425  9.640   27.364  1.00 94.47  ?  -8  TYR B CA    1 
ATOM   1898 C  C     . TYR B 1 44  ? -7.193  10.693  26.563  1.00 93.07  ?  -8  TYR B C     1 
ATOM   1899 O  O     . TYR B 1 44  ? -7.992  10.347  25.688  1.00 94.18  ?  -8  TYR B O     1 
ATOM   1900 C  CB    . TYR B 1 44  ? -6.858  9.650   28.838  1.00 90.51  ?  -8  TYR B CB    1 
ATOM   1901 C  CG    . TYR B 1 44  ? -8.211  9.005   29.118  1.00 92.54  ?  -8  TYR B CG    1 
ATOM   1902 C  CD1   . TYR B 1 44  ? -9.279  9.149   28.233  1.00 90.94  ?  -8  TYR B CD1   1 
ATOM   1903 C  CD2   . TYR B 1 44  ? -8.422  8.265   30.278  1.00 93.14  ?  -8  TYR B CD2   1 
ATOM   1904 C  CE1   . TYR B 1 44  ? -10.506 8.580   28.486  1.00 90.20  ?  -8  TYR B CE1   1 
ATOM   1905 C  CE2   . TYR B 1 44  ? -9.656  7.694   30.545  1.00 94.13  ?  -8  TYR B CE2   1 
ATOM   1906 C  CZ    . TYR B 1 44  ? -10.695 7.855   29.642  1.00 93.77  ?  -8  TYR B CZ    1 
ATOM   1907 O  OH    . TYR B 1 44  ? -11.928 7.289   29.894  1.00 95.15  ?  -8  TYR B OH    1 
ATOM   1908 N  N     . ASP B 1 45  ? -6.968  11.975  26.853  1.00 87.42  ?  -7  ASP B N     1 
ATOM   1909 C  CA    . ASP B 1 45  ? -7.734  13.021  26.190  1.00 89.69  ?  -7  ASP B CA    1 
ATOM   1910 C  C     . ASP B 1 45  ? -6.937  13.814  25.158  1.00 91.18  ?  -7  ASP B C     1 
ATOM   1911 O  O     . ASP B 1 45  ? -7.527  14.646  24.457  1.00 89.57  ?  -7  ASP B O     1 
ATOM   1912 C  CB    . ASP B 1 45  ? -8.348  13.957  27.239  1.00 87.67  ?  -7  ASP B CB    1 
ATOM   1913 C  CG    . ASP B 1 45  ? -9.426  13.260  28.071  1.00 90.29  ?  -7  ASP B CG    1 
ATOM   1914 O  OD1   . ASP B 1 45  ? -9.065  12.441  28.941  1.00 91.02  ?  -7  ASP B OD1   1 
ATOM   1915 O  OD2   . ASP B 1 45  ? -10.633 13.531  27.869  1.00 90.12  ?  -7  ASP B OD2   1 
ATOM   1916 N  N     . TYR B 1 46  ? -5.626  13.574  25.049  1.00 89.52  ?  -6  TYR B N     1 
ATOM   1917 C  CA    . TYR B 1 46  ? -4.781  13.952  23.918  1.00 81.72  ?  -6  TYR B CA    1 
ATOM   1918 C  C     . TYR B 1 46  ? -3.534  13.074  23.987  1.00 75.75  ?  -6  TYR B C     1 
ATOM   1919 O  O     . TYR B 1 46  ? -3.037  12.791  25.081  1.00 71.67  ?  -6  TYR B O     1 
ATOM   1920 C  CB    . TYR B 1 46  ? -4.369  15.434  23.936  1.00 82.04  ?  -6  TYR B CB    1 
ATOM   1921 C  CG    . TYR B 1 46  ? -5.400  16.420  23.414  1.00 90.86  ?  -6  TYR B CG    1 
ATOM   1922 C  CD1   . TYR B 1 46  ? -5.569  17.671  24.024  1.00 92.24  ?  -6  TYR B CD1   1 
ATOM   1923 C  CD2   . TYR B 1 46  ? -6.196  16.116  22.313  1.00 92.02  ?  -6  TYR B CD2   1 
ATOM   1924 C  CE1   . TYR B 1 46  ? -6.510  18.581  23.558  1.00 91.40  ?  -6  TYR B CE1   1 
ATOM   1925 C  CE2   . TYR B 1 46  ? -7.141  17.020  21.841  1.00 95.37  ?  -6  TYR B CE2   1 
ATOM   1926 C  CZ    . TYR B 1 46  ? -7.292  18.247  22.466  1.00 97.08  ?  -6  TYR B CZ    1 
ATOM   1927 O  OH    . TYR B 1 46  ? -8.229  19.134  21.991  1.00 100.18 ?  -6  TYR B OH    1 
ATOM   1928 N  N     . LEU B 1 47  ? -3.036  12.636  22.831  1.00 73.00  ?  -5  LEU B N     1 
ATOM   1929 C  CA    . LEU B 1 47  ? -1.806  11.850  22.768  1.00 67.06  ?  -5  LEU B CA    1 
ATOM   1930 C  C     . LEU B 1 47  ? -0.690  12.747  22.252  1.00 66.46  ?  -5  LEU B C     1 
ATOM   1931 O  O     . LEU B 1 47  ? -0.678  13.111  21.073  1.00 69.67  ?  -5  LEU B O     1 
ATOM   1932 C  CB    . LEU B 1 47  ? -1.968  10.621  21.879  1.00 65.38  ?  -5  LEU B CB    1 
ATOM   1933 C  CG    . LEU B 1 47  ? -0.809  9.622   21.966  1.00 62.06  ?  -5  LEU B CG    1 
ATOM   1934 C  CD1   . LEU B 1 47  ? -0.563  9.235   23.403  1.00 64.23  ?  -5  LEU B CD1   1 
ATOM   1935 C  CD2   . LEU B 1 47  ? -1.085  8.385   21.140  1.00 62.22  ?  -5  LEU B CD2   1 
ATOM   1936 N  N     . ILE B 1 48  ? 0.245   13.101  23.127  1.00 67.10  ?  -4  ILE B N     1 
ATOM   1937 C  CA    . ILE B 1 48  ? 1.386   13.935  22.766  1.00 64.93  ?  -4  ILE B CA    1 
ATOM   1938 C  C     . ILE B 1 48  ? 2.624   13.048  22.749  1.00 62.34  ?  -4  ILE B C     1 
ATOM   1939 O  O     . ILE B 1 48  ? 2.949   12.407  23.756  1.00 61.24  ?  -4  ILE B O     1 
ATOM   1940 C  CB    . ILE B 1 48  ? 1.554   15.118  23.732  1.00 64.93  ?  -4  ILE B CB    1 
ATOM   1941 C  CG1   . ILE B 1 48  ? 0.290   15.985  23.743  1.00 66.40  ?  -4  ILE B CG1   1 
ATOM   1942 C  CG2   . ILE B 1 48  ? 2.764   15.956  23.342  1.00 63.67  ?  -4  ILE B CG2   1 
ATOM   1943 C  CD1   . ILE B 1 48  ? -0.251  16.318  22.359  1.00 68.41  ?  -4  ILE B CD1   1 
ATOM   1944 N  N     . LYS B 1 49  ? 3.301   13.001  21.604  1.00 59.82  ?  -3  LYS B N     1 
ATOM   1945 C  CA    . LYS B 1 49  ? 4.502   12.202  21.412  1.00 57.15  ?  -3  LYS B CA    1 
ATOM   1946 C  C     . LYS B 1 49  ? 5.696   13.113  21.202  1.00 58.03  ?  -3  LYS B C     1 
ATOM   1947 O  O     . LYS B 1 49  ? 5.604   14.093  20.462  1.00 58.34  ?  -3  LYS B O     1 
ATOM   1948 C  CB    . LYS B 1 49  ? 4.360   11.292  20.193  1.00 53.60  ?  -3  LYS B CB    1 
ATOM   1949 C  CG    . LYS B 1 49  ? 3.028   10.561  20.129  1.00 57.08  ?  -3  LYS B CG    1 
ATOM   1950 C  CD    . LYS B 1 49  ? 2.779   9.945   18.759  1.00 60.36  ?  -3  LYS B CD    1 
ATOM   1951 C  CE    . LYS B 1 49  ? 2.270   10.978  17.755  1.00 62.84  ?  -3  LYS B CE    1 
ATOM   1952 N  NZ    . LYS B 1 49  ? 2.277   10.456  16.360  1.00 56.82  ?  -3  LYS B NZ    1 
ATOM   1953 N  N     . PHE B 1 50  ? 6.821   12.802  21.845  1.00 55.12  ?  -2  PHE B N     1 
ATOM   1954 C  CA    . PHE B 1 50  ? 8.067   13.436  21.439  1.00 53.87  ?  -2  PHE B CA    1 
ATOM   1955 C  C     . PHE B 1 50  ? 9.209   12.450  21.594  1.00 49.80  ?  -2  PHE B C     1 
ATOM   1956 O  O     . PHE B 1 50  ? 9.029   11.320  22.050  1.00 51.84  ?  -2  PHE B O     1 
ATOM   1957 C  CB    . PHE B 1 50  ? 8.344   14.745  22.187  1.00 58.10  ?  -2  PHE B CB    1 
ATOM   1958 C  CG    . PHE B 1 50  ? 8.025   14.714  23.625  1.00 58.56  ?  -2  PHE B CG    1 
ATOM   1959 C  CD1   . PHE B 1 50  ? 6.824   15.222  24.084  1.00 63.01  ?  -2  PHE B CD1   1 
ATOM   1960 C  CD2   . PHE B 1 50  ? 8.942   14.208  24.536  1.00 61.34  ?  -2  PHE B CD2   1 
ATOM   1961 C  CE1   . PHE B 1 50  ? 6.528   15.207  25.443  1.00 68.09  ?  -2  PHE B CE1   1 
ATOM   1962 C  CE2   . PHE B 1 50  ? 8.664   14.179  25.900  1.00 63.15  ?  -2  PHE B CE2   1 
ATOM   1963 C  CZ    . PHE B 1 50  ? 7.454   14.681  26.358  1.00 69.39  ?  -2  PHE B CZ    1 
ATOM   1964 N  N     . LEU B 1 51  ? 10.389  12.877  21.163  1.00 47.81  ?  -1  LEU B N     1 
ATOM   1965 C  CA    . LEU B 1 51  ? 11.498  11.969  20.939  1.00 47.90  ?  -1  LEU B CA    1 
ATOM   1966 C  C     . LEU B 1 51  ? 12.776  12.602  21.462  1.00 47.97  ?  -1  LEU B C     1 
ATOM   1967 O  O     . LEU B 1 51  ? 13.033  13.784  21.220  1.00 49.97  ?  -1  LEU B O     1 
ATOM   1968 C  CB    . LEU B 1 51  ? 11.637  11.648  19.439  1.00 46.83  ?  -1  LEU B CB    1 
ATOM   1969 C  CG    . LEU B 1 51  ? 12.728  10.674  19.019  1.00 45.56  ?  -1  LEU B CG    1 
ATOM   1970 C  CD1   . LEU B 1 51  ? 12.284  9.911   17.785  1.00 49.64  ?  -1  LEU B CD1   1 
ATOM   1971 C  CD2   . LEU B 1 51  ? 14.025  11.408  18.733  1.00 48.27  ?  -1  LEU B CD2   1 
ATOM   1972 N  N     . ALA B 1 52  ? 13.586  11.813  22.152  1.00 42.78  ?  0   ALA B N     1 
ATOM   1973 C  CA    . ALA B 1 52  ? 14.864  12.283  22.655  1.00 46.95  ?  0   ALA B CA    1 
ATOM   1974 C  C     . ALA B 1 52  ? 15.972  11.740  21.771  1.00 44.98  ?  0   ALA B C     1 
ATOM   1975 O  O     . ALA B 1 52  ? 15.933  10.579  21.351  1.00 45.82  ?  0   ALA B O     1 
ATOM   1976 C  CB    . ALA B 1 52  ? 15.078  11.850  24.114  1.00 45.07  ?  0   ALA B CB    1 
ATOM   1977 N  N     . LEU B 1 53  ? 16.964  12.578  21.489  1.00 45.05  ?  1   LEU B N     1 
ATOM   1978 C  CA    . LEU B 1 53  ? 18.051  12.151  20.622  1.00 50.48  ?  1   LEU B CA    1 
ATOM   1979 C  C     . LEU B 1 53  ? 19.317  12.901  21.002  1.00 45.98  ?  1   LEU B C     1 
ATOM   1980 O  O     . LEU B 1 53  ? 19.282  13.910  21.707  1.00 47.08  ?  1   LEU B O     1 
ATOM   1981 C  CB    . LEU B 1 53  ? 17.706  12.349  19.130  1.00 49.01  ?  1   LEU B CB    1 
ATOM   1982 C  CG    . LEU B 1 53  ? 17.743  13.762  18.551  1.00 44.65  ?  1   LEU B CG    1 
ATOM   1983 C  CD1   . LEU B 1 53  ? 17.772  13.661  17.066  1.00 53.12  ?  1   LEU B CD1   1 
ATOM   1984 C  CD2   . LEU B 1 53  ? 16.543  14.592  18.976  1.00 47.51  ?  1   LEU B CD2   1 
ATOM   1985 N  N     . GLY B 1 54  ? 20.433  12.396  20.509  1.00 46.74  ?  2   GLY B N     1 
ATOM   1986 C  CA    . GLY B 1 54  ? 21.739  12.904  20.867  1.00 43.55  ?  2   GLY B CA    1 
ATOM   1987 C  C     . GLY B 1 54  ? 22.737  11.773  20.866  1.00 42.42  ?  2   GLY B C     1 
ATOM   1988 O  O     . GLY B 1 54  ? 22.381  10.609  20.777  1.00 48.00  ?  2   GLY B O     1 
ATOM   1989 N  N     . ASP B 1 55  ? 24.010  12.140  20.976  1.00 43.98  ?  3   ASP B N     1 
ATOM   1990 C  CA    . ASP B 1 55  ? 25.075  11.154  20.895  1.00 46.27  ?  3   ASP B CA    1 
ATOM   1991 C  C     . ASP B 1 55  ? 24.885  10.084  21.966  1.00 51.14  ?  3   ASP B C     1 
ATOM   1992 O  O     . ASP B 1 55  ? 24.236  10.300  22.994  1.00 49.68  ?  3   ASP B O     1 
ATOM   1993 C  CB    . ASP B 1 55  ? 26.442  11.831  21.048  1.00 48.89  ?  3   ASP B CB    1 
ATOM   1994 C  CG    . ASP B 1 55  ? 26.935  12.483  19.754  1.00 52.73  ?  3   ASP B CG    1 
ATOM   1995 O  OD1   . ASP B 1 55  ? 26.110  12.818  18.864  1.00 53.16  ?  3   ASP B OD1   1 
ATOM   1996 O  OD2   . ASP B 1 55  ? 28.165  12.663  19.626  1.00 54.57  ?  3   ASP B OD2   1 
ATOM   1997 N  N     . SER B 1 56  ? 25.435  8.900   21.708  1.00 49.76  ?  4   SER B N     1 
ATOM   1998 C  CA    . SER B 1 56  ? 25.384  7.866   22.722  1.00 51.55  ?  4   SER B CA    1 
ATOM   1999 C  C     . SER B 1 56  ? 26.125  8.335   23.974  1.00 52.86  ?  4   SER B C     1 
ATOM   2000 O  O     . SER B 1 56  ? 27.168  8.998   23.888  1.00 51.46  ?  4   SER B O     1 
ATOM   2001 C  CB    . SER B 1 56  ? 25.973  6.563   22.188  1.00 52.71  ?  4   SER B CB    1 
ATOM   2002 O  OG    . SER B 1 56  ? 25.701  5.479   23.091  1.00 55.27  ?  4   SER B OG    1 
ATOM   2003 N  N     . GLY B 1 57  ? 25.527  8.057   25.142  1.00 54.32  ?  5   GLY B N     1 
ATOM   2004 C  CA    . GLY B 1 57  ? 26.106  8.400   26.423  1.00 48.93  ?  5   GLY B CA    1 
ATOM   2005 C  C     . GLY B 1 57  ? 25.809  9.788   26.935  1.00 49.37  ?  5   GLY B C     1 
ATOM   2006 O  O     . GLY B 1 57  ? 26.420  10.203  27.925  1.00 55.98  ?  5   GLY B O     1 
ATOM   2007 N  N     . VAL B 1 58  ? 24.901  10.531  26.307  1.00 49.84  ?  6   VAL B N     1 
ATOM   2008 C  CA    . VAL B 1 58  ? 24.606  11.852  26.847  1.00 50.71  ?  6   VAL B CA    1 
ATOM   2009 C  C     . VAL B 1 58  ? 23.562  11.780  27.947  1.00 47.62  ?  6   VAL B C     1 
ATOM   2010 O  O     . VAL B 1 58  ? 23.459  12.713  28.743  1.00 47.15  ?  6   VAL B O     1 
ATOM   2011 C  CB    . VAL B 1 58  ? 24.143  12.825  25.753  1.00 49.12  ?  6   VAL B CB    1 
ATOM   2012 C  CG1   . VAL B 1 58  ? 25.233  12.995  24.721  1.00 49.18  ?  6   VAL B CG1   1 
ATOM   2013 C  CG2   . VAL B 1 58  ? 22.844  12.345  25.113  1.00 46.20  ?  6   VAL B CG2   1 
ATOM   2014 N  N     . GLY B 1 59  ? 22.793  10.696  28.017  1.00 48.50  ?  7   GLY B N     1 
ATOM   2015 C  CA    . GLY B 1 59  ? 21.849  10.510  29.095  1.00 41.39  ?  7   GLY B CA    1 
ATOM   2016 C  C     . GLY B 1 59  ? 20.400  10.545  28.675  1.00 42.90  ?  7   GLY B C     1 
ATOM   2017 O  O     . GLY B 1 59  ? 19.539  10.904  29.472  1.00 46.99  ?  7   GLY B O     1 
ATOM   2018 N  N     . LYS B 1 60  ? 20.102  10.179  27.432  1.00 47.30  ?  8   LYS B N     1 
ATOM   2019 C  CA    . LYS B 1 60  ? 18.721  10.259  26.969  1.00 47.24  ?  8   LYS B CA    1 
ATOM   2020 C  C     . LYS B 1 60  ? 17.824  9.350   27.798  1.00 42.46  ?  8   LYS B C     1 
ATOM   2021 O  O     . LYS B 1 60  ? 16.757  9.760   28.268  1.00 44.26  ?  8   LYS B O     1 
ATOM   2022 C  CB    . LYS B 1 60  ? 18.639  9.886   25.480  1.00 47.11  ?  8   LYS B CB    1 
ATOM   2023 C  CG    . LYS B 1 60  ? 19.475  10.771  24.546  1.00 48.03  ?  8   LYS B CG    1 
ATOM   2024 C  CD    . LYS B 1 60  ? 19.588  10.189  23.133  1.00 45.33  ?  8   LYS B CD    1 
ATOM   2025 C  CE    . LYS B 1 60  ? 20.463  8.936   23.084  1.00 45.36  ?  8   LYS B CE    1 
ATOM   2026 N  NZ    . LYS B 1 60  ? 21.931  9.242   23.052  1.00 42.91  ?  8   LYS B NZ    1 
ATOM   2027 N  N     . THR B 1 61  ? 18.227  8.092   27.938  1.00 41.36  ?  9   THR B N     1 
ATOM   2028 C  CA    . THR B 1 61  ? 17.461  7.121   28.701  1.00 45.26  ?  9   THR B CA    1 
ATOM   2029 C  C     . THR B 1 61  ? 17.372  7.543   30.168  1.00 45.72  ?  9   THR B C     1 
ATOM   2030 O  O     . THR B 1 61  ? 16.285  7.574   30.760  1.00 44.32  ?  9   THR B O     1 
ATOM   2031 C  CB    . THR B 1 61  ? 18.139  5.752   28.542  1.00 46.00  ?  9   THR B CB    1 
ATOM   2032 O  OG1   . THR B 1 61  ? 18.242  5.431   27.144  1.00 46.43  ?  9   THR B OG1   1 
ATOM   2033 C  CG2   . THR B 1 61  ? 17.402  4.649   29.277  1.00 41.25  ?  9   THR B CG2   1 
ATOM   2034 N  N     . SER B 1 62  ? 18.515  7.904   30.760  1.00 46.62  ?  10  SER B N     1 
ATOM   2035 C  CA    . SER B 1 62  ? 18.538  8.384   32.140  1.00 43.74  ?  10  SER B CA    1 
ATOM   2036 C  C     . SER B 1 62  ? 17.566  9.536   32.340  1.00 47.86  ?  10  SER B C     1 
ATOM   2037 O  O     . SER B 1 62  ? 16.850  9.583   33.348  1.00 52.00  ?  10  SER B O     1 
ATOM   2038 C  CB    . SER B 1 62  ? 19.952  8.823   32.521  1.00 40.94  ?  10  SER B CB    1 
ATOM   2039 O  OG    . SER B 1 62  ? 20.832  7.715   32.590  1.00 41.66  ?  10  SER B OG    1 
ATOM   2040 N  N     . VAL B 1 63  ? 17.520  10.471  31.393  1.00 45.01  ?  11  VAL B N     1 
ATOM   2041 C  CA    . VAL B 1 63  ? 16.691  11.663  31.570  1.00 46.46  ?  11  VAL B CA    1 
ATOM   2042 C  C     . VAL B 1 63  ? 15.221  11.272  31.635  1.00 47.27  ?  11  VAL B C     1 
ATOM   2043 O  O     . VAL B 1 63  ? 14.472  11.742  32.500  1.00 46.05  ?  11  VAL B O     1 
ATOM   2044 C  CB    . VAL B 1 63  ? 16.960  12.678  30.440  1.00 46.28  ?  11  VAL B CB    1 
ATOM   2045 C  CG1   . VAL B 1 63  ? 15.810  13.674  30.299  1.00 43.99  ?  11  VAL B CG1   1 
ATOM   2046 C  CG2   . VAL B 1 63  ? 18.245  13.411  30.688  1.00 44.90  ?  11  VAL B CG2   1 
ATOM   2047 N  N     . LEU B 1 64  ? 14.788  10.399  30.719  1.00 46.91  ?  12  LEU B N     1 
ATOM   2048 C  CA    . LEU B 1 64  ? 13.388  9.986   30.700  1.00 49.02  ?  12  LEU B CA    1 
ATOM   2049 C  C     . LEU B 1 64  ? 13.029  9.179   31.937  1.00 48.68  ?  12  LEU B C     1 
ATOM   2050 O  O     . LEU B 1 64  ? 11.893  9.254   32.417  1.00 49.26  ?  12  LEU B O     1 
ATOM   2051 C  CB    . LEU B 1 64  ? 13.094  9.169   29.446  1.00 47.00  ?  12  LEU B CB    1 
ATOM   2052 C  CG    . LEU B 1 64  ? 13.341  9.836   28.095  1.00 47.92  ?  12  LEU B CG    1 
ATOM   2053 C  CD1   . LEU B 1 64  ? 12.702  8.976   27.029  1.00 51.96  ?  12  LEU B CD1   1 
ATOM   2054 C  CD2   . LEU B 1 64  ? 12.749  11.243  28.041  1.00 47.02  ?  12  LEU B CD2   1 
ATOM   2055 N  N     . TYR B 1 65  ? 13.976  8.394   32.450  1.00 46.46  ?  13  TYR B N     1 
ATOM   2056 C  CA    . TYR B 1 65  ? 13.725  7.552   33.614  1.00 49.51  ?  13  TYR B CA    1 
ATOM   2057 C  C     . TYR B 1 65  ? 13.585  8.405   34.872  1.00 49.92  ?  13  TYR B C     1 
ATOM   2058 O  O     . TYR B 1 65  ? 12.639  8.240   35.653  1.00 49.17  ?  13  TYR B O     1 
ATOM   2059 C  CB    . TYR B 1 65  ? 14.869  6.547   33.740  1.00 46.93  ?  13  TYR B CB    1 
ATOM   2060 C  CG    . TYR B 1 65  ? 14.689  5.496   34.790  1.00 48.95  ?  13  TYR B CG    1 
ATOM   2061 C  CD1   . TYR B 1 65  ? 13.441  4.938   35.034  1.00 53.23  ?  13  TYR B CD1   1 
ATOM   2062 C  CD2   . TYR B 1 65  ? 15.778  5.040   35.531  1.00 45.49  ?  13  TYR B CD2   1 
ATOM   2063 C  CE1   . TYR B 1 65  ? 13.271  3.953   36.012  1.00 54.16  ?  13  TYR B CE1   1 
ATOM   2064 C  CE2   . TYR B 1 65  ? 15.628  4.072   36.503  1.00 47.31  ?  13  TYR B CE2   1 
ATOM   2065 C  CZ    . TYR B 1 65  ? 14.371  3.527   36.747  1.00 54.23  ?  13  TYR B CZ    1 
ATOM   2066 O  OH    . TYR B 1 65  ? 14.209  2.550   37.716  1.00 53.61  ?  13  TYR B OH    1 
ATOM   2067 N  N     . GLN B 1 66  ? 14.513  9.340   35.072  1.00 47.16  ?  14  GLN B N     1 
ATOM   2068 C  CA    . GLN B 1 66  ? 14.370  10.311  36.142  1.00 46.75  ?  14  GLN B CA    1 
ATOM   2069 C  C     . GLN B 1 66  ? 13.002  10.980  36.101  1.00 47.81  ?  14  GLN B C     1 
ATOM   2070 O  O     . GLN B 1 66  ? 12.386  11.231  37.142  1.00 51.74  ?  14  GLN B O     1 
ATOM   2071 C  CB    . GLN B 1 66  ? 15.489  11.346  36.039  1.00 46.19  ?  14  GLN B CB    1 
ATOM   2072 C  CG    . GLN B 1 66  ? 15.435  12.461  37.092  1.00 49.66  ?  14  GLN B CG    1 
ATOM   2073 C  CD    . GLN B 1 66  ? 15.689  11.966  38.517  1.00 49.55  ?  14  GLN B CD    1 
ATOM   2074 O  OE1   . GLN B 1 66  ? 14.788  12.004  39.353  1.00 50.44  ?  14  GLN B OE1   1 
ATOM   2075 N  NE2   . GLN B 1 66  ? 16.912  11.502  38.796  1.00 44.29  ?  14  GLN B NE2   1 
ATOM   2076 N  N     . TYR B 1 67  ? 12.485  11.236  34.913  1.00 49.49  ?  15  TYR B N     1 
ATOM   2077 C  CA    . TYR B 1 67  ? 11.267  12.032  34.839  1.00 50.86  ?  15  TYR B CA    1 
ATOM   2078 C  C     . TYR B 1 67  ? 10.010  11.191  35.044  1.00 49.30  ?  15  TYR B C     1 
ATOM   2079 O  O     . TYR B 1 67  ? 9.017   11.689  35.581  1.00 47.65  ?  15  TYR B O     1 
ATOM   2080 C  CB    . TYR B 1 67  ? 11.234  12.780  33.507  1.00 48.00  ?  15  TYR B CB    1 
ATOM   2081 C  CG    . TYR B 1 67  ? 9.911   13.396  33.160  1.00 48.92  ?  15  TYR B CG    1 
ATOM   2082 C  CD1   . TYR B 1 67  ? 9.528   14.622  33.694  1.00 49.28  ?  15  TYR B CD1   1 
ATOM   2083 C  CD2   . TYR B 1 67  ? 9.037   12.746  32.301  1.00 46.64  ?  15  TYR B CD2   1 
ATOM   2084 C  CE1   . TYR B 1 67  ? 8.298   15.184  33.376  1.00 51.75  ?  15  TYR B CE1   1 
ATOM   2085 C  CE2   . TYR B 1 67  ? 7.820   13.290  31.979  1.00 49.46  ?  15  TYR B CE2   1 
ATOM   2086 C  CZ    . TYR B 1 67  ? 7.451   14.505  32.507  1.00 54.46  ?  15  TYR B CZ    1 
ATOM   2087 O  OH    . TYR B 1 67  ? 6.224   15.025  32.157  1.00 54.46  ?  15  TYR B OH    1 
ATOM   2088 N  N     . THR B 1 68  ? 10.023  9.931   34.638  1.00 46.88  ?  16  THR B N     1 
ATOM   2089 C  CA    . THR B 1 68  ? 8.834   9.107   34.787  1.00 48.56  ?  16  THR B CA    1 
ATOM   2090 C  C     . THR B 1 68  ? 8.758   8.468   36.163  1.00 53.01  ?  16  THR B C     1 
ATOM   2091 O  O     . THR B 1 68  ? 7.655   8.265   36.695  1.00 47.94  ?  16  THR B O     1 
ATOM   2092 C  CB    . THR B 1 68  ? 8.820   8.004   33.722  1.00 48.56  ?  16  THR B CB    1 
ATOM   2093 O  OG1   . THR B 1 68  ? 10.082  7.320   33.742  1.00 53.13  ?  16  THR B OG1   1 
ATOM   2094 C  CG2   . THR B 1 68  ? 8.569   8.567   32.286  1.00 48.42  ?  16  THR B CG2   1 
ATOM   2095 N  N     . ASP B 1 69  ? 9.921   8.165   36.745  1.00 50.57  ?  17  ASP B N     1 
ATOM   2096 C  CA    . ASP B 1 69  ? 10.033  7.353   37.942  1.00 52.43  ?  17  ASP B CA    1 
ATOM   2097 C  C     . ASP B 1 69  ? 10.782  8.025   39.080  1.00 48.18  ?  17  ASP B C     1 
ATOM   2098 O  O     . ASP B 1 69  ? 10.766  7.488   40.187  1.00 47.66  ?  17  ASP B O     1 
ATOM   2099 C  CB    . ASP B 1 69  ? 10.752  6.029   37.630  1.00 49.97  ?  17  ASP B CB    1 
ATOM   2100 C  CG    . ASP B 1 69  ? 9.916   5.082   36.802  1.00 53.64  ?  17  ASP B CG    1 
ATOM   2101 O  OD1   . ASP B 1 69  ? 9.359   5.512   35.772  1.00 54.76  ?  17  ASP B OD1   1 
ATOM   2102 O  OD2   . ASP B 1 69  ? 9.818   3.897   37.179  1.00 60.06  ?  17  ASP B OD2   1 
ATOM   2103 N  N     . GLY B 1 70  ? 11.467  9.143   38.830  1.00 48.53  ?  18  GLY B N     1 
ATOM   2104 C  CA    . GLY B 1 70  ? 12.325  9.767   39.819  1.00 45.98  ?  18  GLY B CA    1 
ATOM   2105 C  C     . GLY B 1 70  ? 13.488  8.917   40.291  1.00 48.93  ?  18  GLY B C     1 
ATOM   2106 O  O     . GLY B 1 70  ? 13.893  9.026   41.453  1.00 48.53  ?  18  GLY B O     1 
ATOM   2107 N  N     . LYS B 1 71  ? 14.056  8.087   39.424  1.00 47.01  ?  19  LYS B N     1 
ATOM   2108 C  CA    . LYS B 1 71  ? 15.156  7.215   39.803  1.00 42.82  ?  19  LYS B CA    1 
ATOM   2109 C  C     . LYS B 1 71  ? 16.304  7.397   38.825  1.00 41.66  ?  19  LYS B C     1 
ATOM   2110 O  O     . LYS B 1 71  ? 16.124  7.939   37.742  1.00 45.04  ?  19  LYS B O     1 
ATOM   2111 C  CB    . LYS B 1 71  ? 14.705  5.754   39.836  1.00 47.03  ?  19  LYS B CB    1 
ATOM   2112 C  CG    . LYS B 1 71  ? 13.567  5.477   40.809  1.00 47.26  ?  19  LYS B CG    1 
ATOM   2113 C  CD    . LYS B 1 71  ? 13.202  4.008   40.773  1.00 46.68  ?  19  LYS B CD    1 
ATOM   2114 C  CE    . LYS B 1 71  ? 12.030  3.692   41.690  1.00 48.22  ?  19  LYS B CE    1 
ATOM   2115 N  NZ    . LYS B 1 71  ? 11.796  2.226   41.619  1.00 48.00  ?  19  LYS B NZ    1 
ATOM   2116 N  N     . PHE B 1 72  ? 17.493  6.948   39.218  1.00 41.48  ?  20  PHE B N     1 
ATOM   2117 C  CA    . PHE B 1 72  ? 18.691  7.113   38.406  1.00 38.32  ?  20  PHE B CA    1 
ATOM   2118 C  C     . PHE B 1 72  ? 19.589  5.921   38.646  1.00 44.01  ?  20  PHE B C     1 
ATOM   2119 O  O     . PHE B 1 72  ? 19.827  5.557   39.801  1.00 47.15  ?  20  PHE B O     1 
ATOM   2120 C  CB    . PHE B 1 72  ? 19.459  8.386   38.761  1.00 40.09  ?  20  PHE B CB    1 
ATOM   2121 C  CG    . PHE B 1 72  ? 20.809  8.498   38.074  1.00 42.17  ?  20  PHE B CG    1 
ATOM   2122 C  CD1   . PHE B 1 72  ? 20.895  8.745   36.714  1.00 43.93  ?  20  PHE B CD1   1 
ATOM   2123 C  CD2   . PHE B 1 72  ? 21.982  8.371   38.796  1.00 43.23  ?  20  PHE B CD2   1 
ATOM   2124 C  CE1   . PHE B 1 72  ? 22.129  8.847   36.078  1.00 43.88  ?  20  PHE B CE1   1 
ATOM   2125 C  CE2   . PHE B 1 72  ? 23.213  8.474   38.176  1.00 43.91  ?  20  PHE B CE2   1 
ATOM   2126 C  CZ    . PHE B 1 72  ? 23.290  8.714   36.809  1.00 44.86  ?  20  PHE B CZ    1 
ATOM   2127 N  N     . ASN B 1 73  ? 20.090  5.325   37.573  1.00 41.80  ?  21  ASN B N     1 
ATOM   2128 C  CA    . ASN B 1 73  ? 20.989  4.184   37.661  1.00 43.17  ?  21  ASN B CA    1 
ATOM   2129 C  C     . ASN B 1 73  ? 22.315  4.591   37.048  1.00 44.03  ?  21  ASN B C     1 
ATOM   2130 O  O     . ASN B 1 73  ? 22.358  5.026   35.896  1.00 49.32  ?  21  ASN B O     1 
ATOM   2131 C  CB    . ASN B 1 73  ? 20.397  2.965   36.958  1.00 45.68  ?  21  ASN B CB    1 
ATOM   2132 C  CG    . ASN B 1 73  ? 21.256  1.729   37.121  1.00 53.17  ?  21  ASN B CG    1 
ATOM   2133 O  OD1   . ASN B 1 73  ? 22.468  1.816   37.377  1.00 53.51  ?  21  ASN B OD1   1 
ATOM   2134 N  ND2   . ASN B 1 73  ? 20.635  0.564   36.981  1.00 56.22  ?  21  ASN B ND2   1 
ATOM   2135 N  N     . SER B 1 74  ? 23.389  4.470   37.814  1.00 44.26  ?  22  SER B N     1 
ATOM   2136 C  CA    . SER B 1 74  ? 24.650  5.046   37.366  1.00 46.72  ?  22  SER B CA    1 
ATOM   2137 C  C     . SER B 1 74  ? 25.428  4.118   36.444  1.00 50.26  ?  22  SER B C     1 
ATOM   2138 O  O     . SER B 1 74  ? 26.486  4.520   35.939  1.00 49.91  ?  22  SER B O     1 
ATOM   2139 C  CB    . SER B 1 74  ? 25.511  5.438   38.567  1.00 49.42  ?  22  SER B CB    1 
ATOM   2140 O  OG    . SER B 1 74  ? 25.989  4.292   39.232  1.00 51.90  ?  22  SER B OG    1 
ATOM   2141 N  N     . LYS B 1 75  ? 24.922  2.907   36.203  1.00 48.78  ?  23  LYS B N     1 
ATOM   2142 C  CA    . LYS B 1 75  ? 25.555  1.934   35.319  1.00 50.21  ?  23  LYS B CA    1 
ATOM   2143 C  C     . LYS B 1 75  ? 25.024  2.109   33.901  1.00 47.99  ?  23  LYS B C     1 
ATOM   2144 O  O     . LYS B 1 75  ? 23.806  2.150   33.695  1.00 45.46  ?  23  LYS B O     1 
ATOM   2145 C  CB    . LYS B 1 75  ? 25.277  0.510   35.800  1.00 46.81  ?  23  LYS B CB    1 
ATOM   2146 C  CG    . LYS B 1 75  ? 25.863  -0.553  34.907  1.00 53.74  ?  23  LYS B CG    1 
ATOM   2147 C  CD    . LYS B 1 75  ? 25.351  -1.943  35.255  1.00 56.01  ?  23  LYS B CD    1 
ATOM   2148 C  CE    . LYS B 1 75  ? 26.113  -2.991  34.449  1.00 55.63  ?  23  LYS B CE    1 
ATOM   2149 N  NZ    . LYS B 1 75  ? 25.215  -4.059  33.919  1.00 64.68  ?  23  LYS B NZ    1 
ATOM   2150 N  N     . PHE B 1 76  ? 25.936  2.188   32.931  1.00 46.48  ?  24  PHE B N     1 
ATOM   2151 C  CA    . PHE B 1 76  ? 25.590  2.503   31.542  1.00 50.68  ?  24  PHE B CA    1 
ATOM   2152 C  C     . PHE B 1 76  ? 25.009  1.265   30.866  1.00 50.48  ?  24  PHE B C     1 
ATOM   2153 O  O     . PHE B 1 76  ? 25.706  0.266   30.675  1.00 50.73  ?  24  PHE B O     1 
ATOM   2154 C  CB    . PHE B 1 76  ? 26.823  3.013   30.800  1.00 48.32  ?  24  PHE B CB    1 
ATOM   2155 C  CG    . PHE B 1 76  ? 26.585  3.316   29.351  1.00 49.96  ?  24  PHE B CG    1 
ATOM   2156 C  CD1   . PHE B 1 76  ? 25.370  3.817   28.918  1.00 52.08  ?  24  PHE B CD1   1 
ATOM   2157 C  CD2   . PHE B 1 76  ? 27.592  3.126   28.420  1.00 46.75  ?  24  PHE B CD2   1 
ATOM   2158 C  CE1   . PHE B 1 76  ? 25.154  4.082   27.566  1.00 52.27  ?  24  PHE B CE1   1 
ATOM   2159 C  CE2   . PHE B 1 76  ? 27.387  3.396   27.088  1.00 49.83  ?  24  PHE B CE2   1 
ATOM   2160 C  CZ    . PHE B 1 76  ? 26.166  3.880   26.655  1.00 48.39  ?  24  PHE B CZ    1 
ATOM   2161 N  N     . ILE B 1 77  ? 23.727  1.313   30.531  1.00 49.84  ?  25  ILE B N     1 
ATOM   2162 C  CA    . ILE B 1 77  ? 23.055  0.233   29.816  1.00 48.81  ?  25  ILE B CA    1 
ATOM   2163 C  C     . ILE B 1 77  ? 22.574  0.838   28.505  1.00 50.90  ?  25  ILE B C     1 
ATOM   2164 O  O     . ILE B 1 77  ? 21.477  1.411   28.420  1.00 49.40  ?  25  ILE B O     1 
ATOM   2165 C  CB    . ILE B 1 77  ? 21.899  -0.380  30.606  1.00 51.08  ?  25  ILE B CB    1 
ATOM   2166 C  CG1   . ILE B 1 77  ? 22.380  -0.938  31.950  1.00 53.58  ?  25  ILE B CG1   1 
ATOM   2167 C  CG2   . ILE B 1 77  ? 21.214  -1.454  29.777  1.00 48.90  ?  25  ILE B CG2   1 
ATOM   2168 C  CD1   . ILE B 1 77  ? 23.615  -1.802  31.878  1.00 54.41  ?  25  ILE B CD1   1 
ATOM   2169 N  N     . THR B 1 78  ? 23.399  0.700   27.467  1.00 54.41  ?  26  THR B N     1 
ATOM   2170 C  CA    . THR B 1 78  ? 23.137  1.349   26.194  1.00 47.90  ?  26  THR B CA    1 
ATOM   2171 C  C     . THR B 1 78  ? 21.862  0.818   25.552  1.00 45.95  ?  26  THR B C     1 
ATOM   2172 O  O     . THR B 1 78  ? 21.528  -0.364  25.657  1.00 50.64  ?  26  THR B O     1 
ATOM   2173 C  CB    . THR B 1 78  ? 24.317  1.153   25.259  1.00 48.99  ?  26  THR B CB    1 
ATOM   2174 O  OG1   . THR B 1 78  ? 24.208  2.106   24.200  1.00 49.07  ?  26  THR B OG1   1 
ATOM   2175 C  CG2   . THR B 1 78  ? 24.347  -0.274  24.689  1.00 42.84  ?  26  THR B CG2   1 
ATOM   2176 N  N     . THR B 1 79  ? 21.145  1.719   24.887  1.00 45.83  ?  27  THR B N     1 
ATOM   2177 C  CA    . THR B 1 79  ? 19.827  1.417   24.336  1.00 46.68  ?  27  THR B CA    1 
ATOM   2178 C  C     . THR B 1 79  ? 19.920  0.567   23.064  1.00 47.68  ?  27  THR B C     1 
ATOM   2179 O  O     . THR B 1 79  ? 20.638  0.907   22.118  1.00 45.98  ?  27  THR B O     1 
ATOM   2180 C  CB    . THR B 1 79  ? 19.102  2.726   24.050  1.00 44.40  ?  27  THR B CB    1 
ATOM   2181 O  OG1   . THR B 1 79  ? 19.014  3.480   25.267  1.00 49.10  ?  27  THR B OG1   1 
ATOM   2182 C  CG2   . THR B 1 79  ? 17.731  2.501   23.445  1.00 43.10  ?  27  THR B CG2   1 
ATOM   2183 N  N     . VAL B 1 80  ? 19.189  -0.544  23.051  1.00 48.17  ?  28  VAL B N     1 
ATOM   2184 C  CA    . VAL B 1 80  ? 19.183  -1.464  21.923  1.00 53.56  ?  28  VAL B CA    1 
ATOM   2185 C  C     . VAL B 1 80  ? 18.255  -0.893  20.859  1.00 53.04  ?  28  VAL B C     1 
ATOM   2186 O  O     . VAL B 1 80  ? 17.072  -1.246  20.784  1.00 52.83  ?  28  VAL B O     1 
ATOM   2187 C  CB    . VAL B 1 80  ? 18.766  -2.882  22.367  1.00 53.67  ?  28  VAL B CB    1 
ATOM   2188 C  CG1   . VAL B 1 80  ? 18.930  -3.872  21.240  1.00 53.98  ?  28  VAL B CG1   1 
ATOM   2189 C  CG2   . VAL B 1 80  ? 19.604  -3.327  23.572  1.00 50.57  ?  28  VAL B CG2   1 
ATOM   2190 N  N     . GLY B 1 81  ? 18.779  0.025   20.055  1.00 51.51  ?  29  GLY B N     1 
ATOM   2191 C  CA    . GLY B 1 81  ? 18.007  0.604   18.983  1.00 48.24  ?  29  GLY B CA    1 
ATOM   2192 C  C     . GLY B 1 81  ? 17.026  1.665   19.411  1.00 49.45  ?  29  GLY B C     1 
ATOM   2193 O  O     . GLY B 1 81  ? 17.260  2.855   19.198  1.00 51.56  ?  29  GLY B O     1 
ATOM   2194 N  N     . ILE B 1 82  ? 15.923  1.258   20.033  1.00 53.65  ?  30  ILE B N     1 
ATOM   2195 C  CA    . ILE B 1 82  ? 14.802  2.166   20.238  1.00 53.79  ?  30  ILE B CA    1 
ATOM   2196 C  C     . ILE B 1 82  ? 14.020  1.688   21.462  1.00 49.80  ?  30  ILE B C     1 
ATOM   2197 O  O     . ILE B 1 82  ? 14.039  0.502   21.799  1.00 51.52  ?  30  ILE B O     1 
ATOM   2198 C  CB    . ILE B 1 82  ? 13.949  2.230   18.941  1.00 50.85  ?  30  ILE B CB    1 
ATOM   2199 C  CG1   . ILE B 1 82  ? 12.902  3.333   19.004  1.00 52.27  ?  30  ILE B CG1   1 
ATOM   2200 C  CG2   . ILE B 1 82  ? 13.305  0.882   18.619  1.00 47.81  ?  30  ILE B CG2   1 
ATOM   2201 C  CD1   . ILE B 1 82  ? 13.485  4.704   18.832  1.00 53.11  ?  30  ILE B CD1   1 
ATOM   2202 N  N     . ASP B 1 83  ? 13.361  2.625   22.150  1.00 52.02  ?  31  ASP B N     1 
ATOM   2203 C  CA    . ASP B 1 83  ? 12.481  2.320   23.281  1.00 52.41  ?  31  ASP B CA    1 
ATOM   2204 C  C     . ASP B 1 83  ? 11.570  3.511   23.567  1.00 50.43  ?  31  ASP B C     1 
ATOM   2205 O  O     . ASP B 1 83  ? 11.712  4.591   22.986  1.00 51.52  ?  31  ASP B O     1 
ATOM   2206 C  CB    . ASP B 1 83  ? 13.264  1.953   24.538  1.00 44.76  ?  31  ASP B CB    1 
ATOM   2207 C  CG    . ASP B 1 83  ? 12.552  0.890   25.365  1.00 55.00  ?  31  ASP B CG    1 
ATOM   2208 O  OD1   . ASP B 1 83  ? 11.304  0.776   25.240  1.00 53.50  ?  31  ASP B OD1   1 
ATOM   2209 O  OD2   . ASP B 1 83  ? 13.232  0.162   26.133  1.00 59.72  ?  31  ASP B OD2   1 
ATOM   2210 N  N     . PHE B 1 84  ? 10.622  3.307   24.473  1.00 51.09  ?  32  PHE B N     1 
ATOM   2211 C  CA    . PHE B 1 84  ? 9.768   4.429   24.840  1.00 52.41  ?  32  PHE B CA    1 
ATOM   2212 C  C     . PHE B 1 84  ? 9.117   4.171   26.189  1.00 50.60  ?  32  PHE B C     1 
ATOM   2213 O  O     . PHE B 1 84  ? 8.894   3.023   26.576  1.00 52.10  ?  32  PHE B O     1 
ATOM   2214 C  CB    . PHE B 1 84  ? 8.702   4.703   23.770  1.00 49.23  ?  32  PHE B CB    1 
ATOM   2215 C  CG    . PHE B 1 84  ? 7.528   3.753   23.807  1.00 51.73  ?  32  PHE B CG    1 
ATOM   2216 C  CD1   . PHE B 1 84  ? 6.420   4.015   24.607  1.00 49.16  ?  32  PHE B CD1   1 
ATOM   2217 C  CD2   . PHE B 1 84  ? 7.513   2.622   22.994  1.00 53.41  ?  32  PHE B CD2   1 
ATOM   2218 C  CE1   . PHE B 1 84  ? 5.338   3.162   24.628  1.00 47.80  ?  32  PHE B CE1   1 
ATOM   2219 C  CE2   . PHE B 1 84  ? 6.430   1.763   22.998  1.00 53.53  ?  32  PHE B CE2   1 
ATOM   2220 C  CZ    . PHE B 1 84  ? 5.341   2.029   23.830  1.00 55.32  ?  32  PHE B CZ    1 
ATOM   2221 N  N     . ARG B 1 85  ? 8.819   5.260   26.889  1.00 51.36  ?  33  ARG B N     1 
ATOM   2222 C  CA    . ARG B 1 85  ? 8.095   5.271   28.149  1.00 52.77  ?  33  ARG B CA    1 
ATOM   2223 C  C     . ARG B 1 85  ? 6.822   6.081   27.956  1.00 50.41  ?  33  ARG B C     1 
ATOM   2224 O  O     . ARG B 1 85  ? 6.611   6.712   26.922  1.00 57.82  ?  33  ARG B O     1 
ATOM   2225 C  CB    . ARG B 1 85  ? 8.949   5.862   29.287  1.00 44.98  ?  33  ARG B CB    1 
ATOM   2226 C  CG    . ARG B 1 85  ? 10.393  5.382   29.305  1.00 43.48  ?  33  ARG B CG    1 
ATOM   2227 C  CD    . ARG B 1 85  ? 11.113  5.680   30.651  1.00 55.61  ?  33  ARG B CD    1 
ATOM   2228 N  NE    . ARG B 1 85  ? 10.558  4.912   31.774  1.00 55.38  ?  33  ARG B NE    1 
ATOM   2229 C  CZ    . ARG B 1 85  ? 11.122  3.827   32.294  1.00 53.77  ?  33  ARG B CZ    1 
ATOM   2230 N  NH1   . ARG B 1 85  ? 12.279  3.382   31.823  1.00 60.52  ?  33  ARG B NH1   1 
ATOM   2231 N  NH2   . ARG B 1 85  ? 10.533  3.183   33.287  1.00 55.26  ?  33  ARG B NH2   1 
ATOM   2232 N  N     . GLU B 1 86  ? 5.953   6.039   28.950  1.00 53.69  ?  34  GLU B N     1 
ATOM   2233 C  CA    . GLU B 1 86  ? 4.760   6.864   28.970  1.00 56.08  ?  34  GLU B CA    1 
ATOM   2234 C  C     . GLU B 1 86  ? 4.609   7.474   30.352  1.00 59.07  ?  34  GLU B C     1 
ATOM   2235 O  O     . GLU B 1 86  ? 5.231   7.042   31.325  1.00 58.15  ?  34  GLU B O     1 
ATOM   2236 C  CB    . GLU B 1 86  ? 3.490   6.076   28.642  1.00 55.51  ?  34  GLU B CB    1 
ATOM   2237 C  CG    . GLU B 1 86  ? 3.701   4.838   27.843  1.00 56.63  ?  34  GLU B CG    1 
ATOM   2238 C  CD    . GLU B 1 86  ? 2.400   4.114   27.601  1.00 63.38  ?  34  GLU B CD    1 
ATOM   2239 O  OE1   . GLU B 1 86  ? 1.355   4.796   27.478  1.00 65.02  ?  34  GLU B OE1   1 
ATOM   2240 O  OE2   . GLU B 1 86  ? 2.424   2.866   27.522  1.00 66.48  ?  34  GLU B OE2   1 
ATOM   2241 N  N     . LYS B 1 87  ? 3.748   8.477   30.426  1.00 58.97  ?  35  LYS B N     1 
ATOM   2242 C  CA    . LYS B 1 87  ? 3.443   9.131   31.681  1.00 57.07  ?  35  LYS B CA    1 
ATOM   2243 C  C     . LYS B 1 87  ? 2.194   9.965   31.473  1.00 61.64  ?  35  LYS B C     1 
ATOM   2244 O  O     . LYS B 1 87  ? 2.160   10.793  30.554  1.00 61.79  ?  35  LYS B O     1 
ATOM   2245 C  CB    . LYS B 1 87  ? 4.610   10.006  32.124  1.00 56.61  ?  35  LYS B CB    1 
ATOM   2246 C  CG    . LYS B 1 87  ? 4.437   10.568  33.511  1.00 58.10  ?  35  LYS B CG    1 
ATOM   2247 C  CD    . LYS B 1 87  ? 5.293   11.803  33.714  1.00 55.90  ?  35  LYS B CD    1 
ATOM   2248 C  CE    . LYS B 1 87  ? 5.385   12.176  35.184  1.00 57.25  ?  35  LYS B CE    1 
ATOM   2249 N  NZ    . LYS B 1 87  ? 6.809   12.113  35.639  1.00 55.14  ?  35  LYS B NZ    1 
ATOM   2250 N  N     . ARG B 1 88  ? 1.157   9.761   32.282  1.00 61.42  ?  36  ARG B N     1 
ATOM   2251 C  CA    . ARG B 1 88  ? -0.015  10.627  32.212  1.00 63.13  ?  36  ARG B CA    1 
ATOM   2252 C  C     . ARG B 1 88  ? 0.199   11.853  33.089  1.00 61.69  ?  36  ARG B C     1 
ATOM   2253 O  O     . ARG B 1 88  ? 0.580   11.732  34.257  1.00 59.79  ?  36  ARG B O     1 
ATOM   2254 C  CB    . ARG B 1 88  ? -1.281  9.870   32.602  1.00 64.34  ?  36  ARG B CB    1 
ATOM   2255 C  CG    . ARG B 1 88  ? -1.526  8.705   31.663  1.00 66.86  ?  36  ARG B CG    1 
ATOM   2256 C  CD    . ARG B 1 88  ? -2.334  7.559   32.278  1.00 74.82  ?  36  ARG B CD    1 
ATOM   2257 N  NE    . ARG B 1 88  ? -2.598  6.506   31.292  1.00 78.28  ?  36  ARG B NE    1 
ATOM   2258 C  CZ    . ARG B 1 88  ? -3.386  6.641   30.227  1.00 78.01  ?  36  ARG B CZ    1 
ATOM   2259 N  NH1   . ARG B 1 88  ? -3.545  5.620   29.393  1.00 80.48  ?  36  ARG B NH1   1 
ATOM   2260 N  NH2   . ARG B 1 88  ? -4.015  7.789   29.986  1.00 80.45  ?  36  ARG B NH2   1 
ATOM   2261 N  N     . VAL B 1 89  ? -0.001  13.032  32.500  1.00 60.68  ?  37  VAL B N     1 
ATOM   2262 C  CA    . VAL B 1 89  ? 0.255   14.311  33.138  1.00 60.59  ?  37  VAL B CA    1 
ATOM   2263 C  C     . VAL B 1 89  ? -0.928  15.227  32.869  1.00 67.87  ?  37  VAL B C     1 
ATOM   2264 O  O     . VAL B 1 89  ? -1.815  14.919  32.074  1.00 71.42  ?  37  VAL B O     1 
ATOM   2265 C  CB    . VAL B 1 89  ? 1.547   14.972  32.629  1.00 57.02  ?  37  VAL B CB    1 
ATOM   2266 C  CG1   . VAL B 1 89  ? 2.705   14.011  32.706  1.00 57.64  ?  37  VAL B CG1   1 
ATOM   2267 C  CG2   . VAL B 1 89  ? 1.348   15.489  31.215  1.00 64.36  ?  37  VAL B CG2   1 
ATOM   2268 N  N     . VAL B 1 90  ? -0.925  16.374  33.536  1.00 68.69  ?  38  VAL B N     1 
ATOM   2269 C  CA    . VAL B 1 90  ? -1.936  17.399  33.328  1.00 71.52  ?  38  VAL B CA    1 
ATOM   2270 C  C     . VAL B 1 90  ? -1.244  18.597  32.712  1.00 73.13  ?  38  VAL B C     1 
ATOM   2271 O  O     . VAL B 1 90  ? -0.249  19.095  33.255  1.00 75.00  ?  38  VAL B O     1 
ATOM   2272 C  CB    . VAL B 1 90  ? -2.637  17.788  34.636  1.00 72.97  ?  38  VAL B CB    1 
ATOM   2273 C  CG1   . VAL B 1 90  ? -3.632  18.926  34.396  1.00 75.52  ?  38  VAL B CG1   1 
ATOM   2274 C  CG2   . VAL B 1 90  ? -3.320  16.579  35.231  1.00 75.12  ?  38  VAL B CG2   1 
ATOM   2275 N  N     . TYR B 1 91  ? -1.752  19.053  31.581  1.00 73.36  ?  39  TYR B N     1 
ATOM   2276 C  CA    . TYR B 1 91  ? -1.221  20.247  30.951  1.00 77.03  ?  39  TYR B CA    1 
ATOM   2277 C  C     . TYR B 1 91  ? -2.182  21.394  31.191  1.00 83.05  ?  39  TYR B C     1 
ATOM   2278 O  O     . TYR B 1 91  ? -3.381  21.276  30.917  1.00 86.24  ?  39  TYR B O     1 
ATOM   2279 C  CB    . TYR B 1 91  ? -1.011  20.051  29.456  1.00 69.81  ?  39  TYR B CB    1 
ATOM   2280 C  CG    . TYR B 1 91  ? -0.704  21.341  28.721  1.00 74.52  ?  39  TYR B CG    1 
ATOM   2281 C  CD1   . TYR B 1 91  ? 0.571   21.883  28.740  1.00 72.83  ?  39  TYR B CD1   1 
ATOM   2282 C  CD2   . TYR B 1 91  ? -1.684  22.009  28.006  1.00 75.81  ?  39  TYR B CD2   1 
ATOM   2283 C  CE1   . TYR B 1 91  ? 0.861   23.048  28.074  1.00 70.46  ?  39  TYR B CE1   1 
ATOM   2284 C  CE2   . TYR B 1 91  ? -1.401  23.172  27.337  1.00 76.55  ?  39  TYR B CE2   1 
ATOM   2285 C  CZ    . TYR B 1 91  ? -0.127  23.687  27.374  1.00 74.43  ?  39  TYR B CZ    1 
ATOM   2286 O  OH    . TYR B 1 91  ? 0.160   24.852  26.704  1.00 79.27  ?  39  TYR B OH    1 
ATOM   2287 N  N     . ARG B 1 92  ? -1.656  22.497  31.698  1.00 80.62  ?  40  ARG B N     1 
ATOM   2288 C  CA    . ARG B 1 92  ? -2.428  23.715  31.864  1.00 86.66  ?  40  ARG B CA    1 
ATOM   2289 C  C     . ARG B 1 92  ? -1.783  24.789  30.994  1.00 88.20  ?  40  ARG B C     1 
ATOM   2290 O  O     . ARG B 1 92  ? -0.623  25.157  31.217  1.00 88.10  ?  40  ARG B O     1 
ATOM   2291 C  CB    . ARG B 1 92  ? -2.488  24.121  33.340  1.00 91.26  ?  40  ARG B CB    1 
ATOM   2292 C  CG    . ARG B 1 92  ? -3.592  23.409  34.151  1.00 89.70  ?  40  ARG B CG    1 
ATOM   2293 C  CD    . ARG B 1 92  ? -3.253  23.294  35.650  1.00 87.28  ?  40  ARG B CD    1 
ATOM   2294 N  NE    . ARG B 1 92  ? -4.416  23.063  36.521  1.00 90.03  ?  40  ARG B NE    1 
ATOM   2295 C  CZ    . ARG B 1 92  ? -5.520  23.817  36.561  1.00 93.95  ?  40  ARG B CZ    1 
ATOM   2296 N  NH1   . ARG B 1 92  ? -5.646  24.890  35.789  1.00 95.05  ?  40  ARG B NH1   1 
ATOM   2297 N  NH2   . ARG B 1 92  ? -6.510  23.509  37.394  1.00 89.76  ?  40  ARG B NH2   1 
ATOM   2298 N  N     . ALA B 1 93  ? -2.527  25.258  29.985  1.00 88.11  ?  41  ALA B N     1 
ATOM   2299 C  CA    . ALA B 1 93  ? -2.039  26.251  29.032  1.00 89.65  ?  41  ALA B CA    1 
ATOM   2300 C  C     . ALA B 1 93  ? -1.546  27.510  29.737  1.00 97.62  ?  41  ALA B C     1 
ATOM   2301 O  O     . ALA B 1 93  ? -2.343  28.254  30.320  1.00 101.04 ?  41  ALA B O     1 
ATOM   2302 C  CB    . ALA B 1 93  ? -3.136  26.609  28.020  1.00 88.33  ?  41  ALA B CB    1 
ATOM   2303 N  N     . SER B 1 94  ? -0.237  27.758  29.682  1.00 99.42  ?  42  SER B N     1 
ATOM   2304 C  CA    . SER B 1 94  ? 0.371   28.895  30.367  1.00 100.00 ?  42  SER B CA    1 
ATOM   2305 C  C     . SER B 1 94  ? 0.194   30.162  29.535  1.00 101.38 ?  42  SER B C     1 
ATOM   2306 O  O     . SER B 1 94  ? 0.661   30.235  28.392  1.00 99.50  ?  42  SER B O     1 
ATOM   2307 C  CB    . SER B 1 94  ? 1.851   28.621  30.621  1.00 95.98  ?  42  SER B CB    1 
ATOM   2308 O  OG    . SER B 1 94  ? 2.060   27.249  30.903  1.00 91.06  ?  42  SER B OG    1 
ATOM   2309 N  N     . GLY B 1 95  ? -0.468  31.162  30.118  1.00 106.28 ?  43  GLY B N     1 
ATOM   2310 C  CA    . GLY B 1 95  ? -0.776  32.395  29.428  1.00 112.13 ?  43  GLY B CA    1 
ATOM   2311 C  C     . GLY B 1 95  ? 0.325   33.437  29.519  1.00 113.81 ?  43  GLY B C     1 
ATOM   2312 O  O     . GLY B 1 95  ? 1.490   33.120  29.789  1.00 112.98 ?  43  GLY B O     1 
ATOM   2313 N  N     . PRO B 1 96  ? -0.030  34.723  29.289  1.00 114.07 ?  44  PRO B N     1 
ATOM   2314 C  CA    . PRO B 1 96  ? 0.989   35.783  29.271  1.00 112.49 ?  44  PRO B CA    1 
ATOM   2315 C  C     . PRO B 1 96  ? 1.208   36.425  30.634  1.00 109.95 ?  44  PRO B C     1 
ATOM   2316 O  O     . PRO B 1 96  ? 0.243   36.833  31.289  1.00 108.57 ?  44  PRO B O     1 
ATOM   2317 C  CB    . PRO B 1 96  ? 0.418   36.789  28.263  1.00 113.01 ?  44  PRO B CB    1 
ATOM   2318 C  CG    . PRO B 1 96  ? -1.093  36.609  28.356  1.00 111.96 ?  44  PRO B CG    1 
ATOM   2319 C  CD    . PRO B 1 96  ? -1.375  35.252  28.988  1.00 113.88 ?  44  PRO B CD    1 
ATOM   2320 N  N     . ASP B 1 97  ? 2.472   36.523  31.059  1.00 107.77 ?  45  ASP B N     1 
ATOM   2321 C  CA    . ASP B 1 97  ? 2.850   37.125  32.339  1.00 104.66 ?  45  ASP B CA    1 
ATOM   2322 C  C     . ASP B 1 97  ? 2.247   36.343  33.515  1.00 107.43 ?  45  ASP B C     1 
ATOM   2323 O  O     . ASP B 1 97  ? 1.514   36.879  34.351  1.00 103.92 ?  45  ASP B O     1 
ATOM   2324 C  CB    . ASP B 1 97  ? 2.453   38.613  32.378  1.00 106.98 ?  45  ASP B CB    1 
ATOM   2325 C  CG    . ASP B 1 97  ? 2.899   39.328  33.667  1.00 97.18  ?  45  ASP B CG    1 
ATOM   2326 O  OD1   . ASP B 1 97  ? 3.697   38.753  34.434  1.00 93.56  ?  45  ASP B OD1   1 
ATOM   2327 O  OD2   . ASP B 1 97  ? 2.440   40.467  33.916  1.00 85.24  ?  45  ASP B OD2   1 
ATOM   2328 N  N     . GLY B 1 98  ? 2.571   35.046  33.566  1.00 106.86 ?  46  GLY B N     1 
ATOM   2329 C  CA    . GLY B 1 98  ? 2.230   34.207  34.700  1.00 100.58 ?  46  GLY B CA    1 
ATOM   2330 C  C     . GLY B 1 98  ? 0.860   33.550  34.664  1.00 106.62 ?  46  GLY B C     1 
ATOM   2331 O  O     . GLY B 1 98  ? 0.567   32.724  35.541  1.00 101.25 ?  46  GLY B O     1 
ATOM   2332 N  N     . ALA B 1 99  ? 0.012   33.879  33.686  1.00 110.60 ?  47  ALA B N     1 
ATOM   2333 C  CA    . ALA B 1 99  ? -1.318  33.284  33.601  1.00 109.22 ?  47  ALA B CA    1 
ATOM   2334 C  C     . ALA B 1 99  ? -1.228  31.784  33.319  1.00 106.99 ?  47  ALA B C     1 
ATOM   2335 O  O     . ALA B 1 99  ? -0.268  31.292  32.713  1.00 106.04 ?  47  ALA B O     1 
ATOM   2336 C  CB    . ALA B 1 99  ? -2.154  33.968  32.509  1.00 101.67 ?  47  ALA B CB    1 
ATOM   2337 N  N     . THR B 1 100 ? -2.242  31.048  33.785  1.00 101.02 ?  48  THR B N     1 
ATOM   2338 C  CA    . THR B 1 100 ? -2.432  29.681  33.307  1.00 100.07 ?  48  THR B CA    1 
ATOM   2339 C  C     . THR B 1 100 ? -3.821  29.531  32.694  1.00 97.83  ?  48  THR B C     1 
ATOM   2340 O  O     . THR B 1 100 ? -4.525  30.526  32.484  1.00 93.41  ?  48  THR B O     1 
ATOM   2341 C  CB    . THR B 1 100 ? -2.224  28.645  34.422  1.00 94.60  ?  48  THR B CB    1 
ATOM   2342 O  OG1   . THR B 1 100 ? -3.392  28.563  35.251  1.00 91.89  ?  48  THR B OG1   1 
ATOM   2343 C  CG2   . THR B 1 100 ? -1.004  28.990  35.271  1.00 92.53  ?  48  THR B CG2   1 
ATOM   2344 N  N     . GLY B 1 101 ? -4.204  28.293  32.383  1.00 97.25  ?  49  GLY B N     1 
ATOM   2345 C  CA    . GLY B 1 101 ? -5.513  27.991  31.836  1.00 95.72  ?  49  GLY B CA    1 
ATOM   2346 C  C     . GLY B 1 101 ? -6.074  26.719  32.438  1.00 96.25  ?  49  GLY B C     1 
ATOM   2347 O  O     . GLY B 1 101 ? -5.593  26.256  33.477  1.00 93.53  ?  49  GLY B O     1 
ATOM   2348 N  N     . ARG B 1 102 ? -7.086  26.139  31.798  1.00 98.23  ?  50  ARG B N     1 
ATOM   2349 C  CA    . ARG B 1 102 ? -7.668  24.913  32.317  1.00 96.11  ?  50  ARG B CA    1 
ATOM   2350 C  C     . ARG B 1 102 ? -6.741  23.723  32.066  1.00 95.54  ?  50  ARG B C     1 
ATOM   2351 O  O     . ARG B 1 102 ? -5.837  23.764  31.224  1.00 94.59  ?  50  ARG B O     1 
ATOM   2352 C  CB    . ARG B 1 102 ? -9.041  24.666  31.691  1.00 93.63  ?  50  ARG B CB    1 
ATOM   2353 C  CG    . ARG B 1 102 ? -10.166 25.394  32.411  1.00 95.42  ?  50  ARG B CG    1 
ATOM   2354 C  CD    . ARG B 1 102 ? -10.121 25.143  33.931  1.00 96.26  ?  50  ARG B CD    1 
ATOM   2355 N  NE    . ARG B 1 102 ? -10.640 23.825  34.299  1.00 95.47  ?  50  ARG B NE    1 
ATOM   2356 C  CZ    . ARG B 1 102 ? -9.974  22.925  35.016  1.00 93.46  ?  50  ARG B CZ    1 
ATOM   2357 N  NH1   . ARG B 1 102 ? -8.752  23.195  35.458  1.00 94.26  ?  50  ARG B NH1   1 
ATOM   2358 N  NH2   . ARG B 1 102 ? -10.535 21.753  35.294  1.00 94.69  ?  50  ARG B NH2   1 
ATOM   2359 N  N     . GLY B 1 103 ? -6.979  22.648  32.817  1.00 95.46  ?  51  GLY B N     1 
ATOM   2360 C  CA    . GLY B 1 103 ? -6.140  21.470  32.737  1.00 91.41  ?  51  GLY B CA    1 
ATOM   2361 C  C     . GLY B 1 103 ? -6.765  20.279  32.042  1.00 89.59  ?  51  GLY B C     1 
ATOM   2362 O  O     . GLY B 1 103 ? -7.582  19.567  32.635  1.00 91.06  ?  51  GLY B O     1 
ATOM   2363 N  N     . GLN B 1 104 ? -6.382  20.048  30.786  1.00 89.75  ?  52  GLN B N     1 
ATOM   2364 C  CA    . GLN B 1 104 ? -6.775  18.838  30.079  1.00 87.18  ?  52  GLN B CA    1 
ATOM   2365 C  C     . GLN B 1 104 ? -5.723  17.749  30.275  1.00 83.21  ?  52  GLN B C     1 
ATOM   2366 O  O     . GLN B 1 104 ? -4.527  18.022  30.432  1.00 77.48  ?  52  GLN B O     1 
ATOM   2367 C  CB    . GLN B 1 104 ? -6.998  19.111  28.586  1.00 85.63  ?  52  GLN B CB    1 
ATOM   2368 C  CG    . GLN B 1 104 ? -5.774  19.574  27.820  1.00 84.19  ?  52  GLN B CG    1 
ATOM   2369 C  CD    . GLN B 1 104 ? -5.827  21.057  27.488  1.00 88.55  ?  52  GLN B CD    1 
ATOM   2370 O  OE1   . GLN B 1 104 ? -6.095  21.888  28.360  1.00 89.28  ?  52  GLN B OE1   1 
ATOM   2371 N  NE2   . GLN B 1 104 ? -5.567  21.397  26.225  1.00 83.46  ?  52  GLN B NE2   1 
ATOM   2372 N  N     . ARG B 1 105 ? -6.191  16.504  30.289  1.00 83.39  ?  53  ARG B N     1 
ATOM   2373 C  CA    . ARG B 1 105 ? -5.322  15.369  30.563  1.00 80.73  ?  53  ARG B CA    1 
ATOM   2374 C  C     . ARG B 1 105 ? -4.495  15.039  29.329  1.00 77.08  ?  53  ARG B C     1 
ATOM   2375 O  O     . ARG B 1 105 ? -5.040  14.868  28.234  1.00 80.92  ?  53  ARG B O     1 
ATOM   2376 C  CB    . ARG B 1 105 ? -6.148  14.157  30.994  1.00 83.67  ?  53  ARG B CB    1 
ATOM   2377 C  CG    . ARG B 1 105 ? -6.762  14.283  32.378  1.00 84.93  ?  53  ARG B CG    1 
ATOM   2378 C  CD    . ARG B 1 105 ? -7.355  12.955  32.845  1.00 91.84  ?  53  ARG B CD    1 
ATOM   2379 N  NE    . ARG B 1 105 ? -8.399  12.474  31.939  1.00 93.81  ?  53  ARG B NE    1 
ATOM   2380 C  CZ    . ARG B 1 105 ? -8.856  11.222  31.910  1.00 93.87  ?  53  ARG B CZ    1 
ATOM   2381 N  NH1   . ARG B 1 105 ? -9.814  10.888  31.052  1.00 93.15  ?  53  ARG B NH1   1 
ATOM   2382 N  NH2   . ARG B 1 105 ? -8.363  10.304  32.737  1.00 89.94  ?  53  ARG B NH2   1 
ATOM   2383 N  N     . ILE B 1 106 ? -3.180  14.945  29.510  1.00 70.04  ?  54  ILE B N     1 
ATOM   2384 C  CA    . ILE B 1 106 ? -2.243  14.682  28.427  1.00 68.35  ?  54  ILE B CA    1 
ATOM   2385 C  C     . ILE B 1 106 ? -1.557  13.350  28.695  1.00 65.21  ?  54  ILE B C     1 
ATOM   2386 O  O     . ILE B 1 106 ? -1.091  13.103  29.809  1.00 64.04  ?  54  ILE B O     1 
ATOM   2387 C  CB    . ILE B 1 106 ? -1.214  15.818  28.289  1.00 69.44  ?  54  ILE B CB    1 
ATOM   2388 C  CG1   . ILE B 1 106 ? -1.911  17.102  27.843  1.00 70.55  ?  54  ILE B CG1   1 
ATOM   2389 C  CG2   . ILE B 1 106 ? -0.150  15.460  27.278  1.00 69.65  ?  54  ILE B CG2   1 
ATOM   2390 C  CD1   . ILE B 1 106 ? -2.557  17.003  26.494  1.00 71.53  ?  54  ILE B CD1   1 
ATOM   2391 N  N     . HIS B 1 107 ? -1.499  12.497  27.673  1.00 66.47  ?  55  HIS B N     1 
ATOM   2392 C  CA    . HIS B 1 107 ? -0.883  11.174  27.746  1.00 61.88  ?  55  HIS B CA    1 
ATOM   2393 C  C     . HIS B 1 107 ? 0.383   11.213  26.899  1.00 61.49  ?  55  HIS B C     1 
ATOM   2394 O  O     . HIS B 1 107 ? 0.307   11.243  25.665  1.00 66.30  ?  55  HIS B O     1 
ATOM   2395 C  CB    . HIS B 1 107 ? -1.857  10.104  27.251  1.00 64.37  ?  55  HIS B CB    1 
ATOM   2396 C  CG    . HIS B 1 107 ? -1.297  8.712   27.227  1.00 67.63  ?  55  HIS B CG    1 
ATOM   2397 N  ND1   . HIS B 1 107 ? -1.955  7.660   26.625  1.00 68.72  ?  55  HIS B ND1   1 
ATOM   2398 C  CD2   . HIS B 1 107 ? -0.154  8.193   27.736  1.00 67.27  ?  55  HIS B CD2   1 
ATOM   2399 C  CE1   . HIS B 1 107 ? -1.243  6.556   26.762  1.00 61.83  ?  55  HIS B CE1   1 
ATOM   2400 N  NE2   . HIS B 1 107 ? -0.142  6.853   27.427  1.00 62.61  ?  55  HIS B NE2   1 
ATOM   2401 N  N     . LEU B 1 108 ? 1.537   11.213  27.557  1.00 56.67  ?  56  LEU B N     1 
ATOM   2402 C  CA    . LEU B 1 108 ? 2.821   11.347  26.887  1.00 54.52  ?  56  LEU B CA    1 
ATOM   2403 C  C     . LEU B 1 108 ? 3.342   9.994   26.448  1.00 55.50  ?  56  LEU B C     1 
ATOM   2404 O  O     . LEU B 1 108 ? 3.253   9.016   27.191  1.00 51.89  ?  56  LEU B O     1 
ATOM   2405 C  CB    . LEU B 1 108 ? 3.860   11.987  27.802  1.00 54.79  ?  56  LEU B CB    1 
ATOM   2406 C  CG    . LEU B 1 108 ? 3.633   13.405  28.303  1.00 60.07  ?  56  LEU B CG    1 
ATOM   2407 C  CD1   . LEU B 1 108 ? 4.742   13.782  29.278  1.00 55.63  ?  56  LEU B CD1   1 
ATOM   2408 C  CD2   . LEU B 1 108 ? 3.578   14.366  27.128  1.00 61.67  ?  56  LEU B CD2   1 
ATOM   2409 N  N     . GLN B 1 109 ? 3.890   9.952   25.230  1.00 57.65  ?  57  GLN B N     1 
ATOM   2410 C  CA    . GLN B 1 109 ? 4.704   8.843   24.747  1.00 52.53  ?  57  GLN B CA    1 
ATOM   2411 C  C     . GLN B 1 109 ? 6.108   9.378   24.515  1.00 52.20  ?  57  GLN B C     1 
ATOM   2412 O  O     . GLN B 1 109 ? 6.307   10.266  23.684  1.00 57.31  ?  57  GLN B O     1 
ATOM   2413 C  CB    . GLN B 1 109 ? 4.131   8.249   23.463  1.00 52.62  ?  57  GLN B CB    1 
ATOM   2414 C  CG    . GLN B 1 109 ? 5.070   7.245   22.774  1.00 55.70  ?  57  GLN B CG    1 
ATOM   2415 C  CD    . GLN B 1 109 ? 4.374   6.469   21.668  1.00 55.11  ?  57  GLN B CD    1 
ATOM   2416 O  OE1   . GLN B 1 109 ? 3.525   7.012   20.965  1.00 52.91  ?  57  GLN B OE1   1 
ATOM   2417 N  NE2   . GLN B 1 109 ? 4.713   5.191   21.523  1.00 52.44  ?  57  GLN B NE2   1 
ATOM   2418 N  N     . LEU B 1 110 ? 7.068   8.862   25.249  1.00 50.03  ?  58  LEU B N     1 
ATOM   2419 C  CA    . LEU B 1 110 ? 8.399   9.453   25.283  1.00 50.62  ?  58  LEU B CA    1 
ATOM   2420 C  C     . LEU B 1 110 ? 9.336   8.517   24.541  1.00 52.72  ?  58  LEU B C     1 
ATOM   2421 O  O     . LEU B 1 110 ? 9.789   7.511   25.098  1.00 49.33  ?  58  LEU B O     1 
ATOM   2422 C  CB    . LEU B 1 110 ? 8.871   9.675   26.715  1.00 52.07  ?  58  LEU B CB    1 
ATOM   2423 C  CG    . LEU B 1 110 ? 8.176   10.702  27.611  1.00 57.46  ?  58  LEU B CG    1 
ATOM   2424 C  CD1   . LEU B 1 110 ? 6.853   10.178  28.136  1.00 59.40  ?  58  LEU B CD1   1 
ATOM   2425 C  CD2   . LEU B 1 110 ? 9.071   11.031  28.791  1.00 55.31  ?  58  LEU B CD2   1 
ATOM   2426 N  N     . TRP B 1 111 ? 9.629   8.858   23.288  1.00 51.08  ?  59  TRP B N     1 
ATOM   2427 C  CA    . TRP B 1 111 ? 10.508  8.036   22.480  1.00 46.95  ?  59  TRP B CA    1 
ATOM   2428 C  C     . TRP B 1 111 ? 11.947  8.235   22.912  1.00 44.51  ?  59  TRP B C     1 
ATOM   2429 O  O     . TRP B 1 111 ? 12.382  9.357   23.168  1.00 46.73  ?  59  TRP B O     1 
ATOM   2430 C  CB    . TRP B 1 111 ? 10.351  8.387   21.003  1.00 49.28  ?  59  TRP B CB    1 
ATOM   2431 C  CG    . TRP B 1 111 ? 9.213   7.704   20.360  1.00 48.17  ?  59  TRP B CG    1 
ATOM   2432 C  CD1   . TRP B 1 111 ? 8.043   8.268   19.939  1.00 50.82  ?  59  TRP B CD1   1 
ATOM   2433 C  CD2   . TRP B 1 111 ? 9.129   6.316   20.045  1.00 45.73  ?  59  TRP B CD2   1 
ATOM   2434 N  NE1   . TRP B 1 111 ? 7.235   7.308   19.370  1.00 49.92  ?  59  TRP B NE1   1 
ATOM   2435 C  CE2   . TRP B 1 111 ? 7.879   6.101   19.434  1.00 47.87  ?  59  TRP B CE2   1 
ATOM   2436 C  CE3   . TRP B 1 111 ? 9.988   5.231   20.227  1.00 46.83  ?  59  TRP B CE3   1 
ATOM   2437 C  CZ2   . TRP B 1 111 ? 7.467   4.849   19.016  1.00 49.71  ?  59  TRP B CZ2   1 
ATOM   2438 C  CZ3   . TRP B 1 111 ? 9.575   3.980   19.807  1.00 47.25  ?  59  TRP B CZ3   1 
ATOM   2439 C  CH2   . TRP B 1 111 ? 8.327   3.800   19.216  1.00 51.12  ?  59  TRP B CH2   1 
ATOM   2440 N  N     . ASP B 1 112 ? 12.697  7.140   22.959  1.00 43.35  ?  60  ASP B N     1 
ATOM   2441 C  CA    . ASP B 1 112 ? 14.075  7.152   23.429  1.00 47.22  ?  60  ASP B CA    1 
ATOM   2442 C  C     . ASP B 1 112 ? 14.915  6.389   22.412  1.00 49.51  ?  60  ASP B C     1 
ATOM   2443 O  O     . ASP B 1 112 ? 14.691  5.196   22.195  1.00 50.25  ?  60  ASP B O     1 
ATOM   2444 C  CB    . ASP B 1 112 ? 14.150  6.521   24.833  1.00 47.15  ?  60  ASP B CB    1 
ATOM   2445 C  CG    . ASP B 1 112 ? 15.573  6.337   25.340  1.00 49.57  ?  60  ASP B CG    1 
ATOM   2446 O  OD1   . ASP B 1 112 ? 16.494  7.065   24.878  1.00 50.13  ?  60  ASP B OD1   1 
ATOM   2447 O  OD2   . ASP B 1 112 ? 15.766  5.462   26.218  1.00 47.64  ?  60  ASP B OD2   1 
ATOM   2448 N  N     . THR B 1 113 ? 15.859  7.063   21.768  1.00 45.19  ?  61  THR B N     1 
ATOM   2449 C  CA    . THR B 1 113 ? 16.561  6.447   20.654  1.00 46.49  ?  61  THR B CA    1 
ATOM   2450 C  C     . THR B 1 113 ? 17.991  6.130   21.048  1.00 48.17  ?  61  THR B C     1 
ATOM   2451 O  O     . THR B 1 113 ? 18.594  6.845   21.851  1.00 49.18  ?  61  THR B O     1 
ATOM   2452 C  CB    . THR B 1 113 ? 16.556  7.364   19.433  1.00 46.25  ?  61  THR B CB    1 
ATOM   2453 O  OG1   . THR B 1 113 ? 17.455  8.468   19.649  1.00 48.31  ?  61  THR B OG1   1 
ATOM   2454 C  CG2   . THR B 1 113 ? 15.159  7.918   19.209  1.00 46.36  ?  61  THR B CG2   1 
ATOM   2455 N  N     . ALA B 1 114 ? 18.527  5.054   20.474  1.00 47.29  ?  62  ALA B N     1 
ATOM   2456 C  CA    . ALA B 1 114 ? 19.952  4.773   20.578  1.00 48.08  ?  62  ALA B CA    1 
ATOM   2457 C  C     . ALA B 1 114 ? 20.749  5.818   19.809  1.00 48.81  ?  62  ALA B C     1 
ATOM   2458 O  O     . ALA B 1 114 ? 20.377  6.216   18.708  1.00 51.00  ?  62  ALA B O     1 
ATOM   2459 C  CB    . ALA B 1 114 ? 20.256  3.377   20.034  1.00 48.65  ?  62  ALA B CB    1 
ATOM   2460 N  N     . GLY B 1 115 ? 21.831  6.298   20.403  1.00 48.58  ?  63  GLY B N     1 
ATOM   2461 C  CA    . GLY B 1 115 ? 22.608  7.301   19.711  1.00 44.52  ?  63  GLY B CA    1 
ATOM   2462 C  C     . GLY B 1 115 ? 23.743  6.730   18.904  1.00 49.17  ?  63  GLY B C     1 
ATOM   2463 O  O     . GLY B 1 115 ? 24.472  7.469   18.235  1.00 49.49  ?  63  GLY B O     1 
ATOM   2464 N  N     . LEU B 1 116 ? 23.937  5.420   18.963  1.00 50.38  ?  64  LEU B N     1 
ATOM   2465 C  CA    . LEU B 1 116 ? 25.023  4.806   18.218  1.00 57.09  ?  64  LEU B CA    1 
ATOM   2466 C  C     . LEU B 1 116 ? 24.739  4.862   16.712  1.00 54.59  ?  64  LEU B C     1 
ATOM   2467 O  O     . LEU B 1 116 ? 23.584  4.830   16.267  1.00 49.42  ?  64  LEU B O     1 
ATOM   2468 C  CB    . LEU B 1 116 ? 25.235  3.364   18.698  1.00 53.55  ?  64  LEU B CB    1 
ATOM   2469 C  CG    . LEU B 1 116 ? 26.133  3.249   19.935  1.00 55.54  ?  64  LEU B CG    1 
ATOM   2470 C  CD1   . LEU B 1 116 ? 26.386  1.812   20.315  1.00 54.79  ?  64  LEU B CD1   1 
ATOM   2471 C  CD2   . LEU B 1 116 ? 27.455  3.960   19.710  1.00 55.93  ?  64  LEU B CD2   1 
ATOM   2472 N  N     . GLU B 1 117 ? 25.808  4.976   15.922  1.00 54.92  ?  65  GLU B N     1 
ATOM   2473 C  CA    . GLU B 1 117 ? 25.621  5.094   14.474  1.00 60.92  ?  65  GLU B CA    1 
ATOM   2474 C  C     . GLU B 1 117 ? 24.976  3.841   13.879  1.00 56.80  ?  65  GLU B C     1 
ATOM   2475 O  O     . GLU B 1 117 ? 24.122  3.941   12.986  1.00 56.16  ?  65  GLU B O     1 
ATOM   2476 C  CB    . GLU B 1 117 ? 26.951  5.422   13.780  1.00 63.72  ?  65  GLU B CB    1 
ATOM   2477 C  CG    . GLU B 1 117 ? 26.992  6.875   13.237  1.00 73.79  ?  65  GLU B CG    1 
ATOM   2478 C  CD    . GLU B 1 117 ? 28.402  7.467   13.097  1.00 82.18  ?  65  GLU B CD    1 
ATOM   2479 O  OE1   . GLU B 1 117 ? 29.366  6.705   12.855  1.00 84.81  ?  65  GLU B OE1   1 
ATOM   2480 O  OE2   . GLU B 1 117 ? 28.538  8.708   13.246  1.00 86.51  ?  65  GLU B OE2   1 
ATOM   2481 N  N     . ARG B 1 118 ? 25.329  2.659   14.389  1.00 52.53  ?  66  ARG B N     1 
ATOM   2482 C  CA    . ARG B 1 118 ? 24.769  1.415   13.870  1.00 49.24  ?  66  ARG B CA    1 
ATOM   2483 C  C     . ARG B 1 118 ? 23.255  1.375   13.921  1.00 49.52  ?  66  ARG B C     1 
ATOM   2484 O  O     . ARG B 1 118 ? 22.653  0.411   13.443  1.00 59.36  ?  66  ARG B O     1 
ATOM   2485 C  CB    . ARG B 1 118 ? 25.272  0.225   14.678  1.00 58.28  ?  66  ARG B CB    1 
ATOM   2486 C  CG    . ARG B 1 118 ? 24.784  0.295   16.127  1.00 61.23  ?  66  ARG B CG    1 
ATOM   2487 C  CD    . ARG B 1 118 ? 25.227  -0.890  16.941  1.00 59.68  ?  66  ARG B CD    1 
ATOM   2488 N  NE    . ARG B 1 118 ? 26.677  -0.942  17.045  1.00 61.75  ?  66  ARG B NE    1 
ATOM   2489 C  CZ    . ARG B 1 118 ? 27.325  -1.776  17.850  1.00 66.82  ?  66  ARG B CZ    1 
ATOM   2490 N  NH1   . ARG B 1 118 ? 26.639  -2.619  18.611  1.00 71.81  ?  66  ARG B NH1   1 
ATOM   2491 N  NH2   . ARG B 1 118 ? 28.652  -1.769  17.901  1.00 66.75  ?  66  ARG B NH2   1 
ATOM   2492 N  N     . PHE B 1 119 ? 22.623  2.344   14.559  1.00 52.61  ?  67  PHE B N     1 
ATOM   2493 C  CA    . PHE B 1 119 ? 21.176  2.356   14.717  1.00 53.57  ?  67  PHE B CA    1 
ATOM   2494 C  C     . PHE B 1 119 ? 20.593  3.581   14.040  1.00 49.60  ?  67  PHE B C     1 
ATOM   2495 O  O     . PHE B 1 119 ? 19.389  3.852   14.162  1.00 47.36  ?  67  PHE B O     1 
ATOM   2496 C  CB    . PHE B 1 119 ? 20.788  2.309   16.213  1.00 51.85  ?  67  PHE B CB    1 
ATOM   2497 C  CG    . PHE B 1 119 ? 20.932  0.936   16.855  1.00 52.68  ?  67  PHE B CG    1 
ATOM   2498 C  CD1   . PHE B 1 119 ? 20.153  -0.138  16.422  1.00 51.03  ?  67  PHE B CD1   1 
ATOM   2499 C  CD2   . PHE B 1 119 ? 21.826  0.722   17.900  1.00 54.25  ?  67  PHE B CD2   1 
ATOM   2500 C  CE1   . PHE B 1 119 ? 20.273  -1.398  16.999  1.00 49.11  ?  67  PHE B CE1   1 
ATOM   2501 C  CE2   . PHE B 1 119 ? 21.951  -0.553  18.494  1.00 54.88  ?  67  PHE B CE2   1 
ATOM   2502 C  CZ    . PHE B 1 119 ? 21.171  -1.613  18.033  1.00 52.17  ?  67  PHE B CZ    1 
ATOM   2503 N  N     . ARG B 1 120 ? 21.432  4.314   13.305  1.00 50.70  ?  68  ARG B N     1 
ATOM   2504 C  CA    . ARG B 1 120 ? 21.032  5.618   12.798  1.00 51.47  ?  68  ARG B CA    1 
ATOM   2505 C  C     . ARG B 1 120 ? 19.839  5.507   11.858  1.00 51.15  ?  68  ARG B C     1 
ATOM   2506 O  O     . ARG B 1 120 ? 18.967  6.385   11.848  1.00 49.78  ?  68  ARG B O     1 
ATOM   2507 C  CB    . ARG B 1 120 ? 22.220  6.288   12.112  1.00 51.47  ?  68  ARG B CB    1 
ATOM   2508 C  CG    . ARG B 1 120 ? 21.991  7.744   11.768  1.00 54.49  ?  68  ARG B CG    1 
ATOM   2509 C  CD    . ARG B 1 120 ? 21.542  8.560   12.984  1.00 60.08  ?  68  ARG B CD    1 
ATOM   2510 N  NE    . ARG B 1 120 ? 22.355  8.351   14.195  1.00 59.51  ?  68  ARG B NE    1 
ATOM   2511 C  CZ    . ARG B 1 120 ? 23.614  8.770   14.350  1.00 59.47  ?  68  ARG B CZ    1 
ATOM   2512 N  NH1   . ARG B 1 120 ? 24.235  9.417   13.372  1.00 60.87  ?  68  ARG B NH1   1 
ATOM   2513 N  NH2   . ARG B 1 120 ? 24.257  8.539   15.492  1.00 61.14  ?  68  ARG B NH2   1 
ATOM   2514 N  N     . SER B 1 121 ? 19.763  4.437   11.064  1.00 49.88  ?  69  SER B N     1 
ATOM   2515 C  CA    . SER B 1 121 ? 18.665  4.406   10.104  1.00 54.04  ?  69  SER B CA    1 
ATOM   2516 C  C     . SER B 1 121 ? 17.390  3.901   10.753  1.00 52.72  ?  69  SER B C     1 
ATOM   2517 O  O     . SER B 1 121 ? 16.301  4.390   10.430  1.00 53.05  ?  69  SER B O     1 
ATOM   2518 C  CB    . SER B 1 121 ? 19.020  3.564   8.872   1.00 55.57  ?  69  SER B CB    1 
ATOM   2519 O  OG    . SER B 1 121 ? 19.767  2.404   9.237   1.00 64.22  ?  69  SER B OG    1 
ATOM   2520 N  N     . LEU B 1 122 ? 17.506  2.971   11.701  1.00 54.87  ?  70  LEU B N     1 
ATOM   2521 C  CA    . LEU B 1 122 ? 16.338  2.561   12.478  1.00 54.07  ?  70  LEU B CA    1 
ATOM   2522 C  C     . LEU B 1 122 ? 15.767  3.716   13.298  1.00 51.95  ?  70  LEU B C     1 
ATOM   2523 O  O     . LEU B 1 122 ? 14.545  3.909   13.348  1.00 50.39  ?  70  LEU B O     1 
ATOM   2524 C  CB    . LEU B 1 122 ? 16.697  1.400   13.394  1.00 48.93  ?  70  LEU B CB    1 
ATOM   2525 C  CG    . LEU B 1 122 ? 15.509  0.920   14.222  1.00 54.29  ?  70  LEU B CG    1 
ATOM   2526 C  CD1   . LEU B 1 122 ? 14.650  -0.065  13.445  1.00 52.95  ?  70  LEU B CD1   1 
ATOM   2527 C  CD2   . LEU B 1 122 ? 15.983  0.307   15.534  1.00 57.45  ?  70  LEU B CD2   1 
ATOM   2528 N  N     . THR B 1 123 ? 16.623  4.488   13.967  1.00 50.95  ?  71  THR B N     1 
ATOM   2529 C  CA    . THR B 1 123 ? 16.066  5.557   14.786  1.00 50.81  ?  71  THR B CA    1 
ATOM   2530 C  C     . THR B 1 123 ? 15.576  6.716   13.931  1.00 53.70  ?  71  THR B C     1 
ATOM   2531 O  O     . THR B 1 123 ? 14.634  7.418   14.323  1.00 52.71  ?  71  THR B O     1 
ATOM   2532 C  CB    . THR B 1 123 ? 17.083  6.055   15.820  1.00 48.86  ?  71  THR B CB    1 
ATOM   2533 O  OG1   . THR B 1 123 ? 18.244  6.568   15.162  1.00 51.27  ?  71  THR B OG1   1 
ATOM   2534 C  CG2   . THR B 1 123 ? 17.497  4.942   16.749  1.00 46.09  ?  71  THR B CG2   1 
ATOM   2535 N  N     . THR B 1 124 ? 16.172  6.923   12.753  1.00 56.20  ?  72  THR B N     1 
ATOM   2536 C  CA    . THR B 1 124 ? 15.775  8.062   11.936  1.00 50.35  ?  72  THR B CA    1 
ATOM   2537 C  C     . THR B 1 124 ? 14.353  7.919   11.413  1.00 52.24  ?  72  THR B C     1 
ATOM   2538 O  O     . THR B 1 124 ? 13.707  8.929   11.108  1.00 54.39  ?  72  THR B O     1 
ATOM   2539 C  CB    . THR B 1 124 ? 16.765  8.232   10.791  1.00 53.90  ?  72  THR B CB    1 
ATOM   2540 O  OG1   . THR B 1 124 ? 18.066  8.493   11.340  1.00 53.11  ?  72  THR B OG1   1 
ATOM   2541 C  CG2   . THR B 1 124 ? 16.362  9.366   9.872   1.00 52.59  ?  72  THR B CG2   1 
ATOM   2542 N  N     . ALA B 1 125 ? 13.834  6.698   11.340  1.00 49.37  ?  73  ALA B N     1 
ATOM   2543 C  CA    . ALA B 1 125 ? 12.486  6.521   10.826  1.00 53.07  ?  73  ALA B CA    1 
ATOM   2544 C  C     . ALA B 1 125 ? 11.408  6.841   11.853  1.00 60.34  ?  73  ALA B C     1 
ATOM   2545 O  O     . ALA B 1 125 ? 10.230  6.914   11.478  1.00 63.83  ?  73  ALA B O     1 
ATOM   2546 C  CB    . ALA B 1 125 ? 12.308  5.094   10.313  1.00 57.52  ?  73  ALA B CB    1 
ATOM   2547 N  N     . PHE B 1 126 ? 11.767  7.040   13.126  1.00 55.96  ?  74  PHE B N     1 
ATOM   2548 C  CA    . PHE B 1 126 ? 10.775  7.372   14.137  1.00 56.34  ?  74  PHE B CA    1 
ATOM   2549 C  C     . PHE B 1 126 ? 10.569  8.877   14.307  1.00 55.86  ?  74  PHE B C     1 
ATOM   2550 O  O     . PHE B 1 126 ? 9.574   9.276   14.921  1.00 57.69  ?  74  PHE B O     1 
ATOM   2551 C  CB    . PHE B 1 126 ? 11.152  6.701   15.467  1.00 53.80  ?  74  PHE B CB    1 
ATOM   2552 C  CG    . PHE B 1 126 ? 10.971  5.204   15.440  1.00 57.03  ?  74  PHE B CG    1 
ATOM   2553 C  CD1   . PHE B 1 126 ? 11.985  4.373   14.980  1.00 59.32  ?  74  PHE B CD1   1 
ATOM   2554 C  CD2   . PHE B 1 126 ? 9.758   4.631   15.805  1.00 58.38  ?  74  PHE B CD2   1 
ATOM   2555 C  CE1   . PHE B 1 126 ? 11.813  2.982   14.918  1.00 56.88  ?  74  PHE B CE1   1 
ATOM   2556 C  CE2   . PHE B 1 126 ? 9.575   3.250   15.750  1.00 59.61  ?  74  PHE B CE2   1 
ATOM   2557 C  CZ    . PHE B 1 126 ? 10.609  2.422   15.304  1.00 56.51  ?  74  PHE B CZ    1 
ATOM   2558 N  N     . PHE B 1 127 ? 11.454  9.711   13.742  1.00 53.83  ?  75  PHE B N     1 
ATOM   2559 C  CA    . PHE B 1 127 ? 11.318  11.166  13.827  1.00 54.06  ?  75  PHE B CA    1 
ATOM   2560 C  C     . PHE B 1 127 ? 9.956   11.653  13.350  1.00 59.35  ?  75  PHE B C     1 
ATOM   2561 O  O     . PHE B 1 127 ? 9.452   12.674  13.838  1.00 59.49  ?  75  PHE B O     1 
ATOM   2562 C  CB    . PHE B 1 127 ? 12.383  11.871  12.974  1.00 52.76  ?  75  PHE B CB    1 
ATOM   2563 C  CG    . PHE B 1 127 ? 13.806  11.640  13.414  1.00 50.47  ?  75  PHE B CG    1 
ATOM   2564 C  CD1   . PHE B 1 127 ? 14.124  10.742  14.410  1.00 51.70  ?  75  PHE B CD1   1 
ATOM   2565 C  CD2   . PHE B 1 127 ? 14.827  12.345  12.817  1.00 47.57  ?  75  PHE B CD2   1 
ATOM   2566 C  CE1   . PHE B 1 127 ? 15.439  10.546  14.787  1.00 53.73  ?  75  PHE B CE1   1 
ATOM   2567 C  CE2   . PHE B 1 127 ? 16.138  12.158  13.196  1.00 48.33  ?  75  PHE B CE2   1 
ATOM   2568 C  CZ    . PHE B 1 127 ? 16.447  11.265  14.175  1.00 48.52  ?  75  PHE B CZ    1 
ATOM   2569 N  N     . ARG B 1 128 ? 9.367   10.978  12.357  1.00 62.38  ?  76  ARG B N     1 
ATOM   2570 C  CA    . ARG B 1 128 ? 8.084   11.435  11.835  1.00 65.49  ?  76  ARG B CA    1 
ATOM   2571 C  C     . ARG B 1 128 ? 6.944   11.140  12.800  1.00 61.16  ?  76  ARG B C     1 
ATOM   2572 O  O     . ARG B 1 128 ? 5.870   11.744  12.676  1.00 65.98  ?  76  ARG B O     1 
ATOM   2573 C  CB    . ARG B 1 128 ? 7.804   10.800  10.465  1.00 65.46  ?  76  ARG B CB    1 
ATOM   2574 C  CG    . ARG B 1 128 ? 8.550   11.469  9.311   1.00 67.52  ?  76  ARG B CG    1 
ATOM   2575 C  CD    . ARG B 1 128 ? 8.042   10.996  7.952   1.00 64.60  ?  76  ARG B CD    1 
ATOM   2576 N  NE    . ARG B 1 128 ? 6.590   10.821  7.966   1.00 64.29  ?  76  ARG B NE    1 
ATOM   2577 C  CZ    . ARG B 1 128 ? 5.719   11.823  7.881   1.00 64.15  ?  76  ARG B CZ    1 
ATOM   2578 N  NH1   . ARG B 1 128 ? 4.413   11.572  7.907   1.00 61.22  ?  76  ARG B NH1   1 
ATOM   2579 N  NH2   . ARG B 1 128 ? 6.155   13.075  7.760   1.00 64.86  ?  76  ARG B NH2   1 
ATOM   2580 N  N     . ASP B 1 129 ? 7.151   10.229  13.751  1.00 58.33  ?  77  ASP B N     1 
ATOM   2581 C  CA    . ASP B 1 129 ? 6.154   9.989   14.786  1.00 61.34  ?  77  ASP B CA    1 
ATOM   2582 C  C     . ASP B 1 129 ? 6.151   11.061  15.870  1.00 59.97  ?  77  ASP B C     1 
ATOM   2583 O  O     . ASP B 1 129 ? 5.179   11.147  16.631  1.00 59.97  ?  77  ASP B O     1 
ATOM   2584 C  CB    . ASP B 1 129 ? 6.369   8.624   15.442  1.00 56.71  ?  77  ASP B CB    1 
ATOM   2585 C  CG    . ASP B 1 129 ? 5.093   8.081   16.061  1.00 59.12  ?  77  ASP B CG    1 
ATOM   2586 O  OD1   . ASP B 1 129 ? 4.015   8.487   15.584  1.00 56.88  ?  77  ASP B OD1   1 
ATOM   2587 O  OD2   . ASP B 1 129 ? 5.155   7.275   17.024  1.00 57.40  ?  77  ASP B OD2   1 
ATOM   2588 N  N     . ALA B 1 130 ? 7.194   11.878  15.952  1.00 56.96  ?  78  ALA B N     1 
ATOM   2589 C  CA    . ALA B 1 130 ? 7.339   12.846  17.021  1.00 56.10  ?  78  ALA B CA    1 
ATOM   2590 C  C     . ALA B 1 130 ? 6.604   14.128  16.676  1.00 58.36  ?  78  ALA B C     1 
ATOM   2591 O  O     . ALA B 1 130 ? 6.447   14.472  15.508  1.00 62.20  ?  78  ALA B O     1 
ATOM   2592 C  CB    . ALA B 1 130 ? 8.813   13.151  17.263  1.00 54.36  ?  78  ALA B CB    1 
ATOM   2593 N  N     . MET B 1 131 ? 6.141   14.828  17.710  1.00 56.57  ?  79  MET B N     1 
ATOM   2594 C  CA    . MET B 1 131 ? 5.661   16.197  17.573  1.00 57.72  ?  79  MET B CA    1 
ATOM   2595 C  C     . MET B 1 131 ? 6.658   17.212  18.103  1.00 53.77  ?  79  MET B C     1 
ATOM   2596 O  O     . MET B 1 131 ? 6.424   18.414  17.966  1.00 55.32  ?  79  MET B O     1 
ATOM   2597 C  CB    . MET B 1 131 ? 4.330   16.376  18.298  1.00 58.70  ?  79  MET B CB    1 
ATOM   2598 C  CG    . MET B 1 131 ? 3.406   15.188  18.189  1.00 57.35  ?  79  MET B CG    1 
ATOM   2599 S  SD    . MET B 1 131 ? 1.946   15.502  19.191  1.00 66.30  ?  79  MET B SD    1 
ATOM   2600 C  CE    . MET B 1 131 ? 0.827   14.319  18.450  1.00 67.46  ?  79  MET B CE    1 
ATOM   2601 N  N     . GLY B 1 132 ? 7.749   16.753  18.710  1.00 54.32  ?  80  GLY B N     1 
ATOM   2602 C  CA    . GLY B 1 132 ? 8.772   17.640  19.239  1.00 53.46  ?  80  GLY B CA    1 
ATOM   2603 C  C     . GLY B 1 132 ? 9.966   16.815  19.674  1.00 49.04  ?  80  GLY B C     1 
ATOM   2604 O  O     . GLY B 1 132 ? 9.888   15.592  19.810  1.00 50.57  ?  80  GLY B O     1 
ATOM   2605 N  N     . PHE B 1 133 ? 11.078  17.507  19.895  1.00 46.70  ?  81  PHE B N     1 
ATOM   2606 C  CA    . PHE B 1 133 ? 12.344  16.812  20.074  1.00 48.18  ?  81  PHE B CA    1 
ATOM   2607 C  C     . PHE B 1 133 ? 13.115  17.348  21.267  1.00 50.18  ?  81  PHE B C     1 
ATOM   2608 O  O     . PHE B 1 133 ? 13.270  18.564  21.420  1.00 51.94  ?  81  PHE B O     1 
ATOM   2609 C  CB    . PHE B 1 133 ? 13.187  16.917  18.811  1.00 48.71  ?  81  PHE B CB    1 
ATOM   2610 C  CG    . PHE B 1 133 ? 12.583  16.219  17.642  1.00 53.07  ?  81  PHE B CG    1 
ATOM   2611 C  CD1   . PHE B 1 133 ? 12.772  14.861  17.460  1.00 50.36  ?  81  PHE B CD1   1 
ATOM   2612 C  CD2   . PHE B 1 133 ? 11.817  16.918  16.723  1.00 54.14  ?  81  PHE B CD2   1 
ATOM   2613 C  CE1   . PHE B 1 133 ? 12.216  14.215  16.372  1.00 51.96  ?  81  PHE B CE1   1 
ATOM   2614 C  CE2   . PHE B 1 133 ? 11.257  16.276  15.641  1.00 56.07  ?  81  PHE B CE2   1 
ATOM   2615 C  CZ    . PHE B 1 133 ? 11.459  14.920  15.467  1.00 53.27  ?  81  PHE B CZ    1 
ATOM   2616 N  N     . LEU B 1 134 ? 13.598  16.428  22.105  1.00 48.58  ?  82  LEU B N     1 
ATOM   2617 C  CA    . LEU B 1 134 ? 14.477  16.737  23.222  1.00 45.94  ?  82  LEU B CA    1 
ATOM   2618 C  C     . LEU B 1 134 ? 15.893  16.418  22.759  1.00 45.23  ?  82  LEU B C     1 
ATOM   2619 O  O     . LEU B 1 134 ? 16.286  15.254  22.677  1.00 46.80  ?  82  LEU B O     1 
ATOM   2620 C  CB    . LEU B 1 134 ? 14.080  15.937  24.458  1.00 48.80  ?  82  LEU B CB    1 
ATOM   2621 C  CG    . LEU B 1 134 ? 14.426  16.522  25.831  1.00 48.69  ?  82  LEU B CG    1 
ATOM   2622 C  CD1   . LEU B 1 134 ? 13.412  17.543  26.268  1.00 51.14  ?  82  LEU B CD1   1 
ATOM   2623 C  CD2   . LEU B 1 134 ? 14.484  15.418  26.850  1.00 50.12  ?  82  LEU B CD2   1 
ATOM   2624 N  N     . LEU B 1 135 ? 16.656  17.450  22.428  1.00 47.00  ?  83  LEU B N     1 
ATOM   2625 C  CA    . LEU B 1 135 ? 18.014  17.246  21.951  1.00 47.94  ?  83  LEU B CA    1 
ATOM   2626 C  C     . LEU B 1 135 ? 18.963  17.321  23.128  1.00 47.70  ?  83  LEU B C     1 
ATOM   2627 O  O     . LEU B 1 135 ? 18.939  18.293  23.882  1.00 51.62  ?  83  LEU B O     1 
ATOM   2628 C  CB    . LEU B 1 135 ? 18.390  18.291  20.904  1.00 47.83  ?  83  LEU B CB    1 
ATOM   2629 C  CG    . LEU B 1 135 ? 19.315  17.744  19.810  1.00 49.62  ?  83  LEU B CG    1 
ATOM   2630 C  CD1   . LEU B 1 135 ? 19.511  18.773  18.724  1.00 50.71  ?  83  LEU B CD1   1 
ATOM   2631 C  CD2   . LEU B 1 135 ? 20.667  17.309  20.353  1.00 50.84  ?  83  LEU B CD2   1 
ATOM   2632 N  N     . LEU B 1 136 ? 19.798  16.310  23.288  1.00 49.49  ?  84  LEU B N     1 
ATOM   2633 C  CA    . LEU B 1 136 ? 20.680  16.248  24.438  1.00 45.44  ?  84  LEU B CA    1 
ATOM   2634 C  C     . LEU B 1 136 ? 22.131  16.227  24.000  1.00 48.22  ?  84  LEU B C     1 
ATOM   2635 O  O     . LEU B 1 136 ? 22.487  15.545  23.037  1.00 50.87  ?  84  LEU B O     1 
ATOM   2636 C  CB    . LEU B 1 136 ? 20.398  15.017  25.267  1.00 46.91  ?  84  LEU B CB    1 
ATOM   2637 C  CG    . LEU B 1 136 ? 19.444  15.216  26.431  1.00 46.12  ?  84  LEU B CG    1 
ATOM   2638 C  CD1   . LEU B 1 136 ? 18.041  15.550  25.957  1.00 45.24  ?  84  LEU B CD1   1 
ATOM   2639 C  CD2   . LEU B 1 136 ? 19.454  13.973  27.257  1.00 43.62  ?  84  LEU B CD2   1 
ATOM   2640 N  N     . PHE B 1 137 ? 22.965  16.977  24.708  1.00 49.73  ?  85  PHE B N     1 
ATOM   2641 C  CA    . PHE B 1 137 ? 24.397  16.734  24.701  1.00 49.23  ?  85  PHE B CA    1 
ATOM   2642 C  C     . PHE B 1 137 ? 24.881  16.623  26.145  1.00 49.34  ?  85  PHE B C     1 
ATOM   2643 O  O     . PHE B 1 137 ? 24.166  16.947  27.092  1.00 47.78  ?  85  PHE B O     1 
ATOM   2644 C  CB    . PHE B 1 137 ? 25.156  17.823  23.946  1.00 45.33  ?  85  PHE B CB    1 
ATOM   2645 C  CG    . PHE B 1 137 ? 25.175  19.156  24.639  1.00 45.29  ?  85  PHE B CG    1 
ATOM   2646 C  CD1   . PHE B 1 137 ? 24.121  20.041  24.487  1.00 43.38  ?  85  PHE B CD1   1 
ATOM   2647 C  CD2   . PHE B 1 137 ? 26.267  19.536  25.418  1.00 45.75  ?  85  PHE B CD2   1 
ATOM   2648 C  CE1   . PHE B 1 137 ? 24.137  21.275  25.112  1.00 43.38  ?  85  PHE B CE1   1 
ATOM   2649 C  CE2   . PHE B 1 137 ? 26.294  20.767  26.058  1.00 45.97  ?  85  PHE B CE2   1 
ATOM   2650 C  CZ    . PHE B 1 137 ? 25.229  21.640  25.903  1.00 46.51  ?  85  PHE B CZ    1 
ATOM   2651 N  N     . ASP B 1 138 ? 26.114  16.154  26.287  1.00 48.97  ?  86  ASP B N     1 
ATOM   2652 C  CA    . ASP B 1 138 ? 26.781  15.954  27.561  1.00 47.86  ?  86  ASP B CA    1 
ATOM   2653 C  C     . ASP B 1 138 ? 27.662  17.166  27.868  1.00 52.68  ?  86  ASP B C     1 
ATOM   2654 O  O     . ASP B 1 138 ? 28.662  17.397  27.179  1.00 52.37  ?  86  ASP B O     1 
ATOM   2655 C  CB    . ASP B 1 138 ? 27.612  14.674  27.471  1.00 52.88  ?  86  ASP B CB    1 
ATOM   2656 C  CG    . ASP B 1 138 ? 28.222  14.248  28.796  1.00 56.27  ?  86  ASP B CG    1 
ATOM   2657 O  OD1   . ASP B 1 138 ? 28.412  15.101  29.697  1.00 53.92  ?  86  ASP B OD1   1 
ATOM   2658 O  OD2   . ASP B 1 138 ? 28.540  13.034  28.919  1.00 58.41  ?  86  ASP B OD2   1 
ATOM   2659 N  N     . LEU B 1 139 ? 27.313  17.917  28.927  1.00 53.53  ?  87  LEU B N     1 
ATOM   2660 C  CA    . LEU B 1 139 ? 28.127  19.058  29.354  1.00 51.41  ?  87  LEU B CA    1 
ATOM   2661 C  C     . LEU B 1 139 ? 29.580  18.679  29.616  1.00 52.80  ?  87  LEU B C     1 
ATOM   2662 O  O     . LEU B 1 139 ? 30.441  19.566  29.670  1.00 53.41  ?  87  LEU B O     1 
ATOM   2663 C  CB    . LEU B 1 139 ? 27.543  19.689  30.616  1.00 51.35  ?  87  LEU B CB    1 
ATOM   2664 C  CG    . LEU B 1 139 ? 26.326  20.588  30.461  1.00 53.64  ?  87  LEU B CG    1 
ATOM   2665 C  CD1   . LEU B 1 139 ? 25.632  20.797  31.813  1.00 48.34  ?  87  LEU B CD1   1 
ATOM   2666 C  CD2   . LEU B 1 139 ? 26.757  21.898  29.863  1.00 51.50  ?  87  LEU B CD2   1 
ATOM   2667 N  N     . THR B 1 140 ? 29.870  17.388  29.786  1.00 53.73  ?  88  THR B N     1 
ATOM   2668 C  CA    . THR B 1 140 ? 31.223  16.901  30.020  1.00 57.57  ?  88  THR B CA    1 
ATOM   2669 C  C     . THR B 1 140 ? 31.880  16.320  28.768  1.00 57.91  ?  88  THR B C     1 
ATOM   2670 O  O     . THR B 1 140 ? 32.929  15.678  28.884  1.00 56.58  ?  88  THR B O     1 
ATOM   2671 C  CB    . THR B 1 140 ? 31.225  15.834  31.117  1.00 56.31  ?  88  THR B CB    1 
ATOM   2672 O  OG1   . THR B 1 140 ? 30.561  14.667  30.626  1.00 53.55  ?  88  THR B OG1   1 
ATOM   2673 C  CG2   . THR B 1 140 ? 30.528  16.341  32.413  1.00 52.00  ?  88  THR B CG2   1 
ATOM   2674 N  N     . ASN B 1 141 ? 31.291  16.514  27.583  1.00 52.20  ?  89  ASN B N     1 
ATOM   2675 C  CA    . ASN B 1 141 ? 31.826  15.942  26.342  1.00 54.88  ?  89  ASN B CA    1 
ATOM   2676 C  C     . ASN B 1 141 ? 31.672  17.001  25.265  1.00 55.15  ?  89  ASN B C     1 
ATOM   2677 O  O     . ASN B 1 141 ? 30.575  17.158  24.716  1.00 55.28  ?  89  ASN B O     1 
ATOM   2678 C  CB    . ASN B 1 141 ? 31.089  14.665  25.962  1.00 57.71  ?  89  ASN B CB    1 
ATOM   2679 C  CG    . ASN B 1 141 ? 31.678  13.981  24.739  1.00 59.41  ?  89  ASN B CG    1 
ATOM   2680 O  OD1   . ASN B 1 141 ? 32.011  14.628  23.751  1.00 61.37  ?  89  ASN B OD1   1 
ATOM   2681 N  ND2   . ASN B 1 141 ? 31.798  12.653  24.798  1.00 57.01  ?  89  ASN B ND2   1 
ATOM   2682 N  N     . GLU B 1 142 ? 32.758  17.733  24.972  1.00 54.80  ?  90  GLU B N     1 
ATOM   2683 C  CA    . GLU B 1 142 ? 32.637  18.841  24.028  1.00 61.12  ?  90  GLU B CA    1 
ATOM   2684 C  C     . GLU B 1 142 ? 32.232  18.340  22.645  1.00 56.39  ?  90  GLU B C     1 
ATOM   2685 O  O     . GLU B 1 142 ? 31.516  19.042  21.918  1.00 56.32  ?  90  GLU B O     1 
ATOM   2686 C  CB    . GLU B 1 142 ? 33.944  19.657  23.965  1.00 64.27  ?  90  GLU B CB    1 
ATOM   2687 C  CG    . GLU B 1 142 ? 34.027  20.744  22.833  1.00 64.92  ?  90  GLU B CG    1 
ATOM   2688 C  CD    . GLU B 1 142 ? 33.807  22.208  23.314  1.00 71.93  ?  90  GLU B CD    1 
ATOM   2689 O  OE1   . GLU B 1 142 ? 33.869  23.148  22.465  1.00 66.59  ?  90  GLU B OE1   1 
ATOM   2690 O  OE2   . GLU B 1 142 ? 33.569  22.421  24.531  1.00 68.57  ?  90  GLU B OE2   1 
ATOM   2691 N  N     . GLN B 1 143 ? 32.628  17.113  22.286  1.00 53.54  ?  91  GLN B N     1 
ATOM   2692 C  CA    . GLN B 1 143 ? 32.313  16.612  20.953  1.00 55.61  ?  91  GLN B CA    1 
ATOM   2693 C  C     . GLN B 1 143 ? 30.829  16.348  20.796  1.00 56.98  ?  91  GLN B C     1 
ATOM   2694 O  O     . GLN B 1 143 ? 30.297  16.477  19.686  1.00 56.77  ?  91  GLN B O     1 
ATOM   2695 C  CB    . GLN B 1 143 ? 33.103  15.344  20.649  1.00 55.07  ?  91  GLN B CB    1 
ATOM   2696 C  CG    . GLN B 1 143 ? 32.866  14.778  19.253  1.00 58.65  ?  91  GLN B CG    1 
ATOM   2697 C  CD    . GLN B 1 143 ? 33.437  15.644  18.143  1.00 58.21  ?  91  GLN B CD    1 
ATOM   2698 O  OE1   . GLN B 1 143 ? 34.638  15.918  18.116  1.00 58.83  ?  91  GLN B OE1   1 
ATOM   2699 N  NE2   . GLN B 1 143 ? 32.575  16.077  17.213  1.00 53.82  ?  91  GLN B NE2   1 
ATOM   2700 N  N     . SER B 1 144 ? 30.143  15.971  21.878  1.00 50.84  ?  92  SER B N     1 
ATOM   2701 C  CA    . SER B 1 144 ? 28.702  15.775  21.777  1.00 48.06  ?  92  SER B CA    1 
ATOM   2702 C  C     . SER B 1 144 ? 28.007  17.102  21.564  1.00 50.48  ?  92  SER B C     1 
ATOM   2703 O  O     . SER B 1 144 ? 26.910  17.149  20.988  1.00 47.10  ?  92  SER B O     1 
ATOM   2704 C  CB    . SER B 1 144 ? 28.167  15.085  23.037  1.00 53.06  ?  92  SER B CB    1 
ATOM   2705 O  OG    . SER B 1 144 ? 28.064  15.993  24.128  1.00 50.29  ?  92  SER B OG    1 
ATOM   2706 N  N     . PHE B 1 145 ? 28.634  18.184  22.038  1.00 51.08  ?  93  PHE B N     1 
ATOM   2707 C  CA    . PHE B 1 145 ? 28.117  19.532  21.852  1.00 51.52  ?  93  PHE B CA    1 
ATOM   2708 C  C     . PHE B 1 145 ? 28.388  20.031  20.437  1.00 49.93  ?  93  PHE B C     1 
ATOM   2709 O  O     . PHE B 1 145 ? 27.518  20.654  19.815  1.00 48.79  ?  93  PHE B O     1 
ATOM   2710 C  CB    . PHE B 1 145 ? 28.743  20.466  22.889  1.00 44.32  ?  93  PHE B CB    1 
ATOM   2711 C  CG    . PHE B 1 145 ? 28.384  21.908  22.705  1.00 45.12  ?  93  PHE B CG    1 
ATOM   2712 C  CD1   . PHE B 1 145 ? 27.080  22.340  22.889  1.00 44.22  ?  93  PHE B CD1   1 
ATOM   2713 C  CD2   . PHE B 1 145 ? 29.355  22.839  22.363  1.00 47.40  ?  93  PHE B CD2   1 
ATOM   2714 C  CE1   . PHE B 1 145 ? 26.754  23.674  22.719  1.00 45.45  ?  93  PHE B CE1   1 
ATOM   2715 C  CE2   . PHE B 1 145 ? 29.030  24.175  22.187  1.00 47.46  ?  93  PHE B CE2   1 
ATOM   2716 C  CZ    . PHE B 1 145 ? 27.732  24.591  22.360  1.00 45.70  ?  93  PHE B CZ    1 
ATOM   2717 N  N     . LEU B 1 146 ? 29.581  19.756  19.908  1.00 47.60  ?  94  LEU B N     1 
ATOM   2718 C  CA    . LEU B 1 146 ? 29.858  20.113  18.522  1.00 51.39  ?  94  LEU B CA    1 
ATOM   2719 C  C     . LEU B 1 146 ? 28.854  19.467  17.580  1.00 52.52  ?  94  LEU B C     1 
ATOM   2720 O  O     . LEU B 1 146 ? 28.403  20.096  16.614  1.00 53.40  ?  94  LEU B O     1 
ATOM   2721 C  CB    . LEU B 1 146 ? 31.285  19.712  18.162  1.00 53.08  ?  94  LEU B CB    1 
ATOM   2722 C  CG    . LEU B 1 146 ? 32.324  20.536  18.926  1.00 52.19  ?  94  LEU B CG    1 
ATOM   2723 C  CD1   . LEU B 1 146 ? 33.740  20.200  18.498  1.00 52.11  ?  94  LEU B CD1   1 
ATOM   2724 C  CD2   . LEU B 1 146 ? 32.040  22.002  18.731  1.00 52.98  ?  94  LEU B CD2   1 
ATOM   2725 N  N     . ASN B 1 147 ? 28.446  18.230  17.881  1.00 51.47  ?  95  ASN B N     1 
ATOM   2726 C  CA    . ASN B 1 147 ? 27.518  17.488  17.041  1.00 49.00  ?  95  ASN B CA    1 
ATOM   2727 C  C     . ASN B 1 147 ? 26.087  18.012  17.097  1.00 49.58  ?  95  ASN B C     1 
ATOM   2728 O  O     . ASN B 1 147 ? 25.273  17.603  16.264  1.00 53.92  ?  95  ASN B O     1 
ATOM   2729 C  CB    . ASN B 1 147 ? 27.530  16.013  17.433  1.00 50.74  ?  95  ASN B CB    1 
ATOM   2730 C  CG    . ASN B 1 147 ? 28.791  15.288  16.971  1.00 55.65  ?  95  ASN B CG    1 
ATOM   2731 O  OD1   . ASN B 1 147 ? 29.528  15.773  16.115  1.00 55.15  ?  95  ASN B OD1   1 
ATOM   2732 N  ND2   . ASN B 1 147 ? 29.043  14.114  17.549  1.00 59.64  ?  95  ASN B ND2   1 
ATOM   2733 N  N     . VAL B 1 148 ? 25.749  18.889  18.043  1.00 49.25  ?  96  VAL B N     1 
ATOM   2734 C  CA    . VAL B 1 148 ? 24.384  19.414  18.113  1.00 49.18  ?  96  VAL B CA    1 
ATOM   2735 C  C     . VAL B 1 148 ? 23.950  20.016  16.775  1.00 49.05  ?  96  VAL B C     1 
ATOM   2736 O  O     . VAL B 1 148 ? 22.760  19.988  16.426  1.00 49.30  ?  96  VAL B O     1 
ATOM   2737 C  CB    . VAL B 1 148 ? 24.276  20.437  19.264  1.00 43.70  ?  96  VAL B CB    1 
ATOM   2738 C  CG1   . VAL B 1 148 ? 22.957  21.166  19.204  1.00 45.73  ?  96  VAL B CG1   1 
ATOM   2739 C  CG2   . VAL B 1 148 ? 24.416  19.747  20.614  1.00 46.95  ?  96  VAL B CG2   1 
ATOM   2740 N  N     . ARG B 1 149 ? 24.896  20.572  16.007  1.00 54.71  ?  97  ARG B N     1 
ATOM   2741 C  CA    . ARG B 1 149 ? 24.574  21.159  14.700  1.00 52.68  ?  97  ARG B CA    1 
ATOM   2742 C  C     . ARG B 1 149 ? 24.094  20.094  13.724  1.00 51.12  ?  97  ARG B C     1 
ATOM   2743 O  O     . ARG B 1 149 ? 23.025  20.220  13.109  1.00 46.34  ?  97  ARG B O     1 
ATOM   2744 C  CB    . ARG B 1 149 ? 25.803  21.859  14.121  1.00 54.23  ?  97  ARG B CB    1 
ATOM   2745 C  CG    . ARG B 1 149 ? 26.047  23.269  14.621  1.00 64.97  ?  97  ARG B CG    1 
ATOM   2746 C  CD    . ARG B 1 149 ? 27.263  23.870  13.922  1.00 71.62  ?  97  ARG B CD    1 
ATOM   2747 N  NE    . ARG B 1 149 ? 28.439  22.998  14.010  1.00 71.55  ?  97  ARG B NE    1 
ATOM   2748 C  CZ    . ARG B 1 149 ? 29.246  22.933  15.069  1.00 69.97  ?  97  ARG B CZ    1 
ATOM   2749 N  NH1   . ARG B 1 149 ? 30.293  22.114  15.055  1.00 66.62  ?  97  ARG B NH1   1 
ATOM   2750 N  NH2   . ARG B 1 149 ? 29.010  23.690  16.141  1.00 66.92  ?  97  ARG B NH2   1 
ATOM   2751 N  N     . ASN B 1 150 ? 24.886  19.034  13.571  1.00 49.99  ?  98  ASN B N     1 
ATOM   2752 C  CA    . ASN B 1 150 ? 24.502  17.948  12.683  1.00 51.94  ?  98  ASN B CA    1 
ATOM   2753 C  C     . ASN B 1 150 ? 23.161  17.355  13.079  1.00 51.99  ?  98  ASN B C     1 
ATOM   2754 O  O     . ASN B 1 150 ? 22.344  17.034  12.209  1.00 52.78  ?  98  ASN B O     1 
ATOM   2755 C  CB    . ASN B 1 150 ? 25.594  16.881  12.671  1.00 50.90  ?  98  ASN B CB    1 
ATOM   2756 C  CG    . ASN B 1 150 ? 26.928  17.430  12.189  1.00 59.24  ?  98  ASN B CG    1 
ATOM   2757 O  OD1   . ASN B 1 150 ? 26.977  18.229  11.244  1.00 62.60  ?  98  ASN B OD1   1 
ATOM   2758 N  ND2   . ASN B 1 150 ? 28.014  17.029  12.850  1.00 60.60  ?  98  ASN B ND2   1 
ATOM   2759 N  N     . TRP B 1 151 ? 22.906  17.210  14.385  1.00 50.75  ?  99  TRP B N     1 
ATOM   2760 C  CA    . TRP B 1 151 ? 21.634  16.637  14.819  1.00 48.06  ?  99  TRP B CA    1 
ATOM   2761 C  C     . TRP B 1 151 ? 20.468  17.524  14.410  1.00 46.87  ?  99  TRP B C     1 
ATOM   2762 O  O     . TRP B 1 151 ? 19.424  17.029  13.973  1.00 49.70  ?  99  TRP B O     1 
ATOM   2763 C  CB    . TRP B 1 151 ? 21.618  16.423  16.337  1.00 49.16  ?  99  TRP B CB    1 
ATOM   2764 C  CG    . TRP B 1 151 ? 22.391  15.236  16.850  1.00 46.94  ?  99  TRP B CG    1 
ATOM   2765 C  CD1   . TRP B 1 151 ? 23.549  15.269  17.580  1.00 47.58  ?  99  TRP B CD1   1 
ATOM   2766 C  CD2   . TRP B 1 151 ? 22.050  13.850  16.711  1.00 49.00  ?  99  TRP B CD2   1 
ATOM   2767 N  NE1   . TRP B 1 151 ? 23.961  13.992  17.889  1.00 45.39  ?  99  TRP B NE1   1 
ATOM   2768 C  CE2   . TRP B 1 151 ? 23.059  13.101  17.370  1.00 50.12  ?  99  TRP B CE2   1 
ATOM   2769 C  CE3   . TRP B 1 151 ? 21.000  13.164  16.091  1.00 47.54  ?  99  TRP B CE3   1 
ATOM   2770 C  CZ2   . TRP B 1 151 ? 23.045  11.699  17.416  1.00 49.69  ?  99  TRP B CZ2   1 
ATOM   2771 C  CZ3   . TRP B 1 151 ? 20.982  11.772  16.157  1.00 46.74  ?  99  TRP B CZ3   1 
ATOM   2772 C  CH2   . TRP B 1 151 ? 22.000  11.058  16.810  1.00 46.20  ?  99  TRP B CH2   1 
ATOM   2773 N  N     . ILE B 1 152 ? 20.622  18.840  14.547  1.00 51.49  ?  100 ILE B N     1 
ATOM   2774 C  CA    . ILE B 1 152 ? 19.519  19.757  14.257  1.00 51.87  ?  100 ILE B CA    1 
ATOM   2775 C  C     . ILE B 1 152 ? 19.156  19.720  12.772  1.00 52.36  ?  100 ILE B C     1 
ATOM   2776 O  O     . ILE B 1 152 ? 17.976  19.806  12.401  1.00 49.91  ?  100 ILE B O     1 
ATOM   2777 C  CB    . ILE B 1 152 ? 19.881  21.180  14.718  1.00 51.07  ?  100 ILE B CB    1 
ATOM   2778 C  CG1   . ILE B 1 152 ? 19.924  21.250  16.245  1.00 48.25  ?  100 ILE B CG1   1 
ATOM   2779 C  CG2   . ILE B 1 152 ? 18.915  22.210  14.126  1.00 50.65  ?  100 ILE B CG2   1 
ATOM   2780 C  CD1   . ILE B 1 152 ? 20.570  22.493  16.784  1.00 43.46  ?  100 ILE B CD1   1 
ATOM   2781 N  N     . SER B 1 153 ? 20.149  19.592  11.893  1.00 49.83  ?  101 SER B N     1 
ATOM   2782 C  CA    . SER B 1 153 ? 19.791  19.539  10.479  1.00 50.03  ?  101 SER B CA    1 
ATOM   2783 C  C     . SER B 1 153 ? 19.131  18.206  10.137  1.00 54.93  ?  101 SER B C     1 
ATOM   2784 O  O     . SER B 1 153 ? 18.169  18.172  9.359   1.00 55.04  ?  101 SER B O     1 
ATOM   2785 C  CB    . SER B 1 153 ? 21.003  19.815  9.597   1.00 50.62  ?  101 SER B CB    1 
ATOM   2786 O  OG    . SER B 1 153 ? 22.110  19.048  9.978   1.00 55.22  ?  101 SER B OG    1 
ATOM   2787 N  N     . GLN B 1 154 ? 19.584  17.100  10.753  1.00 53.35  ?  102 GLN B N     1 
ATOM   2788 C  CA    . GLN B 1 154 ? 18.867  15.839  10.576  1.00 48.13  ?  102 GLN B CA    1 
ATOM   2789 C  C     . GLN B 1 154 ? 17.428  15.944  11.059  1.00 51.41  ?  102 GLN B C     1 
ATOM   2790 O  O     . GLN B 1 154 ? 16.536  15.298  10.504  1.00 54.30  ?  102 GLN B O     1 
ATOM   2791 C  CB    . GLN B 1 154 ? 19.579  14.708  11.297  1.00 45.86  ?  102 GLN B CB    1 
ATOM   2792 C  CG    . GLN B 1 154 ? 20.939  14.372  10.738  1.00 53.77  ?  102 GLN B CG    1 
ATOM   2793 C  CD    . GLN B 1 154 ? 20.862  13.685  9.384   1.00 63.22  ?  102 GLN B CD    1 
ATOM   2794 O  OE1   . GLN B 1 154 ? 19.787  13.246  8.954   1.00 65.21  ?  102 GLN B OE1   1 
ATOM   2795 N  NE2   . GLN B 1 154 ? 22.005  13.590  8.698   1.00 63.82  ?  102 GLN B NE2   1 
ATOM   2796 N  N     . LEU B 1 155 ? 17.179  16.764  12.074  1.00 53.46  ?  103 LEU B N     1 
ATOM   2797 C  CA    . LEU B 1 155 ? 15.819  16.949  12.562  1.00 55.00  ?  103 LEU B CA    1 
ATOM   2798 C  C     . LEU B 1 155 ? 14.986  17.715  11.553  1.00 54.28  ?  103 LEU B C     1 
ATOM   2799 O  O     . LEU B 1 155 ? 13.834  17.362  11.287  1.00 54.19  ?  103 LEU B O     1 
ATOM   2800 C  CB    . LEU B 1 155 ? 15.839  17.695  13.896  1.00 54.37  ?  103 LEU B CB    1 
ATOM   2801 C  CG    . LEU B 1 155 ? 16.078  16.789  15.085  1.00 54.34  ?  103 LEU B CG    1 
ATOM   2802 C  CD1   . LEU B 1 155 ? 16.032  17.557  16.401  1.00 51.94  ?  103 LEU B CD1   1 
ATOM   2803 C  CD2   . LEU B 1 155 ? 15.014  15.709  15.027  1.00 55.53  ?  103 LEU B CD2   1 
ATOM   2804 N  N     . GLN B 1 156 ? 15.545  18.796  11.011  1.00 56.98  ?  104 GLN B N     1 
ATOM   2805 C  CA    . GLN B 1 156 ? 14.834  19.562  9.998   1.00 60.24  ?  104 GLN B CA    1 
ATOM   2806 C  C     . GLN B 1 156 ? 14.569  18.722  8.761   1.00 58.48  ?  104 GLN B C     1 
ATOM   2807 O  O     . GLN B 1 156 ? 13.522  18.871  8.118   1.00 58.43  ?  104 GLN B O     1 
ATOM   2808 C  CB    . GLN B 1 156 ? 15.635  20.814  9.636   1.00 59.94  ?  104 GLN B CB    1 
ATOM   2809 C  CG    . GLN B 1 156 ? 15.632  21.876  10.719  1.00 60.13  ?  104 GLN B CG    1 
ATOM   2810 C  CD    . GLN B 1 156 ? 16.739  22.880  10.527  1.00 63.69  ?  104 GLN B CD    1 
ATOM   2811 O  OE1   . GLN B 1 156 ? 17.513  22.790  9.565   1.00 63.43  ?  104 GLN B OE1   1 
ATOM   2812 N  NE2   . GLN B 1 156 ? 16.828  23.849  11.439  1.00 61.92  ?  104 GLN B NE2   1 
ATOM   2813 N  N     . MET B 1 157 ? 15.485  17.809  8.442   1.00 57.60  ?  105 MET B N     1 
ATOM   2814 C  CA    . MET B 1 157 ? 15.395  17.027  7.218   1.00 58.17  ?  105 MET B CA    1 
ATOM   2815 C  C     . MET B 1 157 ? 14.445  15.840  7.315   1.00 61.12  ?  105 MET B C     1 
ATOM   2816 O  O     . MET B 1 157 ? 13.924  15.409  6.281   1.00 60.93  ?  105 MET B O     1 
ATOM   2817 C  CB    . MET B 1 157 ? 16.781  16.525  6.806   1.00 54.16  ?  105 MET B CB    1 
ATOM   2818 C  CG    . MET B 1 157 ? 16.800  15.822  5.455   1.00 64.83  ?  105 MET B CG    1 
ATOM   2819 S  SD    . MET B 1 157 ? 18.272  14.817  5.170   1.00 75.19  ?  105 MET B SD    1 
ATOM   2820 C  CE    . MET B 1 157 ? 19.461  15.737  6.166   1.00 67.98  ?  105 MET B CE    1 
ATOM   2821 N  N     . HIS B 1 158 ? 14.165  15.314  8.516   1.00 58.98  ?  106 HIS B N     1 
ATOM   2822 C  CA    . HIS B 1 158 ? 13.313  14.134  8.623   1.00 55.73  ?  106 HIS B CA    1 
ATOM   2823 C  C     . HIS B 1 158 ? 12.050  14.311  9.451   1.00 57.44  ?  106 HIS B C     1 
ATOM   2824 O  O     . HIS B 1 158 ? 11.348  13.322  9.675   1.00 60.37  ?  106 HIS B O     1 
ATOM   2825 C  CB    . HIS B 1 158 ? 14.107  12.959  9.189   1.00 50.17  ?  106 HIS B CB    1 
ATOM   2826 C  CG    . HIS B 1 158 ? 15.258  12.541  8.329   1.00 55.17  ?  106 HIS B CG    1 
ATOM   2827 N  ND1   . HIS B 1 158 ? 15.168  11.520  7.411   1.00 55.41  ?  106 HIS B ND1   1 
ATOM   2828 C  CD2   . HIS B 1 158 ? 16.530  13.004  8.252   1.00 55.74  ?  106 HIS B CD2   1 
ATOM   2829 C  CE1   . HIS B 1 158 ? 16.335  11.369  6.806   1.00 54.89  ?  106 HIS B CE1   1 
ATOM   2830 N  NE2   . HIS B 1 158 ? 17.179  12.254  7.301   1.00 55.17  ?  106 HIS B NE2   1 
ATOM   2831 N  N     . ALA B 1 159 ? 11.716  15.518  9.893   1.00 60.75  ?  107 ALA B N     1 
ATOM   2832 C  CA    . ALA B 1 159 ? 10.586  15.677  10.791  1.00 58.61  ?  107 ALA B CA    1 
ATOM   2833 C  C     . ALA B 1 159 ? 9.287   15.781  9.997   1.00 63.36  ?  107 ALA B C     1 
ATOM   2834 O  O     . ALA B 1 159 ? 9.257   15.603  8.783   1.00 63.81  ?  107 ALA B O     1 
ATOM   2835 C  CB    . ALA B 1 159 ? 10.786  16.891  11.686  1.00 59.29  ?  107 ALA B CB    1 
ATOM   2836 N  N     . TYR B 1 160 ? 8.194   16.070  10.698  1.00 68.91  ?  108 TYR B N     1 
ATOM   2837 C  CA    . TYR B 1 160 ? 6.851   16.076  10.115  1.00 69.92  ?  108 TYR B CA    1 
ATOM   2838 C  C     . TYR B 1 160 ? 6.630   17.291  9.227   1.00 71.31  ?  108 TYR B C     1 
ATOM   2839 O  O     . TYR B 1 160 ? 5.785   17.270  8.335   1.00 76.64  ?  108 TYR B O     1 
ATOM   2840 C  CB    . TYR B 1 160 ? 5.787   16.031  11.228  1.00 72.27  ?  108 TYR B CB    1 
ATOM   2841 C  CG    . TYR B 1 160 ? 4.367   15.748  10.750  1.00 75.63  ?  108 TYR B CG    1 
ATOM   2842 C  CD1   . TYR B 1 160 ? 3.363   16.710  10.867  1.00 77.08  ?  108 TYR B CD1   1 
ATOM   2843 C  CD2   . TYR B 1 160 ? 4.026   14.515  10.186  1.00 76.47  ?  108 TYR B CD2   1 
ATOM   2844 C  CE1   . TYR B 1 160 ? 2.056   16.453  10.428  1.00 76.61  ?  108 TYR B CE1   1 
ATOM   2845 C  CE2   . TYR B 1 160 ? 2.723   14.252  9.745   1.00 73.31  ?  108 TYR B CE2   1 
ATOM   2846 C  CZ    . TYR B 1 160 ? 1.749   15.224  9.872   1.00 74.49  ?  108 TYR B CZ    1 
ATOM   2847 O  OH    . TYR B 1 160 ? 0.469   14.959  9.447   1.00 74.74  ?  108 TYR B OH    1 
ATOM   2848 N  N     . CYS B 1 161 ? 7.252   18.245  10.088  1.00 71.47  ?  109 CYS B N     1 
ATOM   2849 C  CA    . CYS B 1 161 ? 6.721   19.568  10.192  1.00 71.81  ?  109 CYS B CA    1 
ATOM   2850 C  C     . CYS B 1 161 ? 7.830   20.538  9.783   1.00 72.69  ?  109 CYS B C     1 
ATOM   2851 O  O     . CYS B 1 161 ? 9.013   20.053  9.625   1.00 69.86  -1 109 CYS B O     1 
ATOM   2852 C  CB    . CYS B 1 161 ? 6.317   19.837  11.663  1.00 73.63  ?  109 CYS B CB    1 
ATOM   2853 S  SG    . CYS B 1 161 ? 4.506   20.173  11.744  0.88 81.88  ?  109 CYS B SG    1 
ATOM   2854 N  N     . GLU B 1 162 ? 7.586   21.650  8.914   1.00 73.19  ?  110 GLU B N     1 
ATOM   2855 C  CA    . GLU B 1 162 ? 8.814   22.107  8.265   1.00 71.56  ?  110 GLU B CA    1 
ATOM   2856 C  C     . GLU B 1 162 ? 9.882   22.487  9.299   1.00 74.59  ?  110 GLU B C     1 
ATOM   2857 O  O     . GLU B 1 162 ? 11.056  22.107  9.167   1.00 73.22  ?  110 GLU B O     1 
ATOM   2858 C  CB    . GLU B 1 162 ? 8.523   23.297  7.348   1.00 30.00  ?  110 GLU B CB    1 
ATOM   2859 N  N     . ASN B 1 163 ? 9.467   23.227  10.331  1.00 63.85  ?  111 ASN B N     1 
ATOM   2860 C  CA    . ASN B 1 163 ? 10.382  23.786  11.322  1.00 67.43  ?  111 ASN B CA    1 
ATOM   2861 C  C     . ASN B 1 163 ? 9.969   23.247  12.690  1.00 68.48  ?  111 ASN B C     1 
ATOM   2862 O  O     . ASN B 1 163 ? 9.139   23.853  13.380  1.00 68.68  ?  111 ASN B O     1 
ATOM   2863 C  CB    . ASN B 1 163 ? 10.350  25.309  11.281  1.00 66.40  ?  111 ASN B CB    1 
ATOM   2864 C  CG    . ASN B 1 163 ? 11.319  25.940  12.251  1.00 67.86  ?  111 ASN B CG    1 
ATOM   2865 O  OD1   . ASN B 1 163 ? 12.123  25.256  12.888  1.00 70.83  ?  111 ASN B OD1   1 
ATOM   2866 N  ND2   . ASN B 1 163 ? 11.250  27.256  12.371  1.00 68.10  ?  111 ASN B ND2   1 
ATOM   2867 N  N     . PRO B 1 164 ? 10.521  22.115  13.112  1.00 64.56  ?  112 PRO B N     1 
ATOM   2868 C  CA    . PRO B 1 164 ? 9.969   21.420  14.282  1.00 67.54  ?  112 PRO B CA    1 
ATOM   2869 C  C     . PRO B 1 164 ? 10.364  22.084  15.598  1.00 63.52  ?  112 PRO B C     1 
ATOM   2870 O  O     . PRO B 1 164 ? 11.338  22.835  15.690  1.00 63.42  ?  112 PRO B O     1 
ATOM   2871 C  CB    . PRO B 1 164 ? 10.568  20.009  14.165  1.00 64.38  ?  112 PRO B CB    1 
ATOM   2872 C  CG    . PRO B 1 164 ? 11.806  20.169  13.364  1.00 60.21  ?  112 PRO B CG    1 
ATOM   2873 C  CD    . PRO B 1 164 ? 11.692  21.430  12.542  1.00 61.98  ?  112 PRO B CD    1 
ATOM   2874 N  N     . ASP B 1 165 ? 9.572   21.802  16.633  1.00 63.13  ?  113 ASP B N     1 
ATOM   2875 C  CA    . ASP B 1 165 ? 9.863   22.333  17.963  1.00 64.05  ?  113 ASP B CA    1 
ATOM   2876 C  C     . ASP B 1 165 ? 10.997  21.537  18.599  1.00 57.02  ?  113 ASP B C     1 
ATOM   2877 O  O     . ASP B 1 165 ? 11.010  20.307  18.534  1.00 56.46  ?  113 ASP B O     1 
ATOM   2878 C  CB    . ASP B 1 165 ? 8.619   22.289  18.853  1.00 64.56  ?  113 ASP B CB    1 
ATOM   2879 C  CG    . ASP B 1 165 ? 7.467   23.138  18.303  1.00 68.70  ?  113 ASP B CG    1 
ATOM   2880 O  OD1   . ASP B 1 165 ? 7.626   24.385  18.206  1.00 66.97  ?  113 ASP B OD1   1 
ATOM   2881 O  OD2   . ASP B 1 165 ? 6.403   22.549  17.978  1.00 70.84  ?  113 ASP B OD2   1 
ATOM   2882 N  N     . ILE B 1 166 ? 11.958  22.232  19.201  1.00 56.89  ?  114 ILE B N     1 
ATOM   2883 C  CA    . ILE B 1 166 ? 13.110  21.575  19.813  1.00 54.89  ?  114 ILE B CA    1 
ATOM   2884 C  C     . ILE B 1 166 ? 13.389  22.214  21.169  1.00 54.26  ?  114 ILE B C     1 
ATOM   2885 O  O     . ILE B 1 166 ? 13.164  23.414  21.359  1.00 55.08  ?  114 ILE B O     1 
ATOM   2886 C  CB    . ILE B 1 166 ? 14.353  21.653  18.906  1.00 53.11  ?  114 ILE B CB    1 
ATOM   2887 C  CG1   . ILE B 1 166 ? 14.062  21.016  17.540  1.00 58.67  ?  114 ILE B CG1   1 
ATOM   2888 C  CG2   . ILE B 1 166 ? 15.537  20.986  19.574  1.00 49.31  ?  114 ILE B CG2   1 
ATOM   2889 C  CD1   . ILE B 1 166 ? 15.170  21.230  16.508  1.00 51.75  ?  114 ILE B CD1   1 
ATOM   2890 N  N     . VAL B 1 167 ? 13.843  21.397  22.122  1.00 56.46  ?  115 VAL B N     1 
ATOM   2891 C  CA    . VAL B 1 167 ? 14.370  21.857  23.405  1.00 51.43  ?  115 VAL B CA    1 
ATOM   2892 C  C     . VAL B 1 167 ? 15.743  21.234  23.603  1.00 46.42  ?  115 VAL B C     1 
ATOM   2893 O  O     . VAL B 1 167 ? 15.864  20.008  23.683  1.00 45.31  ?  115 VAL B O     1 
ATOM   2894 C  CB    . VAL B 1 167 ? 13.455  21.495  24.581  1.00 47.41  ?  115 VAL B CB    1 
ATOM   2895 C  CG1   . VAL B 1 167 ? 14.121  21.921  25.883  1.00 56.08  ?  115 VAL B CG1   1 
ATOM   2896 C  CG2   . VAL B 1 167 ? 12.126  22.183  24.449  1.00 47.86  ?  115 VAL B CG2   1 
ATOM   2897 N  N     . LEU B 1 168 ? 16.768  22.071  23.700  1.00 48.17  ?  116 LEU B N     1 
ATOM   2898 C  CA    . LEU B 1 168 ? 18.139  21.612  23.886  1.00 49.66  ?  116 LEU B CA    1 
ATOM   2899 C  C     . LEU B 1 168 ? 18.454  21.419  25.372  1.00 49.11  ?  116 LEU B C     1 
ATOM   2900 O  O     . LEU B 1 168 ? 18.138  22.281  26.195  1.00 47.43  ?  116 LEU B O     1 
ATOM   2901 C  CB    . LEU B 1 168 ? 19.098  22.625  23.258  1.00 45.10  ?  116 LEU B CB    1 
ATOM   2902 C  CG    . LEU B 1 168 ? 20.577  22.250  23.238  1.00 47.11  ?  116 LEU B CG    1 
ATOM   2903 C  CD1   . LEU B 1 168 ? 20.862  21.136  22.248  1.00 41.48  ?  116 LEU B CD1   1 
ATOM   2904 C  CD2   . LEU B 1 168 ? 21.427  23.473  22.952  1.00 47.40  ?  116 LEU B CD2   1 
ATOM   2905 N  N     . CYS B 1 169 ? 19.083  20.292  25.713  1.00 48.96  ?  117 CYS B N     1 
ATOM   2906 C  CA    . CYS B 1 169 ? 19.512  19.994  27.078  1.00 46.92  ?  117 CYS B CA    1 
ATOM   2907 C  C     . CYS B 1 169 ? 21.003  19.729  27.137  1.00 49.44  ?  117 CYS B C     1 
ATOM   2908 O  O     . CYS B 1 169 ? 21.495  18.810  26.474  1.00 52.34  ?  117 CYS B O     1 
ATOM   2909 C  CB    . CYS B 1 169 ? 18.790  18.783  27.655  1.00 48.00  ?  117 CYS B CB    1 
ATOM   2910 S  SG    . CYS B 1 169 ? 17.021  18.940  27.678  1.00 59.18  ?  117 CYS B SG    1 
ATOM   2911 N  N     . GLY B 1 170 ? 21.717  20.511  27.944  1.00 49.52  ?  118 GLY B N     1 
ATOM   2912 C  CA    . GLY B 1 170 ? 23.070  20.146  28.300  1.00 45.56  ?  118 GLY B CA    1 
ATOM   2913 C  C     . GLY B 1 170 ? 22.918  19.308  29.538  1.00 50.29  ?  118 GLY B C     1 
ATOM   2914 O  O     . GLY B 1 170 ? 22.358  19.778  30.527  1.00 55.50  ?  118 GLY B O     1 
ATOM   2915 N  N     . ASN B 1 171 ? 23.350  18.059  29.503  1.00 51.98  ?  119 ASN B N     1 
ATOM   2916 C  CA    . ASN B 1 171 ? 23.047  17.153  30.596  1.00 49.34  ?  119 ASN B CA    1 
ATOM   2917 C  C     . ASN B 1 171 ? 24.309  16.854  31.385  1.00 50.27  ?  119 ASN B C     1 
ATOM   2918 O  O     . ASN B 1 171 ? 25.420  17.222  30.988  1.00 50.89  ?  119 ASN B O     1 
ATOM   2919 C  CB    . ASN B 1 171 ? 22.414  15.862  30.075  1.00 49.61  ?  119 ASN B CB    1 
ATOM   2920 C  CG    . ASN B 1 171 ? 21.815  15.039  31.174  1.00 47.85  ?  119 ASN B CG    1 
ATOM   2921 O  OD1   . ASN B 1 171 ? 21.206  15.573  32.109  1.00 47.83  ?  119 ASN B OD1   1 
ATOM   2922 N  ND2   . ASN B 1 171 ? 21.999  13.736  31.092  1.00 45.78  ?  119 ASN B ND2   1 
ATOM   2923 N  N     . LYS B 1 172 ? 24.102  16.184  32.524  1.00 52.65  ?  120 LYS B N     1 
ATOM   2924 C  CA    . LYS B 1 172 ? 25.140  15.911  33.519  1.00 49.32  ?  120 LYS B CA    1 
ATOM   2925 C  C     . LYS B 1 172 ? 25.661  17.213  34.126  1.00 48.13  ?  120 LYS B C     1 
ATOM   2926 O  O     . LYS B 1 172 ? 26.867  17.399  34.289  1.00 48.62  ?  120 LYS B O     1 
ATOM   2927 C  CB    . LYS B 1 172 ? 26.280  15.066  32.933  1.00 49.70  ?  120 LYS B CB    1 
ATOM   2928 C  CG    . LYS B 1 172 ? 25.795  13.844  32.146  1.00 46.46  ?  120 LYS B CG    1 
ATOM   2929 C  CD    . LYS B 1 172 ? 26.940  12.918  31.743  1.00 45.29  ?  120 LYS B CD    1 
ATOM   2930 C  CE    . LYS B 1 172 ? 26.438  11.740  30.928  1.00 44.50  ?  120 LYS B CE    1 
ATOM   2931 N  NZ    . LYS B 1 172 ? 27.555  10.827  30.484  1.00 47.38  ?  120 LYS B NZ    1 
ATOM   2932 N  N     . SER B 1 173 ? 24.734  18.123  34.451  1.00 46.05  ?  121 SER B N     1 
ATOM   2933 C  CA    . SER B 1 173 ? 25.074  19.337  35.179  1.00 48.89  ?  121 SER B CA    1 
ATOM   2934 C  C     . SER B 1 173 ? 25.564  19.061  36.601  1.00 54.86  ?  121 SER B C     1 
ATOM   2935 O  O     . SER B 1 173 ? 26.247  19.905  37.189  1.00 56.78  ?  121 SER B O     1 
ATOM   2936 C  CB    . SER B 1 173 ? 23.867  20.265  35.223  1.00 50.44  ?  121 SER B CB    1 
ATOM   2937 O  OG    . SER B 1 173 ? 22.933  19.843  36.199  1.00 51.45  ?  121 SER B OG    1 
ATOM   2938 N  N     . ASP B 1 174 ? 25.244  17.907  37.173  1.00 52.54  ?  122 ASP B N     1 
ATOM   2939 C  CA    . ASP B 1 174 ? 25.776  17.605  38.491  1.00 55.01  ?  122 ASP B CA    1 
ATOM   2940 C  C     . ASP B 1 174 ? 27.250  17.236  38.456  1.00 59.10  ?  122 ASP B C     1 
ATOM   2941 O  O     . ASP B 1 174 ? 27.836  17.015  39.521  1.00 56.87  ?  122 ASP B O     1 
ATOM   2942 C  CB    . ASP B 1 174 ? 25.012  16.449  39.092  1.00 53.09  ?  122 ASP B CB    1 
ATOM   2943 C  CG    . ASP B 1 174 ? 25.123  15.232  38.238  1.00 51.31  ?  122 ASP B CG    1 
ATOM   2944 O  OD1   . ASP B 1 174 ? 24.553  15.257  37.130  1.00 46.19  ?  122 ASP B OD1   1 
ATOM   2945 O  OD2   . ASP B 1 174 ? 25.811  14.277  38.655  1.00 53.41  ?  122 ASP B OD2   1 
ATOM   2946 N  N     . LEU B 1 175 ? 27.855  17.117  37.279  1.00 56.03  ?  123 LEU B N     1 
ATOM   2947 C  CA    . LEU B 1 175 ? 29.271  16.762  37.202  1.00 56.16  ?  123 LEU B CA    1 
ATOM   2948 C  C     . LEU B 1 175 ? 30.099  18.014  36.947  1.00 58.03  ?  123 LEU B C     1 
ATOM   2949 O  O     . LEU B 1 175 ? 30.789  18.155  35.943  1.00 57.09  ?  123 LEU B O     1 
ATOM   2950 C  CB    . LEU B 1 175 ? 29.504  15.700  36.139  1.00 53.01  ?  123 LEU B CB    1 
ATOM   2951 C  CG    . LEU B 1 175 ? 28.911  14.310  36.396  1.00 55.25  ?  123 LEU B CG    1 
ATOM   2952 C  CD1   . LEU B 1 175 ? 29.531  13.273  35.463  1.00 53.36  ?  123 LEU B CD1   1 
ATOM   2953 C  CD2   . LEU B 1 175 ? 29.074  13.884  37.853  1.00 54.99  ?  123 LEU B CD2   1 
ATOM   2954 N  N     . GLU B 1 176 ? 30.009  18.922  37.922  1.00 60.68  ?  124 GLU B N     1 
ATOM   2955 C  CA    . GLU B 1 176 ? 30.558  20.265  37.766  1.00 61.24  ?  124 GLU B CA    1 
ATOM   2956 C  C     . GLU B 1 176 ? 32.063  20.227  37.536  1.00 61.97  ?  124 GLU B C     1 
ATOM   2957 O  O     . GLU B 1 176 ? 32.581  20.934  36.663  1.00 66.24  ?  124 GLU B O     1 
ATOM   2958 C  CB    . GLU B 1 176 ? 30.212  21.122  38.993  1.00 60.45  ?  124 GLU B CB    1 
ATOM   2959 C  CG    . GLU B 1 176 ? 28.690  21.293  39.269  1.00 60.75  ?  124 GLU B CG    1 
ATOM   2960 C  CD    . GLU B 1 176 ? 28.181  20.620  40.593  1.00 68.47  ?  124 GLU B CD    1 
ATOM   2961 O  OE1   . GLU B 1 176 ? 28.944  20.499  41.597  1.00 69.39  ?  124 GLU B OE1   1 
ATOM   2962 O  OE2   . GLU B 1 176 ? 26.980  20.244  40.641  1.00 64.37  ?  124 GLU B OE2   1 
ATOM   2963 N  N     . ASP B 1 177 ? 32.780  19.394  38.276  1.00 61.45  ?  125 ASP B N     1 
ATOM   2964 C  CA    . ASP B 1 177 ? 34.232  19.398  38.153  1.00 65.17  ?  125 ASP B CA    1 
ATOM   2965 C  C     . ASP B 1 177 ? 34.718  18.722  36.877  1.00 69.78  ?  125 ASP B C     1 
ATOM   2966 O  O     . ASP B 1 177 ? 35.928  18.518  36.726  1.00 72.03  ?  125 ASP B O     1 
ATOM   2967 C  CB    . ASP B 1 177 ? 34.869  18.744  39.381  1.00 67.66  ?  125 ASP B CB    1 
ATOM   2968 C  CG    . ASP B 1 177 ? 35.074  19.738  40.530  1.00 81.50  ?  125 ASP B CG    1 
ATOM   2969 O  OD1   . ASP B 1 177 ? 35.702  19.370  41.549  1.00 85.00  ?  125 ASP B OD1   1 
ATOM   2970 O  OD2   . ASP B 1 177 ? 34.606  20.898  40.417  1.00 81.93  ?  125 ASP B OD2   1 
ATOM   2971 N  N     . GLN B 1 178 ? 33.803  18.373  35.964  1.00 65.29  ?  126 GLN B N     1 
ATOM   2972 C  CA    . GLN B 1 178 ? 34.150  17.769  34.693  1.00 60.07  ?  126 GLN B CA    1 
ATOM   2973 C  C     . GLN B 1 178 ? 33.490  18.471  33.523  1.00 62.09  ?  126 GLN B C     1 
ATOM   2974 O  O     . GLN B 1 178 ? 33.683  18.051  32.376  1.00 62.77  ?  126 GLN B O     1 
ATOM   2975 C  CB    . GLN B 1 178 ? 33.764  16.290  34.671  1.00 62.63  ?  126 GLN B CB    1 
ATOM   2976 C  CG    . GLN B 1 178 ? 34.589  15.459  35.610  1.00 66.57  ?  126 GLN B CG    1 
ATOM   2977 C  CD    . GLN B 1 178 ? 33.726  14.596  36.495  1.00 65.95  ?  126 GLN B CD    1 
ATOM   2978 O  OE1   . GLN B 1 178 ? 33.335  13.488  36.110  1.00 71.19  ?  126 GLN B OE1   1 
ATOM   2979 N  NE2   . GLN B 1 178 ? 33.398  15.106  37.678  1.00 60.24  ?  126 GLN B NE2   1 
ATOM   2980 N  N     . ARG B 1 179 ? 32.703  19.505  33.781  1.00 59.14  ?  127 ARG B N     1 
ATOM   2981 C  CA    . ARG B 1 179 ? 32.182  20.335  32.715  1.00 56.79  ?  127 ARG B CA    1 
ATOM   2982 C  C     . ARG B 1 179 ? 33.325  20.833  31.845  1.00 59.62  ?  127 ARG B C     1 
ATOM   2983 O  O     . ARG B 1 179 ? 34.398  21.179  32.345  1.00 59.10  ?  127 ARG B O     1 
ATOM   2984 C  CB    . ARG B 1 179 ? 31.407  21.501  33.307  1.00 52.67  ?  127 ARG B CB    1 
ATOM   2985 C  CG    . ARG B 1 179 ? 30.651  22.299  32.314  1.00 55.42  ?  127 ARG B CG    1 
ATOM   2986 C  CD    . ARG B 1 179 ? 30.084  23.527  32.975  1.00 56.10  ?  127 ARG B CD    1 
ATOM   2987 N  NE    . ARG B 1 179 ? 29.198  24.219  32.057  1.00 57.06  ?  127 ARG B NE    1 
ATOM   2988 C  CZ    . ARG B 1 179 ? 27.897  24.373  32.263  1.00 60.91  ?  127 ARG B CZ    1 
ATOM   2989 N  NH1   . ARG B 1 179 ? 27.346  23.897  33.375  1.00 48.93  ?  127 ARG B NH1   1 
ATOM   2990 N  NH2   . ARG B 1 179 ? 27.156  25.010  31.354  1.00 60.56  ?  127 ARG B NH2   1 
ATOM   2991 N  N     . VAL B 1 180 ? 33.105  20.799  30.533  1.00 64.44  ?  128 VAL B N     1 
ATOM   2992 C  CA    . VAL B 1 180 ? 34.051  21.315  29.547  1.00 62.19  ?  128 VAL B CA    1 
ATOM   2993 C  C     . VAL B 1 180 ? 33.388  22.251  28.556  1.00 59.88  ?  128 VAL B C     1 
ATOM   2994 O  O     . VAL B 1 180 ? 34.094  22.982  27.854  1.00 60.26  ?  128 VAL B O     1 
ATOM   2995 C  CB    . VAL B 1 180 ? 34.756  20.175  28.783  1.00 58.35  ?  128 VAL B CB    1 
ATOM   2996 C  CG1   . VAL B 1 180 ? 35.788  19.496  29.656  1.00 59.19  ?  128 VAL B CG1   1 
ATOM   2997 C  CG2   . VAL B 1 180 ? 33.721  19.162  28.309  1.00 60.57  ?  128 VAL B CG2   1 
ATOM   2998 N  N     . VAL B 1 181 ? 32.066  22.238  28.460  1.00 60.81  ?  129 VAL B N     1 
ATOM   2999 C  CA    . VAL B 1 181 ? 31.315  23.145  27.608  1.00 60.98  ?  129 VAL B CA    1 
ATOM   3000 C  C     . VAL B 1 181 ? 30.925  24.348  28.449  1.00 66.20  ?  129 VAL B C     1 
ATOM   3001 O  O     . VAL B 1 181 ? 30.117  24.222  29.379  1.00 67.24  ?  129 VAL B O     1 
ATOM   3002 C  CB    . VAL B 1 181 ? 30.067  22.457  27.036  1.00 58.69  ?  129 VAL B CB    1 
ATOM   3003 C  CG1   . VAL B 1 181 ? 29.244  23.448  26.226  1.00 55.69  ?  129 VAL B CG1   1 
ATOM   3004 C  CG2   . VAL B 1 181 ? 30.454  21.239  26.222  1.00 57.19  ?  129 VAL B CG2   1 
ATOM   3005 N  N     . LYS B 1 182 ? 31.485  25.512  28.135  1.00 66.66  ?  130 LYS B N     1 
ATOM   3006 C  CA    . LYS B 1 182 ? 31.125  26.714  28.871  1.00 64.43  ?  130 LYS B CA    1 
ATOM   3007 C  C     . LYS B 1 182 ? 29.695  27.109  28.535  1.00 64.20  ?  130 LYS B C     1 
ATOM   3008 O  O     . LYS B 1 182 ? 29.269  27.033  27.379  1.00 66.28  ?  130 LYS B O     1 
ATOM   3009 C  CB    . LYS B 1 182 ? 32.088  27.856  28.545  1.00 66.79  ?  130 LYS B CB    1 
ATOM   3010 N  N     . GLU B 1 183 ? 28.959  27.542  29.559  1.00 65.14  ?  131 GLU B N     1 
ATOM   3011 C  CA    . GLU B 1 183 ? 27.536  27.828  29.401  1.00 64.54  ?  131 GLU B CA    1 
ATOM   3012 C  C     . GLU B 1 183 ? 27.267  28.878  28.331  1.00 65.35  ?  131 GLU B C     1 
ATOM   3013 O  O     . GLU B 1 183 ? 26.216  28.839  27.677  1.00 64.67  ?  131 GLU B O     1 
ATOM   3014 C  CB    . GLU B 1 183 ? 26.953  28.281  30.736  1.00 63.18  ?  131 GLU B CB    1 
ATOM   3015 C  CG    . GLU B 1 183 ? 25.565  28.880  30.626  1.00 66.69  ?  131 GLU B CG    1 
ATOM   3016 C  CD    . GLU B 1 183 ? 24.871  29.006  31.967  1.00 75.53  ?  131 GLU B CD    1 
ATOM   3017 O  OE1   . GLU B 1 183 ? 25.580  29.168  32.987  1.00 78.01  ?  131 GLU B OE1   1 
ATOM   3018 O  OE2   . GLU B 1 183 ? 23.617  28.934  32.002  1.00 78.90  ?  131 GLU B OE2   1 
ATOM   3019 N  N     . GLU B 1 184 ? 28.188  29.828  28.142  1.00 72.94  ?  132 GLU B N     1 
ATOM   3020 C  CA    . GLU B 1 184 ? 27.972  30.883  27.149  1.00 71.57  ?  132 GLU B CA    1 
ATOM   3021 C  C     . GLU B 1 184 ? 27.915  30.314  25.737  1.00 66.48  ?  132 GLU B C     1 
ATOM   3022 O  O     . GLU B 1 184 ? 26.990  30.617  24.974  1.00 62.05  ?  132 GLU B O     1 
ATOM   3023 C  CB    . GLU B 1 184 ? 29.075  31.930  27.242  1.00 73.81  ?  132 GLU B CB    1 
ATOM   3024 C  CG    . GLU B 1 184 ? 29.177  32.570  28.597  1.00 84.86  ?  132 GLU B CG    1 
ATOM   3025 C  CD    . GLU B 1 184 ? 30.600  32.618  29.085  1.00 95.95  ?  132 GLU B CD    1 
ATOM   3026 O  OE1   . GLU B 1 184 ? 31.273  33.643  28.844  1.00 105.97 ?  132 GLU B OE1   1 
ATOM   3027 O  OE2   . GLU B 1 184 ? 31.047  31.621  29.696  1.00 99.74  ?  132 GLU B OE2   1 
ATOM   3028 N  N     . GLU B 1 185 ? 28.916  29.505  25.364  1.00 66.93  ?  133 GLU B N     1 
ATOM   3029 C  CA    . GLU B 1 185 ? 28.882  28.815  24.079  1.00 64.20  ?  133 GLU B CA    1 
ATOM   3030 C  C     . GLU B 1 185 ? 27.560  28.087  23.886  1.00 62.28  ?  133 GLU B C     1 
ATOM   3031 O  O     . GLU B 1 185 ? 27.016  28.055  22.777  1.00 62.08  ?  133 GLU B O     1 
ATOM   3032 C  CB    . GLU B 1 185 ? 30.047  27.825  23.966  1.00 67.19  ?  133 GLU B CB    1 
ATOM   3033 C  CG    . GLU B 1 185 ? 31.357  28.396  23.400  1.00 71.89  ?  133 GLU B CG    1 
ATOM   3034 C  CD    . GLU B 1 185 ? 32.441  27.322  23.192  1.00 79.35  ?  133 GLU B CD    1 
ATOM   3035 O  OE1   . GLU B 1 185 ? 32.252  26.156  23.627  1.00 77.52  ?  133 GLU B OE1   1 
ATOM   3036 O  OE2   . GLU B 1 185 ? 33.500  27.654  22.609  1.00 81.61  ?  133 GLU B OE2   1 
ATOM   3037 N  N     . ALA B 1 186 ? 27.016  27.501  24.955  1.00 60.39  ?  134 ALA B N     1 
ATOM   3038 C  CA    . ALA B 1 186 ? 25.771  26.769  24.766  1.00 58.06  ?  134 ALA B CA    1 
ATOM   3039 C  C     . ALA B 1 186 ? 24.577  27.709  24.655  1.00 57.76  ?  134 ALA B C     1 
ATOM   3040 O  O     . ALA B 1 186 ? 23.664  27.465  23.862  1.00 58.42  ?  134 ALA B O     1 
ATOM   3041 C  CB    . ALA B 1 186 ? 25.567  25.764  25.891  1.00 49.96  ?  134 ALA B CB    1 
ATOM   3042 N  N     . ILE B 1 187 ? 24.558  28.791  25.431  1.00 62.33  ?  135 ILE B N     1 
ATOM   3043 C  CA    . ILE B 1 187 ? 23.422  29.706  25.349  1.00 60.96  ?  135 ILE B CA    1 
ATOM   3044 C  C     . ILE B 1 187 ? 23.407  30.412  23.998  1.00 60.45  ?  135 ILE B C     1 
ATOM   3045 O  O     . ILE B 1 187 ? 22.337  30.725  23.461  1.00 57.02  ?  135 ILE B O     1 
ATOM   3046 C  CB    . ILE B 1 187 ? 23.468  30.691  26.538  1.00 61.18  ?  135 ILE B CB    1 
ATOM   3047 C  CG1   . ILE B 1 187 ? 23.153  29.938  27.842  1.00 62.18  ?  135 ILE B CG1   1 
ATOM   3048 C  CG2   . ILE B 1 187 ? 22.512  31.875  26.337  1.00 50.90  ?  135 ILE B CG2   1 
ATOM   3049 C  CD1   . ILE B 1 187 ? 22.763  30.823  29.018  1.00 60.69  ?  135 ILE B CD1   1 
ATOM   3050 N  N     . ALA B 1 188 ? 24.589  30.644  23.418  1.00 57.88  ?  136 ALA B N     1 
ATOM   3051 C  CA    . ALA B 1 188 ? 24.682  31.354  22.151  1.00 59.85  ?  136 ALA B CA    1 
ATOM   3052 C  C     . ALA B 1 188 ? 24.203  30.485  20.999  1.00 61.09  ?  136 ALA B C     1 
ATOM   3053 O  O     . ALA B 1 188 ? 23.443  30.952  20.139  1.00 58.83  ?  136 ALA B O     1 
ATOM   3054 C  CB    . ALA B 1 188 ? 26.121  31.804  21.915  1.00 58.33  ?  136 ALA B CB    1 
ATOM   3055 N  N     . LEU B 1 189 ? 24.644  29.220  20.967  1.00 60.09  ?  137 LEU B N     1 
ATOM   3056 C  CA    . LEU B 1 189 ? 24.131  28.258  19.998  1.00 56.98  ?  137 LEU B CA    1 
ATOM   3057 C  C     . LEU B 1 189 ? 22.612  28.198  20.039  1.00 56.98  ?  137 LEU B C     1 
ATOM   3058 O  O     . LEU B 1 189 ? 21.945  28.234  18.998  1.00 57.06  ?  137 LEU B O     1 
ATOM   3059 C  CB    . LEU B 1 189 ? 24.711  26.874  20.276  1.00 55.59  ?  137 LEU B CB    1 
ATOM   3060 C  CG    . LEU B 1 189 ? 24.268  25.835  19.249  1.00 55.14  ?  137 LEU B CG    1 
ATOM   3061 C  CD1   . LEU B 1 189 ? 25.186  25.882  18.045  1.00 60.31  ?  137 LEU B CD1   1 
ATOM   3062 C  CD2   . LEU B 1 189 ? 24.262  24.452  19.837  1.00 56.20  ?  137 LEU B CD2   1 
ATOM   3063 N  N     . ALA B 1 190 ? 22.046  28.097  21.242  1.00 54.13  ?  138 ALA B N     1 
ATOM   3064 C  CA    . ALA B 1 190 ? 20.596  27.997  21.356  1.00 55.15  ?  138 ALA B CA    1 
ATOM   3065 C  C     . ALA B 1 190 ? 19.921  29.256  20.840  1.00 55.33  ?  138 ALA B C     1 
ATOM   3066 O  O     . ALA B 1 190 ? 18.900  29.181  20.143  1.00 56.70  ?  138 ALA B O     1 
ATOM   3067 C  CB    . ALA B 1 190 ? 20.196  27.718  22.805  1.00 53.27  ?  138 ALA B CB    1 
ATOM   3068 N  N     . GLU B 1 191 ? 20.493  30.424  21.143  1.00 54.16  ?  139 GLU B N     1 
ATOM   3069 C  CA    . GLU B 1 191 ? 19.900  31.671  20.672  1.00 58.04  ?  139 GLU B CA    1 
ATOM   3070 C  C     . GLU B 1 191 ? 19.943  31.746  19.150  1.00 59.15  ?  139 GLU B C     1 
ATOM   3071 O  O     . GLU B 1 191 ? 18.981  32.193  18.511  1.00 56.62  ?  139 GLU B O     1 
ATOM   3072 C  CB    . GLU B 1 191 ? 20.620  32.868  21.303  1.00 55.25  ?  139 GLU B CB    1 
ATOM   3073 N  N     . LYS B 1 192 ? 21.050  31.280  18.560  1.00 56.54  ?  140 LYS B N     1 
ATOM   3074 C  CA    . LYS B 1 192 ? 21.233  31.285  17.110  1.00 59.68  ?  140 LYS B CA    1 
ATOM   3075 C  C     . LYS B 1 192 ? 20.086  30.597  16.375  1.00 56.31  ?  140 LYS B C     1 
ATOM   3076 O  O     . LYS B 1 192 ? 19.730  30.997  15.263  1.00 49.99  ?  140 LYS B O     1 
ATOM   3077 C  CB    . LYS B 1 192 ? 22.545  30.577  16.784  1.00 60.19  ?  140 LYS B CB    1 
ATOM   3078 C  CG    . LYS B 1 192 ? 23.485  31.305  15.886  1.00 63.56  ?  140 LYS B CG    1 
ATOM   3079 C  CD    . LYS B 1 192 ? 24.923  30.919  16.193  1.00 59.10  ?  140 LYS B CD    1 
ATOM   3080 C  CE    . LYS B 1 192 ? 25.485  31.772  17.312  1.00 67.56  ?  140 LYS B CE    1 
ATOM   3081 N  NZ    . LYS B 1 192 ? 26.958  31.527  17.445  1.00 72.21  ?  140 LYS B NZ    1 
ATOM   3082 N  N     . TYR B 1 193 ? 19.512  29.549  16.971  1.00 57.31  ?  141 TYR B N     1 
ATOM   3083 C  CA    . TYR B 1 193 ? 18.463  28.766  16.341  1.00 51.58  ?  141 TYR B CA    1 
ATOM   3084 C  C     . TYR B 1 193 ? 17.073  29.051  16.892  1.00 53.45  ?  141 TYR B C     1 
ATOM   3085 O  O     . TYR B 1 193 ? 16.099  28.490  16.380  1.00 55.30  ?  141 TYR B O     1 
ATOM   3086 C  CB    . TYR B 1 193 ? 18.741  27.275  16.512  1.00 51.57  ?  141 TYR B CB    1 
ATOM   3087 C  CG    . TYR B 1 193 ? 19.888  26.684  15.722  1.00 47.97  ?  141 TYR B CG    1 
ATOM   3088 C  CD1   . TYR B 1 193 ? 19.658  26.015  14.539  1.00 48.06  ?  141 TYR B CD1   1 
ATOM   3089 C  CD2   . TYR B 1 193 ? 21.184  26.725  16.207  1.00 49.17  ?  141 TYR B CD2   1 
ATOM   3090 C  CE1   . TYR B 1 193 ? 20.693  25.437  13.832  1.00 50.05  ?  141 TYR B CE1   1 
ATOM   3091 C  CE2   . TYR B 1 193 ? 22.228  26.144  15.516  1.00 48.59  ?  141 TYR B CE2   1 
ATOM   3092 C  CZ    . TYR B 1 193 ? 21.978  25.502  14.326  1.00 52.07  ?  141 TYR B CZ    1 
ATOM   3093 O  OH    . TYR B 1 193 ? 23.019  24.928  13.616  1.00 55.28  ?  141 TYR B OH    1 
ATOM   3094 N  N     . GLY B 1 194 ? 16.948  29.869  17.930  1.00 55.48  ?  142 GLY B N     1 
ATOM   3095 C  CA    . GLY B 1 194 ? 15.632  30.120  18.495  1.00 52.74  ?  142 GLY B CA    1 
ATOM   3096 C  C     . GLY B 1 194 ? 15.048  28.964  19.284  1.00 58.05  ?  142 GLY B C     1 
ATOM   3097 O  O     . GLY B 1 194 ? 13.824  28.765  19.261  1.00 59.05  ?  142 GLY B O     1 
ATOM   3098 N  N     . ILE B 1 195 ? 15.883  28.206  19.999  1.00 55.99  ?  143 ILE B N     1 
ATOM   3099 C  CA    . ILE B 1 195 ? 15.424  27.045  20.766  1.00 54.70  ?  143 ILE B CA    1 
ATOM   3100 C  C     . ILE B 1 195 ? 15.687  27.204  22.262  1.00 58.55  ?  143 ILE B C     1 
ATOM   3101 O  O     . ILE B 1 195 ? 16.748  27.711  22.670  1.00 56.05  ?  143 ILE B O     1 
ATOM   3102 C  CB    . ILE B 1 195 ? 16.083  25.760  20.259  1.00 52.57  ?  143 ILE B CB    1 
ATOM   3103 C  CG1   . ILE B 1 195 ? 17.590  25.846  20.441  1.00 53.26  ?  143 ILE B CG1   1 
ATOM   3104 C  CG2   . ILE B 1 195 ? 15.778  25.549  18.794  1.00 53.48  ?  143 ILE B CG2   1 
ATOM   3105 C  CD1   . ILE B 1 195 ? 18.281  24.526  20.221  1.00 53.56  ?  143 ILE B CD1   1 
ATOM   3106 N  N     . PRO B 1 196 ? 14.754  26.774  23.114  1.00 56.35  ?  144 PRO B N     1 
ATOM   3107 C  CA    . PRO B 1 196 ? 14.966  26.884  24.567  1.00 57.87  ?  144 PRO B CA    1 
ATOM   3108 C  C     . PRO B 1 196 ? 16.102  25.996  25.058  1.00 55.72  ?  144 PRO B C     1 
ATOM   3109 O  O     . PRO B 1 196 ? 16.259  24.846  24.635  1.00 56.13  ?  144 PRO B O     1 
ATOM   3110 C  CB    . PRO B 1 196 ? 13.620  26.442  25.164  1.00 54.92  ?  144 PRO B CB    1 
ATOM   3111 C  CG    . PRO B 1 196 ? 12.622  26.615  24.059  1.00 57.32  ?  144 PRO B CG    1 
ATOM   3112 C  CD    . PRO B 1 196 ? 13.384  26.356  22.770  1.00 54.72  ?  144 PRO B CD    1 
ATOM   3113 N  N     . TYR B 1 197 ? 16.892  26.534  25.975  1.00 51.70  ?  145 TYR B N     1 
ATOM   3114 C  CA    . TYR B 1 197 ? 18.044  25.825  26.502  1.00 53.15  ?  145 TYR B CA    1 
ATOM   3115 C  C     . TYR B 1 197 ? 17.871  25.588  27.998  1.00 54.19  ?  145 TYR B C     1 
ATOM   3116 O  O     . TYR B 1 197 ? 17.392  26.462  28.721  1.00 55.86  ?  145 TYR B O     1 
ATOM   3117 C  CB    . TYR B 1 197 ? 19.306  26.614  26.232  1.00 50.10  ?  145 TYR B CB    1 
ATOM   3118 C  CG    . TYR B 1 197 ? 20.543  26.005  26.804  1.00 50.28  ?  145 TYR B CG    1 
ATOM   3119 C  CD1   . TYR B 1 197 ? 20.913  24.725  26.462  1.00 48.81  ?  145 TYR B CD1   1 
ATOM   3120 C  CD2   . TYR B 1 197 ? 21.347  26.716  27.693  1.00 52.40  ?  145 TYR B CD2   1 
ATOM   3121 C  CE1   . TYR B 1 197 ? 22.060  24.149  26.983  1.00 51.74  ?  145 TYR B CE1   1 
ATOM   3122 C  CE2   . TYR B 1 197 ? 22.502  26.153  28.215  1.00 52.32  ?  145 TYR B CE2   1 
ATOM   3123 C  CZ    . TYR B 1 197 ? 22.849  24.863  27.858  1.00 51.93  ?  145 TYR B CZ    1 
ATOM   3124 O  OH    . TYR B 1 197 ? 23.990  24.275  28.374  1.00 49.45  ?  145 TYR B OH    1 
ATOM   3125 N  N     . PHE B 1 198 ? 18.264  24.398  28.451  1.00 55.32  ?  146 PHE B N     1 
ATOM   3126 C  CA    . PHE B 1 198 ? 18.190  23.994  29.850  1.00 49.21  ?  146 PHE B CA    1 
ATOM   3127 C  C     . PHE B 1 198 ? 19.422  23.174  30.198  1.00 53.30  ?  146 PHE B C     1 
ATOM   3128 O  O     . PHE B 1 198 ? 19.790  22.266  29.451  1.00 52.08  ?  146 PHE B O     1 
ATOM   3129 C  CB    . PHE B 1 198 ? 16.951  23.144  30.112  1.00 46.16  ?  146 PHE B CB    1 
ATOM   3130 C  CG    . PHE B 1 198 ? 15.684  23.911  30.114  1.00 51.97  ?  146 PHE B CG    1 
ATOM   3131 C  CD1   . PHE B 1 198 ? 14.934  24.041  28.953  1.00 53.63  ?  146 PHE B CD1   1 
ATOM   3132 C  CD2   . PHE B 1 198 ? 15.229  24.503  31.270  1.00 48.76  ?  146 PHE B CD2   1 
ATOM   3133 C  CE1   . PHE B 1 198 ? 13.741  24.758  28.954  1.00 54.59  ?  146 PHE B CE1   1 
ATOM   3134 C  CE2   . PHE B 1 198 ? 14.051  25.228  31.274  1.00 52.68  ?  146 PHE B CE2   1 
ATOM   3135 C  CZ    . PHE B 1 198 ? 13.300  25.348  30.120  1.00 54.61  ?  146 PHE B CZ    1 
ATOM   3136 N  N     . GLU B 1 199 ? 20.037  23.449  31.341  1.00 56.12  ?  147 GLU B N     1 
ATOM   3137 C  CA    . GLU B 1 199 ? 21.055  22.545  31.856  1.00 54.84  ?  147 GLU B CA    1 
ATOM   3138 C  C     . GLU B 1 199 ? 20.392  21.579  32.834  1.00 54.11  ?  147 GLU B C     1 
ATOM   3139 O  O     . GLU B 1 199 ? 19.702  22.001  33.768  1.00 54.20  ?  147 GLU B O     1 
ATOM   3140 C  CB    . GLU B 1 199 ? 22.192  23.322  32.513  1.00 54.28  ?  147 GLU B CB    1 
ATOM   3141 C  CG    . GLU B 1 199 ? 22.670  24.498  31.657  1.00 58.12  ?  147 GLU B CG    1 
ATOM   3142 C  CD    . GLU B 1 199 ? 24.171  24.728  31.741  1.00 58.94  ?  147 GLU B CD    1 
ATOM   3143 O  OE1   . GLU B 1 199 ? 24.771  25.121  30.722  1.00 57.55  ?  147 GLU B OE1   1 
ATOM   3144 O  OE2   . GLU B 1 199 ? 24.762  24.516  32.824  1.00 61.37  ?  147 GLU B OE2   1 
ATOM   3145 N  N     . THR B 1 200 ? 20.573  20.285  32.596  1.00 51.81  ?  148 THR B N     1 
ATOM   3146 C  CA    . THR B 1 200 ? 19.818  19.253  33.290  1.00 49.85  ?  148 THR B CA    1 
ATOM   3147 C  C     . THR B 1 200 ? 20.767  18.290  33.984  1.00 49.22  ?  148 THR B C     1 
ATOM   3148 O  O     . THR B 1 200 ? 21.970  18.257  33.703  1.00 51.16  ?  148 THR B O     1 
ATOM   3149 C  CB    . THR B 1 200 ? 18.938  18.468  32.313  1.00 53.53  ?  148 THR B CB    1 
ATOM   3150 O  OG1   . THR B 1 200 ? 19.776  17.899  31.308  1.00 53.89  ?  148 THR B OG1   1 
ATOM   3151 C  CG2   . THR B 1 200 ? 17.894  19.360  31.639  1.00 51.41  ?  148 THR B CG2   1 
ATOM   3152 N  N     . SER B 1 201 ? 20.207  17.501  34.904  1.00 48.88  ?  149 SER B N     1 
ATOM   3153 C  CA    . SER B 1 201 ? 20.931  16.374  35.487  1.00 46.54  ?  149 SER B CA    1 
ATOM   3154 C  C     . SER B 1 201 ? 19.937  15.260  35.753  1.00 45.56  ?  149 SER B C     1 
ATOM   3155 O  O     . SER B 1 201 ? 18.988  15.455  36.515  1.00 50.06  ?  149 SER B O     1 
ATOM   3156 C  CB    . SER B 1 201 ? 21.647  16.757  36.782  1.00 46.08  ?  149 SER B CB    1 
ATOM   3157 O  OG    . SER B 1 201 ? 22.197  15.597  37.408  1.00 44.45  ?  149 SER B OG    1 
ATOM   3158 N  N     . ALA B 1 202 ? 20.152  14.103  35.127  1.00 45.95  ?  150 ALA B N     1 
ATOM   3159 C  CA    . ALA B 1 202 ? 19.330  12.928  35.394  1.00 47.44  ?  150 ALA B CA    1 
ATOM   3160 C  C     . ALA B 1 202 ? 19.652  12.274  36.740  1.00 47.63  ?  150 ALA B C     1 
ATOM   3161 O  O     . ALA B 1 202 ? 18.812  11.535  37.285  1.00 43.02  ?  150 ALA B O     1 
ATOM   3162 C  CB    . ALA B 1 202 ? 19.514  11.908  34.271  1.00 46.23  ?  150 ALA B CB    1 
ATOM   3163 N  N     . ALA B 1 203 ? 20.852  12.514  37.276  1.00 46.25  ?  151 ALA B N     1 
ATOM   3164 C  CA    . ALA B 1 203 ? 21.184  11.994  38.595  1.00 45.79  ?  151 ALA B CA    1 
ATOM   3165 C  C     . ALA B 1 203 ? 20.254  12.572  39.651  1.00 44.21  ?  151 ALA B C     1 
ATOM   3166 O  O     . ALA B 1 203 ? 19.666  11.826  40.440  1.00 45.06  ?  151 ALA B O     1 
ATOM   3167 C  CB    . ALA B 1 203 ? 22.644  12.292  38.935  1.00 45.66  ?  151 ALA B CB    1 
ATOM   3168 N  N     . ASN B 1 204 ? 20.076  13.898  39.669  1.00 46.48  ?  152 ASN B N     1 
ATOM   3169 C  CA    . ASN B 1 204 ? 19.305  14.518  40.743  1.00 48.37  ?  152 ASN B CA    1 
ATOM   3170 C  C     . ASN B 1 204 ? 18.038  15.238  40.299  1.00 51.55  ?  152 ASN B C     1 
ATOM   3171 O  O     . ASN B 1 204 ? 17.356  15.821  41.152  1.00 49.93  ?  152 ASN B O     1 
ATOM   3172 C  CB    . ASN B 1 204 ? 20.180  15.487  41.550  1.00 46.91  ?  152 ASN B CB    1 
ATOM   3173 C  CG    . ASN B 1 204 ? 20.674  16.660  40.736  1.00 47.55  ?  152 ASN B CG    1 
ATOM   3174 O  OD1   . ASN B 1 204 ? 19.894  17.350  40.071  1.00 48.02  ?  152 ASN B OD1   1 
ATOM   3175 N  ND2   . ASN B 1 204 ? 21.990  16.915  40.803  1.00 45.37  ?  152 ASN B ND2   1 
ATOM   3176 N  N     . GLY B 1 205 ? 17.698  15.220  39.007  1.00 48.81  ?  153 GLY B N     1 
ATOM   3177 C  CA    . GLY B 1 205 ? 16.406  15.706  38.560  1.00 50.20  ?  153 GLY B CA    1 
ATOM   3178 C  C     . GLY B 1 205 ? 16.334  17.167  38.177  1.00 48.18  ?  153 GLY B C     1 
ATOM   3179 O  O     . GLY B 1 205 ? 15.275  17.614  37.704  1.00 45.06  ?  153 GLY B O     1 
ATOM   3180 N  N     . THR B 1 206 ? 17.412  17.928  38.364  1.00 49.28  ?  154 THR B N     1 
ATOM   3181 C  CA    . THR B 1 206 ? 17.380  19.357  38.067  1.00 51.53  ?  154 THR B CA    1 
ATOM   3182 C  C     . THR B 1 206 ? 16.915  19.628  36.646  1.00 50.41  ?  154 THR B C     1 
ATOM   3183 O  O     . THR B 1 206 ? 17.433  19.048  35.687  1.00 52.20  ?  154 THR B O     1 
ATOM   3184 C  CB    . THR B 1 206 ? 18.762  19.961  38.271  1.00 53.20  ?  154 THR B CB    1 
ATOM   3185 O  OG1   . THR B 1 206 ? 19.266  19.550  39.549  1.00 54.26  ?  154 THR B OG1   1 
ATOM   3186 C  CG2   . THR B 1 206 ? 18.678  21.476  38.217  1.00 48.12  ?  154 THR B CG2   1 
ATOM   3187 N  N     . ASN B 1 207 ? 15.912  20.501  36.522  1.00 52.95  ?  155 ASN B N     1 
ATOM   3188 C  CA    . ASN B 1 207 ? 15.479  21.063  35.247  1.00 52.46  ?  155 ASN B CA    1 
ATOM   3189 C  C     . ASN B 1 207 ? 14.792  20.057  34.337  1.00 52.54  ?  155 ASN B C     1 
ATOM   3190 O  O     . ASN B 1 207 ? 14.243  20.441  33.299  1.00 53.38  ?  155 ASN B O     1 
ATOM   3191 C  CB    . ASN B 1 207 ? 16.662  21.676  34.507  1.00 51.06  ?  155 ASN B CB    1 
ATOM   3192 C  CG    . ASN B 1 207 ? 16.993  23.052  35.006  1.00 53.01  ?  155 ASN B CG    1 
ATOM   3193 O  OD1   . ASN B 1 207 ? 16.103  23.809  35.397  1.00 53.33  ?  155 ASN B OD1   1 
ATOM   3194 N  ND2   . ASN B 1 207 ? 18.274  23.394  34.997  1.00 50.89  ?  155 ASN B ND2   1 
ATOM   3195 N  N     . ILE B 1 208 ? 14.821  18.776  34.716  1.00 52.63  ?  156 ILE B N     1 
ATOM   3196 C  CA    . ILE B 1 208 ? 14.213  17.728  33.900  1.00 49.64  ?  156 ILE B CA    1 
ATOM   3197 C  C     . ILE B 1 208 ? 12.739  18.026  33.661  1.00 51.71  ?  156 ILE B C     1 
ATOM   3198 O  O     . ILE B 1 208 ? 12.246  17.961  32.530  1.00 50.66  ?  156 ILE B O     1 
ATOM   3199 C  CB    . ILE B 1 208 ? 14.408  16.355  34.564  1.00 48.25  ?  156 ILE B CB    1 
ATOM   3200 C  CG1   . ILE B 1 208 ? 15.892  16.019  34.641  1.00 48.63  ?  156 ILE B CG1   1 
ATOM   3201 C  CG2   . ILE B 1 208 ? 13.668  15.282  33.807  1.00 49.33  ?  156 ILE B CG2   1 
ATOM   3202 C  CD1   . ILE B 1 208 ? 16.381  15.164  33.537  1.00 46.64  ?  156 ILE B CD1   1 
ATOM   3203 N  N     . SER B 1 209 ? 12.007  18.349  34.720  1.00 52.79  ?  157 SER B N     1 
ATOM   3204 C  CA    . SER B 1 209 ? 10.584  18.576  34.523  1.00 55.24  ?  157 SER B CA    1 
ATOM   3205 C  C     . SER B 1 209 ? 10.349  19.869  33.755  1.00 57.26  ?  157 SER B C     1 
ATOM   3206 O  O     . SER B 1 209 ? 9.474   19.929  32.879  1.00 58.83  ?  157 SER B O     1 
ATOM   3207 C  CB    . SER B 1 209 ? 9.859   18.584  35.865  1.00 55.94  ?  157 SER B CB    1 
ATOM   3208 O  OG    . SER B 1 209 ? 9.617   19.917  36.279  1.00 64.83  ?  157 SER B OG    1 
ATOM   3209 N  N     . GLN B 1 210 ? 11.145  20.904  34.034  1.00 57.11  ?  158 GLN B N     1 
ATOM   3210 C  CA    . GLN B 1 210 ? 10.931  22.187  33.368  1.00 53.58  ?  158 GLN B CA    1 
ATOM   3211 C  C     . GLN B 1 210 ? 11.243  22.090  31.884  1.00 55.76  ?  158 GLN B C     1 
ATOM   3212 O  O     . GLN B 1 210 ? 10.489  22.605  31.047  1.00 54.36  ?  158 GLN B O     1 
ATOM   3213 C  CB    . GLN B 1 210 ? 11.778  23.268  34.035  1.00 53.22  ?  158 GLN B CB    1 
ATOM   3214 C  CG    . GLN B 1 210 ? 11.357  23.544  35.506  1.00 65.73  ?  158 GLN B CG    1 
ATOM   3215 C  CD    . GLN B 1 210 ? 12.222  22.838  36.568  1.00 58.73  ?  158 GLN B CD    1 
ATOM   3216 O  OE1   . GLN B 1 210 ? 12.372  21.606  36.577  1.00 57.78  ?  158 GLN B OE1   1 
ATOM   3217 N  NE2   . GLN B 1 210 ? 12.774  23.627  37.481  1.00 59.34  ?  158 GLN B NE2   1 
ATOM   3218 N  N     . ALA B 1 211 ? 12.346  21.420  31.543  1.00 54.75  ?  159 ALA B N     1 
ATOM   3219 C  CA    . ALA B 1 211 ? 12.701  21.214  30.143  1.00 53.75  ?  159 ALA B CA    1 
ATOM   3220 C  C     . ALA B 1 211 ? 11.561  20.553  29.374  1.00 57.27  ?  159 ALA B C     1 
ATOM   3221 O  O     . ALA B 1 211 ? 11.081  21.093  28.370  1.00 58.69  ?  159 ALA B O     1 
ATOM   3222 C  CB    . ALA B 1 211 ? 13.974  20.376  30.051  1.00 48.95  ?  159 ALA B CB    1 
ATOM   3223 N  N     . ILE B 1 212 ? 11.105  19.386  29.837  1.00 53.15  ?  160 ILE B N     1 
ATOM   3224 C  CA    . ILE B 1 212 ? 10.070  18.667  29.109  1.00 51.91  ?  160 ILE B CA    1 
ATOM   3225 C  C     . ILE B 1 212 ? 8.771   19.453  29.094  1.00 56.20  ?  160 ILE B C     1 
ATOM   3226 O  O     . ILE B 1 212 ? 8.109   19.563  28.054  1.00 60.40  ?  160 ILE B O     1 
ATOM   3227 C  CB    . ILE B 1 212 ? 9.871   17.273  29.709  1.00 56.69  ?  160 ILE B CB    1 
ATOM   3228 C  CG1   . ILE B 1 212 ? 11.078  16.393  29.390  1.00 52.88  ?  160 ILE B CG1   1 
ATOM   3229 C  CG2   . ILE B 1 212 ? 8.579   16.668  29.194  1.00 57.51  ?  160 ILE B CG2   1 
ATOM   3230 C  CD1   . ILE B 1 212 ? 11.161  15.165  30.272  1.00 52.67  ?  160 ILE B CD1   1 
ATOM   3231 N  N     . GLU B 1 213 ? 8.385   20.021  30.236  1.00 56.70  ?  161 GLU B N     1 
ATOM   3232 C  CA    . GLU B 1 213 ? 7.172   20.834  30.271  1.00 59.48  ?  161 GLU B CA    1 
ATOM   3233 C  C     . GLU B 1 213 ? 7.255   21.998  29.303  1.00 55.76  ?  161 GLU B C     1 
ATOM   3234 O  O     . GLU B 1 213 ? 6.227   22.456  28.792  1.00 56.31  ?  161 GLU B O     1 
ATOM   3235 C  CB    . GLU B 1 213 ? 6.917   21.356  31.684  1.00 56.56  ?  161 GLU B CB    1 
ATOM   3236 C  CG    . GLU B 1 213 ? 6.129   20.397  32.536  1.00 59.52  ?  161 GLU B CG    1 
ATOM   3237 C  CD    . GLU B 1 213 ? 6.507   20.502  33.999  1.00 67.59  ?  161 GLU B CD    1 
ATOM   3238 O  OE1   . GLU B 1 213 ? 6.731   21.641  34.477  1.00 68.64  ?  161 GLU B OE1   1 
ATOM   3239 O  OE2   . GLU B 1 213 ? 6.602   19.445  34.667  1.00 72.44  ?  161 GLU B OE2   1 
ATOM   3240 N  N     . MET B 1 214 ? 8.467   22.494  29.056  1.00 52.98  ?  162 MET B N     1 
ATOM   3241 C  CA    . MET B 1 214 ? 8.659   23.531  28.058  1.00 54.03  ?  162 MET B CA    1 
ATOM   3242 C  C     . MET B 1 214 ? 8.383   22.995  26.651  1.00 61.02  ?  162 MET B C     1 
ATOM   3243 O  O     . MET B 1 214 ? 7.807   23.701  25.812  1.00 58.05  ?  162 MET B O     1 
ATOM   3244 C  CB    . MET B 1 214 ? 10.079  24.087  28.189  1.00 54.20  ?  162 MET B CB    1 
ATOM   3245 C  CG    . MET B 1 214 ? 10.544  25.009  27.071  1.00 56.80  ?  162 MET B CG    1 
ATOM   3246 S  SD    . MET B 1 214 ? 9.678   26.587  26.959  1.00 66.93  ?  162 MET B SD    1 
ATOM   3247 C  CE    . MET B 1 214 ? 10.322  27.475  28.395  1.00 63.72  ?  162 MET B CE    1 
ATOM   3248 N  N     . LEU B 1 215 ? 8.775   21.744  26.374  1.00 57.96  ?  163 LEU B N     1 
ATOM   3249 C  CA    . LEU B 1 215 ? 8.521   21.175  25.051  1.00 58.48  ?  163 LEU B CA    1 
ATOM   3250 C  C     . LEU B 1 215 ? 7.038   20.899  24.858  1.00 60.19  ?  163 LEU B C     1 
ATOM   3251 O  O     . LEU B 1 215 ? 6.473   21.180  23.792  1.00 59.64  ?  163 LEU B O     1 
ATOM   3252 C  CB    . LEU B 1 215 ? 9.326   19.888  24.861  1.00 55.76  ?  163 LEU B CB    1 
ATOM   3253 C  CG    . LEU B 1 215 ? 9.248   19.188  23.500  1.00 54.10  ?  163 LEU B CG    1 
ATOM   3254 C  CD1   . LEU B 1 215 ? 9.967   20.003  22.438  1.00 52.19  ?  163 LEU B CD1   1 
ATOM   3255 C  CD2   . LEU B 1 215 ? 9.833   17.784  23.560  1.00 52.46  ?  163 LEU B CD2   1 
ATOM   3256 N  N     . LEU B 1 216 ? 6.400   20.341  25.886  1.00 61.02  ?  164 LEU B N     1 
ATOM   3257 C  CA    . LEU B 1 216 ? 4.958   20.145  25.871  1.00 60.94  ?  164 LEU B CA    1 
ATOM   3258 C  C     . LEU B 1 216 ? 4.230   21.448  25.554  1.00 63.77  ?  164 LEU B C     1 
ATOM   3259 O  O     . LEU B 1 216 ? 3.326   21.480  24.709  1.00 65.33  ?  164 LEU B O     1 
ATOM   3260 C  CB    . LEU B 1 216 ? 4.523   19.579  27.222  1.00 57.14  ?  164 LEU B CB    1 
ATOM   3261 C  CG    . LEU B 1 216 ? 3.076   19.118  27.376  1.00 63.43  ?  164 LEU B CG    1 
ATOM   3262 C  CD1   . LEU B 1 216 ? 2.727   18.001  26.390  1.00 66.13  ?  164 LEU B CD1   1 
ATOM   3263 C  CD2   . LEU B 1 216 ? 2.857   18.665  28.790  1.00 61.92  ?  164 LEU B CD2   1 
ATOM   3264 N  N     . ASP B 1 217 ? 4.641   22.546  26.206  1.00 64.80  ?  165 ASP B N     1 
ATOM   3265 C  CA    . ASP B 1 217 ? 4.018   23.849  25.968  1.00 67.61  ?  165 ASP B CA    1 
ATOM   3266 C  C     . ASP B 1 217 ? 4.188   24.286  24.521  1.00 65.21  ?  165 ASP B C     1 
ATOM   3267 O  O     . ASP B 1 217 ? 3.244   24.780  23.897  1.00 64.06  ?  165 ASP B O     1 
ATOM   3268 C  CB    . ASP B 1 217 ? 4.619   24.898  26.904  1.00 68.95  ?  165 ASP B CB    1 
ATOM   3269 C  CG    . ASP B 1 217 ? 3.757   26.151  27.021  1.00 72.75  ?  165 ASP B CG    1 
ATOM   3270 O  OD1   . ASP B 1 217 ? 2.523   26.054  26.836  1.00 73.82  ?  165 ASP B OD1   1 
ATOM   3271 O  OD2   . ASP B 1 217 ? 4.318   27.235  27.298  1.00 73.57  ?  165 ASP B OD2   1 
ATOM   3272 N  N     . LEU B 1 218 ? 5.396   24.127  23.983  1.00 65.95  ?  166 LEU B N     1 
ATOM   3273 C  CA    . LEU B 1 218 ? 5.646   24.407  22.577  1.00 61.81  ?  166 LEU B CA    1 
ATOM   3274 C  C     . LEU B 1 218 ? 4.754   23.566  21.679  1.00 66.45  ?  166 LEU B C     1 
ATOM   3275 O  O     . LEU B 1 218 ? 4.274   24.040  20.644  1.00 69.11  ?  166 LEU B O     1 
ATOM   3276 C  CB    . LEU B 1 218 ? 7.107   24.127  22.257  1.00 58.88  ?  166 LEU B CB    1 
ATOM   3277 C  CG    . LEU B 1 218 ? 8.093   25.217  22.628  1.00 59.41  ?  166 LEU B CG    1 
ATOM   3278 C  CD1   . LEU B 1 218 ? 9.469   24.773  22.176  1.00 61.35  ?  166 LEU B CD1   1 
ATOM   3279 C  CD2   . LEU B 1 218 ? 7.686   26.503  21.957  1.00 58.16  ?  166 LEU B CD2   1 
ATOM   3280 N  N     . ILE B 1 219 ? 4.541   22.308  22.043  1.00 64.16  ?  167 ILE B N     1 
ATOM   3281 C  CA    . ILE B 1 219 ? 3.787   21.446  21.149  1.00 63.59  ?  167 ILE B CA    1 
ATOM   3282 C  C     . ILE B 1 219 ? 2.293   21.739  21.238  1.00 67.92  ?  167 ILE B C     1 
ATOM   3283 O  O     . ILE B 1 219 ? 1.580   21.628  20.234  1.00 69.38  ?  167 ILE B O     1 
ATOM   3284 C  CB    . ILE B 1 219 ? 4.123   19.977  21.458  1.00 60.51  ?  167 ILE B CB    1 
ATOM   3285 C  CG1   . ILE B 1 219 ? 5.489   19.617  20.871  1.00 56.78  ?  167 ILE B CG1   1 
ATOM   3286 C  CG2   . ILE B 1 219 ? 3.051   19.031  20.939  1.00 61.16  ?  167 ILE B CG2   1 
ATOM   3287 C  CD1   . ILE B 1 219 ? 6.004   18.302  21.337  1.00 56.61  ?  167 ILE B CD1   1 
ATOM   3288 N  N     . MET B 1 220 ? 1.800   22.148  22.416  1.00 67.92  ?  168 MET B N     1 
ATOM   3289 C  CA    . MET B 1 220 ? 0.376   22.432  22.571  1.00 68.92  ?  168 MET B CA    1 
ATOM   3290 C  C     . MET B 1 220 ? -0.001  23.818  22.089  1.00 67.94  ?  168 MET B C     1 
ATOM   3291 O  O     . MET B 1 220 ? -1.153  24.039  21.697  1.00 70.65  ?  168 MET B O     1 
ATOM   3292 C  CB    . MET B 1 220 ? -0.065  22.293  24.030  1.00 69.57  ?  168 MET B CB    1 
ATOM   3293 C  CG    . MET B 1 220 ? 0.257   20.981  24.634  1.00 68.17  ?  168 MET B CG    1 
ATOM   3294 S  SD    . MET B 1 220 ? -1.032  19.807  24.171  1.00 73.17  ?  168 MET B SD    1 
ATOM   3295 C  CE    . MET B 1 220 ? -2.541  20.586  24.748  1.00 74.39  ?  168 MET B CE    1 
ATOM   3296 N  N     . LYS B 1 221 ? 0.915   24.777  22.191  1.00 66.04  ?  169 LYS B N     1 
ATOM   3297 C  CA    . LYS B 1 221 ? 0.608   26.109  21.694  1.00 73.66  ?  169 LYS B CA    1 
ATOM   3298 C  C     . LYS B 1 221 ? 0.639   26.133  20.179  1.00 75.91  ?  169 LYS B C     1 
ATOM   3299 O  O     . LYS B 1 221 ? -0.167  26.832  19.554  1.00 78.30  ?  169 LYS B O     1 
ATOM   3300 C  CB    . LYS B 1 221 ? 1.586   27.140  22.265  1.00 73.25  ?  169 LYS B CB    1 
ATOM   3301 C  CG    . LYS B 1 221 ? 1.330   27.507  23.727  1.00 72.45  ?  169 LYS B CG    1 
ATOM   3302 C  CD    . LYS B 1 221 ? 2.364   28.504  24.246  1.00 76.06  ?  169 LYS B CD    1 
ATOM   3303 C  CE    . LYS B 1 221 ? 1.974   29.080  25.605  1.00 79.94  ?  169 LYS B CE    1 
ATOM   3304 N  NZ    . LYS B 1 221 ? 3.043   29.968  26.166  1.00 83.95  ?  169 LYS B NZ    1 
ATOM   3305 N  N     . ARG B 1 222 ? 1.547   25.366  19.579  1.00 71.89  ?  170 ARG B N     1 
ATOM   3306 C  CA    . ARG B 1 222 ? 1.587   25.269  18.129  1.00 78.74  ?  170 ARG B CA    1 
ATOM   3307 C  C     . ARG B 1 222 ? 0.324   24.629  17.577  1.00 79.30  ?  170 ARG B C     1 
ATOM   3308 O  O     . ARG B 1 222 ? -0.119  24.978  16.477  1.00 79.22  ?  170 ARG B O     1 
ATOM   3309 C  CB    . ARG B 1 222 ? 2.811   24.474  17.701  1.00 75.95  ?  170 ARG B CB    1 
ATOM   3310 C  CG    . ARG B 1 222 ? 3.004   24.419  16.208  1.00 72.47  ?  170 ARG B CG    1 
ATOM   3311 C  CD    . ARG B 1 222 ? 4.469   24.510  15.929  1.00 71.44  ?  170 ARG B CD    1 
ATOM   3312 N  NE    . ARG B 1 222 ? 4.835   23.855  14.691  1.00 75.25  ?  170 ARG B NE    1 
ATOM   3313 C  CZ    . ARG B 1 222 ? 6.092   23.722  14.293  1.00 77.51  ?  170 ARG B CZ    1 
ATOM   3314 N  NH1   . ARG B 1 222 ? 7.064   24.202  15.062  1.00 70.82  ?  170 ARG B NH1   1 
ATOM   3315 N  NH2   . ARG B 1 222 ? 6.379   23.118  13.141  1.00 76.90  ?  170 ARG B NH2   1 
ATOM   3316 N  N     . MET B 1 223 ? -0.270  23.699  18.320  1.00 79.49  ?  171 MET B N     1 
ATOM   3317 C  CA    . MET B 1 223 ? -1.469  23.033  17.838  1.00 82.07  ?  171 MET B CA    1 
ATOM   3318 C  C     . MET B 1 223 ? -2.724  23.876  18.009  1.00 84.39  ?  171 MET B C     1 
ATOM   3319 O  O     . MET B 1 223 ? -3.784  23.472  17.521  1.00 87.51  ?  171 MET B O     1 
ATOM   3320 C  CB    . MET B 1 223 ? -1.648  21.684  18.542  1.00 76.62  ?  171 MET B CB    1 
ATOM   3321 C  CG    . MET B 1 223 ? -1.105  20.511  17.727  1.00 81.82  ?  171 MET B CG    1 
ATOM   3322 S  SD    . MET B 1 223 ? -1.796  18.899  18.175  1.00 97.26  ?  171 MET B SD    1 
ATOM   3323 C  CE    . MET B 1 223 ? -2.006  19.091  19.955  1.00 59.04  ?  171 MET B CE    1 
ATOM   3324 N  N     . GLU B 1 224 ? -2.645  25.028  18.678  1.00 83.01  ?  172 GLU B N     1 
ATOM   3325 C  CA    . GLU B 1 224 ? -3.807  25.895  18.814  1.00 86.34  ?  172 GLU B CA    1 
ATOM   3326 C  C     . GLU B 1 224 ? -3.744  27.097  17.886  1.00 86.45  ?  172 GLU B C     1 
ATOM   3327 O  O     . GLU B 1 224 ? -4.465  28.076  18.100  1.00 86.90  ?  172 GLU B O     1 
ATOM   3328 C  CB    . GLU B 1 224 ? -3.988  26.342  20.262  1.00 82.68  ?  172 GLU B CB    1 
ATOM   3329 C  CG    . GLU B 1 224 ? -4.431  25.209  21.164  1.00 83.91  ?  172 GLU B CG    1 
ATOM   3330 C  CD    . GLU B 1 224 ? -5.744  24.581  20.715  1.00 87.38  ?  172 GLU B CD    1 
ATOM   3331 O  OE1   . GLU B 1 224 ? -6.801  25.228  20.883  1.00 84.77  ?  172 GLU B OE1   1 
ATOM   3332 O  OE2   . GLU B 1 224 ? -5.712  23.441  20.190  1.00 95.24  ?  172 GLU B OE2   1 
ATOM   3333 N  N     . ARG B 1 225 ? -2.912  27.033  16.851  1.00 86.83  ?  173 ARG B N     1 
ATOM   3334 C  CA    . ARG B 1 225 ? -2.894  28.047  15.814  1.00 85.32  ?  173 ARG B CA    1 
ATOM   3335 C  C     . ARG B 1 225 ? -3.493  27.545  14.508  1.00 90.15  ?  173 ARG B C     1 
ATOM   3336 O  O     . ARG B 1 225 ? -3.554  28.306  13.532  1.00 93.11  ?  173 ARG B O     1 
ATOM   3337 C  CB    . ARG B 1 225 ? -1.463  28.543  15.603  1.00 85.27  ?  173 ARG B CB    1 
ATOM   3338 C  CG    . ARG B 1 225 ? -0.838  29.076  16.883  1.00 78.08  ?  173 ARG B CG    1 
ATOM   3339 C  CD    . ARG B 1 225 ? 0.399   29.910  16.599  1.00 75.24  ?  173 ARG B CD    1 
ATOM   3340 N  NE    . ARG B 1 225 ? 1.553   29.078  16.283  1.00 78.10  ?  173 ARG B NE    1 
ATOM   3341 C  CZ    . ARG B 1 225 ? 2.501   28.749  17.153  1.00 81.55  ?  173 ARG B CZ    1 
ATOM   3342 N  NH1   . ARG B 1 225 ? 2.433   29.180  18.410  1.00 84.98  ?  173 ARG B NH1   1 
ATOM   3343 N  NH2   . ARG B 1 225 ? 3.516   27.983  16.767  1.00 83.60  ?  173 ARG B NH2   1 
ATOM   3344 N  N     . SER B 1 226 ? -3.946  26.292  14.470  1.00 89.95  ?  174 SER B N     1 
ATOM   3345 C  CA    . SER B 1 226 ? -4.717  25.772  13.345  1.00 88.28  ?  174 SER B CA    1 
ATOM   3346 C  C     . SER B 1 226 ? -6.210  25.890  13.646  1.00 89.64  ?  174 SER B C     1 
ATOM   3347 O  O     . SER B 1 226 ? -6.624  25.804  14.808  1.00 87.01  ?  174 SER B O     1 
ATOM   3348 C  CB    . SER B 1 226 ? -4.346  24.314  13.070  1.00 91.85  ?  174 SER B CB    1 
ATOM   3349 O  OG    . SER B 1 226 ? -4.083  23.632  14.291  1.00 92.96  ?  174 SER B OG    1 
HETATM 3350 P  PG    . GNP C 2 .   ? 14.099  -9.028  -1.734  1.00 45.95  ?  201 GNP A PG    1 
HETATM 3351 O  O1G   . GNP C 2 .   ? 15.381  -9.732  -1.393  1.00 38.82  ?  201 GNP A O1G   1 
HETATM 3352 O  O2G   . GNP C 2 .   ? 13.061  -9.134  -0.611  1.00 39.30  ?  201 GNP A O2G   1 
HETATM 3353 O  O3G   . GNP C 2 .   ? 14.410  -7.528  -1.965  1.00 43.84  ?  201 GNP A O3G   1 
HETATM 3354 N  N3B   . GNP C 2 .   ? 13.433  -9.767  -3.115  1.00 41.77  ?  201 GNP A N3B   1 
HETATM 3355 P  PB    . GNP C 2 .   ? 12.030  -9.414  -3.873  1.00 39.80  ?  201 GNP A PB    1 
HETATM 3356 O  O1B   . GNP C 2 .   ? 11.761  -7.937  -3.952  1.00 39.10  ?  201 GNP A O1B   1 
HETATM 3357 O  O2B   . GNP C 2 .   ? 10.821  -10.084 -3.289  1.00 41.44  ?  201 GNP A O2B   1 
HETATM 3358 O  O3A   . GNP C 2 .   ? 12.191  -10.133 -5.348  1.00 46.58  ?  201 GNP A O3A   1 
HETATM 3359 P  PA    . GNP C 2 .   ? 12.630  -9.471  -6.745  1.00 41.01  ?  201 GNP A PA    1 
HETATM 3360 O  O1A   . GNP C 2 .   ? 13.897  -8.655  -6.523  1.00 43.43  ?  201 GNP A O1A   1 
HETATM 3361 O  O2A   . GNP C 2 .   ? 11.546  -8.659  -7.320  1.00 44.08  ?  201 GNP A O2A   1 
HETATM 3362 O  "O5'" . GNP C 2 .   ? 13.364  -10.569 -7.548  1.00 44.36  ?  201 GNP A "O5'" 1 
HETATM 3363 C  "C5'" . GNP C 2 .   ? 12.987  -11.955 -7.472  1.00 44.84  ?  201 GNP A "C5'" 1 
HETATM 3364 C  "C4'" . GNP C 2 .   ? 13.785  -12.675 -8.534  1.00 43.98  ?  201 GNP A "C4'" 1 
HETATM 3365 O  "O4'" . GNP C 2 .   ? 12.874  -13.440 -9.341  1.00 50.18  ?  201 GNP A "O4'" 1 
HETATM 3366 C  "C3'" . GNP C 2 .   ? 14.508  -11.788 -9.541  1.00 45.09  ?  201 GNP A "C3'" 1 
HETATM 3367 O  "O3'" . GNP C 2 .   ? 15.497  -12.498 -10.281 1.00 45.33  ?  201 GNP A "O3'" 1 
HETATM 3368 C  "C2'" . GNP C 2 .   ? 13.385  -11.438 -10.509 1.00 42.09  ?  201 GNP A "C2'" 1 
HETATM 3369 O  "O2'" . GNP C 2 .   ? 13.953  -11.133 -11.777 1.00 45.26  ?  201 GNP A "O2'" 1 
HETATM 3370 C  "C1'" . GNP C 2 .   ? 12.607  -12.755 -10.557 1.00 41.11  ?  201 GNP A "C1'" 1 
HETATM 3371 N  N9    . GNP C 2 .   ? 11.155  -12.574 -10.653 1.00 37.96  ?  201 GNP A N9    1 
HETATM 3372 C  C8    . GNP C 2 .   ? 10.396  -11.768 -9.861  1.00 39.85  ?  201 GNP A C8    1 
HETATM 3373 N  N7    . GNP C 2 .   ? 9.117   -11.814 -10.154 1.00 43.38  ?  201 GNP A N7    1 
HETATM 3374 C  C5    . GNP C 2 .   ? 9.034   -12.712 -11.211 1.00 40.54  ?  201 GNP A C5    1 
HETATM 3375 C  C6    . GNP C 2 .   ? 7.903   -13.187 -11.978 1.00 42.64  ?  201 GNP A C6    1 
HETATM 3376 O  O6    . GNP C 2 .   ? 6.710   -12.869 -11.853 1.00 43.00  ?  201 GNP A O6    1 
HETATM 3377 N  N1    . GNP C 2 .   ? 8.275   -14.086 -12.957 1.00 44.66  ?  201 GNP A N1    1 
HETATM 3378 C  C2    . GNP C 2 .   ? 9.557   -14.501 -13.192 1.00 47.46  ?  201 GNP A C2    1 
HETATM 3379 N  N2    . GNP C 2 .   ? 9.735   -15.386 -14.184 1.00 47.08  ?  201 GNP A N2    1 
HETATM 3380 N  N3    . GNP C 2 .   ? 10.609  -14.079 -12.483 1.00 46.47  ?  201 GNP A N3    1 
HETATM 3381 C  C4    . GNP C 2 .   ? 10.278  -13.199 -11.516 1.00 42.18  ?  201 GNP A C4    1 
HETATM 3382 C  C1    . GOL D 3 .   ? 15.394  -6.729  -8.525  1.00 50.54  ?  202 GOL A C1    1 
HETATM 3383 O  O1    . GOL D 3 .   ? 16.109  -7.938  -8.416  1.00 46.66  ?  202 GOL A O1    1 
HETATM 3384 C  C2    . GOL D 3 .   ? 15.084  -6.485  -10.023 1.00 55.49  ?  202 GOL A C2    1 
HETATM 3385 O  O2    . GOL D 3 .   ? 16.259  -6.585  -10.809 1.00 59.66  ?  202 GOL A O2    1 
HETATM 3386 C  C3    . GOL D 3 .   ? 14.460  -5.041  -10.077 1.00 52.65  ?  202 GOL A C3    1 
HETATM 3387 O  O3    . GOL D 3 .   ? 13.485  -5.050  -11.091 1.00 57.19  ?  202 GOL A O3    1 
HETATM 3388 C  C1    . GOL E 3 .   ? 0.284   -17.589 -18.230 1.00 64.30  ?  203 GOL A C1    1 
HETATM 3389 O  O1    . GOL E 3 .   ? -0.359  -17.369 -19.487 1.00 64.55  ?  203 GOL A O1    1 
HETATM 3390 C  C2    . GOL E 3 .   ? 0.490   -16.171 -17.627 1.00 62.00  ?  203 GOL A C2    1 
HETATM 3391 O  O2    . GOL E 3 .   ? 1.444   -16.110 -16.600 1.00 52.45  ?  203 GOL A O2    1 
HETATM 3392 C  C3    . GOL E 3 .   ? -0.936  -15.769 -17.212 1.00 61.65  ?  203 GOL A C3    1 
HETATM 3393 O  O3    . GOL E 3 .   ? -1.713  -15.897 -18.388 1.00 67.72  ?  203 GOL A O3    1 
HETATM 3394 C  C1    . GOL F 3 .   ? 8.474   -20.540 -19.798 1.00 53.73  ?  204 GOL A C1    1 
HETATM 3395 O  O1    . GOL F 3 .   ? 7.205   -19.942 -19.980 1.00 52.06  ?  204 GOL A O1    1 
HETATM 3396 C  C2    . GOL F 3 .   ? 8.285   -22.027 -19.284 1.00 62.45  ?  204 GOL A C2    1 
HETATM 3397 O  O2    . GOL F 3 .   ? 8.327   -22.150 -17.877 1.00 66.36  ?  204 GOL A O2    1 
HETATM 3398 C  C3    . GOL F 3 .   ? 6.938   -22.497 -19.864 1.00 64.31  ?  204 GOL A C3    1 
HETATM 3399 O  O3    . GOL F 3 .   ? 5.958   -22.008 -18.993 1.00 64.88  ?  204 GOL A O3    1 
HETATM 3400 C  C1    . GOL G 3 .   ? 13.180  -15.572 -12.711 1.00 47.22  ?  205 GOL A C1    1 
HETATM 3401 O  O1    . GOL G 3 .   ? 13.452  -15.996 -11.386 1.00 66.84  ?  205 GOL A O1    1 
HETATM 3402 C  C2    . GOL G 3 .   ? 14.497  -15.580 -13.512 1.00 58.06  ?  205 GOL A C2    1 
HETATM 3403 O  O2    . GOL G 3 .   ? 15.180  -14.360 -13.406 1.00 54.22  ?  205 GOL A O2    1 
HETATM 3404 C  C3    . GOL G 3 .   ? 14.073  -15.934 -15.011 1.00 50.66  ?  205 GOL A C3    1 
HETATM 3405 O  O3    . GOL G 3 .   ? 12.649  -15.875 -15.092 1.00 48.27  ?  205 GOL A O3    1 
HETATM 3406 C  C1    . GOL H 3 .   ? 15.262  0.282   -12.250 1.00 60.75  ?  206 GOL A C1    1 
HETATM 3407 O  O1    . GOL H 3 .   ? 15.157  1.657   -11.923 1.00 62.79  ?  206 GOL A O1    1 
HETATM 3408 C  C2    . GOL H 3 .   ? 15.536  -0.548  -10.933 1.00 65.86  ?  206 GOL A C2    1 
HETATM 3409 O  O2    . GOL H 3 .   ? 16.166  -1.762  -11.204 1.00 71.13  ?  206 GOL A O2    1 
HETATM 3410 C  C3    . GOL H 3 .   ? 14.151  -0.785  -10.249 1.00 59.89  ?  206 GOL A C3    1 
HETATM 3411 O  O3    . GOL H 3 .   ? 14.400  -0.880  -8.879  1.00 65.31  ?  206 GOL A O3    1 
HETATM 3412 C  C1    . GOL I 3 .   ? 11.602  5.824   -8.221  1.00 60.83  ?  207 GOL A C1    1 
HETATM 3413 O  O1    . GOL I 3 .   ? 12.290  5.087   -7.230  1.00 60.74  ?  207 GOL A O1    1 
HETATM 3414 C  C2    . GOL I 3 .   ? 10.247  6.336   -7.617  1.00 60.76  ?  207 GOL A C2    1 
HETATM 3415 O  O2    . GOL I 3 .   ? 10.377  7.569   -6.904  1.00 64.63  ?  207 GOL A O2    1 
HETATM 3416 C  C3    . GOL I 3 .   ? 9.268   6.424   -8.841  1.00 59.66  ?  207 GOL A C3    1 
HETATM 3417 O  O3    . GOL I 3 .   ? 8.854   5.101   -9.158  1.00 55.50  ?  207 GOL A O3    1 
HETATM 3418 C  C05   . WTK J 4 .   ? -8.087  1.222   8.856   0.80 64.90  ?  208 WTK A C05   1 
HETATM 3419 C  C06   . WTK J 4 .   ? -7.338  1.131   7.513   0.82 62.23  ?  208 WTK A C06   1 
HETATM 3420 C  C07   . WTK J 4 .   ? -6.250  2.162   7.487   0.72 58.24  ?  208 WTK A C07   1 
HETATM 3421 C  C09   . WTK J 4 .   ? -5.723  4.707   7.269   1.00 56.18  ?  208 WTK A C09   1 
HETATM 3422 C  C10   . WTK J 4 .   ? -6.178  5.899   6.740   1.00 59.11  ?  208 WTK A C10   1 
HETATM 3423 C  C11   . WTK J 4 .   ? -5.323  7.017   6.718   0.64 61.95  ?  208 WTK A C11   1 
HETATM 3424 C  C12   . WTK J 4 .   ? -4.425  4.606   7.804   1.00 59.37  ?  208 WTK A C12   1 
HETATM 3425 C  C13   . WTK J 4 .   ? -3.580  5.707   7.786   0.00 61.93  ?  208 WTK A C13   1 
HETATM 3426 C  C15   . WTK J 4 .   ? -1.373  4.911   7.605   1.00 62.11  ?  208 WTK A C15   1 
HETATM 3427 C  C16   . WTK J 4 .   ? -4.039  6.899   7.240   1.00 61.61  ?  208 WTK A C16   1 
HETATM 3428 C  C20   . WTK J 4 .   ? -1.403  8.331   9.761   1.00 70.24  ?  208 WTK A C20   1 
HETATM 3429 C  C21   . WTK J 4 .   ? -1.583  8.918   10.954  1.00 72.63  ?  208 WTK A C21   1 
HETATM 3430 C  C22   . WTK J 4 .   ? -3.171  9.238   11.066  1.00 74.33  ?  208 WTK A C22   1 
HETATM 3431 C  C23   . WTK J 4 .   ? -3.562  9.603   9.825   1.00 71.59  ?  208 WTK A C23   1 
HETATM 3432 N  N08   . WTK J 4 .   ? -6.653  3.549   7.293   0.76 56.45  ?  208 WTK A N08   1 
HETATM 3433 N  N19   . WTK J 4 .   ? -2.614  8.803   8.882   1.00 71.88  ?  208 WTK A N19   1 
HETATM 3434 O  O14   . WTK J 4 .   ? -2.281  5.650   8.312   0.65 63.99  ?  208 WTK A O14   1 
HETATM 3435 O  O18   . WTK J 4 .   ? -3.554  9.396   6.467   1.00 65.62  ?  208 WTK A O18   1 
HETATM 3436 O  O24   . WTK J 4 .   ? -1.651  8.012   6.513   1.00 69.56  ?  208 WTK A O24   1 
HETATM 3437 O  O25   . WTK J 4 .   ? -5.106  1.848   7.646   0.72 57.36  ?  208 WTK A O25   1 
HETATM 3438 S  S17   . WTK J 4 .   ? -2.932  8.327   7.229   0.15 66.05  ?  208 WTK A S17   1 
HETATM 3439 MG MG    . MG  K 5 .   ? 13.223  -6.698  -3.469  1.00 44.80  ?  209 MG  A MG    1 
HETATM 3440 P  PG    . GNP L 2 .   ? 22.534  5.476   24.327  1.00 46.44  ?  201 GNP B PG    1 
HETATM 3441 O  O1G   . GNP L 2 .   ? 23.704  4.580   24.039  1.00 41.56  ?  201 GNP B O1G   1 
HETATM 3442 O  O2G   . GNP L 2 .   ? 22.104  6.320   23.136  1.00 46.90  ?  201 GNP B O2G   1 
HETATM 3443 O  O3G   . GNP L 2 .   ? 21.286  4.691   24.835  1.00 46.37  ?  201 GNP B O3G   1 
HETATM 3444 N  N3B   . GNP L 2 .   ? 23.105  6.502   25.556  1.00 48.61  ?  201 GNP B N3B   1 
HETATM 3445 P  PB    . GNP L 2 .   ? 22.130  7.395   26.500  1.00 42.42  ?  201 GNP B PB    1 
HETATM 3446 O  O1B   . GNP L 2 .   ? 20.717  6.858   26.518  1.00 39.07  ?  201 GNP B O1B   1 
HETATM 3447 O  O2B   . GNP L 2 .   ? 22.133  8.855   26.120  1.00 43.76  ?  201 GNP B O2B   1 
HETATM 3448 O  O3A   . GNP L 2 .   ? 22.873  7.383   27.970  1.00 53.23  ?  201 GNP B O3A   1 
HETATM 3449 P  PA    . GNP L 2 .   ? 22.359  6.855   29.376  1.00 41.31  ?  201 GNP B PA    1 
HETATM 3450 O  O1A   . GNP L 2 .   ? 22.545  5.338   29.414  1.00 43.22  ?  201 GNP B O1A   1 
HETATM 3451 O  O2A   . GNP L 2 .   ? 21.001  7.416   29.667  1.00 40.69  ?  201 GNP B O2A   1 
HETATM 3452 O  "O5'" . GNP L 2 .   ? 23.545  7.399   30.236  1.00 46.79  ?  201 GNP B "O5'" 1 
HETATM 3453 C  "C5'" . GNP L 2 .   ? 24.909  7.053   29.922  1.00 45.67  ?  201 GNP B "C5'" 1 
HETATM 3454 C  "C4'" . GNP L 2 .   ? 25.740  7.049   31.188  1.00 44.99  ?  201 GNP B "C4'" 1 
HETATM 3455 O  "O4'" . GNP L 2 .   ? 25.758  8.369   31.770  1.00 48.70  ?  201 GNP B "O4'" 1 
HETATM 3456 C  "C3'" . GNP L 2 .   ? 25.281  6.115   32.302  1.00 44.53  ?  201 GNP B "C3'" 1 
HETATM 3457 O  "O3'" . GNP L 2 .   ? 26.423  5.704   33.039  1.00 47.33  ?  201 GNP B "O3'" 1 
HETATM 3458 C  "C2'" . GNP L 2 .   ? 24.427  7.026   33.176  1.00 44.63  ?  201 GNP B "C2'" 1 
HETATM 3459 O  "O2'" . GNP L 2 .   ? 24.483  6.539   34.510  1.00 49.53  ?  201 GNP B "O2'" 1 
HETATM 3460 C  "C1'" . GNP L 2 .   ? 25.211  8.332   33.078  1.00 46.29  ?  201 GNP B "C1'" 1 
HETATM 3461 N  N9    . GNP L 2 .   ? 24.400  9.543   33.255  1.00 42.28  ?  201 GNP B N9    1 
HETATM 3462 C  C8    . GNP L 2 .   ? 23.299  9.897   32.520  1.00 44.88  ?  201 GNP B C8    1 
HETATM 3463 N  N7    . GNP L 2 .   ? 22.797  11.060  32.876  1.00 49.02  ?  201 GNP B N7    1 
HETATM 3464 C  C5    . GNP L 2 .   ? 23.630  11.491  33.912  1.00 46.57  ?  201 GNP B C5    1 
HETATM 3465 C  C6    . GNP L 2 .   ? 23.611  12.693  34.715  1.00 46.38  ?  201 GNP B C6    1 
HETATM 3466 O  O6    . GNP L 2 .   ? 22.804  13.634  34.651  1.00 44.10  ?  201 GNP B O6    1 
HETATM 3467 N  N1    . GNP L 2 .   ? 24.645  12.723  35.631  1.00 45.02  ?  201 GNP B N1    1 
HETATM 3468 C  C2    . GNP L 2 .   ? 25.586  11.742  35.777  1.00 48.48  ?  201 GNP B C2    1 
HETATM 3469 N  N2    . GNP L 2 .   ? 26.517  11.931  36.713  1.00 52.80  ?  201 GNP B N2    1 
HETATM 3470 N  N3    . GNP L 2 .   ? 25.620  10.636  35.036  1.00 50.07  ?  201 GNP B N3    1 
HETATM 3471 C  C4    . GNP L 2 .   ? 24.625  10.575  34.132  1.00 42.58  ?  201 GNP B C4    1 
HETATM 3472 C  C1    . GOL M 3 .   ? 20.833  3.981   31.824  1.00 50.72  ?  202 GOL B C1    1 
HETATM 3473 O  O1    . GOL M 3 .   ? 21.784  3.318   31.043  1.00 47.06  ?  202 GOL B O1    1 
HETATM 3474 C  C2    . GOL M 3 .   ? 20.075  2.905   32.625  1.00 52.56  ?  202 GOL B C2    1 
HETATM 3475 O  O2    . GOL M 3 .   ? 20.925  2.243   33.526  1.00 56.07  ?  202 GOL B O2    1 
HETATM 3476 C  C3    . GOL M 3 .   ? 18.977  3.688   33.377  1.00 47.53  ?  202 GOL B C3    1 
HETATM 3477 O  O3    . GOL M 3 .   ? 17.820  3.595   32.613  1.00 54.29  ?  202 GOL B O3    1 
HETATM 3478 C  C1    . GOL N 3 .   ? 11.069  25.850  17.257  1.00 71.84  ?  203 GOL B C1    1 
HETATM 3479 O  O1    . GOL N 3 .   ? 11.260  25.544  18.647  1.00 66.70  ?  203 GOL B O1    1 
HETATM 3480 C  C2    . GOL N 3 .   ? 11.036  27.415  17.123  1.00 76.97  ?  203 GOL B C2    1 
HETATM 3481 O  O2    . GOL N 3 .   ? 12.308  27.990  17.187  1.00 75.10  ?  203 GOL B O2    1 
HETATM 3482 C  C3    . GOL N 3 .   ? 10.284  27.749  15.781  1.00 76.65  ?  203 GOL B C3    1 
HETATM 3483 O  O3    . GOL N 3 .   ? 10.472  29.140  15.527  1.00 73.97  ?  203 GOL B O3    1 
HETATM 3484 C  C1    . GOL O 3 .   ? 29.012  1.228   17.011  1.00 62.49  ?  204 GOL B C1    1 
HETATM 3485 O  O1    . GOL O 3 .   ? 30.229  1.246   16.348  1.00 63.47  ?  204 GOL B O1    1 
HETATM 3486 C  C2    . GOL O 3 .   ? 28.031  2.004   16.137  1.00 58.31  ?  204 GOL B C2    1 
HETATM 3487 O  O2    . GOL O 3 .   ? 28.241  3.357   16.259  1.00 66.98  ?  204 GOL B O2    1 
HETATM 3488 C  C3    . GOL O 3 .   ? 28.397  1.604   14.764  1.00 64.50  ?  204 GOL B C3    1 
HETATM 3489 O  O3    . GOL O 3 .   ? 29.532  2.358   14.514  1.00 71.28  ?  204 GOL B O3    1 
HETATM 3490 C  C1    . GOL P 3 .   ? 26.813  12.208  15.486  1.00 61.18  ?  205 GOL B C1    1 
HETATM 3491 O  O1    . GOL P 3 .   ? 27.334  10.872  15.574  1.00 64.80  ?  205 GOL B O1    1 
HETATM 3492 C  C2    . GOL P 3 .   ? 25.510  12.125  14.622  1.00 61.54  ?  205 GOL B C2    1 
HETATM 3493 O  O2    . GOL P 3 .   ? 25.726  11.610  13.321  1.00 62.97  ?  205 GOL B O2    1 
HETATM 3494 C  C3    . GOL P 3 .   ? 24.922  13.531  14.587  1.00 53.30  ?  205 GOL B C3    1 
HETATM 3495 O  O3    . GOL P 3 .   ? 24.022  13.490  13.489  1.00 56.12  ?  205 GOL B O3    1 
HETATM 3496 C  C1    . GOL Q 3 .   ? 18.851  27.338  32.262  1.00 66.39  ?  206 GOL B C1    1 
HETATM 3497 O  O1    . GOL Q 3 .   ? 19.609  26.213  32.668  1.00 61.73  ?  206 GOL B O1    1 
HETATM 3498 C  C2    . GOL Q 3 .   ? 19.843  28.296  31.518  1.00 69.17  ?  206 GOL B C2    1 
HETATM 3499 O  O2    . GOL Q 3 .   ? 21.045  27.651  31.165  1.00 63.12  ?  206 GOL B O2    1 
HETATM 3500 C  C3    . GOL Q 3 .   ? 19.056  28.829  30.274  1.00 68.23  ?  206 GOL B C3    1 
HETATM 3501 O  O3    . GOL Q 3 .   ? 18.121  29.775  30.746  1.00 75.88  ?  206 GOL B O3    1 
HETATM 3502 C  C1    . GOL R 3 .   ? 13.998  28.904  28.756  1.00 64.30  ?  207 GOL B C1    1 
HETATM 3503 O  O1    . GOL R 3 .   ? 15.037  28.638  29.672  1.00 67.84  ?  207 GOL B O1    1 
HETATM 3504 C  C2    . GOL R 3 .   ? 14.644  29.125  27.351  1.00 65.70  ?  207 GOL B C2    1 
HETATM 3505 O  O2    . GOL R 3 .   ? 14.072  30.195  26.635  1.00 69.63  ?  207 GOL B O2    1 
HETATM 3506 C  C3    . GOL R 3 .   ? 16.170  29.327  27.593  1.00 66.53  ?  207 GOL B C3    1 
HETATM 3507 O  O3    . GOL R 3 .   ? 16.782  29.257  26.321  1.00 63.30  ?  207 GOL B O3    1 
HETATM 3508 C  C05   . WTK S 4 .   ? 4.112   20.907  13.457  1.00 78.73  ?  208 WTK B C05   1 
HETATM 3509 C  C06   . WTK S 4 .   ? 4.739   20.030  14.547  1.00 73.37  ?  208 WTK B C06   1 
HETATM 3510 C  C07   . WTK S 4 .   ? 4.154   18.648  14.526  0.97 70.61  ?  208 WTK B C07   1 
HETATM 3511 C  C09   . WTK S 4 .   ? 1.943   17.228  14.803  0.92 67.09  ?  208 WTK B C09   1 
HETATM 3512 C  C10   . WTK S 4 .   ? 0.603   17.284  15.148  1.00 67.04  ?  208 WTK B C10   1 
HETATM 3513 C  C11   . WTK S 4 .   ? -0.164  16.098  15.203  1.00 70.34  ?  208 WTK B C11   1 
HETATM 3514 C  C12   . WTK S 4 .   ? 2.537   15.977  14.518  0.46 67.09  ?  208 WTK B C12   1 
HETATM 3515 C  C13   . WTK S 4 .   ? 1.783   14.800  14.577  0.78 68.20  ?  208 WTK B C13   1 
HETATM 3516 C  C15   . WTK S 4 .   ? 3.673   13.402  14.608  1.00 62.77  ?  208 WTK B C15   1 
HETATM 3517 C  C16   . WTK S 4 .   ? 0.431   14.866  14.918  0.68 68.61  ?  208 WTK B C16   1 
HETATM 3518 C  C20   . WTK S 4 .   ? -2.291  13.741  12.648  1.00 73.56  ?  208 WTK B C20   1 
HETATM 3519 C  C21   . WTK S 4 .   ? -1.748  13.861  11.430  1.00 71.30  ?  208 WTK B C21   1 
HETATM 3520 C  C22   . WTK S 4 .   ? -0.968  12.463  11.162  1.00 73.44  ?  208 WTK B C22   1 
HETATM 3521 C  C23   . WTK S 4 .   ? -0.547  12.002  12.365  1.00 74.61  ?  208 WTK B C23   1 
HETATM 3522 N  N08   . WTK S 4 .   ? 2.709   18.512  14.772  1.00 66.61  ?  208 WTK B N08   1 
HETATM 3523 N  N19   . WTK S 4 .   ? -1.242  12.889  13.446  0.62 73.94  ?  208 WTK B N19   1 
HETATM 3524 O  O14   . WTK S 4 .   ? 2.349   13.547  14.293  1.00 66.79  ?  208 WTK B O14   1 
HETATM 3525 O  O18   . WTK S 4 .   ? 0.259   12.240  15.539  0.84 71.02  ?  208 WTK B O18   1 
HETATM 3526 O  O24   . WTK S 4 .   ? -1.605  13.441  16.051  0.74 68.68  ?  208 WTK B O24   1 
HETATM 3527 O  O25   . WTK S 4 .   ? 4.875   17.713  14.288  1.00 68.95  ?  208 WTK B O25   1 
HETATM 3528 S  S17   . WTK S 4 .   ? -0.546  13.326  14.998  0.41 69.13  ?  208 WTK B S17   1 
HETATM 3529 MG MG    . MG  T 5 .   ? 20.080  5.066   26.215  1.00 45.93  ?  209 MG  B MG    1 
HETATM 3530 O  O     . HOH U 6 .   ? -6.253  -7.142  13.131  1.00 65.26  ?  301 HOH A O     1 
HETATM 3531 O  O     . HOH U 6 .   ? 14.994  -6.641  -5.052  1.00 43.75  ?  302 HOH A O     1 
HETATM 3532 O  O     . HOH U 6 .   ? 4.549   -20.910 -11.625 1.00 48.15  ?  303 HOH A O     1 
HETATM 3533 O  O     . HOH U 6 .   ? 11.996  -5.966  -1.831  1.00 43.51  ?  304 HOH A O     1 
HETATM 3534 O  O     . HOH U 6 .   ? 21.145  -8.986  -5.054  1.00 45.10  ?  305 HOH A O     1 
HETATM 3535 O  O     . HOH U 6 .   ? 10.507  9.357   6.946   1.00 62.90  ?  306 HOH A O     1 
HETATM 3536 O  O     . HOH U 6 .   ? 7.191   7.761   7.045   1.00 58.43  ?  307 HOH A O     1 
HETATM 3537 O  O     . HOH U 6 .   ? 11.827  -19.525 -9.274  1.00 53.20  ?  308 HOH A O     1 
HETATM 3538 O  O     . HOH U 6 .   ? 17.500  -7.933  1.081   1.00 39.92  ?  309 HOH A O     1 
HETATM 3539 O  O     . HOH U 6 .   ? 6.494   -14.936 1.302   1.00 45.79  ?  310 HOH A O     1 
HETATM 3540 O  O     . HOH U 6 .   ? 9.189   -25.601 -3.177  1.00 55.09  ?  311 HOH A O     1 
HETATM 3541 O  O     . HOH U 6 .   ? 11.848  -17.600 -4.168  1.00 49.75  ?  312 HOH A O     1 
HETATM 3542 O  O     . HOH U 6 .   ? 11.348  -15.052 6.055   1.00 59.27  ?  313 HOH A O     1 
HETATM 3543 O  O     . HOH U 6 .   ? 7.738   -13.392 9.361   1.00 53.24  ?  314 HOH A O     1 
HETATM 3544 O  O     . HOH U 6 .   ? 2.118   -9.466  -21.733 1.00 51.25  ?  315 HOH A O     1 
HETATM 3545 O  O     . HOH U 6 .   ? 17.405  -0.813  -2.129  1.00 54.95  ?  316 HOH A O     1 
HETATM 3546 O  O     . HOH U 6 .   ? 5.814   21.352  5.473   1.00 72.30  ?  317 HOH A O     1 
HETATM 3547 O  O     . HOH U 6 .   ? 20.791  -4.888  -14.839 1.00 59.32  ?  318 HOH A O     1 
HETATM 3548 O  O     . HOH U 6 .   ? 12.798  -14.615 3.731   1.00 50.36  ?  319 HOH A O     1 
HETATM 3549 O  O     . HOH U 6 .   ? 10.789  -6.215  -12.616 1.00 43.50  ?  320 HOH A O     1 
HETATM 3550 O  O     . HOH U 6 .   ? 12.643  -0.493  -5.232  1.00 52.30  ?  321 HOH A O     1 
HETATM 3551 O  O     . HOH U 6 .   ? 0.796   17.692  -8.033  1.00 78.15  ?  322 HOH A O     1 
HETATM 3552 O  O     . HOH U 6 .   ? 3.787   2.172   -17.340 1.00 53.21  ?  323 HOH A O     1 
HETATM 3553 O  O     . HOH U 6 .   ? 17.709  1.585   -2.099  1.00 49.51  ?  324 HOH A O     1 
HETATM 3554 O  O     . HOH U 6 .   ? 7.864   -15.132 8.087   1.00 49.19  ?  325 HOH A O     1 
HETATM 3555 O  O     . HOH U 6 .   ? 11.004  -13.562 12.690  1.00 53.31  ?  326 HOH A O     1 
HETATM 3556 O  O     . HOH U 6 .   ? 19.438  -2.698  11.770  1.00 57.66  ?  327 HOH A O     1 
HETATM 3557 O  O     . HOH U 6 .   ? -3.558  6.236   12.954  1.00 66.84  ?  328 HOH A O     1 
HETATM 3558 O  O     . HOH V 6 .   ? 13.065  17.682  37.513  1.00 50.44  ?  301 HOH B O     1 
HETATM 3559 O  O     . HOH V 6 .   ? 27.279  29.263  17.496  1.00 64.37  ?  302 HOH B O     1 
HETATM 3560 O  O     . HOH V 6 .   ? 14.923  15.885  41.403  1.00 55.03  ?  303 HOH B O     1 
HETATM 3561 O  O     . HOH V 6 .   ? 18.887  5.889   24.732  1.00 44.35  ?  304 HOH B O     1 
HETATM 3562 O  O     . HOH V 6 .   ? 19.750  9.384   19.252  1.00 45.60  ?  305 HOH B O     1 
HETATM 3563 O  O     . HOH V 6 .   ? 23.017  1.520   21.593  1.00 49.70  ?  306 HOH B O     1 
HETATM 3564 O  O     . HOH V 6 .   ? 20.915  3.891   27.783  1.00 47.79  ?  307 HOH B O     1 
HETATM 3565 O  O     . HOH V 6 .   ? -9.722  14.432  30.608  1.00 75.29  ?  308 HOH B O     1 
HETATM 3566 O  O     . HOH V 6 .   ? 28.546  1.653   33.610  1.00 54.51  ?  309 HOH B O     1 
HETATM 3567 O  O     . HOH V 6 .   ? 30.648  16.452  13.690  1.00 61.11  ?  310 HOH B O     1 
HETATM 3568 O  O     . HOH V 6 .   ? 19.427  6.221   35.016  1.00 44.83  ?  311 HOH B O     1 
HETATM 3569 O  O     . HOH V 6 .   ? 25.658  -0.858  27.993  1.00 53.94  ?  312 HOH B O     1 
HETATM 3570 O  O     . HOH V 6 .   ? 31.454  12.866  16.824  1.00 56.58  ?  313 HOH B O     1 
HETATM 3571 O  O     . HOH V 6 .   ? 21.110  6.370   15.994  1.00 49.17  ?  314 HOH B O     1 
HETATM 3572 O  O     . HOH V 6 .   ? 14.501  21.502  38.907  1.00 48.32  ?  315 HOH B O     1 
HETATM 3573 O  O     . HOH V 6 .   ? 27.067  8.745   18.833  1.00 53.42  ?  316 HOH B O     1 
HETATM 3574 O  O     . HOH V 6 .   ? 24.895  15.020  21.355  1.00 49.31  ?  317 HOH B O     1 
HETATM 3575 O  O     . HOH V 6 .   ? 12.333  0.764   33.685  1.00 54.06  ?  318 HOH B O     1 
HETATM 3576 O  O     . HOH V 6 .   ? 15.086  2.166   32.912  1.00 59.60  ?  319 HOH B O     1 
HETATM 3577 O  O     . HOH V 6 .   ? 29.674  11.002  26.733  1.00 56.77  ?  320 HOH B O     1 
HETATM 3578 O  O     . HOH V 6 .   ? 22.764  11.079  6.873   1.00 69.81  ?  321 HOH B O     1 
HETATM 3579 O  O     . HOH V 6 .   ? 9.507   6.587   8.192   1.00 72.22  ?  322 HOH B O     1 
HETATM 3580 O  O     . HOH V 6 .   ? 16.548  -1.209  25.119  1.00 49.32  ?  323 HOH B O     1 
HETATM 3581 O  O     . HOH V 6 .   ? 7.940   10.228  39.687  1.00 52.09  ?  324 HOH B O     1 
HETATM 3582 O  O     . HOH V 6 .   ? -15.399 7.826   28.605  1.00 61.55  ?  325 HOH B O     1 
HETATM 3583 O  O     . HOH V 6 .   ? 31.170  19.225  11.611  1.00 63.47  ?  326 HOH B O     1 
HETATM 3584 O  O     . HOH V 6 .   ? 2.388   14.884  36.726  1.00 56.45  ?  327 HOH B O     1 
HETATM 3585 O  O     . HOH V 6 .   ? 24.030  8.478   9.010   1.00 66.39  ?  328 HOH B O     1 
HETATM 3586 O  O     . HOH V 6 .   ? 36.107  20.883  14.977  1.00 60.27  ?  329 HOH B O     1 
# 
