data_8P3J
# 
_entry.id   8P3J 
# 
_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   8P3J         pdb_00008p3j 10.2210/pdb8p3j/pdb 
WWPDB D_1292129006 ?            ?                   
# 
_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                        8P3J 
_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' 25882.146 2  3.6.5.2 Q78L,C123A,C188S ? ? 
2 non-polymer syn '~{N}-(4-pyrrolidin-1-ylsulfonylphenyl)prop-2-enamide'     280.343   4  ?       ?                ? ? 
3 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'              522.196   2  ?       ?                ? ? 
4 non-polymer syn GLYCEROL                                                   92.094    3  ?       ?                ? ? 
5 non-polymer syn 'MAGNESIUM ION'                                            24.305    2  ?       ?                ? ? 
6 water       nat water                                                      18.015    97 ?       ?                ? ? 
# 
_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
AENPDIVLCGNKSDLEDQRVVKEEEAIALAEKYGIPYFETSAANGTNISQAIEMLLDLIMKRMERSVDKS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GHMSFLTEEEQEAIMKVLQRDAALKRAEEERGSGSGSGMSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTV
GIDFREKRVVYRASGPDGATGRGQRIHLQLWDTAGLERFRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMHAY
AENPDIVLCGNKSDLEDQRVVKEEEAIALAEKYGIPYFETSAANGTNISQAIEMLLDLIMKRMERSVDKS
;
_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 '~{N}-(4-pyrrolidin-1-ylsulfonylphenyl)prop-2-enamide' WT6 
3 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'          GNP 
4 GLYCEROL                                               GOL 
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 ALA 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  32  human ? 'SYTL2, KIAA1597, SGA72M, SLP2, SLP2A' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? 
? ? 
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
866768 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 33 230 human ? '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 
WT6 non-polymer         . '~{N}-(4-pyrrolidin-1-ylsulfonylphenyl)prop-2-enamide' ?                               'C13 H16 N2 O3 S' 
280.343 
# 
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  -7  ?   ?   ?   A . n 
A 1 32  GLY 32  -6  ?   ?   ?   A . n 
A 1 33  SER 33  -5  ?   ?   ?   A . n 
A 1 34  GLY 34  -4  ?   ?   ?   A . n 
A 1 35  SER 35  -3  ?   ?   ?   A . n 
A 1 36  GLY 36  -2  ?   ?   ?   A . n 
A 1 37  SER 37  -1  ?   ?   ?   A . n 
A 1 38  GLY 38  0   ?   ?   ?   A . n 
A 1 39  MET 39  1   ?   ?   ?   A . n 
A 1 40  SER 40  2   ?   ?   ?   A . n 
A 1 41  ASP 41  3   ?   ?   ?   A . n 
A 1 42  GLY 42  4   ?   ?   ?   A . n 
A 1 43  ASP 43  5   ?   ?   ?   A . n 
A 1 44  TYR 44  6   ?   ?   ?   A . n 
A 1 45  ASP 45  7   7   ASP ASP A . n 
A 1 46  TYR 46  8   8   TYR TYR A . n 
A 1 47  LEU 47  9   9   LEU LEU A . n 
A 1 48  ILE 48  10  10  ILE ILE A . n 
A 1 49  LYS 49  11  11  LYS LYS A . n 
A 1 50  PHE 50  12  12  PHE PHE A . n 
A 1 51  LEU 51  13  13  LEU LEU A . n 
A 1 52  ALA 52  14  14  ALA ALA A . n 
A 1 53  LEU 53  15  15  LEU LEU A . n 
A 1 54  GLY 54  16  16  GLY GLY A . n 
A 1 55  ASP 55  17  17  ASP ASP A . n 
A 1 56  SER 56  18  18  SER SER A . n 
A 1 57  GLY 57  19  19  GLY GLY A . n 
A 1 58  VAL 58  20  20  VAL VAL A . n 
A 1 59  GLY 59  21  21  GLY GLY A . n 
A 1 60  LYS 60  22  22  LYS LYS A . n 
A 1 61  THR 61  23  23  THR THR A . n 
A 1 62  SER 62  24  24  SER SER A . n 
A 1 63  VAL 63  25  25  VAL VAL A . n 
A 1 64  LEU 64  26  26  LEU LEU A . n 
A 1 65  TYR 65  27  27  TYR TYR A . n 
A 1 66  GLN 66  28  28  GLN GLN A . n 
A 1 67  TYR 67  29  29  TYR TYR A . n 
A 1 68  THR 68  30  30  THR THR A . n 
A 1 69  ASP 69  31  31  ASP ASP A . n 
A 1 70  GLY 70  32  32  GLY GLY A . n 
A 1 71  LYS 71  33  33  LYS LYS A . n 
A 1 72  PHE 72  34  34  PHE PHE A . n 
A 1 73  ASN 73  35  35  ASN ASN A . n 
A 1 74  SER 74  36  36  SER SER A . n 
A 1 75  LYS 75  37  37  LYS LYS A . n 
A 1 76  PHE 76  38  38  PHE PHE A . n 
A 1 77  ILE 77  39  39  ILE ILE A . n 
A 1 78  THR 78  40  40  THR THR A . n 
A 1 79  THR 79  41  41  THR THR A . n 
A 1 80  VAL 80  42  42  VAL VAL A . n 
A 1 81  GLY 81  43  43  GLY GLY A . n 
A 1 82  ILE 82  44  44  ILE ILE A . n 
A 1 83  ASP 83  45  45  ASP ASP A . n 
A 1 84  PHE 84  46  46  PHE PHE A . n 
A 1 85  ARG 85  47  47  ARG ARG A . n 
A 1 86  GLU 86  48  48  GLU GLU A . n 
A 1 87  LYS 87  49  49  LYS LYS A . n 
A 1 88  ARG 88  50  50  ARG ARG A . n 
A 1 89  VAL 89  51  51  VAL VAL A . n 
A 1 90  VAL 90  52  52  VAL VAL A . n 
A 1 91  TYR 91  53  53  TYR TYR A . n 
A 1 92  ARG 92  54  54  ARG ARG A . n 
A 1 93  ALA 93  55  55  ALA ALA A . n 
A 1 94  SER 94  56  56  SER SER A . n 
A 1 95  GLY 95  57  57  GLY GLY A . n 
A 1 96  PRO 96  58  58  PRO PRO A . n 
A 1 97  ASP 97  59  59  ASP ASP A . n 
A 1 98  GLY 98  60  60  GLY GLY A . n 
A 1 99  ALA 99  61  61  ALA ALA A . n 
A 1 100 THR 100 62  62  THR THR A . n 
A 1 101 GLY 101 63  63  GLY GLY A . n 
A 1 102 ARG 102 64  64  ARG ARG A . n 
A 1 103 GLY 103 65  65  GLY GLY A . n 
A 1 104 GLN 104 66  66  GLN GLN A . n 
A 1 105 ARG 105 67  67  ARG ARG A . n 
A 1 106 ILE 106 68  68  ILE ILE A . n 
A 1 107 HIS 107 69  69  HIS HIS A . n 
A 1 108 LEU 108 70  70  LEU LEU A . n 
A 1 109 GLN 109 71  71  GLN GLN A . n 
A 1 110 LEU 110 72  72  LEU LEU A . n 
A 1 111 TRP 111 73  73  TRP TRP A . n 
A 1 112 ASP 112 74  74  ASP ASP A . n 
A 1 113 THR 113 75  75  THR THR A . n 
A 1 114 ALA 114 76  76  ALA ALA A . n 
A 1 115 GLY 115 77  77  GLY GLY A . n 
A 1 116 LEU 116 78  78  LEU LEU A . n 
A 1 117 GLU 117 79  79  GLU GLU A . n 
A 1 118 ARG 118 80  80  ARG ARG A . n 
A 1 119 PHE 119 81  81  PHE PHE A . n 
A 1 120 ARG 120 82  82  ARG ARG A . n 
A 1 121 SER 121 83  83  SER SER A . n 
A 1 122 LEU 122 84  84  LEU LEU A . n 
A 1 123 THR 123 85  85  THR THR A . n 
A 1 124 THR 124 86  86  THR THR A . n 
A 1 125 ALA 125 87  87  ALA ALA A . n 
A 1 126 PHE 126 88  88  PHE PHE A . n 
A 1 127 PHE 127 89  89  PHE PHE A . n 
A 1 128 ARG 128 90  90  ARG ARG A . n 
A 1 129 ASP 129 91  91  ASP ASP A . n 
A 1 130 ALA 130 92  92  ALA ALA A . n 
A 1 131 MET 131 93  93  MET MET A . n 
A 1 132 GLY 132 94  94  GLY GLY A . n 
A 1 133 PHE 133 95  95  PHE PHE A . n 
A 1 134 LEU 134 96  96  LEU LEU A . n 
A 1 135 LEU 135 97  97  LEU LEU A . n 
A 1 136 LEU 136 98  98  LEU LEU A . n 
A 1 137 PHE 137 99  99  PHE PHE A . n 
A 1 138 ASP 138 100 100 ASP ASP A . n 
A 1 139 LEU 139 101 101 LEU LEU A . n 
A 1 140 THR 140 102 102 THR THR A . n 
A 1 141 ASN 141 103 103 ASN ASN A . n 
A 1 142 GLU 142 104 104 GLU GLU A . n 
A 1 143 GLN 143 105 105 GLN GLN A . n 
A 1 144 SER 144 106 106 SER SER A . n 
A 1 145 PHE 145 107 107 PHE PHE A . n 
A 1 146 LEU 146 108 108 LEU LEU A . n 
A 1 147 ASN 147 109 109 ASN ASN A . n 
A 1 148 VAL 148 110 110 VAL VAL A . n 
A 1 149 ARG 149 111 111 ARG ARG A . n 
A 1 150 ASN 150 112 112 ASN ASN A . n 
A 1 151 TRP 151 113 113 TRP TRP A . n 
A 1 152 ILE 152 114 114 ILE ILE A . n 
A 1 153 SER 153 115 115 SER SER A . n 
A 1 154 GLN 154 116 116 GLN GLN A . n 
A 1 155 LEU 155 117 117 LEU LEU A . n 
A 1 156 GLN 156 118 118 GLN GLN A . n 
A 1 157 MET 157 119 119 MET MET A . n 
A 1 158 HIS 158 120 120 HIS HIS A . n 
A 1 159 ALA 159 121 121 ALA ALA A . n 
A 1 160 TYR 160 122 122 TYR TYR A . n 
A 1 161 ALA 161 123 123 ALA ALA A . n 
A 1 162 GLU 162 124 124 GLU GLU A . n 
A 1 163 ASN 163 125 125 ASN ASN A . n 
A 1 164 PRO 164 126 126 PRO PRO A . n 
A 1 165 ASP 165 127 127 ASP ASP A . n 
A 1 166 ILE 166 128 128 ILE ILE A . n 
A 1 167 VAL 167 129 129 VAL VAL A . n 
A 1 168 LEU 168 130 130 LEU LEU A . n 
A 1 169 CYS 169 131 131 CYS CYS A . n 
A 1 170 GLY 170 132 132 GLY GLY A . n 
A 1 171 ASN 171 133 133 ASN ASN A . n 
A 1 172 LYS 172 134 134 LYS LYS A . n 
A 1 173 SER 173 135 135 SER SER A . n 
A 1 174 ASP 174 136 136 ASP ASP A . n 
A 1 175 LEU 175 137 137 LEU LEU A . n 
A 1 176 GLU 176 138 138 GLU GLU A . n 
A 1 177 ASP 177 139 139 ASP ASP A . n 
A 1 178 GLN 178 140 140 GLN GLN A . n 
A 1 179 ARG 179 141 141 ARG ARG A . n 
A 1 180 VAL 180 142 142 VAL VAL A . n 
A 1 181 VAL 181 143 143 VAL VAL A . n 
A 1 182 LYS 182 144 144 LYS LYS A . n 
A 1 183 GLU 183 145 145 GLU GLU A . n 
A 1 184 GLU 184 146 146 GLU GLU A . n 
A 1 185 GLU 185 147 147 GLU GLU A . n 
A 1 186 ALA 186 148 148 ALA ALA A . n 
A 1 187 ILE 187 149 149 ILE ILE A . n 
A 1 188 ALA 188 150 150 ALA ALA A . n 
A 1 189 LEU 189 151 151 LEU LEU A . n 
A 1 190 ALA 190 152 152 ALA ALA A . n 
A 1 191 GLU 191 153 153 GLU GLU A . n 
A 1 192 LYS 192 154 154 LYS LYS A . n 
A 1 193 TYR 193 155 155 TYR TYR A . n 
A 1 194 GLY 194 156 156 GLY GLY A . n 
A 1 195 ILE 195 157 157 ILE ILE A . n 
A 1 196 PRO 196 158 158 PRO PRO A . n 
A 1 197 TYR 197 159 159 TYR TYR A . n 
A 1 198 PHE 198 160 160 PHE PHE A . n 
A 1 199 GLU 199 161 161 GLU GLU A . n 
A 1 200 THR 200 162 162 THR THR A . n 
A 1 201 SER 201 163 163 SER SER A . n 
A 1 202 ALA 202 164 164 ALA ALA A . n 
A 1 203 ALA 203 165 165 ALA ALA A . n 
A 1 204 ASN 204 166 166 ASN ASN A . n 
A 1 205 GLY 205 167 167 GLY GLY A . n 
A 1 206 THR 206 168 168 THR THR A . n 
A 1 207 ASN 207 169 169 ASN ASN A . n 
A 1 208 ILE 208 170 170 ILE ILE A . n 
A 1 209 SER 209 171 171 SER SER A . n 
A 1 210 GLN 210 172 172 GLN GLN A . n 
A 1 211 ALA 211 173 173 ALA ALA A . n 
A 1 212 ILE 212 174 174 ILE ILE A . n 
A 1 213 GLU 213 175 175 GLU GLU A . n 
A 1 214 MET 214 176 176 MET MET A . n 
A 1 215 LEU 215 177 177 LEU LEU A . n 
A 1 216 LEU 216 178 178 LEU LEU A . n 
A 1 217 ASP 217 179 179 ASP ASP A . n 
A 1 218 LEU 218 180 180 LEU LEU A . n 
A 1 219 ILE 219 181 181 ILE ILE A . n 
A 1 220 MET 220 182 182 MET MET A . n 
A 1 221 LYS 221 183 183 LYS LYS A . n 
A 1 222 ARG 222 184 184 ARG ARG A . n 
A 1 223 MET 223 185 185 MET MET A . n 
A 1 224 GLU 224 186 186 GLU GLU A . n 
A 1 225 ARG 225 187 187 ARG ARG A . n 
A 1 226 SER 226 188 188 SER SER A . n 
A 1 227 VAL 227 189 ?   ?   ?   A . n 
A 1 228 ASP 228 190 ?   ?   ?   A . n 
A 1 229 LYS 229 191 ?   ?   ?   A . n 
A 1 230 SER 230 192 ?   ?   ?   A . n 
B 1 1   GLY 1   -38 -38 GLY GLY 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  -8  -8  ARG ARG B . n 
B 1 32  GLY 32  -6  ?   ?   ?   B . n 
B 1 33  SER 33  -5  ?   ?   ?   B . n 
B 1 34  GLY 34  -4  ?   ?   ?   B . n 
B 1 35  SER 35  -3  ?   ?   ?   B . n 
B 1 36  GLY 36  -2  ?   ?   ?   B . n 
B 1 37  SER 37  -1  ?   ?   ?   B . n 
B 1 38  GLY 38  0   ?   ?   ?   B . n 
B 1 39  MET 39  1   ?   ?   ?   B . n 
B 1 40  SER 40  2   ?   ?   ?   B . n 
B 1 41  ASP 41  3   ?   ?   ?   B . n 
B 1 42  GLY 42  4   ?   ?   ?   B . n 
B 1 43  ASP 43  5   ?   ?   ?   B . n 
B 1 44  TYR 44  6   6   TYR ALA B . n 
B 1 45  ASP 45  7   7   ASP ASP B . n 
B 1 46  TYR 46  8   8   TYR TYR B . n 
B 1 47  LEU 47  9   9   LEU LEU B . n 
B 1 48  ILE 48  10  10  ILE ILE B . n 
B 1 49  LYS 49  11  11  LYS LYS B . n 
B 1 50  PHE 50  12  12  PHE PHE B . n 
B 1 51  LEU 51  13  13  LEU LEU B . n 
B 1 52  ALA 52  14  14  ALA ALA B . n 
B 1 53  LEU 53  15  15  LEU LEU B . n 
B 1 54  GLY 54  16  16  GLY GLY B . n 
B 1 55  ASP 55  17  17  ASP ASP B . n 
B 1 56  SER 56  18  18  SER SER B . n 
B 1 57  GLY 57  19  19  GLY GLY B . n 
B 1 58  VAL 58  20  20  VAL VAL B . n 
B 1 59  GLY 59  21  21  GLY GLY B . n 
B 1 60  LYS 60  22  22  LYS LYS B . n 
B 1 61  THR 61  23  23  THR THR B . n 
B 1 62  SER 62  24  24  SER SER B . n 
B 1 63  VAL 63  25  25  VAL VAL B . n 
B 1 64  LEU 64  26  26  LEU LEU B . n 
B 1 65  TYR 65  27  27  TYR TYR B . n 
B 1 66  GLN 66  28  28  GLN GLN B . n 
B 1 67  TYR 67  29  29  TYR TYR B . n 
B 1 68  THR 68  30  30  THR THR B . n 
B 1 69  ASP 69  31  31  ASP ASP B . n 
B 1 70  GLY 70  32  32  GLY GLY B . n 
B 1 71  LYS 71  33  33  LYS LYS B . n 
B 1 72  PHE 72  34  34  PHE PHE B . n 
B 1 73  ASN 73  35  35  ASN ASN B . n 
B 1 74  SER 74  36  36  SER SER B . n 
B 1 75  LYS 75  37  37  LYS LYS B . n 
B 1 76  PHE 76  38  38  PHE PHE B . n 
B 1 77  ILE 77  39  39  ILE ILE B . n 
B 1 78  THR 78  40  40  THR THR B . n 
B 1 79  THR 79  41  41  THR THR B . n 
B 1 80  VAL 80  42  42  VAL VAL B . n 
B 1 81  GLY 81  43  43  GLY GLY B . n 
B 1 82  ILE 82  44  44  ILE ILE B . n 
B 1 83  ASP 83  45  45  ASP ASP B . n 
B 1 84  PHE 84  46  46  PHE PHE B . n 
B 1 85  ARG 85  47  47  ARG ARG B . n 
B 1 86  GLU 86  48  48  GLU GLU B . n 
B 1 87  LYS 87  49  49  LYS LYS B . n 
B 1 88  ARG 88  50  50  ARG ARG B . n 
B 1 89  VAL 89  51  51  VAL VAL B . n 
B 1 90  VAL 90  52  52  VAL VAL B . n 
B 1 91  TYR 91  53  53  TYR TYR B . n 
B 1 92  ARG 92  54  54  ARG ARG B . n 
B 1 93  ALA 93  55  55  ALA ALA B . n 
B 1 94  SER 94  56  56  SER SER B . n 
B 1 95  GLY 95  57  57  GLY GLY B . n 
B 1 96  PRO 96  58  58  PRO PRO B . n 
B 1 97  ASP 97  59  59  ASP ASP B . n 
B 1 98  GLY 98  60  60  GLY GLY B . n 
B 1 99  ALA 99  61  61  ALA ALA B . n 
B 1 100 THR 100 62  62  THR THR B . n 
B 1 101 GLY 101 63  63  GLY GLY B . n 
B 1 102 ARG 102 64  64  ARG ARG B . n 
B 1 103 GLY 103 65  65  GLY GLY B . n 
B 1 104 GLN 104 66  66  GLN GLN B . n 
B 1 105 ARG 105 67  67  ARG ARG B . n 
B 1 106 ILE 106 68  68  ILE ILE B . n 
B 1 107 HIS 107 69  69  HIS HIS B . n 
B 1 108 LEU 108 70  70  LEU LEU B . n 
B 1 109 GLN 109 71  71  GLN GLN B . n 
B 1 110 LEU 110 72  72  LEU LEU B . n 
B 1 111 TRP 111 73  73  TRP TRP B . n 
B 1 112 ASP 112 74  74  ASP ASP B . n 
B 1 113 THR 113 75  75  THR THR B . n 
B 1 114 ALA 114 76  76  ALA ALA B . n 
B 1 115 GLY 115 77  77  GLY GLY B . n 
B 1 116 LEU 116 78  78  LEU LEU B . n 
B 1 117 GLU 117 79  79  GLU GLU B . n 
B 1 118 ARG 118 80  80  ARG ARG B . n 
B 1 119 PHE 119 81  81  PHE PHE B . n 
B 1 120 ARG 120 82  82  ARG ARG B . n 
B 1 121 SER 121 83  83  SER SER B . n 
B 1 122 LEU 122 84  84  LEU LEU B . n 
B 1 123 THR 123 85  85  THR THR B . n 
B 1 124 THR 124 86  86  THR THR B . n 
B 1 125 ALA 125 87  87  ALA ALA B . n 
B 1 126 PHE 126 88  88  PHE PHE B . n 
B 1 127 PHE 127 89  89  PHE PHE B . n 
B 1 128 ARG 128 90  90  ARG ARG B . n 
B 1 129 ASP 129 91  91  ASP ASP B . n 
B 1 130 ALA 130 92  92  ALA ALA B . n 
B 1 131 MET 131 93  93  MET MET B . n 
B 1 132 GLY 132 94  94  GLY GLY B . n 
B 1 133 PHE 133 95  95  PHE PHE B . n 
B 1 134 LEU 134 96  96  LEU LEU B . n 
B 1 135 LEU 135 97  97  LEU LEU B . n 
B 1 136 LEU 136 98  98  LEU LEU B . n 
B 1 137 PHE 137 99  99  PHE PHE B . n 
B 1 138 ASP 138 100 100 ASP ASP B . n 
B 1 139 LEU 139 101 101 LEU LEU B . n 
B 1 140 THR 140 102 102 THR THR B . n 
B 1 141 ASN 141 103 103 ASN ASN B . n 
B 1 142 GLU 142 104 104 GLU GLU B . n 
B 1 143 GLN 143 105 105 GLN GLN B . n 
B 1 144 SER 144 106 106 SER SER B . n 
B 1 145 PHE 145 107 107 PHE PHE B . n 
B 1 146 LEU 146 108 108 LEU LEU B . n 
B 1 147 ASN 147 109 109 ASN ASN B . n 
B 1 148 VAL 148 110 110 VAL VAL B . n 
B 1 149 ARG 149 111 111 ARG ARG B . n 
B 1 150 ASN 150 112 112 ASN ASN B . n 
B 1 151 TRP 151 113 113 TRP TRP B . n 
B 1 152 ILE 152 114 114 ILE ILE B . n 
B 1 153 SER 153 115 115 SER SER B . n 
B 1 154 GLN 154 116 116 GLN GLN B . n 
B 1 155 LEU 155 117 117 LEU LEU B . n 
B 1 156 GLN 156 118 118 GLN GLN B . n 
B 1 157 MET 157 119 119 MET MET B . n 
B 1 158 HIS 158 120 120 HIS HIS B . n 
B 1 159 ALA 159 121 121 ALA ALA B . n 
B 1 160 TYR 160 122 122 TYR TYR B . n 
B 1 161 ALA 161 123 123 ALA ALA B . n 
B 1 162 GLU 162 124 124 GLU GLU B . n 
B 1 163 ASN 163 125 125 ASN ASN B . n 
B 1 164 PRO 164 126 126 PRO PRO B . n 
B 1 165 ASP 165 127 127 ASP ASP B . n 
B 1 166 ILE 166 128 128 ILE ILE B . n 
B 1 167 VAL 167 129 129 VAL VAL B . n 
B 1 168 LEU 168 130 130 LEU LEU B . n 
B 1 169 CYS 169 131 131 CYS CYS B . n 
B 1 170 GLY 170 132 132 GLY GLY B . n 
B 1 171 ASN 171 133 133 ASN ASN B . n 
B 1 172 LYS 172 134 134 LYS LYS B . n 
B 1 173 SER 173 135 135 SER SER B . n 
B 1 174 ASP 174 136 136 ASP ASP B . n 
B 1 175 LEU 175 137 137 LEU LEU B . n 
B 1 176 GLU 176 138 138 GLU GLU B . n 
B 1 177 ASP 177 139 139 ASP ASP B . n 
B 1 178 GLN 178 140 140 GLN GLN B . n 
B 1 179 ARG 179 141 141 ARG ARG B . n 
B 1 180 VAL 180 142 142 VAL VAL B . n 
B 1 181 VAL 181 143 143 VAL VAL B . n 
B 1 182 LYS 182 144 144 LYS LYS B . n 
B 1 183 GLU 183 145 145 GLU GLU B . n 
B 1 184 GLU 184 146 146 GLU GLU B . n 
B 1 185 GLU 185 147 147 GLU GLU B . n 
B 1 186 ALA 186 148 148 ALA ALA B . n 
B 1 187 ILE 187 149 149 ILE ILE B . n 
B 1 188 ALA 188 150 150 ALA ALA B . n 
B 1 189 LEU 189 151 151 LEU LEU B . n 
B 1 190 ALA 190 152 152 ALA ALA B . n 
B 1 191 GLU 191 153 153 GLU GLU B . n 
B 1 192 LYS 192 154 154 LYS LYS B . n 
B 1 193 TYR 193 155 155 TYR TYR B . n 
B 1 194 GLY 194 156 156 GLY GLY B . n 
B 1 195 ILE 195 157 157 ILE ILE B . n 
B 1 196 PRO 196 158 158 PRO PRO B . n 
B 1 197 TYR 197 159 159 TYR TYR B . n 
B 1 198 PHE 198 160 160 PHE PHE B . n 
B 1 199 GLU 199 161 161 GLU GLU B . n 
B 1 200 THR 200 162 162 THR THR B . n 
B 1 201 SER 201 163 163 SER SER B . n 
B 1 202 ALA 202 164 164 ALA ALA B . n 
B 1 203 ALA 203 165 165 ALA ALA B . n 
B 1 204 ASN 204 166 166 ASN ASN B . n 
B 1 205 GLY 205 167 167 GLY GLY B . n 
B 1 206 THR 206 168 168 THR THR B . n 
B 1 207 ASN 207 169 169 ASN ASN B . n 
B 1 208 ILE 208 170 170 ILE ILE B . n 
B 1 209 SER 209 171 171 SER SER B . n 
B 1 210 GLN 210 172 172 GLN GLN B . n 
B 1 211 ALA 211 173 173 ALA ALA B . n 
B 1 212 ILE 212 174 174 ILE ILE B . n 
B 1 213 GLU 213 175 175 GLU GLU B . n 
B 1 214 MET 214 176 176 MET MET B . n 
B 1 215 LEU 215 177 177 LEU LEU B . n 
B 1 216 LEU 216 178 178 LEU LEU B . n 
B 1 217 ASP 217 179 179 ASP ASP B . n 
B 1 218 LEU 218 180 180 LEU LEU B . n 
B 1 219 ILE 219 181 181 ILE ILE B . n 
B 1 220 MET 220 182 182 MET MET B . n 
B 1 221 LYS 221 183 183 LYS LYS B . n 
B 1 222 ARG 222 184 184 ARG ARG B . n 
B 1 223 MET 223 185 185 MET MET B . n 
B 1 224 GLU 224 186 186 GLU GLU B . n 
B 1 225 ARG 225 187 187 ARG ARG B . n 
B 1 226 SER 226 188 188 SER SER B . n 
B 1 227 VAL 227 189 ?   ?   ?   B . n 
B 1 228 ASP 228 190 ?   ?   ?   B . n 
B 1 229 LYS 229 191 ?   ?   ?   B . n 
B 1 230 SER 230 192 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WT6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WT6 
_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 WT6 1  201 201 WT6 C01 A . 
D 2 WT6 1  202 301 WT6 C01 A . 
E 3 GNP 1  203 401 GNP GNP A . 
F 4 GOL 1  204 501 GOL GOL A . 
G 5 MG  1  205 4   MG  MG  A . 
H 2 WT6 1  201 201 WT6 C01 B . 
I 3 GNP 1  202 301 GNP GNP B . 
J 2 WT6 1  203 401 WT6 C01 B . 
K 4 GOL 1  204 501 GOL GOL B . 
L 4 GOL 1  205 601 GOL GOL B . 
M 5 MG  1  206 3   MG  MG  B . 
N 6 HOH 1  301 16  HOH HOH A . 
N 6 HOH 2  302 79  HOH HOH A . 
N 6 HOH 3  303 9   HOH HOH A . 
N 6 HOH 4  304 29  HOH HOH A . 
N 6 HOH 5  305 64  HOH HOH A . 
N 6 HOH 6  306 55  HOH HOH A . 
N 6 HOH 7  307 8   HOH HOH A . 
N 6 HOH 8  308 59  HOH HOH A . 
N 6 HOH 9  309 67  HOH HOH A . 
N 6 HOH 10 310 75  HOH HOH A . 
N 6 HOH 11 311 21  HOH HOH A . 
N 6 HOH 12 312 96  HOH HOH A . 
N 6 HOH 13 313 56  HOH HOH A . 
N 6 HOH 14 314 31  HOH HOH A . 
N 6 HOH 15 315 88  HOH HOH A . 
N 6 HOH 16 316 30  HOH HOH A . 
N 6 HOH 17 317 77  HOH HOH A . 
N 6 HOH 18 318 17  HOH HOH A . 
N 6 HOH 19 319 86  HOH HOH A . 
N 6 HOH 20 320 62  HOH HOH A . 
N 6 HOH 21 321 50  HOH HOH A . 
N 6 HOH 22 322 4   HOH HOH A . 
N 6 HOH 23 323 53  HOH HOH A . 
N 6 HOH 24 324 23  HOH HOH A . 
N 6 HOH 25 325 92  HOH HOH A . 
N 6 HOH 26 326 12  HOH HOH A . 
N 6 HOH 27 327 93  HOH HOH A . 
N 6 HOH 28 328 60  HOH HOH A . 
N 6 HOH 29 329 66  HOH HOH A . 
N 6 HOH 30 330 15  HOH HOH A . 
N 6 HOH 31 331 58  HOH HOH A . 
N 6 HOH 32 332 83  HOH HOH A . 
N 6 HOH 33 333 70  HOH HOH A . 
N 6 HOH 34 334 80  HOH HOH A . 
N 6 HOH 35 335 34  HOH HOH A . 
N 6 HOH 36 336 65  HOH HOH A . 
N 6 HOH 37 337 63  HOH HOH A . 
N 6 HOH 38 338 72  HOH HOH A . 
N 6 HOH 39 339 76  HOH HOH A . 
N 6 HOH 40 340 87  HOH HOH A . 
N 6 HOH 41 341 89  HOH HOH A . 
N 6 HOH 42 342 52  HOH HOH A . 
N 6 HOH 43 343 101 HOH HOH A . 
N 6 HOH 44 344 27  HOH HOH A . 
N 6 HOH 45 345 103 HOH HOH A . 
N 6 HOH 46 346 97  HOH HOH A . 
N 6 HOH 47 347 73  HOH HOH A . 
N 6 HOH 48 348 102 HOH HOH A . 
N 6 HOH 49 349 74  HOH HOH A . 
N 6 HOH 50 350 26  HOH HOH A . 
N 6 HOH 51 351 71  HOH HOH A . 
N 6 HOH 52 352 54  HOH HOH A . 
N 6 HOH 53 353 90  HOH HOH A . 
N 6 HOH 54 354 94  HOH HOH A . 
N 6 HOH 55 355 98  HOH HOH A . 
N 6 HOH 56 356 57  HOH HOH A . 
N 6 HOH 57 357 48  HOH HOH A . 
N 6 HOH 58 358 61  HOH HOH A . 
N 6 HOH 59 359 81  HOH HOH A . 
N 6 HOH 60 360 49  HOH HOH A . 
N 6 HOH 61 361 78  HOH HOH A . 
N 6 HOH 62 362 82  HOH HOH A . 
N 6 HOH 63 363 51  HOH HOH A . 
N 6 HOH 64 364 47  HOH HOH A . 
N 6 HOH 65 365 69  HOH HOH A . 
N 6 HOH 66 366 68  HOH HOH A . 
N 6 HOH 67 367 84  HOH HOH A . 
N 6 HOH 68 368 85  HOH HOH A . 
O 6 HOH 1  301 22  HOH HOH B . 
O 6 HOH 2  302 25  HOH HOH B . 
O 6 HOH 3  303 6   HOH HOH B . 
O 6 HOH 4  304 20  HOH HOH B . 
O 6 HOH 5  305 38  HOH HOH B . 
O 6 HOH 6  306 13  HOH HOH B . 
O 6 HOH 7  307 18  HOH HOH B . 
O 6 HOH 8  308 41  HOH HOH B . 
O 6 HOH 9  309 42  HOH HOH B . 
O 6 HOH 10 310 10  HOH HOH B . 
O 6 HOH 11 311 5   HOH HOH B . 
O 6 HOH 12 312 7   HOH HOH B . 
O 6 HOH 13 313 1   HOH HOH B . 
O 6 HOH 14 314 99  HOH HOH B . 
O 6 HOH 15 315 35  HOH HOH B . 
O 6 HOH 16 316 45  HOH HOH B . 
O 6 HOH 17 317 2   HOH HOH B . 
O 6 HOH 18 318 100 HOH HOH B . 
O 6 HOH 19 319 46  HOH HOH B . 
O 6 HOH 20 320 36  HOH HOH B . 
O 6 HOH 21 321 91  HOH HOH B . 
O 6 HOH 22 322 43  HOH HOH B . 
O 6 HOH 23 323 24  HOH HOH B . 
O 6 HOH 24 324 33  HOH HOH B . 
O 6 HOH 25 325 32  HOH HOH B . 
O 6 HOH 26 326 37  HOH HOH B . 
O 6 HOH 27 327 44  HOH HOH B . 
O 6 HOH 28 328 39  HOH HOH B . 
O 6 HOH 29 329 95  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 B HIS -37 ? CG  ? B HIS 2  CG  
6  1 Y 1 B HIS -37 ? ND1 ? B HIS 2  ND1 
7  1 Y 1 B HIS -37 ? CD2 ? B HIS 2  CD2 
8  1 Y 1 B HIS -37 ? CE1 ? B HIS 2  CE1 
9  1 Y 1 B HIS -37 ? NE2 ? B HIS 2  NE2 
10 1 Y 1 B GLU -30 ? CG  ? B GLU 9  CG  
11 1 Y 1 B GLU -30 ? CD  ? B GLU 9  CD  
12 1 Y 1 B GLU -30 ? OE1 ? B GLU 9  OE1 
13 1 Y 1 B GLU -30 ? OE2 ? B GLU 9  OE2 
14 1 Y 1 B TYR 6   ? CG  ? B TYR 44 CG  
15 1 Y 1 B TYR 6   ? CD1 ? B TYR 44 CD1 
16 1 Y 1 B TYR 6   ? CD2 ? B TYR 44 CD2 
17 1 Y 1 B TYR 6   ? CE1 ? B TYR 44 CE1 
18 1 Y 1 B TYR 6   ? CE2 ? B TYR 44 CE2 
19 1 Y 1 B TYR 6   ? CZ  ? B TYR 44 CZ  
20 1 Y 1 B TYR 6   ? OH  ? B TYR 44 OH  
# 
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                     8P3J 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.436 
_cell.length_a_esd                 ? 
_cell.length_b                     75.828 
_cell.length_b_esd                 ? 
_cell.length_c                     118.530 
_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                         8P3J 
_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                   8P3J 
_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             2.89 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.48 
_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 XE 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         2021-03-02 
_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   0.9795 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8P3J 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.16 
_reflns.d_resolution_low                               63.88 
_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                                     30872 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           96.39 
_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                          2.80 
_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                                   0.972 
_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                                    2.16 
_reflns_shell.d_res_low                                     2.237 
_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                             3056 
_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                                  0.325 
_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                                 8P3J 
_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                            2.16 
_refine.ls_d_res_low                             63.88 
_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                     29767 
_refine.ls_number_reflns_R_free                  1522 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.39 
_refine.ls_percent_reflns_R_free                 5.11 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2875 
_refine.ls_R_factor_R_free                       0.3508 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2840 
_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                 39.16 
_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                            0.51 
_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                       2.16 
_refine_hist.d_res_low                        63.88 
_refine_hist.number_atoms_solvent             97 
_refine_hist.number_atoms_total               3650 
_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        3393 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         160 
_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  ? 3650 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.173  ? 4928 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 24.530 ? 520  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.053  ? 522  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 622  ? 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' 2.16 2.23  . . 108 1982 75.00  . . . . 0.6704 . . . . . . . . . . . 0.7369 
'X-RAY DIFFRACTION' 2.23 2.31  . . 128 2227 86.00  . . . . 0.5627 . . . . . . . . . . . 0.6231 
'X-RAY DIFFRACTION' 2.31 2.40  . . 160 2594 100.00 . . . . 0.4841 . . . . . . . . . . . 0.5707 
'X-RAY DIFFRACTION' 2.40 2.51  . . 146 2616 100.00 . . . . 0.3419 . . . . . . . . . . . 0.3930 
'X-RAY DIFFRACTION' 2.51 2.64  . . 128 2627 100.00 . . . . 0.3038 . . . . . . . . . . . 0.3544 
'X-RAY DIFFRACTION' 2.64 2.81  . . 141 2667 100.00 . . . . 0.2779 . . . . . . . . . . . 0.3279 
'X-RAY DIFFRACTION' 2.81 3.03  . . 159 2611 100.00 . . . . 0.2697 . . . . . . . . . . . 0.3065 
'X-RAY DIFFRACTION' 3.03 3.33  . . 141 2655 100.00 . . . . 0.2364 . . . . . . . . . . . 0.3085 
'X-RAY DIFFRACTION' 3.33 3.81  . . 122 2707 100.00 . . . . 0.2174 . . . . . . . . . . . 0.3125 
'X-RAY DIFFRACTION' 3.81 4.80  . . 130 2731 100.00 . . . . 0.1804 . . . . . . . . . . . 0.2223 
'X-RAY DIFFRACTION' 4.80 63.88 . . 159 2828 100.00 . . . . 0.2000 . . . . . . . . . . . 0.2480 
# 
_struct.entry_id                     8P3J 
_struct.title                        'Fusion hSlp2-a_Rab27A non-covalent complex with hit fragment IMP-1704' 
_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        8P3J 
_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 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 2 ? 
I N N 3 ? 
J N N 2 ? 
K N N 4 ? 
L N N 4 ? 
M N N 5 ? 
N N N 6 ? 
O 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 8P3J A 4  ? 31  ? Q9HCH5 5 ? 32  ? -35 -7  
2 2 8P3J A 39 ? 230 ? P51159 1 ? 192 ? 1   192 
3 1 8P3J B 4  ? 31  ? Q9HCH5 5 ? 32  ? -35 -8  
4 2 8P3J B 39 ? 230 ? P51159 1 ? 192 ? 1   192 
# 
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 8P3J GLY A 1   ? UNP Q9HCH5 ?   ?   'expression tag'      -38 1  
1 8P3J HIS A 2   ? UNP Q9HCH5 ?   ?   'expression tag'      -37 2  
1 8P3J MET A 3   ? UNP Q9HCH5 ?   ?   'expression tag'      -36 3  
1 8P3J GLY A 32  ? UNP Q9HCH5 ?   ?   linker                -6  4  
1 8P3J SER A 33  ? UNP Q9HCH5 ?   ?   linker                -5  5  
1 8P3J GLY A 34  ? UNP Q9HCH5 ?   ?   linker                -4  6  
1 8P3J SER A 35  ? UNP Q9HCH5 ?   ?   linker                -3  7  
1 8P3J GLY A 36  ? UNP Q9HCH5 ?   ?   linker                -2  8  
1 8P3J SER A 37  ? UNP Q9HCH5 ?   ?   linker                -1  9  
1 8P3J GLY A 38  ? UNP Q9HCH5 ?   ?   linker                0   10 
2 8P3J LEU A 116 ? UNP P51159 GLN 78  'engineered mutation' 78  11 
2 8P3J ALA A 161 ? UNP P51159 CYS 123 'engineered mutation' 123 12 
2 8P3J SER A 226 ? UNP P51159 CYS 188 'engineered mutation' 188 13 
3 8P3J GLY B 1   ? UNP Q9HCH5 ?   ?   'expression tag'      -38 14 
3 8P3J HIS B 2   ? UNP Q9HCH5 ?   ?   'expression tag'      -37 15 
3 8P3J MET B 3   ? UNP Q9HCH5 ?   ?   'expression tag'      -36 16 
3 8P3J GLY B 32  ? UNP Q9HCH5 ?   ?   linker                -6  17 
3 8P3J SER B 33  ? UNP Q9HCH5 ?   ?   linker                -5  18 
3 8P3J GLY B 34  ? UNP Q9HCH5 ?   ?   linker                -4  19 
3 8P3J SER B 35  ? UNP Q9HCH5 ?   ?   linker                -3  20 
3 8P3J GLY B 36  ? UNP Q9HCH5 ?   ?   linker                -2  21 
3 8P3J SER B 37  ? UNP Q9HCH5 ?   ?   linker                -1  22 
3 8P3J GLY B 38  ? UNP Q9HCH5 ?   ?   linker                0   23 
4 8P3J LEU B 116 ? UNP P51159 GLN 78  'engineered mutation' 78  24 
4 8P3J ALA B 161 ? UNP P51159 CYS 123 'engineered mutation' 123 25 
4 8P3J SER B 226 ? UNP P51159 CYS 188 'engineered mutation' 188 26 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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)' 5750  ? 
1 MORE         -41   ? 
1 'SSA (A^2)'  20300 ? 
# 
_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 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 30  ? THR A -32 GLU A -9  1 ? 24 
HELX_P HELX_P2  AA2 GLY A 59  ? GLY A 70  ? GLY A 21  GLY A 32  1 ? 12 
HELX_P HELX_P3  AA3 LEU A 116 ? ARG A 118 ? LEU A 78  ARG A 80  5 ? 3  
HELX_P HELX_P4  AA4 PHE A 119 ? THR A 124 ? PHE A 81  THR A 86  1 ? 6  
HELX_P HELX_P5  AA5 ALA A 125 ? ALA A 130 ? ALA A 87  ALA A 92  5 ? 6  
HELX_P HELX_P6  AA6 ASN A 141 ? ASN A 147 ? ASN A 103 ASN A 109 1 ? 7  
HELX_P HELX_P7  AA7 ASN A 147 ? ALA A 159 ? ASN A 109 ALA A 121 1 ? 13 
HELX_P HELX_P8  AA8 LYS A 182 ? TYR A 193 ? LYS A 144 TYR A 155 1 ? 12 
HELX_P HELX_P9  AA9 ASN A 207 ? GLU A 224 ? ASN A 169 GLU A 186 1 ? 18 
HELX_P HELX_P10 AB1 THR B 7   ? GLU B 28  ? THR B -32 GLU B -11 1 ? 22 
HELX_P HELX_P11 AB2 GLY B 59  ? GLY B 70  ? GLY B 21  GLY B 32  1 ? 12 
HELX_P HELX_P12 AB3 LEU B 116 ? ARG B 118 ? LEU B 78  ARG B 80  5 ? 3  
HELX_P HELX_P13 AB4 PHE B 119 ? ALA B 125 ? PHE B 81  ALA B 87  1 ? 7  
HELX_P HELX_P14 AB5 PHE B 126 ? ALA B 130 ? PHE B 88  ALA B 92  5 ? 5  
HELX_P HELX_P15 AB6 ASN B 141 ? ASN B 147 ? ASN B 103 ASN B 109 1 ? 7  
HELX_P HELX_P16 AB7 ASN B 147 ? ALA B 159 ? ASN B 109 ALA B 121 1 ? 13 
HELX_P HELX_P17 AB8 LYS B 182 ? GLY B 194 ? LYS B 144 GLY B 156 1 ? 13 
HELX_P HELX_P18 AB9 ASN B 207 ? GLU B 224 ? ASN B 169 GLU B 186 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A THR 61 OG1 ? ? ? 1_555 G MG  . MG ? ? A THR 23  A MG  205 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
metalc2  metalc ? ? A THR 79 OG1 ? ? ? 1_555 G MG  . MG ? ? A THR 41  A MG  205 1_555 ? ? ? ? ? ? ? 2.240 ? ? 
metalc3  metalc ? ? E GNP .  O1G ? ? ? 1_555 G MG  . MG ? ? A GNP 203 A MG  205 1_555 ? ? ? ? ? ? ? 1.909 ? ? 
metalc4  metalc ? ? E GNP .  O2B ? ? ? 1_555 G MG  . MG ? ? A GNP 203 A MG  205 1_555 ? ? ? ? ? ? ? 2.001 ? ? 
metalc5  metalc ? ? G MG  .  MG  ? ? ? 1_555 N HOH . O  ? ? A MG  205 A HOH 303 1_555 ? ? ? ? ? ? ? 2.372 ? ? 
metalc6  metalc ? ? G MG  .  MG  ? ? ? 1_555 N HOH . O  ? ? A MG  205 A HOH 307 1_555 ? ? ? ? ? ? ? 2.151 ? ? 
metalc7  metalc ? ? B THR 61 OG1 ? ? ? 1_555 M MG  . MG ? ? B THR 23  B MG  206 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc8  metalc ? ? B THR 79 OG1 ? ? ? 1_555 M MG  . MG ? ? B THR 41  B MG  206 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
metalc9  metalc ? ? I GNP .  O1G ? ? ? 1_555 M MG  . MG ? ? B GNP 202 B MG  206 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
metalc10 metalc ? ? I GNP .  O1B ? ? ? 1_555 M MG  . MG ? ? B GNP 202 B MG  206 1_555 ? ? ? ? ? ? ? 1.970 ? ? 
metalc11 metalc ? ? M MG  .  MG  ? ? ? 1_555 O HOH . O  ? ? B MG  206 B HOH 303 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc12 metalc ? ? M MG  .  MG  ? ? ? 1_555 O HOH . O  ? ? B MG  206 B HOH 312 1_555 ? ? ? ? ? ? ? 1.930 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG1 ? A THR 61 ? A THR 23  ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 OG1 ? A THR 79 ? A THR 41  ? 1_555 83.4  ? 
2  OG1 ? A THR 61 ? A THR 23  ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O1G ? E GNP .  ? A GNP 203 ? 1_555 166.8 ? 
3  OG1 ? A THR 79 ? A THR 41  ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O1G ? E GNP .  ? A GNP 203 ? 1_555 92.4  ? 
4  OG1 ? A THR 61 ? A THR 23  ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O2B ? E GNP .  ? A GNP 203 ? 1_555 98.3  ? 
5  OG1 ? A THR 79 ? A THR 41  ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O2B ? E GNP .  ? A GNP 203 ? 1_555 177.3 ? 
6  O1G ? E GNP .  ? A GNP 203 ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O2B ? E GNP .  ? A GNP 203 ? 1_555 86.4  ? 
7  OG1 ? A THR 61 ? A THR 23  ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O   ? N HOH .  ? A HOH 303 ? 1_555 82.0  ? 
8  OG1 ? A THR 79 ? A THR 41  ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O   ? N HOH .  ? A HOH 303 ? 1_555 91.1  ? 
9  O1G ? E GNP .  ? A GNP 203 ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O   ? N HOH .  ? A HOH 303 ? 1_555 85.7  ? 
10 O2B ? E GNP .  ? A GNP 203 ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O   ? N HOH .  ? A HOH 303 ? 1_555 91.2  ? 
11 OG1 ? A THR 61 ? A THR 23  ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O   ? N HOH .  ? A HOH 307 ? 1_555 97.4  ? 
12 OG1 ? A THR 79 ? A THR 41  ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O   ? N HOH .  ? A HOH 307 ? 1_555 84.7  ? 
13 O1G ? E GNP .  ? A GNP 203 ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O   ? N HOH .  ? A HOH 307 ? 1_555 94.6  ? 
14 O2B ? E GNP .  ? A GNP 203 ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O   ? N HOH .  ? A HOH 307 ? 1_555 93.0  ? 
15 O   ? N HOH .  ? A HOH 303 ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O   ? N HOH .  ? A HOH 307 ? 1_555 175.8 ? 
16 OG1 ? B THR 61 ? B THR 23  ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 OG1 ? B THR 79 ? B THR 41  ? 1_555 88.4  ? 
17 OG1 ? B THR 61 ? B THR 23  ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 O1G ? I GNP .  ? B GNP 202 ? 1_555 163.9 ? 
18 OG1 ? B THR 79 ? B THR 41  ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 O1G ? I GNP .  ? B GNP 202 ? 1_555 87.6  ? 
19 OG1 ? B THR 61 ? B THR 23  ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 O1B ? I GNP .  ? B GNP 202 ? 1_555 93.6  ? 
20 OG1 ? B THR 79 ? B THR 41  ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 O1B ? I GNP .  ? B GNP 202 ? 1_555 163.7 ? 
21 O1G ? I GNP .  ? B GNP 202 ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 O1B ? I GNP .  ? B GNP 202 ? 1_555 86.0  ? 
22 OG1 ? B THR 61 ? B THR 23  ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 O   ? O HOH .  ? B HOH 303 ? 1_555 81.2  ? 
23 OG1 ? B THR 79 ? B THR 41  ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 O   ? O HOH .  ? B HOH 303 ? 1_555 78.6  ? 
24 O1G ? I GNP .  ? B GNP 202 ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 O   ? O HOH .  ? B HOH 303 ? 1_555 82.7  ? 
25 O1B ? I GNP .  ? B GNP 202 ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 O   ? O HOH .  ? B HOH 303 ? 1_555 85.8  ? 
26 OG1 ? B THR 61 ? B THR 23  ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 O   ? O HOH .  ? B HOH 312 ? 1_555 103.5 ? 
27 OG1 ? B THR 79 ? B THR 41  ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 O   ? O HOH .  ? B HOH 312 ? 1_555 92.4  ? 
28 O1G ? I GNP .  ? B GNP 202 ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 O   ? O HOH .  ? B HOH 312 ? 1_555 92.3  ? 
29 O1B ? I GNP .  ? B GNP 202 ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 O   ? O HOH .  ? B HOH 312 ? 1_555 102.8 ? 
30 O   ? O HOH .  ? B HOH 303 ? 1_555 MG ? M MG . ? B MG 206 ? 1_555 O   ? O HOH .  ? B HOH 312 ? 1_555 169.8 ? 
# 
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  ? TYR A 91  ? ILE A 44  TYR A 53  
AA1 2 GLN A 104 ? THR A 113 ? GLN A 66  THR A 75  
AA1 3 LEU A 47  ? GLY A 54  ? LEU A 9   GLY A 16  
AA1 4 PHE A 133 ? ASP A 138 ? PHE A 95  ASP A 100 
AA1 5 ILE A 166 ? ASN A 171 ? ILE A 128 ASN A 133 
AA1 6 TYR A 197 ? GLU A 199 ? TYR A 159 GLU A 161 
AA2 1 ILE B 82  ? TYR B 91  ? ILE B 44  TYR B 53  
AA2 2 GLN B 104 ? THR B 113 ? GLN B 66  THR B 75  
AA2 3 TYR B 46  ? GLY B 54  ? TYR B 8   GLY B 16  
AA2 4 PHE B 133 ? ASP B 138 ? PHE B 95  ASP B 100 
AA2 5 ILE B 166 ? ASN B 171 ? ILE B 128 ASN B 133 
AA2 6 TYR B 197 ? GLU B 199 ? TYR B 159 GLU B 161 
# 
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 45  O ASP A 112 ? O ASP A 74  
AA1 2 3 O TRP A 111 ? O TRP A 73  N ALA A 52  ? N ALA A 14  
AA1 3 4 N LEU A 51  ? N LEU A 13  O LEU A 134 ? O LEU A 96  
AA1 4 5 N LEU A 135 ? N LEU A 97  O CYS A 169 ? O CYS A 131 
AA1 5 6 N LEU A 168 ? N LEU A 130 O PHE A 198 ? O PHE A 160 
AA2 1 2 N ASP B 83  ? N ASP B 45  O ASP B 112 ? O ASP B 74  
AA2 2 3 O TRP B 111 ? O TRP B 73  N PHE B 50  ? N PHE B 12  
AA2 3 4 N LEU B 51  ? N LEU B 13  O LEU B 134 ? O LEU B 96  
AA2 4 5 N LEU B 135 ? N LEU B 97  O CYS B 169 ? O CYS B 131 
AA2 5 6 N LEU B 168 ? N LEU B 130 O PHE B 198 ? O PHE B 160 
# 
_pdbx_entry_details.entry_id                   8P3J 
_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   N 
# 
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 NZ  A LYS 11  ? ? O19 A WT6 201 ? ? 1.30 
2 1 ND2 B ASN 125 ? ? C04 B WT6 203 ? ? 1.68 
3 1 ND2 B ASN 125 ? ? C05 B WT6 203 ? ? 1.98 
4 1 OD1 B ASP -18 ? ? NZ  B LYS -14 ? ? 2.10 
5 1 O   A LYS -14 ? ? O   A HOH 301 ? ? 2.17 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 OE2 A GLU 138 ? ? 1_555 OE1 B GLU 138 ? ? 2_554 1.46 
2 1 CD  A GLU 138 ? ? 1_555 OE1 B GLU 138 ? ? 2_554 1.87 
3 1 NH2 A ARG 67  ? ? 1_555 OG  B SER 115 ? ? 4_455 2.15 
# 
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 VAL A 42  ? ? -63.64  73.10   
2 1 ASN A 125 ? ? 60.06   61.26   
3 1 GLU B -9  ? ? -55.58  59.98   
4 1 SER B 56  ? ? -110.92 -154.80 
5 1 THR B 62  ? ? 24.30   62.77   
6 1 ASN B 125 ? ? 50.68   72.42   
7 1 VAL B 142 ? ? -145.54 -12.73  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ASP 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    7 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   TYR 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    8 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            148.15 
# 
_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                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       368 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.33 
_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 -7  ? A ARG 31  
2  1 Y 1 A GLY -6  ? A GLY 32  
3  1 Y 1 A SER -5  ? A SER 33  
4  1 Y 1 A GLY -4  ? A GLY 34  
5  1 Y 1 A SER -3  ? A SER 35  
6  1 Y 1 A GLY -2  ? A GLY 36  
7  1 Y 1 A SER -1  ? A SER 37  
8  1 Y 1 A GLY 0   ? A GLY 38  
9  1 Y 1 A MET 1   ? A MET 39  
10 1 Y 1 A SER 2   ? A SER 40  
11 1 Y 1 A ASP 3   ? A ASP 41  
12 1 Y 1 A GLY 4   ? A GLY 42  
13 1 Y 1 A ASP 5   ? A ASP 43  
14 1 Y 1 A TYR 6   ? A TYR 44  
15 1 Y 1 A VAL 189 ? A VAL 227 
16 1 Y 1 A ASP 190 ? A ASP 228 
17 1 Y 1 A LYS 191 ? A LYS 229 
18 1 Y 1 A SER 192 ? A SER 230 
19 1 Y 1 B GLY -6  ? B GLY 32  
20 1 Y 1 B SER -5  ? B SER 33  
21 1 Y 1 B GLY -4  ? B GLY 34  
22 1 Y 1 B SER -3  ? B SER 35  
23 1 Y 1 B GLY -2  ? B GLY 36  
24 1 Y 1 B SER -1  ? B SER 37  
25 1 Y 1 B GLY 0   ? B GLY 38  
26 1 Y 1 B MET 1   ? B MET 39  
27 1 Y 1 B SER 2   ? B SER 40  
28 1 Y 1 B ASP 3   ? B ASP 41  
29 1 Y 1 B GLY 4   ? B GLY 42  
30 1 Y 1 B ASP 5   ? B ASP 43  
31 1 Y 1 B VAL 189 ? B VAL 227 
32 1 Y 1 B ASP 190 ? B ASP 228 
33 1 Y 1 B LYS 191 ? B LYS 229 
34 1 Y 1 B SER 192 ? 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 
WT6 C10    C  N N 455 
WT6 C16    C  N N 456 
WT6 C17    C  N N 457 
WT6 C03    C  Y N 458 
WT6 C04    C  Y N 459 
WT6 C05    C  Y N 460 
WT6 C06    C  Y N 461 
WT6 C08    C  N N 462 
WT6 C09    C  N N 463 
WT6 C12    C  Y N 464 
WT6 C13    C  Y N 465 
WT6 C15    C  N N 466 
WT6 C18    C  N N 467 
WT6 N07    N  N N 468 
WT6 N14    N  N N 469 
WT6 O01    O  N N 470 
WT6 O11    O  N N 471 
WT6 O19    O  N N 472 
WT6 S02    S  N N 473 
WT6 H1     H  N N 474 
WT6 H2     H  N N 475 
WT6 H3     H  N N 476 
WT6 H4     H  N N 477 
WT6 H5     H  N N 478 
WT6 H6     H  N N 479 
WT6 H7     H  N N 480 
WT6 H8     H  N N 481 
WT6 H9     H  N N 482 
WT6 H10    H  N N 483 
WT6 H11    H  N N 484 
WT6 H12    H  N N 485 
WT6 H13    H  N N 486 
WT6 H14    H  N N 487 
WT6 H15    H  N N 488 
WT6 H16    H  N N 489 
# 
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 
WT6 C10   C09    doub N N 440 
WT6 O11   C08    doub N N 441 
WT6 C09   C08    sing N N 442 
WT6 C08   N07    sing N N 443 
WT6 O19   S02    doub N N 444 
WT6 C05   C04    doub Y N 445 
WT6 C05   C06    sing Y N 446 
WT6 C04   C03    sing Y N 447 
WT6 N07   C06    sing N N 448 
WT6 C06   C12    doub Y N 449 
WT6 S02   C03    sing N N 450 
WT6 S02   O01    doub N N 451 
WT6 S02   N14    sing N N 452 
WT6 C03   C13    doub Y N 453 
WT6 C15   N14    sing N N 454 
WT6 C15   C16    sing N N 455 
WT6 C12   C13    sing Y N 456 
WT6 N14   C18    sing N N 457 
WT6 C16   C17    sing N N 458 
WT6 C18   C17    sing N N 459 
WT6 C10   H1     sing N N 460 
WT6 C10   H2     sing N N 461 
WT6 C16   H3     sing N N 462 
WT6 C16   H4     sing N N 463 
WT6 C17   H5     sing N N 464 
WT6 C17   H6     sing N N 465 
WT6 C04   H7     sing N N 466 
WT6 C05   H8     sing N N 467 
WT6 C09   H9     sing N N 468 
WT6 C12   H10    sing N N 469 
WT6 C13   H11    sing N N 470 
WT6 C15   H12    sing N N 471 
WT6 C15   H13    sing N N 472 
WT6 C18   H14    sing N N 473 
WT6 C18   H15    sing N N 474 
WT6 N07   H16    sing N N 475 
# 
_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                    8P3J 
_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]   0.016016 
_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]   0.013188 
_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]   0.008437 
_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   ? 23.820  -18.214 12.647  1.00 44.45  ? -38 GLY A N     1 
ATOM   2    C  CA    . GLY A 1 1   ? 23.342  -17.125 13.478  1.00 28.09  ? -38 GLY A CA    1 
ATOM   3    C  C     . GLY A 1 1   ? 24.390  -16.063 13.731  1.00 35.93  ? -38 GLY A C     1 
ATOM   4    O  O     . GLY A 1 1   ? 24.809  -15.844 14.871  1.00 45.78  ? -38 GLY A O     1 
ATOM   5    N  N     . HIS A 1 2   ? 24.829  -15.387 12.664  1.00 39.59  ? -37 HIS A N     1 
ATOM   6    C  CA    . HIS A 1 2   ? 25.838  -14.334 12.779  1.00 46.61  ? -37 HIS A CA    1 
ATOM   7    C  C     . HIS A 1 2   ? 25.474  -13.181 11.827  1.00 43.13  ? -37 HIS A C     1 
ATOM   8    O  O     . HIS A 1 2   ? 26.142  -12.902 10.832  1.00 40.59  ? -37 HIS A O     1 
ATOM   9    C  CB    . HIS A 1 2   ? 27.243  -14.882 12.510  1.00 42.91  ? -37 HIS A CB    1 
ATOM   10   C  CG    . HIS A 1 2   ? 27.739  -15.819 13.571  1.00 44.30  ? -37 HIS A CG    1 
ATOM   11   N  ND1   . HIS A 1 2   ? 28.628  -15.430 14.550  1.00 52.86  ? -37 HIS A ND1   1 
ATOM   12   C  CD2   . HIS A 1 2   ? 27.481  -17.130 13.797  1.00 44.72  ? -37 HIS A CD2   1 
ATOM   13   C  CE1   . HIS A 1 2   ? 28.889  -16.458 15.338  1.00 54.90  ? -37 HIS A CE1   1 
ATOM   14   N  NE2   . HIS A 1 2   ? 28.204  -17.502 14.903  1.00 45.53  ? -37 HIS A NE2   1 
ATOM   15   N  N     . MET A 1 3   ? 24.395  -12.472 12.157  1.00 41.73  ? -36 MET A N     1 
ATOM   16   C  CA    . MET A 1 3   ? 23.945  -11.349 11.340  1.00 45.62  ? -36 MET A CA    1 
ATOM   17   C  C     . MET A 1 3   ? 24.864  -10.150 11.532  1.00 44.51  ? -36 MET A C     1 
ATOM   18   O  O     . MET A 1 3   ? 24.994  -9.636  12.648  1.00 45.80  ? -36 MET A O     1 
ATOM   19   C  CB    . MET A 1 3   ? 22.519  -10.966 11.711  1.00 44.00  ? -36 MET A CB    1 
ATOM   20   C  CG    . MET A 1 3   ? 21.451  -11.891 11.203  1.00 39.65  ? -36 MET A CG    1 
ATOM   21   S  SD    . MET A 1 3   ? 19.926  -11.433 12.026  1.00 41.47  ? -36 MET A SD    1 
ATOM   22   C  CE    . MET A 1 3   ? 18.981  -12.953 11.897  1.00 43.56  ? -36 MET A CE    1 
ATOM   23   N  N     . SER A 1 4   ? 25.488  -9.696  10.445  1.00 30.70  ? -35 SER A N     1 
ATOM   24   C  CA    . SER A 1 4   ? 26.308  -8.499  10.513  1.00 35.58  ? -35 SER A CA    1 
ATOM   25   C  C     . SER A 1 4   ? 25.422  -7.271  10.644  1.00 38.63  ? -35 SER A C     1 
ATOM   26   O  O     . SER A 1 4   ? 24.297  -7.232  10.142  1.00 34.75  ? -35 SER A O     1 
ATOM   27   C  CB    . SER A 1 4   ? 27.187  -8.371  9.267   1.00 42.73  ? -35 SER A CB    1 
ATOM   28   O  OG    . SER A 1 4   ? 28.085  -9.460  9.150   1.00 46.31  ? -35 SER A OG    1 
ATOM   29   N  N     . PHE A 1 5   ? 25.933  -6.261  11.338  1.00 35.54  ? -34 PHE A N     1 
ATOM   30   C  CA    . PHE A 1 5   ? 25.272  -4.970  11.305  1.00 36.65  ? -34 PHE A CA    1 
ATOM   31   C  C     . PHE A 1 5   ? 25.353  -4.398  9.891   1.00 36.98  ? -34 PHE A C     1 
ATOM   32   O  O     . PHE A 1 5   ? 25.990  -4.959  8.992   1.00 30.05  ? -34 PHE A O     1 
ATOM   33   C  CB    . PHE A 1 5   ? 25.892  -4.021  12.331  1.00 36.81  ? -34 PHE A CB    1 
ATOM   34   C  CG    . PHE A 1 5   ? 25.394  -4.242  13.723  1.00 42.31  ? -34 PHE A CG    1 
ATOM   35   C  CD1   . PHE A 1 5   ? 24.105  -3.876  14.076  1.00 41.31  ? -34 PHE A CD1   1 
ATOM   36   C  CD2   . PHE A 1 5   ? 26.206  -4.831  14.680  1.00 47.98  ? -34 PHE A CD2   1 
ATOM   37   C  CE1   . PHE A 1 5   ? 23.637  -4.089  15.362  1.00 38.92  ? -34 PHE A CE1   1 
ATOM   38   C  CE2   . PHE A 1 5   ? 25.744  -5.046  15.970  1.00 43.05  ? -34 PHE A CE2   1 
ATOM   39   C  CZ    . PHE A 1 5   ? 24.458  -4.675  16.307  1.00 42.51  ? -34 PHE A CZ    1 
ATOM   40   N  N     . LEU A 1 6   ? 24.690  -3.268  9.687   1.00 25.66  ? -33 LEU A N     1 
ATOM   41   C  CA    . LEU A 1 6   ? 24.734  -2.626  8.385   1.00 24.48  ? -33 LEU A CA    1 
ATOM   42   C  C     . LEU A 1 6   ? 26.120  -2.047  8.133   1.00 24.23  ? -33 LEU A C     1 
ATOM   43   O  O     . LEU A 1 6   ? 26.663  -1.319  8.969   1.00 28.53  ? -33 LEU A O     1 
ATOM   44   C  CB    . LEU A 1 6   ? 23.680  -1.529  8.315   1.00 30.79  ? -33 LEU A CB    1 
ATOM   45   C  CG    . LEU A 1 6   ? 22.290  -1.969  8.790   1.00 27.25  ? -33 LEU A CG    1 
ATOM   46   C  CD1   . LEU A 1 6   ? 21.442  -0.787  9.274   1.00 23.04  ? -33 LEU A CD1   1 
ATOM   47   C  CD2   . LEU A 1 6   ? 21.598  -2.707  7.664   1.00 27.91  ? -33 LEU A CD2   1 
ATOM   48   N  N     . THR A 1 7   ? 26.702  -2.390  6.989   1.00 23.25  ? -32 THR A N     1 
ATOM   49   C  CA    . THR A 1 7   ? 27.880  -1.685  6.514   1.00 27.73  ? -32 THR A CA    1 
ATOM   50   C  C     . THR A 1 7   ? 27.546  -0.213  6.287   1.00 26.39  ? -32 THR A C     1 
ATOM   51   O  O     . THR A 1 7   ? 26.381  0.184   6.252   1.00 24.35  ? -32 THR A O     1 
ATOM   52   C  CB    . THR A 1 7   ? 28.380  -2.324  5.220   1.00 30.36  ? -32 THR A CB    1 
ATOM   53   O  OG1   . THR A 1 7   ? 27.532  -1.928  4.139   1.00 29.40  ? -32 THR A OG1   1 
ATOM   54   C  CG2   . THR A 1 7   ? 28.310  -3.834  5.343   1.00 32.97  ? -32 THR A CG2   1 
ATOM   55   N  N     . GLU A 1 8   ? 28.580  0.611   6.135   1.00 28.68  ? -31 GLU A N     1 
ATOM   56   C  CA    . GLU A 1 8   ? 28.310  2.024   5.886   1.00 29.78  ? -31 GLU A CA    1 
ATOM   57   C  C     . GLU A 1 8   ? 27.755  2.277   4.490   1.00 24.57  ? -31 GLU A C     1 
ATOM   58   O  O     . GLU A 1 8   ? 27.116  3.311   4.273   1.00 29.31  ? -31 GLU A O     1 
ATOM   59   C  CB    . GLU A 1 8   ? 29.566  2.862   6.108   1.00 39.62  ? -31 GLU A CB    1 
ATOM   60   C  CG    . GLU A 1 8   ? 30.136  2.725   7.511   1.00 54.79  ? -31 GLU A CG    1 
ATOM   61   C  CD    . GLU A 1 8   ? 31.528  3.322   7.641   1.00 73.46  ? -31 GLU A CD    1 
ATOM   62   O  OE1   . GLU A 1 8   ? 31.913  4.125   6.760   1.00 62.26  ? -31 GLU A OE1   1 
ATOM   63   O  OE2   . GLU A 1 8   ? 32.237  2.977   8.620   1.00 53.57  ? -31 GLU A OE2   1 
ATOM   64   N  N     . GLU A 1 9   ? 27.985  1.369   3.542   1.00 23.90  ? -30 GLU A N     1 
ATOM   65   C  CA    . GLU A 1 9   ? 27.330  1.477   2.244   1.00 20.71  ? -30 GLU A CA    1 
ATOM   66   C  C     . GLU A 1 9   ? 25.843  1.180   2.376   1.00 21.41  ? -30 GLU A C     1 
ATOM   67   O  O     . GLU A 1 9   ? 25.001  1.939   1.882   1.00 27.91  ? -30 GLU A O     1 
ATOM   68   C  CB    . GLU A 1 9   ? 27.997  0.534   1.234   1.00 25.23  ? -30 GLU A CB    1 
ATOM   69   N  N     . GLU A 1 10  ? 25.499  0.092   3.064   1.00 22.13  ? -29 GLU A N     1 
ATOM   70   C  CA    . GLU A 1 10  ? 24.095  -0.178  3.351   1.00 20.45  ? -29 GLU A CA    1 
ATOM   71   C  C     . GLU A 1 10  ? 23.473  0.981   4.111   1.00 26.62  ? -29 GLU A C     1 
ATOM   72   O  O     . GLU A 1 10  ? 22.416  1.498   3.727   1.00 24.39  ? -29 GLU A O     1 
ATOM   73   C  CB    . GLU A 1 10  ? 23.959  -1.471  4.155   1.00 22.14  ? -29 GLU A CB    1 
ATOM   74   C  CG    . GLU A 1 10  ? 24.465  -2.715  3.464   1.00 26.81  ? -29 GLU A CG    1 
ATOM   75   C  CD    . GLU A 1 10  ? 24.492  -3.931  4.382   1.00 28.92  ? -29 GLU A CD    1 
ATOM   76   O  OE1   . GLU A 1 10  ? 23.983  -4.990  3.959   1.00 23.07  ? -29 GLU A OE1   1 
ATOM   77   O  OE2   . GLU A 1 10  ? 25.037  -3.846  5.509   1.00 30.38  ? -29 GLU A OE2   1 
ATOM   78   N  N     . GLN A 1 11  ? 24.136  1.408   5.195   1.00 27.52  ? -28 GLN A N     1 
ATOM   79   C  CA    . GLN A 1 11  ? 23.635  2.503   6.021   1.00 28.03  ? -28 GLN A CA    1 
ATOM   80   C  C     . GLN A 1 11  ? 23.410  3.746   5.169   1.00 17.01  ? -28 GLN A C     1 
ATOM   81   O  O     . GLN A 1 11  ? 22.390  4.427   5.313   1.00 26.68  ? -28 GLN A O     1 
ATOM   82   C  CB    . GLN A 1 11  ? 24.637  2.759   7.170   1.00 29.30  ? -28 GLN A CB    1 
ATOM   83   C  CG    . GLN A 1 11  ? 24.217  3.634   8.364   1.00 26.76  ? -28 GLN A CG    1 
ATOM   84   C  CD    . GLN A 1 11  ? 23.590  2.856   9.548   1.00 33.37  ? -28 GLN A CD    1 
ATOM   85   O  OE1   . GLN A 1 11  ? 22.434  3.075   9.921   1.00 35.46  ? -28 GLN A OE1   1 
ATOM   86   N  NE2   . GLN A 1 11  ? 24.358  1.945   10.128  1.00 21.89  ? -28 GLN A NE2   1 
ATOM   87   N  N     . GLU A 1 12  ? 24.324  4.012   4.228   1.00 29.15  ? -27 GLU A N     1 
ATOM   88   C  CA    . GLU A 1 12  ? 24.209  5.167   3.339   1.00 27.02  ? -27 GLU A CA    1 
ATOM   89   C  C     . GLU A 1 12  ? 22.971  5.070   2.463   1.00 27.49  ? -27 GLU A C     1 
ATOM   90   O  O     . GLU A 1 12  ? 22.224  6.044   2.301   1.00 20.04  ? -27 GLU A O     1 
ATOM   91   C  CB    . GLU A 1 12  ? 25.455  5.275   2.462   1.00 31.24  ? -27 GLU A CB    1 
ATOM   92   C  CG    . GLU A 1 12  ? 25.465  6.487   1.527   1.00 51.15  ? -27 GLU A CG    1 
ATOM   93   C  CD    . GLU A 1 12  ? 26.732  7.354   1.663   1.00 67.56  ? -27 GLU A CD    1 
ATOM   94   O  OE1   . GLU A 1 12  ? 27.128  7.992   0.659   1.00 51.42  ? -27 GLU A OE1   1 
ATOM   95   O  OE2   . GLU A 1 12  ? 27.331  7.399   2.769   1.00 66.53  ? -27 GLU A OE2   1 
ATOM   96   N  N     . ALA A 1 13  ? 22.741  3.896   1.885   1.00 29.07  ? -26 ALA A N     1 
ATOM   97   C  CA    . ALA A 1 13  ? 21.603  3.724   0.996   1.00 23.20  ? -26 ALA A CA    1 
ATOM   98   C  C     . ALA A 1 13  ? 20.291  3.955   1.729   1.00 16.55  ? -26 ALA A C     1 
ATOM   99   O  O     . ALA A 1 13  ? 19.427  4.694   1.248   1.00 37.18  ? -26 ALA A O     1 
ATOM   100  C  CB    . ALA A 1 13  ? 21.640  2.331   0.367   1.00 24.71  ? -26 ALA A CB    1 
ATOM   101  N  N     . ILE A 1 14  ? 20.116  3.329   2.896   1.00 13.36  ? -25 ILE A N     1 
ATOM   102  C  CA    . ILE A 1 14  ? 18.833  3.446   3.591   1.00 18.38  ? -25 ILE A CA    1 
ATOM   103  C  C     . ILE A 1 14  ? 18.579  4.884   4.051   1.00 12.84  ? -25 ILE A C     1 
ATOM   104  O  O     . ILE A 1 14  ? 17.427  5.322   4.151   1.00 16.08  ? -25 ILE A O     1 
ATOM   105  C  CB    . ILE A 1 14  ? 18.780  2.440   4.760   1.00 13.77  ? -25 ILE A CB    1 
ATOM   106  C  CG1   . ILE A 1 14  ? 18.530  1.026   4.248   1.00 14.05  ? -25 ILE A CG1   1 
ATOM   107  C  CG2   . ILE A 1 14  ? 17.683  2.804   5.750   1.00 18.10  ? -25 ILE A CG2   1 
ATOM   108  C  CD1   . ILE A 1 14  ? 19.156  -0.038  5.114   1.00 21.32  ? -25 ILE A CD1   1 
ATOM   109  N  N     . MET A 1 15  ? 19.635  5.646   4.326   1.00 14.14  ? -24 MET A N     1 
ATOM   110  C  CA    . MET A 1 15  ? 19.435  7.022   4.762   1.00 17.28  ? -24 MET A CA    1 
ATOM   111  C  C     . MET A 1 15  ? 19.039  7.911   3.598   1.00 17.40  ? -24 MET A C     1 
ATOM   112  O  O     . MET A 1 15  ? 18.271  8.861   3.776   1.00 17.79  ? -24 MET A O     1 
ATOM   113  C  CB    . MET A 1 15  ? 20.696  7.564   5.440   1.00 19.59  ? -24 MET A CB    1 
ATOM   114  C  CG    . MET A 1 15  ? 21.081  6.867   6.738   1.00 23.54  ? -24 MET A CG    1 
ATOM   115  S  SD    . MET A 1 15  ? 20.249  7.410   8.247   1.00 33.19  ? -24 MET A SD    1 
ATOM   116  C  CE    . MET A 1 15  ? 21.271  8.767   8.780   1.00 31.48  ? -24 MET A CE    1 
ATOM   117  N  N     . LYS A 1 16  ? 19.538  7.627   2.397   1.00 24.27  ? -23 LYS A N     1 
ATOM   118  C  CA    . LYS A 1 16  ? 19.077  8.412   1.261   1.00 26.68  ? -23 LYS A CA    1 
ATOM   119  C  C     . LYS A 1 16  ? 17.627  8.078   0.923   1.00 18.23  ? -23 LYS A C     1 
ATOM   120  O  O     . LYS A 1 16  ? 16.891  8.956   0.462   1.00 22.18  ? -23 LYS A O     1 
ATOM   121  C  CB    . LYS A 1 16  ? 20.020  8.230   0.058   1.00 26.38  ? -23 LYS A CB    1 
ATOM   122  C  CG    . LYS A 1 16  ? 19.816  9.273   -1.054  1.00 40.84  ? -23 LYS A CG    1 
ATOM   123  C  CD    . LYS A 1 16  ? 19.993  10.716  -0.553  1.00 42.49  ? -23 LYS A CD    1 
ATOM   124  C  CE    . LYS A 1 16  ? 21.455  11.144  -0.404  1.00 49.85  ? -23 LYS A CE    1 
ATOM   125  N  NZ    . LYS A 1 16  ? 21.849  12.131  -1.462  1.00 51.87  ? -23 LYS A NZ    1 
ATOM   126  N  N     . VAL A 1 17  ? 17.183  6.844   1.202   1.00 18.22  ? -22 VAL A N     1 
ATOM   127  C  CA    . VAL A 1 17  ? 15.768  6.491   1.039   1.00 21.36  ? -22 VAL A CA    1 
ATOM   128  C  C     . VAL A 1 17  ? 14.894  7.274   2.021   1.00 26.55  ? -22 VAL A C     1 
ATOM   129  O  O     . VAL A 1 17  ? 13.805  7.748   1.666   1.00 29.21  ? -22 VAL A O     1 
ATOM   130  C  CB    . VAL A 1 17  ? 15.564  4.970   1.213   1.00 26.21  ? -22 VAL A CB    1 
ATOM   131  C  CG1   . VAL A 1 17  ? 14.074  4.635   1.402   1.00 18.58  ? -22 VAL A CG1   1 
ATOM   132  C  CG2   . VAL A 1 17  ? 16.147  4.187   0.039   1.00 15.59  ? -22 VAL A CG2   1 
ATOM   133  N  N     . LEU A 1 18  ? 15.345  7.398   3.277   1.00 21.83  ? -21 LEU A N     1 
ATOM   134  C  CA    . LEU A 1 18  ? 14.576  8.115   4.285   1.00 21.13  ? -21 LEU A CA    1 
ATOM   135  C  C     . LEU A 1 18  ? 14.589  9.608   4.043   1.00 21.75  ? -21 LEU A C     1 
ATOM   136  O  O     . LEU A 1 18  ? 13.642  10.296  4.428   1.00 20.10  ? -21 LEU A O     1 
ATOM   137  C  CB    . LEU A 1 18  ? 15.103  7.830   5.690   1.00 21.00  ? -21 LEU A CB    1 
ATOM   138  C  CG    . LEU A 1 18  ? 15.069  6.391   6.199   1.00 18.84  ? -21 LEU A CG    1 
ATOM   139  C  CD1   . LEU A 1 18  ? 15.943  6.217   7.436   1.00 24.05  ? -21 LEU A CD1   1 
ATOM   140  C  CD2   . LEU A 1 18  ? 13.641  6.032   6.510   1.00 34.95  ? -21 LEU A CD2   1 
ATOM   141  N  N     . GLN A 1 19  ? 15.650  10.130  3.434   1.00 23.91  ? -20 GLN A N     1 
ATOM   142  C  CA    . GLN A 1 19  ? 15.622  11.524  3.016   1.00 23.09  ? -20 GLN A CA    1 
ATOM   143  C  C     . GLN A 1 19  ? 14.612  11.734  1.900   1.00 18.23  ? -20 GLN A C     1 
ATOM   144  O  O     . GLN A 1 19  ? 13.763  12.630  1.974   1.00 25.27  ? -20 GLN A O     1 
ATOM   145  C  CB    . GLN A 1 19  ? 17.004  11.973  2.571   1.00 33.80  ? -20 GLN A CB    1 
ATOM   146  C  CG    . GLN A 1 19  ? 17.159  13.470  2.643   1.00 46.72  ? -20 GLN A CG    1 
ATOM   147  C  CD    . GLN A 1 19  ? 18.366  13.951  1.889   1.00 45.62  ? -20 GLN A CD    1 
ATOM   148  O  OE1   . GLN A 1 19  ? 19.073  13.157  1.270   1.00 35.33  ? -20 GLN A OE1   1 
ATOM   149  N  NE2   . GLN A 1 19  ? 18.618  15.256  1.939   1.00 47.34  ? -20 GLN A NE2   1 
ATOM   150  N  N     . ARG A 1 20  ? 14.682  10.906  0.859   1.00 29.43  ? -19 ARG A N     1 
ATOM   151  C  CA    . ARG A 1 20  ? 13.643  10.909  -0.164  1.00 28.29  ? -19 ARG A CA    1 
ATOM   152  C  C     . ARG A 1 20  ? 12.251  10.873  0.465   1.00 31.42  ? -19 ARG A C     1 
ATOM   153  O  O     . ARG A 1 20  ? 11.347  11.608  0.048   1.00 29.98  ? -19 ARG A O     1 
ATOM   154  C  CB    . ARG A 1 20  ? 13.851  9.721   -1.102  1.00 17.71  ? -19 ARG A CB    1 
ATOM   155  C  CG    . ARG A 1 20  ? 15.062  9.872   -2.020  1.00 11.08  ? -19 ARG A CG    1 
ATOM   156  C  CD    . ARG A 1 20  ? 15.272  8.645   -2.919  1.00 18.22  ? -19 ARG A CD    1 
ATOM   157  N  NE    . ARG A 1 20  ? 14.027  8.061   -3.438  1.00 19.67  ? -19 ARG A NE    1 
ATOM   158  C  CZ    . ARG A 1 20  ? 13.700  6.775   -3.327  1.00 19.46  ? -19 ARG A CZ    1 
ATOM   159  N  NH1   . ARG A 1 20  ? 14.524  5.929   -2.709  1.00 17.56  ? -19 ARG A NH1   1 
ATOM   160  N  NH2   . ARG A 1 20  ? 12.548  6.328   -3.833  1.00 15.05  ? -19 ARG A NH2   1 
ATOM   161  N  N     . ASP A 1 21  ? 12.069  10.048  1.500   1.00 32.98  ? -18 ASP A N     1 
ATOM   162  C  CA    . ASP A 1 21  ? 10.743  9.904   2.090   1.00 24.07  ? -18 ASP A CA    1 
ATOM   163  C  C     . ASP A 1 21  ? 10.336  11.159  2.857   1.00 29.62  ? -18 ASP A C     1 
ATOM   164  O  O     . ASP A 1 21  ? 9.187   11.608  2.758   1.00 28.06  ? -18 ASP A O     1 
ATOM   165  C  CB    . ASP A 1 21  ? 10.713  8.665   2.985   1.00 26.57  ? -18 ASP A CB    1 
ATOM   166  C  CG    . ASP A 1 21  ? 9.418   8.521   3.743   1.00 27.63  ? -18 ASP A CG    1 
ATOM   167  O  OD1   . ASP A 1 21  ? 8.337   8.457   3.108   1.00 29.85  ? -18 ASP A OD1   1 
ATOM   168  O  OD2   . ASP A 1 21  ? 9.480   8.460   4.983   1.00 35.70  ? -18 ASP A OD2   1 
ATOM   169  N  N     . ALA A 1 22  ? 11.264  11.752  3.609   1.00 24.05  ? -17 ALA A N     1 
ATOM   170  C  CA    . ALA A 1 22  ? 10.923  12.938  4.383   1.00 28.56  ? -17 ALA A CA    1 
ATOM   171  C  C     . ALA A 1 22  ? 10.586  14.103  3.472   1.00 27.94  ? -17 ALA A C     1 
ATOM   172  O  O     . ALA A 1 22  ? 9.650   14.862  3.747   1.00 34.52  ? -17 ALA A O     1 
ATOM   173  C  CB    . ALA A 1 22  ? 12.068  13.306  5.332   1.00 32.41  ? -17 ALA A CB    1 
ATOM   174  N  N     . ALA A 1 23  ? 11.342  14.264  2.383   1.00 34.66  ? -16 ALA A N     1 
ATOM   175  C  CA    . ALA A 1 23  ? 11.038  15.323  1.424   1.00 33.89  ? -16 ALA A CA    1 
ATOM   176  C  C     . ALA A 1 23  ? 9.652   15.130  0.825   1.00 36.05  ? -16 ALA A C     1 
ATOM   177  O  O     . ALA A 1 23  ? 8.865   16.078  0.739   1.00 33.91  ? -16 ALA A O     1 
ATOM   178  C  CB    . ALA A 1 23  ? 12.099  15.355  0.327   1.00 36.45  ? -16 ALA A CB    1 
ATOM   179  N  N     . LEU A 1 24  ? 9.335   13.895  0.436   1.00 39.65  ? -15 LEU A N     1 
ATOM   180  C  CA    . LEU A 1 24  ? 8.024   13.574  -0.114  1.00 31.02  ? -15 LEU A CA    1 
ATOM   181  C  C     . LEU A 1 24  ? 6.905   13.943  0.857   1.00 31.09  ? -15 LEU A C     1 
ATOM   182  O  O     . LEU A 1 24  ? 5.917   14.579  0.469   1.00 34.68  ? -15 LEU A O     1 
ATOM   183  C  CB    . LEU A 1 24  ? 7.985   12.084  -0.473  1.00 21.29  ? -15 LEU A CB    1 
ATOM   184  C  CG    . LEU A 1 24  ? 6.672   11.518  -0.995  1.00 19.11  ? -15 LEU A CG    1 
ATOM   185  C  CD1   . LEU A 1 24  ? 6.054   12.476  -1.985  1.00 23.87  ? -15 LEU A CD1   1 
ATOM   186  C  CD2   . LEU A 1 24  ? 6.925   10.214  -1.660  1.00 27.03  ? -15 LEU A CD2   1 
ATOM   187  N  N     . LYS A 1 25  ? 7.034   13.543  2.123   1.00 25.73  ? -14 LYS A N     1 
ATOM   188  C  CA    . LYS A 1 25  ? 6.000   13.876  3.097   1.00 33.14  ? -14 LYS A CA    1 
ATOM   189  C  C     . LYS A 1 25  ? 5.889   15.381  3.284   1.00 38.01  ? -14 LYS A C     1 
ATOM   190  O  O     . LYS A 1 25  ? 4.791   15.915  3.476   1.00 46.75  ? -14 LYS A O     1 
ATOM   191  C  CB    . LYS A 1 25  ? 6.289   13.201  4.440   1.00 31.17  ? -14 LYS A CB    1 
ATOM   192  C  CG    . LYS A 1 25  ? 6.265   11.696  4.387   1.00 31.26  ? -14 LYS A CG    1 
ATOM   193  C  CD    . LYS A 1 25  ? 4.862   11.175  4.148   1.00 38.79  ? -14 LYS A CD    1 
ATOM   194  C  CE    . LYS A 1 25  ? 4.676   9.768   4.709   1.00 34.80  ? -14 LYS A CE    1 
ATOM   195  N  NZ    . LYS A 1 25  ? 5.546   8.767   4.023   1.00 30.98  ? -14 LYS A NZ    1 
ATOM   196  N  N     . ARG A 1 26  ? 7.014   16.088  3.237   1.00 33.22  ? -13 ARG A N     1 
ATOM   197  C  CA    . ARG A 1 26  ? 6.958   17.518  3.506   1.00 39.42  ? -13 ARG A CA    1 
ATOM   198  C  C     . ARG A 1 26  ? 6.261   18.259  2.370   1.00 42.38  ? -13 ARG A C     1 
ATOM   199  O  O     . ARG A 1 26  ? 5.447   19.156  2.614   1.00 46.39  ? -13 ARG A O     1 
ATOM   200  C  CB    . ARG A 1 26  ? 8.363   18.055  3.760   1.00 38.01  ? -13 ARG A CB    1 
ATOM   201  C  CG    . ARG A 1 26  ? 8.876   17.736  5.158   1.00 39.04  ? -13 ARG A CG    1 
ATOM   202  C  CD    . ARG A 1 26  ? 10.020  18.648  5.540   1.00 39.14  ? -13 ARG A CD    1 
ATOM   203  N  NE    . ARG A 1 26  ? 11.305  18.010  5.294   1.00 37.71  ? -13 ARG A NE    1 
ATOM   204  C  CZ    . ARG A 1 26  ? 12.301  17.972  6.169   1.00 40.29  ? -13 ARG A CZ    1 
ATOM   205  N  NH1   . ARG A 1 26  ? 12.173  18.542  7.361   1.00 42.72  ? -13 ARG A NH1   1 
ATOM   206  N  NH2   . ARG A 1 26  ? 13.428  17.359  5.846   1.00 42.27  ? -13 ARG A NH2   1 
ATOM   207  N  N     . ALA A 1 27  ? 6.539   17.870  1.123   1.00 46.32  ? -12 ALA A N     1 
ATOM   208  C  CA    . ALA A 1 27  ? 5.804   18.421  -0.011  1.00 39.99  ? -12 ALA A CA    1 
ATOM   209  C  C     . ALA A 1 27  ? 4.320   18.078  0.065   1.00 49.19  ? -12 ALA A C     1 
ATOM   210  O  O     . ALA A 1 27  ? 3.476   18.883  -0.345  1.00 49.74  ? -12 ALA A O     1 
ATOM   211  C  CB    . ALA A 1 27  ? 6.406   17.910  -1.317  1.00 28.91  ? -12 ALA A CB    1 
ATOM   212  N  N     . GLU A 1 28  ? 3.985   16.895  0.595   1.00 56.90  ? -11 GLU A N     1 
ATOM   213  C  CA    . GLU A 1 28  ? 2.585   16.518  0.795   1.00 52.63  ? -11 GLU A CA    1 
ATOM   214  C  C     . GLU A 1 28  ? 1.903   17.423  1.815   1.00 54.37  ? -11 GLU A C     1 
ATOM   215  O  O     . GLU A 1 28  ? 0.709   17.720  1.697   1.00 58.83  ? -11 GLU A O     1 
ATOM   216  C  CB    . GLU A 1 28  ? 2.499   15.059  1.247   1.00 52.12  ? -11 GLU A CB    1 
ATOM   217  C  CG    . GLU A 1 28  ? 1.198   14.671  1.959   1.00 44.58  ? -11 GLU A CG    1 
ATOM   218  C  CD    . GLU A 1 28  ? 0.116   14.205  0.988   1.00 55.73  ? -11 GLU A CD    1 
ATOM   219  O  OE1   . GLU A 1 28  ? 0.311   14.347  -0.249  1.00 54.41  ? -11 GLU A OE1   1 
ATOM   220  O  OE2   . GLU A 1 28  ? -0.919  13.682  1.468   1.00 46.28  ? -11 GLU A OE2   1 
ATOM   221  N  N     . GLU A 1 29  ? 2.641   17.859  2.834   1.00 55.71  ? -10 GLU A N     1 
ATOM   222  C  CA    . GLU A 1 29  ? 2.072   18.798  3.792   1.00 63.76  ? -10 GLU A CA    1 
ATOM   223  C  C     . GLU A 1 29  ? 1.685   20.112  3.119   1.00 64.61  ? -10 GLU A C     1 
ATOM   224  O  O     . GLU A 1 29  ? 0.675   20.728  3.478   1.00 69.02  ? -10 GLU A O     1 
ATOM   225  C  CB    . GLU A 1 29  ? 3.056   19.042  4.931   1.00 54.92  ? -10 GLU A CB    1 
ATOM   226  C  CG    . GLU A 1 29  ? 2.540   20.000  5.978   1.00 48.86  ? -10 GLU A CG    1 
ATOM   227  C  CD    . GLU A 1 29  ? 2.801   19.502  7.375   1.00 64.95  ? -10 GLU A CD    1 
ATOM   228  O  OE1   . GLU A 1 29  ? 1.823   19.098  8.045   1.00 58.58  ? -10 GLU A OE1   1 
ATOM   229  O  OE2   . GLU A 1 29  ? 3.981   19.508  7.797   1.00 66.76  ? -10 GLU A OE2   1 
ATOM   230  N  N     . GLU A 1 30  ? 2.465   20.549  2.132   1.00 60.96  ? -9  GLU A N     1 
ATOM   231  C  CA    . GLU A 1 30  ? 2.159   21.773  1.390   1.00 64.85  ? -9  GLU A CA    1 
ATOM   232  C  C     . GLU A 1 30  ? 1.104   21.517  0.306   1.00 65.01  ? -9  GLU A C     1 
ATOM   233  O  O     . GLU A 1 30  ? 1.083   22.180  -0.735  1.00 47.01  ? -9  GLU A O     1 
ATOM   234  C  CB    . GLU A 1 30  ? 3.430   22.357  0.759   1.00 51.60  ? -9  GLU A CB    1 
ATOM   235  C  CG    . GLU A 1 30  ? 4.418   22.990  1.751   1.00 58.53  ? -9  GLU A CG    1 
ATOM   236  C  CD    . GLU A 1 30  ? 5.621   22.092  2.072   1.00 67.80  ? -9  GLU A CD    1 
ATOM   237  O  OE1   . GLU A 1 30  ? 5.973   21.948  3.268   1.00 49.53  ? -9  GLU A OE1   1 
ATOM   238  O  OE2   . GLU A 1 30  ? 6.217   21.522  1.128   1.00 65.19  ? -9  GLU A OE2   1 
ATOM   239  N  N     . ASP A 1 45  ? -3.886  13.955  -5.012  1.00 31.23  ? 7   ASP A N     1 
ATOM   240  C  CA    . ASP A 1 45  ? -4.245  14.701  -3.817  1.00 47.28  ? 7   ASP A CA    1 
ATOM   241  C  C     . ASP A 1 45  ? -4.917  13.788  -2.781  1.00 55.31  ? 7   ASP A C     1 
ATOM   242  O  O     . ASP A 1 45  ? -5.877  14.142  -2.089  1.00 54.20  ? 7   ASP A O     1 
ATOM   243  C  CB    . ASP A 1 45  ? -5.112  15.892  -4.194  1.00 46.22  ? 7   ASP A CB    1 
ATOM   244  C  CG    . ASP A 1 45  ? -4.340  16.912  -5.002  1.00 54.88  ? 7   ASP A CG    1 
ATOM   245  O  OD1   . ASP A 1 45  ? -4.629  18.126  -4.895  1.00 54.18  ? 7   ASP A OD1   1 
ATOM   246  O  OD2   . ASP A 1 45  ? -3.417  16.483  -5.733  1.00 56.06  ? 7   ASP A OD2   1 
ATOM   247  N  N     . TYR A 1 46  ? -4.394  12.570  -2.736  1.00 43.61  ? 8   TYR A N     1 
ATOM   248  C  CA    . TYR A 1 46  ? -4.325  11.769  -1.526  1.00 30.65  ? 8   TYR A CA    1 
ATOM   249  C  C     . TYR A 1 46  ? -3.004  11.048  -1.636  1.00 29.00  ? 8   TYR A C     1 
ATOM   250  O  O     . TYR A 1 46  ? -2.775  10.361  -2.635  1.00 30.45  ? 8   TYR A O     1 
ATOM   251  C  CB    . TYR A 1 46  ? -5.457  10.747  -1.400  1.00 39.09  ? 8   TYR A CB    1 
ATOM   252  C  CG    . TYR A 1 46  ? -6.753  11.266  -0.844  1.00 46.97  ? 8   TYR A CG    1 
ATOM   253  C  CD1   . TYR A 1 46  ? -7.873  11.379  -1.652  1.00 44.36  ? 8   TYR A CD1   1 
ATOM   254  C  CD2   . TYR A 1 46  ? -6.868  11.615  0.494   1.00 51.77  ? 8   TYR A CD2   1 
ATOM   255  C  CE1   . TYR A 1 46  ? -9.069  11.840  -1.151  1.00 48.82  ? 8   TYR A CE1   1 
ATOM   256  C  CE2   . TYR A 1 46  ? -8.059  12.080  1.008   1.00 47.99  ? 8   TYR A CE2   1 
ATOM   257  C  CZ    . TYR A 1 46  ? -9.159  12.194  0.181   1.00 56.20  ? 8   TYR A CZ    1 
ATOM   258  O  OH    . TYR A 1 46  ? -10.352 12.662  0.688   1.00 65.11  ? 8   TYR A OH    1 
ATOM   259  N  N     . LEU A 1 47  ? -2.127  11.237  -0.654  1.00 29.74  ? 9   LEU A N     1 
ATOM   260  C  CA    . LEU A 1 47  ? -0.996  10.331  -0.500  1.00 25.27  ? 9   LEU A CA    1 
ATOM   261  C  C     . LEU A 1 47  ? -1.540  9.008   0.009   1.00 21.67  ? 9   LEU A C     1 
ATOM   262  O  O     . LEU A 1 47  ? -2.105  8.943   1.102   1.00 31.81  ? 9   LEU A O     1 
ATOM   263  C  CB    . LEU A 1 47  ? 0.044   10.908  0.454   1.00 23.19  ? 9   LEU A CB    1 
ATOM   264  C  CG    . LEU A 1 47  ? 1.340   10.115  0.627   1.00 20.74  ? 9   LEU A CG    1 
ATOM   265  C  CD1   . LEU A 1 47  ? 1.955   9.778   -0.732  1.00 26.02  ? 9   LEU A CD1   1 
ATOM   266  C  CD2   . LEU A 1 47  ? 2.336   10.894  1.476   1.00 22.26  ? 9   LEU A CD2   1 
ATOM   267  N  N     . ILE A 1 48  ? -1.436  7.967   -0.803  1.00 25.33  ? 10  ILE A N     1 
ATOM   268  C  CA    . ILE A 1 48  ? -1.874  6.623   -0.441  1.00 29.90  ? 10  ILE A CA    1 
ATOM   269  C  C     . ILE A 1 48  ? -0.634  5.762   -0.390  1.00 23.55  ? 10  ILE A C     1 
ATOM   270  O  O     . ILE A 1 48  ? 0.071   5.658   -1.397  1.00 22.60  ? 10  ILE A O     1 
ATOM   271  C  CB    . ILE A 1 48  ? -2.879  6.055   -1.453  1.00 27.62  ? 10  ILE A CB    1 
ATOM   272  C  CG1   . ILE A 1 48  ? -4.164  6.843   -1.373  1.00 24.52  ? 10  ILE A CG1   1 
ATOM   273  C  CG2   . ILE A 1 48  ? -3.166  4.598   -1.154  1.00 19.11  ? 10  ILE A CG2   1 
ATOM   274  C  CD1   . ILE A 1 48  ? -4.545  7.184   0.071   1.00 33.60  ? 10  ILE A CD1   1 
ATOM   275  N  N     . LYS A 1 49  ? -0.361  5.150   0.768   1.00 23.78  ? 11  LYS A N     1 
ATOM   276  C  CA    . LYS A 1 49  ? 0.859   4.370   0.974   1.00 27.70  ? 11  LYS A CA    1 
ATOM   277  C  C     . LYS A 1 49  ? 0.515   2.909   1.233   1.00 23.37  ? 11  LYS A C     1 
ATOM   278  O  O     . LYS A 1 49  ? -0.373  2.612   2.035   1.00 25.86  ? 11  LYS A O     1 
ATOM   279  C  CB    . LYS A 1 49  ? 1.684   4.900   2.164   1.00 20.92  ? 11  LYS A CB    1 
ATOM   280  C  CG    . LYS A 1 49  ? 2.077   6.369   2.115   1.00 21.76  ? 11  LYS A CG    1 
ATOM   281  C  CD    . LYS A 1 49  ? 2.240   6.943   3.528   1.00 26.92  ? 11  LYS A CD    1 
ATOM   282  C  CE    . LYS A 1 49  ? 0.913   7.448   4.111   1.00 41.15  ? 11  LYS A CE    1 
ATOM   283  N  NZ    . LYS A 1 49  ? 0.769   7.388   5.614   1.00 45.80  ? 11  LYS A NZ    1 
ATOM   284  N  N     . PHE A 1 50  ? 1.216   1.994   0.567   1.00 21.36  ? 12  PHE A N     1 
ATOM   285  C  CA    A PHE A 1 50  ? 1.200   0.602   0.991   0.61 20.90  ? 12  PHE A CA    1 
ATOM   286  C  CA    B PHE A 1 50  ? 1.187   0.588   0.938   0.39 21.24  ? 12  PHE A CA    1 
ATOM   287  C  C     . PHE A 1 50  ? 2.602   0.030   0.854   1.00 14.33  ? 12  PHE A C     1 
ATOM   288  O  O     . PHE A 1 50  ? 3.541   0.714   0.445   1.00 19.50  ? 12  PHE A O     1 
ATOM   289  C  CB    A PHE A 1 50  ? 0.159   -0.252  0.245   0.61 24.11  ? 12  PHE A CB    1 
ATOM   290  C  CB    B PHE A 1 50  ? 0.196   -0.207  0.079   0.39 24.05  ? 12  PHE A CB    1 
ATOM   291  C  CG    A PHE A 1 50  ? -0.086  0.133   -1.188  0.61 23.03  ? 12  PHE A CG    1 
ATOM   292  C  CG    B PHE A 1 50  ? 0.463   -0.146  -1.396  0.39 22.97  ? 12  PHE A CG    1 
ATOM   293  C  CD1   A PHE A 1 50  ? 0.906   -0.002  -2.144  0.61 22.71  ? 12  PHE A CD1   1 
ATOM   294  C  CD1   B PHE A 1 50  ? 0.069   0.953   -2.142  0.39 24.55  ? 12  PHE A CD1   1 
ATOM   295  C  CD2   A PHE A 1 50  ? -1.345  0.566   -1.588  0.61 23.64  ? 12  PHE A CD2   1 
ATOM   296  C  CD2   B PHE A 1 50  ? 1.078   -1.206  -2.042  0.39 23.53  ? 12  PHE A CD2   1 
ATOM   297  C  CE1   A PHE A 1 50  ? 0.660   0.329   -3.471  0.61 26.92  ? 12  PHE A CE1   1 
ATOM   298  C  CE1   B PHE A 1 50  ? 0.302   1.001   -3.504  0.39 26.00  ? 12  PHE A CE1   1 
ATOM   299  C  CE2   A PHE A 1 50  ? -1.603  0.892   -2.910  0.61 26.59  ? 12  PHE A CE2   1 
ATOM   300  C  CE2   B PHE A 1 50  ? 1.311   -1.167  -3.401  0.39 23.87  ? 12  PHE A CE2   1 
ATOM   301  C  CZ    A PHE A 1 50  ? -0.601  0.776   -3.855  0.61 24.46  ? 12  PHE A CZ    1 
ATOM   302  C  CZ    B PHE A 1 50  ? 0.919   -0.066  -4.134  0.39 24.91  ? 12  PHE A CZ    1 
ATOM   303  N  N     . LEU A 1 51  ? 2.749   -1.224  1.255   1.00 19.70  ? 13  LEU A N     1 
ATOM   304  C  CA    . LEU A 1 51  ? 4.055   -1.835  1.438   1.00 11.79  ? 13  LEU A CA    1 
ATOM   305  C  C     . LEU A 1 51  ? 4.039   -3.258  0.902   1.00 18.68  ? 13  LEU A C     1 
ATOM   306  O  O     . LEU A 1 51  ? 3.103   -4.016  1.180   1.00 18.57  ? 13  LEU A O     1 
ATOM   307  C  CB    . LEU A 1 51  ? 4.431   -1.830  2.924   1.00 15.08  ? 13  LEU A CB    1 
ATOM   308  C  CG    . LEU A 1 51  ? 5.727   -2.424  3.449   1.00 16.17  ? 13  LEU A CG    1 
ATOM   309  C  CD1   . LEU A 1 51  ? 6.115   -1.603  4.688   1.00 14.89  ? 13  LEU A CD1   1 
ATOM   310  C  CD2   . LEU A 1 51  ? 5.523   -3.890  3.821   1.00 12.56  ? 13  LEU A CD2   1 
ATOM   311  N  N     . ALA A 1 52  ? 5.074   -3.604  0.131   1.00 14.51  ? 14  ALA A N     1 
ATOM   312  C  CA    . ALA A 1 52  ? 5.289   -4.963  -0.338  1.00 21.06  ? 14  ALA A CA    1 
ATOM   313  C  C     . ALA A 1 52  ? 6.081   -5.736  0.703   1.00 18.04  ? 14  ALA A C     1 
ATOM   314  O  O     . ALA A 1 52  ? 6.996   -5.197  1.326   1.00 18.68  ? 14  ALA A O     1 
ATOM   315  C  CB    . ALA A 1 52  ? 6.052   -4.972  -1.666  1.00 11.40  ? 14  ALA A CB    1 
ATOM   316  N  N     . LEU A 1 53  ? 5.742   -7.006  0.877   1.00 17.95  ? 15  LEU A N     1 
ATOM   317  C  CA    . LEU A 1 53  ? 6.425   -7.802  1.887   1.00 17.52  ? 15  LEU A CA    1 
ATOM   318  C  C     . LEU A 1 53  ? 6.249   -9.276  1.548   1.00 13.54  ? 15  LEU A C     1 
ATOM   319  O  O     . LEU A 1 53  ? 5.372   -9.654  0.771   1.00 12.31  ? 15  LEU A O     1 
ATOM   320  C  CB    . LEU A 1 53  ? 5.902   -7.487  3.289   1.00 20.76  ? 15  LEU A CB    1 
ATOM   321  C  CG    . LEU A 1 53  ? 4.623   -8.158  3.771   1.00 14.02  ? 15  LEU A CG    1 
ATOM   322  C  CD1   . LEU A 1 53  ? 4.652   -8.031  5.287   1.00 16.20  ? 15  LEU A CD1   1 
ATOM   323  C  CD2   . LEU A 1 53  ? 3.337   -7.600  3.175   1.00 22.99  ? 15  LEU A CD2   1 
ATOM   324  N  N     . GLY A 1 54  ? 7.092   -10.095 2.138   1.00 13.23  ? 16  GLY A N     1 
ATOM   325  C  CA    . GLY A 1 54  ? 7.162   -11.499 1.781   1.00 17.14  ? 16  GLY A CA    1 
ATOM   326  C  C     . GLY A 1 54  ? 8.591   -11.994 1.866   1.00 16.95  ? 16  GLY A C     1 
ATOM   327  O  O     . GLY A 1 54  ? 9.517   -11.244 2.163   1.00 26.48  ? 16  GLY A O     1 
ATOM   328  N  N     . ASP A 1 55  ? 8.749   -13.295 1.622   1.00 20.41  ? 17  ASP A N     1 
ATOM   329  C  CA    . ASP A 1 55  ? 10.067  -13.911 1.706   1.00 20.30  ? 17  ASP A CA    1 
ATOM   330  C  C     . ASP A 1 55  ? 11.014  -13.271 0.684   1.00 22.20  ? 17  ASP A C     1 
ATOM   331  O  O     . ASP A 1 55  ? 10.595  -12.594 -0.254  1.00 16.95  ? 17  ASP A O     1 
ATOM   332  C  CB    . ASP A 1 55  ? 9.981   -15.423 1.455   1.00 20.57  ? 17  ASP A CB    1 
ATOM   333  C  CG    . ASP A 1 55  ? 9.716   -16.249 2.731   1.00 22.80  ? 17  ASP A CG    1 
ATOM   334  O  OD1   . ASP A 1 55  ? 9.530   -15.698 3.835   1.00 17.51  ? 17  ASP A OD1   1 
ATOM   335  O  OD2   . ASP A 1 55  ? 9.695   -17.490 2.617   1.00 21.29  ? 17  ASP A OD2   1 
ATOM   336  N  N     . SER A 1 56  ? 12.311  -13.474 0.879   1.00 15.77  ? 18  SER A N     1 
ATOM   337  C  CA    . SER A 1 56  ? 13.272  -12.896 -0.041  1.00 17.81  ? 18  SER A CA    1 
ATOM   338  C  C     . SER A 1 56  ? 13.370  -13.756 -1.300  1.00 22.22  ? 18  SER A C     1 
ATOM   339  O  O     . SER A 1 56  ? 13.370  -14.994 -1.237  1.00 15.64  ? 18  SER A O     1 
ATOM   340  C  CB    . SER A 1 56  ? 14.646  -12.752 0.614   1.00 16.51  ? 18  SER A CB    1 
ATOM   341  O  OG    . SER A 1 56  ? 15.673  -12.837 -0.364  1.00 18.27  ? 18  SER A OG    1 
ATOM   342  N  N     . GLY A 1 57  ? 13.459  -13.087 -2.449  1.00 16.30  ? 19  GLY A N     1 
ATOM   343  C  CA    . GLY A 1 57  ? 13.501  -13.760 -3.728  1.00 17.92  ? 19  GLY A CA    1 
ATOM   344  C  C     . GLY A 1 57  ? 12.148  -14.093 -4.317  1.00 15.17  ? 19  GLY A C     1 
ATOM   345  O  O     . GLY A 1 57  ? 12.097  -14.776 -5.341  1.00 27.91  ? 19  GLY A O     1 
ATOM   346  N  N     . VAL A 1 58  ? 11.049  -13.640 -3.707  1.00 21.59  ? 20  VAL A N     1 
ATOM   347  C  CA    . VAL A 1 58  ? 9.719   -13.951 -4.221  1.00 11.84  ? 20  VAL A CA    1 
ATOM   348  C  C     . VAL A 1 58  ? 9.249   -12.933 -5.256  1.00 19.44  ? 20  VAL A C     1 
ATOM   349  O  O     . VAL A 1 58  ? 8.292   -13.213 -5.992  1.00 11.77  ? 20  VAL A O     1 
ATOM   350  C  CB    . VAL A 1 58  ? 8.672   -14.071 -3.088  1.00 15.00  ? 20  VAL A CB    1 
ATOM   351  C  CG1   . VAL A 1 58  ? 9.097   -15.050 -2.059  1.00 14.65  ? 20  VAL A CG1   1 
ATOM   352  C  CG2   . VAL A 1 58  ? 8.371   -12.742 -2.444  1.00 10.23  ? 20  VAL A CG2   1 
ATOM   353  N  N     . GLY A 1 59  ? 9.878   -11.756 -5.326  1.00 16.78  ? 21  GLY A N     1 
ATOM   354  C  CA    . GLY A 1 59  ? 9.590   -10.835 -6.407  1.00 13.70  ? 21  GLY A CA    1 
ATOM   355  C  C     . GLY A 1 59  ? 8.974   -9.507  -6.018  1.00 15.95  ? 21  GLY A C     1 
ATOM   356  O  O     . GLY A 1 59  ? 8.150   -8.963  -6.757  1.00 15.34  ? 21  GLY A O     1 
ATOM   357  N  N     . LYS A 1 60  ? 9.377   -8.952  -4.878  1.00 13.24  ? 22  LYS A N     1 
ATOM   358  C  CA    . LYS A 1 60  ? 8.783   -7.706  -4.412  1.00 8.55   ? 22  LYS A CA    1 
ATOM   359  C  C     . LYS A 1 60  ? 9.251   -6.524  -5.250  1.00 10.93  ? 22  LYS A C     1 
ATOM   360  O  O     . LYS A 1 60  ? 8.437   -5.748  -5.766  1.00 19.00  ? 22  LYS A O     1 
ATOM   361  C  CB    . LYS A 1 60  ? 9.130   -7.486  -2.935  1.00 16.64  ? 22  LYS A CB    1 
ATOM   362  C  CG    . LYS A 1 60  ? 8.379   -8.371  -1.978  1.00 18.58  ? 22  LYS A CG    1 
ATOM   363  C  CD    . LYS A 1 60  ? 8.835   -8.131  -0.543  1.00 19.56  ? 22  LYS A CD    1 
ATOM   364  C  CE    . LYS A 1 60  ? 10.086  -8.907  -0.192  1.00 12.31  ? 22  LYS A CE    1 
ATOM   365  N  NZ    . LYS A 1 60  ? 10.220  -10.020 -1.143  1.00 16.82  ? 22  LYS A NZ    1 
ATOM   366  N  N     . THR A 1 61  ? 10.566  -6.348  -5.368  1.00 12.26  ? 23  THR A N     1 
ATOM   367  C  CA    . THR A 1 61  ? 11.106  -5.274  -6.197  1.00 14.00  ? 23  THR A CA    1 
ATOM   368  C  C     . THR A 1 61  ? 10.625  -5.392  -7.648  1.00 21.51  ? 23  THR A C     1 
ATOM   369  O  O     . THR A 1 61  ? 10.200  -4.399  -8.256  1.00 20.73  ? 23  THR A O     1 
ATOM   370  C  CB    . THR A 1 61  ? 12.634  -5.294  -6.120  1.00 16.57  ? 23  THR A CB    1 
ATOM   371  O  OG1   . THR A 1 61  ? 13.048  -5.329  -4.740  1.00 22.25  ? 23  THR A OG1   1 
ATOM   372  C  CG2   . THR A 1 61  ? 13.229  -4.077  -6.789  1.00 14.49  ? 23  THR A CG2   1 
ATOM   373  N  N     . SER A 1 62  ? 10.670  -6.603  -8.221  1.00 19.12  ? 24  SER A N     1 
ATOM   374  C  CA    . SER A 1 62  ? 10.298  -6.760  -9.626  1.00 14.61  ? 24  SER A CA    1 
ATOM   375  C  C     . SER A 1 62  ? 8.834   -6.408  -9.858  1.00 17.93  ? 24  SER A C     1 
ATOM   376  O  O     . SER A 1 62  ? 8.487   -5.765  -10.860 1.00 13.39  ? 24  SER A O     1 
ATOM   377  C  CB    . SER A 1 62  ? 10.581  -8.186  -10.085 1.00 11.23  ? 24  SER A CB    1 
ATOM   378  O  OG    . SER A 1 62  ? 11.914  -8.551  -9.789  1.00 15.13  ? 24  SER A OG    1 
ATOM   379  N  N     . VAL A 1 63  ? 7.957   -6.827  -8.942  1.00 20.75  ? 25  VAL A N     1 
ATOM   380  C  CA    . VAL A 1 63  ? 6.530   -6.583  -9.127  1.00 16.19  ? 25  VAL A CA    1 
ATOM   381  C  C     . VAL A 1 63  ? 6.236   -5.088  -9.122  1.00 18.47  ? 25  VAL A C     1 
ATOM   382  O  O     . VAL A 1 63  ? 5.401   -4.604  -9.898  1.00 19.94  ? 25  VAL A O     1 
ATOM   383  C  CB    . VAL A 1 63  ? 5.712   -7.339  -8.063  1.00 11.90  ? 25  VAL A CB    1 
ATOM   384  C  CG1   . VAL A 1 63  ? 4.366   -6.710  -7.901  1.00 8.21   ? 25  VAL A CG1   1 
ATOM   385  C  CG2   . VAL A 1 63  ? 5.565   -8.803  -8.465  1.00 11.21  ? 25  VAL A CG2   1 
ATOM   386  N  N     . LEU A 1 64  ? 6.948   -4.327  -8.290  1.00 15.49  ? 26  LEU A N     1 
ATOM   387  C  CA    . LEU A 1 64  ? 6.722   -2.884  -8.232  1.00 20.37  ? 26  LEU A CA    1 
ATOM   388  C  C     . LEU A 1 64  ? 7.320   -2.168  -9.447  1.00 16.33  ? 26  LEU A C     1 
ATOM   389  O  O     . LEU A 1 64  ? 6.743   -1.205  -9.956  1.00 15.82  ? 26  LEU A O     1 
ATOM   390  C  CB    . LEU A 1 64  ? 7.298   -2.321  -6.929  1.00 9.99   ? 26  LEU A CB    1 
ATOM   391  C  CG    . LEU A 1 64  ? 6.644   -2.751  -5.610  1.00 22.54  ? 26  LEU A CG    1 
ATOM   392  C  CD1   . LEU A 1 64  ? 7.307   -2.064  -4.444  1.00 14.68  ? 26  LEU A CD1   1 
ATOM   393  C  CD2   . LEU A 1 64  ? 5.144   -2.483  -5.572  1.00 19.07  ? 26  LEU A CD2   1 
ATOM   394  N  N     . TYR A 1 65  ? 8.484   -2.615  -9.909  1.00 17.43  ? 27  TYR A N     1 
ATOM   395  C  CA    . TYR A 1 65  ? 9.099   -2.063  -11.118 1.00 14.08  ? 27  TYR A CA    1 
ATOM   396  C  C     . TYR A 1 65  ? 8.276   -2.373  -12.370 1.00 20.89  ? 27  TYR A C     1 
ATOM   397  O  O     . TYR A 1 65  ? 8.244   -1.576  -13.317 1.00 15.39  ? 27  TYR A O     1 
ATOM   398  C  CB    . TYR A 1 65  ? 10.502  -2.649  -11.245 1.00 18.98  ? 27  TYR A CB    1 
ATOM   399  C  CG    . TYR A 1 65  ? 11.422  -2.007  -12.227 1.00 20.75  ? 27  TYR A CG    1 
ATOM   400  C  CD1   . TYR A 1 65  ? 11.617  -0.640  -12.238 1.00 19.37  ? 27  TYR A CD1   1 
ATOM   401  C  CD2   . TYR A 1 65  ? 12.146  -2.790  -13.122 1.00 14.33  ? 27  TYR A CD2   1 
ATOM   402  C  CE1   . TYR A 1 65  ? 12.499  -0.066  -13.135 1.00 19.03  ? 27  TYR A CE1   1 
ATOM   403  C  CE2   . TYR A 1 65  ? 13.027  -2.233  -14.002 1.00 17.01  ? 27  TYR A CE2   1 
ATOM   404  C  CZ    . TYR A 1 65  ? 13.201  -0.873  -14.016 1.00 18.21  ? 27  TYR A CZ    1 
ATOM   405  O  OH    . TYR A 1 65  ? 14.073  -0.318  -14.928 1.00 9.17   ? 27  TYR A OH    1 
ATOM   406  N  N     . GLN A 1 66  ? 7.643   -3.550  -12.423 1.00 11.26  ? 28  GLN A N     1 
ATOM   407  C  CA    . GLN A 1 66  ? 6.735   -3.804  -13.530 1.00 14.12  ? 28  GLN A CA    1 
ATOM   408  C  C     . GLN A 1 66  ? 5.576   -2.822  -13.485 1.00 16.31  ? 28  GLN A C     1 
ATOM   409  O  O     . GLN A 1 66  ? 5.210   -2.237  -14.511 1.00 16.96  ? 28  GLN A O     1 
ATOM   410  C  CB    . GLN A 1 66  ? 6.251   -5.259  -13.506 1.00 10.82  ? 28  GLN A CB    1 
ATOM   411  C  CG    . GLN A 1 66  ? 5.322   -5.664  -14.654 1.00 16.99  ? 28  GLN A CG    1 
ATOM   412  C  CD    . GLN A 1 66  ? 5.967   -5.612  -16.039 1.00 21.62  ? 28  GLN A CD    1 
ATOM   413  O  OE1   . GLN A 1 66  ? 5.540   -4.842  -16.893 1.00 26.02  ? 28  GLN A OE1   1 
ATOM   414  N  NE2   . GLN A 1 66  ? 6.993   -6.423  -16.261 1.00 14.82  ? 28  GLN A NE2   1 
ATOM   415  N  N     . TYR A 1 67  ? 5.040   -2.566  -12.287 1.00 18.99  ? 29  TYR A N     1 
ATOM   416  C  CA    . TYR A 1 67  ? 3.913   -1.645  -12.156 1.00 16.29  ? 29  TYR A CA    1 
ATOM   417  C  C     . TYR A 1 67  ? 4.300   -0.226  -12.560 1.00 16.46  ? 29  TYR A C     1 
ATOM   418  O  O     . TYR A 1 67  ? 3.611   0.401   -13.370 1.00 17.76  ? 29  TYR A O     1 
ATOM   419  C  CB    . TYR A 1 67  ? 3.370   -1.666  -10.726 1.00 19.23  ? 29  TYR A CB    1 
ATOM   420  C  CG    . TYR A 1 67  ? 2.093   -0.863  -10.521 1.00 23.78  ? 29  TYR A CG    1 
ATOM   421  C  CD1   . TYR A 1 67  ? 0.913   -1.179  -11.200 1.00 18.12  ? 29  TYR A CD1   1 
ATOM   422  C  CD2   . TYR A 1 67  ? 2.068   0.201   -9.631  1.00 14.16  ? 29  TYR A CD2   1 
ATOM   423  C  CE1   . TYR A 1 67  ? -0.256  -0.446  -10.993 1.00 14.12  ? 29  TYR A CE1   1 
ATOM   424  C  CE2   . TYR A 1 67  ? 0.916   0.931   -9.412  1.00 15.80  ? 29  TYR A CE2   1 
ATOM   425  C  CZ    . TYR A 1 67  ? -0.238  0.615   -10.088 1.00 21.61  ? 29  TYR A CZ    1 
ATOM   426  O  OH    . TYR A 1 67  ? -1.359  1.381   -9.842  1.00 15.99  ? 29  TYR A OH    1 
ATOM   427  N  N     . THR A 1 68  ? 5.395   0.310   -12.008 1.00 14.38  ? 30  THR A N     1 
ATOM   428  C  CA    . THR A 1 68  ? 5.678   1.713   -12.285 1.00 10.52  ? 30  THR A CA    1 
ATOM   429  C  C     . THR A 1 68  ? 6.273   1.920   -13.680 1.00 19.52  ? 30  THR A C     1 
ATOM   430  O  O     . THR A 1 68  ? 5.844   2.832   -14.394 1.00 26.68  ? 30  THR A O     1 
ATOM   431  C  CB    . THR A 1 68  ? 6.582   2.316   -11.216 1.00 14.94  ? 30  THR A CB    1 
ATOM   432  O  OG1   . THR A 1 68  ? 7.844   1.647   -11.210 1.00 17.58  ? 30  THR A OG1   1 
ATOM   433  C  CG2   . THR A 1 68  ? 5.931   2.217   -9.847  1.00 13.43  ? 30  THR A CG2   1 
ATOM   434  N  N     . ASP A 1 69  ? 7.236   1.081   -14.107 1.00 16.76  ? 31  ASP A N     1 
ATOM   435  C  CA    . ASP A 1 69  ? 8.021   1.354   -15.314 1.00 17.31  ? 31  ASP A CA    1 
ATOM   436  C  C     . ASP A 1 69  ? 7.821   0.366   -16.463 1.00 21.47  ? 31  ASP A C     1 
ATOM   437  O  O     . ASP A 1 69  ? 8.386   0.585   -17.548 1.00 20.50  ? 31  ASP A O     1 
ATOM   438  C  CB    . ASP A 1 69  ? 9.521   1.396   -14.990 1.00 12.61  ? 31  ASP A CB    1 
ATOM   439  C  CG    . ASP A 1 69  ? 9.891   2.547   -14.086 1.00 19.26  ? 31  ASP A CG    1 
ATOM   440  O  OD1   . ASP A 1 69  ? 9.167   2.776   -13.095 1.00 21.70  ? 31  ASP A OD1   1 
ATOM   441  O  OD2   . ASP A 1 69  ? 10.913  3.222   -14.359 1.00 22.14  ? 31  ASP A OD2   1 
ATOM   442  N  N     . GLY A 1 70  ? 7.062   -0.708  -16.264 1.00 13.98  ? 32  GLY A N     1 
ATOM   443  C  CA    . GLY A 1 70  ? 6.816   -1.673  -17.313 1.00 8.56   ? 32  GLY A CA    1 
ATOM   444  C  C     . GLY A 1 70  ? 8.005   -2.499  -17.744 1.00 15.87  ? 32  GLY A C     1 
ATOM   445  O  O     . GLY A 1 70  ? 7.937   -3.153  -18.780 1.00 24.38  ? 32  GLY A O     1 
ATOM   446  N  N     . LYS A 1 71  ? 9.089   -2.512  -16.985 1.00 20.80  ? 33  LYS A N     1 
ATOM   447  C  CA    . LYS A 1 71  ? 10.279  -3.253  -17.367 1.00 20.03  ? 33  LYS A CA    1 
ATOM   448  C  C     . LYS A 1 71  ? 10.551  -4.336  -16.337 1.00 16.33  ? 33  LYS A C     1 
ATOM   449  O  O     . LYS A 1 71  ? 9.926   -4.392  -15.283 1.00 17.70  ? 33  LYS A O     1 
ATOM   450  C  CB    . LYS A 1 71  ? 11.476  -2.313  -17.522 1.00 17.57  ? 33  LYS A CB    1 
ATOM   451  C  CG    . LYS A 1 71  ? 11.139  -1.118  -18.408 1.00 14.18  ? 33  LYS A CG    1 
ATOM   452  C  CD    . LYS A 1 71  ? 12.110  0.009   -18.190 1.00 16.94  ? 33  LYS A CD    1 
ATOM   453  C  CE    . LYS A 1 71  ? 12.227  0.871   -19.427 1.00 22.34  ? 33  LYS A CE    1 
ATOM   454  N  NZ    . LYS A 1 71  ? 13.439  1.714   -19.279 1.00 32.01  ? 33  LYS A NZ    1 
ATOM   455  N  N     . PHE A 1 72  ? 11.480  -5.223  -16.661 1.00 16.91  ? 34  PHE A N     1 
ATOM   456  C  CA    . PHE A 1 72  ? 11.788  -6.331  -15.777 1.00 17.35  ? 34  PHE A CA    1 
ATOM   457  C  C     . PHE A 1 72  ? 13.242  -6.721  -15.965 1.00 22.21  ? 34  PHE A C     1 
ATOM   458  O  O     . PHE A 1 72  ? 13.707  -6.882  -17.097 1.00 20.39  ? 34  PHE A O     1 
ATOM   459  C  CB    . PHE A 1 72  ? 10.878  -7.528  -16.045 1.00 16.02  ? 34  PHE A CB    1 
ATOM   460  C  CG    . PHE A 1 72  ? 11.320  -8.790  -15.367 1.00 15.83  ? 34  PHE A CG    1 
ATOM   461  C  CD1   . PHE A 1 72  ? 11.034  -9.013  -14.029 1.00 15.18  ? 34  PHE A CD1   1 
ATOM   462  C  CD2   . PHE A 1 72  ? 12.004  -9.765  -16.072 1.00 15.80  ? 34  PHE A CD2   1 
ATOM   463  C  CE1   . PHE A 1 72  ? 11.415  -10.185 -13.407 1.00 13.78  ? 34  PHE A CE1   1 
ATOM   464  C  CE2   . PHE A 1 72  ? 12.396  -10.936 -15.463 1.00 11.83  ? 34  PHE A CE2   1 
ATOM   465  C  CZ    . PHE A 1 72  ? 12.104  -11.151 -14.123 1.00 18.76  ? 34  PHE A CZ    1 
ATOM   466  N  N     . ASN A 1 73  ? 13.929  -6.901  -14.845 1.00 19.84  ? 35  ASN A N     1 
ATOM   467  C  CA    . ASN A 1 73  ? 15.359  -7.150  -14.777 1.00 16.90  ? 35  ASN A CA    1 
ATOM   468  C  C     . ASN A 1 73  ? 15.555  -8.586  -14.315 1.00 13.79  ? 35  ASN A C     1 
ATOM   469  O  O     . ASN A 1 73  ? 15.013  -8.989  -13.287 1.00 26.19  ? 35  ASN A O     1 
ATOM   470  C  CB    . ASN A 1 73  ? 15.991  -6.155  -13.806 1.00 25.84  ? 35  ASN A CB    1 
ATOM   471  C  CG    . ASN A 1 73  ? 17.477  -6.054  -13.942 1.00 44.05  ? 35  ASN A CG    1 
ATOM   472  O  OD1   . ASN A 1 73  ? 18.224  -6.275  -12.974 1.00 50.49  ? 35  ASN A OD1   1 
ATOM   473  N  ND2   . ASN A 1 73  ? 17.932  -5.690  -15.137 1.00 31.61  ? 35  ASN A ND2   1 
ATOM   474  N  N     . SER A 1 74  ? 16.294  -9.369  -15.080 1.00 24.38  ? 36  SER A N     1 
ATOM   475  C  CA    . SER A 1 74  ? 16.482  -10.758 -14.691 1.00 18.34  ? 36  SER A CA    1 
ATOM   476  C  C     . SER A 1 74  ? 17.505  -10.887 -13.567 1.00 25.20  ? 36  SER A C     1 
ATOM   477  O  O     . SER A 1 74  ? 17.453  -11.842 -12.788 1.00 28.33  ? 36  SER A O     1 
ATOM   478  C  CB    . SER A 1 74  ? 16.919  -11.580 -15.907 1.00 14.55  ? 36  SER A CB    1 
ATOM   479  O  OG    . SER A 1 74  ? 15.793  -12.099 -16.599 1.00 25.02  ? 36  SER A OG    1 
ATOM   480  N  N     . LYS A 1 75  ? 18.458  -9.965  -13.488 1.00 24.42  ? 37  LYS A N     1 
ATOM   481  C  CA    . LYS A 1 75  ? 19.490  -10.056 -12.470 1.00 18.85  ? 37  LYS A CA    1 
ATOM   482  C  C     . LYS A 1 75  ? 18.894  -9.788  -11.086 1.00 19.82  ? 37  LYS A C     1 
ATOM   483  O  O     . LYS A 1 75  ? 18.250  -8.758  -10.867 1.00 20.15  ? 37  LYS A O     1 
ATOM   484  C  CB    . LYS A 1 75  ? 20.614  -9.069  -12.779 1.00 16.08  ? 37  LYS A CB    1 
ATOM   485  C  CG    . LYS A 1 75  ? 21.889  -9.310  -11.974 1.00 29.60  ? 37  LYS A CG    1 
ATOM   486  C  CD    . LYS A 1 75  ? 23.069  -8.483  -12.485 1.00 36.96  ? 37  LYS A CD    1 
ATOM   487  C  CE    . LYS A 1 75  ? 23.115  -7.092  -11.851 1.00 43.83  ? 37  LYS A CE    1 
ATOM   488  N  NZ    . LYS A 1 75  ? 23.158  -7.142  -10.357 1.00 40.98  ? 37  LYS A NZ    1 
ATOM   489  N  N     . PHE A 1 76  ? 19.104  -10.731 -10.162 1.00 18.12  ? 38  PHE A N     1 
ATOM   490  C  CA    . PHE A 1 76  ? 18.716  -10.572 -8.760  1.00 17.10  ? 38  PHE A CA    1 
ATOM   491  C  C     . PHE A 1 76  ? 19.582  -9.504  -8.125  1.00 23.45  ? 38  PHE A C     1 
ATOM   492  O  O     . PHE A 1 76  ? 20.815  -9.606  -8.137  1.00 16.92  ? 38  PHE A O     1 
ATOM   493  C  CB    . PHE A 1 76  ? 18.871  -11.901 -8.025  1.00 13.22  ? 38  PHE A CB    1 
ATOM   494  C  CG    . PHE A 1 76  ? 18.442  -11.888 -6.566  1.00 25.35  ? 38  PHE A CG    1 
ATOM   495  C  CD1   . PHE A 1 76  ? 17.462  -11.037 -6.095  1.00 20.31  ? 38  PHE A CD1   1 
ATOM   496  C  CD2   . PHE A 1 76  ? 19.042  -12.772 -5.657  1.00 27.13  ? 38  PHE A CD2   1 
ATOM   497  C  CE1   . PHE A 1 76  ? 17.091  -11.061 -4.732  1.00 19.01  ? 38  PHE A CE1   1 
ATOM   498  C  CE2   . PHE A 1 76  ? 18.672  -12.813 -4.318  1.00 12.57  ? 38  PHE A CE2   1 
ATOM   499  C  CZ    . PHE A 1 76  ? 17.693  -11.955 -3.855  1.00 13.01  ? 38  PHE A CZ    1 
ATOM   500  N  N     . ILE A 1 77  ? 18.940  -8.452  -7.630  1.00 11.99  ? 39  ILE A N     1 
ATOM   501  C  CA    . ILE A 1 77  ? 19.611  -7.404  -6.881  1.00 18.17  ? 39  ILE A CA    1 
ATOM   502  C  C     . ILE A 1 77  ? 18.810  -7.244  -5.604  1.00 15.91  ? 39  ILE A C     1 
ATOM   503  O  O     . ILE A 1 77  ? 17.774  -6.571  -5.586  1.00 14.45  ? 39  ILE A O     1 
ATOM   504  C  CB    . ILE A 1 77  ? 19.705  -6.087  -7.640  1.00 22.74  ? 39  ILE A CB    1 
ATOM   505  C  CG1   . ILE A 1 77  ? 20.661  -6.239  -8.821  1.00 30.15  ? 39  ILE A CG1   1 
ATOM   506  C  CG2   . ILE A 1 77  ? 20.192  -5.021  -6.705  1.00 15.44  ? 39  ILE A CG2   1 
ATOM   507  C  CD1   . ILE A 1 77  ? 20.158  -5.599  -10.107 1.00 31.16  ? 39  ILE A CD1   1 
ATOM   508  N  N     . THR A 1 78  ? 19.273  -7.875  -4.541  1.00 16.89  ? 40  THR A N     1 
ATOM   509  C  CA    . THR A 1 78  ? 18.479  -7.929  -3.327  1.00 21.99  ? 40  THR A CA    1 
ATOM   510  C  C     . THR A 1 78  ? 18.373  -6.552  -2.670  1.00 11.02  ? 40  THR A C     1 
ATOM   511  O  O     . THR A 1 78  ? 19.289  -5.726  -2.725  1.00 19.65  ? 40  THR A O     1 
ATOM   512  C  CB    . THR A 1 78  ? 19.072  -8.968  -2.380  1.00 11.83  ? 40  THR A CB    1 
ATOM   513  O  OG1   . THR A 1 78  ? 18.069  -9.391  -1.449  1.00 14.98  ? 40  THR A OG1   1 
ATOM   514  C  CG2   . THR A 1 78  ? 20.344  -8.462  -1.695  1.00 8.98   ? 40  THR A CG2   1 
ATOM   515  N  N     . THR A 1 79  ? 17.232  -6.309  -2.048  1.00 14.84  ? 41  THR A N     1 
ATOM   516  C  CA    . THR A 1 79  ? 16.945  -4.987  -1.503  1.00 15.27  ? 41  THR A CA    1 
ATOM   517  C  C     . THR A 1 79  ? 17.747  -4.714  -0.233  1.00 21.35  ? 41  THR A C     1 
ATOM   518  O  O     . THR A 1 79  ? 17.604  -5.414  0.781   1.00 19.54  ? 41  THR A O     1 
ATOM   519  C  CB    . THR A 1 79  ? 15.455  -4.856  -1.235  1.00 19.95  ? 41  THR A CB    1 
ATOM   520  O  OG1   . THR A 1 79  ? 14.754  -4.935  -2.483  1.00 20.00  ? 41  THR A OG1   1 
ATOM   521  C  CG2   . THR A 1 79  ? 15.155  -3.532  -0.528  1.00 18.51  ? 41  THR A CG2   1 
ATOM   522  N  N     . VAL A 1 80  ? 18.592  -3.690  -0.292  1.00 10.86  ? 42  VAL A N     1 
ATOM   523  C  CA    . VAL A 1 80  ? 19.261  -3.152  0.880   1.00 16.30  ? 42  VAL A CA    1 
ATOM   524  C  C     . VAL A 1 80  ? 18.243  -2.574  1.852   1.00 20.34  ? 42  VAL A C     1 
ATOM   525  O  O     . VAL A 1 80  ? 18.120  -1.348  1.975   1.00 23.49  ? 42  VAL A O     1 
ATOM   526  C  CB    . VAL A 1 80  ? 20.275  -2.076  0.474   1.00 19.89  ? 42  VAL A CB    1 
ATOM   527  C  CG1   . VAL A 1 80  ? 21.148  -1.651  1.682   1.00 21.16  ? 42  VAL A CG1   1 
ATOM   528  C  CG2   . VAL A 1 80  ? 21.110  -2.582  -0.683  1.00 9.43   ? 42  VAL A CG2   1 
ATOM   529  N  N     . GLY A 1 81  ? 17.500  -3.444  2.534   1.00 16.52  ? 43  GLY A N     1 
ATOM   530  C  CA    . GLY A 1 81  ? 16.630  -3.004  3.609   1.00 19.99  ? 43  GLY A CA    1 
ATOM   531  C  C     . GLY A 1 81  ? 15.296  -2.406  3.228   1.00 16.16  ? 43  GLY A C     1 
ATOM   532  O  O     . GLY A 1 81  ? 14.251  -3.013  3.457   1.00 25.09  ? 43  GLY A O     1 
ATOM   533  N  N     . ILE A 1 82  ? 15.308  -1.213  2.657   1.00 19.24  ? 44  ILE A N     1 
ATOM   534  C  CA    . ILE A 1 82  ? 14.073  -0.486  2.410   1.00 17.16  ? 44  ILE A CA    1 
ATOM   535  C  C     . ILE A 1 82  ? 14.264  0.373   1.167   1.00 23.49  ? 44  ILE A C     1 
ATOM   536  O  O     . ILE A 1 82  ? 15.353  0.898   0.918   1.00 21.94  ? 44  ILE A O     1 
ATOM   537  C  CB    . ILE A 1 82  ? 13.682  0.367   3.640   1.00 21.92  ? 44  ILE A CB    1 
ATOM   538  C  CG1   . ILE A 1 82  ? 12.238  0.853   3.532   1.00 22.42  ? 44  ILE A CG1   1 
ATOM   539  C  CG2   . ILE A 1 82  ? 14.603  1.577   3.784   1.00 15.67  ? 44  ILE A CG2   1 
ATOM   540  C  CD1   . ILE A 1 82  ? 11.229  -0.268  3.414   1.00 22.00  ? 44  ILE A CD1   1 
ATOM   541  N  N     . ASP A 1 83  ? 13.203  0.483   0.371   1.00 23.53  ? 45  ASP A N     1 
ATOM   542  C  CA    . ASP A 1 83  ? 13.125  1.427   -0.733  1.00 15.17  ? 45  ASP A CA    1 
ATOM   543  C  C     . ASP A 1 83  ? 11.655  1.682   -1.007  1.00 21.22  ? 45  ASP A C     1 
ATOM   544  O  O     . ASP A 1 83  ? 10.777  0.998   -0.479  1.00 18.73  ? 45  ASP A O     1 
ATOM   545  C  CB    . ASP A 1 83  ? 13.818  0.902   -1.994  1.00 22.81  ? 45  ASP A CB    1 
ATOM   546  C  CG    . ASP A 1 83  ? 14.499  2.007   -2.800  1.00 25.50  ? 45  ASP A CG    1 
ATOM   547  O  OD1   . ASP A 1 83  ? 15.425  1.674   -3.564  1.00 28.24  ? 45  ASP A OD1   1 
ATOM   548  O  OD2   . ASP A 1 83  ? 14.132  3.201   -2.664  1.00 16.05  ? 45  ASP A OD2   1 
ATOM   549  N  N     . PHE A 1 84  ? 11.388  2.666   -1.855  1.00 27.38  ? 46  PHE A N     1 
ATOM   550  C  CA    . PHE A 1 84  ? 10.031  2.832   -2.347  1.00 16.46  ? 46  PHE A CA    1 
ATOM   551  C  C     . PHE A 1 84  ? 10.060  3.340   -3.780  1.00 17.41  ? 46  PHE A C     1 
ATOM   552  O  O     . PHE A 1 84  ? 11.083  3.824   -4.276  1.00 12.39  ? 46  PHE A O     1 
ATOM   553  C  CB    . PHE A 1 84  ? 9.210   3.769   -1.444  1.00 15.56  ? 46  PHE A CB    1 
ATOM   554  C  CG    . PHE A 1 84  ? 9.671   5.187   -1.445  1.00 12.40  ? 46  PHE A CG    1 
ATOM   555  C  CD1   . PHE A 1 84  ? 9.091   6.121   -2.286  1.00 19.35  ? 46  PHE A CD1   1 
ATOM   556  C  CD2   . PHE A 1 84  ? 10.657  5.606   -0.569  1.00 21.22  ? 46  PHE A CD2   1 
ATOM   557  C  CE1   . PHE A 1 84  ? 9.514   7.441   -2.282  1.00 23.14  ? 46  PHE A CE1   1 
ATOM   558  C  CE2   . PHE A 1 84  ? 11.075  6.920   -0.557  1.00 20.50  ? 46  PHE A CE2   1 
ATOM   559  C  CZ    . PHE A 1 84  ? 10.511  7.836   -1.417  1.00 13.20  ? 46  PHE A CZ    1 
ATOM   560  N  N     . ARG A 1 85  ? 8.907   3.218   -4.434  1.00 18.55  ? 47  ARG A N     1 
ATOM   561  C  CA    . ARG A 1 85  ? 8.632   3.775   -5.747  1.00 19.02  ? 47  ARG A CA    1 
ATOM   562  C  C     . ARG A 1 85  ? 7.370   4.622   -5.664  1.00 19.63  ? 47  ARG A C     1 
ATOM   563  O  O     . ARG A 1 85  ? 6.640   4.595   -4.665  1.00 18.67  ? 47  ARG A O     1 
ATOM   564  C  CB    . ARG A 1 85  ? 8.482   2.665   -6.803  1.00 22.03  ? 47  ARG A CB    1 
ATOM   565  C  CG    . ARG A 1 85  ? 9.717   1.775   -6.942  1.00 13.88  ? 47  ARG A CG    1 
ATOM   566  C  CD    . ARG A 1 85  ? 9.656   0.897   -8.200  1.00 25.69  ? 47  ARG A CD    1 
ATOM   567  N  NE    . ARG A 1 85  ? 9.999   1.686   -9.375  1.00 19.97  ? 47  ARG A NE    1 
ATOM   568  C  CZ    . ARG A 1 85  ? 11.246  1.959   -9.739  1.00 23.23  ? 47  ARG A CZ    1 
ATOM   569  N  NH1   . ARG A 1 85  ? 12.256  1.482   -9.027  1.00 25.29  ? 47  ARG A NH1   1 
ATOM   570  N  NH2   . ARG A 1 85  ? 11.483  2.702   -10.813 1.00 26.74  ? 47  ARG A NH2   1 
ATOM   571  N  N     . GLU A 1 86  ? 7.134   5.407   -6.717  1.00 20.19  ? 48  GLU A N     1 
ATOM   572  C  CA    . GLU A 1 86  ? 5.940   6.230   -6.830  1.00 20.87  ? 48  GLU A CA    1 
ATOM   573  C  C     . GLU A 1 86  ? 5.271   6.016   -8.183  1.00 20.54  ? 48  GLU A C     1 
ATOM   574  O  O     . GLU A 1 86  ? 5.900   5.593   -9.156  1.00 23.57  ? 48  GLU A O     1 
ATOM   575  C  CB    . GLU A 1 86  ? 6.253   7.713   -6.648  1.00 19.90  ? 48  GLU A CB    1 
ATOM   576  C  CG    . GLU A 1 86  ? 7.327   7.990   -5.617  1.00 23.31  ? 48  GLU A CG    1 
ATOM   577  C  CD    . GLU A 1 86  ? 7.525   9.464   -5.362  1.00 22.97  ? 48  GLU A CD    1 
ATOM   578  O  OE1   . GLU A 1 86  ? 6.607   10.252  -5.673  1.00 28.77  ? 48  GLU A OE1   1 
ATOM   579  O  OE2   . GLU A 1 86  ? 8.588   9.842   -4.835  1.00 33.20  ? 48  GLU A OE2   1 
ATOM   580  N  N     . LYS A 1 87  ? 3.969   6.275   -8.206  1.00 17.54  ? 49  LYS A N     1 
ATOM   581  C  CA    . LYS A 1 87  ? 3.169   6.342   -9.415  1.00 32.16  ? 49  LYS A CA    1 
ATOM   582  C  C     . LYS A 1 87  ? 2.037   7.320   -9.146  1.00 28.57  ? 49  LYS A C     1 
ATOM   583  O  O     . LYS A 1 87  ? 1.593   7.469   -8.006  1.00 32.20  ? 49  LYS A O     1 
ATOM   584  C  CB    . LYS A 1 87  ? 2.612   4.970   -9.820  1.00 17.67  ? 49  LYS A CB    1 
ATOM   585  C  CG    . LYS A 1 87  ? 2.540   4.748   -11.330 1.00 21.82  ? 49  LYS A CG    1 
ATOM   586  C  CD    . LYS A 1 87  ? 1.732   3.512   -11.669 1.00 12.79  ? 49  LYS A CD    1 
ATOM   587  C  CE    . LYS A 1 87  ? 1.994   3.053   -13.062 1.00 12.35  ? 49  LYS A CE    1 
ATOM   588  N  NZ    . LYS A 1 87  ? 0.807   2.329   -13.592 1.00 29.74  ? 49  LYS A NZ    1 
ATOM   589  N  N     . ARG A 1 88  ? 1.586   7.999   -10.188 1.00 17.82  ? 50  ARG A N     1 
ATOM   590  C  CA    . ARG A 1 88  ? 0.394   8.825   -10.105 1.00 20.36  ? 50  ARG A CA    1 
ATOM   591  C  C     . ARG A 1 88  ? -0.720  8.150   -10.891 1.00 23.20  ? 50  ARG A C     1 
ATOM   592  O  O     . ARG A 1 88  ? -0.564  7.862   -12.083 1.00 30.96  ? 50  ARG A O     1 
ATOM   593  C  CB    . ARG A 1 88  ? 0.680   10.232  -10.608 1.00 24.53  ? 50  ARG A CB    1 
ATOM   594  C  CG    . ARG A 1 88  ? 1.431   11.027  -9.565  1.00 32.90  ? 50  ARG A CG    1 
ATOM   595  C  CD    . ARG A 1 88  ? 1.739   12.456  -9.976  1.00 46.12  ? 50  ARG A CD    1 
ATOM   596  N  NE    . ARG A 1 88  ? 2.609   13.079  -8.983  1.00 34.95  ? 50  ARG A NE    1 
ATOM   597  C  CZ    . ARG A 1 88  ? 2.215   13.397  -7.751  1.00 42.45  ? 50  ARG A CZ    1 
ATOM   598  N  NH1   . ARG A 1 88  ? 3.072   13.950  -6.894  1.00 52.15  ? 50  ARG A NH1   1 
ATOM   599  N  NH2   . ARG A 1 88  ? 0.958   13.163  -7.376  1.00 35.51  ? 50  ARG A NH2   1 
ATOM   600  N  N     . VAL A 1 89  ? -1.836  7.882   -10.217 1.00 21.67  ? 51  VAL A N     1 
ATOM   601  C  CA    . VAL A 1 89  ? -2.903  7.064   -10.770 1.00 17.41  ? 51  VAL A CA    1 
ATOM   602  C  C     . VAL A 1 89  ? -4.234  7.751   -10.524 1.00 14.72  ? 51  VAL A C     1 
ATOM   603  O  O     . VAL A 1 89  ? -4.361  8.639   -9.683  1.00 18.63  ? 51  VAL A O     1 
ATOM   604  C  CB    . VAL A 1 89  ? -2.923  5.643   -10.164 1.00 25.82  ? 51  VAL A CB    1 
ATOM   605  C  CG1   . VAL A 1 89  ? -1.573  4.982   -10.329 1.00 27.76  ? 51  VAL A CG1   1 
ATOM   606  C  CG2   . VAL A 1 89  ? -3.333  5.682   -8.697  1.00 18.29  ? 51  VAL A CG2   1 
ATOM   607  N  N     . VAL A 1 90  ? -5.233  7.321   -11.280 1.00 22.20  ? 52  VAL A N     1 
ATOM   608  C  CA    . VAL A 1 90  ? -6.572  7.883   -11.233 1.00 21.18  ? 52  VAL A CA    1 
ATOM   609  C  C     . VAL A 1 90  ? -7.501  6.773   -10.774 1.00 18.53  ? 52  VAL A C     1 
ATOM   610  O  O     . VAL A 1 90  ? -7.636  5.749   -11.454 1.00 16.25  ? 52  VAL A O     1 
ATOM   611  C  CB    . VAL A 1 90  ? -6.982  8.444   -12.603 1.00 21.01  ? 52  VAL A CB    1 
ATOM   612  C  CG1   . VAL A 1 90  ? -8.406  8.986   -12.593 1.00 18.37  ? 52  VAL A CG1   1 
ATOM   613  C  CG2   . VAL A 1 90  ? -6.006  9.516   -13.009 1.00 16.34  ? 52  VAL A CG2   1 
ATOM   614  N  N     . TYR A 1 91  ? -8.092  6.947   -9.601  1.00 20.01  ? 53  TYR A N     1 
ATOM   615  C  CA    . TYR A 1 91  ? -8.925  5.923   -8.995  1.00 19.47  ? 53  TYR A CA    1 
ATOM   616  C  C     . TYR A 1 91  ? -10.371 6.377   -9.006  1.00 20.71  ? 53  TYR A C     1 
ATOM   617  O  O     . TYR A 1 91  ? -10.674 7.507   -8.617  1.00 28.90  ? 53  TYR A O     1 
ATOM   618  C  CB    . TYR A 1 91  ? -8.481  5.634   -7.568  1.00 21.65  ? 53  TYR A CB    1 
ATOM   619  C  CG    . TYR A 1 91  ? -9.538  4.930   -6.741  1.00 19.98  ? 53  TYR A CG    1 
ATOM   620  C  CD1   . TYR A 1 91  ? -9.619  3.553   -6.732  1.00 21.76  ? 53  TYR A CD1   1 
ATOM   621  C  CD2   . TYR A 1 91  ? -10.456 5.648   -5.984  1.00 17.41  ? 53  TYR A CD2   1 
ATOM   622  C  CE1   . TYR A 1 91  ? -10.579 2.909   -5.999  1.00 28.22  ? 53  TYR A CE1   1 
ATOM   623  C  CE2   . TYR A 1 91  ? -11.425 5.017   -5.256  1.00 23.77  ? 53  TYR A CE2   1 
ATOM   624  C  CZ    . TYR A 1 91  ? -11.476 3.638   -5.255  1.00 27.73  ? 53  TYR A CZ    1 
ATOM   625  O  OH    . TYR A 1 91  ? -12.428 2.977   -4.514  1.00 25.69  ? 53  TYR A OH    1 
ATOM   626  N  N     . ARG A 1 92  ? -11.263 5.490   -9.420  1.00 24.08  ? 54  ARG A N     1 
ATOM   627  C  CA    . ARG A 1 92  ? -12.685 5.777   -9.444  1.00 24.88  ? 54  ARG A CA    1 
ATOM   628  C  C     . ARG A 1 92  ? -13.413 4.750   -8.598  1.00 23.88  ? 54  ARG A C     1 
ATOM   629  O  O     . ARG A 1 92  ? -13.130 3.554   -8.693  1.00 28.79  ? 54  ARG A O     1 
ATOM   630  C  CB    . ARG A 1 92  ? -13.227 5.760   -10.877 1.00 25.92  ? 54  ARG A CB    1 
ATOM   631  C  CG    . ARG A 1 92  ? -12.412 6.590   -11.849 1.00 33.24  ? 54  ARG A CG    1 
ATOM   632  C  CD    . ARG A 1 92  ? -12.795 6.286   -13.280 1.00 32.02  ? 54  ARG A CD    1 
ATOM   633  N  NE    . ARG A 1 92  ? -14.159 6.705   -13.577 1.00 30.91  ? 54  ARG A NE    1 
ATOM   634  C  CZ    . ARG A 1 92  ? -14.888 6.189   -14.560 1.00 31.24  ? 54  ARG A CZ    1 
ATOM   635  N  NH1   . ARG A 1 92  ? -14.378 5.229   -15.324 1.00 22.86  ? 54  ARG A NH1   1 
ATOM   636  N  NH2   . ARG A 1 92  ? -16.125 6.620   -14.764 1.00 28.57  ? 54  ARG A NH2   1 
ATOM   637  N  N     . ALA A 1 93  ? -14.359 5.219   -7.790  1.00 27.33  ? 55  ALA A N     1 
ATOM   638  C  CA    . ALA A 1 93  ? -15.085 4.366   -6.862  1.00 21.86  ? 55  ALA A CA    1 
ATOM   639  C  C     . ALA A 1 93  ? -16.078 3.463   -7.586  1.00 30.79  ? 55  ALA A C     1 
ATOM   640  O  O     . ALA A 1 93  ? -16.503 3.728   -8.712  1.00 39.05  ? 55  ALA A O     1 
ATOM   641  C  CB    . ALA A 1 93  ? -15.836 5.203   -5.824  1.00 24.39  ? 55  ALA A CB    1 
ATOM   642  N  N     . SER A 1 94  ? -16.467 2.394   -6.901  1.00 31.91  ? 56  SER A N     1 
ATOM   643  C  CA    . SER A 1 94  ? -17.472 1.463   -7.388  1.00 37.51  ? 56  SER A CA    1 
ATOM   644  C  C     . SER A 1 94  ? -18.749 1.642   -6.585  1.00 46.31  ? 56  SER A C     1 
ATOM   645  O  O     . SER A 1 94  ? -18.712 1.645   -5.350  1.00 51.96  ? 56  SER A O     1 
ATOM   646  C  CB    . SER A 1 94  ? -16.977 0.020   -7.290  1.00 38.50  ? 56  SER A CB    1 
ATOM   647  O  OG    . SER A 1 94  ? -15.675 -0.106  -7.845  1.00 50.19  ? 56  SER A OG    1 
ATOM   648  N  N     . GLY A 1 95  ? -19.867 1.814   -7.289  1.00 52.44  ? 57  GLY A N     1 
ATOM   649  C  CA    . GLY A 1 95  ? -21.179 1.844   -6.685  1.00 61.65  ? 57  GLY A CA    1 
ATOM   650  C  C     . GLY A 1 95  ? -22.052 0.737   -7.250  1.00 78.89  ? 57  GLY A C     1 
ATOM   651  O  O     . GLY A 1 95  ? -21.552 -0.294  -7.715  1.00 79.29  ? 57  GLY A O     1 
ATOM   652  N  N     . PRO A 1 96  ? -23.372 0.921   -7.222  1.00 83.36  ? 58  PRO A N     1 
ATOM   653  C  CA    . PRO A 1 96  ? -24.261 -0.030  -7.897  1.00 82.20  ? 58  PRO A CA    1 
ATOM   654  C  C     . PRO A 1 96  ? -24.206 0.156   -9.405  1.00 88.37  ? 58  PRO A C     1 
ATOM   655  O  O     . PRO A 1 96  ? -23.898 1.239   -9.905  1.00 94.36  ? 58  PRO A O     1 
ATOM   656  C  CB    . PRO A 1 96  ? -25.644 0.338   -7.352  1.00 72.02  ? 58  PRO A CB    1 
ATOM   657  C  CG    . PRO A 1 96  ? -25.542 1.810   -7.100  1.00 71.22  ? 58  PRO A CG    1 
ATOM   658  C  CD    . PRO A 1 96  ? -24.116 2.057   -6.645  1.00 71.87  ? 58  PRO A CD    1 
ATOM   659  N  N     . ASP A 1 97  ? -24.500 -0.921  -10.134 1.00 83.45  ? 59  ASP A N     1 
ATOM   660  C  CA    . ASP A 1 97  ? -24.585 -0.866  -11.598 1.00 92.57  ? 59  ASP A CA    1 
ATOM   661  C  C     . ASP A 1 97  ? -23.298 -0.333  -12.226 1.00 96.41  ? 59  ASP A C     1 
ATOM   662  O  O     . ASP A 1 97  ? -23.314 0.223   -13.331 1.00 91.40  ? 59  ASP A O     1 
ATOM   663  C  CB    . ASP A 1 97  ? -25.774 -0.013  -12.049 1.00 78.09  ? 59  ASP A CB    1 
ATOM   664  C  CG    . ASP A 1 97  ? -26.999 -0.838  -12.352 1.00 92.38  ? 59  ASP A CG    1 
ATOM   665  O  OD1   . ASP A 1 97  ? -28.020 -0.658  -11.655 1.00 96.49  ? 59  ASP A OD1   1 
ATOM   666  O  OD2   . ASP A 1 97  ? -26.943 -1.664  -13.289 1.00 96.50  ? 59  ASP A OD2   1 
ATOM   667  N  N     . GLY A 1 98  ? -22.178 -0.499  -11.529 1.00 82.03  ? 60  GLY A N     1 
ATOM   668  C  CA    . GLY A 1 98  ? -20.970 0.209   -11.887 1.00 77.59  ? 60  GLY A CA    1 
ATOM   669  C  C     . GLY A 1 98  ? -20.887 1.527   -11.143 1.00 77.81  ? 60  GLY A C     1 
ATOM   670  O  O     . GLY A 1 98  ? -20.126 1.642   -10.177 1.00 75.21  ? 60  GLY A O     1 
ATOM   671  N  N     . ALA A 1 99  ? -21.685 2.515   -11.573 1.00 77.13  ? 61  ALA A N     1 
ATOM   672  C  CA    . ALA A 1 99  ? -21.691 3.867   -11.010 1.00 75.59  ? 61  ALA A CA    1 
ATOM   673  C  C     . ALA A 1 99  ? -20.278 4.359   -10.739 1.00 67.10  ? 61  ALA A C     1 
ATOM   674  O  O     . ALA A 1 99  ? -20.000 4.922   -9.672  1.00 57.97  ? 61  ALA A O     1 
ATOM   675  C  CB    . ALA A 1 99  ? -22.516 3.933   -9.721  1.00 67.02  ? 61  ALA A CB    1 
ATOM   676  N  N     . THR A 1 100 ? -19.380 4.130   -11.692 1.00 45.52  ? 62  THR A N     1 
ATOM   677  C  CA    . THR A 1 100 ? -17.995 4.516   -11.507 1.00 43.97  ? 62  THR A CA    1 
ATOM   678  C  C     . THR A 1 100 ? -17.903 6.022   -11.314 1.00 38.11  ? 62  THR A C     1 
ATOM   679  O  O     . THR A 1 100 ? -18.261 6.798   -12.203 1.00 33.64  ? 62  THR A O     1 
ATOM   680  C  CB    . THR A 1 100 ? -17.174 4.039   -12.696 1.00 39.46  ? 62  THR A CB    1 
ATOM   681  O  OG1   . THR A 1 100 ? -17.686 2.768   -13.111 1.00 52.31  ? 62  THR A OG1   1 
ATOM   682  C  CG2   . THR A 1 100 ? -15.722 3.880   -12.315 1.00 29.23  ? 62  THR A CG2   1 
ATOM   683  N  N     . GLY A 1 101 ? -17.466 6.420   -10.121 1.00 37.98  ? 63  GLY A N     1 
ATOM   684  C  CA    . GLY A 1 101 ? -17.503 7.799   -9.693  1.00 38.44  ? 63  GLY A CA    1 
ATOM   685  C  C     . GLY A 1 101 ? -16.413 8.627   -10.335 1.00 29.04  ? 63  GLY A C     1 
ATOM   686  O  O     . GLY A 1 101 ? -15.745 8.217   -11.285 1.00 34.69  ? 63  GLY A O     1 
ATOM   687  N  N     . ARG A 1 102 ? -16.257 9.840   -9.805  1.00 29.27  ? 64  ARG A N     1 
ATOM   688  C  CA    . ARG A 1 102 ? -15.281 10.784  -10.332 1.00 30.59  ? 64  ARG A CA    1 
ATOM   689  C  C     . ARG A 1 102 ? -13.876 10.205  -10.232 1.00 28.73  ? 64  ARG A C     1 
ATOM   690  O  O     . ARG A 1 102 ? -13.562 9.429   -9.325  1.00 35.08  ? 64  ARG A O     1 
ATOM   691  C  CB    . ARG A 1 102 ? -15.358 12.118  -9.577  1.00 33.82  ? 64  ARG A CB    1 
ATOM   692  C  CG    . ARG A 1 102 ? -14.874 12.070  -8.125  1.00 25.69  ? 64  ARG A CG    1 
ATOM   693  C  CD    . ARG A 1 102 ? -14.907 13.437  -7.471  1.00 30.18  ? 64  ARG A CD    1 
ATOM   694  N  NE    . ARG A 1 102 ? -13.803 13.630  -6.524  1.00 40.46  ? 64  ARG A NE    1 
ATOM   695  C  CZ    . ARG A 1 102 ? -13.834 13.253  -5.246  1.00 38.83  ? 64  ARG A CZ    1 
ATOM   696  N  NH1   . ARG A 1 102 ? -14.907 12.645  -4.743  1.00 35.62  ? 64  ARG A NH1   1 
ATOM   697  N  NH2   . ARG A 1 102 ? -12.782 13.463  -4.470  1.00 34.76  ? 64  ARG A NH2   1 
ATOM   698  N  N     . GLY A 1 103 ? -13.038 10.562  -11.204 1.00 25.67  ? 65  GLY A N     1 
ATOM   699  C  CA    . GLY A 1 103 ? -11.667 10.115  -11.203 1.00 17.80  ? 65  GLY A CA    1 
ATOM   700  C  C     . GLY A 1 103 ? -10.905 10.885  -10.156 1.00 24.88  ? 65  GLY A C     1 
ATOM   701  O  O     . GLY A 1 103 ? -10.698 12.089  -10.300 1.00 37.42  ? 65  GLY A O     1 
ATOM   702  N  N     . GLN A 1 104 ? -10.523 10.225  -9.076  1.00 22.11  ? 66  GLN A N     1 
ATOM   703  C  CA    . GLN A 1 104 ? -9.766  10.880  -8.027  1.00 22.96  ? 66  GLN A CA    1 
ATOM   704  C  C     . GLN A 1 104 ? -8.285  10.724  -8.302  1.00 22.89  ? 66  GLN A C     1 
ATOM   705  O  O     . GLN A 1 104 ? -7.844  9.708   -8.843  1.00 23.96  ? 66  GLN A O     1 
ATOM   706  C  CB    . GLN A 1 104 ? -10.114 10.280  -6.671  1.00 16.17  ? 66  GLN A CB    1 
ATOM   707  C  CG    . GLN A 1 104 ? -11.584 10.347  -6.361  1.00 24.50  ? 66  GLN A CG    1 
ATOM   708  C  CD    . GLN A 1 104 ? -11.913 9.803   -4.992  1.00 25.45  ? 66  GLN A CD    1 
ATOM   709  O  OE1   . GLN A 1 104 ? -11.462 10.330  -3.961  1.00 22.05  ? 66  GLN A OE1   1 
ATOM   710  N  NE2   . GLN A 1 104 ? -12.709 8.744   -4.967  1.00 26.42  ? 66  GLN A NE2   1 
ATOM   711  N  N     . ARG A 1 105 ? -7.507  11.739  -7.942  1.00 19.63  ? 67  ARG A N     1 
ATOM   712  C  CA    . ARG A 1 105 ? -6.070  11.634  -8.131  1.00 16.94  ? 67  ARG A CA    1 
ATOM   713  C  C     . ARG A 1 105 ? -5.433  11.006  -6.898  1.00 28.50  ? 67  ARG A C     1 
ATOM   714  O  O     . ARG A 1 105 ? -5.562  11.512  -5.774  1.00 24.81  ? 67  ARG A O     1 
ATOM   715  C  CB    . ARG A 1 105 ? -5.445  12.978  -8.478  1.00 26.38  ? 67  ARG A CB    1 
ATOM   716  C  CG    . ARG A 1 105 ? -5.889  13.421  -9.856  1.00 30.43  ? 67  ARG A CG    1 
ATOM   717  C  CD    . ARG A 1 105 ? -6.263  14.848  -9.821  1.00 39.54  ? 67  ARG A CD    1 
ATOM   718  N  NE    . ARG A 1 105 ? -5.095  15.678  -10.072 1.00 47.12  ? 67  ARG A NE    1 
ATOM   719  C  CZ    . ARG A 1 105 ? -4.998  16.951  -9.711  1.00 54.04  ? 67  ARG A CZ    1 
ATOM   720  N  NH1   . ARG A 1 105 ? -3.909  17.654  -10.003 1.00 51.09  ? 67  ARG A NH1   1 
ATOM   721  N  NH2   . ARG A 1 105 ? -5.956  17.495  -8.974  1.00 52.32  ? 67  ARG A NH2   1 
ATOM   722  N  N     . ILE A 1 106 ? -4.775  9.878   -7.117  1.00 23.88  ? 68  ILE A N     1 
ATOM   723  C  CA    . ILE A 1 106 ? -4.067  9.154   -6.083  1.00 15.08  ? 68  ILE A CA    1 
ATOM   724  C  C     . ILE A 1 106 ? -2.589  9.229   -6.406  1.00 20.06  ? 68  ILE A C     1 
ATOM   725  O  O     . ILE A 1 106 ? -2.178  8.983   -7.547  1.00 23.41  ? 68  ILE A O     1 
ATOM   726  C  CB    . ILE A 1 106 ? -4.538  7.697   -5.989  1.00 24.39  ? 68  ILE A CB    1 
ATOM   727  C  CG1   . ILE A 1 106 ? -6.033  7.628   -5.633  1.00 21.15  ? 68  ILE A CG1   1 
ATOM   728  C  CG2   . ILE A 1 106 ? -3.708  6.967   -4.977  1.00 16.77  ? 68  ILE A CG2   1 
ATOM   729  C  CD1   . ILE A 1 106 ? -6.403  8.423   -4.422  1.00 21.08  ? 68  ILE A CD1   1 
ATOM   730  N  N     . HIS A 1 107 ? -1.804  9.604   -5.416  1.00 32.70  ? 69  HIS A N     1 
ATOM   731  C  CA    . HIS A 1 107 ? -0.351  9.632   -5.494  1.00 28.99  ? 69  HIS A CA    1 
ATOM   732  C  C     . HIS A 1 107 ? 0.113   8.506   -4.573  1.00 26.43  ? 69  HIS A C     1 
ATOM   733  O  O     . HIS A 1 107 ? 0.102   8.652   -3.348  1.00 25.90  ? 69  HIS A O     1 
ATOM   734  C  CB    . HIS A 1 107 ? 0.170   11.012  -5.089  1.00 24.30  ? 69  HIS A CB    1 
ATOM   735  C  CG    . HIS A 1 107 ? 1.645   11.070  -4.830  1.00 30.98  ? 69  HIS A CG    1 
ATOM   736  N  ND1   . HIS A 1 107 ? 2.556   10.280  -5.501  1.00 27.43  ? 69  HIS A ND1   1 
ATOM   737  C  CD2   . HIS A 1 107 ? 2.371   11.850  -3.990  1.00 22.66  ? 69  HIS A CD2   1 
ATOM   738  C  CE1   . HIS A 1 107 ? 3.775   10.554  -5.072  1.00 23.13  ? 69  HIS A CE1   1 
ATOM   739  N  NE2   . HIS A 1 107 ? 3.690   11.506  -4.157  1.00 19.71  ? 69  HIS A NE2   1 
ATOM   740  N  N     . LEU A 1 108 ? 0.477   7.368   -5.172  1.00 25.84  ? 70  LEU A N     1 
ATOM   741  C  CA    . LEU A 1 108 ? 0.802   6.154   -4.437  1.00 21.32  ? 70  LEU A CA    1 
ATOM   742  C  C     . LEU A 1 108 ? 2.280   6.119   -4.092  1.00 18.49  ? 70  LEU A C     1 
ATOM   743  O  O     . LEU A 1 108 ? 3.122   6.131   -4.992  1.00 23.27  ? 70  LEU A O     1 
ATOM   744  C  CB    . LEU A 1 108 ? 0.481   4.910   -5.254  1.00 20.07  ? 70  LEU A CB    1 
ATOM   745  C  CG    . LEU A 1 108 ? -0.850  4.618   -5.898  1.00 19.35  ? 70  LEU A CG    1 
ATOM   746  C  CD1   . LEU A 1 108 ? -0.570  3.630   -6.987  1.00 16.98  ? 70  LEU A CD1   1 
ATOM   747  C  CD2   . LEU A 1 108 ? -1.746  4.007   -4.880  1.00 21.08  ? 70  LEU A CD2   1 
ATOM   748  N  N     . GLN A 1 109 ? 2.591   6.010   -2.804  1.00 23.22  ? 71  GLN A N     1 
ATOM   749  C  CA    . GLN A 1 109 ? 3.920   5.620   -2.354  1.00 18.35  ? 71  GLN A CA    1 
ATOM   750  C  C     . GLN A 1 109 ? 3.910   4.116   -2.131  1.00 22.01  ? 71  GLN A C     1 
ATOM   751  O  O     . GLN A 1 109 ? 3.001   3.594   -1.476  1.00 23.89  ? 71  GLN A O     1 
ATOM   752  C  CB    . GLN A 1 109 ? 4.313   6.345   -1.071  1.00 23.00  ? 71  GLN A CB    1 
ATOM   753  C  CG    . GLN A 1 109 ? 5.807   6.502   -0.873  1.00 18.06  ? 71  GLN A CG    1 
ATOM   754  C  CD    . GLN A 1 109 ? 6.132   7.136   0.470   1.00 22.89  ? 71  GLN A CD    1 
ATOM   755  O  OE1   . GLN A 1 109 ? 5.249   7.644   1.159   1.00 32.78  ? 71  GLN A OE1   1 
ATOM   756  N  NE2   . GLN A 1 109 ? 7.403   7.117   0.842   1.00 20.45  ? 71  GLN A NE2   1 
ATOM   757  N  N     . LEU A 1 110 ? 4.903   3.420   -2.688  1.00 20.32  ? 72  LEU A N     1 
ATOM   758  C  CA    . LEU A 1 110 ? 4.934   1.956   -2.690  1.00 17.44  ? 72  LEU A CA    1 
ATOM   759  C  C     . LEU A 1 110 ? 6.185   1.470   -1.966  1.00 19.92  ? 72  LEU A C     1 
ATOM   760  O  O     . LEU A 1 110 ? 7.269   1.426   -2.553  1.00 22.33  ? 72  LEU A O     1 
ATOM   761  C  CB    . LEU A 1 110 ? 4.882   1.409   -4.115  1.00 26.03  ? 72  LEU A CB    1 
ATOM   762  C  CG    . LEU A 1 110 ? 3.751   1.850   -5.042  1.00 14.42  ? 72  LEU A CG    1 
ATOM   763  C  CD1   . LEU A 1 110 ? 4.121   3.113   -5.745  1.00 12.68  ? 72  LEU A CD1   1 
ATOM   764  C  CD2   . LEU A 1 110 ? 3.513   0.765   -6.064  1.00 26.39  ? 72  LEU A CD2   1 
ATOM   765  N  N     . TRP A 1 111 ? 6.038   1.073   -0.704  1.00 17.92  ? 73  TRP A N     1 
ATOM   766  C  CA    . TRP A 1 111 ? 7.203   0.698   0.084   1.00 21.18  ? 73  TRP A CA    1 
ATOM   767  C  C     . TRP A 1 111 ? 7.646   -0.715  -0.268  1.00 20.20  ? 73  TRP A C     1 
ATOM   768  O  O     . TRP A 1 111 ? 6.825   -1.636  -0.358  1.00 18.19  ? 73  TRP A O     1 
ATOM   769  C  CB    . TRP A 1 111 ? 6.914   0.814   1.578   1.00 16.45  ? 73  TRP A CB    1 
ATOM   770  C  CG    . TRP A 1 111 ? 6.933   2.235   2.110   1.00 16.89  ? 73  TRP A CG    1 
ATOM   771  C  CD1   . TRP A 1 111 ? 5.850   3.022   2.369   1.00 24.03  ? 73  TRP A CD1   1 
ATOM   772  C  CD2   . TRP A 1 111 ? 8.085   3.018   2.463   1.00 18.55  ? 73  TRP A CD2   1 
ATOM   773  N  NE1   . TRP A 1 111 ? 6.250   4.245   2.852   1.00 30.12  ? 73  TRP A NE1   1 
ATOM   774  C  CE2   . TRP A 1 111 ? 7.616   4.267   2.926   1.00 21.22  ? 73  TRP A CE2   1 
ATOM   775  C  CE3   . TRP A 1 111 ? 9.465   2.786   2.430   1.00 20.95  ? 73  TRP A CE3   1 
ATOM   776  C  CZ2   . TRP A 1 111 ? 8.472   5.277   3.363   1.00 20.24  ? 73  TRP A CZ2   1 
ATOM   777  C  CZ3   . TRP A 1 111 ? 10.316  3.796   2.858   1.00 27.21  ? 73  TRP A CZ3   1 
ATOM   778  C  CH2   . TRP A 1 111 ? 9.811   5.030   3.324   1.00 21.97  ? 73  TRP A CH2   1 
ATOM   779  N  N     . ASP A 1 112 ? 8.957   -0.875  -0.451  1.00 18.14  ? 74  ASP A N     1 
ATOM   780  C  CA    . ASP A 1 112 ? 9.586   -2.128  -0.836  1.00 16.77  ? 74  ASP A CA    1 
ATOM   781  C  C     . ASP A 1 112 ? 10.560  -2.529  0.258   1.00 18.57  ? 74  ASP A C     1 
ATOM   782  O  O     . ASP A 1 112 ? 11.436  -1.743  0.642   1.00 19.36  ? 74  ASP A O     1 
ATOM   783  C  CB    . ASP A 1 112 ? 10.313  -1.976  -2.173  1.00 12.97  ? 74  ASP A CB    1 
ATOM   784  C  CG    . ASP A 1 112 ? 10.900  -3.269  -2.670  1.00 18.98  ? 74  ASP A CG    1 
ATOM   785  O  OD1   . ASP A 1 112 ? 10.576  -4.331  -2.083  1.00 20.76  ? 74  ASP A OD1   1 
ATOM   786  O  OD2   . ASP A 1 112 ? 11.678  -3.228  -3.664  1.00 19.89  ? 74  ASP A OD2   1 
ATOM   787  N  N     . THR A 1 113 ? 10.421  -3.748  0.753   1.00 15.28  ? 75  THR A N     1 
ATOM   788  C  CA    . THR A 1 113 ? 11.156  -4.169  1.929   1.00 22.26  ? 75  THR A CA    1 
ATOM   789  C  C     . THR A 1 113 ? 12.037  -5.360  1.611   1.00 23.13  ? 75  THR A C     1 
ATOM   790  O  O     . THR A 1 113 ? 11.637  -6.256  0.861   1.00 25.01  ? 75  THR A O     1 
ATOM   791  C  CB    . THR A 1 113 ? 10.206  -4.547  3.045   1.00 18.80  ? 75  THR A CB    1 
ATOM   792  O  OG1   . THR A 1 113 ? 9.728   -5.875  2.803   1.00 21.31  ? 75  THR A OG1   1 
ATOM   793  C  CG2   . THR A 1 113 ? 9.055   -3.605  3.041   1.00 19.09  ? 75  THR A CG2   1 
ATOM   794  N  N     . ALA A 1 114 ? 13.218  -5.380  2.222   1.00 20.49  ? 76  ALA A N     1 
ATOM   795  C  CA    . ALA A 1 114 ? 14.036  -6.580  2.184   1.00 20.55  ? 76  ALA A CA    1 
ATOM   796  C  C     . ALA A 1 114 ? 13.316  -7.720  2.900   1.00 20.65  ? 76  ALA A C     1 
ATOM   797  O  O     . ALA A 1 114 ? 12.495  -7.503  3.799   1.00 28.07  ? 76  ALA A O     1 
ATOM   798  C  CB    . ALA A 1 114 ? 15.401  -6.309  2.815   1.00 13.56  ? 76  ALA A CB    1 
ATOM   799  N  N     . GLY A 1 115 ? 13.622  -8.947  2.490   1.00 17.85  ? 77  GLY A N     1 
ATOM   800  C  CA    . GLY A 1 115 ? 12.896  -10.093 3.004   1.00 12.66  ? 77  GLY A CA    1 
ATOM   801  C  C     . GLY A 1 115 ? 13.723  -10.887 3.980   1.00 16.24  ? 77  GLY A C     1 
ATOM   802  O  O     . GLY A 1 115 ? 13.184  -11.630 4.804   1.00 26.06  ? 77  GLY A O     1 
ATOM   803  N  N     . LEU A 1 116 ? 15.039  -10.720 3.908   1.00 17.54  ? 78  LEU A N     1 
ATOM   804  C  CA    . LEU A 1 116 ? 15.946  -11.499 4.736   1.00 23.49  ? 78  LEU A CA    1 
ATOM   805  C  C     . LEU A 1 116 ? 15.822  -11.068 6.191   1.00 29.57  ? 78  LEU A C     1 
ATOM   806  O  O     . LEU A 1 116 ? 15.956  -9.884  6.508   1.00 26.09  ? 78  LEU A O     1 
ATOM   807  C  CB    . LEU A 1 116 ? 17.386  -11.334 4.244   1.00 16.40  ? 78  LEU A CB    1 
ATOM   808  C  CG    . LEU A 1 116 ? 17.612  -11.786 2.793   1.00 18.11  ? 78  LEU A CG    1 
ATOM   809  C  CD1   . LEU A 1 116 ? 18.757  -11.051 2.136   1.00 14.07  ? 78  LEU A CD1   1 
ATOM   810  C  CD2   . LEU A 1 116 ? 17.837  -13.271 2.749   1.00 13.12  ? 78  LEU A CD2   1 
ATOM   811  N  N     . GLU A 1 117 ? 15.583  -12.038 7.078   1.00 33.81  ? 79  GLU A N     1 
ATOM   812  C  CA    . GLU A 1 117 ? 15.292  -11.775 8.484   1.00 30.53  ? 79  GLU A CA    1 
ATOM   813  C  C     . GLU A 1 117 ? 16.342  -10.893 9.152   1.00 30.48  ? 79  GLU A C     1 
ATOM   814  O  O     . GLU A 1 117 ? 16.078  -10.331 10.215  1.00 36.54  ? 79  GLU A O     1 
ATOM   815  C  CB    . GLU A 1 117 ? 15.142  -13.094 9.243   1.00 32.22  ? 79  GLU A CB    1 
ATOM   816  C  CG    . GLU A 1 117 ? 16.258  -14.101 9.003   1.00 37.27  ? 79  GLU A CG    1 
ATOM   817  C  CD    . GLU A 1 117 ? 15.943  -15.111 7.886   1.00 54.50  ? 79  GLU A CD    1 
ATOM   818  O  OE1   . GLU A 1 117 ? 16.268  -14.850 6.684   1.00 23.70  ? 79  GLU A OE1   1 
ATOM   819  O  OE2   . GLU A 1 117 ? 15.352  -16.168 8.225   1.00 46.86  ? 79  GLU A OE2   1 
ATOM   820  N  N     . ARG A 1 118 ? 17.520  -10.749 8.528   1.00 31.18  ? 80  ARG A N     1 
ATOM   821  C  CA    . ARG A 1 118 ? 18.545  -9.834  9.031   1.00 29.04  ? 80  ARG A CA    1 
ATOM   822  C  C     . ARG A 1 118 ? 18.054  -8.392  9.064   1.00 33.13  ? 80  ARG A C     1 
ATOM   823  O  O     . ARG A 1 118 ? 18.494  -7.607  9.915   1.00 25.47  ? 80  ARG A O     1 
ATOM   824  C  CB    . ARG A 1 118 ? 19.812  -9.943  8.170   1.00 34.89  ? 80  ARG A CB    1 
ATOM   825  C  CG    . ARG A 1 118 ? 20.732  -8.720  8.213   1.00 37.48  ? 80  ARG A CG    1 
ATOM   826  C  CD    . ARG A 1 118 ? 22.150  -9.024  7.714   1.00 39.91  ? 80  ARG A CD    1 
ATOM   827  N  NE    . ARG A 1 118 ? 23.030  -7.850  7.768   1.00 37.93  ? 80  ARG A NE    1 
ATOM   828  C  CZ    . ARG A 1 118 ? 23.356  -7.119  6.702   1.00 31.20  ? 80  ARG A CZ    1 
ATOM   829  N  NH1   . ARG A 1 118 ? 22.865  -7.447  5.517   1.00 26.00  ? 80  ARG A NH1   1 
ATOM   830  N  NH2   . ARG A 1 118 ? 24.158  -6.064  6.817   1.00 24.55  ? 80  ARG A NH2   1 
ATOM   831  N  N     . PHE A 1 119 ? 17.159  -8.025  8.139   1.00 34.67  ? 81  PHE A N     1 
ATOM   832  C  CA    . PHE A 1 119 ? 16.571  -6.691  8.038   1.00 28.17  ? 81  PHE A CA    1 
ATOM   833  C  C     . PHE A 1 119 ? 15.237  -6.574  8.754   1.00 18.97  ? 81  PHE A C     1 
ATOM   834  O  O     . PHE A 1 119 ? 14.603  -5.514  8.677   1.00 17.46  ? 81  PHE A O     1 
ATOM   835  C  CB    . PHE A 1 119 ? 16.363  -6.303  6.567   1.00 14.69  ? 81  PHE A CB    1 
ATOM   836  C  CG    . PHE A 1 119 ? 17.623  -5.980  5.849   1.00 17.61  ? 81  PHE A CG    1 
ATOM   837  C  CD1   . PHE A 1 119 ? 18.238  -4.759  6.033   1.00 19.08  ? 81  PHE A CD1   1 
ATOM   838  C  CD2   . PHE A 1 119 ? 18.196  -6.896  4.981   1.00 26.05  ? 81  PHE A CD2   1 
ATOM   839  C  CE1   . PHE A 1 119 ? 19.407  -4.448  5.374   1.00 17.16  ? 81  PHE A CE1   1 
ATOM   840  C  CE2   . PHE A 1 119 ? 19.374  -6.600  4.314   1.00 21.28  ? 81  PHE A CE2   1 
ATOM   841  C  CZ    . PHE A 1 119 ? 19.982  -5.374  4.515   1.00 19.62  ? 81  PHE A CZ    1 
ATOM   842  N  N     . ARG A 1 120 ? 14.804  -7.634  9.438   1.00 23.25  ? 82  ARG A N     1 
ATOM   843  C  CA    . ARG A 1 120 ? 13.429  -7.706  9.915   1.00 28.65  ? 82  ARG A CA    1 
ATOM   844  C  C     . ARG A 1 120 ? 13.109  -6.583  10.896  1.00 18.70  ? 82  ARG A C     1 
ATOM   845  O  O     . ARG A 1 120 ? 11.987  -6.061  10.899  1.00 16.94  ? 82  ARG A O     1 
ATOM   846  C  CB    . ARG A 1 120 ? 13.182  -9.081  10.533  1.00 24.09  ? 82  ARG A CB    1 
ATOM   847  C  CG    . ARG A 1 120 ? 11.747  -9.355  10.921  1.00 22.93  ? 82  ARG A CG    1 
ATOM   848  C  CD    . ARG A 1 120 ? 10.865  -9.863  9.767   1.00 49.94  ? 82  ARG A CD    1 
ATOM   849  N  NE    . ARG A 1 120 ? 11.564  -10.665 8.753   1.00 48.99  ? 82  ARG A NE    1 
ATOM   850  C  CZ    . ARG A 1 120 ? 11.253  -11.924 8.441   1.00 42.38  ? 82  ARG A CZ    1 
ATOM   851  N  NH1   . ARG A 1 120 ? 10.254  -12.544 9.073   1.00 35.43  ? 82  ARG A NH1   1 
ATOM   852  N  NH2   . ARG A 1 120 ? 11.936  -12.566 7.492   1.00 25.16  ? 82  ARG A NH2   1 
ATOM   853  N  N     . SER A 1 121 ? 14.076  -6.166  11.710  1.00 25.43  ? 83  SER A N     1 
ATOM   854  C  CA    . SER A 1 121 ? 13.763  -5.125  12.683  1.00 26.25  ? 83  SER A CA    1 
ATOM   855  C  C     . SER A 1 121 ? 13.602  -3.772  12.005  1.00 27.92  ? 83  SER A C     1 
ATOM   856  O  O     . SER A 1 121 ? 12.766  -2.970  12.435  1.00 21.44  ? 83  SER A O     1 
ATOM   857  C  CB    . SER A 1 121 ? 14.827  -5.071  13.787  1.00 27.47  ? 83  SER A CB    1 
ATOM   858  O  OG    . SER A 1 121 ? 15.853  -4.142  13.480  1.00 36.89  ? 83  SER A OG    1 
ATOM   859  N  N     . LEU A 1 122 ? 14.346  -3.518  10.920  1.00 24.05  ? 84  LEU A N     1 
ATOM   860  C  CA    . LEU A 1 122 ? 14.216  -2.243  10.220  1.00 16.21  ? 84  LEU A CA    1 
ATOM   861  C  C     . LEU A 1 122 ? 12.968  -2.193  9.351   1.00 24.90  ? 84  LEU A C     1 
ATOM   862  O  O     . LEU A 1 122 ? 12.259  -1.184  9.350   1.00 22.87  ? 84  LEU A O     1 
ATOM   863  C  CB    . LEU A 1 122 ? 15.453  -1.961  9.367   1.00 23.39  ? 84  LEU A CB    1 
ATOM   864  C  CG    . LEU A 1 122 ? 15.300  -0.683  8.539   1.00 28.20  ? 84  LEU A CG    1 
ATOM   865  C  CD1   . LEU A 1 122 ? 15.493  0.533   9.420   1.00 31.40  ? 84  LEU A CD1   1 
ATOM   866  C  CD2   . LEU A 1 122 ? 16.282  -0.645  7.379   1.00 28.79  ? 84  LEU A CD2   1 
ATOM   867  N  N     . THR A 1 123 ? 12.696  -3.255  8.575   1.00 26.18  ? 85  THR A N     1 
ATOM   868  C  CA    . THR A 1 123 ? 11.523  -3.230  7.694   1.00 31.68  ? 85  THR A CA    1 
ATOM   869  C  C     . THR A 1 123 ? 10.242  -3.035  8.489   1.00 32.62  ? 85  THR A C     1 
ATOM   870  O  O     . THR A 1 123 ? 9.341   -2.308  8.055   1.00 31.12  ? 85  THR A O     1 
ATOM   871  C  CB    . THR A 1 123 ? 11.413  -4.513  6.867   1.00 24.26  ? 85  THR A CB    1 
ATOM   872  O  OG1   . THR A 1 123 ? 11.469  -5.653  7.738   1.00 27.94  ? 85  THR A OG1   1 
ATOM   873  C  CG2   . THR A 1 123 ? 12.511  -4.586  5.812   1.00 25.22  ? 85  THR A CG2   1 
ATOM   874  N  N     . THR A 1 124 ? 10.148  -3.680  9.661   1.00 23.36  ? 86  THR A N     1 
ATOM   875  C  CA    . THR A 1 124 ? 8.968   -3.594  10.513  1.00 22.81  ? 86  THR A CA    1 
ATOM   876  C  C     . THR A 1 124 ? 8.745   -2.188  11.056  1.00 24.64  ? 86  THR A C     1 
ATOM   877  O  O     . THR A 1 124 ? 7.620   -1.849  11.435  1.00 23.85  ? 86  THR A O     1 
ATOM   878  C  CB    . THR A 1 124 ? 9.129   -4.602  11.647  1.00 27.84  ? 86  THR A CB    1 
ATOM   879  O  OG1   . THR A 1 124 ? 9.416   -5.881  11.078  1.00 28.16  ? 86  THR A OG1   1 
ATOM   880  C  CG2   . THR A 1 124 ? 7.890   -4.695  12.515  1.00 23.03  ? 86  THR A CG2   1 
ATOM   881  N  N     . ALA A 1 125 ? 9.791   -1.362  11.092  1.00 25.60  ? 87  ALA A N     1 
ATOM   882  C  CA    . ALA A 1 125 ? 9.656   0.040   11.460  1.00 23.99  ? 87  ALA A CA    1 
ATOM   883  C  C     . ALA A 1 125 ? 8.798   0.841   10.483  1.00 22.70  ? 87  ALA A C     1 
ATOM   884  O  O     . ALA A 1 125 ? 8.453   1.992   10.777  1.00 31.07  ? 87  ALA A O     1 
ATOM   885  C  CB    . ALA A 1 125 ? 11.049  0.671   11.564  1.00 14.58  ? 87  ALA A CB    1 
ATOM   886  N  N     . PHE A 1 126 ? 8.458   0.285   9.328   1.00 30.10  ? 88  PHE A N     1 
ATOM   887  C  CA    . PHE A 1 126 ? 7.775   1.047   8.297   1.00 23.84  ? 88  PHE A CA    1 
ATOM   888  C  C     . PHE A 1 126 ? 6.318   0.653   8.140   1.00 22.35  ? 88  PHE A C     1 
ATOM   889  O  O     . PHE A 1 126 ? 5.610   1.277   7.345   1.00 25.72  ? 88  PHE A O     1 
ATOM   890  C  CB    . PHE A 1 126 ? 8.525   0.911   6.967   1.00 25.22  ? 88  PHE A CB    1 
ATOM   891  C  CG    . PHE A 1 126 ? 9.839   1.625   6.964   1.00 21.30  ? 88  PHE A CG    1 
ATOM   892  C  CD1   . PHE A 1 126 ? 10.912  1.114   7.682   1.00 18.84  ? 88  PHE A CD1   1 
ATOM   893  C  CD2   . PHE A 1 126 ? 9.991   2.829   6.291   1.00 20.00  ? 88  PHE A CD2   1 
ATOM   894  C  CE1   . PHE A 1 126 ? 12.115  1.773   7.720   1.00 15.07  ? 88  PHE A CE1   1 
ATOM   895  C  CE2   . PHE A 1 126 ? 11.196  3.500   6.319   1.00 16.95  ? 88  PHE A CE2   1 
ATOM   896  C  CZ    . PHE A 1 126 ? 12.263  2.969   7.037   1.00 23.74  ? 88  PHE A CZ    1 
ATOM   897  N  N     . PHE A 1 127 ? 5.842   -0.337  8.903   1.00 17.42  ? 89  PHE A N     1 
ATOM   898  C  CA    . PHE A 1 127 ? 4.411   -0.624  8.919   1.00 23.45  ? 89  PHE A CA    1 
ATOM   899  C  C     . PHE A 1 127 ? 3.595   0.596   9.340   1.00 29.35  ? 89  PHE A C     1 
ATOM   900  O  O     . PHE A 1 127 ? 2.455   0.765   8.889   1.00 29.77  ? 89  PHE A O     1 
ATOM   901  C  CB    . PHE A 1 127 ? 4.111   -1.781  9.856   1.00 17.70  ? 89  PHE A CB    1 
ATOM   902  C  CG    . PHE A 1 127 ? 4.656   -3.102  9.411   1.00 21.64  ? 89  PHE A CG    1 
ATOM   903  C  CD1   . PHE A 1 127 ? 5.603   -3.199  8.399   1.00 23.73  ? 89  PHE A CD1   1 
ATOM   904  C  CD2   . PHE A 1 127 ? 4.198   -4.269  10.006  1.00 19.24  ? 89  PHE A CD2   1 
ATOM   905  C  CE1   . PHE A 1 127 ? 6.086   -4.439  7.996   1.00 27.92  ? 89  PHE A CE1   1 
ATOM   906  C  CE2   . PHE A 1 127 ? 4.680   -5.516  9.612   1.00 22.64  ? 89  PHE A CE2   1 
ATOM   907  C  CZ    . PHE A 1 127 ? 5.618   -5.607  8.612   1.00 15.36  ? 89  PHE A CZ    1 
ATOM   908  N  N     A ARG A 1 128 ? 4.163   1.453   10.195  0.60 30.54  ? 90  ARG A N     1 
ATOM   909  N  N     B ARG A 1 128 ? 4.154   1.448   10.205  0.40 30.53  ? 90  ARG A N     1 
ATOM   910  C  CA    A ARG A 1 128 ? 3.454   2.640   10.662  0.60 31.75  ? 90  ARG A CA    1 
ATOM   911  C  CA    B ARG A 1 128 ? 3.433   2.637   10.647  0.40 31.76  ? 90  ARG A CA    1 
ATOM   912  C  C     A ARG A 1 128 ? 3.013   3.530   9.504   0.60 34.36  ? 90  ARG A C     1 
ATOM   913  C  C     B ARG A 1 128 ? 2.963   3.470   9.463   0.40 34.31  ? 90  ARG A C     1 
ATOM   914  O  O     A ARG A 1 128 ? 1.951   4.159   9.574   0.60 31.82  ? 90  ARG A O     1 
ATOM   915  O  O     B ARG A 1 128 ? 1.844   3.997   9.468   0.40 31.90  ? 90  ARG A O     1 
ATOM   916  C  CB    A ARG A 1 128 ? 4.341   3.407   11.647  0.60 32.89  ? 90  ARG A CB    1 
ATOM   917  C  CB    B ARG A 1 128 ? 4.314   3.473   11.575  0.40 32.90  ? 90  ARG A CB    1 
ATOM   918  C  CG    A ARG A 1 128 ? 4.002   4.885   11.835  0.60 34.92  ? 90  ARG A CG    1 
ATOM   919  C  CG    B ARG A 1 128 ? 3.891   4.934   11.686  0.40 34.87  ? 90  ARG A CG    1 
ATOM   920  C  CD    A ARG A 1 128 ? 5.038   5.602   12.716  0.60 34.73  ? 90  ARG A CD    1 
ATOM   921  C  CD    B ARG A 1 128 ? 4.874   5.729   12.531  0.40 34.50  ? 90  ARG A CD    1 
ATOM   922  N  NE    A ARG A 1 128 ? 6.424   5.304   12.356  0.60 29.09  ? 90  ARG A NE    1 
ATOM   923  N  NE    B ARG A 1 128 ? 5.089   5.092   13.828  0.40 36.20  ? 90  ARG A NE    1 
ATOM   924  C  CZ    A ARG A 1 128 ? 7.221   4.497   13.051  0.60 28.75  ? 90  ARG A CZ    1 
ATOM   925  C  CZ    B ARG A 1 128 ? 4.215   5.117   14.828  0.40 28.01  ? 90  ARG A CZ    1 
ATOM   926  N  NH1   A ARG A 1 128 ? 8.469   4.288   12.647  0.60 25.52  ? 90  ARG A NH1   1 
ATOM   927  N  NH1   B ARG A 1 128 ? 4.508   4.515   15.958  0.40 29.19  ? 90  ARG A NH1   1 
ATOM   928  N  NH2   A ARG A 1 128 ? 6.767   3.894   14.147  0.60 29.43  ? 90  ARG A NH2   1 
ATOM   929  N  NH2   B ARG A 1 128 ? 3.064   5.764   14.708  0.40 25.16  ? 90  ARG A NH2   1 
ATOM   930  N  N     . ASP A 1 129 ? 3.789   3.576   8.423   1.00 34.96  ? 91  ASP A N     1 
ATOM   931  C  CA    . ASP A 1 129 ? 3.393   4.370   7.273   1.00 43.84  ? 91  ASP A CA    1 
ATOM   932  C  C     . ASP A 1 129 ? 2.445   3.644   6.317   1.00 29.95  ? 91  ASP A C     1 
ATOM   933  O  O     . ASP A 1 129 ? 1.765   4.308   5.533   1.00 34.55  ? 91  ASP A O     1 
ATOM   934  C  CB    . ASP A 1 129 ? 4.627   4.862   6.515   1.00 36.47  ? 91  ASP A CB    1 
ATOM   935  C  CG    . ASP A 1 129 ? 4.452   6.276   6.007   1.00 40.02  ? 91  ASP A CG    1 
ATOM   936  O  OD1   . ASP A 1 129 ? 3.639   7.019   6.611   1.00 41.50  ? 91  ASP A OD1   1 
ATOM   937  O  OD2   . ASP A 1 129 ? 5.100   6.636   4.997   1.00 38.09  ? 91  ASP A OD2   1 
ATOM   938  N  N     . ALA A 1 130 ? 2.340   2.322   6.379   1.00 28.44  ? 92  ALA A N     1 
ATOM   939  C  CA    . ALA A 1 130 ? 1.620   1.580   5.347   1.00 23.06  ? 92  ALA A CA    1 
ATOM   940  C  C     . ALA A 1 130 ? 0.117   1.567   5.613   1.00 28.17  ? 92  ALA A C     1 
ATOM   941  O  O     . ALA A 1 130 ? -0.324  1.084   6.660   1.00 35.06  ? 92  ALA A O     1 
ATOM   942  C  CB    . ALA A 1 130 ? 2.162   0.154   5.273   1.00 30.00  ? 92  ALA A CB    1 
ATOM   943  N  N     . MET A 1 131 ? -0.681  2.061   4.657   1.00 25.28  ? 93  MET A N     1 
ATOM   944  C  CA    . MET A 1 131 ? -2.136  1.942   4.760   1.00 24.08  ? 93  MET A CA    1 
ATOM   945  C  C     . MET A 1 131 ? -2.661  0.584   4.300   1.00 24.16  ? 93  MET A C     1 
ATOM   946  O  O     . MET A 1 131 ? -3.881  0.373   4.294   1.00 22.79  ? 93  MET A O     1 
ATOM   947  C  CB    . MET A 1 131 ? -2.836  3.046   3.955   1.00 25.28  ? 93  MET A CB    1 
ATOM   948  C  CG    . MET A 1 131 ? -2.192  4.431   4.050   1.00 23.74  ? 93  MET A CG    1 
ATOM   949  S  SD    . MET A 1 131 ? -3.152  5.686   3.163   1.00 30.11  ? 93  MET A SD    1 
ATOM   950  C  CE    . MET A 1 131 ? -2.465  7.197   3.816   1.00 32.30  ? 93  MET A CE    1 
ATOM   951  N  N     . GLY A 1 132 ? -1.780  -0.342  3.943   1.00 17.41  ? 94  GLY A N     1 
ATOM   952  C  CA    . GLY A 1 132 ? -2.188  -1.633  3.409   1.00 16.56  ? 94  GLY A CA    1 
ATOM   953  C  C     . GLY A 1 132 ? -0.950  -2.396  2.992   1.00 23.20  ? 94  GLY A C     1 
ATOM   954  O  O     . GLY A 1 132 ? 0.157   -1.850  2.952   1.00 25.07  ? 94  GLY A O     1 
ATOM   955  N  N     . PHE A 1 133 ? -1.147  -3.681  2.683   1.00 23.61  ? 95  PHE A N     1 
ATOM   956  C  CA    . PHE A 1 133 ? -0.025  -4.586  2.470   1.00 25.04  ? 95  PHE A CA    1 
ATOM   957  C  C     . PHE A 1 133 ? -0.259  -5.460  1.255   1.00 24.49  ? 95  PHE A C     1 
ATOM   958  O  O     . PHE A 1 133 ? -1.383  -5.862  0.962   1.00 20.42  ? 95  PHE A O     1 
ATOM   959  C  CB    . PHE A 1 133 ? 0.226   -5.480  3.689   1.00 24.06  ? 95  PHE A CB    1 
ATOM   960  C  CG    . PHE A 1 133 ? 0.530   -4.705  4.917   1.00 20.58  ? 95  PHE A CG    1 
ATOM   961  C  CD1   . PHE A 1 133 ? 1.782   -4.187  5.109   1.00 9.35   ? 95  PHE A CD1   1 
ATOM   962  C  CD2   . PHE A 1 133 ? -0.458  -4.445  5.844   1.00 18.48  ? 95  PHE A CD2   1 
ATOM   963  C  CE1   . PHE A 1 133 ? 2.066   -3.455  6.219   1.00 24.73  ? 95  PHE A CE1   1 
ATOM   964  C  CE2   . PHE A 1 133 ? -0.185  -3.710  6.938   1.00 21.28  ? 95  PHE A CE2   1 
ATOM   965  C  CZ    . PHE A 1 133 ? 1.082   -3.210  7.136   1.00 24.67  ? 95  PHE A CZ    1 
ATOM   966  N  N     . LEU A 1 134 ? 0.827   -5.769  0.574   1.00 14.71  ? 96  LEU A N     1 
ATOM   967  C  CA    . LEU A 1 134 ? 0.803   -6.643  -0.585  1.00 20.67  ? 96  LEU A CA    1 
ATOM   968  C  C     . LEU A 1 134 ? 1.703   -7.837  -0.271  1.00 19.71  ? 96  LEU A C     1 
ATOM   969  O  O     . LEU A 1 134 ? 2.923   -7.759  -0.417  1.00 19.73  ? 96  LEU A O     1 
ATOM   970  C  CB    . LEU A 1 134 ? 1.250   -5.864  -1.809  1.00 24.15  ? 96  LEU A CB    1 
ATOM   971  C  CG    . LEU A 1 134 ? 1.066   -6.495  -3.176  1.00 25.21  ? 96  LEU A CG    1 
ATOM   972  C  CD1   . LEU A 1 134 ? -0.290  -6.151  -3.741  1.00 20.51  ? 96  LEU A CD1   1 
ATOM   973  C  CD2   . LEU A 1 134 ? 2.160   -5.939  -4.024  1.00 8.01   ? 96  LEU A CD2   1 
ATOM   974  N  N     . LEU A 1 135 ? 1.096   -8.929  0.189   1.00 16.85  ? 97  LEU A N     1 
ATOM   975  C  CA    . LEU A 1 135 ? 1.825   -10.122 0.591   1.00 15.42  ? 97  LEU A CA    1 
ATOM   976  C  C     . LEU A 1 135 ? 2.176   -10.971 -0.621  1.00 17.90  ? 97  LEU A C     1 
ATOM   977  O  O     . LEU A 1 135 ? 1.286   -11.368 -1.384  1.00 21.70  ? 97  LEU A O     1 
ATOM   978  C  CB    . LEU A 1 135 ? 0.971   -10.948 1.562   1.00 15.14  ? 97  LEU A CB    1 
ATOM   979  C  CG    . LEU A 1 135 ? 1.674   -11.979 2.443   1.00 23.93  ? 97  LEU A CG    1 
ATOM   980  C  CD1   . LEU A 1 135 ? 3.082   -11.562 2.803   1.00 10.75  ? 97  LEU A CD1   1 
ATOM   981  C  CD2   . LEU A 1 135 ? 0.868   -12.161 3.710   1.00 21.88  ? 97  LEU A CD2   1 
ATOM   982  N  N     . LEU A 1 136 ? 3.456   -11.301 -0.772  1.00 11.13  ? 98  LEU A N     1 
ATOM   983  C  CA    . LEU A 1 136 ? 3.918   -12.131 -1.878  1.00 12.84  ? 98  LEU A CA    1 
ATOM   984  C  C     . LEU A 1 136 ? 4.478   -13.452 -1.384  1.00 16.78  ? 98  LEU A C     1 
ATOM   985  O  O     . LEU A 1 136 ? 5.180   -13.497 -0.368  1.00 17.84  ? 98  LEU A O     1 
ATOM   986  C  CB    . LEU A 1 136 ? 5.000   -11.424 -2.694  1.00 12.10  ? 98  LEU A CB    1 
ATOM   987  C  CG    . LEU A 1 136 ? 4.519   -10.746 -3.964  1.00 18.30  ? 98  LEU A CG    1 
ATOM   988  C  CD1   . LEU A 1 136 ? 3.701   -9.522  -3.612  1.00 12.24  ? 98  LEU A CD1   1 
ATOM   989  C  CD2   . LEU A 1 136 ? 5.730   -10.359 -4.775  1.00 15.83  ? 98  LEU A CD2   1 
ATOM   990  N  N     . PHE A 1 137 ? 4.157   -14.525 -2.105  1.00 15.46  ? 99  PHE A N     1 
ATOM   991  C  CA    . PHE A 1 137 ? 4.963   -15.737 -2.089  1.00 14.22  ? 99  PHE A CA    1 
ATOM   992  C  C     . PHE A 1 137 ? 5.371   -16.043 -3.524  1.00 17.22  ? 99  PHE A C     1 
ATOM   993  O  O     . PHE A 1 137 ? 4.931   -15.384 -4.468  1.00 13.36  ? 99  PHE A O     1 
ATOM   994  C  CB    . PHE A 1 137 ? 4.225   -16.924 -1.441  1.00 15.22  ? 99  PHE A CB    1 
ATOM   995  C  CG    . PHE A 1 137 ? 2.975   -17.336 -2.159  1.00 13.16  ? 99  PHE A CG    1 
ATOM   996  C  CD1   . PHE A 1 137 ? 1.767   -16.714 -1.878  1.00 11.52  ? 99  PHE A CD1   1 
ATOM   997  C  CD2   . PHE A 1 137 ? 3.006   -18.338 -3.124  1.00 12.49  ? 99  PHE A CD2   1 
ATOM   998  C  CE1   . PHE A 1 137 ? 0.606   -17.093 -2.530  1.00 11.86  ? 99  PHE A CE1   1 
ATOM   999  C  CE2   . PHE A 1 137 ? 1.852   -18.731 -3.780  1.00 10.79  ? 99  PHE A CE2   1 
ATOM   1000 C  CZ    . PHE A 1 137 ? 0.651   -18.104 -3.493  1.00 12.81  ? 99  PHE A CZ    1 
ATOM   1001 N  N     . ASP A 1 138 ? 6.245   -17.032 -3.675  1.00 16.97  ? 100 ASP A N     1 
ATOM   1002 C  CA    . ASP A 1 138 ? 6.711   -17.497 -4.977  1.00 19.40  ? 100 ASP A CA    1 
ATOM   1003 C  C     . ASP A 1 138 ? 5.921   -18.733 -5.376  1.00 16.71  ? 100 ASP A C     1 
ATOM   1004 O  O     . ASP A 1 138 ? 5.853   -19.690 -4.603  1.00 24.60  ? 100 ASP A O     1 
ATOM   1005 C  CB    . ASP A 1 138 ? 8.199   -17.836 -4.904  1.00 24.80  ? 100 ASP A CB    1 
ATOM   1006 C  CG    . ASP A 1 138 ? 8.819   -18.157 -6.262  1.00 22.67  ? 100 ASP A CG    1 
ATOM   1007 O  OD1   . ASP A 1 138 ? 8.151   -18.761 -7.135  1.00 24.77  ? 100 ASP A OD1   1 
ATOM   1008 O  OD2   . ASP A 1 138 ? 10.016  -17.841 -6.425  1.00 13.42  ? 100 ASP A OD2   1 
ATOM   1009 N  N     . LEU A 1 139 ? 5.349   -18.733 -6.590  1.00 15.55  ? 101 LEU A N     1 
ATOM   1010 C  CA    . LEU A 1 139 ? 4.604   -19.917 -7.023  1.00 12.93  ? 101 LEU A CA    1 
ATOM   1011 C  C     . LEU A 1 139 ? 5.513   -21.138 -7.133  1.00 18.24  ? 101 LEU A C     1 
ATOM   1012 O  O     . LEU A 1 139 ? 5.047   -22.273 -6.988  1.00 19.07  ? 101 LEU A O     1 
ATOM   1013 C  CB    . LEU A 1 139 ? 3.884   -19.651 -8.349  1.00 17.41  ? 101 LEU A CB    1 
ATOM   1014 C  CG    . LEU A 1 139 ? 2.660   -18.735 -8.170  1.00 27.22  ? 101 LEU A CG    1 
ATOM   1015 C  CD1   . LEU A 1 139 ? 1.971   -18.373 -9.484  1.00 11.07  ? 101 LEU A CD1   1 
ATOM   1016 C  CD2   . LEU A 1 139 ? 1.648   -19.309 -7.174  1.00 18.20  ? 101 LEU A CD2   1 
ATOM   1017 N  N     . THR A 1 140 ? 6.810   -20.929 -7.346  1.00 20.83  ? 102 THR A N     1 
ATOM   1018 C  CA    . THR A 1 140 ? 7.771   -22.012 -7.518  1.00 18.54  ? 102 THR A CA    1 
ATOM   1019 C  C     . THR A 1 140 ? 8.536   -22.360 -6.240  1.00 22.34  ? 102 THR A C     1 
ATOM   1020 O  O     . THR A 1 140 ? 9.479   -23.150 -6.305  1.00 20.56  ? 102 THR A O     1 
ATOM   1021 C  CB    . THR A 1 140 ? 8.779   -21.649 -8.606  1.00 23.11  ? 102 THR A CB    1 
ATOM   1022 O  OG1   . THR A 1 140 ? 9.726   -20.703 -8.084  1.00 23.57  ? 102 THR A OG1   1 
ATOM   1023 C  CG2   . THR A 1 140 ? 8.078   -21.052 -9.814  1.00 18.72  ? 102 THR A CG2   1 
ATOM   1024 N  N     . ASN A 1 141 ? 8.180   -21.783 -5.094  1.00 17.14  ? 103 ASN A N     1 
ATOM   1025 C  CA    . ASN A 1 141 ? 8.857   -22.073 -3.826  1.00 18.00  ? 103 ASN A CA    1 
ATOM   1026 C  C     . ASN A 1 141 ? 7.816   -22.341 -2.729  1.00 20.47  ? 103 ASN A C     1 
ATOM   1027 O  O     . ASN A 1 141 ? 7.216   -21.403 -2.190  1.00 21.56  ? 103 ASN A O     1 
ATOM   1028 C  CB    . ASN A 1 141 ? 9.794   -20.922 -3.441  1.00 18.99  ? 103 ASN A CB    1 
ATOM   1029 C  CG    . ASN A 1 141 ? 10.532  -21.187 -2.137  1.00 20.17  ? 103 ASN A CG    1 
ATOM   1030 O  OD1   . ASN A 1 141 ? 9.923   -21.532 -1.125  1.00 25.68  ? 103 ASN A OD1   1 
ATOM   1031 N  ND2   . ASN A 1 141 ? 11.851  -21.049 -2.161  1.00 10.92  ? 103 ASN A ND2   1 
ATOM   1032 N  N     . GLU A 1 142 ? 7.624   -23.617 -2.368  1.00 16.27  ? 104 GLU A N     1 
ATOM   1033 C  CA    . GLU A 1 142 ? 6.579   -23.963 -1.408  1.00 22.15  ? 104 GLU A CA    1 
ATOM   1034 C  C     . GLU A 1 142 ? 6.837   -23.318 -0.049  1.00 22.04  ? 104 GLU A C     1 
ATOM   1035 O  O     . GLU A 1 142 ? 5.902   -22.845 0.610   1.00 21.43  ? 104 GLU A O     1 
ATOM   1036 C  CB    . GLU A 1 142 ? 6.457   -25.490 -1.285  1.00 26.45  ? 104 GLU A CB    1 
ATOM   1037 C  CG    . GLU A 1 142 ? 5.388   -25.996 -0.270  1.00 17.98  ? 104 GLU A CG    1 
ATOM   1038 C  CD    . GLU A 1 142 ? 3.953   -25.815 -0.738  1.00 37.78  ? 104 GLU A CD    1 
ATOM   1039 O  OE1   . GLU A 1 142 ? 3.706   -25.849 -1.970  1.00 44.11  ? 104 GLU A OE1   1 
ATOM   1040 O  OE2   . GLU A 1 142 ? 3.065   -25.645 0.132   1.00 35.62  ? 104 GLU A OE2   1 
ATOM   1041 N  N     . GLN A 1 143 ? 8.098   -23.262 0.379   1.00 19.07  ? 105 GLN A N     1 
ATOM   1042 C  CA    . GLN A 1 143 ? 8.382   -22.661 1.672   1.00 15.56  ? 105 GLN A CA    1 
ATOM   1043 C  C     . GLN A 1 143 ? 8.028   -21.186 1.703   1.00 20.76  ? 105 GLN A C     1 
ATOM   1044 O  O     . GLN A 1 143 ? 7.689   -20.662 2.765   1.00 19.82  ? 105 GLN A O     1 
ATOM   1045 C  CB    . GLN A 1 143 ? 9.845   -22.836 2.051   1.00 17.83  ? 105 GLN A CB    1 
ATOM   1046 C  CG    . GLN A 1 143 ? 10.142  -22.391 3.485   1.00 32.56  ? 105 GLN A CG    1 
ATOM   1047 C  CD    . GLN A 1 143 ? 9.467   -23.273 4.547   1.00 21.10  ? 105 GLN A CD    1 
ATOM   1048 O  OE1   . GLN A 1 143 ? 9.692   -24.490 4.605   1.00 16.90  ? 105 GLN A OE1   1 
ATOM   1049 N  NE2   . GLN A 1 143 ? 8.647   -22.655 5.400   1.00 26.38  ? 105 GLN A NE2   1 
ATOM   1050 N  N     . SER A 1 144 ? 8.125   -20.489 0.571   1.00 21.02  ? 106 SER A N     1 
ATOM   1051 C  CA    . SER A 1 144 ? 7.682   -19.104 0.570   1.00 16.08  ? 106 SER A CA    1 
ATOM   1052 C  C     . SER A 1 144 ? 6.185   -19.022 0.787   1.00 15.63  ? 106 SER A C     1 
ATOM   1053 O  O     . SER A 1 144 ? 5.698   -18.063 1.400   1.00 23.97  ? 106 SER A O     1 
ATOM   1054 C  CB    . SER A 1 144 ? 8.070   -18.413 -0.737  1.00 19.10  ? 106 SER A CB    1 
ATOM   1055 O  OG    . SER A 1 144 ? 7.172   -18.752 -1.796  1.00 23.45  ? 106 SER A OG    1 
ATOM   1056 N  N     . PHE A 1 145 ? 5.441   -20.016 0.307   1.00 15.34  ? 107 PHE A N     1 
ATOM   1057 C  CA    . PHE A 1 145 ? 4.001   -19.980 0.488   1.00 13.25  ? 107 PHE A CA    1 
ATOM   1058 C  C     . PHE A 1 145 ? 3.626   -20.398 1.907   1.00 18.96  ? 107 PHE A C     1 
ATOM   1059 O  O     . PHE A 1 145 ? 2.711   -19.821 2.510   1.00 15.51  ? 107 PHE A O     1 
ATOM   1060 C  CB    . PHE A 1 145 ? 3.323   -20.863 -0.551  1.00 11.79  ? 107 PHE A CB    1 
ATOM   1061 C  CG    . PHE A 1 145 ? 1.940   -21.277 -0.165  1.00 13.78  ? 107 PHE A CG    1 
ATOM   1062 C  CD1   . PHE A 1 145 ? 0.890   -20.407 -0.296  1.00 16.38  ? 107 PHE A CD1   1 
ATOM   1063 C  CD2   . PHE A 1 145 ? 1.706   -22.524 0.373   1.00 11.14  ? 107 PHE A CD2   1 
ATOM   1064 C  CE1   . PHE A 1 145 ? -0.376  -20.780 0.073   1.00 15.91  ? 107 PHE A CE1   1 
ATOM   1065 C  CE2   . PHE A 1 145 ? 0.449   -22.900 0.756   1.00 19.98  ? 107 PHE A CE2   1 
ATOM   1066 C  CZ    . PHE A 1 145 ? -0.594  -22.029 0.608   1.00 21.74  ? 107 PHE A CZ    1 
ATOM   1067 N  N     . LEU A 1 146 ? 4.333   -21.386 2.460   1.00 14.85  ? 108 LEU A N     1 
ATOM   1068 C  CA    . LEU A 1 146 ? 4.081   -21.794 3.836   1.00 21.40  ? 108 LEU A CA    1 
ATOM   1069 C  C     . LEU A 1 146 ? 4.415   -20.682 4.818   1.00 20.22  ? 108 LEU A C     1 
ATOM   1070 O  O     . LEU A 1 146 ? 3.798   -20.591 5.880   1.00 24.74  ? 108 LEU A O     1 
ATOM   1071 C  CB    . LEU A 1 146 ? 4.892   -23.041 4.180   1.00 19.00  ? 108 LEU A CB    1 
ATOM   1072 C  CG    . LEU A 1 146 ? 4.562   -24.321 3.430   1.00 22.25  ? 108 LEU A CG    1 
ATOM   1073 C  CD1   . LEU A 1 146 ? 5.283   -25.468 4.087   1.00 13.99  ? 108 LEU A CD1   1 
ATOM   1074 C  CD2   . LEU A 1 146 ? 3.057   -24.570 3.364   1.00 22.11  ? 108 LEU A CD2   1 
ATOM   1075 N  N     . ASN A 1 147 ? 5.388   -19.838 4.495   1.00 19.73  ? 109 ASN A N     1 
ATOM   1076 C  CA    . ASN A 1 147 ? 5.690   -18.737 5.390   1.00 22.53  ? 109 ASN A CA    1 
ATOM   1077 C  C     . ASN A 1 147 ? 4.579   -17.704 5.441   1.00 21.69  ? 109 ASN A C     1 
ATOM   1078 O  O     . ASN A 1 147 ? 4.558   -16.907 6.383   1.00 16.86  ? 109 ASN A O     1 
ATOM   1079 C  CB    . ASN A 1 147 ? 6.991   -18.079 4.970   1.00 21.67  ? 109 ASN A CB    1 
ATOM   1080 C  CG    . ASN A 1 147 ? 8.193   -18.889 5.371   1.00 21.58  ? 109 ASN A CG    1 
ATOM   1081 O  OD1   . ASN A 1 147 ? 8.088   -19.824 6.163   1.00 25.55  ? 109 ASN A OD1   1 
ATOM   1082 N  ND2   . ASN A 1 147 ? 9.346   -18.540 4.829   1.00 26.98  ? 109 ASN A ND2   1 
ATOM   1083 N  N     . VAL A 1 148 ? 3.651   -17.721 4.477   1.00 20.69  ? 110 VAL A N     1 
ATOM   1084 C  CA    . VAL A 1 148 ? 2.624   -16.679 4.407   1.00 18.85  ? 110 VAL A CA    1 
ATOM   1085 C  C     . VAL A 1 148 ? 1.945   -16.504 5.764   1.00 20.44  ? 110 VAL A C     1 
ATOM   1086 O  O     . VAL A 1 148 ? 1.842   -15.389 6.292   1.00 23.33  ? 110 VAL A O     1 
ATOM   1087 C  CB    . VAL A 1 148 ? 1.607   -17.001 3.302   1.00 12.91  ? 110 VAL A CB    1 
ATOM   1088 C  CG1   . VAL A 1 148 ? 0.390   -16.090 3.419   1.00 12.43  ? 110 VAL A CG1   1 
ATOM   1089 C  CG2   . VAL A 1 148 ? 2.248   -16.847 1.921   1.00 17.45  ? 110 VAL A CG2   1 
ATOM   1090 N  N     . ARG A 1 149 ? 1.507   -17.610 6.364   1.00 23.16  ? 111 ARG A N     1 
ATOM   1091 C  CA    . ARG A 1 149 ? 0.836   -17.555 7.657   1.00 18.66  ? 111 ARG A CA    1 
ATOM   1092 C  C     . ARG A 1 149 ? 1.625   -16.713 8.662   1.00 29.41  ? 111 ARG A C     1 
ATOM   1093 O  O     . ARG A 1 149 ? 1.096   -15.745 9.215   1.00 30.08  ? 111 ARG A O     1 
ATOM   1094 C  CB    . ARG A 1 149 ? 0.600   -18.976 8.171   1.00 21.41  ? 111 ARG A CB    1 
ATOM   1095 C  CG    . ARG A 1 149 ? 0.031   -19.056 9.604   1.00 52.34  ? 111 ARG A CG    1 
ATOM   1096 C  CD    . ARG A 1 149 ? -1.023  -17.963 9.879   1.00 52.77  ? 111 ARG A CD    1 
ATOM   1097 N  NE    . ARG A 1 149 ? -1.293  -17.713 11.300  1.00 56.64  ? 111 ARG A NE    1 
ATOM   1098 C  CZ    . ARG A 1 149 ? -1.692  -16.542 11.803  1.00 53.03  ? 111 ARG A CZ    1 
ATOM   1099 N  NH1   . ARG A 1 149 ? -1.918  -16.427 13.109  1.00 53.87  ? 111 ARG A NH1   1 
ATOM   1100 N  NH2   . ARG A 1 149 ? -1.860  -15.484 11.014  1.00 30.19  ? 111 ARG A NH2   1 
ATOM   1101 N  N     . ASN A 1 150 ? 2.901   -17.056 8.901   1.00 29.65  ? 112 ASN A N     1 
ATOM   1102 C  CA    . ASN A 1 150 ? 3.726   -16.252 9.807   1.00 25.01  ? 112 ASN A CA    1 
ATOM   1103 C  C     . ASN A 1 150 ? 3.735   -14.790 9.387   1.00 26.00  ? 112 ASN A C     1 
ATOM   1104 O  O     . ASN A 1 150 ? 3.734   -13.891 10.234  1.00 25.04  ? 112 ASN A O     1 
ATOM   1105 C  CB    . ASN A 1 150 ? 5.169   -16.764 9.856   1.00 33.19  ? 112 ASN A CB    1 
ATOM   1106 C  CG    . ASN A 1 150 ? 5.267   -18.238 10.182  1.00 36.50  ? 112 ASN A CG    1 
ATOM   1107 O  OD1   . ASN A 1 150 ? 4.369   -18.815 10.805  1.00 30.14  ? 112 ASN A OD1   1 
ATOM   1108 N  ND2   . ASN A 1 150 ? 6.379   -18.856 9.780   1.00 31.31  ? 112 ASN A ND2   1 
ATOM   1109 N  N     . TRP A 1 151 ? 3.748   -14.529 8.084   1.00 23.17  ? 113 TRP A N     1 
ATOM   1110 C  CA    . TRP A 1 151 ? 3.718   -13.146 7.640   1.00 25.70  ? 113 TRP A CA    1 
ATOM   1111 C  C     . TRP A 1 151 ? 2.418   -12.475 8.046   1.00 16.24  ? 113 TRP A C     1 
ATOM   1112 O  O     . TRP A 1 151 ? 2.410   -11.303 8.430   1.00 25.54  ? 113 TRP A O     1 
ATOM   1113 C  CB    . TRP A 1 151 ? 3.906   -13.071 6.130   1.00 18.59  ? 113 TRP A CB    1 
ATOM   1114 C  CG    . TRP A 1 151 ? 5.326   -13.138 5.687   1.00 20.48  ? 113 TRP A CG    1 
ATOM   1115 C  CD1   . TRP A 1 151 ? 5.913   -14.138 4.968   1.00 15.54  ? 113 TRP A CD1   1 
ATOM   1116 C  CD2   . TRP A 1 151 ? 6.342   -12.150 5.905   1.00 27.03  ? 113 TRP A CD2   1 
ATOM   1117 N  NE1   . TRP A 1 151 ? 7.233   -13.835 4.724   1.00 17.19  ? 113 TRP A NE1   1 
ATOM   1118 C  CE2   . TRP A 1 151 ? 7.520   -12.618 5.284   1.00 18.49  ? 113 TRP A CE2   1 
ATOM   1119 C  CE3   . TRP A 1 151 ? 6.371   -10.916 6.564   1.00 18.95  ? 113 TRP A CE3   1 
ATOM   1120 C  CZ2   . TRP A 1 151 ? 8.709   -11.900 5.306   1.00 18.18  ? 113 TRP A CZ2   1 
ATOM   1121 C  CZ3   . TRP A 1 151 ? 7.555   -10.205 6.582   1.00 21.50  ? 113 TRP A CZ3   1 
ATOM   1122 C  CH2   . TRP A 1 151 ? 8.705   -10.698 5.957   1.00 20.44  ? 113 TRP A CH2   1 
ATOM   1123 N  N     . ILE A 1 152 ? 1.305   -13.188 7.962   1.00 18.88  ? 114 ILE A N     1 
ATOM   1124 C  CA    . ILE A 1 152 ? 0.049   -12.530 8.287   1.00 19.70  ? 114 ILE A CA    1 
ATOM   1125 C  C     . ILE A 1 152 ? -0.025  -12.230 9.785   1.00 28.54  ? 114 ILE A C     1 
ATOM   1126 O  O     . ILE A 1 152 ? -0.455  -11.142 10.182  1.00 25.85  ? 114 ILE A O     1 
ATOM   1127 C  CB    . ILE A 1 152 ? -1.133  -13.367 7.781   1.00 22.54  ? 114 ILE A CB    1 
ATOM   1128 C  CG1   . ILE A 1 152 ? -1.366  -13.048 6.300   1.00 22.63  ? 114 ILE A CG1   1 
ATOM   1129 C  CG2   . ILE A 1 152 ? -2.395  -13.061 8.575   1.00 20.15  ? 114 ILE A CG2   1 
ATOM   1130 C  CD1   . ILE A 1 152 ? -2.041  -14.162 5.504   1.00 18.73  ? 114 ILE A CD1   1 
ATOM   1131 N  N     . SER A 1 153 ? 0.453   -13.151 10.638  1.00 20.73  ? 115 SER A N     1 
ATOM   1132 C  CA    . SER A 1 153 ? 0.480   -12.876 12.072  1.00 24.13  ? 115 SER A CA    1 
ATOM   1133 C  C     . SER A 1 153 ? 1.419   -11.723 12.398  1.00 23.31  ? 115 SER A C     1 
ATOM   1134 O  O     . SER A 1 153 ? 1.096   -10.870 13.230  1.00 18.16  ? 115 SER A O     1 
ATOM   1135 C  CB    . SER A 1 153 ? 0.883   -14.116 12.851  1.00 21.63  ? 115 SER A CB    1 
ATOM   1136 O  OG    . SER A 1 153 ? 1.853   -14.842 12.149  1.00 31.89  ? 115 SER A OG    1 
ATOM   1137 N  N     . GLN A 1 154 ? 2.576   -11.675 11.742  1.00 25.55  ? 116 GLN A N     1 
ATOM   1138 C  CA    . GLN A 1 154 ? 3.414   -10.488 11.811  1.00 13.32  ? 116 GLN A CA    1 
ATOM   1139 C  C     . GLN A 1 154 ? 2.629   -9.231  11.450  1.00 21.79  ? 116 GLN A C     1 
ATOM   1140 O  O     . GLN A 1 154 ? 2.838   -8.168  12.043  1.00 25.13  ? 116 GLN A O     1 
ATOM   1141 C  CB    . GLN A 1 154 ? 4.612   -10.649 10.879  1.00 27.01  ? 116 GLN A CB    1 
ATOM   1142 C  CG    . GLN A 1 154 ? 5.748   -11.458 11.451  1.00 29.00  ? 116 GLN A CG    1 
ATOM   1143 C  CD    . GLN A 1 154 ? 6.610   -10.625 12.365  1.00 41.66  ? 116 GLN A CD    1 
ATOM   1144 O  OE1   . GLN A 1 154 ? 7.682   -10.154 11.965  1.00 39.35  ? 116 GLN A OE1   1 
ATOM   1145 N  NE2   . GLN A 1 154 ? 6.140   -10.417 13.599  1.00 24.00  ? 116 GLN A NE2   1 
ATOM   1146 N  N     . LEU A 1 155 ? 1.733   -9.322  10.464  1.00 15.86  ? 117 LEU A N     1 
ATOM   1147 C  CA    . LEU A 1 155 ? 0.980   -8.142  10.058  1.00 21.54  ? 117 LEU A CA    1 
ATOM   1148 C  C     . LEU A 1 155 ? -0.062  -7.776  11.108  1.00 23.65  ? 117 LEU A C     1 
ATOM   1149 O  O     . LEU A 1 155 ? -0.198  -6.603  11.482  1.00 25.97  ? 117 LEU A O     1 
ATOM   1150 C  CB    . LEU A 1 155 ? 0.317   -8.379  8.696   1.00 22.21  ? 117 LEU A CB    1 
ATOM   1151 C  CG    . LEU A 1 155 ? 1.205   -8.307  7.458   1.00 23.81  ? 117 LEU A CG    1 
ATOM   1152 C  CD1   . LEU A 1 155 ? 0.467   -8.796  6.209   1.00 23.17  ? 117 LEU A CD1   1 
ATOM   1153 C  CD2   . LEU A 1 155 ? 1.691   -6.879  7.285   1.00 18.48  ? 117 LEU A CD2   1 
ATOM   1154 N  N     . GLN A 1 156 ? -0.818  -8.771  11.582  1.00 18.29  ? 118 GLN A N     1 
ATOM   1155 C  CA    . GLN A 1 156 ? -1.749  -8.552  12.688  1.00 31.60  ? 118 GLN A CA    1 
ATOM   1156 C  C     . GLN A 1 156 ? -1.046  -7.911  13.884  1.00 33.72  ? 118 GLN A C     1 
ATOM   1157 O  O     . GLN A 1 156 ? -1.457  -6.847  14.370  1.00 29.82  ? 118 GLN A O     1 
ATOM   1158 C  CB    . GLN A 1 156 ? -2.396  -9.878  13.103  1.00 29.45  ? 118 GLN A CB    1 
ATOM   1159 C  CG    . GLN A 1 156 ? -2.980  -10.681 11.963  1.00 21.37  ? 118 GLN A CG    1 
ATOM   1160 C  CD    . GLN A 1 156 ? -4.331  -10.160 11.538  1.00 39.55  ? 118 GLN A CD    1 
ATOM   1161 O  OE1   . GLN A 1 156 ? -5.253  -10.051 12.355  1.00 29.23  ? 118 GLN A OE1   1 
ATOM   1162 N  NE2   . GLN A 1 156 ? -4.458  -9.821  10.256  1.00 29.17  ? 118 GLN A NE2   1 
ATOM   1163 N  N     . MET A 1 157 ? 0.042   -8.535  14.351  1.00 24.97  ? 119 MET A N     1 
ATOM   1164 C  CA    . MET A 1 157 ? 0.725   -8.049  15.538  1.00 21.88  ? 119 MET A CA    1 
ATOM   1165 C  C     . MET A 1 157 ? 1.388   -6.700  15.316  1.00 28.41  ? 119 MET A C     1 
ATOM   1166 O  O     . MET A 1 157 ? 1.525   -5.919  16.261  1.00 31.26  ? 119 MET A O     1 
ATOM   1167 C  CB    . MET A 1 157 ? 1.764   -9.069  16.007  1.00 31.61  ? 119 MET A CB    1 
ATOM   1168 C  CG    . MET A 1 157 ? 2.664   -8.564  17.148  1.00 27.26  ? 119 MET A CG    1 
ATOM   1169 S  SD    . MET A 1 157 ? 4.120   -9.590  17.453  1.00 47.93  ? 119 MET A SD    1 
ATOM   1170 C  CE    . MET A 1 157 ? 3.351   -11.124 18.007  1.00 33.52  ? 119 MET A CE    1 
ATOM   1171 N  N     . HIS A 1 158 ? 1.804   -6.379  14.099  1.00 27.22  ? 120 HIS A N     1 
ATOM   1172 C  CA    . HIS A 1 158 ? 2.599   -5.171  13.957  1.00 19.10  ? 120 HIS A CA    1 
ATOM   1173 C  C     . HIS A 1 158 ? 1.942   -4.044  13.173  1.00 23.53  ? 120 HIS A C     1 
ATOM   1174 O  O     . HIS A 1 158 ? 2.444   -2.918  13.242  1.00 21.85  ? 120 HIS A O     1 
ATOM   1175 C  CB    . HIS A 1 158 ? 3.953   -5.504  13.339  1.00 27.39  ? 120 HIS A CB    1 
ATOM   1176 C  CG    . HIS A 1 158 ? 4.949   -6.006  14.334  1.00 25.97  ? 120 HIS A CG    1 
ATOM   1177 N  ND1   . HIS A 1 158 ? 5.633   -5.164  15.186  1.00 26.54  ? 120 HIS A ND1   1 
ATOM   1178 C  CD2   . HIS A 1 158 ? 5.363   -7.261  14.626  1.00 23.50  ? 120 HIS A CD2   1 
ATOM   1179 C  CE1   . HIS A 1 158 ? 6.436   -5.880  15.952  1.00 27.67  ? 120 HIS A CE1   1 
ATOM   1180 N  NE2   . HIS A 1 158 ? 6.289   -7.155  15.634  1.00 27.62  ? 120 HIS A NE2   1 
ATOM   1181 N  N     . ALA A 1 159 ? 0.849   -4.292  12.444  1.00 21.31  ? 121 ALA A N     1 
ATOM   1182 C  CA    . ALA A 1 159 ? 0.227   -3.205  11.693  1.00 18.47  ? 121 ALA A CA    1 
ATOM   1183 C  C     . ALA A 1 159 ? -0.269  -2.127  12.644  1.00 27.28  ? 121 ALA A C     1 
ATOM   1184 O  O     . ALA A 1 159 ? -0.564  -2.379  13.819  1.00 29.37  ? 121 ALA A O     1 
ATOM   1185 C  CB    . ALA A 1 159 ? -0.930  -3.715  10.837  1.00 19.27  ? 121 ALA A CB    1 
ATOM   1186 N  N     . TYR A 1 160 ? -0.349  -0.906  12.136  1.00 31.81  ? 122 TYR A N     1 
ATOM   1187 C  CA    . TYR A 1 160 ? -0.702  0.226   12.975  1.00 28.43  ? 122 TYR A CA    1 
ATOM   1188 C  C     . TYR A 1 160 ? -2.180  0.569   12.892  1.00 37.19  ? 122 TYR A C     1 
ATOM   1189 O  O     . TYR A 1 160 ? -2.627  1.526   13.538  1.00 40.46  ? 122 TYR A O     1 
ATOM   1190 C  CB    . TYR A 1 160 ? 0.184   1.426   12.630  1.00 34.42  ? 122 TYR A CB    1 
ATOM   1191 C  CG    . TYR A 1 160 ? 1.563   1.273   13.257  1.00 39.89  ? 122 TYR A CG    1 
ATOM   1192 C  CD1   . TYR A 1 160 ? 2.456   0.292   12.803  1.00 33.26  ? 122 TYR A CD1   1 
ATOM   1193 C  CD2   . TYR A 1 160 ? 1.950   2.063   14.341  1.00 31.51  ? 122 TYR A CD2   1 
ATOM   1194 C  CE1   . TYR A 1 160 ? 3.709   0.137   13.390  1.00 34.50  ? 122 TYR A CE1   1 
ATOM   1195 C  CE2   . TYR A 1 160 ? 3.190   1.909   14.936  1.00 28.10  ? 122 TYR A CE2   1 
ATOM   1196 C  CZ    . TYR A 1 160 ? 4.066   0.952   14.460  1.00 32.54  ? 122 TYR A CZ    1 
ATOM   1197 O  OH    . TYR A 1 160 ? 5.303   0.807   15.048  1.00 24.84  ? 122 TYR A OH    1 
ATOM   1198 N  N     . ALA A 1 161 ? -2.941  -0.207  12.129  1.00 26.65  ? 123 ALA A N     1 
ATOM   1199 C  CA    . ALA A 1 161 ? -4.385  -0.304  12.259  1.00 27.38  ? 123 ALA A CA    1 
ATOM   1200 C  C     . ALA A 1 161 ? -4.727  -1.785  12.323  1.00 31.66  ? 123 ALA A C     1 
ATOM   1201 O  O     . ALA A 1 161 ? -4.022  -2.619  11.749  1.00 30.38  ? 123 ALA A O     1 
ATOM   1202 C  CB    . ALA A 1 161 ? -5.120  0.376   11.099  1.00 37.74  ? 123 ALA A CB    1 
ATOM   1203 N  N     . GLU A 1 162 ? -5.784  -2.118  13.050  1.00 31.36  ? 124 GLU A N     1 
ATOM   1204 C  CA    . GLU A 1 162 ? -6.103  -3.522  13.264  1.00 39.47  ? 124 GLU A CA    1 
ATOM   1205 C  C     . GLU A 1 162 ? -6.986  -4.052  12.140  1.00 42.13  ? 124 GLU A C     1 
ATOM   1206 O  O     . GLU A 1 162 ? -7.782  -3.316  11.546  1.00 34.19  ? 124 GLU A O     1 
ATOM   1207 C  CB    . GLU A 1 162 ? -6.793  -3.717  14.616  1.00 30.00  ? 124 GLU A CB    1 
ATOM   1208 C  CG    . GLU A 1 162 ? -5.898  -3.442  15.815  1.00 30.00  ? 124 GLU A CG    1 
ATOM   1209 C  CD    . GLU A 1 162 ? -6.637  -3.576  17.133  1.00 30.00  ? 124 GLU A CD    1 
ATOM   1210 O  OE1   . GLU A 1 162 ? -7.879  -3.694  17.111  1.00 30.00  ? 124 GLU A OE1   1 
ATOM   1211 O  OE2   . GLU A 1 162 ? -5.974  -3.560  18.192  1.00 30.00  ? 124 GLU A OE2   1 
ATOM   1212 N  N     . ASN A 1 163 ? -6.822  -5.352  11.849  1.00 44.66  ? 125 ASN A N     1 
ATOM   1213 C  CA    . ASN A 1 163 ? -7.377  -6.027  10.677  1.00 36.89  ? 125 ASN A CA    1 
ATOM   1214 C  C     . ASN A 1 163 ? -6.858  -5.394  9.395   1.00 39.97  ? 125 ASN A C     1 
ATOM   1215 O  O     . ASN A 1 163 ? -7.650  -4.896  8.584   1.00 45.55  ? 125 ASN A O     1 
ATOM   1216 C  CB    . ASN A 1 163 ? -8.901  -5.986  10.672  1.00 45.29  ? 125 ASN A CB    1 
ATOM   1217 C  CG    . ASN A 1 163 ? -9.504  -7.223  11.239  1.00 50.92  ? 125 ASN A CG    1 
ATOM   1218 O  OD1   . ASN A 1 163 ? -9.622  -7.369  12.460  1.00 68.40  ? 125 ASN A OD1   1 
ATOM   1219 N  ND2   . ASN A 1 163 ? -9.876  -8.148  10.363  1.00 53.43  ? 125 ASN A ND2   1 
ATOM   1220 N  N     . PRO A 1 164 ? -5.551  -5.415  9.164   1.00 36.26  ? 126 PRO A N     1 
ATOM   1221 C  CA    . PRO A 1 164 ? -4.993  -4.656  8.040   1.00 27.08  ? 126 PRO A CA    1 
ATOM   1222 C  C     . PRO A 1 164 ? -5.472  -5.184  6.690   1.00 39.08  ? 126 PRO A C     1 
ATOM   1223 O  O     . PRO A 1 164 ? -5.742  -6.375  6.517   1.00 36.15  ? 126 PRO A O     1 
ATOM   1224 C  CB    . PRO A 1 164 ? -3.482  -4.840  8.208   1.00 31.49  ? 126 PRO A CB    1 
ATOM   1225 C  CG    . PRO A 1 164 ? -3.340  -6.125  8.978   1.00 38.85  ? 126 PRO A CG    1 
ATOM   1226 C  CD    . PRO A 1 164 ? -4.535  -6.200  9.886   1.00 29.28  ? 126 PRO A CD    1 
ATOM   1227 N  N     . ASP A 1 165 ? -5.584  -4.270  5.727   1.00 34.18  ? 127 ASP A N     1 
ATOM   1228 C  CA    . ASP A 1 165 ? -5.899  -4.663  4.361   1.00 31.74  ? 127 ASP A CA    1 
ATOM   1229 C  C     . ASP A 1 165 ? -4.684  -5.326  3.720   1.00 27.81  ? 127 ASP A C     1 
ATOM   1230 O  O     . ASP A 1 165 ? -3.574  -4.786  3.768   1.00 27.48  ? 127 ASP A O     1 
ATOM   1231 C  CB    . ASP A 1 165 ? -6.340  -3.449  3.543   1.00 23.42  ? 127 ASP A CB    1 
ATOM   1232 C  CG    . ASP A 1 165 ? -7.748  -2.981  3.894   1.00 36.97  ? 127 ASP A CG    1 
ATOM   1233 O  OD1   . ASP A 1 165 ? -8.698  -3.795  3.836   1.00 41.12  ? 127 ASP A OD1   1 
ATOM   1234 O  OD2   . ASP A 1 165 ? -7.904  -1.784  4.221   1.00 38.11  ? 127 ASP A OD2   1 
ATOM   1235 N  N     . ILE A 1 166 ? -4.895  -6.508  3.136   1.00 19.41  ? 128 ILE A N     1 
ATOM   1236 C  CA    . ILE A 1 166 ? -3.845  -7.285  2.486   1.00 25.09  ? 128 ILE A CA    1 
ATOM   1237 C  C     . ILE A 1 166 ? -4.385  -7.825  1.168   1.00 20.15  ? 128 ILE A C     1 
ATOM   1238 O  O     . ILE A 1 166 ? -5.515  -8.314  1.104   1.00 14.49  ? 128 ILE A O     1 
ATOM   1239 C  CB    . ILE A 1 166 ? -3.353  -8.459  3.371   1.00 25.02  ? 128 ILE A CB    1 
ATOM   1240 C  CG1   . ILE A 1 166 ? -2.796  -7.969  4.714   1.00 25.89  ? 128 ILE A CG1   1 
ATOM   1241 C  CG2   . ILE A 1 166 ? -2.291  -9.246  2.664   1.00 15.94  ? 128 ILE A CG2   1 
ATOM   1242 C  CD1   . ILE A 1 166 ? -3.182  -8.867  5.897   1.00 17.59  ? 128 ILE A CD1   1 
ATOM   1243 N  N     . VAL A 1 167 ? -3.576  -7.748  0.116   1.00 24.53  ? 129 VAL A N     1 
ATOM   1244 C  CA    . VAL A 1 167 ? -3.753  -8.583  -1.065  1.00 15.99  ? 129 VAL A CA    1 
ATOM   1245 C  C     . VAL A 1 167 ? -2.597  -9.568  -1.120  1.00 17.10  ? 129 VAL A C     1 
ATOM   1246 O  O     . VAL A 1 167 ? -1.445  -9.208  -0.855  1.00 18.14  ? 129 VAL A O     1 
ATOM   1247 C  CB    . VAL A 1 167 ? -3.845  -7.745  -2.350  1.00 21.87  ? 129 VAL A CB    1 
ATOM   1248 C  CG1   . VAL A 1 167 ? -4.149  -8.647  -3.526  1.00 18.23  ? 129 VAL A CG1   1 
ATOM   1249 C  CG2   . VAL A 1 167 ? -4.929  -6.693  -2.198  1.00 10.52  ? 129 VAL A CG2   1 
ATOM   1250 N  N     . LEU A 1 168 ? -2.915  -10.821 -1.423  1.00 18.90  ? 130 LEU A N     1 
ATOM   1251 C  CA    . LEU A 1 168 ? -1.927  -11.881 -1.561  1.00 18.23  ? 130 LEU A CA    1 
ATOM   1252 C  C     . LEU A 1 168 ? -1.584  -12.086 -3.037  1.00 18.75  ? 130 LEU A C     1 
ATOM   1253 O  O     . LEU A 1 168 ? -2.469  -12.056 -3.903  1.00 13.25  ? 130 LEU A O     1 
ATOM   1254 C  CB    . LEU A 1 168 ? -2.478  -13.173 -0.957  1.00 15.19  ? 130 LEU A CB    1 
ATOM   1255 C  CG    . LEU A 1 168 ? -1.553  -14.363 -0.782  1.00 20.41  ? 130 LEU A CG    1 
ATOM   1256 C  CD1   . LEU A 1 168 ? -0.501  -14.048 0.248   1.00 21.82  ? 130 LEU A CD1   1 
ATOM   1257 C  CD2   . LEU A 1 168 ? -2.368  -15.586 -0.364  1.00 12.52  ? 130 LEU A CD2   1 
ATOM   1258 N  N     . CYS A 1 169 ? -0.299  -12.299 -3.322  1.00 24.75  ? 131 CYS A N     1 
ATOM   1259 C  CA    . CYS A 1 169 ? 0.175   -12.463 -4.697  1.00 21.07  ? 131 CYS A CA    1 
ATOM   1260 C  C     . CYS A 1 169 ? 1.113   -13.661 -4.763  1.00 13.70  ? 131 CYS A C     1 
ATOM   1261 O  O     . CYS A 1 169 ? 2.231   -13.609 -4.244  1.00 16.73  ? 131 CYS A O     1 
ATOM   1262 C  CB    . CYS A 1 169 ? 0.891   -11.210 -5.197  1.00 16.64  ? 131 CYS A CB    1 
ATOM   1263 S  SG    . CYS A 1 169 ? -0.175  -9.804  -5.439  1.00 20.97  ? 131 CYS A SG    1 
ATOM   1264 N  N     . GLY A 1 170 ? 0.655   -14.743 -5.381  1.00 18.12  ? 132 GLY A N     1 
ATOM   1265 C  CA    . GLY A 1 170 ? 1.572   -15.776 -5.827  1.00 17.91  ? 132 GLY A CA    1 
ATOM   1266 C  C     . GLY A 1 170 ? 2.246   -15.318 -7.106  1.00 16.55  ? 132 GLY A C     1 
ATOM   1267 O  O     . GLY A 1 170 ? 1.612   -15.218 -8.154  1.00 19.74  ? 132 GLY A O     1 
ATOM   1268 N  N     . ASN A 1 171 ? 3.520   -14.991 -7.012  1.00 17.42  ? 133 ASN A N     1 
ATOM   1269 C  CA    . ASN A 1 171 ? 4.258   -14.356 -8.083  1.00 17.59  ? 133 ASN A CA    1 
ATOM   1270 C  C     . ASN A 1 171 ? 4.946   -15.420 -8.937  1.00 16.89  ? 133 ASN A C     1 
ATOM   1271 O  O     . ASN A 1 171 ? 4.920   -16.609 -8.627  1.00 28.15  ? 133 ASN A O     1 
ATOM   1272 C  CB    . ASN A 1 171 ? 5.275   -13.374 -7.492  1.00 15.80  ? 133 ASN A CB    1 
ATOM   1273 C  CG    . ASN A 1 171 ? 5.897   -12.482 -8.545  1.00 15.24  ? 133 ASN A CG    1 
ATOM   1274 O  OD1   . ASN A 1 171 ? 5.190   -11.935 -9.393  1.00 19.23  ? 133 ASN A OD1   1 
ATOM   1275 N  ND2   . ASN A 1 171 ? 7.222   -12.342 -8.508  1.00 14.27  ? 133 ASN A ND2   1 
ATOM   1276 N  N     . LYS A 1 172 ? 5.572   -14.971 -10.024 1.00 19.18  ? 134 LYS A N     1 
ATOM   1277 C  CA    . LYS A 1 172 ? 6.349   -15.816 -10.945 1.00 22.04  ? 134 LYS A CA    1 
ATOM   1278 C  C     . LYS A 1 172 ? 5.459   -16.781 -11.727 1.00 12.07  ? 134 LYS A C     1 
ATOM   1279 O  O     . LYS A 1 172 ? 5.823   -17.925 -11.983 1.00 12.95  ? 134 LYS A O     1 
ATOM   1280 C  CB    . LYS A 1 172 ? 7.462   -16.570 -10.215 1.00 13.58  ? 134 LYS A CB    1 
ATOM   1281 C  CG    . LYS A 1 172 ? 8.515   -15.651 -9.763  1.00 10.76  ? 134 LYS A CG    1 
ATOM   1282 C  CD    . LYS A 1 172 ? 9.646   -16.352 -9.099  1.00 16.59  ? 134 LYS A CD    1 
ATOM   1283 C  CE    . LYS A 1 172 ? 10.323  -15.362 -8.163  1.00 12.66  ? 134 LYS A CE    1 
ATOM   1284 N  NZ    . LYS A 1 172 ? 11.653  -15.831 -7.743  1.00 11.64  ? 134 LYS A NZ    1 
ATOM   1285 N  N     . SER A 1 173 ? 4.286   -16.322 -12.115 1.00 9.97   ? 135 SER A N     1 
ATOM   1286 C  CA    . SER A 1 173 ? 3.405   -17.262 -12.763 1.00 14.64  ? 135 SER A CA    1 
ATOM   1287 C  C     . SER A 1 173 ? 3.863   -17.620 -14.167 1.00 21.45  ? 135 SER A C     1 
ATOM   1288 O  O     . SER A 1 173 ? 3.364   -18.600 -14.716 1.00 12.50  ? 135 SER A O     1 
ATOM   1289 C  CB    . SER A 1 173 ? 1.984   -16.717 -12.796 1.00 11.65  ? 135 SER A CB    1 
ATOM   1290 O  OG    . SER A 1 173 ? 1.910   -15.515 -13.521 1.00 15.10  ? 135 SER A OG    1 
ATOM   1291 N  N     . ASP A 1 174 ? 4.810   -16.881 -14.750 1.00 24.30  ? 136 ASP A N     1 
ATOM   1292 C  CA    . ASP A 1 174 ? 5.324   -17.238 -16.070 1.00 20.91  ? 136 ASP A CA    1 
ATOM   1293 C  C     . ASP A 1 174 ? 6.141   -18.518 -16.053 1.00 31.86  ? 136 ASP A C     1 
ATOM   1294 O  O     . ASP A 1 174 ? 6.419   -19.057 -17.130 1.00 28.71  ? 136 ASP A O     1 
ATOM   1295 C  CB    . ASP A 1 174 ? 6.179   -16.109 -16.615 1.00 17.31  ? 136 ASP A CB    1 
ATOM   1296 C  CG    . ASP A 1 174 ? 7.128   -15.582 -15.580 1.00 19.44  ? 136 ASP A CG    1 
ATOM   1297 O  OD1   . ASP A 1 174 ? 6.648   -15.015 -14.572 1.00 13.94  ? 136 ASP A OD1   1 
ATOM   1298 O  OD2   . ASP A 1 174 ? 8.346   -15.769 -15.754 1.00 17.32  ? 136 ASP A OD2   1 
ATOM   1299 N  N     . LEU A 1 175 ? 6.527   -19.013 -14.869 1.00 21.63  ? 137 LEU A N     1 
ATOM   1300 C  CA    . LEU A 1 175 ? 7.325   -20.232 -14.763 1.00 17.90  ? 137 LEU A CA    1 
ATOM   1301 C  C     . LEU A 1 175 ? 6.423   -21.425 -14.465 1.00 29.48  ? 137 LEU A C     1 
ATOM   1302 O  O     . LEU A 1 175 ? 6.403   -21.967 -13.348 1.00 26.46  ? 137 LEU A O     1 
ATOM   1303 C  CB    . LEU A 1 175 ? 8.389   -20.072 -13.690 1.00 18.85  ? 137 LEU A CB    1 
ATOM   1304 C  CG    . LEU A 1 175 ? 9.241   -18.821 -13.766 1.00 15.70  ? 137 LEU A CG    1 
ATOM   1305 C  CD1   . LEU A 1 175 ? 10.206  -18.813 -12.581 1.00 17.54  ? 137 LEU A CD1   1 
ATOM   1306 C  CD2   . LEU A 1 175 ? 10.000  -18.760 -15.088 1.00 14.85  ? 137 LEU A CD2   1 
ATOM   1307 N  N     . GLU A 1 176 ? 5.659   -21.830 -15.490 1.00 26.87  ? 138 GLU A N     1 
ATOM   1308 C  CA    . GLU A 1 176 ? 4.720   -22.937 -15.309 1.00 20.00  ? 138 GLU A CA    1 
ATOM   1309 C  C     . GLU A 1 176 ? 5.449   -24.231 -15.015 1.00 25.14  ? 138 GLU A C     1 
ATOM   1310 O  O     . GLU A 1 176 ? 5.049   -24.987 -14.124 1.00 23.18  ? 138 GLU A O     1 
ATOM   1311 C  CB    . GLU A 1 176 ? 3.834   -23.087 -16.544 1.00 22.00  ? 138 GLU A CB    1 
ATOM   1312 C  CG    . GLU A 1 176 ? 2.553   -22.274 -16.530 1.00 33.75  ? 138 GLU A CG    1 
ATOM   1313 C  CD    . GLU A 1 176 ? 2.818   -20.820 -16.826 1.00 55.83  ? 138 GLU A CD    1 
ATOM   1314 O  OE1   . GLU A 1 176 ? 2.108   -19.915 -16.307 1.00 51.08  ? 138 GLU A OE1   1 
ATOM   1315 O  OE2   . GLU A 1 176 ? 3.827   -20.596 -17.517 1.00 58.62  ? 138 GLU A OE2   1 
ATOM   1316 N  N     . ASP A 1 177 ? 6.523   -24.495 -15.752 1.00 30.49  ? 139 ASP A N     1 
ATOM   1317 C  CA    . ASP A 1 177 ? 7.282   -25.717 -15.555 1.00 27.43  ? 139 ASP A CA    1 
ATOM   1318 C  C     . ASP A 1 177 ? 7.906   -25.790 -14.168 1.00 28.34  ? 139 ASP A C     1 
ATOM   1319 O  O     . ASP A 1 177 ? 8.191   -26.890 -13.691 1.00 23.69  ? 139 ASP A O     1 
ATOM   1320 C  CB    . ASP A 1 177 ? 8.363   -25.820 -16.634 1.00 32.06  ? 139 ASP A CB    1 
ATOM   1321 C  CG    . ASP A 1 177 ? 7.825   -26.335 -17.976 1.00 39.12  ? 139 ASP A CG    1 
ATOM   1322 O  OD1   . ASP A 1 177 ? 6.615   -26.614 -18.094 1.00 29.73  ? 139 ASP A OD1   1 
ATOM   1323 O  OD2   . ASP A 1 177 ? 8.621   -26.452 -18.928 1.00 39.47  ? 139 ASP A OD2   1 
ATOM   1324 N  N     . GLN A 1 178 ? 8.130   -24.653 -13.509 1.00 28.29  ? 140 GLN A N     1 
ATOM   1325 C  CA    . GLN A 1 178 ? 8.697   -24.653 -12.168 1.00 27.61  ? 140 GLN A CA    1 
ATOM   1326 C  C     . GLN A 1 178 ? 7.656   -24.515 -11.074 1.00 21.87  ? 140 GLN A C     1 
ATOM   1327 O  O     . GLN A 1 178 ? 8.024   -24.441 -9.900  1.00 21.64  ? 140 GLN A O     1 
ATOM   1328 C  CB    . GLN A 1 178 ? 9.726   -23.530 -12.016 1.00 32.08  ? 140 GLN A CB    1 
ATOM   1329 C  CG    . GLN A 1 178 ? 11.017  -23.800 -12.740 1.00 23.25  ? 140 GLN A CG    1 
ATOM   1330 C  CD    . GLN A 1 178 ? 11.043  -23.127 -14.088 1.00 38.17  ? 140 GLN A CD    1 
ATOM   1331 O  OE1   . GLN A 1 178 ? 10.183  -23.374 -14.944 1.00 30.39  ? 140 GLN A OE1   1 
ATOM   1332 N  NE2   . GLN A 1 178 ? 12.017  -22.241 -14.281 1.00 40.79  ? 140 GLN A NE2   1 
ATOM   1333 N  N     . ARG A 1 179 ? 6.376   -24.464 -11.420 1.00 22.49  ? 141 ARG A N     1 
ATOM   1334 C  CA    . ARG A 1 179 ? 5.361   -24.153 -10.425 1.00 26.71  ? 141 ARG A CA    1 
ATOM   1335 C  C     . ARG A 1 179 ? 5.223   -25.306 -9.450  1.00 25.03  ? 141 ARG A C     1 
ATOM   1336 O  O     . ARG A 1 179 ? 5.014   -26.451 -9.859  1.00 22.40  ? 141 ARG A O     1 
ATOM   1337 C  CB    . ARG A 1 179 ? 4.024   -23.866 -11.097 1.00 22.18  ? 141 ARG A CB    1 
ATOM   1338 C  CG    . ARG A 1 179 ? 2.845   -24.203 -10.237 1.00 18.10  ? 141 ARG A CG    1 
ATOM   1339 C  CD    . ARG A 1 179 ? 1.612   -23.476 -10.698 1.00 21.21  ? 141 ARG A CD    1 
ATOM   1340 N  NE    . ARG A 1 179 ? 0.836   -23.058 -9.548  1.00 24.07  ? 141 ARG A NE    1 
ATOM   1341 C  CZ    . ARG A 1 179 ? -0.151  -22.186 -9.607  1.00 25.74  ? 141 ARG A CZ    1 
ATOM   1342 N  NH1   . ARG A 1 179 ? -0.472  -21.636 -10.768 1.00 14.84  ? 141 ARG A NH1   1 
ATOM   1343 N  NH2   . ARG A 1 179 ? -0.806  -21.864 -8.501  1.00 22.00  ? 141 ARG A NH2   1 
ATOM   1344 N  N     . VAL A 1 180 ? 5.344   -25.018 -8.156  1.00 22.71  ? 142 VAL A N     1 
ATOM   1345 C  CA    . VAL A 1 180 ? 5.188   -26.061 -7.151  1.00 22.21  ? 142 VAL A CA    1 
ATOM   1346 C  C     . VAL A 1 180 ? 4.046   -25.801 -6.175  1.00 22.65  ? 142 VAL A C     1 
ATOM   1347 O  O     . VAL A 1 180 ? 3.503   -26.766 -5.620  1.00 24.52  ? 142 VAL A O     1 
ATOM   1348 C  CB    . VAL A 1 180 ? 6.504   -26.302 -6.391  1.00 23.14  ? 142 VAL A CB    1 
ATOM   1349 C  CG1   . VAL A 1 180 ? 7.661   -26.425 -7.394  1.00 22.51  ? 142 VAL A CG1   1 
ATOM   1350 C  CG2   . VAL A 1 180 ? 6.763   -25.191 -5.368  1.00 21.76  ? 142 VAL A CG2   1 
ATOM   1351 N  N     . VAL A 1 181 ? 3.606   -24.565 -5.973  1.00 23.18  ? 143 VAL A N     1 
ATOM   1352 C  CA    . VAL A 1 181 ? 2.505   -24.314 -5.046  1.00 23.03  ? 143 VAL A CA    1 
ATOM   1353 C  C     . VAL A 1 181 ? 1.194   -24.653 -5.740  1.00 25.22  ? 143 VAL A C     1 
ATOM   1354 O  O     . VAL A 1 181 ? 0.907   -24.149 -6.836  1.00 28.19  ? 143 VAL A O     1 
ATOM   1355 C  CB    . VAL A 1 181 ? 2.516   -22.855 -4.559  1.00 16.89  ? 143 VAL A CB    1 
ATOM   1356 C  CG1   . VAL A 1 181 ? 1.205   -22.518 -3.917  1.00 18.10  ? 143 VAL A CG1   1 
ATOM   1357 C  CG2   . VAL A 1 181 ? 3.682   -22.600 -3.628  1.00 16.26  ? 143 VAL A CG2   1 
ATOM   1358 N  N     . LYS A 1 182 ? 0.398   -25.516 -5.114  1.00 29.06  ? 144 LYS A N     1 
ATOM   1359 C  CA    . LYS A 1 182 ? -0.899  -25.865 -5.679  1.00 21.70  ? 144 LYS A CA    1 
ATOM   1360 C  C     . LYS A 1 182 ? -1.852  -24.685 -5.573  1.00 24.95  ? 144 LYS A C     1 
ATOM   1361 O  O     . LYS A 1 182 ? -1.835  -23.935 -4.596  1.00 31.76  ? 144 LYS A O     1 
ATOM   1362 C  CB    . LYS A 1 182 ? -1.492  -27.073 -4.962  1.00 32.89  ? 144 LYS A CB    1 
ATOM   1363 C  CG    . LYS A 1 182 ? -0.573  -28.274 -4.888  1.00 25.13  ? 144 LYS A CG    1 
ATOM   1364 C  CD    . LYS A 1 182 ? -1.328  -29.471 -4.329  1.00 41.05  ? 144 LYS A CD    1 
ATOM   1365 C  CE    . LYS A 1 182 ? -0.387  -30.483 -3.682  1.00 45.65  ? 144 LYS A CE    1 
ATOM   1366 N  NZ    . LYS A 1 182 ? -0.977  -31.858 -3.655  1.00 39.48  ? 144 LYS A NZ    1 
ATOM   1367 N  N     . GLU A 1 183 ? -2.675  -24.505 -6.599  1.00 25.25  ? 145 GLU A N     1 
ATOM   1368 C  CA    . GLU A 1 183 ? -3.622  -23.399 -6.574  1.00 21.78  ? 145 GLU A CA    1 
ATOM   1369 C  C     . GLU A 1 183 ? -4.686  -23.609 -5.506  1.00 27.44  ? 145 GLU A C     1 
ATOM   1370 O  O     . GLU A 1 183 ? -5.222  -22.642 -4.949  1.00 20.96  ? 145 GLU A O     1 
ATOM   1371 C  CB    . GLU A 1 183 ? -4.259  -23.250 -7.947  1.00 16.36  ? 145 GLU A CB    1 
ATOM   1372 C  CG    . GLU A 1 183 ? -5.021  -21.975 -8.159  1.00 18.84  ? 145 GLU A CG    1 
ATOM   1373 C  CD    . GLU A 1 183 ? -6.160  -22.168 -9.143  1.00 32.21  ? 145 GLU A CD    1 
ATOM   1374 O  OE1   . GLU A 1 183 ? -6.859  -23.203 -9.026  1.00 26.49  ? 145 GLU A OE1   1 
ATOM   1375 O  OE2   . GLU A 1 183 ? -6.337  -21.305 -10.044 1.00 33.07  ? 145 GLU A OE2   1 
ATOM   1376 N  N     . GLU A 1 184 ? -4.993  -24.863 -5.199  1.00 27.81  ? 146 GLU A N     1 
ATOM   1377 C  CA    . GLU A 1 184 ? -5.985  -25.140 -4.175  1.00 27.10  ? 146 GLU A CA    1 
ATOM   1378 C  C     . GLU A 1 184 ? -5.508  -24.651 -2.817  1.00 18.95  ? 146 GLU A C     1 
ATOM   1379 O  O     . GLU A 1 184 ? -6.262  -24.010 -2.083  1.00 14.73  ? 146 GLU A O     1 
ATOM   1380 C  CB    . GLU A 1 184 ? -6.294  -26.632 -4.151  1.00 35.14  ? 146 GLU A CB    1 
ATOM   1381 C  CG    . GLU A 1 184 ? -6.887  -27.152 -5.449  1.00 34.82  ? 146 GLU A CG    1 
ATOM   1382 C  CD    . GLU A 1 184 ? -5.868  -27.256 -6.566  1.00 36.99  ? 146 GLU A CD    1 
ATOM   1383 O  OE1   . GLU A 1 184 ? -6.177  -26.827 -7.708  1.00 24.56  ? 146 GLU A OE1   1 
ATOM   1384 O  OE2   . GLU A 1 184 ? -4.754  -27.757 -6.286  1.00 36.45  ? 146 GLU A OE2   1 
ATOM   1385 N  N     . GLU A 1 185 ? -4.238  -24.907 -2.483  1.00 18.65  ? 147 GLU A N     1 
ATOM   1386 C  CA    . GLU A 1 185 ? -3.716  -24.466 -1.188  1.00 23.56  ? 147 GLU A CA    1 
ATOM   1387 C  C     . GLU A 1 185 ? -3.733  -22.946 -1.069  1.00 25.19  ? 147 GLU A C     1 
ATOM   1388 O  O     . GLU A 1 185 ? -3.970  -22.411 0.022   1.00 21.86  ? 147 GLU A O     1 
ATOM   1389 C  CB    . GLU A 1 185 ? -2.295  -25.015 -0.958  1.00 16.52  ? 147 GLU A CB    1 
ATOM   1390 C  CG    . GLU A 1 185 ? -2.257  -26.535 -0.710  1.00 21.81  ? 147 GLU A CG    1 
ATOM   1391 C  CD    . GLU A 1 185 ? -0.865  -27.168 -0.850  1.00 43.96  ? 147 GLU A CD    1 
ATOM   1392 O  OE1   . GLU A 1 185 ? 0.153   -26.470 -0.628  1.00 29.48  ? 147 GLU A OE1   1 
ATOM   1393 O  OE2   . GLU A 1 185 ? -0.796  -28.378 -1.197  1.00 44.37  ? 147 GLU A OE2   1 
ATOM   1394 N  N     . ALA A 1 186 ? -3.513  -22.232 -2.174  1.00 25.22  ? 148 ALA A N     1 
ATOM   1395 C  CA    . ALA A 1 186 ? -3.460  -20.774 -2.106  1.00 20.31  ? 148 ALA A CA    1 
ATOM   1396 C  C     . ALA A 1 186 ? -4.850  -20.173 -1.935  1.00 19.57  ? 148 ALA A C     1 
ATOM   1397 O  O     . ALA A 1 186 ? -5.094  -19.397 -1.003  1.00 21.31  ? 148 ALA A O     1 
ATOM   1398 C  CB    . ALA A 1 186 ? -2.782  -20.219 -3.356  1.00 18.92  ? 148 ALA A CB    1 
ATOM   1399 N  N     . ILE A 1 187 ? -5.774  -20.524 -2.829  1.00 17.25  ? 149 ILE A N     1 
ATOM   1400 C  CA    . ILE A 1 187 ? -7.150  -20.045 -2.724  1.00 24.44  ? 149 ILE A CA    1 
ATOM   1401 C  C     . ILE A 1 187 ? -7.762  -20.426 -1.374  1.00 23.65  ? 149 ILE A C     1 
ATOM   1402 O  O     . ILE A 1 187 ? -8.408  -19.604 -0.709  1.00 23.19  ? 149 ILE A O     1 
ATOM   1403 C  CB    . ILE A 1 187 ? -7.968  -20.586 -3.912  1.00 18.52  ? 149 ILE A CB    1 
ATOM   1404 C  CG1   . ILE A 1 187 ? -7.212  -20.344 -5.204  1.00 25.25  ? 149 ILE A CG1   1 
ATOM   1405 C  CG2   . ILE A 1 187 ? -9.298  -19.917 -4.008  1.00 12.36  ? 149 ILE A CG2   1 
ATOM   1406 C  CD1   . ILE A 1 187 ? -7.852  -20.987 -6.398  1.00 18.02  ? 149 ILE A CD1   1 
ATOM   1407 N  N     . ALA A 1 188 ? -7.565  -21.669 -0.942  1.00 20.65  ? 150 ALA A N     1 
ATOM   1408 C  CA    . ALA A 1 188 ? -8.017  -22.061 0.390   1.00 18.86  ? 150 ALA A CA    1 
ATOM   1409 C  C     . ALA A 1 188 ? -7.475  -21.122 1.457   1.00 23.77  ? 150 ALA A C     1 
ATOM   1410 O  O     . ALA A 1 188 ? -8.211  -20.719 2.375   1.00 16.25  ? 150 ALA A O     1 
ATOM   1411 C  CB    . ALA A 1 188 ? -7.600  -23.499 0.693   1.00 8.68   ? 150 ALA A CB    1 
ATOM   1412 N  N     . LEU A 1 189 ? -6.194  -20.753 1.351   1.00 17.10  ? 151 LEU A N     1 
ATOM   1413 C  CA    . LEU A 1 189 ? -5.607  -19.888 2.371   1.00 19.97  ? 151 LEU A CA    1 
ATOM   1414 C  C     . LEU A 1 189 ? -6.177  -18.479 2.294   1.00 24.88  ? 151 LEU A C     1 
ATOM   1415 O  O     . LEU A 1 189 ? -6.457  -17.862 3.332   1.00 21.32  ? 151 LEU A O     1 
ATOM   1416 C  CB    . LEU A 1 189 ? -4.085  -19.849 2.250   1.00 15.98  ? 151 LEU A CB    1 
ATOM   1417 C  CG    . LEU A 1 189 ? -3.419  -19.207 3.470   1.00 19.63  ? 151 LEU A CG    1 
ATOM   1418 C  CD1   . LEU A 1 189 ? -3.648  -20.076 4.691   1.00 23.28  ? 151 LEU A CD1   1 
ATOM   1419 C  CD2   . LEU A 1 189 ? -1.934  -19.001 3.260   1.00 17.85  ? 151 LEU A CD2   1 
ATOM   1420 N  N     . ALA A 1 190 ? -6.370  -17.955 1.077   1.00 23.68  ? 152 ALA A N     1 
ATOM   1421 C  CA    . ALA A 1 190 ? -6.903  -16.604 0.962   1.00 16.79  ? 152 ALA A CA    1 
ATOM   1422 C  C     . ALA A 1 190 ? -8.323  -16.522 1.495   1.00 18.15  ? 152 ALA A C     1 
ATOM   1423 O  O     . ALA A 1 190 ? -8.742  -15.468 1.991   1.00 17.15  ? 152 ALA A O     1 
ATOM   1424 C  CB    . ALA A 1 190 ? -6.843  -16.138 -0.484  1.00 19.05  ? 152 ALA A CB    1 
ATOM   1425 N  N     . GLU A 1 191 ? -9.074  -17.619 1.400   1.00 22.30  ? 153 GLU A N     1 
ATOM   1426 C  CA    . GLU A 1 191 ? -10.422 -17.655 1.955   1.00 18.61  ? 153 GLU A CA    1 
ATOM   1427 C  C     . GLU A 1 191 ? -10.383 -17.683 3.473   1.00 20.30  ? 153 GLU A C     1 
ATOM   1428 O  O     . GLU A 1 191 ? -11.115 -16.943 4.136   1.00 22.48  ? 153 GLU A O     1 
ATOM   1429 C  CB    . GLU A 1 191 ? -11.176 -18.873 1.424   1.00 13.22  ? 153 GLU A CB    1 
ATOM   1430 C  CG    . GLU A 1 191 ? -12.669 -18.833 1.680   1.00 19.94  ? 153 GLU A CG    1 
ATOM   1431 C  CD    . GLU A 1 191 ? -13.421 -18.018 0.638   1.00 34.28  ? 153 GLU A CD    1 
ATOM   1432 O  OE1   . GLU A 1 191 ? -14.475 -17.431 0.971   1.00 42.05  ? 153 GLU A OE1   1 
ATOM   1433 O  OE2   . GLU A 1 191 ? -12.958 -17.964 -0.524  1.00 50.13  ? 153 GLU A OE2   1 
ATOM   1434 N  N     . LYS A 1 192 ? -9.529  -18.535 4.043   1.00 30.93  ? 154 LYS A N     1 
ATOM   1435 C  CA    . LYS A 1 192 ? -9.443  -18.612 5.494   1.00 24.61  ? 154 LYS A CA    1 
ATOM   1436 C  C     . LYS A 1 192 ? -9.212  -17.242 6.107   1.00 21.43  ? 154 LYS A C     1 
ATOM   1437 O  O     . LYS A 1 192 ? -9.696  -16.969 7.206   1.00 32.15  ? 154 LYS A O     1 
ATOM   1438 C  CB    . LYS A 1 192 ? -8.336  -19.580 5.905   1.00 20.60  ? 154 LYS A CB    1 
ATOM   1439 C  CG    . LYS A 1 192 ? -8.200  -19.817 7.401   1.00 16.43  ? 154 LYS A CG    1 
ATOM   1440 C  CD    . LYS A 1 192 ? -7.036  -20.786 7.697   1.00 23.26  ? 154 LYS A CD    1 
ATOM   1441 C  CE    . LYS A 1 192 ? -7.102  -21.389 9.129   1.00 27.83  ? 154 LYS A CE    1 
ATOM   1442 N  NZ    . LYS A 1 192 ? -6.257  -22.630 9.340   1.00 15.98  ? 154 LYS A NZ    1 
ATOM   1443 N  N     . TYR A 1 193 ? -8.522  -16.351 5.403   1.00 22.21  ? 155 TYR A N     1 
ATOM   1444 C  CA    . TYR A 1 193 ? -8.179  -15.046 5.958   1.00 16.96  ? 155 TYR A CA    1 
ATOM   1445 C  C     . TYR A 1 193 ? -8.984  -13.909 5.358   1.00 16.74  ? 155 TYR A C     1 
ATOM   1446 O  O     . TYR A 1 193 ? -8.769  -12.757 5.737   1.00 25.72  ? 155 TYR A O     1 
ATOM   1447 C  CB    . TYR A 1 193 ? -6.677  -14.775 5.789   1.00 23.80  ? 155 TYR A CB    1 
ATOM   1448 C  CG    . TYR A 1 193 ? -5.852  -15.691 6.657   1.00 21.80  ? 155 TYR A CG    1 
ATOM   1449 C  CD1   . TYR A 1 193 ? -5.379  -15.275 7.897   1.00 19.25  ? 155 TYR A CD1   1 
ATOM   1450 C  CD2   . TYR A 1 193 ? -5.593  -16.993 6.261   1.00 22.40  ? 155 TYR A CD2   1 
ATOM   1451 C  CE1   . TYR A 1 193 ? -4.646  -16.131 8.712   1.00 21.17  ? 155 TYR A CE1   1 
ATOM   1452 C  CE2   . TYR A 1 193 ? -4.868  -17.846 7.053   1.00 21.49  ? 155 TYR A CE2   1 
ATOM   1453 C  CZ    . TYR A 1 193 ? -4.395  -17.414 8.279   1.00 37.42  ? 155 TYR A CZ    1 
ATOM   1454 O  OH    . TYR A 1 193 ? -3.688  -18.290 9.062   1.00 33.38  ? 155 TYR A OH    1 
ATOM   1455 N  N     . GLY A 1 194 ? -9.912  -14.190 4.449   1.00 16.46  ? 156 GLY A N     1 
ATOM   1456 C  CA    . GLY A 1 194 ? -10.686 -13.118 3.835   1.00 17.85  ? 156 GLY A CA    1 
ATOM   1457 C  C     . GLY A 1 194 ? -9.879  -12.120 3.029   1.00 23.34  ? 156 GLY A C     1 
ATOM   1458 O  O     . GLY A 1 194 ? -10.293 -10.961 2.910   1.00 30.21  ? 156 GLY A O     1 
ATOM   1459 N  N     . ILE A 1 195 ? -8.736  -12.523 2.478   1.00 14.83  ? 157 ILE A N     1 
ATOM   1460 C  CA    . ILE A 1 195 ? -7.911  -11.613 1.677   1.00 24.97  ? 157 ILE A CA    1 
ATOM   1461 C  C     . ILE A 1 195 ? -7.956  -12.014 0.203   1.00 24.82  ? 157 ILE A C     1 
ATOM   1462 O  O     . ILE A 1 195 ? -8.022  -13.213 -0.114  1.00 25.53  ? 157 ILE A O     1 
ATOM   1463 C  CB    . ILE A 1 195 ? -6.457  -11.562 2.188   1.00 27.36  ? 157 ILE A CB    1 
ATOM   1464 C  CG1   . ILE A 1 195 ? -5.695  -12.837 1.850   1.00 25.71  ? 157 ILE A CG1   1 
ATOM   1465 C  CG2   . ILE A 1 195 ? -6.404  -11.360 3.693   1.00 19.40  ? 157 ILE A CG2   1 
ATOM   1466 C  CD1   . ILE A 1 195 ? -4.335  -12.899 2.496   1.00 16.26  ? 157 ILE A CD1   1 
ATOM   1467 N  N     . PRO A 1 196 ? -7.950  -11.062 -0.728  1.00 26.81  ? 158 PRO A N     1 
ATOM   1468 C  CA    . PRO A 1 196 ? -8.003  -11.418 -2.143  1.00 17.95  ? 158 PRO A CA    1 
ATOM   1469 C  C     . PRO A 1 196 ? -6.661  -11.948 -2.612  1.00 19.48  ? 158 PRO A C     1 
ATOM   1470 O  O     . PRO A 1 196 ? -5.599  -11.526 -2.144  1.00 16.66  ? 158 PRO A O     1 
ATOM   1471 C  CB    . PRO A 1 196 ? -8.333  -10.086 -2.832  1.00 17.41  ? 158 PRO A CB    1 
ATOM   1472 C  CG    . PRO A 1 196 ? -8.659  -9.139  -1.746  1.00 15.87  ? 158 PRO A CG    1 
ATOM   1473 C  CD    . PRO A 1 196 ? -7.920  -9.605  -0.557  1.00 15.85  ? 158 PRO A CD    1 
ATOM   1474 N  N     . TYR A 1 197 ? -6.723  -12.876 -3.562  1.00 20.10  ? 159 TYR A N     1 
ATOM   1475 C  CA    . TYR A 1 197 ? -5.546  -13.568 -4.062  1.00 24.47  ? 159 TYR A CA    1 
ATOM   1476 C  C     . TYR A 1 197 ? -5.401  -13.373 -5.565  1.00 14.11  ? 159 TYR A C     1 
ATOM   1477 O  O     . TYR A 1 197 ? -6.368  -13.495 -6.310  1.00 21.93  ? 159 TYR A O     1 
ATOM   1478 C  CB    . TYR A 1 197 ? -5.642  -15.053 -3.742  1.00 20.05  ? 159 TYR A CB    1 
ATOM   1479 C  CG    . TYR A 1 197 ? -4.544  -15.901 -4.339  1.00 15.92  ? 159 TYR A CG    1 
ATOM   1480 C  CD1   . TYR A 1 197 ? -3.211  -15.552 -4.201  1.00 14.94  ? 159 TYR A CD1   1 
ATOM   1481 C  CD2   . TYR A 1 197 ? -4.850  -17.044 -5.054  1.00 22.20  ? 159 TYR A CD2   1 
ATOM   1482 C  CE1   . TYR A 1 197 ? -2.217  -16.334 -4.738  1.00 17.41  ? 159 TYR A CE1   1 
ATOM   1483 C  CE2   . TYR A 1 197 ? -3.863  -17.834 -5.596  1.00 18.02  ? 159 TYR A CE2   1 
ATOM   1484 C  CZ    . TYR A 1 197 ? -2.555  -17.485 -5.429  1.00 19.38  ? 159 TYR A CZ    1 
ATOM   1485 O  OH    . TYR A 1 197 ? -1.592  -18.291 -5.988  1.00 21.88  ? 159 TYR A OH    1 
ATOM   1486 N  N     . PHE A 1 198 ? -4.190  -13.090 -6.010  1.00 17.18  ? 160 PHE A N     1 
ATOM   1487 C  CA    . PHE A 1 198 ? -3.871  -13.025 -7.428  1.00 13.08  ? 160 PHE A CA    1 
ATOM   1488 C  C     . PHE A 1 198 ? -2.588  -13.795 -7.682  1.00 19.80  ? 160 PHE A C     1 
ATOM   1489 O  O     . PHE A 1 198 ? -1.619  -13.660 -6.930  1.00 19.89  ? 160 PHE A O     1 
ATOM   1490 C  CB    . PHE A 1 198 ? -3.672  -11.573 -7.928  1.00 22.64  ? 160 PHE A CB    1 
ATOM   1491 C  CG    . PHE A 1 198 ? -4.868  -10.678 -7.749  1.00 22.93  ? 160 PHE A CG    1 
ATOM   1492 C  CD1   . PHE A 1 198 ? -5.110  -10.051 -6.541  1.00 17.93  ? 160 PHE A CD1   1 
ATOM   1493 C  CD2   . PHE A 1 198 ? -5.739  -10.449 -8.799  1.00 22.90  ? 160 PHE A CD2   1 
ATOM   1494 C  CE1   . PHE A 1 198 ? -6.195  -9.228  -6.380  1.00 19.27  ? 160 PHE A CE1   1 
ATOM   1495 C  CE2   . PHE A 1 198 ? -6.849  -9.620  -8.634  1.00 13.71  ? 160 PHE A CE2   1 
ATOM   1496 C  CZ    . PHE A 1 198 ? -7.064  -9.005  -7.434  1.00 19.26  ? 160 PHE A CZ    1 
ATOM   1497 N  N     . GLU A 1 199 ? -2.560  -14.586 -8.752  1.00 24.43  ? 161 GLU A N     1 
ATOM   1498 C  CA    . GLU A 1 199 ? -1.294  -15.114 -9.246  1.00 19.24  ? 161 GLU A CA    1 
ATOM   1499 C  C     . GLU A 1 199 ? -0.763  -14.135 -10.288 1.00 19.70  ? 161 GLU A C     1 
ATOM   1500 O  O     . GLU A 1 199 ? -1.467  -13.796 -11.249 1.00 14.42  ? 161 GLU A O     1 
ATOM   1501 C  CB    . GLU A 1 199 ? -1.451  -16.511 -9.838  1.00 23.46  ? 161 GLU A CB    1 
ATOM   1502 C  CG    . GLU A 1 199 ? -2.434  -17.384 -9.112  1.00 16.20  ? 161 GLU A CG    1 
ATOM   1503 C  CD    . GLU A 1 199 ? -2.083  -18.855 -9.210  1.00 25.77  ? 161 GLU A CD    1 
ATOM   1504 O  OE1   . GLU A 1 199 ? -2.124  -19.549 -8.162  1.00 24.83  ? 161 GLU A OE1   1 
ATOM   1505 O  OE2   . GLU A 1 199 ? -1.770  -19.316 -10.338 1.00 27.68  ? 161 GLU A OE2   1 
ATOM   1506 N  N     . THR A 1 200 ? 0.459   -13.664 -10.088 1.00 14.84  ? 162 THR A N     1 
ATOM   1507 C  CA    . THR A 1 200 ? 1.002   -12.566 -10.862 1.00 14.22  ? 162 THR A CA    1 
ATOM   1508 C  C     . THR A 1 200 ? 2.320   -12.974 -11.517 1.00 10.87  ? 162 THR A C     1 
ATOM   1509 O  O     . THR A 1 200 ? 2.899   -14.023 -11.225 1.00 15.03  ? 162 THR A O     1 
ATOM   1510 C  CB    . THR A 1 200 ? 1.222   -11.338 -9.966  1.00 22.34  ? 162 THR A CB    1 
ATOM   1511 O  OG1   . THR A 1 200 ? 2.071   -11.705 -8.874  1.00 17.56  ? 162 THR A OG1   1 
ATOM   1512 C  CG2   . THR A 1 200 ? -0.095  -10.801 -9.421  1.00 17.80  ? 162 THR A CG2   1 
ATOM   1513 N  N     . SER A 1 201 ? 2.803   -12.112 -12.402 1.00 12.93  ? 163 SER A N     1 
ATOM   1514 C  CA    . SER A 1 201 ? 4.128   -12.262 -12.981 1.00 12.59  ? 163 SER A CA    1 
ATOM   1515 C  C     . SER A 1 201 ? 4.709   -10.870 -13.150 1.00 14.71  ? 163 SER A C     1 
ATOM   1516 O  O     . SER A 1 201 ? 4.084   -9.997  -13.763 1.00 16.25  ? 163 SER A O     1 
ATOM   1517 C  CB    . SER A 1 201 ? 4.103   -12.992 -14.338 1.00 14.15  ? 163 SER A CB    1 
ATOM   1518 O  OG    . SER A 1 201 ? 5.194   -12.589 -15.160 1.00 16.33  ? 163 SER A OG    1 
ATOM   1519 N  N     . ALA A 1 202 ? 5.887   -10.662 -12.579 1.00 11.22  ? 164 ALA A N     1 
ATOM   1520 C  CA    . ALA A 1 202 ? 6.587   -9.404  -12.730 1.00 11.48  ? 164 ALA A CA    1 
ATOM   1521 C  C     . ALA A 1 202 ? 7.437   -9.395  -13.972 1.00 15.30  ? 164 ALA A C     1 
ATOM   1522 O  O     . ALA A 1 202 ? 8.071   -8.379  -14.262 1.00 21.04  ? 164 ALA A O     1 
ATOM   1523 C  CB    . ALA A 1 202 ? 7.474   -9.125  -11.517 1.00 8.98   ? 164 ALA A CB    1 
ATOM   1524 N  N     . ALA A 1 203 ? 7.490   -10.519 -14.678 1.00 20.67  ? 165 ALA A N     1 
ATOM   1525 C  CA    . ALA A 1 203 ? 8.159   -10.573 -15.965 1.00 17.57  ? 165 ALA A CA    1 
ATOM   1526 C  C     . ALA A 1 203 ? 7.261   -10.041 -17.079 1.00 22.59  ? 165 ALA A C     1 
ATOM   1527 O  O     . ALA A 1 203 ? 7.725   -9.274  -17.930 1.00 21.44  ? 165 ALA A O     1 
ATOM   1528 C  CB    . ALA A 1 203 ? 8.606   -12.005 -16.257 1.00 17.60  ? 165 ALA A CB    1 
ATOM   1529 N  N     . ASN A 1 204 ? 5.973   -10.425 -17.094 1.00 18.49  ? 166 ASN A N     1 
ATOM   1530 C  CA    . ASN A 1 204 ? 5.088   -10.058 -18.200 1.00 17.72  ? 166 ASN A CA    1 
ATOM   1531 C  C     . ASN A 1 204 ? 3.874   -9.247  -17.764 1.00 25.98  ? 166 ASN A C     1 
ATOM   1532 O  O     . ASN A 1 204 ? 2.999   -8.953  -18.594 1.00 23.26  ? 166 ASN A O     1 
ATOM   1533 C  CB    . ASN A 1 204 ? 4.646   -11.299 -18.993 1.00 23.99  ? 166 ASN A CB    1 
ATOM   1534 C  CG    . ASN A 1 204 ? 3.876   -12.325 -18.157 1.00 27.63  ? 166 ASN A CG    1 
ATOM   1535 O  OD1   . ASN A 1 204 ? 3.147   -11.982 -17.226 1.00 24.83  ? 166 ASN A OD1   1 
ATOM   1536 N  ND2   . ASN A 1 204 ? 4.004   -13.595 -18.532 1.00 23.89  ? 166 ASN A ND2   1 
ATOM   1537 N  N     . GLY A 1 205 ? 3.798   -8.869  -16.491 1.00 27.75  ? 167 GLY A N     1 
ATOM   1538 C  CA    . GLY A 1 205 ? 2.812   -7.913  -16.043 1.00 23.48  ? 167 GLY A CA    1 
ATOM   1539 C  C     . GLY A 1 205 ? 1.454   -8.484  -15.757 1.00 16.03  ? 167 GLY A C     1 
ATOM   1540 O  O     . GLY A 1 205 ? 0.527   -7.719  -15.473 1.00 31.82  ? 167 GLY A O     1 
ATOM   1541 N  N     . THR A 1 206 ? 1.302   -9.800  -15.816 1.00 23.46  ? 168 THR A N     1 
ATOM   1542 C  CA    . THR A 1 206 ? -0.001  -10.408 -15.600 1.00 20.77  ? 168 THR A CA    1 
ATOM   1543 C  C     . THR A 1 206 ? -0.448  -10.163 -14.169 1.00 17.23  ? 168 THR A C     1 
ATOM   1544 O  O     . THR A 1 206 ? 0.275   -10.479 -13.224 1.00 19.18  ? 168 THR A O     1 
ATOM   1545 C  CB    . THR A 1 206 ? 0.056   -11.909 -15.899 1.00 20.54  ? 168 THR A CB    1 
ATOM   1546 O  OG1   . THR A 1 206 ? 0.184   -12.128 -17.318 1.00 27.73  ? 168 THR A OG1   1 
ATOM   1547 C  CG2   . THR A 1 206 ? -1.206  -12.573 -15.428 1.00 18.46  ? 168 THR A CG2   1 
ATOM   1548 N  N     . ASN A 1 207 ? -1.620  -9.555  -14.015 1.00 26.06  ? 169 ASN A N     1 
ATOM   1549 C  CA    . ASN A 1 207 ? -2.318  -9.352  -12.749 1.00 26.76  ? 169 ASN A CA    1 
ATOM   1550 C  C     . ASN A 1 207 ? -1.610  -8.399  -11.785 1.00 22.74  ? 169 ASN A C     1 
ATOM   1551 O  O     . ASN A 1 207 ? -2.096  -8.202  -10.672 1.00 21.50  ? 169 ASN A O     1 
ATOM   1552 C  CB    . ASN A 1 207 ? -2.575  -10.679 -12.031 1.00 27.27  ? 169 ASN A CB    1 
ATOM   1553 C  CG    . ASN A 1 207 ? -3.716  -11.460 -12.653 1.00 26.49  ? 169 ASN A CG    1 
ATOM   1554 O  OD1   . ASN A 1 207 ? -4.500  -10.931 -13.457 1.00 22.66  ? 169 ASN A OD1   1 
ATOM   1555 N  ND2   . ASN A 1 207 ? -3.817  -12.731 -12.281 1.00 23.68  ? 169 ASN A ND2   1 
ATOM   1556 N  N     . ILE A 1 208 ? -0.484  -7.805  -12.168 1.00 19.85  ? 170 ILE A N     1 
ATOM   1557 C  CA    . ILE A 1 208 ? 0.153   -6.814  -11.308 1.00 17.45  ? 170 ILE A CA    1 
ATOM   1558 C  C     . ILE A 1 208 ? -0.802  -5.659  -11.056 1.00 21.61  ? 170 ILE A C     1 
ATOM   1559 O  O     . ILE A 1 208 ? -1.179  -5.375  -9.915  1.00 30.05  ? 170 ILE A O     1 
ATOM   1560 C  CB    . ILE A 1 208 ? 1.465   -6.320  -11.935 1.00 20.62  ? 170 ILE A CB    1 
ATOM   1561 C  CG1   . ILE A 1 208 ? 2.402   -7.486  -12.221 1.00 22.11  ? 170 ILE A CG1   1 
ATOM   1562 C  CG2   . ILE A 1 208 ? 2.133   -5.330  -11.027 1.00 28.45  ? 170 ILE A CG2   1 
ATOM   1563 C  CD1   . ILE A 1 208 ? 2.800   -8.274  -10.974 1.00 17.11  ? 170 ILE A CD1   1 
ATOM   1564 N  N     . SER A 1 209 ? -1.233  -4.999  -12.132 1.00 30.00  ? 171 SER A N     1 
ATOM   1565 C  CA    . SER A 1 209 ? -2.128  -3.854  -12.005 1.00 23.77  ? 171 SER A CA    1 
ATOM   1566 C  C     . SER A 1 209 ? -3.406  -4.216  -11.266 1.00 18.52  ? 171 SER A C     1 
ATOM   1567 O  O     . SER A 1 209 ? -3.897  -3.448  -10.429 1.00 15.78  ? 171 SER A O     1 
ATOM   1568 C  CB    . SER A 1 209 ? -2.462  -3.323  -13.387 1.00 15.34  ? 171 SER A CB    1 
ATOM   1569 O  OG    . SER A 1 209 ? -1.543  -2.314  -13.714 1.00 27.64  ? 171 SER A OG    1 
ATOM   1570 N  N     . GLN A 1 210 ? -3.967  -5.375  -11.581 1.00 24.04  ? 172 GLN A N     1 
ATOM   1571 C  CA    . GLN A 1 210 ? -5.221  -5.783  -10.973 1.00 21.30  ? 172 GLN A CA    1 
ATOM   1572 C  C     . GLN A 1 210 ? -5.057  -5.961  -9.476  1.00 23.23  ? 172 GLN A C     1 
ATOM   1573 O  O     . GLN A 1 210 ? -5.957  -5.632  -8.700  1.00 22.94  ? 172 GLN A O     1 
ATOM   1574 C  CB    . GLN A 1 210 ? -5.704  -7.073  -11.634 1.00 28.43  ? 172 GLN A CB    1 
ATOM   1575 C  CG    . GLN A 1 210 ? -5.982  -6.917  -13.133 1.00 29.82  ? 172 GLN A CG    1 
ATOM   1576 C  CD    . GLN A 1 210 ? -4.755  -7.081  -14.009 1.00 24.75  ? 172 GLN A CD    1 
ATOM   1577 O  OE1   . GLN A 1 210 ? -3.936  -6.175  -14.131 1.00 31.96  ? 172 GLN A OE1   1 
ATOM   1578 N  NE2   . GLN A 1 210 ? -4.647  -8.228  -14.659 1.00 38.20  ? 172 GLN A NE2   1 
ATOM   1579 N  N     . ALA A 1 211 ? -3.896  -6.452  -9.053  1.00 26.94  ? 173 ALA A N     1 
ATOM   1580 C  CA    . ALA A 1 211 ? -3.685  -6.723  -7.641  1.00 23.61  ? 173 ALA A CA    1 
ATOM   1581 C  C     . ALA A 1 211 ? -3.459  -5.436  -6.872  1.00 24.62  ? 173 ALA A C     1 
ATOM   1582 O  O     . ALA A 1 211 ? -3.983  -5.263  -5.764  1.00 28.90  ? 173 ALA A O     1 
ATOM   1583 C  CB    . ALA A 1 211 ? -2.498  -7.669  -7.468  1.00 11.04  ? 173 ALA A CB    1 
ATOM   1584 N  N     . ILE A 1 212 ? -2.679  -4.523  -7.445  1.00 15.08  ? 174 ILE A N     1 
ATOM   1585 C  CA    . ILE A 1 212 ? -2.401  -3.279  -6.757  1.00 16.65  ? 174 ILE A CA    1 
ATOM   1586 C  C     . ILE A 1 212 ? -3.648  -2.404  -6.707  1.00 22.62  ? 174 ILE A C     1 
ATOM   1587 O  O     . ILE A 1 212 ? -3.993  -1.860  -5.647  1.00 19.49  ? 174 ILE A O     1 
ATOM   1588 C  CB    . ILE A 1 212 ? -1.210  -2.579  -7.427  1.00 16.47  ? 174 ILE A CB    1 
ATOM   1589 C  CG1   . ILE A 1 212 ? 0.050   -3.387  -7.154  1.00 12.20  ? 174 ILE A CG1   1 
ATOM   1590 C  CG2   . ILE A 1 212 ? -1.070  -1.149  -6.927  1.00 18.68  ? 174 ILE A CG2   1 
ATOM   1591 C  CD1   . ILE A 1 212 ? 1.293   -2.838  -7.810  1.00 22.96  ? 174 ILE A CD1   1 
ATOM   1592 N  N     . GLU A 1 213 ? -4.358  -2.276  -7.841  1.00 16.76  ? 175 GLU A N     1 
ATOM   1593 C  CA    . GLU A 1 213 ? -5.605  -1.514  -7.871  1.00 19.77  ? 175 GLU A CA    1 
ATOM   1594 C  C     . GLU A 1 213 ? -6.638  -2.075  -6.900  1.00 16.27  ? 175 GLU A C     1 
ATOM   1595 O  O     . GLU A 1 213 ? -7.456  -1.328  -6.349  1.00 14.82  ? 175 GLU A O     1 
ATOM   1596 C  CB    . GLU A 1 213 ? -6.189  -1.500  -9.286  1.00 15.39  ? 175 GLU A CB    1 
ATOM   1597 C  CG    . GLU A 1 213 ? -5.621  -0.403  -10.184 1.00 27.85  ? 175 GLU A CG    1 
ATOM   1598 C  CD    . GLU A 1 213 ? -5.535  -0.809  -11.666 1.00 27.96  ? 175 GLU A CD    1 
ATOM   1599 O  OE1   . GLU A 1 213 ? -4.773  -0.168  -12.420 1.00 20.92  ? 175 GLU A OE1   1 
ATOM   1600 O  OE2   . GLU A 1 213 ? -6.240  -1.754  -12.083 1.00 28.82  ? 175 GLU A OE2   1 
ATOM   1601 N  N     . MET A 1 214 ? -6.648  -3.387  -6.712  1.00 22.71  ? 176 MET A N     1 
ATOM   1602 C  CA    . MET A 1 214 ? -7.601  -3.974  -5.788  1.00 13.09  ? 176 MET A CA    1 
ATOM   1603 C  C     . MET A 1 214 ? -7.282  -3.569  -4.360  1.00 25.76  ? 176 MET A C     1 
ATOM   1604 O  O     . MET A 1 214 ? -8.182  -3.202  -3.592  1.00 24.18  ? 176 MET A O     1 
ATOM   1605 C  CB    . MET A 1 214 ? -7.594  -5.489  -5.934  1.00 13.41  ? 176 MET A CB    1 
ATOM   1606 C  CG    . MET A 1 214 ? -8.312  -6.248  -4.812  1.00 25.75  ? 176 MET A CG    1 
ATOM   1607 S  SD    . MET A 1 214 ? -10.096 -6.018  -4.822  1.00 38.11  ? 176 MET A SD    1 
ATOM   1608 C  CE    . MET A 1 214 ? -10.645 -7.617  -5.372  1.00 19.33  ? 176 MET A CE    1 
ATOM   1609 N  N     . LEU A 1 215 ? -6.005  -3.632  -3.987  1.00 21.58  ? 177 LEU A N     1 
ATOM   1610 C  CA    . LEU A 1 215 ? -5.598  -3.152  -2.677  1.00 19.13  ? 177 LEU A CA    1 
ATOM   1611 C  C     . LEU A 1 215 ? -5.955  -1.685  -2.513  1.00 24.61  ? 177 LEU A C     1 
ATOM   1612 O  O     . LEU A 1 215 ? -6.432  -1.266  -1.455  1.00 27.31  ? 177 LEU A O     1 
ATOM   1613 C  CB    . LEU A 1 215 ? -4.100  -3.387  -2.492  1.00 16.50  ? 177 LEU A CB    1 
ATOM   1614 C  CG    . LEU A 1 215 ? -3.430  -2.938  -1.191  1.00 27.92  ? 177 LEU A CG    1 
ATOM   1615 C  CD1   . LEU A 1 215 ? -3.929  -3.724  0.034   1.00 21.79  ? 177 LEU A CD1   1 
ATOM   1616 C  CD2   . LEU A 1 215 ? -1.934  -3.069  -1.313  1.00 20.75  ? 177 LEU A CD2   1 
ATOM   1617 N  N     . LEU A 1 216 ? -5.775  -0.895  -3.573  1.00 29.65  ? 178 LEU A N     1 
ATOM   1618 C  CA    . LEU A 1 216 ? -6.132  0.518   -3.513  1.00 27.46  ? 178 LEU A CA    1 
ATOM   1619 C  C     . LEU A 1 216 ? -7.633  0.718   -3.360  1.00 26.23  ? 178 LEU A C     1 
ATOM   1620 O  O     . LEU A 1 216 ? -8.057  1.696   -2.737  1.00 28.15  ? 178 LEU A O     1 
ATOM   1621 C  CB    . LEU A 1 216 ? -5.619  1.251   -4.754  1.00 21.03  ? 178 LEU A CB    1 
ATOM   1622 C  CG    . LEU A 1 216 ? -6.037  2.716   -4.929  1.00 30.29  ? 178 LEU A CG    1 
ATOM   1623 C  CD1   . LEU A 1 216 ? -5.525  3.603   -3.788  1.00 31.21  ? 178 LEU A CD1   1 
ATOM   1624 C  CD2   . LEU A 1 216 ? -5.596  3.253   -6.291  1.00 25.01  ? 178 LEU A CD2   1 
ATOM   1625 N  N     . ASP A 1 217 ? -8.452  -0.181  -3.911  1.00 22.17  ? 179 ASP A N     1 
ATOM   1626 C  CA    . ASP A 1 217 ? -9.893  -0.071  -3.687  1.00 25.34  ? 179 ASP A CA    1 
ATOM   1627 C  C     . ASP A 1 217 ? -10.246 -0.321  -2.221  1.00 24.79  ? 179 ASP A C     1 
ATOM   1628 O  O     . ASP A 1 217 ? -11.072 0.396   -1.648  1.00 29.39  ? 179 ASP A O     1 
ATOM   1629 C  CB    . ASP A 1 217 ? -10.644 -1.036  -4.605  1.00 23.05  ? 179 ASP A CB    1 
ATOM   1630 C  CG    . ASP A 1 217 ? -12.106 -0.654  -4.787  1.00 31.11  ? 179 ASP A CG    1 
ATOM   1631 O  OD1   . ASP A 1 217 ? -12.389 0.546   -4.993  1.00 33.73  ? 179 ASP A OD1   1 
ATOM   1632 O  OD2   . ASP A 1 217 ? -12.971 -1.555  -4.734  1.00 36.91  ? 179 ASP A OD2   1 
ATOM   1633 N  N     . LEU A 1 218 ? -9.616  -1.317  -1.593  1.00 25.71  ? 180 LEU A N     1 
ATOM   1634 C  CA    . LEU A 1 218 ? -9.895  -1.624  -0.191  1.00 29.47  ? 180 LEU A CA    1 
ATOM   1635 C  C     . LEU A 1 218 ? -9.456  -0.487  0.731   1.00 26.40  ? 180 LEU A C     1 
ATOM   1636 O  O     . LEU A 1 218 ? -10.114 -0.207  1.742   1.00 23.95  ? 180 LEU A O     1 
ATOM   1637 C  CB    . LEU A 1 218 ? -9.198  -2.930  0.211   1.00 24.62  ? 180 LEU A CB    1 
ATOM   1638 C  CG    . LEU A 1 218 ? -9.496  -4.261  -0.480  1.00 18.74  ? 180 LEU A CG    1 
ATOM   1639 C  CD1   . LEU A 1 218 ? -8.510  -5.252  0.018   1.00 11.67  ? 180 LEU A CD1   1 
ATOM   1640 C  CD2   . LEU A 1 218 ? -10.909 -4.752  -0.182  1.00 15.29  ? 180 LEU A CD2   1 
ATOM   1641 N  N     . ILE A 1 219 ? -8.325  0.149   0.425   1.00 17.73  ? 181 ILE A N     1 
ATOM   1642 C  CA    . ILE A 1 219 ? -7.892  1.300   1.202   1.00 20.25  ? 181 ILE A CA    1 
ATOM   1643 C  C     . ILE A 1 219 ? -8.855  2.460   0.995   1.00 27.42  ? 181 ILE A C     1 
ATOM   1644 O  O     . ILE A 1 219 ? -9.325  3.082   1.957   1.00 16.58  ? 181 ILE A O     1 
ATOM   1645 C  CB    . ILE A 1 219 ? -6.446  1.676   0.828   1.00 26.73  ? 181 ILE A CB    1 
ATOM   1646 C  CG1   . ILE A 1 219 ? -5.481  0.592   1.334   1.00 19.69  ? 181 ILE A CG1   1 
ATOM   1647 C  CG2   . ILE A 1 219 ? -6.078  3.065   1.367   1.00 13.62  ? 181 ILE A CG2   1 
ATOM   1648 C  CD1   . ILE A 1 219 ? -4.209  0.434   0.513   1.00 22.32  ? 181 ILE A CD1   1 
ATOM   1649 N  N     . MET A 1 220 ? -9.187  2.742   -0.269  1.00 26.90  ? 182 MET A N     1 
ATOM   1650 C  CA    . MET A 1 220 ? -10.156 3.788   -0.588  1.00 26.21  ? 182 MET A CA    1 
ATOM   1651 C  C     . MET A 1 220 ? -11.515 3.513   0.061   1.00 29.15  ? 182 MET A C     1 
ATOM   1652 O  O     . MET A 1 220 ? -12.058 4.359   0.784   1.00 30.31  ? 182 MET A O     1 
ATOM   1653 C  CB    . MET A 1 220 ? -10.296 3.914   -2.103  1.00 16.38  ? 182 MET A CB    1 
ATOM   1654 C  CG    . MET A 1 220 ? -9.183  4.699   -2.759  1.00 22.95  ? 182 MET A CG    1 
ATOM   1655 S  SD    . MET A 1 220 ? -8.959  6.376   -2.138  1.00 24.49  ? 182 MET A SD    1 
ATOM   1656 C  CE    . MET A 1 220 ? -7.499  6.094   -1.196  1.00 15.64  ? 182 MET A CE    1 
ATOM   1657 N  N     . LYS A 1 221 ? -12.089 2.333   -0.196  1.00 21.30  ? 183 LYS A N     1 
ATOM   1658 C  CA    . LYS A 1 221 ? -13.398 2.017   0.366   1.00 24.42  ? 183 LYS A CA    1 
ATOM   1659 C  C     . LYS A 1 221 ? -13.372 2.112   1.887   1.00 35.44  ? 183 LYS A C     1 
ATOM   1660 O  O     . LYS A 1 221 ? -14.332 2.587   2.503   1.00 32.67  ? 183 LYS A O     1 
ATOM   1661 C  CB    . LYS A 1 221 ? -13.850 0.624   -0.085  1.00 19.47  ? 183 LYS A CB    1 
ATOM   1662 C  CG    . LYS A 1 221 ? -14.461 0.592   -1.494  1.00 25.47  ? 183 LYS A CG    1 
ATOM   1663 C  CD    . LYS A 1 221 ? -14.633 -0.823  -2.067  1.00 27.48  ? 183 LYS A CD    1 
ATOM   1664 C  CE    . LYS A 1 221 ? -15.253 -1.780  -1.053  1.00 32.07  ? 183 LYS A CE    1 
ATOM   1665 N  NZ    . LYS A 1 221 ? -14.931 -3.209  -1.349  1.00 30.16  ? 183 LYS A NZ    1 
ATOM   1666 N  N     . ARG A 1 222 ? -12.260 1.709   2.505   1.00 33.66  ? 184 ARG A N     1 
ATOM   1667 C  CA    . ARG A 1 222 ? -12.177 1.742   3.958   1.00 29.68  ? 184 ARG A CA    1 
ATOM   1668 C  C     . ARG A 1 222 ? -12.006 3.157   4.493   1.00 37.66  ? 184 ARG A C     1 
ATOM   1669 O  O     . ARG A 1 222 ? -12.494 3.463   5.589   1.00 48.74  ? 184 ARG A O     1 
ATOM   1670 C  CB    . ARG A 1 222 ? -11.038 0.857   4.433   1.00 33.64  ? 184 ARG A CB    1 
ATOM   1671 C  CG    . ARG A 1 222 ? -10.944 0.715   5.926   1.00 30.41  ? 184 ARG A CG    1 
ATOM   1672 C  CD    . ARG A 1 222 ? -10.001 -0.410  6.271   1.00 42.54  ? 184 ARG A CD    1 
ATOM   1673 N  NE    . ARG A 1 222 ? -9.701  -0.450  7.697   1.00 57.97  ? 184 ARG A NE    1 
ATOM   1674 C  CZ    . ARG A 1 222 ? -8.880  -1.328  8.257   1.00 53.21  ? 184 ARG A CZ    1 
ATOM   1675 N  NH1   . ARG A 1 222 ? -8.282  -2.239  7.499   1.00 42.93  ? 184 ARG A NH1   1 
ATOM   1676 N  NH2   . ARG A 1 222 ? -8.658  -1.297  9.569   1.00 46.36  ? 184 ARG A NH2   1 
ATOM   1677 N  N     . MET A 1 223 ? -11.314 4.031   3.762   1.00 28.37  ? 185 MET A N     1 
ATOM   1678 C  CA    . MET A 1 223 ? -11.273 5.419   4.200   1.00 30.11  ? 185 MET A CA    1 
ATOM   1679 C  C     . MET A 1 223 ? -12.649 6.062   4.091   1.00 38.99  ? 185 MET A C     1 
ATOM   1680 O  O     . MET A 1 223 ? -12.993 6.941   4.891   1.00 35.23  ? 185 MET A O     1 
ATOM   1681 C  CB    . MET A 1 223 ? -10.241 6.202   3.393   1.00 26.24  ? 185 MET A CB    1 
ATOM   1682 C  CG    . MET A 1 223 ? -8.818  5.794   3.687   1.00 41.96  ? 185 MET A CG    1 
ATOM   1683 S  SD    . MET A 1 223 ? -7.676  7.174   3.575   1.00 63.57  ? 185 MET A SD    1 
ATOM   1684 C  CE    . MET A 1 223 ? -8.188  7.923   2.014   1.00 19.22  ? 185 MET A CE    1 
ATOM   1685 N  N     . GLU A 1 224 ? -13.458 5.604   3.133   1.00 38.79  ? 186 GLU A N     1 
ATOM   1686 C  CA    . GLU A 1 224 ? -14.789 6.143   2.905   1.00 34.22  ? 186 GLU A CA    1 
ATOM   1687 C  C     . GLU A 1 224 ? -15.790 5.763   3.997   1.00 42.69  ? 186 GLU A C     1 
ATOM   1688 O  O     . GLU A 1 224 ? -16.867 6.368   4.059   1.00 34.80  ? 186 GLU A O     1 
ATOM   1689 C  CB    . GLU A 1 224 ? -15.295 5.675   1.537   1.00 28.85  ? 186 GLU A CB    1 
ATOM   1690 C  CG    . GLU A 1 224 ? -16.218 6.675   0.843   1.00 30.53  ? 186 GLU A CG    1 
ATOM   1691 C  CD    . GLU A 1 224 ? -17.708 6.351   1.020   1.00 57.04  ? 186 GLU A CD    1 
ATOM   1692 O  OE1   . GLU A 1 224 ? -18.051 5.250   1.528   1.00 51.33  ? 186 GLU A OE1   1 
ATOM   1693 O  OE2   . GLU A 1 224 ? -18.541 7.206   0.644   1.00 58.72  ? 186 GLU A OE2   1 
ATOM   1694 N  N     . ARG A 1 225 ? -15.483 4.785   4.852   1.00 40.86  ? 187 ARG A N     1 
ATOM   1695 C  CA    . ARG A 1 225 ? -16.457 4.395   5.866   1.00 44.57  ? 187 ARG A CA    1 
ATOM   1696 C  C     . ARG A 1 225 ? -16.465 5.351   7.052   1.00 45.31  ? 187 ARG A C     1 
ATOM   1697 O  O     . ARG A 1 225 ? -17.527 5.594   7.635   1.00 56.18  ? 187 ARG A O     1 
ATOM   1698 C  CB    . ARG A 1 225 ? -16.196 2.967   6.330   1.00 38.81  ? 187 ARG A CB    1 
ATOM   1699 C  CG    . ARG A 1 225 ? -16.602 1.932   5.307   1.00 37.21  ? 187 ARG A CG    1 
ATOM   1700 C  CD    . ARG A 1 225 ? -15.960 0.578   5.596   1.00 44.63  ? 187 ARG A CD    1 
ATOM   1701 N  NE    . ARG A 1 225 ? -15.910 -0.253  4.394   1.00 44.06  ? 187 ARG A NE    1 
ATOM   1702 C  CZ    . ARG A 1 225 ? -14.878 -1.021  4.054   1.00 45.43  ? 187 ARG A CZ    1 
ATOM   1703 N  NH1   . ARG A 1 225 ? -13.798 -1.070  4.835   1.00 47.22  ? 187 ARG A NH1   1 
ATOM   1704 N  NH2   . ARG A 1 225 ? -14.923 -1.733  2.928   1.00 31.54  ? 187 ARG A NH2   1 
ATOM   1705 N  N     . SER A 1 226 ? -15.313 5.906   7.406   1.00 39.57  ? 188 SER A N     1 
ATOM   1706 C  CA    . SER A 1 226 ? -15.222 6.957   8.412   1.00 43.88  ? 188 SER A CA    1 
ATOM   1707 C  C     . SER A 1 226 ? -16.042 8.185   8.004   1.00 46.46  ? 188 SER A C     1 
ATOM   1708 O  O     . SER A 1 226 ? -15.868 8.733   6.910   1.00 35.69  ? 188 SER A O     1 
ATOM   1709 C  CB    . SER A 1 226 ? -13.761 7.353   8.614   1.00 49.67  ? 188 SER A CB    1 
ATOM   1710 O  OG    . SER A 1 226 ? -12.920 6.211   8.523   1.00 48.32  ? 188 SER A OG    1 
ATOM   1711 N  N     . GLY B 1 1   ? 38.027  -8.098  20.858  1.00 56.02  ? -38 GLY B N     1 
ATOM   1712 C  CA    . GLY B 1 1   ? 36.919  -8.965  20.500  1.00 56.95  ? -38 GLY B CA    1 
ATOM   1713 C  C     . GLY B 1 1   ? 36.560  -8.929  19.024  1.00 65.30  ? -38 GLY B C     1 
ATOM   1714 O  O     . GLY B 1 1   ? 36.985  -8.034  18.291  1.00 61.14  ? -38 GLY B O     1 
ATOM   1715 N  N     . HIS B 1 2   ? 35.796  -9.928  18.581  1.00 71.71  ? -37 HIS B N     1 
ATOM   1716 C  CA    . HIS B 1 2   ? 35.273  -9.932  17.222  1.00 58.16  ? -37 HIS B CA    1 
ATOM   1717 C  C     . HIS B 1 2   ? 34.305  -8.776  17.038  1.00 62.37  ? -37 HIS B C     1 
ATOM   1718 O  O     . HIS B 1 2   ? 33.813  -8.183  18.002  1.00 64.74  ? -37 HIS B O     1 
ATOM   1719 C  CB    . HIS B 1 2   ? 34.567  -11.253 16.911  1.00 50.39  ? -37 HIS B CB    1 
ATOM   1720 N  N     . MET B 1 3   ? 34.037  -8.450  15.781  1.00 68.71  ? -36 MET B N     1 
ATOM   1721 C  CA    . MET B 1 3   ? 33.056  -7.411  15.514  1.00 66.09  ? -36 MET B CA    1 
ATOM   1722 C  C     . MET B 1 3   ? 31.699  -7.893  16.007  1.00 61.26  ? -36 MET B C     1 
ATOM   1723 O  O     . MET B 1 3   ? 31.184  -8.911  15.534  1.00 66.42  ? -36 MET B O     1 
ATOM   1724 C  CB    . MET B 1 3   ? 33.038  -7.052  14.028  1.00 69.78  ? -36 MET B CB    1 
ATOM   1725 C  CG    . MET B 1 3   ? 34.440  -6.826  13.472  1.00 74.18  ? -36 MET B CG    1 
ATOM   1726 S  SD    . MET B 1 3   ? 34.503  -5.825  11.976  1.00 102.06 ? -36 MET B SD    1 
ATOM   1727 C  CE    . MET B 1 3   ? 35.603  -4.489  12.472  1.00 37.28  ? -36 MET B CE    1 
ATOM   1728 N  N     . SER B 1 4   ? 31.159  -7.193  17.004  1.00 58.10  ? -35 SER B N     1 
ATOM   1729 C  CA    . SER B 1 4   ? 29.861  -7.513  17.581  1.00 51.94  ? -35 SER B CA    1 
ATOM   1730 C  C     . SER B 1 4   ? 28.806  -7.692  16.493  1.00 53.25  ? -35 SER B C     1 
ATOM   1731 O  O     . SER B 1 4   ? 28.821  -7.007  15.464  1.00 42.87  ? -35 SER B O     1 
ATOM   1732 C  CB    . SER B 1 4   ? 29.458  -6.396  18.555  1.00 49.90  ? -35 SER B CB    1 
ATOM   1733 O  OG    . SER B 1 4   ? 28.105  -6.493  18.959  1.00 42.60  ? -35 SER B OG    1 
ATOM   1734 N  N     . PHE B 1 5   ? 27.890  -8.626  16.721  1.00 54.62  ? -34 PHE B N     1 
ATOM   1735 C  CA    . PHE B 1 5   ? 26.872  -8.965  15.740  1.00 49.34  ? -34 PHE B CA    1 
ATOM   1736 C  C     . PHE B 1 5   ? 25.495  -8.467  16.167  1.00 46.72  ? -34 PHE B C     1 
ATOM   1737 O  O     . PHE B 1 5   ? 25.280  -7.983  17.281  1.00 44.64  ? -34 PHE B O     1 
ATOM   1738 C  CB    . PHE B 1 5   ? 26.803  -10.480 15.521  1.00 42.78  ? -34 PHE B CB    1 
ATOM   1739 C  CG    . PHE B 1 5   ? 27.956  -11.044 14.752  1.00 50.79  ? -34 PHE B CG    1 
ATOM   1740 C  CD1   . PHE B 1 5   ? 28.871  -11.885 15.372  1.00 41.83  ? -34 PHE B CD1   1 
ATOM   1741 C  CD2   . PHE B 1 5   ? 28.112  -10.760 13.398  1.00 51.33  ? -34 PHE B CD2   1 
ATOM   1742 C  CE1   . PHE B 1 5   ? 29.934  -12.424 14.656  1.00 52.02  ? -34 PHE B CE1   1 
ATOM   1743 C  CE2   . PHE B 1 5   ? 29.174  -11.293 12.675  1.00 46.72  ? -34 PHE B CE2   1 
ATOM   1744 C  CZ    . PHE B 1 5   ? 30.087  -12.125 13.303  1.00 38.75  ? -34 PHE B CZ    1 
ATOM   1745 N  N     . LEU B 1 6   ? 24.570  -8.572  15.220  1.00 42.09  ? -33 LEU B N     1 
ATOM   1746 C  CA    . LEU B 1 6   ? 23.144  -8.638  15.508  1.00 48.33  ? -33 LEU B CA    1 
ATOM   1747 C  C     . LEU B 1 6   ? 22.843  -9.956  16.211  1.00 47.95  ? -33 LEU B C     1 
ATOM   1748 O  O     . LEU B 1 6   ? 23.087  -11.025 15.641  1.00 54.29  ? -33 LEU B O     1 
ATOM   1749 C  CB    . LEU B 1 6   ? 22.369  -8.562  14.194  1.00 46.82  ? -33 LEU B CB    1 
ATOM   1750 C  CG    . LEU B 1 6   ? 21.370  -7.470  13.829  1.00 46.91  ? -33 LEU B CG    1 
ATOM   1751 C  CD1   . LEU B 1 6   ? 20.638  -7.922  12.578  1.00 38.30  ? -33 LEU B CD1   1 
ATOM   1752 C  CD2   . LEU B 1 6   ? 20.392  -7.205  14.966  1.00 35.66  ? -33 LEU B CD2   1 
ATOM   1753 N  N     . THR B 1 7   ? 22.336  -9.912  17.441  1.00 45.28  ? -32 THR B N     1 
ATOM   1754 C  CA    . THR B 1 7   ? 21.952  -11.160 18.087  1.00 47.86  ? -32 THR B CA    1 
ATOM   1755 C  C     . THR B 1 7   ? 20.476  -11.429 17.867  1.00 43.79  ? -32 THR B C     1 
ATOM   1756 O  O     . THR B 1 7   ? 19.705  -10.553 17.474  1.00 45.67  ? -32 THR B O     1 
ATOM   1757 C  CB    . THR B 1 7   ? 22.229  -11.158 19.591  1.00 46.11  ? -32 THR B CB    1 
ATOM   1758 O  OG1   . THR B 1 7   ? 21.905  -9.885  20.145  1.00 55.95  ? -32 THR B OG1   1 
ATOM   1759 C  CG2   . THR B 1 7   ? 23.660  -11.486 19.882  1.00 33.47  ? -32 THR B CG2   1 
ATOM   1760 N  N     . GLU B 1 8   ? 20.086  -12.676 18.127  1.00 56.61  ? -31 GLU B N     1 
ATOM   1761 C  CA    . GLU B 1 8   ? 18.669  -12.982 18.254  1.00 58.15  ? -31 GLU B CA    1 
ATOM   1762 C  C     . GLU B 1 8   ? 18.060  -12.206 19.413  1.00 48.21  ? -31 GLU B C     1 
ATOM   1763 O  O     . GLU B 1 8   ? 16.998  -11.587 19.266  1.00 47.44  ? -31 GLU B O     1 
ATOM   1764 C  CB    . GLU B 1 8   ? 18.464  -14.488 18.437  1.00 65.97  ? -31 GLU B CB    1 
ATOM   1765 C  CG    . GLU B 1 8   ? 19.320  -15.134 19.531  1.00 66.34  ? -31 GLU B CG    1 
ATOM   1766 C  CD    . GLU B 1 8   ? 20.595  -15.760 18.980  1.00 78.58  ? -31 GLU B CD    1 
ATOM   1767 O  OE1   . GLU B 1 8   ? 21.488  -15.003 18.535  1.00 76.42  ? -31 GLU B OE1   1 
ATOM   1768 O  OE2   . GLU B 1 8   ? 20.694  -17.010 18.978  1.00 71.53  ? -31 GLU B OE2   1 
ATOM   1769 N  N     . GLU B 1 9   ? 18.735  -12.213 20.572  1.00 46.52  ? -30 GLU B N     1 
ATOM   1770 C  CA    . GLU B 1 9   ? 18.215  -11.524 21.747  1.00 37.19  ? -30 GLU B CA    1 
ATOM   1771 C  C     . GLU B 1 9   ? 17.857  -10.077 21.428  1.00 37.79  ? -30 GLU B C     1 
ATOM   1772 O  O     . GLU B 1 9   ? 16.756  -9.616  21.754  1.00 39.26  ? -30 GLU B O     1 
ATOM   1773 C  CB    . GLU B 1 9   ? 19.230  -11.598 22.885  1.00 36.78  ? -30 GLU B CB    1 
ATOM   1774 N  N     . GLU B 1 10  ? 18.749  -9.363  20.738  1.00 36.35  ? -29 GLU B N     1 
ATOM   1775 C  CA    . GLU B 1 10  ? 18.553  -7.931  20.523  1.00 35.27  ? -29 GLU B CA    1 
ATOM   1776 C  C     . GLU B 1 10  ? 17.530  -7.621  19.434  1.00 30.93  ? -29 GLU B C     1 
ATOM   1777 O  O     . GLU B 1 10  ? 16.811  -6.625  19.549  1.00 36.52  ? -29 GLU B O     1 
ATOM   1778 C  CB    . GLU B 1 10  ? 19.891  -7.251  20.206  1.00 37.40  ? -29 GLU B CB    1 
ATOM   1779 C  CG    . GLU B 1 10  ? 20.928  -7.349  21.334  1.00 31.91  ? -29 GLU B CG    1 
ATOM   1780 C  CD    . GLU B 1 10  ? 22.351  -7.005  20.885  1.00 50.46  ? -29 GLU B CD    1 
ATOM   1781 O  OE1   . GLU B 1 10  ? 22.627  -6.996  19.657  1.00 49.37  ? -29 GLU B OE1   1 
ATOM   1782 O  OE2   . GLU B 1 10  ? 23.208  -6.773  21.769  1.00 70.61  ? -29 GLU B OE2   1 
ATOM   1783 N  N     . GLN B 1 11  ? 17.432  -8.432  18.377  1.00 28.87  ? -28 GLN B N     1 
ATOM   1784 C  CA    . GLN B 1 11  ? 16.388  -8.168  17.391  1.00 29.78  ? -28 GLN B CA    1 
ATOM   1785 C  C     . GLN B 1 11  ? 15.007  -8.445  17.963  1.00 27.24  ? -28 GLN B C     1 
ATOM   1786 O  O     . GLN B 1 11  ? 14.043  -7.758  17.608  1.00 21.57  ? -28 GLN B O     1 
ATOM   1787 C  CB    . GLN B 1 11  ? 16.611  -8.984  16.117  1.00 40.13  ? -28 GLN B CB    1 
ATOM   1788 C  CG    . GLN B 1 11  ? 15.654  -8.615  14.965  1.00 37.13  ? -28 GLN B CG    1 
ATOM   1789 C  CD    . GLN B 1 11  ? 16.321  -8.687  13.606  1.00 36.38  ? -28 GLN B CD    1 
ATOM   1790 O  OE1   . GLN B 1 11  ? 16.403  -7.689  12.893  1.00 34.23  ? -28 GLN B OE1   1 
ATOM   1791 N  NE2   . GLN B 1 11  ? 16.807  -9.872  13.241  1.00 43.77  ? -28 GLN B NE2   1 
ATOM   1792 N  N     . GLU B 1 12  ? 14.899  -9.441  18.845  1.00 36.05  ? -27 GLU B N     1 
ATOM   1793 C  CA    . GLU B 1 12  ? 13.660  -9.670  19.583  1.00 39.00  ? -27 GLU B CA    1 
ATOM   1794 C  C     . GLU B 1 12  ? 13.256  -8.424  20.371  1.00 32.57  ? -27 GLU B C     1 
ATOM   1795 O  O     . GLU B 1 12  ? 12.098  -7.995  20.327  1.00 29.41  ? -27 GLU B O     1 
ATOM   1796 C  CB    . GLU B 1 12  ? 13.836  -10.878 20.516  1.00 37.73  ? -27 GLU B CB    1 
ATOM   1797 C  CG    . GLU B 1 12  ? 12.568  -11.714 20.790  1.00 56.68  ? -27 GLU B CG    1 
ATOM   1798 C  CD    . GLU B 1 12  ? 11.582  -11.060 21.771  1.00 56.73  ? -27 GLU B CD    1 
ATOM   1799 O  OE1   . GLU B 1 12  ? 10.351  -11.155 21.545  1.00 58.49  ? -27 GLU B OE1   1 
ATOM   1800 O  OE2   . GLU B 1 12  ? 12.037  -10.456 22.771  1.00 62.29  ? -27 GLU B OE2   1 
ATOM   1801 N  N     . ALA B 1 13  ? 14.209  -7.821  21.087  1.00 34.60  ? -26 ALA B N     1 
ATOM   1802 C  CA    . ALA B 1 13  ? 13.899  -6.658  21.913  1.00 29.55  ? -26 ALA B CA    1 
ATOM   1803 C  C     . ALA B 1 13  ? 13.335  -5.524  21.071  1.00 28.05  ? -26 ALA B C     1 
ATOM   1804 O  O     . ALA B 1 13  ? 12.317  -4.920  21.420  1.00 31.21  ? -26 ALA B O     1 
ATOM   1805 C  CB    . ALA B 1 13  ? 15.150  -6.200  22.661  1.00 19.52  ? -26 ALA B CB    1 
ATOM   1806 N  N     . ILE B 1 14  ? 13.987  -5.231  19.947  1.00 28.38  ? -25 ILE B N     1 
ATOM   1807 C  CA    . ILE B 1 14  ? 13.545  -4.146  19.078  1.00 24.05  ? -25 ILE B CA    1 
ATOM   1808 C  C     . ILE B 1 14  ? 12.159  -4.438  18.517  1.00 24.98  ? -25 ILE B C     1 
ATOM   1809 O  O     . ILE B 1 14  ? 11.327  -3.533  18.378  1.00 26.92  ? -25 ILE B O     1 
ATOM   1810 C  CB    . ILE B 1 14  ? 14.585  -3.927  17.965  1.00 34.02  ? -25 ILE B CB    1 
ATOM   1811 C  CG1   . ILE B 1 14  ? 15.946  -3.635  18.591  1.00 27.10  ? -25 ILE B CG1   1 
ATOM   1812 C  CG2   . ILE B 1 14  ? 14.163  -2.812  17.014  1.00 19.38  ? -25 ILE B CG2   1 
ATOM   1813 C  CD1   . ILE B 1 14  ? 17.044  -3.549  17.590  1.00 24.82  ? -25 ILE B CD1   1 
ATOM   1814 N  N     . MET B 1 15  ? 11.882  -5.704  18.193  1.00 28.52  ? -24 MET B N     1 
ATOM   1815 C  CA    . MET B 1 15  ? 10.541  -6.070  17.746  1.00 28.33  ? -24 MET B CA    1 
ATOM   1816 C  C     . MET B 1 15  ? 9.530   -6.080  18.887  1.00 28.16  ? -24 MET B C     1 
ATOM   1817 O  O     . MET B 1 15  ? 8.331   -5.923  18.634  1.00 29.27  ? -24 MET B O     1 
ATOM   1818 C  CB    . MET B 1 15  ? 10.570  -7.430  17.050  1.00 23.13  ? -24 MET B CB    1 
ATOM   1819 C  CG    . MET B 1 15  ? 11.505  -7.440  15.863  1.00 31.96  ? -24 MET B CG    1 
ATOM   1820 S  SD    . MET B 1 15  ? 10.675  -6.959  14.335  1.00 29.24  ? -24 MET B SD    1 
ATOM   1821 C  CE    . MET B 1 15  ? 10.098  -8.552  13.812  1.00 25.83  ? -24 MET B CE    1 
ATOM   1822 N  N     . LYS B 1 16  ? 9.977   -6.253  20.133  1.00 31.86  ? -23 LYS B N     1 
ATOM   1823 C  CA    . LYS B 1 16  ? 9.060   -6.104  21.261  1.00 25.87  ? -23 LYS B CA    1 
ATOM   1824 C  C     . LYS B 1 16  ? 8.634   -4.645  21.413  1.00 24.38  ? -23 LYS B C     1 
ATOM   1825 O  O     . LYS B 1 16  ? 7.455   -4.352  21.653  1.00 23.41  ? -23 LYS B O     1 
ATOM   1826 C  CB    . LYS B 1 16  ? 9.717   -6.639  22.543  1.00 28.88  ? -23 LYS B CB    1 
ATOM   1827 C  CG    . LYS B 1 16  ? 8.748   -6.983  23.689  1.00 28.69  ? -23 LYS B CG    1 
ATOM   1828 C  CD    . LYS B 1 16  ? 7.803   -8.131  23.331  1.00 42.78  ? -23 LYS B CD    1 
ATOM   1829 C  CE    . LYS B 1 16  ? 7.074   -8.667  24.564  1.00 52.84  ? -23 LYS B CE    1 
ATOM   1830 N  NZ    . LYS B 1 16  ? 5.928   -9.553  24.204  1.00 58.23  ? -23 LYS B NZ    1 
ATOM   1831 N  N     . VAL B 1 17  ? 9.573   -3.716  21.237  1.00 18.55  ? -22 VAL B N     1 
ATOM   1832 C  CA    . VAL B 1 17  ? 9.247   -2.294  21.276  1.00 20.93  ? -22 VAL B CA    1 
ATOM   1833 C  C     . VAL B 1 17  ? 8.255   -1.939  20.174  1.00 27.82  ? -22 VAL B C     1 
ATOM   1834 O  O     . VAL B 1 17  ? 7.339   -1.126  20.377  1.00 27.68  ? -22 VAL B O     1 
ATOM   1835 C  CB    . VAL B 1 17  ? 10.543  -1.468  21.162  1.00 26.18  ? -22 VAL B CB    1 
ATOM   1836 C  CG1   . VAL B 1 17  ? 10.252  0.034   21.047  1.00 13.75  ? -22 VAL B CG1   1 
ATOM   1837 C  CG2   . VAL B 1 17  ? 11.472  -1.775  22.318  1.00 20.11  ? -22 VAL B CG2   1 
ATOM   1838 N  N     . LEU B 1 18  ? 8.424   -2.544  18.987  1.00 32.20  ? -21 LEU B N     1 
ATOM   1839 C  CA    . LEU B 1 18  ? 7.550   -2.260  17.848  1.00 18.13  ? -21 LEU B CA    1 
ATOM   1840 C  C     . LEU B 1 18  ? 6.166   -2.852  18.049  1.00 25.80  ? -21 LEU B C     1 
ATOM   1841 O  O     . LEU B 1 18  ? 5.160   -2.206  17.717  1.00 22.73  ? -21 LEU B O     1 
ATOM   1842 C  CB    . LEU B 1 18  ? 8.183   -2.791  16.568  1.00 20.01  ? -21 LEU B CB    1 
ATOM   1843 C  CG    . LEU B 1 18  ? 9.265   -1.870  16.009  1.00 25.26  ? -21 LEU B CG    1 
ATOM   1844 C  CD1   . LEU B 1 18  ? 10.176  -2.647  15.084  1.00 10.32  ? -21 LEU B CD1   1 
ATOM   1845 C  CD2   . LEU B 1 18  ? 8.642   -0.667  15.304  1.00 26.32  ? -21 LEU B CD2   1 
ATOM   1846 N  N     . GLN B 1 19  ? 6.097   -4.089  18.570  1.00 21.30  ? -20 GLN B N     1 
ATOM   1847 C  CA    . GLN B 1 19  ? 4.830   -4.625  19.054  1.00 23.54  ? -20 GLN B CA    1 
ATOM   1848 C  C     . GLN B 1 19  ? 4.134   -3.610  19.948  1.00 18.20  ? -20 GLN B C     1 
ATOM   1849 O  O     . GLN B 1 19  ? 3.004   -3.194  19.668  1.00 23.88  ? -20 GLN B O     1 
ATOM   1850 C  CB    . GLN B 1 19  ? 5.053   -5.951  19.799  1.00 25.50  ? -20 GLN B CB    1 
ATOM   1851 C  CG    . GLN B 1 19  ? 3.744   -6.709  20.111  1.00 22.33  ? -20 GLN B CG    1 
ATOM   1852 C  CD    . GLN B 1 19  ? 3.930   -7.969  20.965  1.00 27.96  ? -20 GLN B CD    1 
ATOM   1853 O  OE1   . GLN B 1 19  ? 5.044   -8.450  21.163  1.00 28.61  ? -20 GLN B OE1   1 
ATOM   1854 N  NE2   . GLN B 1 19  ? 2.818   -8.522  21.449  1.00 33.74  ? -20 GLN B NE2   1 
ATOM   1855 N  N     . ARG B 1 20  ? 4.828   -3.147  20.994  1.00 20.36  ? -19 ARG B N     1 
ATOM   1856 C  CA    . ARG B 1 20  ? 4.217   -2.247  21.973  1.00 30.38  ? -19 ARG B CA    1 
ATOM   1857 C  C     . ARG B 1 20  ? 3.690   -0.981  21.305  1.00 25.41  ? -19 ARG B C     1 
ATOM   1858 O  O     . ARG B 1 20  ? 2.553   -0.558  21.540  1.00 28.15  ? -19 ARG B O     1 
ATOM   1859 C  CB    . ARG B 1 20  ? 5.230   -1.885  23.069  1.00 29.41  ? -19 ARG B CB    1 
ATOM   1860 C  CG    . ARG B 1 20  ? 5.736   -3.050  23.918  1.00 32.67  ? -19 ARG B CG    1 
ATOM   1861 C  CD    . ARG B 1 20  ? 6.930   -2.623  24.788  1.00 25.47  ? -19 ARG B CD    1 
ATOM   1862 N  NE    . ARG B 1 20  ? 6.694   -1.306  25.378  1.00 30.22  ? -19 ARG B NE    1 
ATOM   1863 C  CZ    . ARG B 1 20  ? 7.651   -0.442  25.694  1.00 23.48  ? -19 ARG B CZ    1 
ATOM   1864 N  NH1   . ARG B 1 20  ? 8.917   -0.751  25.477  1.00 18.31  ? -19 ARG B NH1   1 
ATOM   1865 N  NH2   . ARG B 1 20  ? 7.337   0.738   26.214  1.00 18.45  ? -19 ARG B NH2   1 
ATOM   1866 N  N     . ASP B 1 21  ? 4.516   -0.358  20.473  1.00 26.62  ? -18 ASP B N     1 
ATOM   1867 C  CA    . ASP B 1 21  ? 4.105   0.848   19.770  1.00 24.37  ? -18 ASP B CA    1 
ATOM   1868 C  C     . ASP B 1 21  ? 2.831   0.615   18.957  1.00 28.05  ? -18 ASP B C     1 
ATOM   1869 O  O     . ASP B 1 21  ? 1.839   1.344   19.106  1.00 24.51  ? -18 ASP B O     1 
ATOM   1870 C  CB    . ASP B 1 21  ? 5.247   1.307   18.869  1.00 21.02  ? -18 ASP B CB    1 
ATOM   1871 C  CG    . ASP B 1 21  ? 4.893   2.532   18.082  1.00 27.14  ? -18 ASP B CG    1 
ATOM   1872 O  OD1   . ASP B 1 21  ? 4.234   3.425   18.665  1.00 29.42  ? -18 ASP B OD1   1 
ATOM   1873 O  OD2   . ASP B 1 21  ? 5.270   2.613   16.892  1.00 27.64  ? -18 ASP B OD2   1 
ATOM   1874 N  N     . ALA B 1 22  ? 2.848   -0.396  18.079  1.00 22.86  ? -17 ALA B N     1 
ATOM   1875 C  CA    . ALA B 1 22  ? 1.666   -0.696  17.278  1.00 26.17  ? -17 ALA B CA    1 
ATOM   1876 C  C     . ALA B 1 22  ? 0.443   -0.865  18.166  1.00 27.20  ? -17 ALA B C     1 
ATOM   1877 O  O     . ALA B 1 22  ? -0.658  -0.427  17.810  1.00 24.09  ? -17 ALA B O     1 
ATOM   1878 C  CB    . ALA B 1 22  ? 1.901   -1.950  16.430  1.00 18.86  ? -17 ALA B CB    1 
ATOM   1879 N  N     . ALA B 1 23  ? 0.622   -1.464  19.348  1.00 25.14  ? -16 ALA B N     1 
ATOM   1880 C  CA    . ALA B 1 23  ? -0.500  -1.607  20.271  1.00 26.32  ? -16 ALA B CA    1 
ATOM   1881 C  C     . ALA B 1 23  ? -0.961  -0.247  20.783  1.00 28.88  ? -16 ALA B C     1 
ATOM   1882 O  O     . ALA B 1 23  ? -2.159  0.061   20.772  1.00 33.45  ? -16 ALA B O     1 
ATOM   1883 C  CB    . ALA B 1 23  ? -0.108  -2.526  21.425  1.00 19.06  ? -16 ALA B CB    1 
ATOM   1884 N  N     . LEU B 1 24  ? -0.013  0.592   21.209  1.00 34.39  ? -15 LEU B N     1 
ATOM   1885 C  CA    . LEU B 1 24  ? -0.352  1.907   21.746  1.00 26.55  ? -15 LEU B CA    1 
ATOM   1886 C  C     . LEU B 1 24  ? -0.999  2.792   20.683  1.00 30.74  ? -15 LEU B C     1 
ATOM   1887 O  O     . LEU B 1 24  ? -1.919  3.561   20.981  1.00 35.46  ? -15 LEU B O     1 
ATOM   1888 C  CB    . LEU B 1 24  ? 0.910   2.566   22.327  1.00 23.73  ? -15 LEU B CB    1 
ATOM   1889 C  CG    . LEU B 1 24  ? 0.938   4.068   22.647  1.00 16.44  ? -15 LEU B CG    1 
ATOM   1890 C  CD1   . LEU B 1 24  ? -0.186  4.422   23.591  1.00 32.62  ? -15 LEU B CD1   1 
ATOM   1891 C  CD2   . LEU B 1 24  ? 2.276   4.483   23.257  1.00 18.44  ? -15 LEU B CD2   1 
ATOM   1892 N  N     . LYS B 1 25  ? -0.533  2.705   19.438  1.00 25.58  ? -14 LYS B N     1 
ATOM   1893 C  CA    . LYS B 1 25  ? -1.170  3.486   18.384  1.00 32.38  ? -14 LYS B CA    1 
ATOM   1894 C  C     . LYS B 1 25  ? -2.590  3.006   18.135  1.00 31.40  ? -14 LYS B C     1 
ATOM   1895 O  O     . LYS B 1 25  ? -3.484  3.815   17.867  1.00 36.21  ? -14 LYS B O     1 
ATOM   1896 C  CB    . LYS B 1 25  ? -0.361  3.421   17.084  1.00 39.21  ? -14 LYS B CB    1 
ATOM   1897 C  CG    . LYS B 1 25  ? 0.986   4.115   17.132  1.00 34.41  ? -14 LYS B CG    1 
ATOM   1898 C  CD    . LYS B 1 25  ? 0.860   5.554   17.614  1.00 34.66  ? -14 LYS B CD    1 
ATOM   1899 C  CE    . LYS B 1 25  ? 2.236   6.149   17.844  1.00 32.41  ? -14 LYS B CE    1 
ATOM   1900 N  NZ    . LYS B 1 25  ? 3.077   5.175   18.604  1.00 23.45  ? -14 LYS B NZ    1 
ATOM   1901 N  N     . ARG B 1 26  ? -2.814  1.691   18.197  1.00 32.99  ? -13 ARG B N     1 
ATOM   1902 C  CA    . ARG B 1 26  ? -4.156  1.172   17.960  1.00 34.45  ? -13 ARG B CA    1 
ATOM   1903 C  C     . ARG B 1 26  ? -5.081  1.539   19.110  1.00 48.22  ? -13 ARG B C     1 
ATOM   1904 O  O     . ARG B 1 26  ? -6.254  1.871   18.892  1.00 53.04  ? -13 ARG B O     1 
ATOM   1905 C  CB    . ARG B 1 26  ? -4.117  -0.344  17.754  1.00 26.36  ? -13 ARG B CB    1 
ATOM   1906 C  CG    . ARG B 1 26  ? -3.902  -0.753  16.300  1.00 34.05  ? -13 ARG B CG    1 
ATOM   1907 C  CD    . ARG B 1 26  ? -3.869  -2.258  16.116  1.00 23.83  ? -13 ARG B CD    1 
ATOM   1908 N  NE    . ARG B 1 26  ? -2.708  -2.849  16.751  1.00 28.68  ? -13 ARG B NE    1 
ATOM   1909 C  CZ    . ARG B 1 26  ? -2.491  -4.155  16.851  1.00 46.54  ? -13 ARG B CZ    1 
ATOM   1910 N  NH1   . ARG B 1 26  ? -3.375  -5.001  16.339  1.00 48.65  ? -13 ARG B NH1   1 
ATOM   1911 N  NH2   . ARG B 1 26  ? -1.393  -4.616  17.460  1.00 34.17  ? -13 ARG B NH2   1 
ATOM   1912 N  N     . ALA B 1 27  ? -4.564  1.501   20.340  1.00 40.03  ? -12 ALA B N     1 
ATOM   1913 C  CA    . ALA B 1 27  ? -5.343  1.954   21.486  1.00 45.50  ? -12 ALA B CA    1 
ATOM   1914 C  C     . ALA B 1 27  ? -5.908  3.350   21.244  1.00 46.65  ? -12 ALA B C     1 
ATOM   1915 O  O     . ALA B 1 27  ? -7.127  3.536   21.179  1.00 51.88  ? -12 ALA B O     1 
ATOM   1916 C  CB    . ALA B 1 27  ? -4.489  1.917   22.756  1.00 32.25  ? -12 ALA B CB    1 
ATOM   1917 N  N     . GLU B 1 28  ? -5.037  4.347   21.064  1.00 51.66  ? -11 GLU B N     1 
ATOM   1918 C  CA    . GLU B 1 28  ? -5.607  5.687   21.003  1.00 52.68  ? -11 GLU B CA    1 
ATOM   1919 C  C     . GLU B 1 28  ? -6.361  5.950   19.708  1.00 56.73  ? -11 GLU B C     1 
ATOM   1920 O  O     . GLU B 1 28  ? -6.834  7.074   19.506  1.00 64.58  ? -11 GLU B O     1 
ATOM   1921 C  CB    . GLU B 1 28  ? -4.539  6.763   21.225  1.00 45.75  ? -11 GLU B CB    1 
ATOM   1922 C  CG    . GLU B 1 28  ? -5.127  7.898   22.048  1.00 56.07  ? -11 GLU B CG    1 
ATOM   1923 C  CD    . GLU B 1 28  ? -4.241  9.101   22.230  1.00 60.87  ? -11 GLU B CD    1 
ATOM   1924 O  OE1   . GLU B 1 28  ? -3.407  9.094   23.169  1.00 54.79  ? -11 GLU B OE1   1 
ATOM   1925 O  OE2   . GLU B 1 28  ? -4.418  10.073  21.456  1.00 56.02  ? -11 GLU B OE2   1 
ATOM   1926 N  N     . GLU B 1 29  ? -6.505  4.949   18.839  1.00 61.83  ? -10 GLU B N     1 
ATOM   1927 C  CA    . GLU B 1 29  ? -7.454  5.070   17.737  1.00 62.89  ? -10 GLU B CA    1 
ATOM   1928 C  C     . GLU B 1 29  ? -8.887  4.990   18.252  1.00 59.09  ? -10 GLU B C     1 
ATOM   1929 O  O     . GLU B 1 29  ? -9.715  5.861   17.959  1.00 57.83  ? -10 GLU B O     1 
ATOM   1930 C  CB    . GLU B 1 29  ? -7.188  3.984   16.695  1.00 55.82  ? -10 GLU B CB    1 
ATOM   1931 C  CG    . GLU B 1 29  ? -8.037  4.103   15.453  1.00 56.99  ? -10 GLU B CG    1 
ATOM   1932 C  CD    . GLU B 1 29  ? -7.682  5.320   14.630  1.00 65.97  ? -10 GLU B CD    1 
ATOM   1933 O  OE1   . GLU B 1 29  ? -6.488  5.691   14.592  1.00 70.93  ? -10 GLU B OE1   1 
ATOM   1934 O  OE2   . GLU B 1 29  ? -8.598  5.912   14.024  1.00 65.17  ? -10 GLU B OE2   1 
ATOM   1935 N  N     . GLU B 1 30  ? -9.180  3.964   19.053  1.00 61.05  ? -9  GLU B N     1 
ATOM   1936 C  CA    . GLU B 1 30  ? -10.494 3.708   19.635  1.00 59.60  ? -9  GLU B CA    1 
ATOM   1937 C  C     . GLU B 1 30  ? -11.063 4.872   20.444  1.00 72.07  ? -9  GLU B C     1 
ATOM   1938 O  O     . GLU B 1 30  ? -11.338 4.710   21.639  1.00 71.91  ? -9  GLU B O     1 
ATOM   1939 C  CB    . GLU B 1 30  ? -10.402 2.483   20.541  1.00 57.43  ? -9  GLU B CB    1 
ATOM   1940 C  CG    . GLU B 1 30  ? -10.884 1.195   19.925  1.00 73.77  ? -9  GLU B CG    1 
ATOM   1941 C  CD    . GLU B 1 30  ? -11.569 0.307   20.947  1.00 82.68  ? -9  GLU B CD    1 
ATOM   1942 O  OE1   . GLU B 1 30  ? -12.798 0.450   21.128  1.00 82.15  ? -9  GLU B OE1   1 
ATOM   1943 O  OE2   . GLU B 1 30  ? -10.879 -0.527  21.574  1.00 73.77  ? -9  GLU B OE2   1 
ATOM   1944 N  N     . ARG B 1 31  ? -11.259 6.036   19.821  1.00 73.16  ? -8  ARG B N     1 
ATOM   1945 C  CA    . ARG B 1 31  ? -11.746 7.216   20.548  1.00 65.03  ? -8  ARG B CA    1 
ATOM   1946 C  C     . ARG B 1 31  ? -12.619 8.146   19.710  1.00 62.70  ? -8  ARG B C     1 
ATOM   1947 O  O     . ARG B 1 31  ? -13.280 9.038   20.249  1.00 57.79  ? -8  ARG B O     1 
ATOM   1948 C  CB    . ARG B 1 31  ? -10.574 8.011   21.103  1.00 54.39  ? -8  ARG B CB    1 
ATOM   1949 C  CG    . ARG B 1 31  ? -9.903  7.365   22.282  1.00 51.79  ? -8  ARG B CG    1 
ATOM   1950 C  CD    . ARG B 1 31  ? -8.438  7.689   22.277  1.00 54.10  ? -8  ARG B CD    1 
ATOM   1951 N  NE    . ARG B 1 31  ? -8.204  9.132   22.343  1.00 57.67  ? -8  ARG B NE    1 
ATOM   1952 C  CZ    . ARG B 1 31  ? -8.025  9.812   23.473  1.00 62.71  ? -8  ARG B CZ    1 
ATOM   1953 N  NH1   . ARG B 1 31  ? -8.033  9.182   24.648  1.00 47.58  ? -8  ARG B NH1   1 
ATOM   1954 N  NH2   . ARG B 1 31  ? -7.826  11.125  23.430  1.00 55.14  ? -8  ARG B NH2   1 
ATOM   1955 N  N     . TYR B 1 44  ? -4.269  11.390  28.078  1.00 43.31  ? 6   TYR B N     1 
ATOM   1956 C  CA    . TYR B 1 44  ? -5.545  10.844  27.641  1.00 53.68  ? 6   TYR B CA    1 
ATOM   1957 C  C     . TYR B 1 44  ? -6.089  11.613  26.439  1.00 53.63  ? 6   TYR B C     1 
ATOM   1958 O  O     . TYR B 1 44  ? -6.117  11.083  25.330  1.00 59.87  ? 6   TYR B O     1 
ATOM   1959 C  CB    . TYR B 1 44  ? -6.563  10.854  28.797  1.00 48.35  ? 6   TYR B CB    1 
ATOM   1960 N  N     . ASP B 1 45  ? -6.490  12.869  26.668  1.00 46.34  ? 7   ASP B N     1 
ATOM   1961 C  CA    . ASP B 1 45  ? -7.187  13.648  25.643  1.00 54.20  ? 7   ASP B CA    1 
ATOM   1962 C  C     . ASP B 1 45  ? -6.368  13.768  24.350  1.00 53.01  ? 7   ASP B C     1 
ATOM   1963 O  O     . ASP B 1 45  ? -6.895  13.559  23.252  1.00 52.72  ? 7   ASP B O     1 
ATOM   1964 C  CB    . ASP B 1 45  ? -7.537  15.027  26.207  1.00 49.53  ? 7   ASP B CB    1 
ATOM   1965 C  CG    . ASP B 1 45  ? -8.792  15.621  25.576  1.00 71.95  ? 7   ASP B CG    1 
ATOM   1966 O  OD1   . ASP B 1 45  ? -9.827  14.914  25.515  1.00 65.14  ? 7   ASP B OD1   1 
ATOM   1967 O  OD2   . ASP B 1 45  ? -8.752  16.805  25.166  1.00 71.45  ? 7   ASP B OD2   1 
ATOM   1968 N  N     . TYR B 1 46  ? -5.077  14.104  24.458  1.00 54.04  ? 8   TYR B N     1 
ATOM   1969 C  CA    . TYR B 1 46  ? -4.179  14.277  23.317  1.00 39.57  ? 8   TYR B CA    1 
ATOM   1970 C  C     . TYR B 1 46  ? -3.035  13.272  23.381  1.00 46.13  ? 8   TYR B C     1 
ATOM   1971 O  O     . TYR B 1 46  ? -2.606  12.877  24.469  1.00 44.74  ? 8   TYR B O     1 
ATOM   1972 C  CB    . TYR B 1 46  ? -3.549  15.659  23.292  1.00 36.35  ? 8   TYR B CB    1 
ATOM   1973 C  CG    . TYR B 1 46  ? -4.300  16.749  22.571  1.00 58.53  ? 8   TYR B CG    1 
ATOM   1974 C  CD1   . TYR B 1 46  ? -4.931  16.517  21.356  1.00 58.02  ? 8   TYR B CD1   1 
ATOM   1975 C  CD2   . TYR B 1 46  ? -4.341  18.042  23.099  1.00 61.89  ? 8   TYR B CD2   1 
ATOM   1976 C  CE1   . TYR B 1 46  ? -5.604  17.549  20.694  1.00 60.22  ? 8   TYR B CE1   1 
ATOM   1977 C  CE2   . TYR B 1 46  ? -5.002  19.071  22.449  1.00 56.18  ? 8   TYR B CE2   1 
ATOM   1978 C  CZ    . TYR B 1 46  ? -5.629  18.822  21.248  1.00 55.56  ? 8   TYR B CZ    1 
ATOM   1979 O  OH    . TYR B 1 46  ? -6.288  19.850  20.618  1.00 60.94  ? 8   TYR B OH    1 
ATOM   1980 N  N     . LEU B 1 47  ? -2.509  12.890  22.208  1.00 40.84  ? 9   LEU B N     1 
ATOM   1981 C  CA    . LEU B 1 47  ? -1.305  12.064  22.124  1.00 33.31  ? 9   LEU B CA    1 
ATOM   1982 C  C     . LEU B 1 47  ? -0.157  12.898  21.579  1.00 31.99  ? 9   LEU B C     1 
ATOM   1983 O  O     . LEU B 1 47  ? -0.095  13.157  20.374  1.00 34.96  ? 9   LEU B O     1 
ATOM   1984 C  CB    . LEU B 1 47  ? -1.502  10.841  21.240  1.00 21.35  ? 9   LEU B CB    1 
ATOM   1985 C  CG    . LEU B 1 47  ? -0.226  9.977   21.121  1.00 38.19  ? 9   LEU B CG    1 
ATOM   1986 C  CD1   . LEU B 1 47  ? 0.166   9.306   22.447  1.00 32.64  ? 9   LEU B CD1   1 
ATOM   1987 C  CD2   . LEU B 1 47  ? -0.303  8.943   19.997  1.00 28.57  ? 9   LEU B CD2   1 
ATOM   1988 N  N     . ILE B 1 48  ? 0.769   13.288  22.451  1.00 30.13  ? 10  ILE B N     1 
ATOM   1989 C  CA    . ILE B 1 48  ? 1.975   13.995  22.046  1.00 18.48  ? 10  ILE B CA    1 
ATOM   1990 C  C     . ILE B 1 48  ? 3.147   13.034  22.124  1.00 24.47  ? 10  ILE B C     1 
ATOM   1991 O  O     . ILE B 1 48  ? 3.336   12.359  23.143  1.00 26.45  ? 10  ILE B O     1 
ATOM   1992 C  CB    . ILE B 1 48  ? 2.241   15.231  22.914  1.00 27.86  ? 10  ILE B CB    1 
ATOM   1993 C  CG1   . ILE B 1 48  ? 1.004   16.137  22.968  1.00 24.02  ? 10  ILE B CG1   1 
ATOM   1994 C  CG2   . ILE B 1 48  ? 3.488   15.947  22.399  1.00 17.42  ? 10  ILE B CG2   1 
ATOM   1995 C  CD1   . ILE B 1 48  ? 0.434   16.528  21.594  1.00 31.22  ? 10  ILE B CD1   1 
ATOM   1996 N  N     . LYS B 1 49  ? 3.926   12.970  21.046  1.00 22.66  ? 11  LYS B N     1 
ATOM   1997 C  CA    . LYS B 1 49  ? 5.119   12.146  20.960  1.00 19.78  ? 11  LYS B CA    1 
ATOM   1998 C  C     . LYS B 1 49  ? 6.315   13.042  20.714  1.00 22.08  ? 11  LYS B C     1 
ATOM   1999 O  O     . LYS B 1 49  ? 6.241   13.957  19.895  1.00 24.81  ? 11  LYS B O     1 
ATOM   2000 C  CB    . LYS B 1 49  ? 5.000   11.143  19.825  1.00 14.47  ? 11  LYS B CB    1 
ATOM   2001 C  CG    . LYS B 1 49  ? 3.756   10.315  19.912  1.00 21.29  ? 11  LYS B CG    1 
ATOM   2002 C  CD    . LYS B 1 49  ? 3.470   9.655   18.590  1.00 35.67  ? 11  LYS B CD    1 
ATOM   2003 C  CE    . LYS B 1 49  ? 2.935   10.653  17.589  1.00 28.51  ? 11  LYS B CE    1 
ATOM   2004 N  NZ    . LYS B 1 49  ? 2.738   9.982   16.289  1.00 31.78  ? 11  LYS B NZ    1 
ATOM   2005 N  N     . PHE B 1 50  ? 7.413   12.806  21.424  1.00 16.49  ? 12  PHE B N     1 
ATOM   2006 C  CA    . PHE B 1 50  ? 8.664   13.421  21.007  1.00 22.48  ? 12  PHE B CA    1 
ATOM   2007 C  C     . PHE B 1 50  ? 9.783   12.408  21.149  1.00 23.14  ? 12  PHE B C     1 
ATOM   2008 O  O     . PHE B 1 50  ? 9.582   11.302  21.657  1.00 23.15  ? 12  PHE B O     1 
ATOM   2009 C  CB    . PHE B 1 50  ? 8.974   14.725  21.752  1.00 27.76  ? 12  PHE B CB    1 
ATOM   2010 C  CG    . PHE B 1 50  ? 8.846   14.655  23.242  1.00 26.89  ? 12  PHE B CG    1 
ATOM   2011 C  CD1   . PHE B 1 50  ? 9.650   13.808  23.990  1.00 32.76  ? 12  PHE B CD1   1 
ATOM   2012 C  CD2   . PHE B 1 50  ? 7.972   15.501  23.903  1.00 30.06  ? 12  PHE B CD2   1 
ATOM   2013 C  CE1   . PHE B 1 50  ? 9.555   13.763  25.364  1.00 26.37  ? 12  PHE B CE1   1 
ATOM   2014 C  CE2   . PHE B 1 50  ? 7.875   15.467  25.280  1.00 44.23  ? 12  PHE B CE2   1 
ATOM   2015 C  CZ    . PHE B 1 50  ? 8.674   14.586  26.015  1.00 35.69  ? 12  PHE B CZ    1 
ATOM   2016 N  N     . LEU B 1 51  ? 10.963  12.788  20.652  1.00 23.60  ? 13  LEU B N     1 
ATOM   2017 C  CA    . LEU B 1 51  ? 12.072  11.859  20.470  1.00 22.02  ? 13  LEU B CA    1 
ATOM   2018 C  C     . LEU B 1 51  ? 13.369  12.447  21.009  1.00 23.19  ? 13  LEU B C     1 
ATOM   2019 O  O     . LEU B 1 51  ? 13.741  13.576  20.667  1.00 21.43  ? 13  LEU B O     1 
ATOM   2020 C  CB    . LEU B 1 51  ? 12.253  11.495  18.994  1.00 20.84  ? 13  LEU B CB    1 
ATOM   2021 C  CG    . LEU B 1 51  ? 13.376  10.492  18.712  1.00 17.68  ? 13  LEU B CG    1 
ATOM   2022 C  CD1   . LEU B 1 51  ? 12.905  9.462   17.701  1.00 19.85  ? 13  LEU B CD1   1 
ATOM   2023 C  CD2   . LEU B 1 51  ? 14.647  11.192  18.221  1.00 16.22  ? 13  LEU B CD2   1 
ATOM   2024 N  N     . ALA B 1 52  ? 14.070  11.652  21.815  1.00 19.89  ? 14  ALA B N     1 
ATOM   2025 C  CA    . ALA B 1 52  ? 15.314  12.045  22.459  1.00 24.69  ? 14  ALA B CA    1 
ATOM   2026 C  C     . ALA B 1 52  ? 16.481  11.459  21.680  1.00 16.29  ? 14  ALA B C     1 
ATOM   2027 O  O     . ALA B 1 52  ? 16.429  10.309  21.237  1.00 17.56  ? 14  ALA B O     1 
ATOM   2028 C  CB    . ALA B 1 52  ? 15.349  11.560  23.919  1.00 10.79  ? 14  ALA B CB    1 
ATOM   2029 N  N     . LEU B 1 53  ? 17.533  12.247  21.507  1.00 20.16  ? 15  LEU B N     1 
ATOM   2030 C  CA    . LEU B 1 53  ? 18.598  11.798  20.622  1.00 21.59  ? 15  LEU B CA    1 
ATOM   2031 C  C     . LEU B 1 53  ? 19.879  12.556  20.941  1.00 22.16  ? 15  LEU B C     1 
ATOM   2032 O  O     . LEU B 1 53  ? 19.858  13.659  21.489  1.00 22.18  ? 15  LEU B O     1 
ATOM   2033 C  CB    . LEU B 1 53  ? 18.214  11.960  19.146  1.00 19.49  ? 15  LEU B CB    1 
ATOM   2034 C  CG    . LEU B 1 53  ? 18.499  13.303  18.467  1.00 14.40  ? 15  LEU B CG    1 
ATOM   2035 C  CD1   . LEU B 1 53  ? 18.369  13.137  16.986  1.00 27.45  ? 15  LEU B CD1   1 
ATOM   2036 C  CD2   . LEU B 1 53  ? 17.543  14.366  18.944  1.00 10.80  ? 15  LEU B CD2   1 
ATOM   2037 N  N     . GLY B 1 54  ? 20.991  11.928  20.598  1.00 17.42  ? 16  GLY B N     1 
ATOM   2038 C  CA    . GLY B 1 54  ? 22.296  12.518  20.781  1.00 19.41  ? 16  GLY B CA    1 
ATOM   2039 C  C     . GLY B 1 54  ? 23.342  11.436  20.803  1.00 18.31  ? 16  GLY B C     1 
ATOM   2040 O  O     . GLY B 1 54  ? 23.036  10.246  20.751  1.00 25.12  ? 16  GLY B O     1 
ATOM   2041 N  N     . ASP B 1 55  ? 24.598  11.877  20.857  1.00 24.19  ? 17  ASP B N     1 
ATOM   2042 C  CA    . ASP B 1 55  ? 25.712  10.947  20.952  1.00 19.92  ? 17  ASP B CA    1 
ATOM   2043 C  C     . ASP B 1 55  ? 25.434  9.915   22.034  1.00 28.09  ? 17  ASP B C     1 
ATOM   2044 O  O     . ASP B 1 55  ? 24.843  10.223  23.072  1.00 25.66  ? 17  ASP B O     1 
ATOM   2045 C  CB    . ASP B 1 55  ? 27.007  11.703  21.260  1.00 23.33  ? 17  ASP B CB    1 
ATOM   2046 C  CG    . ASP B 1 55  ? 27.622  12.354  20.026  1.00 26.59  ? 17  ASP B CG    1 
ATOM   2047 O  OD1   . ASP B 1 55  ? 26.875  12.724  19.097  1.00 31.01  ? 17  ASP B OD1   1 
ATOM   2048 O  OD2   . ASP B 1 55  ? 28.857  12.514  19.992  1.00 23.67  ? 17  ASP B OD2   1 
ATOM   2049 N  N     . SER B 1 56  ? 25.833  8.675   21.781  1.00 20.15  ? 18  SER B N     1 
ATOM   2050 C  CA    . SER B 1 56  ? 25.680  7.659   22.806  1.00 22.05  ? 18  SER B CA    1 
ATOM   2051 C  C     . SER B 1 56  ? 26.462  8.044   24.058  1.00 18.06  ? 18  SER B C     1 
ATOM   2052 O  O     . SER B 1 56  ? 27.508  8.702   23.998  1.00 20.25  ? 18  SER B O     1 
ATOM   2053 C  CB    . SER B 1 56  ? 26.146  6.305   22.291  1.00 22.05  ? 18  SER B CB    1 
ATOM   2054 O  OG    . SER B 1 56  ? 26.567  5.504   23.373  1.00 22.56  ? 18  SER B OG    1 
ATOM   2055 N  N     . GLY B 1 57  ? 25.927  7.644   25.205  1.00 18.74  ? 19  GLY B N     1 
ATOM   2056 C  CA    . GLY B 1 57  ? 26.545  7.908   26.484  1.00 14.87  ? 19  GLY B CA    1 
ATOM   2057 C  C     . GLY B 1 57  ? 26.327  9.294   27.057  1.00 16.36  ? 19  GLY B C     1 
ATOM   2058 O  O     . GLY B 1 57  ? 26.871  9.584   28.128  1.00 28.96  ? 19  GLY B O     1 
ATOM   2059 N  N     . VAL B 1 58  ? 25.552  10.159  26.396  1.00 22.74  ? 20  VAL B N     1 
ATOM   2060 C  CA    . VAL B 1 58  ? 25.291  11.487  26.951  1.00 21.37  ? 20  VAL B CA    1 
ATOM   2061 C  C     . VAL B 1 58  ? 24.151  11.477  27.957  1.00 22.61  ? 20  VAL B C     1 
ATOM   2062 O  O     . VAL B 1 58  ? 24.024  12.424  28.738  1.00 20.95  ? 20  VAL B O     1 
ATOM   2063 C  CB    . VAL B 1 58  ? 24.969  12.524  25.859  1.00 21.95  ? 20  VAL B CB    1 
ATOM   2064 C  CG1   . VAL B 1 58  ? 26.102  12.628  24.881  1.00 21.77  ? 20  VAL B CG1   1 
ATOM   2065 C  CG2   . VAL B 1 58  ? 23.659  12.184  25.148  1.00 18.49  ? 20  VAL B CG2   1 
ATOM   2066 N  N     . GLY B 1 59  ? 23.301  10.456  27.941  1.00 20.53  ? 21  GLY B N     1 
ATOM   2067 C  CA    . GLY B 1 59  ? 22.292  10.310  28.968  1.00 18.76  ? 21  GLY B CA    1 
ATOM   2068 C  C     . GLY B 1 59  ? 20.823  10.356  28.583  1.00 20.14  ? 21  GLY B C     1 
ATOM   2069 O  O     . GLY B 1 59  ? 19.997  10.677  29.439  1.00 18.23  ? 21  GLY B O     1 
ATOM   2070 N  N     . LYS B 1 60  ? 20.457  10.037  27.335  1.00 23.59  ? 22  LYS B N     1 
ATOM   2071 C  CA    . LYS B 1 60  ? 19.057  10.198  26.937  1.00 17.28  ? 22  LYS B CA    1 
ATOM   2072 C  C     . LYS B 1 60  ? 18.147  9.216   27.665  1.00 18.82  ? 22  LYS B C     1 
ATOM   2073 O  O     . LYS B 1 60  ? 17.005  9.548   28.008  1.00 17.71  ? 22  LYS B O     1 
ATOM   2074 C  CB    . LYS B 1 60  ? 18.900  10.014  25.434  1.00 22.88  ? 22  LYS B CB    1 
ATOM   2075 C  CG    . LYS B 1 60  ? 19.927  10.710  24.583  1.00 26.70  ? 22  LYS B CG    1 
ATOM   2076 C  CD    . LYS B 1 60  ? 19.948  10.057  23.226  1.00 14.57  ? 22  LYS B CD    1 
ATOM   2077 C  CE    . LYS B 1 60  ? 20.799  8.833   23.224  1.00 16.94  ? 22  LYS B CE    1 
ATOM   2078 N  NZ    . LYS B 1 60  ? 22.195  9.265   23.414  1.00 19.92  ? 22  LYS B NZ    1 
ATOM   2079 N  N     . THR B 1 61  ? 18.608  7.983   27.848  1.00 14.23  ? 23  THR B N     1 
ATOM   2080 C  CA    . THR B 1 61  ? 17.822  7.006   28.594  1.00 13.45  ? 23  THR B CA    1 
ATOM   2081 C  C     . THR B 1 61  ? 17.709  7.411   30.071  1.00 15.38  ? 23  THR B C     1 
ATOM   2082 O  O     . THR B 1 61  ? 16.617  7.403   30.652  1.00 12.99  ? 23  THR B O     1 
ATOM   2083 C  CB    . THR B 1 61  ? 18.467  5.630   28.411  1.00 14.74  ? 23  THR B CB    1 
ATOM   2084 O  OG1   . THR B 1 61  ? 18.506  5.319   27.005  1.00 14.91  ? 23  THR B OG1   1 
ATOM   2085 C  CG2   . THR B 1 61  ? 17.714  4.545   29.133  1.00 3.24   ? 23  THR B CG2   1 
ATOM   2086 N  N     . SER B 1 62  ? 18.822  7.815   30.684  1.00 16.61  ? 24  SER B N     1 
ATOM   2087 C  CA    . SER B 1 62  ? 18.768  8.295   32.062  1.00 14.07  ? 24  SER B CA    1 
ATOM   2088 C  C     . SER B 1 62  ? 17.843  9.500   32.226  1.00 16.46  ? 24  SER B C     1 
ATOM   2089 O  O     . SER B 1 62  ? 17.141  9.608   33.239  1.00 22.04  ? 24  SER B O     1 
ATOM   2090 C  CB    . SER B 1 62  ? 20.170  8.627   32.553  1.00 13.27  ? 24  SER B CB    1 
ATOM   2091 O  OG    . SER B 1 62  ? 20.996  7.485   32.533  1.00 15.08  ? 24  SER B OG    1 
ATOM   2092 N  N     . VAL B 1 63  ? 17.834  10.422  31.258  1.00 12.21  ? 25  VAL B N     1 
ATOM   2093 C  CA    . VAL B 1 63  ? 17.006  11.625  31.373  1.00 13.86  ? 25  VAL B CA    1 
ATOM   2094 C  C     . VAL B 1 63  ? 15.532  11.262  31.493  1.00 15.88  ? 25  VAL B C     1 
ATOM   2095 O  O     . VAL B 1 63  ? 14.789  11.852  32.289  1.00 27.10  ? 25  VAL B O     1 
ATOM   2096 C  CB    . VAL B 1 63  ? 17.242  12.568  30.172  1.00 18.15  ? 25  VAL B CB    1 
ATOM   2097 C  CG1   . VAL B 1 63  ? 16.026  13.448  29.904  1.00 10.33  ? 25  VAL B CG1   1 
ATOM   2098 C  CG2   . VAL B 1 63  ? 18.421  13.441  30.395  1.00 7.50   ? 25  VAL B CG2   1 
ATOM   2099 N  N     . LEU B 1 64  ? 15.069  10.310  30.692  1.00 19.05  ? 26  LEU B N     1 
ATOM   2100 C  CA    . LEU B 1 64  ? 13.635  10.066  30.677  1.00 19.92  ? 26  LEU B CA    1 
ATOM   2101 C  C     . LEU B 1 64  ? 13.224  9.175   31.833  1.00 19.39  ? 26  LEU B C     1 
ATOM   2102 O  O     . LEU B 1 64  ? 12.096  9.288   32.323  1.00 27.38  ? 26  LEU B O     1 
ATOM   2103 C  CB    . LEU B 1 64  ? 13.209  9.458   29.333  1.00 25.86  ? 26  LEU B CB    1 
ATOM   2104 C  CG    . LEU B 1 64  ? 13.879  9.960   28.032  1.00 28.35  ? 26  LEU B CG    1 
ATOM   2105 C  CD1   . LEU B 1 64  ? 13.482  9.073   26.892  1.00 16.95  ? 26  LEU B CD1   1 
ATOM   2106 C  CD2   . LEU B 1 64  ? 13.579  11.415  27.657  1.00 16.27  ? 26  LEU B CD2   1 
ATOM   2107 N  N     . TYR B 1 65  ? 14.128  8.301   32.288  1.00 28.95  ? 27  TYR B N     1 
ATOM   2108 C  CA    . TYR B 1 65  ? 13.859  7.499   33.478  1.00 16.10  ? 27  TYR B CA    1 
ATOM   2109 C  C     . TYR B 1 65  ? 13.713  8.395   34.692  1.00 24.76  ? 27  TYR B C     1 
ATOM   2110 O  O     . TYR B 1 65  ? 12.800  8.216   35.510  1.00 20.24  ? 27  TYR B O     1 
ATOM   2111 C  CB    . TYR B 1 65  ? 14.979  6.477   33.689  1.00 12.09  ? 27  TYR B CB    1 
ATOM   2112 C  CG    . TYR B 1 65  ? 14.705  5.500   34.810  1.00 15.94  ? 27  TYR B CG    1 
ATOM   2113 C  CD1   . TYR B 1 65  ? 13.512  4.802   34.861  1.00 19.04  ? 27  TYR B CD1   1 
ATOM   2114 C  CD2   . TYR B 1 65  ? 15.636  5.275   35.814  1.00 12.94  ? 27  TYR B CD2   1 
ATOM   2115 C  CE1   . TYR B 1 65  ? 13.246  3.904   35.881  1.00 17.47  ? 27  TYR B CE1   1 
ATOM   2116 C  CE2   . TYR B 1 65  ? 15.378  4.388   36.839  1.00 10.80  ? 27  TYR B CE2   1 
ATOM   2117 C  CZ    . TYR B 1 65  ? 14.174  3.708   36.869  1.00 15.54  ? 27  TYR B CZ    1 
ATOM   2118 O  OH    . TYR B 1 65  ? 13.894  2.807   37.875  1.00 18.91  ? 27  TYR B OH    1 
ATOM   2119 N  N     . GLN B 1 66  ? 14.595  9.384   34.813  1.00 20.20  ? 28  GLN B N     1 
ATOM   2120 C  CA    . GLN B 1 66  ? 14.425  10.400  35.841  1.00 22.09  ? 28  GLN B CA    1 
ATOM   2121 C  C     . GLN B 1 66  ? 13.032  11.013  35.753  1.00 21.19  ? 28  GLN B C     1 
ATOM   2122 O  O     . GLN B 1 66  ? 12.271  10.994  36.725  1.00 21.52  ? 28  GLN B O     1 
ATOM   2123 C  CB    . GLN B 1 66  ? 15.525  11.461  35.703  1.00 17.00  ? 28  GLN B CB    1 
ATOM   2124 C  CG    . GLN B 1 66  ? 15.505  12.565  36.743  1.00 24.14  ? 28  GLN B CG    1 
ATOM   2125 C  CD    . GLN B 1 66  ? 15.504  12.061  38.192  1.00 22.22  ? 28  GLN B CD    1 
ATOM   2126 O  OE1   . GLN B 1 66  ? 14.565  12.324  38.939  1.00 33.40  ? 28  GLN B OE1   1 
ATOM   2127 N  NE2   . GLN B 1 66  ? 16.563  11.358  38.594  1.00 15.87  ? 28  GLN B NE2   1 
ATOM   2128 N  N     . TYR B 1 67  ? 12.646  11.488  34.565  1.00 22.84  ? 29  TYR B N     1 
ATOM   2129 C  CA    . TYR B 1 67  ? 11.417  12.273  34.448  1.00 16.89  ? 29  TYR B CA    1 
ATOM   2130 C  C     . TYR B 1 67  ? 10.157  11.434  34.646  1.00 22.04  ? 29  TYR B C     1 
ATOM   2131 O  O     . TYR B 1 67  ? 9.144   11.958  35.121  1.00 18.10  ? 29  TYR B O     1 
ATOM   2132 C  CB    . TYR B 1 67  ? 11.394  12.969  33.095  1.00 21.57  ? 29  TYR B CB    1 
ATOM   2133 C  CG    . TYR B 1 67  ? 10.087  13.584  32.667  1.00 14.40  ? 29  TYR B CG    1 
ATOM   2134 C  CD1   . TYR B 1 67  ? 9.646   14.791  33.187  1.00 16.11  ? 29  TYR B CD1   1 
ATOM   2135 C  CD2   . TYR B 1 67  ? 9.325   12.981  31.697  1.00 11.10  ? 29  TYR B CD2   1 
ATOM   2136 C  CE1   . TYR B 1 67  ? 8.451   15.356  32.759  1.00 19.60  ? 29  TYR B CE1   1 
ATOM   2137 C  CE2   . TYR B 1 67  ? 8.148   13.533  31.264  1.00 17.06  ? 29  TYR B CE2   1 
ATOM   2138 C  CZ    . TYR B 1 67  ? 7.706   14.711  31.786  1.00 19.26  ? 29  TYR B CZ    1 
ATOM   2139 O  OH    . TYR B 1 67  ? 6.513   15.225  31.309  1.00 11.50  ? 29  TYR B OH    1 
ATOM   2140 N  N     . THR B 1 68  ? 10.178  10.151  34.279  1.00 19.10  ? 30  THR B N     1 
ATOM   2141 C  CA    . THR B 1 68  ? 8.979   9.343   34.473  1.00 25.91  ? 30  THR B CA    1 
ATOM   2142 C  C     . THR B 1 68  ? 8.930   8.690   35.840  1.00 23.46  ? 30  THR B C     1 
ATOM   2143 O  O     . THR B 1 68  ? 7.831   8.482   36.366  1.00 24.03  ? 30  THR B O     1 
ATOM   2144 C  CB    . THR B 1 68  ? 8.861   8.236   33.417  1.00 21.34  ? 30  THR B CB    1 
ATOM   2145 O  OG1   . THR B 1 68  ? 10.089  7.504   33.354  1.00 16.56  ? 30  THR B OG1   1 
ATOM   2146 C  CG2   . THR B 1 68  ? 8.498   8.803   32.063  1.00 17.27  ? 30  THR B CG2   1 
ATOM   2147 N  N     . ASP B 1 69  ? 10.095  8.364   36.422  1.00 26.90  ? 31  ASP B N     1 
ATOM   2148 C  CA    . ASP B 1 69  ? 10.187  7.631   37.686  1.00 23.19  ? 31  ASP B CA    1 
ATOM   2149 C  C     . ASP B 1 69  ? 10.803  8.414   38.829  1.00 20.02  ? 31  ASP B C     1 
ATOM   2150 O  O     . ASP B 1 69  ? 10.538  8.086   39.981  1.00 22.78  ? 31  ASP B O     1 
ATOM   2151 C  CB    . ASP B 1 69  ? 11.027  6.344   37.529  1.00 20.49  ? 31  ASP B CB    1 
ATOM   2152 C  CG    . ASP B 1 69  ? 10.284  5.236   36.818  1.00 25.75  ? 31  ASP B CG    1 
ATOM   2153 O  OD1   . ASP B 1 69  ? 9.352   5.549   36.058  1.00 25.69  ? 31  ASP B OD1   1 
ATOM   2154 O  OD2   . ASP B 1 69  ? 10.616  4.050   37.035  1.00 35.92  ? 31  ASP B OD2   1 
ATOM   2155 N  N     . GLY B 1 70  ? 11.644  9.404   38.554  1.00 20.98  ? 32  GLY B N     1 
ATOM   2156 C  CA    . GLY B 1 70  ? 12.411  10.025  39.617  1.00 18.20  ? 32  GLY B CA    1 
ATOM   2157 C  C     . GLY B 1 70  ? 13.518  9.170   40.202  1.00 20.99  ? 32  GLY B C     1 
ATOM   2158 O  O     . GLY B 1 70  ? 13.788  9.260   41.402  1.00 27.98  ? 32  GLY B O     1 
ATOM   2159 N  N     . LYS B 1 71  ? 14.171  8.349   39.389  1.00 18.63  ? 33  LYS B N     1 
ATOM   2160 C  CA    . LYS B 1 71  ? 15.218  7.446   39.842  1.00 15.54  ? 33  LYS B CA    1 
ATOM   2161 C  C     . LYS B 1 71  ? 16.378  7.546   38.866  1.00 12.06  ? 33  LYS B C     1 
ATOM   2162 O  O     . LYS B 1 71  ? 16.263  8.178   37.821  1.00 21.42  ? 33  LYS B O     1 
ATOM   2163 C  CB    . LYS B 1 71  ? 14.701  6.010   39.948  1.00 14.56  ? 33  LYS B CB    1 
ATOM   2164 C  CG    . LYS B 1 71  ? 13.397  5.866   40.766  1.00 10.12  ? 33  LYS B CG    1 
ATOM   2165 C  CD    . LYS B 1 71  ? 13.333  4.481   41.327  1.00 11.54  ? 33  LYS B CD    1 
ATOM   2166 C  CE    . LYS B 1 71  ? 11.971  3.835   41.297  1.00 11.25  ? 33  LYS B CE    1 
ATOM   2167 N  NZ    . LYS B 1 71  ? 12.236  2.389   41.616  1.00 13.75  ? 33  LYS B NZ    1 
ATOM   2168 N  N     . PHE B 1 72  ? 17.514  6.941   39.207  1.00 16.85  ? 34  PHE B N     1 
ATOM   2169 C  CA    . PHE B 1 72  ? 18.691  7.065   38.351  1.00 14.91  ? 34  PHE B CA    1 
ATOM   2170 C  C     . PHE B 1 72  ? 19.624  5.879   38.584  1.00 16.87  ? 34  PHE B C     1 
ATOM   2171 O  O     . PHE B 1 72  ? 20.198  5.751   39.662  1.00 19.08  ? 34  PHE B O     1 
ATOM   2172 C  CB    . PHE B 1 72  ? 19.424  8.370   38.602  1.00 21.82  ? 34  PHE B CB    1 
ATOM   2173 C  CG    . PHE B 1 72  ? 20.813  8.420   38.006  1.00 16.36  ? 34  PHE B CG    1 
ATOM   2174 C  CD1   . PHE B 1 72  ? 20.995  8.483   36.644  1.00 19.53  ? 34  PHE B CD1   1 
ATOM   2175 C  CD2   . PHE B 1 72  ? 21.931  8.424   38.825  1.00 18.81  ? 34  PHE B CD2   1 
ATOM   2176 C  CE1   . PHE B 1 72  ? 22.272  8.535   36.101  1.00 22.39  ? 34  PHE B CE1   1 
ATOM   2177 C  CE2   . PHE B 1 72  ? 23.213  8.480   38.305  1.00 17.68  ? 34  PHE B CE2   1 
ATOM   2178 C  CZ    . PHE B 1 72  ? 23.387  8.536   36.947  1.00 26.88  ? 34  PHE B CZ    1 
ATOM   2179 N  N     A ASN B 1 73  ? 19.743  5.025   37.577  0.43 21.23  ? 35  ASN B N     1 
ATOM   2180 N  N     B ASN B 1 73  ? 19.785  5.068   37.555  0.57 21.07  ? 35  ASN B N     1 
ATOM   2181 C  CA    A ASN B 1 73  ? 20.724  3.947   37.619  0.43 19.24  ? 35  ASN B CA    1 
ATOM   2182 C  CA    B ASN B 1 73  ? 20.736  3.968   37.590  0.57 19.23  ? 35  ASN B CA    1 
ATOM   2183 C  C     A ASN B 1 73  ? 22.076  4.479   37.155  0.43 20.09  ? 35  ASN B C     1 
ATOM   2184 C  C     B ASN B 1 73  ? 22.100  4.451   37.117  0.57 20.10  ? 35  ASN B C     1 
ATOM   2185 O  O     A ASN B 1 73  ? 22.162  5.198   36.155  0.43 21.22  ? 35  ASN B O     1 
ATOM   2186 O  O     B ASN B 1 73  ? 22.213  5.100   36.074  0.57 21.32  ? 35  ASN B O     1 
ATOM   2187 C  CB    A ASN B 1 73  ? 20.265  2.775   36.745  0.43 17.20  ? 35  ASN B CB    1 
ATOM   2188 C  CB    B ASN B 1 73  ? 20.230  2.819   36.724  0.57 16.91  ? 35  ASN B CB    1 
ATOM   2189 C  CG    A ASN B 1 73  ? 21.344  1.706   36.575  0.43 20.80  ? 35  ASN B CG    1 
ATOM   2190 C  CG    B ASN B 1 73  ? 18.977  2.229   37.268  0.57 17.56  ? 35  ASN B CG    1 
ATOM   2191 O  OD1   A ASN B 1 73  ? 22.183  1.492   37.461  0.43 15.84  ? 35  ASN B OD1   1 
ATOM   2192 O  OD1   B ASN B 1 73  ? 18.575  2.553   38.392  0.57 19.04  ? 35  ASN B OD1   1 
ATOM   2193 N  ND2   A ASN B 1 73  ? 21.329  1.036   35.423  0.43 20.16  ? 35  ASN B ND2   1 
ATOM   2194 N  ND2   B ASN B 1 73  ? 18.336  1.359   36.493  0.57 15.54  ? 35  ASN B ND2   1 
ATOM   2195 N  N     . SER B 1 74  ? 23.134  4.141   37.896  1.00 17.71  ? 36  SER B N     1 
ATOM   2196 C  CA    . SER B 1 74  ? 24.468  4.597   37.549  1.00 19.66  ? 36  SER B CA    1 
ATOM   2197 C  C     . SER B 1 74  ? 25.136  3.712   36.520  1.00 20.44  ? 36  SER B C     1 
ATOM   2198 O  O     . SER B 1 74  ? 26.097  4.150   35.882  1.00 16.62  ? 36  SER B O     1 
ATOM   2199 C  CB    . SER B 1 74  ? 25.353  4.650   38.793  1.00 16.77  ? 36  SER B CB    1 
ATOM   2200 O  OG    . SER B 1 74  ? 25.110  5.850   39.492  1.00 29.05  ? 36  SER B OG    1 
ATOM   2201 N  N     . LYS B 1 75  ? 24.678  2.473   36.386  1.00 19.41  ? 37  LYS B N     1 
ATOM   2202 C  CA    . LYS B 1 75  ? 25.316  1.498   35.518  1.00 20.34  ? 37  LYS B CA    1 
ATOM   2203 C  C     . LYS B 1 75  ? 24.921  1.761   34.074  1.00 20.63  ? 37  LYS B C     1 
ATOM   2204 O  O     . LYS B 1 75  ? 23.731  1.770   33.752  1.00 13.45  ? 37  LYS B O     1 
ATOM   2205 C  CB    . LYS B 1 75  ? 24.903  0.086   35.906  1.00 16.67  ? 37  LYS B CB    1 
ATOM   2206 C  CG    . LYS B 1 75  ? 25.740  -0.973  35.239  1.00 17.03  ? 37  LYS B CG    1 
ATOM   2207 C  CD    . LYS B 1 75  ? 25.005  -2.295  35.172  1.00 27.14  ? 37  LYS B CD    1 
ATOM   2208 C  CE    . LYS B 1 75  ? 25.832  -3.327  34.420  1.00 18.46  ? 37  LYS B CE    1 
ATOM   2209 N  NZ    . LYS B 1 75  ? 25.053  -4.588  34.203  1.00 22.89  ? 37  LYS B NZ    1 
ATOM   2210 N  N     . PHE B 1 76  ? 25.910  1.938   33.202  1.00 14.49  ? 38  PHE B N     1 
ATOM   2211 C  CA    . PHE B 1 76  ? 25.621  2.216   31.803  1.00 19.93  ? 38  PHE B CA    1 
ATOM   2212 C  C     . PHE B 1 76  ? 25.095  0.964   31.116  1.00 18.67  ? 38  PHE B C     1 
ATOM   2213 O  O     . PHE B 1 76  ? 25.825  -0.006  30.914  1.00 15.15  ? 38  PHE B O     1 
ATOM   2214 C  CB    . PHE B 1 76  ? 26.855  2.736   31.086  1.00 21.29  ? 38  PHE B CB    1 
ATOM   2215 C  CG    . PHE B 1 76  ? 26.623  3.029   29.640  1.00 19.00  ? 38  PHE B CG    1 
ATOM   2216 C  CD1   . PHE B 1 76  ? 25.380  3.448   29.191  1.00 25.55  ? 38  PHE B CD1   1 
ATOM   2217 C  CD2   . PHE B 1 76  ? 27.642  2.886   28.727  1.00 24.86  ? 38  PHE B CD2   1 
ATOM   2218 C  CE1   . PHE B 1 76  ? 25.163  3.713   27.865  1.00 19.10  ? 38  PHE B CE1   1 
ATOM   2219 C  CE2   . PHE B 1 76  ? 27.432  3.158   27.397  1.00 12.36  ? 38  PHE B CE2   1 
ATOM   2220 C  CZ    . PHE B 1 76  ? 26.193  3.572   26.967  1.00 21.25  ? 38  PHE B CZ    1 
ATOM   2221 N  N     . ILE B 1 77  ? 23.817  0.988   30.767  1.00 20.72  ? 39  ILE B N     1 
ATOM   2222 C  CA    . ILE B 1 77  ? 23.205  -0.033  29.941  1.00 18.04  ? 39  ILE B CA    1 
ATOM   2223 C  C     . ILE B 1 77  ? 22.817  0.659   28.637  1.00 21.18  ? 39  ILE B C     1 
ATOM   2224 O  O     . ILE B 1 77  ? 21.741  1.267   28.536  1.00 22.50  ? 39  ILE B O     1 
ATOM   2225 C  CB    . ILE B 1 77  ? 21.997  -0.666  30.657  1.00 24.39  ? 39  ILE B CB    1 
ATOM   2226 C  CG1   . ILE B 1 77  ? 22.430  -1.369  31.946  1.00 24.09  ? 39  ILE B CG1   1 
ATOM   2227 C  CG2   . ILE B 1 77  ? 21.255  -1.622  29.755  1.00 16.18  ? 39  ILE B CG2   1 
ATOM   2228 C  CD1   . ILE B 1 77  ? 21.271  -1.541  32.938  1.00 31.97  ? 39  ILE B CD1   1 
ATOM   2229 N  N     . THR B 1 78  ? 23.714  0.611   27.647  1.00 25.26  ? 40  THR B N     1 
ATOM   2230 C  CA    . THR B 1 78  ? 23.455  1.235   26.353  1.00 18.85  ? 40  THR B CA    1 
ATOM   2231 C  C     . THR B 1 78  ? 22.201  0.666   25.710  1.00 20.30  ? 40  THR B C     1 
ATOM   2232 O  O     . THR B 1 78  ? 21.818  -0.485  25.944  1.00 25.18  ? 40  THR B O     1 
ATOM   2233 C  CB    . THR B 1 78  ? 24.654  1.056   25.418  1.00 21.20  ? 40  THR B CB    1 
ATOM   2234 O  OG1   . THR B 1 78  ? 24.620  2.063   24.401  1.00 19.51  ? 40  THR B OG1   1 
ATOM   2235 C  CG2   . THR B 1 78  ? 24.661  -0.297  24.786  1.00 13.79  ? 40  THR B CG2   1 
ATOM   2236 N  N     . THR B 1 79  ? 21.553  1.499   24.900  1.00 22.04  ? 41  THR B N     1 
ATOM   2237 C  CA    . THR B 1 79  ? 20.243  1.186   24.345  1.00 20.69  ? 41  THR B CA    1 
ATOM   2238 C  C     . THR B 1 79  ? 20.352  0.332   23.089  1.00 21.94  ? 41  THR B C     1 
ATOM   2239 O  O     . THR B 1 79  ? 21.196  0.583   22.226  1.00 30.50  ? 41  THR B O     1 
ATOM   2240 C  CB    . THR B 1 79  ? 19.501  2.477   24.032  1.00 24.69  ? 41  THR B CB    1 
ATOM   2241 O  OG1   . THR B 1 79  ? 19.291  3.177   25.263  1.00 11.67  ? 41  THR B OG1   1 
ATOM   2242 C  CG2   . THR B 1 79  ? 18.152  2.218   23.286  1.00 12.45  ? 41  THR B CG2   1 
ATOM   2243 N  N     . VAL B 1 80  ? 19.485  -0.684  23.002  1.00 22.30  ? 42  VAL B N     1 
ATOM   2244 C  CA    . VAL B 1 80  ? 19.371  -1.548  21.833  1.00 23.28  ? 42  VAL B CA    1 
ATOM   2245 C  C     . VAL B 1 80  ? 18.537  -0.861  20.759  1.00 24.77  ? 42  VAL B C     1 
ATOM   2246 O  O     . VAL B 1 80  ? 17.410  -1.274  20.470  1.00 24.97  ? 42  VAL B O     1 
ATOM   2247 C  CB    . VAL B 1 80  ? 18.762  -2.906  22.216  1.00 26.07  ? 42  VAL B CB    1 
ATOM   2248 C  CG1   . VAL B 1 80  ? 18.870  -3.891  21.053  1.00 21.70  ? 42  VAL B CG1   1 
ATOM   2249 C  CG2   . VAL B 1 80  ? 19.443  -3.447  23.444  1.00 14.35  ? 42  VAL B CG2   1 
ATOM   2250 N  N     . GLY B 1 81  ? 19.074  0.202   20.173  1.00 26.57  ? 43  GLY B N     1 
ATOM   2251 C  CA    . GLY B 1 81  ? 18.432  0.802   19.024  1.00 21.59  ? 43  GLY B CA    1 
ATOM   2252 C  C     . GLY B 1 81  ? 17.336  1.786   19.342  1.00 22.16  ? 43  GLY B C     1 
ATOM   2253 O  O     . GLY B 1 81  ? 17.480  2.990   19.105  1.00 31.67  ? 43  GLY B O     1 
ATOM   2254 N  N     . ILE B 1 82  ? 16.232  1.287   19.887  1.00 22.36  ? 44  ILE B N     1 
ATOM   2255 C  CA    . ILE B 1 82  ? 15.030  2.085   20.043  1.00 16.87  ? 44  ILE B CA    1 
ATOM   2256 C  C     . ILE B 1 82  ? 14.305  1.617   21.301  1.00 21.40  ? 44  ILE B C     1 
ATOM   2257 O  O     . ILE B 1 82  ? 14.397  0.448   21.688  1.00 20.56  ? 44  ILE B O     1 
ATOM   2258 C  CB    . ILE B 1 82  ? 14.166  1.976   18.756  1.00 15.40  ? 44  ILE B CB    1 
ATOM   2259 C  CG1   . ILE B 1 82  ? 13.283  3.201   18.586  1.00 19.23  ? 44  ILE B CG1   1 
ATOM   2260 C  CG2   . ILE B 1 82  ? 13.355  0.703   18.732  1.00 16.10  ? 44  ILE B CG2   1 
ATOM   2261 C  CD1   . ILE B 1 82  ? 14.081  4.483   18.533  1.00 19.50  ? 44  ILE B CD1   1 
ATOM   2262 N  N     . ASP B 1 83  ? 13.628  2.557   21.973  1.00 19.63  ? 45  ASP B N     1 
ATOM   2263 C  CA    . ASP B 1 83  ? 12.726  2.277   23.095  1.00 18.65  ? 45  ASP B CA    1 
ATOM   2264 C  C     . ASP B 1 83  ? 11.969  3.546   23.453  1.00 16.08  ? 45  ASP B C     1 
ATOM   2265 O  O     . ASP B 1 83  ? 12.371  4.657   23.097  1.00 25.38  ? 45  ASP B O     1 
ATOM   2266 C  CB    . ASP B 1 83  ? 13.462  1.747   24.339  1.00 13.43  ? 45  ASP B CB    1 
ATOM   2267 C  CG    . ASP B 1 83  ? 12.543  0.973   25.273  1.00 14.74  ? 45  ASP B CG    1 
ATOM   2268 O  OD1   . ASP B 1 83  ? 11.307  1.096   25.150  1.00 18.29  ? 45  ASP B OD1   1 
ATOM   2269 O  OD2   . ASP B 1 83  ? 13.048  0.196   26.105  1.00 20.52  ? 45  ASP B OD2   1 
ATOM   2270 N  N     . PHE B 1 84  ? 10.880  3.373   24.192  1.00 20.86  ? 46  PHE B N     1 
ATOM   2271 C  CA    . PHE B 1 84  ? 10.056  4.512   24.533  1.00 16.17  ? 46  PHE B CA    1 
ATOM   2272 C  C     . PHE B 1 84  ? 9.413   4.296   25.894  1.00 18.51  ? 46  PHE B C     1 
ATOM   2273 O  O     . PHE B 1 84  ? 9.293   3.172   26.381  1.00 13.18  ? 46  PHE B O     1 
ATOM   2274 C  CB    . PHE B 1 84  ? 8.982   4.769   23.467  1.00 14.77  ? 46  PHE B CB    1 
ATOM   2275 C  CG    . PHE B 1 84  ? 7.782   3.846   23.557  1.00 18.73  ? 46  PHE B CG    1 
ATOM   2276 C  CD1   . PHE B 1 84  ? 6.721   4.135   24.411  1.00 13.99  ? 46  PHE B CD1   1 
ATOM   2277 C  CD2   . PHE B 1 84  ? 7.694   2.715   22.753  1.00 16.29  ? 46  PHE B CD2   1 
ATOM   2278 C  CE1   . PHE B 1 84  ? 5.623   3.303   24.496  1.00 13.49  ? 46  PHE B CE1   1 
ATOM   2279 C  CE2   . PHE B 1 84  ? 6.598   1.890   22.818  1.00 14.18  ? 46  PHE B CE2   1 
ATOM   2280 C  CZ    . PHE B 1 84  ? 5.566   2.173   23.692  1.00 25.04  ? 46  PHE B CZ    1 
ATOM   2281 N  N     . ARG B 1 85  ? 8.967   5.405   26.476  1.00 13.22  ? 47  ARG B N     1 
ATOM   2282 C  CA    . ARG B 1 85  ? 8.227   5.442   27.720  1.00 18.47  ? 47  ARG B CA    1 
ATOM   2283 C  C     . ARG B 1 85  ? 6.956   6.234   27.479  1.00 18.53  ? 47  ARG B C     1 
ATOM   2284 O  O     . ARG B 1 85  ? 6.763   6.832   26.417  1.00 20.97  ? 47  ARG B O     1 
ATOM   2285 C  CB    . ARG B 1 85  ? 9.047   6.098   28.853  1.00 17.27  ? 47  ARG B CB    1 
ATOM   2286 C  CG    . ARG B 1 85  ? 10.465  5.549   29.035  1.00 10.00  ? 47  ARG B CG    1 
ATOM   2287 C  CD    . ARG B 1 85  ? 11.065  5.923   30.425  1.00 17.44  ? 47  ARG B CD    1 
ATOM   2288 N  NE    . ARG B 1 85  ? 10.626  4.980   31.442  1.00 24.33  ? 47  ARG B NE    1 
ATOM   2289 C  CZ    . ARG B 1 85  ? 11.383  4.018   31.954  1.00 22.22  ? 47  ARG B CZ    1 
ATOM   2290 N  NH1   . ARG B 1 85  ? 12.645  3.894   31.562  1.00 25.06  ? 47  ARG B NH1   1 
ATOM   2291 N  NH2   . ARG B 1 85  ? 10.870  3.186   32.854  1.00 14.40  ? 47  ARG B NH2   1 
ATOM   2292 N  N     . GLU B 1 86  ? 6.100   6.257   28.493  1.00 21.08  ? 48  GLU B N     1 
ATOM   2293 C  CA    . GLU B 1 86  ? 4.888   7.052   28.480  1.00 20.74  ? 48  GLU B CA    1 
ATOM   2294 C  C     . GLU B 1 86  ? 4.788   7.835   29.778  1.00 31.03  ? 48  GLU B C     1 
ATOM   2295 O  O     . GLU B 1 86  ? 5.434   7.511   30.781  1.00 23.22  ? 48  GLU B O     1 
ATOM   2296 C  CB    . GLU B 1 86  ? 3.653   6.178   28.310  1.00 23.53  ? 48  GLU B CB    1 
ATOM   2297 C  CG    . GLU B 1 86  ? 3.759   5.272   27.117  1.00 22.41  ? 48  GLU B CG    1 
ATOM   2298 C  CD    . GLU B 1 86  ? 2.748   4.168   27.160  1.00 28.13  ? 48  GLU B CD    1 
ATOM   2299 O  OE1   . GLU B 1 86  ? 1.572   4.482   27.447  1.00 35.39  ? 48  GLU B OE1   1 
ATOM   2300 O  OE2   . GLU B 1 86  ? 3.126   2.996   26.898  1.00 31.54  ? 48  GLU B OE2   1 
ATOM   2301 N  N     . LYS B 1 87  ? 3.971   8.882   29.747  1.00 25.16  ? 49  LYS B N     1 
ATOM   2302 C  CA    . LYS B 1 87  ? 3.691   9.628   30.963  1.00 22.22  ? 49  LYS B CA    1 
ATOM   2303 C  C     . LYS B 1 87  ? 2.437   10.437  30.738  1.00 19.61  ? 49  LYS B C     1 
ATOM   2304 O  O     . LYS B 1 87  ? 2.380   11.218  29.790  1.00 27.86  ? 49  LYS B O     1 
ATOM   2305 C  CB    . LYS B 1 87  ? 4.845   10.537  31.340  1.00 29.71  ? 49  LYS B CB    1 
ATOM   2306 C  CG    . LYS B 1 87  ? 4.677   11.182  32.716  1.00 27.17  ? 49  LYS B CG    1 
ATOM   2307 C  CD    . LYS B 1 87  ? 6.024   11.535  33.314  1.00 14.49  ? 49  LYS B CD    1 
ATOM   2308 C  CE    . LYS B 1 87  ? 5.911   12.723  34.248  1.00 16.29  ? 49  LYS B CE    1 
ATOM   2309 N  NZ    . LYS B 1 87  ? 6.078   12.311  35.662  1.00 25.98  ? 49  LYS B NZ    1 
ATOM   2310 N  N     . ARG B 1 88  ? 1.435   10.224  31.586  1.00 29.37  ? 50  ARG B N     1 
ATOM   2311 C  CA    . ARG B 1 88  ? 0.284   11.108  31.659  1.00 25.14  ? 50  ARG B CA    1 
ATOM   2312 C  C     . ARG B 1 88  ? 0.685   12.365  32.412  1.00 25.49  ? 50  ARG B C     1 
ATOM   2313 O  O     . ARG B 1 88  ? 1.307   12.286  33.471  1.00 32.15  ? 50  ARG B O     1 
ATOM   2314 C  CB    . ARG B 1 88  ? -0.869  10.406  32.366  1.00 26.25  ? 50  ARG B CB    1 
ATOM   2315 C  CG    . ARG B 1 88  ? -1.069  8.969   31.907  1.00 30.65  ? 50  ARG B CG    1 
ATOM   2316 C  CD    . ARG B 1 88  ? -1.708  8.949   30.528  1.00 34.87  ? 50  ARG B CD    1 
ATOM   2317 N  NE    . ARG B 1 88  ? -1.973  7.591   30.050  1.00 46.81  ? 50  ARG B NE    1 
ATOM   2318 C  CZ    . ARG B 1 88  ? -2.975  7.268   29.233  1.00 50.32  ? 50  ARG B CZ    1 
ATOM   2319 N  NH1   . ARG B 1 88  ? -3.138  6.007   28.852  1.00 51.42  ? 50  ARG B NH1   1 
ATOM   2320 N  NH2   . ARG B 1 88  ? -3.821  8.199   28.801  1.00 40.49  ? 50  ARG B NH2   1 
ATOM   2321 N  N     . VAL B 1 89  ? 0.359   13.526  31.854  1.00 30.79  ? 51  VAL B N     1 
ATOM   2322 C  CA    . VAL B 1 89  ? 0.696   14.815  32.445  1.00 28.37  ? 51  VAL B CA    1 
ATOM   2323 C  C     . VAL B 1 89  ? -0.419  15.797  32.098  1.00 33.45  ? 51  VAL B C     1 
ATOM   2324 O  O     . VAL B 1 89  ? -1.297  15.507  31.282  1.00 32.21  ? 51  VAL B O     1 
ATOM   2325 C  CB    . VAL B 1 89  ? 2.063   15.350  31.954  1.00 28.34  ? 51  VAL B CB    1 
ATOM   2326 C  CG1   . VAL B 1 89  ? 3.201   14.369  32.282  1.00 20.99  ? 51  VAL B CG1   1 
ATOM   2327 C  CG2   . VAL B 1 89  ? 2.011   15.650  30.464  1.00 33.77  ? 51  VAL B CG2   1 
ATOM   2328 N  N     . VAL B 1 90  ? -0.391  16.971  32.730  1.00 29.28  ? 52  VAL B N     1 
ATOM   2329 C  CA    . VAL B 1 90  ? -1.349  18.039  32.467  1.00 30.06  ? 52  VAL B CA    1 
ATOM   2330 C  C     . VAL B 1 90  ? -0.596  19.230  31.900  1.00 33.85  ? 52  VAL B C     1 
ATOM   2331 O  O     . VAL B 1 90  ? 0.340   19.740  32.527  1.00 42.53  ? 52  VAL B O     1 
ATOM   2332 C  CB    . VAL B 1 90  ? -2.135  18.443  33.721  1.00 30.08  ? 52  VAL B CB    1 
ATOM   2333 C  CG1   . VAL B 1 90  ? -3.215  17.439  33.978  1.00 22.60  ? 52  VAL B CG1   1 
ATOM   2334 C  CG2   . VAL B 1 90  ? -1.210  18.528  34.927  1.00 31.07  ? 52  VAL B CG2   1 
ATOM   2335 N  N     . TYR B 1 91  ? -1.005  19.663  30.715  1.00 35.18  ? 53  TYR B N     1 
ATOM   2336 C  CA    . TYR B 1 91  ? -0.429  20.810  30.047  1.00 26.39  ? 53  TYR B CA    1 
ATOM   2337 C  C     . TYR B 1 91  ? -1.215  22.056  30.416  1.00 34.26  ? 53  TYR B C     1 
ATOM   2338 O  O     . TYR B 1 91  ? -2.427  22.002  30.619  1.00 42.70  ? 53  TYR B O     1 
ATOM   2339 C  CB    . TYR B 1 91  ? -0.453  20.606  28.532  1.00 33.29  ? 53  TYR B CB    1 
ATOM   2340 C  CG    . TYR B 1 91  ? -0.031  21.837  27.773  1.00 31.59  ? 53  TYR B CG    1 
ATOM   2341 C  CD1   . TYR B 1 91  ? 1.226   22.375  27.958  1.00 25.79  ? 53  TYR B CD1   1 
ATOM   2342 C  CD2   . TYR B 1 91  ? -0.895  22.479  26.893  1.00 33.59  ? 53  TYR B CD2   1 
ATOM   2343 C  CE1   . TYR B 1 91  ? 1.623   23.500  27.282  1.00 36.92  ? 53  TYR B CE1   1 
ATOM   2344 C  CE2   . TYR B 1 91  ? -0.504  23.619  26.212  1.00 21.20  ? 53  TYR B CE2   1 
ATOM   2345 C  CZ    . TYR B 1 91  ? 0.760   24.116  26.411  1.00 28.64  ? 53  TYR B CZ    1 
ATOM   2346 O  OH    . TYR B 1 91  ? 1.192   25.242  25.760  1.00 34.70  ? 53  TYR B OH    1 
ATOM   2347 N  N     . ARG B 1 92  ? -0.522  23.189  30.509  1.00 39.33  ? 54  ARG B N     1 
ATOM   2348 C  CA    . ARG B 1 92  ? -1.185  24.458  30.798  1.00 45.30  ? 54  ARG B CA    1 
ATOM   2349 C  C     . ARG B 1 92  ? -0.737  25.491  29.774  1.00 54.03  ? 54  ARG B C     1 
ATOM   2350 O  O     . ARG B 1 92  ? 0.417   25.936  29.795  1.00 56.43  ? 54  ARG B O     1 
ATOM   2351 C  CB    . ARG B 1 92  ? -0.907  24.909  32.233  1.00 59.19  ? 54  ARG B CB    1 
ATOM   2352 C  CG    . ARG B 1 92  ? -1.277  23.825  33.241  1.00 51.24  ? 54  ARG B CG    1 
ATOM   2353 C  CD    . ARG B 1 92  ? -1.259  24.275  34.695  1.00 41.05  ? 54  ARG B CD    1 
ATOM   2354 N  NE    . ARG B 1 92  ? -1.649  23.160  35.558  1.00 44.97  ? 54  ARG B NE    1 
ATOM   2355 C  CZ    . ARG B 1 92  ? -2.909  22.803  35.814  1.00 45.30  ? 54  ARG B CZ    1 
ATOM   2356 N  NH1   . ARG B 1 92  ? -3.933  23.479  35.289  1.00 41.45  ? 54  ARG B NH1   1 
ATOM   2357 N  NH2   . ARG B 1 92  ? -3.144  21.763  36.602  1.00 35.58  ? 54  ARG B NH2   1 
ATOM   2358 N  N     . ALA B 1 93  ? -1.657  25.855  28.877  1.00 56.97  ? 55  ALA B N     1 
ATOM   2359 C  CA    . ALA B 1 93  ? -1.373  26.804  27.808  1.00 50.30  ? 55  ALA B CA    1 
ATOM   2360 C  C     . ALA B 1 93  ? -1.198  28.210  28.364  1.00 57.51  ? 55  ALA B C     1 
ATOM   2361 O  O     . ALA B 1 93  ? -2.029  28.687  29.141  1.00 70.10  ? 55  ALA B O     1 
ATOM   2362 C  CB    . ALA B 1 93  ? -2.503  26.784  26.781  1.00 46.42  ? 55  ALA B CB    1 
ATOM   2363 N  N     . SER B 1 94  ? -0.132  28.889  27.943  1.00 57.92  ? 56  SER B N     1 
ATOM   2364 C  CA    . SER B 1 94  ? 0.246   30.182  28.481  1.00 67.08  ? 56  SER B CA    1 
ATOM   2365 C  C     . SER B 1 94  ? 0.036   31.290  27.433  1.00 82.28  ? 56  SER B C     1 
ATOM   2366 O  O     . SER B 1 94  ? -0.809  31.147  26.525  1.00 52.11  ? 56  SER B O     1 
ATOM   2367 C  CB    . SER B 1 94  ? 1.678   30.087  29.007  1.00 58.89  ? 56  SER B CB    1 
ATOM   2368 O  OG    . SER B 1 94  ? 2.618   30.002  27.949  1.00 57.44  ? 56  SER B OG    1 
ATOM   2369 N  N     . GLY B 1 95  ? 0.788   32.384  27.569  1.00 90.21  ? 57  GLY B N     1 
ATOM   2370 C  CA    . GLY B 1 95  ? 0.631   33.597  26.797  1.00 82.78  ? 57  GLY B CA    1 
ATOM   2371 C  C     . GLY B 1 95  ? 1.395   34.708  27.498  1.00 95.19  ? 57  GLY B C     1 
ATOM   2372 O  O     . GLY B 1 95  ? 1.825   34.542  28.647  1.00 95.63  ? 57  GLY B O     1 
ATOM   2373 N  N     . PRO B 1 96  ? 1.593   35.874  26.827  1.00 104.65 ? 58  PRO B N     1 
ATOM   2374 C  CA    . PRO B 1 96  ? 2.362   36.959  27.465  1.00 96.91  ? 58  PRO B CA    1 
ATOM   2375 C  C     . PRO B 1 96  ? 1.700   37.344  28.774  1.00 95.27  ? 58  PRO B C     1 
ATOM   2376 O  O     . PRO B 1 96  ? 2.308   37.288  29.850  1.00 86.10  ? 58  PRO B O     1 
ATOM   2377 C  CB    . PRO B 1 96  ? 2.302   38.104  26.443  1.00 88.31  ? 58  PRO B CB    1 
ATOM   2378 C  CG    . PRO B 1 96  ? 1.853   37.471  25.157  1.00 90.56  ? 58  PRO B CG    1 
ATOM   2379 C  CD    . PRO B 1 96  ? 0.986   36.308  25.556  1.00 91.23  ? 58  PRO B CD    1 
ATOM   2380 N  N     . ASP B 1 97  ? 0.437   37.749  28.659  1.00 102.60 ? 59  ASP B N     1 
ATOM   2381 C  CA    . ASP B 1 97  ? -0.509  37.651  29.760  1.00 87.55  ? 59  ASP B CA    1 
ATOM   2382 C  C     . ASP B 1 97  ? -0.469  36.236  30.310  1.00 90.74  ? 59  ASP B C     1 
ATOM   2383 O  O     . ASP B 1 97  ? -0.739  35.276  29.577  1.00 87.71  ? 59  ASP B O     1 
ATOM   2384 C  CB    . ASP B 1 97  ? -1.918  37.965  29.261  1.00 78.32  ? 59  ASP B CB    1 
ATOM   2385 C  CG    . ASP B 1 97  ? -1.941  39.128  28.302  1.00 86.73  ? 59  ASP B CG    1 
ATOM   2386 O  OD1   . ASP B 1 97  ? -2.505  40.183  28.654  1.00 77.88  ? 59  ASP B OD1   1 
ATOM   2387 O  OD2   . ASP B 1 97  ? -1.370  38.985  27.198  1.00 88.53  ? 59  ASP B OD2   1 
ATOM   2388 N  N     . GLY B 1 98  ? -0.101  36.097  31.583  1.00 93.92  ? 60  GLY B N     1 
ATOM   2389 C  CA    . GLY B 1 98  ? -0.155  34.791  32.210  1.00 89.39  ? 60  GLY B CA    1 
ATOM   2390 C  C     . GLY B 1 98  ? -1.525  34.150  32.109  1.00 91.16  ? 60  GLY B C     1 
ATOM   2391 O  O     . GLY B 1 98  ? -2.240  34.047  33.110  1.00 80.33  ? 60  GLY B O     1 
ATOM   2392 N  N     . ALA B 1 99  ? -1.901  33.719  30.899  1.00 91.05  ? 61  ALA B N     1 
ATOM   2393 C  CA    . ALA B 1 99  ? -3.214  33.117  30.701  1.00 85.17  ? 61  ALA B CA    1 
ATOM   2394 C  C     . ALA B 1 99  ? -3.338  31.807  31.469  1.00 84.24  ? 61  ALA B C     1 
ATOM   2395 O  O     . ALA B 1 99  ? -4.394  31.527  32.052  1.00 75.49  ? 61  ALA B O     1 
ATOM   2396 C  CB    . ALA B 1 99  ? -3.473  32.900  29.208  1.00 76.51  ? 61  ALA B CB    1 
ATOM   2397 N  N     . THR B 1 100 ? -2.249  31.018  31.511  1.00 79.51  ? 62  THR B N     1 
ATOM   2398 C  CA    . THR B 1 100 ? -2.179  29.669  32.083  1.00 76.75  ? 62  THR B CA    1 
ATOM   2399 C  C     . THR B 1 100 ? -3.548  28.997  32.102  1.00 79.90  ? 62  THR B C     1 
ATOM   2400 O  O     . THR B 1 100 ? -4.092  28.684  33.169  1.00 71.03  ? 62  THR B O     1 
ATOM   2401 C  CB    . THR B 1 100 ? -1.561  29.698  33.487  1.00 71.71  ? 62  THR B CB    1 
ATOM   2402 O  OG1   . THR B 1 100 ? -1.995  30.869  34.188  1.00 67.98  ? 62  THR B OG1   1 
ATOM   2403 C  CG2   . THR B 1 100 ? -0.032  29.690  33.401  1.00 55.26  ? 62  THR B CG2   1 
ATOM   2404 N  N     . GLY B 1 101 ? -4.103  28.789  30.907  1.00 78.74  ? 63  GLY B N     1 
ATOM   2405 C  CA    . GLY B 1 101 ? -5.472  28.356  30.718  1.00 76.19  ? 63  GLY B CA    1 
ATOM   2406 C  C     . GLY B 1 101 ? -5.820  27.009  31.309  1.00 77.36  ? 63  GLY B C     1 
ATOM   2407 O  O     . GLY B 1 101 ? -5.088  26.458  32.142  1.00 74.17  ? 63  GLY B O     1 
ATOM   2408 N  N     . ARG B 1 102 ? -6.951  26.464  30.877  1.00 74.61  ? 64  ARG B N     1 
ATOM   2409 C  CA    . ARG B 1 102 ? -7.464  25.257  31.503  1.00 71.23  ? 64  ARG B CA    1 
ATOM   2410 C  C     . ARG B 1 102 ? -6.630  24.057  31.080  1.00 61.36  ? 64  ARG B C     1 
ATOM   2411 O  O     . ARG B 1 102 ? -6.454  23.796  29.883  1.00 57.88  ? 64  ARG B O     1 
ATOM   2412 C  CB    . ARG B 1 102 ? -8.939  25.068  31.166  1.00 57.69  ? 64  ARG B CB    1 
ATOM   2413 C  CG    . ARG B 1 102 ? -9.820  25.904  32.072  1.00 62.88  ? 64  ARG B CG    1 
ATOM   2414 C  CD    . ARG B 1 102 ? -9.307  25.859  33.530  1.00 65.22  ? 64  ARG B CD    1 
ATOM   2415 N  NE    . ARG B 1 102 ? -9.467  24.535  34.134  1.00 50.52  ? 64  ARG B NE    1 
ATOM   2416 C  CZ    . ARG B 1 102 ? -8.482  23.811  34.656  1.00 51.17  ? 64  ARG B CZ    1 
ATOM   2417 N  NH1   . ARG B 1 102 ? -7.235  24.278  34.678  1.00 51.03  ? 64  ARG B NH1   1 
ATOM   2418 N  NH2   . ARG B 1 102 ? -8.755  22.619  35.176  1.00 44.02  ? 64  ARG B NH2   1 
ATOM   2419 N  N     . GLY B 1 103 ? -6.095  23.354  32.076  1.00 53.39  ? 65  GLY B N     1 
ATOM   2420 C  CA    . GLY B 1 103 ? -5.244  22.209  31.862  1.00 51.65  ? 65  GLY B CA    1 
ATOM   2421 C  C     . GLY B 1 103 ? -5.847  21.195  30.919  1.00 51.41  ? 65  GLY B C     1 
ATOM   2422 O  O     . GLY B 1 103 ? -6.969  20.723  31.123  1.00 51.79  ? 65  GLY B O     1 
ATOM   2423 N  N     . GLN B 1 104 ? -5.112  20.872  29.866  1.00 49.88  ? 66  GLN B N     1 
ATOM   2424 C  CA    . GLN B 1 104 ? -5.510  19.843  28.921  1.00 42.49  ? 66  GLN B CA    1 
ATOM   2425 C  C     . GLN B 1 104 ? -4.758  18.563  29.260  1.00 37.19  ? 66  GLN B C     1 
ATOM   2426 O  O     . GLN B 1 104 ? -3.541  18.587  29.464  1.00 38.92  ? 66  GLN B O     1 
ATOM   2427 C  CB    . GLN B 1 104 ? -5.229  20.303  27.489  1.00 39.21  ? 66  GLN B CB    1 
ATOM   2428 C  CG    . GLN B 1 104 ? -5.186  21.831  27.364  1.00 43.95  ? 66  GLN B CG    1 
ATOM   2429 C  CD    . GLN B 1 104 ? -4.673  22.308  26.011  1.00 39.86  ? 66  GLN B CD    1 
ATOM   2430 O  OE1   . GLN B 1 104 ? -4.623  21.538  25.057  1.00 34.25  ? 66  GLN B OE1   1 
ATOM   2431 N  NE2   . GLN B 1 104 ? -4.279  23.586  25.930  1.00 36.12  ? 66  GLN B NE2   1 
ATOM   2432 N  N     . ARG B 1 105 ? -5.487  17.458  29.353  1.00 35.56  ? 67  ARG B N     1 
ATOM   2433 C  CA    . ARG B 1 105 ? -4.881  16.178  29.689  1.00 34.24  ? 67  ARG B CA    1 
ATOM   2434 C  C     . ARG B 1 105 ? -4.038  15.699  28.509  1.00 40.63  ? 67  ARG B C     1 
ATOM   2435 O  O     . ARG B 1 105 ? -4.539  15.587  27.383  1.00 45.50  ? 67  ARG B O     1 
ATOM   2436 C  CB    . ARG B 1 105 ? -5.977  15.172  30.038  1.00 44.19  ? 67  ARG B CB    1 
ATOM   2437 C  CG    . ARG B 1 105 ? -6.761  15.552  31.301  1.00 36.25  ? 67  ARG B CG    1 
ATOM   2438 C  CD    . ARG B 1 105 ? -8.167  14.915  31.394  1.00 42.20  ? 67  ARG B CD    1 
ATOM   2439 N  NE    . ARG B 1 105 ? -8.388  13.806  30.463  1.00 43.73  ? 67  ARG B NE    1 
ATOM   2440 C  CZ    . ARG B 1 105 ? -9.574  13.237  30.238  1.00 56.20  ? 67  ARG B CZ    1 
ATOM   2441 N  NH1   . ARG B 1 105 ? -9.674  12.226  29.372  1.00 50.70  ? 67  ARG B NH1   1 
ATOM   2442 N  NH2   . ARG B 1 105 ? -10.659 13.659  30.895  1.00 35.93  ? 67  ARG B NH2   1 
ATOM   2443 N  N     . ILE B 1 106 ? -2.757  15.434  28.754  1.00 40.28  ? 68  ILE B N     1 
ATOM   2444 C  CA    . ILE B 1 106 ? -1.816  15.062  27.704  1.00 32.65  ? 68  ILE B CA    1 
ATOM   2445 C  C     . ILE B 1 106 ? -1.191  13.712  28.028  1.00 32.12  ? 68  ILE B C     1 
ATOM   2446 O  O     . ILE B 1 106 ? -0.814  13.445  29.173  1.00 38.27  ? 68  ILE B O     1 
ATOM   2447 C  CB    . ILE B 1 106 ? -0.727  16.132  27.510  1.00 33.21  ? 68  ILE B CB    1 
ATOM   2448 C  CG1   . ILE B 1 106 ? -1.362  17.429  27.028  1.00 38.37  ? 68  ILE B CG1   1 
ATOM   2449 C  CG2   . ILE B 1 106 ? 0.287   15.671  26.469  1.00 34.61  ? 68  ILE B CG2   1 
ATOM   2450 C  CD1   . ILE B 1 106 ? -1.434  17.535  25.516  1.00 28.63  ? 68  ILE B CD1   1 
ATOM   2451 N  N     . HIS B 1 107 ? -1.084  12.864  27.009  1.00 29.71  ? 69  HIS B N     1 
ATOM   2452 C  CA    . HIS B 1 107 ? -0.524  11.524  27.114  1.00 30.32  ? 69  HIS B CA    1 
ATOM   2453 C  C     . HIS B 1 107 ? 0.730   11.491  26.258  1.00 34.01  ? 69  HIS B C     1 
ATOM   2454 O  O     . HIS B 1 107 ? 0.642   11.445  25.027  1.00 34.66  ? 69  HIS B O     1 
ATOM   2455 C  CB    . HIS B 1 107 ? -1.532  10.473  26.651  1.00 36.87  ? 69  HIS B CB    1 
ATOM   2456 C  CG    . HIS B 1 107 ? -0.975  9.084   26.580  1.00 38.61  ? 69  HIS B CG    1 
ATOM   2457 N  ND1   . HIS B 1 107 ? -0.195  8.542   27.580  1.00 39.90  ? 69  HIS B ND1   1 
ATOM   2458 C  CD2   . HIS B 1 107 ? -1.103  8.119   25.641  1.00 29.18  ? 69  HIS B CD2   1 
ATOM   2459 C  CE1   . HIS B 1 107 ? 0.142   7.307   27.255  1.00 31.77  ? 69  HIS B CE1   1 
ATOM   2460 N  NE2   . HIS B 1 107 ? -0.394  7.026   26.083  1.00 24.72  ? 69  HIS B NE2   1 
ATOM   2461 N  N     . LEU B 1 108 ? 1.887   11.515  26.909  1.00 30.57  ? 70  LEU B N     1 
ATOM   2462 C  CA    . LEU B 1 108 ? 3.174   11.592  26.241  1.00 31.86  ? 70  LEU B CA    1 
ATOM   2463 C  C     . LEU B 1 108 ? 3.683   10.223  25.821  1.00 27.52  ? 70  LEU B C     1 
ATOM   2464 O  O     . LEU B 1 108 ? 3.455   9.216   26.496  1.00 30.61  ? 70  LEU B O     1 
ATOM   2465 C  CB    . LEU B 1 108 ? 4.220   12.223  27.157  1.00 23.66  ? 70  LEU B CB    1 
ATOM   2466 C  CG    . LEU B 1 108 ? 3.964   13.657  27.585  1.00 30.79  ? 70  LEU B CG    1 
ATOM   2467 C  CD1   . LEU B 1 108 ? 5.212   14.215  28.265  1.00 20.27  ? 70  LEU B CD1   1 
ATOM   2468 C  CD2   . LEU B 1 108 ? 3.571   14.479  26.378  1.00 32.23  ? 70  LEU B CD2   1 
ATOM   2469 N  N     . GLN B 1 109 ? 4.425   10.210  24.716  1.00 24.36  ? 71  GLN B N     1 
ATOM   2470 C  CA    . GLN B 1 109 ? 5.226   9.062   24.309  1.00 23.76  ? 71  GLN B CA    1 
ATOM   2471 C  C     . GLN B 1 109 ? 6.638   9.564   24.072  1.00 28.49  ? 71  GLN B C     1 
ATOM   2472 O  O     . GLN B 1 109 ? 6.903   10.242  23.073  1.00 31.46  ? 71  GLN B O     1 
ATOM   2473 C  CB    . GLN B 1 109 ? 4.691   8.390   23.046  1.00 26.55  ? 71  GLN B CB    1 
ATOM   2474 C  CG    . GLN B 1 109 ? 5.579   7.235   22.597  1.00 18.84  ? 71  GLN B CG    1 
ATOM   2475 C  CD    . GLN B 1 109 ? 4.933   6.408   21.522  1.00 20.73  ? 71  GLN B CD    1 
ATOM   2476 O  OE1   . GLN B 1 109 ? 4.035   6.885   20.818  1.00 23.29  ? 71  GLN B OE1   1 
ATOM   2477 N  NE2   . GLN B 1 109 ? 5.372   5.157   21.386  1.00 14.18  ? 71  GLN B NE2   1 
ATOM   2478 N  N     . LEU B 1 110 ? 7.537   9.221   24.977  1.00 28.31  ? 72  LEU B N     1 
ATOM   2479 C  CA    . LEU B 1 110 ? 8.905   9.708   24.942  1.00 23.88  ? 72  LEU B CA    1 
ATOM   2480 C  C     . LEU B 1 110 ? 9.754   8.635   24.274  1.00 17.53  ? 72  LEU B C     1 
ATOM   2481 O  O     . LEU B 1 110 ? 10.026  7.594   24.875  1.00 20.32  ? 72  LEU B O     1 
ATOM   2482 C  CB    . LEU B 1 110 ? 9.396   10.026  26.356  1.00 17.69  ? 72  LEU B CB    1 
ATOM   2483 C  CG    . LEU B 1 110 ? 8.506   10.921  27.240  1.00 21.17  ? 72  LEU B CG    1 
ATOM   2484 C  CD1   . LEU B 1 110 ? 7.495   10.107  28.009  1.00 17.57  ? 72  LEU B CD1   1 
ATOM   2485 C  CD2   . LEU B 1 110 ? 9.333   11.761  28.224  1.00 20.48  ? 72  LEU B CD2   1 
ATOM   2486 N  N     . TRP B 1 111 ? 10.162  8.883   23.032  1.00 19.73  ? 73  TRP B N     1 
ATOM   2487 C  CA    . TRP B 1 111 ? 11.037  7.951   22.340  1.00 15.26  ? 73  TRP B CA    1 
ATOM   2488 C  C     . TRP B 1 111 ? 12.476  8.143   22.790  1.00 13.48  ? 73  TRP B C     1 
ATOM   2489 O  O     . TRP B 1 111 ? 12.917  9.246   23.115  1.00 21.00  ? 73  TRP B O     1 
ATOM   2490 C  CB    . TRP B 1 111 ? 10.951  8.136   20.830  1.00 19.57  ? 73  TRP B CB    1 
ATOM   2491 C  CG    . TRP B 1 111 ? 9.699   7.576   20.178  1.00 20.56  ? 73  TRP B CG    1 
ATOM   2492 C  CD1   . TRP B 1 111 ? 8.590   8.283   19.759  1.00 22.25  ? 73  TRP B CD1   1 
ATOM   2493 C  CD2   . TRP B 1 111 ? 9.450   6.212   19.834  1.00 14.18  ? 73  TRP B CD2   1 
ATOM   2494 N  NE1   . TRP B 1 111 ? 7.659   7.428   19.198  1.00 18.05  ? 73  TRP B NE1   1 
ATOM   2495 C  CE2   . TRP B 1 111 ? 8.165   6.154   19.232  1.00 17.23  ? 73  TRP B CE2   1 
ATOM   2496 C  CE3   . TRP B 1 111 ? 10.165  5.024   20.010  1.00 14.50  ? 73  TRP B CE3   1 
ATOM   2497 C  CZ2   . TRP B 1 111 ? 7.609   4.962   18.788  1.00 15.97  ? 73  TRP B CZ2   1 
ATOM   2498 C  CZ3   . TRP B 1 111 ? 9.606   3.845   19.572  1.00 9.80   ? 73  TRP B CZ3   1 
ATOM   2499 C  CH2   . TRP B 1 111 ? 8.349   3.820   18.962  1.00 18.21  ? 73  TRP B CH2   1 
ATOM   2500 N  N     . ASP B 1 112 ? 13.209  7.053   22.803  1.00 11.87  ? 74  ASP B N     1 
ATOM   2501 C  CA    . ASP B 1 112 ? 14.598  7.035   23.202  1.00 14.94  ? 74  ASP B CA    1 
ATOM   2502 C  C     . ASP B 1 112 ? 15.347  6.330   22.082  1.00 14.25  ? 74  ASP B C     1 
ATOM   2503 O  O     . ASP B 1 112 ? 14.910  5.268   21.622  1.00 12.22  ? 74  ASP B O     1 
ATOM   2504 C  CB    . ASP B 1 112 ? 14.706  6.310   24.560  1.00 12.79  ? 74  ASP B CB    1 
ATOM   2505 C  CG    . ASP B 1 112 ? 16.123  6.222   25.114  1.00 19.32  ? 74  ASP B CG    1 
ATOM   2506 O  OD1   . ASP B 1 112 ? 17.073  6.848   24.574  1.00 21.07  ? 74  ASP B OD1   1 
ATOM   2507 O  OD2   . ASP B 1 112 ? 16.276  5.476   26.114  1.00 19.55  ? 74  ASP B OD2   1 
ATOM   2508 N  N     . THR B 1 113 ? 16.448  6.924   21.624  1.00 22.04  ? 75  THR B N     1 
ATOM   2509 C  CA    . THR B 1 113 ? 17.213  6.384   20.507  1.00 18.13  ? 75  THR B CA    1 
ATOM   2510 C  C     . THR B 1 113 ? 18.617  6.034   20.952  1.00 14.20  ? 75  THR B C     1 
ATOM   2511 O  O     . THR B 1 113 ? 19.210  6.744   21.759  1.00 24.35  ? 75  THR B O     1 
ATOM   2512 C  CB    . THR B 1 113 ? 17.295  7.380   19.344  1.00 18.92  ? 75  THR B CB    1 
ATOM   2513 O  OG1   . THR B 1 113 ? 18.175  8.465   19.678  1.00 27.38  ? 75  THR B OG1   1 
ATOM   2514 C  CG2   . THR B 1 113 ? 15.934  7.920   19.015  1.00 23.83  ? 75  THR B CG2   1 
ATOM   2515 N  N     . ALA B 1 114 ? 19.144  4.944   20.419  1.00 18.38  ? 76  ALA B N     1 
ATOM   2516 C  CA    . ALA B 1 114 ? 20.572  4.680   20.529  1.00 23.24  ? 76  ALA B CA    1 
ATOM   2517 C  C     . ALA B 1 114 ? 21.363  5.666   19.684  1.00 22.32  ? 76  ALA B C     1 
ATOM   2518 O  O     . ALA B 1 114 ? 20.999  5.955   18.539  1.00 24.83  ? 76  ALA B O     1 
ATOM   2519 C  CB    . ALA B 1 114 ? 20.887  3.260   20.069  1.00 28.11  ? 76  ALA B CB    1 
ATOM   2520 N  N     . GLY B 1 115 ? 22.467  6.164   20.245  1.00 18.01  ? 77  GLY B N     1 
ATOM   2521 C  CA    . GLY B 1 115 ? 23.322  7.096   19.536  1.00 19.47  ? 77  GLY B CA    1 
ATOM   2522 C  C     . GLY B 1 115 ? 24.403  6.474   18.682  1.00 12.76  ? 77  GLY B C     1 
ATOM   2523 O  O     . GLY B 1 115 ? 25.023  7.163   17.877  1.00 17.91  ? 77  GLY B O     1 
ATOM   2524 N  N     . LEU B 1 116 ? 24.653  5.184   18.842  1.00 21.40  ? 78  LEU B N     1 
ATOM   2525 C  CA    . LEU B 1 116 ? 25.716  4.518   18.106  1.00 20.42  ? 78  LEU B CA    1 
ATOM   2526 C  C     . LEU B 1 116 ? 25.404  4.433   16.616  1.00 23.48  ? 78  LEU B C     1 
ATOM   2527 O  O     . LEU B 1 116 ? 24.261  4.194   16.217  1.00 25.07  ? 78  LEU B O     1 
ATOM   2528 C  CB    . LEU B 1 116 ? 25.910  3.119   18.655  1.00 23.51  ? 78  LEU B CB    1 
ATOM   2529 C  CG    . LEU B 1 116 ? 26.390  3.109   20.083  1.00 15.57  ? 78  LEU B CG    1 
ATOM   2530 C  CD1   . LEU B 1 116 ? 26.401  1.676   20.490  1.00 16.87  ? 78  LEU B CD1   1 
ATOM   2531 C  CD2   . LEU B 1 116 ? 27.779  3.708   20.173  1.00 12.45  ? 78  LEU B CD2   1 
ATOM   2532 N  N     . GLU B 1 117 ? 26.446  4.593   15.797  1.00 29.25  ? 79  GLU B N     1 
ATOM   2533 C  CA    . GLU B 1 117 ? 26.273  4.622   14.348  1.00 24.22  ? 79  GLU B CA    1 
ATOM   2534 C  C     . GLU B 1 117 ? 25.470  3.431   13.840  1.00 18.52  ? 79  GLU B C     1 
ATOM   2535 O  O     . GLU B 1 117 ? 24.627  3.583   12.952  1.00 27.81  ? 79  GLU B O     1 
ATOM   2536 C  CB    . GLU B 1 117 ? 27.638  4.668   13.664  1.00 29.30  ? 79  GLU B CB    1 
ATOM   2537 C  CG    . GLU B 1 117 ? 28.105  6.064   13.285  1.00 44.19  ? 79  GLU B CG    1 
ATOM   2538 C  CD    . GLU B 1 117 ? 27.321  6.662   12.114  1.00 51.71  ? 79  GLU B CD    1 
ATOM   2539 O  OE1   . GLU B 1 117 ? 26.844  7.812   12.252  1.00 48.32  ? 79  GLU B OE1   1 
ATOM   2540 O  OE2   . GLU B 1 117 ? 27.187  5.993   11.060  1.00 54.27  ? 79  GLU B OE2   1 
ATOM   2541 N  N     . ARG B 1 118 ? 25.693  2.244   14.407  1.00 19.35  ? 80  ARG B N     1 
ATOM   2542 C  CA    . ARG B 1 118 ? 25.044  1.026   13.922  1.00 23.42  ? 80  ARG B CA    1 
ATOM   2543 C  C     . ARG B 1 118 ? 23.535  1.068   14.031  1.00 20.98  ? 80  ARG B C     1 
ATOM   2544 O  O     . ARG B 1 118 ? 22.864  0.161   13.531  1.00 21.68  ? 80  ARG B O     1 
ATOM   2545 C  CB    . ARG B 1 118 ? 25.541  -0.184  14.700  1.00 28.23  ? 80  ARG B CB    1 
ATOM   2546 C  CG    . ARG B 1 118 ? 24.923  -0.293  16.077  1.00 25.74  ? 80  ARG B CG    1 
ATOM   2547 C  CD    . ARG B 1 118 ? 25.976  -0.463  17.159  1.00 33.99  ? 80  ARG B CD    1 
ATOM   2548 N  NE    . ARG B 1 118 ? 26.555  -1.805  17.199  1.00 35.64  ? 80  ARG B NE    1 
ATOM   2549 C  CZ    . ARG B 1 118 ? 27.803  -2.066  17.581  1.00 45.97  ? 80  ARG B CZ    1 
ATOM   2550 N  NH1   . ARG B 1 118 ? 28.617  -1.077  17.942  1.00 33.84  ? 80  ARG B NH1   1 
ATOM   2551 N  NH2   . ARG B 1 118 ? 28.244  -3.318  17.587  1.00 55.47  ? 80  ARG B NH2   1 
ATOM   2552 N  N     . PHE B 1 119 ? 22.984  2.051   14.727  1.00 30.09  ? 81  PHE B N     1 
ATOM   2553 C  CA    . PHE B 1 119 ? 21.545  2.207   14.817  1.00 27.21  ? 81  PHE B CA    1 
ATOM   2554 C  C     . PHE B 1 119 ? 21.078  3.454   14.093  1.00 17.10  ? 81  PHE B C     1 
ATOM   2555 O  O     . PHE B 1 119 ? 19.930  3.869   14.266  1.00 22.28  ? 81  PHE B O     1 
ATOM   2556 C  CB    . PHE B 1 119 ? 21.107  2.233   16.283  1.00 20.30  ? 81  PHE B CB    1 
ATOM   2557 C  CG    . PHE B 1 119 ? 21.361  0.939   17.018  1.00 24.76  ? 81  PHE B CG    1 
ATOM   2558 C  CD1   . PHE B 1 119 ? 20.737  -0.232  16.624  1.00 20.43  ? 81  PHE B CD1   1 
ATOM   2559 C  CD2   . PHE B 1 119 ? 22.224  0.897   18.112  1.00 25.06  ? 81  PHE B CD2   1 
ATOM   2560 C  CE1   . PHE B 1 119 ? 20.975  -1.425  17.298  1.00 18.51  ? 81  PHE B CE1   1 
ATOM   2561 C  CE2   . PHE B 1 119 ? 22.455  -0.289  18.807  1.00 10.91  ? 81  PHE B CE2   1 
ATOM   2562 C  CZ    . PHE B 1 119 ? 21.831  -1.452  18.397  1.00 15.70  ? 81  PHE B CZ    1 
ATOM   2563 N  N     . ARG B 1 120 ? 21.939  4.062   13.281  1.00 19.54  ? 82  ARG B N     1 
ATOM   2564 C  CA    . ARG B 1 120 ? 21.586  5.344   12.686  1.00 20.50  ? 82  ARG B CA    1 
ATOM   2565 C  C     . ARG B 1 120 ? 20.377  5.210   11.772  1.00 20.01  ? 82  ARG B C     1 
ATOM   2566 O  O     . ARG B 1 120 ? 19.420  5.980   11.883  1.00 20.56  ? 82  ARG B O     1 
ATOM   2567 C  CB    . ARG B 1 120 ? 22.781  5.929   11.936  1.00 29.40  ? 82  ARG B CB    1 
ATOM   2568 C  CG    . ARG B 1 120 ? 22.666  7.428   11.695  1.00 32.63  ? 82  ARG B CG    1 
ATOM   2569 C  CD    . ARG B 1 120 ? 22.199  8.169   12.947  1.00 22.06  ? 82  ARG B CD    1 
ATOM   2570 N  NE    . ARG B 1 120 ? 23.072  7.919   14.092  1.00 20.94  ? 82  ARG B NE    1 
ATOM   2571 C  CZ    . ARG B 1 120 ? 24.223  8.558   14.324  1.00 35.69  ? 82  ARG B CZ    1 
ATOM   2572 N  NH1   . ARG B 1 120 ? 24.660  9.499   13.488  1.00 34.11  ? 82  ARG B NH1   1 
ATOM   2573 N  NH2   . ARG B 1 120 ? 24.944  8.262   15.400  1.00 28.26  ? 82  ARG B NH2   1 
ATOM   2574 N  N     . SER B 1 121 ? 20.390  4.223   10.870  1.00 27.82  ? 83  SER B N     1 
ATOM   2575 C  CA    . SER B 1 121 ? 19.252  4.058   9.968   1.00 31.61  ? 83  SER B CA    1 
ATOM   2576 C  C     . SER B 1 121 ? 17.977  3.817   10.750  1.00 15.92  ? 83  SER B C     1 
ATOM   2577 O  O     . SER B 1 121 ? 16.949  4.440   10.483  1.00 25.79  ? 83  SER B O     1 
ATOM   2578 C  CB    . SER B 1 121 ? 19.480  2.915   8.976   1.00 22.81  ? 83  SER B CB    1 
ATOM   2579 O  OG    . SER B 1 121 ? 20.725  3.038   8.328   1.00 34.97  ? 83  SER B OG    1 
ATOM   2580 N  N     . LEU B 1 122 ? 18.037  2.938   11.744  1.00 25.62  ? 84  LEU B N     1 
ATOM   2581 C  CA    . LEU B 1 122 ? 16.818  2.496   12.411  1.00 20.56  ? 84  LEU B CA    1 
ATOM   2582 C  C     . LEU B 1 122 ? 16.217  3.603   13.273  1.00 26.41  ? 84  LEU B C     1 
ATOM   2583 O  O     . LEU B 1 122 ? 14.995  3.790   13.290  1.00 27.57  ? 84  LEU B O     1 
ATOM   2584 C  CB    . LEU B 1 122 ? 17.116  1.256   13.249  1.00 21.89  ? 84  LEU B CB    1 
ATOM   2585 C  CG    . LEU B 1 122 ? 16.001  0.911   14.222  1.00 24.88  ? 84  LEU B CG    1 
ATOM   2586 C  CD1   . LEU B 1 122 ? 15.007  -0.007  13.531  1.00 21.44  ? 84  LEU B CD1   1 
ATOM   2587 C  CD2   . LEU B 1 122 ? 16.563  0.294   15.509  1.00 32.20  ? 84  LEU B CD2   1 
ATOM   2588 N  N     . THR B 1 123 ? 17.054  4.346   13.996  1.00 21.22  ? 85  THR B N     1 
ATOM   2589 C  CA    . THR B 1 123 ? 16.532  5.422   14.831  1.00 24.07  ? 85  THR B CA    1 
ATOM   2590 C  C     . THR B 1 123 ? 15.984  6.545   13.977  1.00 25.84  ? 85  THR B C     1 
ATOM   2591 O  O     . THR B 1 123 ? 14.884  7.056   14.228  1.00 26.26  ? 85  THR B O     1 
ATOM   2592 C  CB    . THR B 1 123 ? 17.618  5.964   15.767  1.00 23.92  ? 85  THR B CB    1 
ATOM   2593 O  OG1   . THR B 1 123 ? 18.714  6.479   15.001  1.00 22.64  ? 85  THR B OG1   1 
ATOM   2594 C  CG2   . THR B 1 123 ? 18.107  4.880   16.718  1.00 22.97  ? 85  THR B CG2   1 
ATOM   2595 N  N     . THR B 1 124 ? 16.752  6.951   12.963  1.00 25.72  ? 86  THR B N     1 
ATOM   2596 C  CA    . THR B 1 124 ? 16.313  8.003   12.058  1.00 20.88  ? 86  THR B CA    1 
ATOM   2597 C  C     . THR B 1 124 ? 14.941  7.702   11.471  1.00 19.31  ? 86  THR B C     1 
ATOM   2598 O  O     . THR B 1 124 ? 14.189  8.626   11.138  1.00 24.21  ? 86  THR B O     1 
ATOM   2599 C  CB    . THR B 1 124 ? 17.348  8.177   10.953  1.00 24.32  ? 86  THR B CB    1 
ATOM   2600 O  OG1   . THR B 1 124 ? 18.654  8.172   11.539  1.00 21.78  ? 86  THR B OG1   1 
ATOM   2601 C  CG2   . THR B 1 124 ? 17.143  9.483   10.221  1.00 32.83  ? 86  THR B CG2   1 
ATOM   2602 N  N     . ALA B 1 125 ? 14.578  6.425   11.381  1.00 18.49  ? 87  ALA B N     1 
ATOM   2603 C  CA    . ALA B 1 125 ? 13.272  6.055   10.858  1.00 22.68  ? 87  ALA B CA    1 
ATOM   2604 C  C     . ALA B 1 125 ? 12.146  6.476   11.783  1.00 25.32  ? 87  ALA B C     1 
ATOM   2605 O  O     . ALA B 1 125 ? 10.988  6.538   11.357  1.00 21.88  ? 87  ALA B O     1 
ATOM   2606 C  CB    . ALA B 1 125 ? 13.210  4.549   10.627  1.00 18.13  ? 87  ALA B CB    1 
ATOM   2607 N  N     . PHE B 1 126 ? 12.454  6.757   13.039  1.00 31.90  ? 88  PHE B N     1 
ATOM   2608 C  CA    . PHE B 1 126 ? 11.411  7.081   13.990  1.00 30.34  ? 88  PHE B CA    1 
ATOM   2609 C  C     . PHE B 1 126 ? 11.213  8.579   14.148  1.00 26.77  ? 88  PHE B C     1 
ATOM   2610 O  O     . PHE B 1 126 ? 10.371  8.993   14.949  1.00 25.25  ? 88  PHE B O     1 
ATOM   2611 C  CB    . PHE B 1 126 ? 11.722  6.400   15.318  1.00 27.36  ? 88  PHE B CB    1 
ATOM   2612 C  CG    . PHE B 1 126 ? 11.405  4.939   15.310  1.00 25.44  ? 88  PHE B CG    1 
ATOM   2613 C  CD1   . PHE B 1 126 ? 12.395  4.003   15.060  1.00 21.49  ? 88  PHE B CD1   1 
ATOM   2614 C  CD2   . PHE B 1 126 ? 10.097  4.498   15.508  1.00 30.89  ? 88  PHE B CD2   1 
ATOM   2615 C  CE1   . PHE B 1 126 ? 12.095  2.642   15.044  1.00 33.27  ? 88  PHE B CE1   1 
ATOM   2616 C  CE2   . PHE B 1 126 ? 9.785   3.143   15.498  1.00 26.21  ? 88  PHE B CE2   1 
ATOM   2617 C  CZ    . PHE B 1 126 ? 10.784  2.212   15.268  1.00 31.73  ? 88  PHE B CZ    1 
ATOM   2618 N  N     . PHE B 1 127 ? 11.946  9.391   13.374  1.00 21.67  ? 89  PHE B N     1 
ATOM   2619 C  CA    . PHE B 1 127 ? 11.676  10.824  13.307  1.00 23.15  ? 89  PHE B CA    1 
ATOM   2620 C  C     . PHE B 1 127 ? 10.313  11.123  12.691  1.00 30.12  ? 89  PHE B C     1 
ATOM   2621 O  O     . PHE B 1 127 ? 9.765   12.207  12.923  1.00 38.55  ? 89  PHE B O     1 
ATOM   2622 C  CB    . PHE B 1 127 ? 12.731  11.559  12.478  1.00 23.30  ? 89  PHE B CB    1 
ATOM   2623 C  CG    . PHE B 1 127 ? 14.140  11.468  13.004  1.00 19.93  ? 89  PHE B CG    1 
ATOM   2624 C  CD1   . PHE B 1 127 ? 14.465  10.705  14.112  1.00 27.58  ? 89  PHE B CD1   1 
ATOM   2625 C  CD2   . PHE B 1 127 ? 15.139  12.193  12.385  1.00 12.90  ? 89  PHE B CD2   1 
ATOM   2626 C  CE1   . PHE B 1 127 ? 15.775  10.651  14.571  1.00 19.55  ? 89  PHE B CE1   1 
ATOM   2627 C  CE2   . PHE B 1 127 ? 16.433  12.134  12.820  1.00 16.80  ? 89  PHE B CE2   1 
ATOM   2628 C  CZ    . PHE B 1 127 ? 16.759  11.365  13.923  1.00 22.83  ? 89  PHE B CZ    1 
ATOM   2629 N  N     . ARG B 1 128 ? 9.773   10.214  11.877  1.00 25.65  ? 90  ARG B N     1 
ATOM   2630 C  CA    . ARG B 1 128 ? 8.430   10.413  11.342  1.00 31.38  ? 90  ARG B CA    1 
ATOM   2631 C  C     . ARG B 1 128 ? 7.419   10.540  12.472  1.00 33.09  ? 90  ARG B C     1 
ATOM   2632 O  O     . ARG B 1 128 ? 6.505   11.372  12.414  1.00 34.18  ? 90  ARG B O     1 
ATOM   2633 C  CB    . ARG B 1 128 ? 8.061   9.253   10.401  1.00 38.51  ? 90  ARG B CB    1 
ATOM   2634 C  CG    . ARG B 1 128 ? 6.682   9.350   9.720   1.00 34.72  ? 90  ARG B CG    1 
ATOM   2635 C  CD    . ARG B 1 128 ? 6.382   8.162   8.774   1.00 51.62  ? 90  ARG B CD    1 
ATOM   2636 N  NE    . ARG B 1 128 ? 7.551   7.755   7.988   1.00 52.75  ? 90  ARG B NE    1 
ATOM   2637 C  CZ    . ARG B 1 128 ? 8.312   6.701   8.270   1.00 49.30  ? 90  ARG B CZ    1 
ATOM   2638 N  NH1   . ARG B 1 128 ? 8.018   5.930   9.313   1.00 43.70  ? 90  ARG B NH1   1 
ATOM   2639 N  NH2   . ARG B 1 128 ? 9.366   6.421   7.512   1.00 39.11  ? 90  ARG B NH2   1 
ATOM   2640 N  N     . ASP B 1 129 ? 7.586   9.738   13.519  1.00 32.41  ? 91  ASP B N     1 
ATOM   2641 C  CA    . ASP B 1 129 ? 6.636   9.698   14.618  1.00 38.35  ? 91  ASP B CA    1 
ATOM   2642 C  C     . ASP B 1 129 ? 6.857   10.817  15.635  1.00 31.51  ? 91  ASP B C     1 
ATOM   2643 O  O     . ASP B 1 129 ? 6.022   10.997  16.526  1.00 30.07  ? 91  ASP B O     1 
ATOM   2644 C  CB    . ASP B 1 129 ? 6.719   8.325   15.298  1.00 32.38  ? 91  ASP B CB    1 
ATOM   2645 C  CG    . ASP B 1 129 ? 5.381   7.839   15.812  1.00 36.92  ? 91  ASP B CG    1 
ATOM   2646 O  OD1   . ASP B 1 129 ? 4.375   7.954   15.077  1.00 42.30  ? 91  ASP B OD1   1 
ATOM   2647 O  OD2   . ASP B 1 129 ? 5.337   7.323   16.951  1.00 37.23  ? 91  ASP B OD2   1 
ATOM   2648 N  N     . ALA B 1 130 ? 7.928   11.591  15.511  1.00 26.35  ? 92  ALA B N     1 
ATOM   2649 C  CA    . ALA B 1 130 ? 8.227   12.614  16.495  1.00 22.53  ? 92  ALA B CA    1 
ATOM   2650 C  C     . ALA B 1 130 ? 7.567   13.938  16.135  1.00 28.46  ? 92  ALA B C     1 
ATOM   2651 O  O     . ALA B 1 130 ? 7.537   14.341  14.969  1.00 22.70  ? 92  ALA B O     1 
ATOM   2652 C  CB    . ALA B 1 130 ? 9.734   12.797  16.631  1.00 24.15  ? 92  ALA B CB    1 
ATOM   2653 N  N     . MET B 1 131 ? 7.029   14.603  17.156  1.00 21.00  ? 93  MET B N     1 
ATOM   2654 C  CA    . MET B 1 131 ? 6.452   15.935  17.049  1.00 26.23  ? 93  MET B CA    1 
ATOM   2655 C  C     . MET B 1 131 ? 7.417   17.026  17.485  1.00 21.20  ? 93  MET B C     1 
ATOM   2656 O  O     . MET B 1 131 ? 7.149   18.206  17.243  1.00 24.75  ? 93  MET B O     1 
ATOM   2657 C  CB    . MET B 1 131 ? 5.181   16.030  17.903  1.00 30.70  ? 93  MET B CB    1 
ATOM   2658 C  CG    . MET B 1 131 ? 4.118   14.969  17.607  1.00 27.82  ? 93  MET B CG    1 
ATOM   2659 S  SD    . MET B 1 131 ? 2.579   15.279  18.500  1.00 32.44  ? 93  MET B SD    1 
ATOM   2660 C  CE    . MET B 1 131 ? 1.526   14.015  17.815  1.00 31.72  ? 93  MET B CE    1 
ATOM   2661 N  N     . GLY B 1 132 ? 8.509   16.650  18.135  1.00 14.98  ? 94  GLY B N     1 
ATOM   2662 C  CA    . GLY B 1 132 ? 9.514   17.575  18.617  1.00 10.02  ? 94  GLY B CA    1 
ATOM   2663 C  C     . GLY B 1 132 ? 10.688  16.743  19.088  1.00 19.16  ? 94  GLY B C     1 
ATOM   2664 O  O     . GLY B 1 132 ? 10.581  15.521  19.226  1.00 19.68  ? 94  GLY B O     1 
ATOM   2665 N  N     . PHE B 1 133 ? 11.812  17.412  19.317  1.00 16.10  ? 95  PHE B N     1 
ATOM   2666 C  CA    . PHE B 1 133 ? 13.041  16.672  19.574  1.00 16.31  ? 95  PHE B CA    1 
ATOM   2667 C  C     . PHE B 1 133 ? 13.766  17.171  20.806  1.00 14.78  ? 95  PHE B C     1 
ATOM   2668 O  O     . PHE B 1 133 ? 13.849  18.376  21.047  1.00 22.22  ? 95  PHE B O     1 
ATOM   2669 C  CB    . PHE B 1 133 ? 13.961  16.741  18.385  1.00 13.75  ? 95  PHE B CB    1 
ATOM   2670 C  CG    . PHE B 1 133 ? 13.397  16.090  17.185  1.00 20.84  ? 95  PHE B CG    1 
ATOM   2671 C  CD1   . PHE B 1 133 ? 13.541  14.728  16.996  1.00 21.40  ? 95  PHE B CD1   1 
ATOM   2672 C  CD2   . PHE B 1 133 ? 12.685  16.827  16.247  1.00 26.82  ? 95  PHE B CD2   1 
ATOM   2673 C  CE1   . PHE B 1 133 ? 13.007  14.114  15.888  1.00 19.73  ? 95  PHE B CE1   1 
ATOM   2674 C  CE2   . PHE B 1 133 ? 12.160  16.213  15.142  1.00 26.03  ? 95  PHE B CE2   1 
ATOM   2675 C  CZ    . PHE B 1 133 ? 12.321  14.854  14.966  1.00 24.10  ? 95  PHE B CZ    1 
ATOM   2676 N  N     . LEU B 1 134 ? 14.296  16.222  21.572  1.00 24.18  ? 96  LEU B N     1 
ATOM   2677 C  CA    . LEU B 1 134 ? 15.123  16.485  22.747  1.00 19.89  ? 96  LEU B CA    1 
ATOM   2678 C  C     . LEU B 1 134 ? 16.566  16.113  22.424  1.00 20.21  ? 96  LEU B C     1 
ATOM   2679 O  O     . LEU B 1 134 ? 16.943  14.936  22.483  1.00 19.50  ? 96  LEU B O     1 
ATOM   2680 C  CB    . LEU B 1 134 ? 14.626  15.691  23.941  1.00 19.21  ? 96  LEU B CB    1 
ATOM   2681 C  CG    . LEU B 1 134 ? 15.028  16.347  25.256  1.00 16.34  ? 96  LEU B CG    1 
ATOM   2682 C  CD1   . LEU B 1 134 ? 14.221  17.593  25.451  1.00 24.18  ? 96  LEU B CD1   1 
ATOM   2683 C  CD2   . LEU B 1 134 ? 14.800  15.398  26.394  1.00 15.06  ? 96  LEU B CD2   1 
ATOM   2684 N  N     . LEU B 1 135 ? 17.381  17.118  22.110  1.00 16.87  ? 97  LEU B N     1 
ATOM   2685 C  CA    . LEU B 1 135 ? 18.769  16.894  21.741  1.00 22.07  ? 97  LEU B CA    1 
ATOM   2686 C  C     . LEU B 1 135 ? 19.678  17.054  22.958  1.00 21.79  ? 97  LEU B C     1 
ATOM   2687 O  O     . LEU B 1 135 ? 19.668  18.096  23.619  1.00 21.68  ? 97  LEU B O     1 
ATOM   2688 C  CB    . LEU B 1 135 ? 19.181  17.849  20.617  1.00 22.39  ? 97  LEU B CB    1 
ATOM   2689 C  CG    . LEU B 1 135 ? 20.596  17.689  20.052  1.00 15.98  ? 97  LEU B CG    1 
ATOM   2690 C  CD1   . LEU B 1 135 ? 20.958  16.239  19.907  1.00 16.15  ? 97  LEU B CD1   1 
ATOM   2691 C  CD2   . LEU B 1 135 ? 20.696  18.392  18.717  1.00 20.88  ? 97  LEU B CD2   1 
ATOM   2692 N  N     . LEU B 1 136 ? 20.485  16.032  23.226  1.00 18.32  ? 98  LEU B N     1 
ATOM   2693 C  CA    . LEU B 1 136 ? 21.348  15.992  24.393  1.00 21.07  ? 98  LEU B CA    1 
ATOM   2694 C  C     . LEU B 1 136 ? 22.818  15.962  23.992  1.00 29.53  ? 98  LEU B C     1 
ATOM   2695 O  O     . LEU B 1 136 ? 23.197  15.360  22.981  1.00 24.97  ? 98  LEU B O     1 
ATOM   2696 C  CB    . LEU B 1 136 ? 21.025  14.775  25.258  1.00 16.15  ? 98  LEU B CB    1 
ATOM   2697 C  CG    . LEU B 1 136 ? 19.978  14.992  26.346  1.00 23.44  ? 98  LEU B CG    1 
ATOM   2698 C  CD1   . LEU B 1 136 ? 18.571  15.105  25.778  1.00 15.45  ? 98  LEU B CD1   1 
ATOM   2699 C  CD2   . LEU B 1 136 ? 20.078  13.852  27.344  1.00 21.04  ? 98  LEU B CD2   1 
ATOM   2700 N  N     . PHE B 1 137 ? 23.641  16.635  24.788  1.00 25.68  ? 99  PHE B N     1 
ATOM   2701 C  CA    . PHE B 1 137 ? 25.073  16.416  24.777  1.00 26.56  ? 99  PHE B CA    1 
ATOM   2702 C  C     . PHE B 1 137 ? 25.528  16.325  26.223  1.00 21.09  ? 99  PHE B C     1 
ATOM   2703 O  O     . PHE B 1 137 ? 24.762  16.576  27.150  1.00 22.00  ? 99  PHE B O     1 
ATOM   2704 C  CB    . PHE B 1 137 ? 25.834  17.512  24.002  1.00 18.52  ? 99  PHE B CB    1 
ATOM   2705 C  CG    . PHE B 1 137 ? 25.764  18.864  24.623  1.00 13.05  ? 99  PHE B CG    1 
ATOM   2706 C  CD1   . PHE B 1 137 ? 24.661  19.677  24.412  1.00 8.43   ? 99  PHE B CD1   1 
ATOM   2707 C  CD2   . PHE B 1 137 ? 26.802  19.329  25.419  1.00 17.85  ? 99  PHE B CD2   1 
ATOM   2708 C  CE1   . PHE B 1 137 ? 24.588  20.928  24.962  1.00 9.44   ? 99  PHE B CE1   1 
ATOM   2709 C  CE2   . PHE B 1 137 ? 26.736  20.589  26.006  1.00 22.09  ? 99  PHE B CE2   1 
ATOM   2710 C  CZ    . PHE B 1 137 ? 25.626  21.393  25.776  1.00 16.09  ? 99  PHE B CZ    1 
ATOM   2711 N  N     . ASP B 1 138 ? 26.785  15.946  26.399  1.00 29.71  ? 100 ASP B N     1 
ATOM   2712 C  CA    . ASP B 1 138 ? 27.387  15.681  27.697  1.00 23.22  ? 100 ASP B CA    1 
ATOM   2713 C  C     . ASP B 1 138 ? 28.327  16.839  28.030  1.00 28.29  ? 100 ASP B C     1 
ATOM   2714 O  O     . ASP B 1 138 ? 29.339  17.041  27.346  1.00 22.10  ? 100 ASP B O     1 
ATOM   2715 C  CB    . ASP B 1 138 ? 28.124  14.341  27.639  1.00 29.60  ? 100 ASP B CB    1 
ATOM   2716 C  CG    . ASP B 1 138 ? 28.638  13.873  28.990  1.00 30.60  ? 100 ASP B CG    1 
ATOM   2717 O  OD1   . ASP B 1 138 ? 28.768  14.706  29.916  1.00 31.99  ? 100 ASP B OD1   1 
ATOM   2718 O  OD2   . ASP B 1 138 ? 28.936  12.658  29.118  1.00 31.34  ? 100 ASP B OD2   1 
ATOM   2719 N  N     . LEU B 1 139 ? 27.989  17.599  29.084  1.00 22.99  ? 101 LEU B N     1 
ATOM   2720 C  CA    . LEU B 1 139 ? 28.863  18.659  29.578  1.00 19.95  ? 101 LEU B CA    1 
ATOM   2721 C  C     . LEU B 1 139 ? 30.255  18.156  29.937  1.00 21.17  ? 101 LEU B C     1 
ATOM   2722 O  O     . LEU B 1 139 ? 31.173  18.965  30.096  1.00 17.48  ? 101 LEU B O     1 
ATOM   2723 C  CB    . LEU B 1 139 ? 28.260  19.324  30.815  1.00 28.31  ? 101 LEU B CB    1 
ATOM   2724 C  CG    . LEU B 1 139 ? 27.004  20.163  30.615  1.00 29.33  ? 101 LEU B CG    1 
ATOM   2725 C  CD1   . LEU B 1 139 ? 26.308  20.318  31.925  1.00 12.84  ? 101 LEU B CD1   1 
ATOM   2726 C  CD2   . LEU B 1 139 ? 27.345  21.510  30.026  1.00 17.77  ? 101 LEU B CD2   1 
ATOM   2727 N  N     . THR B 1 140 ? 30.437  16.848  30.089  1.00 21.87  ? 102 THR B N     1 
ATOM   2728 C  CA    . THR B 1 140 ? 31.756  16.293  30.344  1.00 24.61  ? 102 THR B CA    1 
ATOM   2729 C  C     . THR B 1 140 ? 32.400  15.696  29.081  1.00 36.62  ? 102 THR B C     1 
ATOM   2730 O  O     . THR B 1 140 ? 33.400  14.973  29.186  1.00 25.12  ? 102 THR B O     1 
ATOM   2731 C  CB    . THR B 1 140 ? 31.666  15.246  31.453  1.00 22.03  ? 102 THR B CB    1 
ATOM   2732 O  OG1   . THR B 1 140 ? 30.775  14.209  31.045  1.00 22.49  ? 102 THR B OG1   1 
ATOM   2733 C  CG2   . THR B 1 140 ? 31.110  15.875  32.738  1.00 24.92  ? 102 THR B CG2   1 
ATOM   2734 N  N     . ASN B 1 141 ? 31.863  15.995  27.889  1.00 23.58  ? 103 ASN B N     1 
ATOM   2735 C  CA    . ASN B 1 141 ? 32.359  15.389  26.649  1.00 25.01  ? 103 ASN B CA    1 
ATOM   2736 C  C     . ASN B 1 141 ? 32.293  16.408  25.513  1.00 28.87  ? 103 ASN B C     1 
ATOM   2737 O  O     . ASN B 1 141 ? 31.241  16.582  24.893  1.00 30.00  ? 103 ASN B O     1 
ATOM   2738 C  CB    . ASN B 1 141 ? 31.564  14.138  26.313  1.00 28.24  ? 103 ASN B CB    1 
ATOM   2739 C  CG    . ASN B 1 141 ? 32.046  13.466  25.057  1.00 25.40  ? 103 ASN B CG    1 
ATOM   2740 O  OD1   . ASN B 1 141 ? 32.100  14.077  23.995  1.00 32.86  ? 103 ASN B OD1   1 
ATOM   2741 N  ND2   . ASN B 1 141 ? 32.400  12.198  25.168  1.00 14.60  ? 103 ASN B ND2   1 
ATOM   2742 N  N     . GLU B 1 142 ? 33.431  17.035  25.201  1.00 25.69  ? 104 GLU B N     1 
ATOM   2743 C  CA    . GLU B 1 142 ? 33.423  18.124  24.231  1.00 29.20  ? 104 GLU B CA    1 
ATOM   2744 C  C     . GLU B 1 142 ? 33.034  17.636  22.841  1.00 34.64  ? 104 GLU B C     1 
ATOM   2745 O  O     . GLU B 1 142 ? 32.514  18.420  22.031  1.00 30.59  ? 104 GLU B O     1 
ATOM   2746 C  CB    . GLU B 1 142 ? 34.792  18.815  24.204  1.00 27.22  ? 104 GLU B CB    1 
ATOM   2747 C  CG    . GLU B 1 142 ? 34.886  19.988  23.237  1.00 27.74  ? 104 GLU B CG    1 
ATOM   2748 C  CD    . GLU B 1 142 ? 34.455  21.309  23.848  1.00 32.02  ? 104 GLU B CD    1 
ATOM   2749 O  OE1   . GLU B 1 142 ? 34.801  21.560  25.019  1.00 41.37  ? 104 GLU B OE1   1 
ATOM   2750 O  OE2   . GLU B 1 142 ? 33.772  22.107  23.162  1.00 36.70  ? 104 GLU B OE2   1 
ATOM   2751 N  N     . GLN B 1 143 ? 33.268  16.352  22.545  1.00 24.07  ? 105 GLN B N     1 
ATOM   2752 C  CA    . GLN B 1 143 ? 32.942  15.847  21.219  1.00 18.27  ? 105 GLN B CA    1 
ATOM   2753 C  C     . GLN B 1 143 ? 31.434  15.799  21.002  1.00 27.87  ? 105 GLN B C     1 
ATOM   2754 O  O     . GLN B 1 143 ? 30.935  16.205  19.944  1.00 27.68  ? 105 GLN B O     1 
ATOM   2755 C  CB    . GLN B 1 143 ? 33.559  14.470  21.011  1.00 18.25  ? 105 GLN B CB    1 
ATOM   2756 C  CG    . GLN B 1 143 ? 33.329  13.922  19.595  1.00 29.79  ? 105 GLN B CG    1 
ATOM   2757 C  CD    . GLN B 1 143 ? 33.794  14.886  18.506  1.00 28.30  ? 105 GLN B CD    1 
ATOM   2758 O  OE1   . GLN B 1 143 ? 32.992  15.449  17.747  1.00 35.62  ? 105 GLN B OE1   1 
ATOM   2759 N  NE2   . GLN B 1 143 ? 35.092  15.080  18.431  1.00 24.18  ? 105 GLN B NE2   1 
ATOM   2760 N  N     . SER B 1 144 ? 30.696  15.308  21.998  1.00 28.81  ? 106 SER B N     1 
ATOM   2761 C  CA    . SER B 1 144 ? 29.243  15.303  21.912  1.00 22.78  ? 106 SER B CA    1 
ATOM   2762 C  C     . SER B 1 144 ? 28.692  16.699  21.713  1.00 20.13  ? 106 SER B C     1 
ATOM   2763 O  O     . SER B 1 144 ? 27.677  16.870  21.031  1.00 20.99  ? 106 SER B O     1 
ATOM   2764 C  CB    . SER B 1 144 ? 28.636  14.698  23.173  1.00 24.70  ? 106 SER B CB    1 
ATOM   2765 O  OG    . SER B 1 144 ? 28.848  15.545  24.278  1.00 26.28  ? 106 SER B OG    1 
ATOM   2766 N  N     . PHE B 1 145 ? 29.328  17.701  22.315  1.00 17.25  ? 107 PHE B N     1 
ATOM   2767 C  CA    . PHE B 1 145 ? 28.897  19.074  22.093  1.00 21.97  ? 107 PHE B CA    1 
ATOM   2768 C  C     . PHE B 1 145 ? 29.118  19.491  20.641  1.00 23.30  ? 107 PHE B C     1 
ATOM   2769 O  O     . PHE B 1 145 ? 28.186  19.923  19.959  1.00 27.58  ? 107 PHE B O     1 
ATOM   2770 C  CB    . PHE B 1 145 ? 29.632  20.013  23.045  1.00 21.81  ? 107 PHE B CB    1 
ATOM   2771 C  CG    . PHE B 1 145 ? 29.248  21.453  22.887  1.00 15.58  ? 107 PHE B CG    1 
ATOM   2772 C  CD1   . PHE B 1 145 ? 27.974  21.881  23.206  1.00 14.38  ? 107 PHE B CD1   1 
ATOM   2773 C  CD2   . PHE B 1 145 ? 30.163  22.380  22.404  1.00 15.93  ? 107 PHE B CD2   1 
ATOM   2774 C  CE1   . PHE B 1 145 ? 27.611  23.213  23.059  1.00 15.24  ? 107 PHE B CE1   1 
ATOM   2775 C  CE2   . PHE B 1 145 ? 29.808  23.710  22.258  1.00 17.59  ? 107 PHE B CE2   1 
ATOM   2776 C  CZ    . PHE B 1 145 ? 28.526  24.125  22.586  1.00 14.72  ? 107 PHE B CZ    1 
ATOM   2777 N  N     . LEU B 1 146 ? 30.341  19.355  20.144  1.00 21.96  ? 108 LEU B N     1 
ATOM   2778 C  CA    . LEU B 1 146 ? 30.608  19.713  18.761  1.00 28.06  ? 108 LEU B CA    1 
ATOM   2779 C  C     . LEU B 1 146 ? 29.749  18.928  17.782  1.00 33.08  ? 108 LEU B C     1 
ATOM   2780 O  O     . LEU B 1 146 ? 29.534  19.389  16.651  1.00 27.31  ? 108 LEU B O     1 
ATOM   2781 C  CB    . LEU B 1 146 ? 32.072  19.485  18.438  1.00 19.54  ? 108 LEU B CB    1 
ATOM   2782 C  CG    . LEU B 1 146 ? 32.967  20.361  19.285  1.00 19.00  ? 108 LEU B CG    1 
ATOM   2783 C  CD1   . LEU B 1 146 ? 34.380  20.106  18.884  1.00 12.60  ? 108 LEU B CD1   1 
ATOM   2784 C  CD2   . LEU B 1 146 ? 32.581  21.812  19.090  1.00 22.63  ? 108 LEU B CD2   1 
ATOM   2785 N  N     . ASN B 1 147 ? 29.259  17.756  18.186  1.00 26.78  ? 109 ASN B N     1 
ATOM   2786 C  CA    . ASN B 1 147 ? 28.415  16.985  17.293  1.00 23.81  ? 109 ASN B CA    1 
ATOM   2787 C  C     . ASN B 1 147 ? 27.005  17.545  17.204  1.00 25.89  ? 109 ASN B C     1 
ATOM   2788 O  O     . ASN B 1 147 ? 26.252  17.131  16.307  1.00 30.64  ? 109 ASN B O     1 
ATOM   2789 C  CB    . ASN B 1 147 ? 28.386  15.514  17.722  1.00 21.89  ? 109 ASN B CB    1 
ATOM   2790 C  CG    . ASN B 1 147 ? 29.495  14.690  17.068  1.00 23.66  ? 109 ASN B CG    1 
ATOM   2791 O  OD1   . ASN B 1 147 ? 30.167  15.154  16.148  1.00 34.47  ? 109 ASN B OD1   1 
ATOM   2792 N  ND2   . ASN B 1 147 ? 29.674  13.459  17.532  1.00 21.98  ? 109 ASN B ND2   1 
ATOM   2793 N  N     . VAL B 1 148 ? 26.650  18.508  18.064  1.00 18.58  ? 110 VAL B N     1 
ATOM   2794 C  CA    . VAL B 1 148 ? 25.269  18.998  18.092  1.00 27.06  ? 110 VAL B CA    1 
ATOM   2795 C  C     . VAL B 1 148 ? 24.868  19.588  16.737  1.00 25.71  ? 110 VAL B C     1 
ATOM   2796 O  O     . VAL B 1 148 ? 23.725  19.424  16.289  1.00 19.84  ? 110 VAL B O     1 
ATOM   2797 C  CB    . VAL B 1 148 ? 25.079  20.010  19.241  1.00 20.07  ? 110 VAL B CB    1 
ATOM   2798 C  CG1   . VAL B 1 148 ? 23.725  20.666  19.144  1.00 13.03  ? 110 VAL B CG1   1 
ATOM   2799 C  CG2   . VAL B 1 148 ? 25.206  19.322  20.592  1.00 15.57  ? 110 VAL B CG2   1 
ATOM   2800 N  N     . ARG B 1 149 ? 25.802  20.281  16.067  1.00 35.77  ? 111 ARG B N     1 
ATOM   2801 C  CA    . ARG B 1 149 ? 25.512  20.862  14.759  1.00 25.78  ? 111 ARG B CA    1 
ATOM   2802 C  C     . ARG B 1 149 ? 25.072  19.797  13.775  1.00 28.74  ? 111 ARG B C     1 
ATOM   2803 O  O     . ARG B 1 149 ? 24.139  20.015  12.992  1.00 27.56  ? 111 ARG B O     1 
ATOM   2804 C  CB    . ARG B 1 149 ? 26.730  21.607  14.201  1.00 35.64  ? 111 ARG B CB    1 
ATOM   2805 C  CG    . ARG B 1 149 ? 27.530  22.382  15.223  1.00 49.63  ? 111 ARG B CG    1 
ATOM   2806 C  CD    . ARG B 1 149 ? 28.699  23.139  14.610  1.00 37.39  ? 111 ARG B CD    1 
ATOM   2807 N  NE    . ARG B 1 149 ? 29.389  22.372  13.575  1.00 56.00  ? 111 ARG B NE    1 
ATOM   2808 C  CZ    . ARG B 1 149 ? 29.546  22.773  12.311  1.00 61.23  ? 111 ARG B CZ    1 
ATOM   2809 N  NH1   . ARG B 1 149 ? 30.197  22.004  11.442  1.00 52.34  ? 111 ARG B NH1   1 
ATOM   2810 N  NH2   . ARG B 1 149 ? 29.064  23.943  11.914  1.00 53.50  ? 111 ARG B NH2   1 
ATOM   2811 N  N     . ASN B 1 150 ? 25.727  18.636  13.801  1.00 25.76  ? 112 ASN B N     1 
ATOM   2812 C  CA    . ASN B 1 150 ? 25.372  17.578  12.864  1.00 21.68  ? 112 ASN B CA    1 
ATOM   2813 C  C     . ASN B 1 150 ? 24.007  17.002  13.207  1.00 25.77  ? 112 ASN B C     1 
ATOM   2814 O  O     . ASN B 1 150 ? 23.157  16.841  12.323  1.00 24.37  ? 112 ASN B O     1 
ATOM   2815 C  CB    . ASN B 1 150 ? 26.449  16.487  12.847  1.00 20.24  ? 112 ASN B CB    1 
ATOM   2816 C  CG    . ASN B 1 150 ? 27.787  16.979  12.287  1.00 25.05  ? 112 ASN B CG    1 
ATOM   2817 O  OD1   . ASN B 1 150 ? 27.942  18.155  11.933  1.00 37.29  ? 112 ASN B OD1   1 
ATOM   2818 N  ND2   . ASN B 1 150 ? 28.764  16.079  12.219  1.00 29.07  ? 112 ASN B ND2   1 
ATOM   2819 N  N     . TRP B 1 151 ? 23.762  16.724  14.494  1.00 19.68  ? 113 TRP B N     1 
ATOM   2820 C  CA    . TRP B 1 151 ? 22.442  16.253  14.904  1.00 23.19  ? 113 TRP B CA    1 
ATOM   2821 C  C     . TRP B 1 151 ? 21.352  17.198  14.420  1.00 16.64  ? 113 TRP B C     1 
ATOM   2822 O  O     . TRP B 1 151 ? 20.341  16.764  13.863  1.00 22.29  ? 113 TRP B O     1 
ATOM   2823 C  CB    . TRP B 1 151 ? 22.373  16.084  16.431  1.00 15.20  ? 113 TRP B CB    1 
ATOM   2824 C  CG    . TRP B 1 151 ? 23.078  14.869  16.929  1.00 10.72  ? 113 TRP B CG    1 
ATOM   2825 C  CD1   . TRP B 1 151 ? 24.238  14.830  17.659  1.00 14.95  ? 113 TRP B CD1   1 
ATOM   2826 C  CD2   . TRP B 1 151 ? 22.676  13.499  16.745  1.00 19.54  ? 113 TRP B CD2   1 
ATOM   2827 N  NE1   . TRP B 1 151 ? 24.590  13.523  17.926  1.00 11.83  ? 113 TRP B NE1   1 
ATOM   2828 C  CE2   . TRP B 1 151 ? 23.650  12.687  17.375  1.00 13.56  ? 113 TRP B CE2   1 
ATOM   2829 C  CE3   . TRP B 1 151 ? 21.595  12.878  16.096  1.00 16.86  ? 113 TRP B CE3   1 
ATOM   2830 C  CZ2   . TRP B 1 151 ? 23.564  11.289  17.392  1.00 11.56  ? 113 TRP B CZ2   1 
ATOM   2831 C  CZ3   . TRP B 1 151 ? 21.512  11.487  16.119  1.00 13.34  ? 113 TRP B CZ3   1 
ATOM   2832 C  CH2   . TRP B 1 151 ? 22.490  10.712  16.768  1.00 13.87  ? 113 TRP B CH2   1 
ATOM   2833 N  N     . ILE B 1 152 ? 21.545  18.503  14.609  1.00 26.30  ? 114 ILE B N     1 
ATOM   2834 C  CA    . ILE B 1 152 ? 20.539  19.458  14.156  1.00 25.30  ? 114 ILE B CA    1 
ATOM   2835 C  C     . ILE B 1 152 ? 20.318  19.326  12.659  1.00 25.70  ? 114 ILE B C     1 
ATOM   2836 O  O     . ILE B 1 152 ? 19.175  19.345  12.180  1.00 27.86  ? 114 ILE B O     1 
ATOM   2837 C  CB    . ILE B 1 152 ? 20.946  20.890  14.520  1.00 25.75  ? 114 ILE B CB    1 
ATOM   2838 C  CG1   . ILE B 1 152 ? 20.850  21.121  16.024  1.00 20.14  ? 114 ILE B CG1   1 
ATOM   2839 C  CG2   . ILE B 1 152 ? 20.076  21.857  13.756  1.00 28.26  ? 114 ILE B CG2   1 
ATOM   2840 C  CD1   . ILE B 1 152 ? 21.798  22.177  16.514  1.00 16.39  ? 114 ILE B CD1   1 
ATOM   2841 N  N     . SER B 1 153 ? 21.409  19.190  11.897  1.00 22.39  ? 115 SER B N     1 
ATOM   2842 C  CA    . SER B 1 153 ? 21.300  19.049  10.448  1.00 19.40  ? 115 SER B CA    1 
ATOM   2843 C  C     . SER B 1 153 ? 20.489  17.815  10.073  1.00 18.81  ? 115 SER B C     1 
ATOM   2844 O  O     . SER B 1 153 ? 19.599  17.879  9.220   1.00 28.50  ? 115 SER B O     1 
ATOM   2845 C  CB    . SER B 1 153 ? 22.688  18.977  9.825   1.00 30.42  ? 115 SER B CB    1 
ATOM   2846 O  OG    . SER B 1 153 ? 23.405  20.179  10.030  1.00 36.69  ? 115 SER B OG    1 
ATOM   2847 N  N     . GLN B 1 154 ? 20.791  16.675  10.699  1.00 25.94  ? 116 GLN B N     1 
ATOM   2848 C  CA    . GLN B 1 154 ? 19.982  15.479  10.502  1.00 18.48  ? 116 GLN B CA    1 
ATOM   2849 C  C     . GLN B 1 154 ? 18.520  15.760  10.781  1.00 21.17  ? 116 GLN B C     1 
ATOM   2850 O  O     . GLN B 1 154 ? 17.647  15.324  10.028  1.00 29.70  ? 116 GLN B O     1 
ATOM   2851 C  CB    . GLN B 1 154 ? 20.486  14.355  11.396  1.00 17.25  ? 116 GLN B CB    1 
ATOM   2852 C  CG    . GLN B 1 154 ? 21.802  13.798  10.958  1.00 18.96  ? 116 GLN B CG    1 
ATOM   2853 C  CD    . GLN B 1 154 ? 21.660  12.948  9.697   1.00 28.53  ? 116 GLN B CD    1 
ATOM   2854 O  OE1   . GLN B 1 154 ? 22.306  13.214  8.682   1.00 32.49  ? 116 GLN B OE1   1 
ATOM   2855 N  NE2   . GLN B 1 154 ? 20.801  11.930  9.759   1.00 28.80  ? 116 GLN B NE2   1 
ATOM   2856 N  N     . LEU B 1 155 ? 18.237  16.511  11.848  1.00 19.63  ? 117 LEU B N     1 
ATOM   2857 C  CA    . LEU B 1 155 ? 16.856  16.816  12.200  1.00 21.66  ? 117 LEU B CA    1 
ATOM   2858 C  C     . LEU B 1 155 ? 16.156  17.618  11.105  1.00 24.58  ? 117 LEU B C     1 
ATOM   2859 O  O     . LEU B 1 155 ? 14.980  17.381  10.816  1.00 20.57  ? 117 LEU B O     1 
ATOM   2860 C  CB    . LEU B 1 155 ? 16.814  17.570  13.533  1.00 21.50  ? 117 LEU B CB    1 
ATOM   2861 C  CG    . LEU B 1 155 ? 17.126  16.709  14.760  1.00 26.19  ? 117 LEU B CG    1 
ATOM   2862 C  CD1   . LEU B 1 155 ? 17.113  17.535  16.054  1.00 19.46  ? 117 LEU B CD1   1 
ATOM   2863 C  CD2   . LEU B 1 155 ? 16.158  15.556  14.839  1.00 14.61  ? 117 LEU B CD2   1 
ATOM   2864 N  N     . GLN B 1 156 ? 16.848  18.587  10.496  1.00 25.48  ? 118 GLN B N     1 
ATOM   2865 C  CA    . GLN B 1 156 ? 16.203  19.370  9.443   1.00 28.74  ? 118 GLN B CA    1 
ATOM   2866 C  C     . GLN B 1 156 ? 16.065  18.557  8.167   1.00 26.56  ? 118 GLN B C     1 
ATOM   2867 O  O     . GLN B 1 156 ? 15.071  18.694  7.445   1.00 31.49  ? 118 GLN B O     1 
ATOM   2868 C  CB    . GLN B 1 156 ? 16.981  20.663  9.182   1.00 25.73  ? 118 GLN B CB    1 
ATOM   2869 C  CG    . GLN B 1 156 ? 16.880  21.638  10.343  1.00 32.08  ? 118 GLN B CG    1 
ATOM   2870 C  CD    . GLN B 1 156 ? 17.959  22.702  10.323  1.00 48.91  ? 118 GLN B CD    1 
ATOM   2871 O  OE1   . GLN B 1 156 ? 18.633  22.907  9.302   1.00 42.85  ? 118 GLN B OE1   1 
ATOM   2872 N  NE2   . GLN B 1 156 ? 18.133  23.392  11.461  1.00 34.96  ? 118 GLN B NE2   1 
ATOM   2873 N  N     . MET B 1 157 ? 17.034  17.688  7.906   1.00 28.25  ? 119 MET B N     1 
ATOM   2874 C  CA    . MET B 1 157 ? 17.047  16.837  6.728   1.00 22.77  ? 119 MET B CA    1 
ATOM   2875 C  C     . MET B 1 157 ? 16.059  15.685  6.831   1.00 28.73  ? 119 MET B C     1 
ATOM   2876 O  O     . MET B 1 157 ? 15.457  15.298  5.824   1.00 34.07  ? 119 MET B O     1 
ATOM   2877 C  CB    . MET B 1 157 ? 18.464  16.308  6.518   1.00 28.72  ? 119 MET B CB    1 
ATOM   2878 C  CG    . MET B 1 157 ? 18.576  15.121  5.587   1.00 42.73  ? 119 MET B CG    1 
ATOM   2879 S  SD    . MET B 1 157 ? 20.216  15.132  4.858   1.00 52.15  ? 119 MET B SD    1 
ATOM   2880 C  CE    . MET B 1 157 ? 20.278  16.844  4.338   1.00 28.06  ? 119 MET B CE    1 
ATOM   2881 N  N     . HIS B 1 158 ? 15.855  15.142  8.028   1.00 31.81  ? 120 HIS B N     1 
ATOM   2882 C  CA    . HIS B 1 158 ? 15.123  13.898  8.175   1.00 21.41  ? 120 HIS B CA    1 
ATOM   2883 C  C     . HIS B 1 158 ? 13.825  14.006  8.950   1.00 23.32  ? 120 HIS B C     1 
ATOM   2884 O  O     . HIS B 1 158 ? 13.040  13.057  8.912   1.00 36.19  ? 120 HIS B O     1 
ATOM   2885 C  CB    . HIS B 1 158 ? 16.009  12.841  8.844   1.00 21.92  ? 120 HIS B CB    1 
ATOM   2886 C  CG    . HIS B 1 158 ? 16.890  12.109  7.884   1.00 29.67  ? 120 HIS B CG    1 
ATOM   2887 N  ND1   . HIS B 1 158 ? 16.431  11.081  7.088   1.00 25.00  ? 120 HIS B ND1   1 
ATOM   2888 C  CD2   . HIS B 1 158 ? 18.202  12.256  7.589   1.00 26.74  ? 120 HIS B CD2   1 
ATOM   2889 C  CE1   . HIS B 1 158 ? 17.426  10.623  6.350   1.00 22.24  ? 120 HIS B CE1   1 
ATOM   2890 N  NE2   . HIS B 1 158 ? 18.512  11.318  6.635   1.00 23.18  ? 120 HIS B NE2   1 
ATOM   2891 N  N     . ALA B 1 159 ? 13.574  15.097  9.668   1.00 29.85  ? 121 ALA B N     1 
ATOM   2892 C  CA    . ALA B 1 159 ? 12.285  15.218  10.331  1.00 29.08  ? 121 ALA B CA    1 
ATOM   2893 C  C     . ALA B 1 159 ? 11.203  15.517  9.304   1.00 36.65  ? 121 ALA B C     1 
ATOM   2894 O  O     . ALA B 1 159 ? 11.472  15.799  8.132   1.00 39.03  ? 121 ALA B O     1 
ATOM   2895 C  CB    . ALA B 1 159 ? 12.300  16.310  11.398  1.00 30.48  ? 121 ALA B CB    1 
ATOM   2896 N  N     . TYR B 1 160 ? 9.960   15.463  9.755   1.00 33.43  ? 122 TYR B N     1 
ATOM   2897 C  CA    . TYR B 1 160 ? 8.840   15.534  8.831   1.00 49.83  ? 122 TYR B CA    1 
ATOM   2898 C  C     . TYR B 1 160 ? 8.084   16.850  8.969   1.00 41.32  ? 122 TYR B C     1 
ATOM   2899 O  O     . TYR B 1 160 ? 7.077   17.065  8.277   1.00 44.73  ? 122 TYR B O     1 
ATOM   2900 C  CB    . TYR B 1 160 ? 7.933   14.291  9.002   1.00 46.96  ? 122 TYR B CB    1 
ATOM   2901 C  CG    . TYR B 1 160 ? 8.583   12.995  8.470   1.00 38.49  ? 122 TYR B CG    1 
ATOM   2902 C  CD1   . TYR B 1 160 ? 7.935   12.174  7.545   1.00 43.38  ? 122 TYR B CD1   1 
ATOM   2903 C  CD2   . TYR B 1 160 ? 9.853   12.608  8.892   1.00 42.69  ? 122 TYR B CD2   1 
ATOM   2904 C  CE1   . TYR B 1 160 ? 8.551   10.999  7.052   1.00 38.63  ? 122 TYR B CE1   1 
ATOM   2905 C  CE2   . TYR B 1 160 ? 10.472  11.453  8.409   1.00 44.90  ? 122 TYR B CE2   1 
ATOM   2906 C  CZ    . TYR B 1 160 ? 9.827   10.651  7.491   1.00 44.00  ? 122 TYR B CZ    1 
ATOM   2907 O  OH    . TYR B 1 160 ? 10.476  9.509   7.040   1.00 38.05  ? 122 TYR B OH    1 
ATOM   2908 N  N     . ALA B 1 161 ? 8.580   17.750  9.815   1.00 33.82  ? 123 ALA B N     1 
ATOM   2909 C  CA    . ALA B 1 161 ? 8.304   19.176  9.732   1.00 32.33  ? 123 ALA B CA    1 
ATOM   2910 C  C     . ALA B 1 161 ? 9.619   19.920  9.524   1.00 37.99  ? 123 ALA B C     1 
ATOM   2911 O  O     . ALA B 1 161 ? 10.681  19.476  9.970   1.00 40.13  ? 123 ALA B O     1 
ATOM   2912 C  CB    . ALA B 1 161 ? 7.597   19.695  10.983  1.00 41.26  ? 123 ALA B CB    1 
ATOM   2913 N  N     . GLU B 1 162 ? 9.542   21.044  8.822   1.00 37.66  ? 124 GLU B N     1 
ATOM   2914 C  CA    . GLU B 1 162 ? 10.703  21.846  8.469   1.00 44.16  ? 124 GLU B CA    1 
ATOM   2915 C  C     . GLU B 1 162 ? 10.960  22.897  9.539   1.00 46.49  ? 124 GLU B C     1 
ATOM   2916 O  O     . GLU B 1 162 ? 10.027  23.586  9.981   1.00 43.36  ? 124 GLU B O     1 
ATOM   2917 C  CB    . GLU B 1 162 ? 10.508  22.511  7.105   1.00 30.00  ? 124 GLU B CB    1 
ATOM   2918 C  CG    . GLU B 1 162 ? 10.478  21.536  5.938   1.00 30.00  ? 124 GLU B CG    1 
ATOM   2919 C  CD    . GLU B 1 162 ? 10.211  22.225  4.613   1.00 30.00  ? 124 GLU B CD    1 
ATOM   2920 O  OE1   . GLU B 1 162 ? 9.862   23.424  4.624   1.00 30.00  ? 124 GLU B OE1   1 
ATOM   2921 O  OE2   . GLU B 1 162 ? 10.347  21.566  3.560   1.00 30.00  ? 124 GLU B OE2   1 
ATOM   2922 N  N     . ASN B 1 163 ? 12.249  23.041  9.925   1.00 36.54  ? 125 ASN B N     1 
ATOM   2923 C  CA    . ASN B 1 163 ? 12.531  23.794  11.136  1.00 37.79  ? 125 ASN B CA    1 
ATOM   2924 C  C     . ASN B 1 163 ? 11.640  23.230  12.237  1.00 36.07  ? 125 ASN B C     1 
ATOM   2925 O  O     . ASN B 1 163 ? 10.638  23.846  12.634  1.00 43.70  ? 125 ASN B O     1 
ATOM   2926 C  CB    . ASN B 1 163 ? 12.422  25.302  10.829  1.00 41.22  ? 125 ASN B CB    1 
ATOM   2927 C  CG    . ASN B 1 163 ? 12.839  26.239  12.013  1.00 48.07  ? 125 ASN B CG    1 
ATOM   2928 O  OD1   . ASN B 1 163 ? 13.160  27.386  11.766  1.00 55.78  ? 125 ASN B OD1   1 
ATOM   2929 N  ND2   . ASN B 1 163 ? 12.459  25.882  13.236  1.00 60.89  ? 125 ASN B ND2   1 
ATOM   2930 N  N     . PRO B 1 164 ? 11.961  22.024  12.714  1.00 29.86  ? 126 PRO B N     1 
ATOM   2931 C  CA    . PRO B 1 164 ? 11.137  21.372  13.736  1.00 33.66  ? 126 PRO B CA    1 
ATOM   2932 C  C     . PRO B 1 164 ? 11.543  21.785  15.141  1.00 29.56  ? 126 PRO B C     1 
ATOM   2933 O  O     . PRO B 1 164 ? 12.689  22.137  15.407  1.00 30.08  ? 126 PRO B O     1 
ATOM   2934 C  CB    . PRO B 1 164 ? 11.426  19.883  13.501  1.00 20.73  ? 126 PRO B CB    1 
ATOM   2935 C  CG    . PRO B 1 164 ? 12.846  19.876  13.082  1.00 24.29  ? 126 PRO B CG    1 
ATOM   2936 C  CD    . PRO B 1 164 ? 13.101  21.171  12.324  1.00 27.12  ? 126 PRO B CD    1 
ATOM   2937 N  N     . ASP B 1 165 ? 10.576  21.733  16.049  1.00 29.54  ? 127 ASP B N     1 
ATOM   2938 C  CA    . ASP B 1 165 ? 10.810  22.106  17.440  1.00 30.02  ? 127 ASP B CA    1 
ATOM   2939 C  C     . ASP B 1 165 ? 11.889  21.254  18.120  1.00 26.54  ? 127 ASP B C     1 
ATOM   2940 O  O     . ASP B 1 165 ? 11.683  20.068  18.391  1.00 25.66  ? 127 ASP B O     1 
ATOM   2941 C  CB    . ASP B 1 165 ? 9.502   22.004  18.220  1.00 27.60  ? 127 ASP B CB    1 
ATOM   2942 C  CG    . ASP B 1 165 ? 8.436   22.938  17.699  1.00 31.21  ? 127 ASP B CG    1 
ATOM   2943 O  OD1   . ASP B 1 165 ? 8.735   24.145  17.556  1.00 31.57  ? 127 ASP B OD1   1 
ATOM   2944 O  OD2   . ASP B 1 165 ? 7.300   22.459  17.449  1.00 23.98  ? 127 ASP B OD2   1 
ATOM   2945 N  N     . ILE B 1 166 ? 13.033  21.856  18.422  1.00 22.09  ? 128 ILE B N     1 
ATOM   2946 C  CA    . ILE B 1 166 ? 14.115  21.212  19.151  1.00 24.88  ? 128 ILE B CA    1 
ATOM   2947 C  C     . ILE B 1 166 ? 14.278  21.914  20.493  1.00 28.02  ? 128 ILE B C     1 
ATOM   2948 O  O     . ILE B 1 166 ? 14.057  23.125  20.610  1.00 29.49  ? 128 ILE B O     1 
ATOM   2949 C  CB    . ILE B 1 166 ? 15.437  21.255  18.350  1.00 24.49  ? 128 ILE B CB    1 
ATOM   2950 C  CG1   . ILE B 1 166 ? 15.260  20.655  16.957  1.00 22.43  ? 128 ILE B CG1   1 
ATOM   2951 C  CG2   . ILE B 1 166 ? 16.532  20.522  19.054  1.00 16.18  ? 128 ILE B CG2   1 
ATOM   2952 C  CD1   . ILE B 1 166 ? 16.368  21.060  16.038  1.00 22.92  ? 128 ILE B CD1   1 
ATOM   2953 N  N     . VAL B 1 167 ? 14.659  21.142  21.515  1.00 26.42  ? 129 VAL B N     1 
ATOM   2954 C  CA    . VAL B 1 167 ? 15.029  21.662  22.829  1.00 25.36  ? 129 VAL B CA    1 
ATOM   2955 C  C     . VAL B 1 167 ? 16.334  20.987  23.236  1.00 25.33  ? 129 VAL B C     1 
ATOM   2956 O  O     . VAL B 1 167 ? 16.426  19.753  23.255  1.00 20.54  ? 129 VAL B O     1 
ATOM   2957 C  CB    . VAL B 1 167 ? 13.937  21.416  23.892  1.00 25.71  ? 129 VAL B CB    1 
ATOM   2958 C  CG1   . VAL B 1 167 ? 14.488  21.677  25.282  1.00 20.00  ? 129 VAL B CG1   1 
ATOM   2959 C  CG2   . VAL B 1 167 ? 12.739  22.299  23.647  1.00 18.80  ? 129 VAL B CG2   1 
ATOM   2960 N  N     . LEU B 1 168 ? 17.339  21.783  23.567  1.00 15.61  ? 130 LEU B N     1 
ATOM   2961 C  CA    . LEU B 1 168 ? 18.690  21.268  23.658  1.00 17.81  ? 130 LEU B CA    1 
ATOM   2962 C  C     . LEU B 1 168 ? 19.098  21.156  25.122  1.00 24.45  ? 130 LEU B C     1 
ATOM   2963 O  O     . LEU B 1 168 ? 18.843  22.062  25.919  1.00 17.67  ? 130 LEU B O     1 
ATOM   2964 C  CB    . LEU B 1 168 ? 19.633  22.170  22.864  1.00 16.53  ? 130 LEU B CB    1 
ATOM   2965 C  CG    . LEU B 1 168 ? 21.131  22.110  23.061  1.00 9.92   ? 130 LEU B CG    1 
ATOM   2966 C  CD1   . LEU B 1 168 ? 21.732  20.778  22.622  1.00 11.05  ? 130 LEU B CD1   1 
ATOM   2967 C  CD2   . LEU B 1 168 ? 21.749  23.277  22.314  1.00 19.67  ? 130 LEU B CD2   1 
ATOM   2968 N  N     . CYS B 1 169 ? 19.720  20.032  25.472  1.00 18.04  ? 131 CYS B N     1 
ATOM   2969 C  CA    . CYS B 1 169 ? 20.058  19.715  26.858  1.00 28.31  ? 131 CYS B CA    1 
ATOM   2970 C  C     . CYS B 1 169 ? 21.538  19.392  26.998  1.00 18.94  ? 131 CYS B C     1 
ATOM   2971 O  O     . CYS B 1 169 ? 22.024  18.420  26.412  1.00 23.53  ? 131 CYS B O     1 
ATOM   2972 C  CB    . CYS B 1 169 ? 19.232  18.534  27.366  1.00 24.48  ? 131 CYS B CB    1 
ATOM   2973 S  SG    . CYS B 1 169 ? 17.540  18.933  27.671  1.00 25.70  ? 131 CYS B SG    1 
ATOM   2974 N  N     . GLY B 1 170 ? 22.244  20.186  27.788  1.00 12.76  ? 132 GLY B N     1 
ATOM   2975 C  CA    . GLY B 1 170 ? 23.577  19.800  28.191  1.00 16.24  ? 132 GLY B CA    1 
ATOM   2976 C  C     . GLY B 1 170 ? 23.437  19.029  29.480  1.00 21.46  ? 132 GLY B C     1 
ATOM   2977 O  O     . GLY B 1 170 ? 23.050  19.600  30.500  1.00 21.16  ? 132 GLY B O     1 
ATOM   2978 N  N     . ASN B 1 171 ? 23.707  17.732  29.447  1.00 21.73  ? 133 ASN B N     1 
ATOM   2979 C  CA    . ASN B 1 171 ? 23.416  16.847  30.563  1.00 16.73  ? 133 ASN B CA    1 
ATOM   2980 C  C     . ASN B 1 171 ? 24.670  16.546  31.376  1.00 20.27  ? 133 ASN B C     1 
ATOM   2981 O  O     . ASN B 1 171 ? 25.797  16.845  30.968  1.00 21.84  ? 133 ASN B O     1 
ATOM   2982 C  CB    . ASN B 1 171 ? 22.798  15.547  30.050  1.00 17.59  ? 133 ASN B CB    1 
ATOM   2983 C  CG    . ASN B 1 171 ? 22.091  14.781  31.128  1.00 18.36  ? 133 ASN B CG    1 
ATOM   2984 O  OD1   . ASN B 1 171 ? 21.366  15.353  31.950  1.00 23.25  ? 133 ASN B OD1   1 
ATOM   2985 N  ND2   . ASN B 1 171 ? 22.300  13.478  31.147  1.00 16.00  ? 133 ASN B ND2   1 
ATOM   2986 N  N     . LYS B 1 172 ? 24.444  15.901  32.533  1.00 18.35  ? 134 LYS B N     1 
ATOM   2987 C  CA    . LYS B 1 172 ? 25.465  15.596  33.545  1.00 20.29  ? 134 LYS B CA    1 
ATOM   2988 C  C     . LYS B 1 172 ? 25.980  16.878  34.196  1.00 16.61  ? 134 LYS B C     1 
ATOM   2989 O  O     . LYS B 1 172 ? 27.154  17.006  34.546  1.00 22.82  ? 134 LYS B O     1 
ATOM   2990 C  CB    . LYS B 1 172 ? 26.597  14.740  32.976  1.00 21.80  ? 134 LYS B CB    1 
ATOM   2991 C  CG    . LYS B 1 172 ? 26.061  13.533  32.206  1.00 18.65  ? 134 LYS B CG    1 
ATOM   2992 C  CD    . LYS B 1 172 ? 27.161  12.623  31.723  1.00 16.93  ? 134 LYS B CD    1 
ATOM   2993 C  CE    . LYS B 1 172 ? 26.597  11.407  31.025  1.00 17.22  ? 134 LYS B CE    1 
ATOM   2994 N  NZ    . LYS B 1 172 ? 27.721  10.580  30.502  1.00 24.81  ? 134 LYS B NZ    1 
ATOM   2995 N  N     . SER B 1 173 ? 25.063  17.829  34.372  1.00 14.25  ? 135 SER B N     1 
ATOM   2996 C  CA    . SER B 1 173 ? 25.336  19.066  35.068  1.00 15.99  ? 135 SER B CA    1 
ATOM   2997 C  C     . SER B 1 173 ? 25.725  18.846  36.514  1.00 21.54  ? 135 SER B C     1 
ATOM   2998 O  O     . SER B 1 173 ? 26.204  19.784  37.152  1.00 19.43  ? 135 SER B O     1 
ATOM   2999 C  CB    . SER B 1 173 ? 24.113  19.976  34.978  1.00 14.75  ? 135 SER B CB    1 
ATOM   3000 O  OG    . SER B 1 173 ? 23.158  19.653  35.970  1.00 14.87  ? 135 SER B OG    1 
ATOM   3001 N  N     . ASP B 1 174 ? 25.524  17.645  37.040  1.00 25.26  ? 136 ASP B N     1 
ATOM   3002 C  CA    . ASP B 1 174 ? 25.951  17.293  38.379  1.00 22.43  ? 136 ASP B CA    1 
ATOM   3003 C  C     . ASP B 1 174 ? 27.417  16.872  38.437  1.00 36.72  ? 136 ASP B C     1 
ATOM   3004 O  O     . ASP B 1 174 ? 27.927  16.612  39.533  1.00 33.53  ? 136 ASP B O     1 
ATOM   3005 C  CB    . ASP B 1 174 ? 25.057  16.182  38.924  1.00 23.89  ? 136 ASP B CB    1 
ATOM   3006 C  CG    . ASP B 1 174 ? 25.146  14.931  38.105  1.00 20.48  ? 136 ASP B CG    1 
ATOM   3007 O  OD1   . ASP B 1 174 ? 24.705  14.953  36.937  1.00 25.55  ? 136 ASP B OD1   1 
ATOM   3008 O  OD2   . ASP B 1 174 ? 25.683  13.930  38.618  1.00 26.81  ? 136 ASP B OD2   1 
ATOM   3009 N  N     . LEU B 1 175 ? 28.123  16.848  37.306  1.00 25.32  ? 137 LEU B N     1 
ATOM   3010 C  CA    . LEU B 1 175 ? 29.551  16.532  37.282  1.00 22.09  ? 137 LEU B CA    1 
ATOM   3011 C  C     . LEU B 1 175 ? 30.314  17.808  36.927  1.00 29.75  ? 137 LEU B C     1 
ATOM   3012 O  O     . LEU B 1 175 ? 30.710  18.023  35.783  1.00 24.11  ? 137 LEU B O     1 
ATOM   3013 C  CB    . LEU B 1 175 ? 29.855  15.373  36.290  1.00 20.20  ? 137 LEU B CB    1 
ATOM   3014 C  CG    . LEU B 1 175 ? 29.042  14.084  36.487  1.00 22.19  ? 137 LEU B CG    1 
ATOM   3015 C  CD1   . LEU B 1 175 ? 29.418  12.959  35.504  1.00 17.60  ? 137 LEU B CD1   1 
ATOM   3016 C  CD2   . LEU B 1 175 ? 29.152  13.599  37.935  1.00 27.76  ? 137 LEU B CD2   1 
ATOM   3017 N  N     . GLU B 1 176 ? 30.518  18.663  37.934  1.00 31.53  ? 138 GLU B N     1 
ATOM   3018 C  CA    . GLU B 1 176 ? 31.174  19.954  37.722  1.00 33.58  ? 138 GLU B CA    1 
ATOM   3019 C  C     . GLU B 1 176 ? 32.669  19.784  37.592  1.00 28.12  ? 138 GLU B C     1 
ATOM   3020 O  O     . GLU B 1 176 ? 33.303  20.378  36.713  1.00 35.21  ? 138 GLU B O     1 
ATOM   3021 C  CB    . GLU B 1 176 ? 30.875  20.899  38.882  1.00 26.54  ? 138 GLU B CB    1 
ATOM   3022 C  CG    . GLU B 1 176 ? 29.468  21.385  38.914  1.00 31.79  ? 138 GLU B CG    1 
ATOM   3023 C  CD    . GLU B 1 176 ? 28.565  20.293  39.462  1.00 47.86  ? 138 GLU B CD    1 
ATOM   3024 O  OE1   . GLU B 1 176 ? 28.307  20.206  40.680  1.00 45.79  ? 138 GLU B OE1   1 
ATOM   3025 O  OE2   . GLU B 1 176 ? 28.192  19.442  38.637  1.00 56.06  ? 138 GLU B OE2   1 
ATOM   3026 N  N     . ASP B 1 177 ? 33.237  18.960  38.467  1.00 35.46  ? 139 ASP B N     1 
ATOM   3027 C  CA    . ASP B 1 177 ? 34.652  18.639  38.451  1.00 36.16  ? 139 ASP B CA    1 
ATOM   3028 C  C     . ASP B 1 177 ? 35.113  18.116  37.100  1.00 37.35  ? 139 ASP B C     1 
ATOM   3029 O  O     . ASP B 1 177 ? 36.322  18.058  36.860  1.00 49.88  ? 139 ASP B O     1 
ATOM   3030 C  CB    . ASP B 1 177 ? 34.926  17.605  39.542  1.00 37.91  ? 139 ASP B CB    1 
ATOM   3031 C  CG    . ASP B 1 177 ? 34.859  18.202  40.931  1.00 54.36  ? 139 ASP B CG    1 
ATOM   3032 O  OD1   . ASP B 1 177 ? 34.951  17.424  41.902  1.00 69.33  ? 139 ASP B OD1   1 
ATOM   3033 O  OD2   . ASP B 1 177 ? 34.719  19.444  41.055  1.00 48.09  ? 139 ASP B OD2   1 
ATOM   3034 N  N     . GLN B 1 178 ? 34.190  17.720  36.220  1.00 40.80  ? 140 GLN B N     1 
ATOM   3035 C  CA    . GLN B 1 178 ? 34.544  17.093  34.956  1.00 29.21  ? 140 GLN B CA    1 
ATOM   3036 C  C     . GLN B 1 178 ? 33.938  17.806  33.760  1.00 27.46  ? 140 GLN B C     1 
ATOM   3037 O  O     . GLN B 1 178 ? 34.060  17.315  32.631  1.00 27.48  ? 140 GLN B O     1 
ATOM   3038 C  CB    . GLN B 1 178 ? 34.124  15.626  34.971  1.00 29.12  ? 140 GLN B CB    1 
ATOM   3039 C  CG    . GLN B 1 178 ? 34.597  14.893  36.213  1.00 27.91  ? 140 GLN B CG    1 
ATOM   3040 C  CD    . GLN B 1 178 ? 33.483  14.140  36.887  1.00 39.08  ? 140 GLN B CD    1 
ATOM   3041 O  OE1   . GLN B 1 178 ? 32.958  13.169  36.329  1.00 41.65  ? 140 GLN B OE1   1 
ATOM   3042 N  NE2   . GLN B 1 178 ? 33.097  14.588  38.092  1.00 37.36  ? 140 GLN B NE2   1 
ATOM   3043 N  N     . ARG B 1 179 ? 33.292  18.948  33.972  1.00 30.16  ? 141 ARG B N     1 
ATOM   3044 C  CA    . ARG B 1 179 ? 32.746  19.709  32.859  1.00 21.27  ? 141 ARG B CA    1 
ATOM   3045 C  C     . ARG B 1 179 ? 33.870  20.175  31.938  1.00 21.45  ? 141 ARG B C     1 
ATOM   3046 O  O     . ARG B 1 179 ? 35.018  20.324  32.359  1.00 26.72  ? 141 ARG B O     1 
ATOM   3047 C  CB    . ARG B 1 179 ? 31.956  20.897  33.394  1.00 23.61  ? 141 ARG B CB    1 
ATOM   3048 C  CG    . ARG B 1 179 ? 31.098  21.576  32.376  1.00 16.36  ? 141 ARG B CG    1 
ATOM   3049 C  CD    . ARG B 1 179 ? 30.743  22.976  32.817  1.00 25.13  ? 141 ARG B CD    1 
ATOM   3050 N  NE    . ARG B 1 179 ? 29.804  23.590  31.887  1.00 33.20  ? 141 ARG B NE    1 
ATOM   3051 C  CZ    . ARG B 1 179 ? 28.564  23.949  32.190  1.00 27.27  ? 141 ARG B CZ    1 
ATOM   3052 N  NH1   . ARG B 1 179 ? 28.089  23.767  33.415  1.00 32.69  ? 141 ARG B NH1   1 
ATOM   3053 N  NH2   . ARG B 1 179 ? 27.802  24.498  31.256  1.00 28.00  ? 141 ARG B NH2   1 
ATOM   3054 N  N     . VAL B 1 180 ? 33.549  20.360  30.655  1.00 23.52  ? 142 VAL B N     1 
ATOM   3055 C  CA    . VAL B 1 180 ? 34.521  20.887  29.693  1.00 31.18  ? 142 VAL B CA    1 
ATOM   3056 C  C     . VAL B 1 180 ? 33.823  21.763  28.660  1.00 29.31  ? 142 VAL B C     1 
ATOM   3057 O  O     . VAL B 1 180 ? 34.480  22.461  27.884  1.00 30.35  ? 142 VAL B O     1 
ATOM   3058 C  CB    . VAL B 1 180 ? 35.317  19.784  28.960  1.00 21.99  ? 142 VAL B CB    1 
ATOM   3059 C  CG1   . VAL B 1 180 ? 36.077  18.881  29.911  1.00 23.86  ? 142 VAL B CG1   1 
ATOM   3060 C  CG2   . VAL B 1 180 ? 34.389  18.958  28.069  1.00 29.78  ? 142 VAL B CG2   1 
ATOM   3061 N  N     . VAL B 1 181 ? 32.503  21.715  28.606  1.00 19.58  ? 143 VAL B N     1 
ATOM   3062 C  CA    . VAL B 1 181 ? 31.761  22.564  27.687  1.00 21.76  ? 143 VAL B CA    1 
ATOM   3063 C  C     . VAL B 1 181 ? 31.475  23.869  28.402  1.00 33.17  ? 143 VAL B C     1 
ATOM   3064 O  O     . VAL B 1 181 ? 30.818  23.880  29.453  1.00 35.08  ? 143 VAL B O     1 
ATOM   3065 C  CB    . VAL B 1 181 ? 30.461  21.894  27.219  1.00 25.71  ? 143 VAL B CB    1 
ATOM   3066 C  CG1   . VAL B 1 181 ? 29.579  22.899  26.488  1.00 15.54  ? 143 VAL B CG1   1 
ATOM   3067 C  CG2   . VAL B 1 181 ? 30.774  20.691  26.338  1.00 28.60  ? 143 VAL B CG2   1 
ATOM   3068 N  N     . LYS B 1 182 ? 31.961  24.968  27.841  1.00 25.76  ? 144 LYS B N     1 
ATOM   3069 C  CA    . LYS B 1 182 ? 31.704  26.260  28.454  1.00 28.40  ? 144 LYS B CA    1 
ATOM   3070 C  C     . LYS B 1 182 ? 30.238  26.630  28.283  1.00 30.74  ? 144 LYS B C     1 
ATOM   3071 O  O     . LYS B 1 182 ? 29.678  26.508  27.186  1.00 30.11  ? 144 LYS B O     1 
ATOM   3072 C  CB    . LYS B 1 182 ? 32.616  27.324  27.855  1.00 35.94  ? 144 LYS B CB    1 
ATOM   3073 C  CG    . LYS B 1 182 ? 33.922  27.476  28.615  1.00 34.47  ? 144 LYS B CG    1 
ATOM   3074 C  CD    . LYS B 1 182 ? 35.057  27.953  27.714  1.00 53.45  ? 144 LYS B CD    1 
ATOM   3075 C  CE    . LYS B 1 182 ? 36.348  28.124  28.508  1.00 48.26  ? 144 LYS B CE    1 
ATOM   3076 N  NZ    . LYS B 1 182 ? 37.489  27.362  27.906  1.00 44.49  ? 144 LYS B NZ    1 
ATOM   3077 N  N     . GLU B 1 183 ? 29.607  27.041  29.390  1.00 35.52  ? 145 GLU B N     1 
ATOM   3078 C  CA    . GLU B 1 183 ? 28.201  27.432  29.354  1.00 27.18  ? 145 GLU B CA    1 
ATOM   3079 C  C     . GLU B 1 183 ? 27.940  28.445  28.248  1.00 26.11  ? 145 GLU B C     1 
ATOM   3080 O  O     . GLU B 1 183 ? 26.947  28.349  27.521  1.00 26.43  ? 145 GLU B O     1 
ATOM   3081 C  CB    . GLU B 1 183 ? 27.792  28.004  30.712  1.00 21.57  ? 145 GLU B CB    1 
ATOM   3082 C  CG    . GLU B 1 183 ? 26.279  28.199  30.916  1.00 28.54  ? 145 GLU B CG    1 
ATOM   3083 C  CD    . GLU B 1 183 ? 25.898  28.443  32.387  1.00 43.61  ? 145 GLU B CD    1 
ATOM   3084 O  OE1   . GLU B 1 183 ? 26.092  29.574  32.878  1.00 43.13  ? 145 GLU B OE1   1 
ATOM   3085 O  OE2   . GLU B 1 183 ? 25.416  27.504  33.060  1.00 33.04  ? 145 GLU B OE2   1 
ATOM   3086 N  N     . GLU B 1 184 ? 28.829  29.424  28.112  1.00 32.44  ? 146 GLU B N     1 
ATOM   3087 C  CA    . GLU B 1 184 ? 28.679  30.456  27.092  1.00 33.61  ? 146 GLU B CA    1 
ATOM   3088 C  C     . GLU B 1 184 ? 28.660  29.867  25.684  1.00 32.99  ? 146 GLU B C     1 
ATOM   3089 O  O     . GLU B 1 184 ? 27.901  30.325  24.820  1.00 20.83  ? 146 GLU B O     1 
ATOM   3090 C  CB    . GLU B 1 184 ? 29.816  31.462  27.236  1.00 30.49  ? 146 GLU B CB    1 
ATOM   3091 C  CG    . GLU B 1 184 ? 30.008  31.928  28.666  1.00 45.51  ? 146 GLU B CG    1 
ATOM   3092 C  CD    . GLU B 1 184 ? 31.300  31.419  29.303  1.00 60.72  ? 146 GLU B CD    1 
ATOM   3093 O  OE1   . GLU B 1 184 ? 31.385  30.210  29.637  1.00 52.31  ? 146 GLU B OE1   1 
ATOM   3094 O  OE2   . GLU B 1 184 ? 32.234  32.239  29.466  1.00 45.86  ? 146 GLU B OE2   1 
ATOM   3095 N  N     . GLU B 1 185 ? 29.497  28.860  25.430  1.00 34.30  ? 147 GLU B N     1 
ATOM   3096 C  CA    . GLU B 1 185 ? 29.540  28.264  24.100  1.00 29.78  ? 147 GLU B CA    1 
ATOM   3097 C  C     . GLU B 1 185 ? 28.217  27.599  23.752  1.00 32.36  ? 147 GLU B C     1 
ATOM   3098 O  O     . GLU B 1 185 ? 27.766  27.663  22.599  1.00 35.34  ? 147 GLU B O     1 
ATOM   3099 C  CB    . GLU B 1 185 ? 30.681  27.254  24.010  1.00 37.47  ? 147 GLU B CB    1 
ATOM   3100 C  CG    . GLU B 1 185 ? 32.060  27.877  24.010  1.00 37.96  ? 147 GLU B CG    1 
ATOM   3101 C  CD    . GLU B 1 185 ? 33.093  26.960  23.388  1.00 45.14  ? 147 GLU B CD    1 
ATOM   3102 O  OE1   . GLU B 1 185 ? 32.840  25.726  23.351  1.00 27.34  ? 147 GLU B OE1   1 
ATOM   3103 O  OE2   . GLU B 1 185 ? 34.138  27.478  22.923  1.00 44.67  ? 147 GLU B OE2   1 
ATOM   3104 N  N     . ALA B 1 186 ? 27.580  26.957  24.738  1.00 28.73  ? 148 ALA B N     1 
ATOM   3105 C  CA    . ALA B 1 186 ? 26.281  26.333  24.499  1.00 26.96  ? 148 ALA B CA    1 
ATOM   3106 C  C     . ALA B 1 186 ? 25.188  27.382  24.334  1.00 17.96  ? 148 ALA B C     1 
ATOM   3107 O  O     . ALA B 1 186 ? 24.379  27.303  23.407  1.00 18.99  ? 148 ALA B O     1 
ATOM   3108 C  CB    . ALA B 1 186 ? 25.936  25.367  25.634  1.00 16.78  ? 148 ALA B CB    1 
ATOM   3109 N  N     . ILE B 1 187 ? 25.135  28.367  25.234  1.00 27.38  ? 149 ILE B N     1 
ATOM   3110 C  CA    . ILE B 1 187 ? 24.170  29.452  25.078  1.00 28.31  ? 149 ILE B CA    1 
ATOM   3111 C  C     . ILE B 1 187 ? 24.287  30.060  23.689  1.00 25.73  ? 149 ILE B C     1 
ATOM   3112 O  O     . ILE B 1 187 ? 23.278  30.322  23.019  1.00 31.07  ? 149 ILE B O     1 
ATOM   3113 C  CB    . ILE B 1 187 ? 24.370  30.506  26.183  1.00 30.22  ? 149 ILE B CB    1 
ATOM   3114 C  CG1   . ILE B 1 187 ? 23.986  29.911  27.532  1.00 26.55  ? 149 ILE B CG1   1 
ATOM   3115 C  CG2   . ILE B 1 187 ? 23.555  31.781  25.901  1.00 10.42  ? 149 ILE B CG2   1 
ATOM   3116 C  CD1   . ILE B 1 187 ? 24.403  30.758  28.716  1.00 20.07  ? 149 ILE B CD1   1 
ATOM   3117 N  N     . ALA B 1 188 ? 25.525  30.255  23.222  1.00 30.09  ? 150 ALA B N     1 
ATOM   3118 C  CA    . ALA B 1 188 ? 25.749  30.830  21.899  1.00 25.55  ? 150 ALA B CA    1 
ATOM   3119 C  C     . ALA B 1 188 ? 25.261  29.895  20.807  1.00 28.33  ? 150 ALA B C     1 
ATOM   3120 O  O     . ALA B 1 188 ? 24.552  30.321  19.891  1.00 24.19  ? 150 ALA B O     1 
ATOM   3121 C  CB    . ALA B 1 188 ? 27.230  31.146  21.700  1.00 14.60  ? 150 ALA B CB    1 
ATOM   3122 N  N     . LEU B 1 189 ? 25.645  28.618  20.878  1.00 27.98  ? 151 LEU B N     1 
ATOM   3123 C  CA    . LEU B 1 189 ? 25.179  27.666  19.880  1.00 24.60  ? 151 LEU B CA    1 
ATOM   3124 C  C     . LEU B 1 189 ? 23.665  27.688  19.797  1.00 22.51  ? 151 LEU B C     1 
ATOM   3125 O  O     . LEU B 1 189 ? 23.096  27.882  18.719  1.00 23.57  ? 151 LEU B O     1 
ATOM   3126 C  CB    . LEU B 1 189 ? 25.670  26.255  20.206  1.00 27.80  ? 151 LEU B CB    1 
ATOM   3127 C  CG    . LEU B 1 189 ? 25.365  25.235  19.102  1.00 20.47  ? 151 LEU B CG    1 
ATOM   3128 C  CD1   . LEU B 1 189 ? 26.119  25.583  17.825  1.00 24.53  ? 151 LEU B CD1   1 
ATOM   3129 C  CD2   . LEU B 1 189 ? 25.704  23.834  19.542  1.00 30.90  ? 151 LEU B CD2   1 
ATOM   3130 N  N     . ALA B 1 190 ? 22.993  27.544  20.946  1.00 17.92  ? 152 ALA B N     1 
ATOM   3131 C  CA    . ALA B 1 190 ? 21.540  27.439  20.936  1.00 17.29  ? 152 ALA B CA    1 
ATOM   3132 C  C     . ALA B 1 190 ? 20.895  28.747  20.525  1.00 17.21  ? 152 ALA B C     1 
ATOM   3133 O  O     . ALA B 1 190 ? 19.814  28.738  19.937  1.00 20.70  ? 152 ALA B O     1 
ATOM   3134 C  CB    . ALA B 1 190 ? 21.018  26.992  22.307  1.00 18.99  ? 152 ALA B CB    1 
ATOM   3135 N  N     . GLU B 1 191 ? 21.538  29.874  20.822  1.00 16.77  ? 153 GLU B N     1 
ATOM   3136 C  CA    . GLU B 1 191 ? 21.053  31.161  20.334  1.00 19.18  ? 153 GLU B CA    1 
ATOM   3137 C  C     . GLU B 1 191 ? 21.206  31.278  18.820  1.00 23.13  ? 153 GLU B C     1 
ATOM   3138 O  O     . GLU B 1 191 ? 20.312  31.806  18.147  1.00 16.56  ? 153 GLU B O     1 
ATOM   3139 C  CB    . GLU B 1 191 ? 21.798  32.292  21.044  1.00 19.07  ? 153 GLU B CB    1 
ATOM   3140 C  CG    . GLU B 1 191 ? 21.869  33.598  20.289  1.00 29.55  ? 153 GLU B CG    1 
ATOM   3141 C  CD    . GLU B 1 191 ? 20.572  34.388  20.334  1.00 42.88  ? 153 GLU B CD    1 
ATOM   3142 O  OE1   . GLU B 1 191 ? 20.380  35.270  19.463  1.00 39.74  ? 153 GLU B OE1   1 
ATOM   3143 O  OE2   . GLU B 1 191 ? 19.741  34.130  21.234  1.00 47.05  ? 153 GLU B OE2   1 
ATOM   3144 N  N     A LYS B 1 192 ? 22.336  30.804  18.274  0.55 24.97  ? 154 LYS B N     1 
ATOM   3145 N  N     B LYS B 1 192 ? 22.334  30.796  18.276  0.45 24.95  ? 154 LYS B N     1 
ATOM   3146 C  CA    A LYS B 1 192 ? 22.560  30.838  16.829  0.55 23.86  ? 154 LYS B CA    1 
ATOM   3147 C  CA    B LYS B 1 192 ? 22.566  30.829  16.833  0.45 23.82  ? 154 LYS B CA    1 
ATOM   3148 C  C     A LYS B 1 192 ? 21.423  30.162  16.067  0.55 21.77  ? 154 LYS B C     1 
ATOM   3149 C  C     B LYS B 1 192 ? 21.433  30.155  16.065  0.45 22.29  ? 154 LYS B C     1 
ATOM   3150 O  O     A LYS B 1 192 ? 21.101  30.560  14.942  0.55 21.24  ? 154 LYS B O     1 
ATOM   3151 O  O     B LYS B 1 192 ? 21.127  30.545  14.934  0.45 20.92  ? 154 LYS B O     1 
ATOM   3152 C  CB    A LYS B 1 192 ? 23.904  30.174  16.493  0.55 20.19  ? 154 LYS B CB    1 
ATOM   3153 C  CB    B LYS B 1 192 ? 23.911  30.164  16.502  0.45 20.21  ? 154 LYS B CB    1 
ATOM   3154 C  CG    A LYS B 1 192 ? 25.103  31.140  16.366  0.55 21.56  ? 154 LYS B CG    1 
ATOM   3155 C  CG    B LYS B 1 192 ? 25.147  31.051  16.748  0.45 21.55  ? 154 LYS B CG    1 
ATOM   3156 C  CD    A LYS B 1 192 ? 26.434  30.455  16.715  0.55 21.94  ? 154 LYS B CD    1 
ATOM   3157 C  CD    B LYS B 1 192 ? 26.466  30.390  16.300  0.45 21.75  ? 154 LYS B CD    1 
ATOM   3158 C  CE    A LYS B 1 192 ? 27.642  31.379  16.561  0.55 15.28  ? 154 LYS B CE    1 
ATOM   3159 C  CE    B LYS B 1 192 ? 26.816  29.159  17.140  0.45 20.59  ? 154 LYS B CE    1 
ATOM   3160 N  NZ    A LYS B 1 192 ? 27.696  32.442  17.608  0.55 16.29  ? 154 LYS B NZ    1 
ATOM   3161 N  NZ    B LYS B 1 192 ? 28.259  28.770  17.097  0.45 18.43  ? 154 LYS B NZ    1 
ATOM   3162 N  N     . TYR B 1 193 ? 20.784  29.163  16.672  1.00 24.60  ? 155 TYR B N     1 
ATOM   3163 C  CA    . TYR B 1 193 ? 19.681  28.455  16.047  1.00 23.58  ? 155 TYR B CA    1 
ATOM   3164 C  C     . TYR B 1 193 ? 18.315  28.843  16.586  1.00 25.05  ? 155 TYR B C     1 
ATOM   3165 O  O     . TYR B 1 193 ? 17.302  28.382  16.047  1.00 29.63  ? 155 TYR B O     1 
ATOM   3166 C  CB    . TYR B 1 193 ? 19.855  26.950  16.245  1.00 22.71  ? 155 TYR B CB    1 
ATOM   3167 C  CG    . TYR B 1 193 ? 20.951  26.313  15.452  1.00 24.84  ? 155 TYR B CG    1 
ATOM   3168 C  CD1   . TYR B 1 193 ? 20.723  25.872  14.161  1.00 24.91  ? 155 TYR B CD1   1 
ATOM   3169 C  CD2   . TYR B 1 193 ? 22.210  26.120  16.005  1.00 21.99  ? 155 TYR B CD2   1 
ATOM   3170 C  CE1   . TYR B 1 193 ? 21.715  25.265  13.431  1.00 24.78  ? 155 TYR B CE1   1 
ATOM   3171 C  CE2   . TYR B 1 193 ? 23.221  25.507  15.283  1.00 20.77  ? 155 TYR B CE2   1 
ATOM   3172 C  CZ    . TYR B 1 193 ? 22.967  25.078  13.990  1.00 29.80  ? 155 TYR B CZ    1 
ATOM   3173 O  OH    . TYR B 1 193 ? 23.958  24.458  13.245  1.00 27.79  ? 155 TYR B OH    1 
ATOM   3174 N  N     . GLY B 1 194 ? 18.252  29.649  17.638  1.00 23.46  ? 156 GLY B N     1 
ATOM   3175 C  CA    . GLY B 1 194 ? 16.963  29.941  18.249  1.00 26.03  ? 156 GLY B CA    1 
ATOM   3176 C  C     . GLY B 1 194 ? 16.370  28.743  18.974  1.00 24.68  ? 156 GLY B C     1 
ATOM   3177 O  O     . GLY B 1 194 ? 15.140  28.576  18.954  1.00 26.42  ? 156 GLY B O     1 
ATOM   3178 N  N     . ILE B 1 195 ? 17.200  27.944  19.593  1.00 18.42  ? 157 ILE B N     1 
ATOM   3179 C  CA    . ILE B 1 195 ? 16.787  26.683  20.237  1.00 27.90  ? 157 ILE B CA    1 
ATOM   3180 C  C     . ILE B 1 195 ? 16.887  26.888  21.758  1.00 22.68  ? 157 ILE B C     1 
ATOM   3181 O  O     . ILE B 1 195 ? 17.900  27.369  22.242  1.00 22.71  ? 157 ILE B O     1 
ATOM   3182 C  CB    . ILE B 1 195 ? 17.667  25.501  19.779  1.00 23.55  ? 157 ILE B CB    1 
ATOM   3183 C  CG1   . ILE B 1 195 ? 17.328  25.141  18.339  1.00 23.10  ? 157 ILE B CG1   1 
ATOM   3184 C  CG2   . ILE B 1 195 ? 17.467  24.270  20.643  1.00 22.52  ? 157 ILE B CG2   1 
ATOM   3185 C  CD1   . ILE B 1 195 ? 18.302  24.177  17.729  1.00 25.36  ? 157 ILE B CD1   1 
ATOM   3186 N  N     . PRO B 1 196 ? 15.817  26.562  22.502  1.00 27.80  ? 158 PRO B N     1 
ATOM   3187 C  CA    . PRO B 1 196 ? 15.893  26.731  23.967  1.00 21.20  ? 158 PRO B CA    1 
ATOM   3188 C  C     . PRO B 1 196 ? 16.898  25.770  24.569  1.00 21.81  ? 158 PRO B C     1 
ATOM   3189 O  O     . PRO B 1 196 ? 16.989  24.606  24.169  1.00 24.67  ? 158 PRO B O     1 
ATOM   3190 C  CB    . PRO B 1 196 ? 14.466  26.399  24.434  1.00 21.06  ? 158 PRO B CB    1 
ATOM   3191 C  CG    . PRO B 1 196 ? 13.615  26.456  23.203  1.00 26.86  ? 158 PRO B CG    1 
ATOM   3192 C  CD    . PRO B 1 196 ? 14.512  26.056  22.071  1.00 25.08  ? 158 PRO B CD    1 
ATOM   3193 N  N     . TYR B 1 197 ? 17.633  26.255  25.566  1.00 22.45  ? 159 TYR B N     1 
ATOM   3194 C  CA    . TYR B 1 197 ? 18.721  25.500  26.172  1.00 19.91  ? 159 TYR B CA    1 
ATOM   3195 C  C     . TYR B 1 197 ? 18.513  25.338  27.669  1.00 22.39  ? 159 TYR B C     1 
ATOM   3196 O  O     . TYR B 1 197 ? 18.166  26.302  28.359  1.00 25.67  ? 159 TYR B O     1 
ATOM   3197 C  CB    . TYR B 1 197 ? 20.032  26.202  25.914  1.00 15.99  ? 159 TYR B CB    1 
ATOM   3198 C  CG    . TYR B 1 197 ? 21.216  25.554  26.548  1.00 14.12  ? 159 TYR B CG    1 
ATOM   3199 C  CD1   . TYR B 1 197 ? 21.519  24.228  26.304  1.00 17.49  ? 159 TYR B CD1   1 
ATOM   3200 C  CD2   . TYR B 1 197 ? 22.075  26.291  27.352  1.00 16.31  ? 159 TYR B CD2   1 
ATOM   3201 C  CE1   . TYR B 1 197 ? 22.649  23.650  26.862  1.00 18.35  ? 159 TYR B CE1   1 
ATOM   3202 C  CE2   . TYR B 1 197 ? 23.192  25.727  27.915  1.00 13.11  ? 159 TYR B CE2   1 
ATOM   3203 C  CZ    . TYR B 1 197 ? 23.481  24.418  27.667  1.00 11.37  ? 159 TYR B CZ    1 
ATOM   3204 O  OH    . TYR B 1 197 ? 24.600  23.869  28.254  1.00 23.22  ? 159 TYR B OH    1 
ATOM   3205 N  N     . PHE B 1 198 ? 18.732  24.119  28.167  1.00 25.31  ? 160 PHE B N     1 
ATOM   3206 C  CA    . PHE B 1 198 ? 18.822  23.850  29.594  1.00 20.40  ? 160 PHE B CA    1 
ATOM   3207 C  C     . PHE B 1 198 ? 20.015  22.948  29.867  1.00 21.36  ? 160 PHE B C     1 
ATOM   3208 O  O     . PHE B 1 198 ? 20.277  22.002  29.114  1.00 21.43  ? 160 PHE B O     1 
ATOM   3209 C  CB    . PHE B 1 198 ? 17.556  23.173  30.155  1.00 14.54  ? 160 PHE B CB    1 
ATOM   3210 C  CG    . PHE B 1 198 ? 16.300  23.913  29.873  1.00 25.00  ? 160 PHE B CG    1 
ATOM   3211 C  CD1   . PHE B 1 198 ? 15.694  23.822  28.629  1.00 22.57  ? 160 PHE B CD1   1 
ATOM   3212 C  CD2   . PHE B 1 198 ? 15.707  24.698  30.855  1.00 19.06  ? 160 PHE B CD2   1 
ATOM   3213 C  CE1   . PHE B 1 198 ? 14.519  24.507  28.366  1.00 25.48  ? 160 PHE B CE1   1 
ATOM   3214 C  CE2   . PHE B 1 198 ? 14.537  25.393  30.592  1.00 13.72  ? 160 PHE B CE2   1 
ATOM   3215 C  CZ    . PHE B 1 198 ? 13.942  25.288  29.346  1.00 24.72  ? 160 PHE B CZ    1 
ATOM   3216 N  N     . GLU B 1 199 ? 20.735  23.244  30.950  1.00 21.40  ? 161 GLU B N     1 
ATOM   3217 C  CA    . GLU B 1 199 ? 21.686  22.304  31.525  1.00 20.60  ? 161 GLU B CA    1 
ATOM   3218 C  C     . GLU B 1 199 ? 20.935  21.414  32.505  1.00 25.59  ? 161 GLU B C     1 
ATOM   3219 O  O     . GLU B 1 199 ? 20.226  21.919  33.382  1.00 30.29  ? 161 GLU B O     1 
ATOM   3220 C  CB    . GLU B 1 199 ? 22.821  23.042  32.229  1.00 21.71  ? 161 GLU B CB    1 
ATOM   3221 C  CG    . GLU B 1 199 ? 23.360  24.205  31.417  1.00 27.36  ? 161 GLU B CG    1 
ATOM   3222 C  CD    . GLU B 1 199 ? 24.801  24.527  31.722  1.00 22.21  ? 161 GLU B CD    1 
ATOM   3223 O  OE1   . GLU B 1 199 ? 25.622  24.446  30.791  1.00 30.47  ? 161 GLU B OE1   1 
ATOM   3224 O  OE2   . GLU B 1 199 ? 25.123  24.853  32.886  1.00 35.50  ? 161 GLU B OE2   1 
ATOM   3225 N  N     . THR B 1 200 ? 21.062  20.096  32.341  1.00 15.99  ? 162 THR B N     1 
ATOM   3226 C  CA    . THR B 1 200 ? 20.258  19.153  33.106  1.00 21.48  ? 162 THR B CA    1 
ATOM   3227 C  C     . THR B 1 200 ? 21.152  18.110  33.778  1.00 16.03  ? 162 THR B C     1 
ATOM   3228 O  O     . THR B 1 200 ? 22.341  17.984  33.479  1.00 15.49  ? 162 THR B O     1 
ATOM   3229 C  CB    . THR B 1 200 ? 19.203  18.453  32.223  1.00 22.06  ? 162 THR B CB    1 
ATOM   3230 O  OG1   . THR B 1 200 ? 19.846  17.497  31.393  1.00 13.85  ? 162 THR B OG1   1 
ATOM   3231 C  CG2   . THR B 1 200 ? 18.435  19.431  31.353  1.00 16.64  ? 162 THR B CG2   1 
ATOM   3232 N  N     . SER B 1 201 ? 20.569  17.365  34.715  1.00 14.36  ? 163 SER B N     1 
ATOM   3233 C  CA    . SER B 1 201 ? 21.228  16.204  35.308  1.00 17.32  ? 163 SER B CA    1 
ATOM   3234 C  C     . SER B 1 201 ? 20.170  15.129  35.451  1.00 23.01  ? 163 SER B C     1 
ATOM   3235 O  O     . SER B 1 201 ? 19.115  15.377  36.047  1.00 21.27  ? 163 SER B O     1 
ATOM   3236 C  CB    . SER B 1 201 ? 21.860  16.504  36.678  1.00 21.12  ? 163 SER B CB    1 
ATOM   3237 O  OG    . SER B 1 201 ? 21.950  15.320  37.486  1.00 17.87  ? 163 SER B OG    1 
ATOM   3238 N  N     . ALA B 1 202 ? 20.436  13.948  34.888  1.00 15.06  ? 164 ALA B N     1 
ATOM   3239 C  CA    . ALA B 1 202 ? 19.519  12.838  35.087  1.00 12.69  ? 164 ALA B CA    1 
ATOM   3240 C  C     . ALA B 1 202 ? 19.635  12.216  36.477  1.00 21.18  ? 164 ALA B C     1 
ATOM   3241 O  O     . ALA B 1 202 ? 18.797  11.385  36.842  1.00 20.67  ? 164 ALA B O     1 
ATOM   3242 C  CB    . ALA B 1 202 ? 19.751  11.760  34.029  1.00 11.28  ? 164 ALA B CB    1 
ATOM   3243 N  N     . ALA B 1 203 ? 20.651  12.585  37.251  1.00 16.69  ? 165 ALA B N     1 
ATOM   3244 C  CA    . ALA B 1 203 ? 20.841  11.960  38.549  1.00 16.33  ? 165 ALA B CA    1 
ATOM   3245 C  C     . ALA B 1 203 ? 20.006  12.668  39.616  1.00 15.99  ? 165 ALA B C     1 
ATOM   3246 O  O     . ALA B 1 203 ? 19.199  12.030  40.302  1.00 19.62  ? 165 ALA B O     1 
ATOM   3247 C  CB    . ALA B 1 203 ? 22.328  11.942  38.883  1.00 17.61  ? 165 ALA B CB    1 
ATOM   3248 N  N     . ASN B 1 204 ? 20.104  13.996  39.702  1.00 14.19  ? 166 ASN B N     1 
ATOM   3249 C  CA    . ASN B 1 204 ? 19.349  14.754  40.692  1.00 14.30  ? 166 ASN B CA    1 
ATOM   3250 C  C     . ASN B 1 204 ? 18.112  15.450  40.117  1.00 21.15  ? 166 ASN B C     1 
ATOM   3251 O  O     . ASN B 1 204 ? 17.381  16.109  40.865  1.00 25.28  ? 166 ASN B O     1 
ATOM   3252 C  CB    . ASN B 1 204 ? 20.273  15.759  41.394  1.00 17.95  ? 166 ASN B CB    1 
ATOM   3253 C  CG    . ASN B 1 204 ? 20.834  16.820  40.462  1.00 17.69  ? 166 ASN B CG    1 
ATOM   3254 O  OD1   . ASN B 1 204 ? 20.146  17.312  39.574  1.00 23.30  ? 166 ASN B OD1   1 
ATOM   3255 N  ND2   . ASN B 1 204 ? 22.078  17.216  40.698  1.00 20.95  ? 166 ASN B ND2   1 
ATOM   3256 N  N     . GLY B 1 205 ? 17.850  15.314  38.816  1.00 19.66  ? 167 GLY B N     1 
ATOM   3257 C  CA    . GLY B 1 205 ? 16.638  15.839  38.210  1.00 19.82  ? 167 GLY B CA    1 
ATOM   3258 C  C     . GLY B 1 205 ? 16.673  17.283  37.750  1.00 20.42  ? 167 GLY B C     1 
ATOM   3259 O  O     . GLY B 1 205 ? 15.683  17.747  37.154  1.00 22.49  ? 167 GLY B O     1 
ATOM   3260 N  N     . THR B 1 206 ? 17.762  18.012  38.005  1.00 17.06  ? 168 THR B N     1 
ATOM   3261 C  CA    . THR B 1 206 ? 17.805  19.445  37.725  1.00 16.59  ? 168 THR B CA    1 
ATOM   3262 C  C     . THR B 1 206 ? 17.447  19.719  36.271  1.00 17.99  ? 168 THR B C     1 
ATOM   3263 O  O     . THR B 1 206 ? 18.097  19.207  35.361  1.00 21.33  ? 168 THR B O     1 
ATOM   3264 C  CB    . THR B 1 206 ? 19.198  20.001  38.042  1.00 22.40  ? 168 THR B CB    1 
ATOM   3265 O  OG1   . THR B 1 206 ? 19.649  19.517  39.319  1.00 16.73  ? 168 THR B OG1   1 
ATOM   3266 C  CG2   . THR B 1 206 ? 19.172  21.502  38.088  1.00 14.85  ? 168 THR B CG2   1 
ATOM   3267 N  N     . ASN B 1 207 ? 16.386  20.496  36.063  1.00 17.41  ? 169 ASN B N     1 
ATOM   3268 C  CA    . ASN B 1 207 ? 15.887  20.995  34.787  1.00 25.28  ? 169 ASN B CA    1 
ATOM   3269 C  C     . ASN B 1 207 ? 15.279  19.921  33.899  1.00 20.98  ? 169 ASN B C     1 
ATOM   3270 O  O     . ASN B 1 207 ? 14.834  20.244  32.797  1.00 27.81  ? 169 ASN B O     1 
ATOM   3271 C  CB    . ASN B 1 207 ? 16.966  21.729  33.987  1.00 20.77  ? 169 ASN B CB    1 
ATOM   3272 C  CG    . ASN B 1 207 ? 17.121  23.153  34.417  1.00 18.05  ? 169 ASN B CG    1 
ATOM   3273 O  OD1   . ASN B 1 207 ? 16.140  23.834  34.727  1.00 26.44  ? 169 ASN B OD1   1 
ATOM   3274 N  ND2   . ASN B 1 207 ? 18.354  23.624  34.438  1.00 18.41  ? 169 ASN B ND2   1 
ATOM   3275 N  N     . ILE B 1 208 ? 15.218  18.665  34.349  1.00 21.19  ? 170 ILE B N     1 
ATOM   3276 C  CA    . ILE B 1 208 ? 14.655  17.592  33.534  1.00 19.96  ? 170 ILE B CA    1 
ATOM   3277 C  C     . ILE B 1 208 ? 13.244  17.942  33.076  1.00 25.26  ? 170 ILE B C     1 
ATOM   3278 O  O     . ILE B 1 208 ? 12.967  18.036  31.877  1.00 27.58  ? 170 ILE B O     1 
ATOM   3279 C  CB    . ILE B 1 208 ? 14.675  16.263  34.303  1.00 22.11  ? 170 ILE B CB    1 
ATOM   3280 C  CG1   . ILE B 1 208 ? 16.117  15.857  34.629  1.00 19.43  ? 170 ILE B CG1   1 
ATOM   3281 C  CG2   . ILE B 1 208 ? 14.010  15.214  33.473  1.00 16.36  ? 170 ILE B CG2   1 
ATOM   3282 C  CD1   . ILE B 1 208 ? 16.978  15.551  33.417  1.00 14.33  ? 170 ILE B CD1   1 
ATOM   3283 N  N     . SER B 1 209 ? 12.330  18.154  34.025  1.00 27.08  ? 171 SER B N     1 
ATOM   3284 C  CA    . SER B 1 209 ? 10.952  18.469  33.657  1.00 22.40  ? 171 SER B CA    1 
ATOM   3285 C  C     . SER B 1 209 ? 10.833  19.851  33.021  1.00 24.40  ? 171 SER B C     1 
ATOM   3286 O  O     . SER B 1 209 ? 9.962   20.071  32.168  1.00 25.40  ? 171 SER B O     1 
ATOM   3287 C  CB    . SER B 1 209 ? 10.067  18.386  34.887  1.00 20.70  ? 171 SER B CB    1 
ATOM   3288 O  OG    . SER B 1 209 ? 10.486  19.366  35.799  1.00 28.23  ? 171 SER B OG    1 
ATOM   3289 N  N     . GLN B 1 210 ? 11.667  20.802  33.437  1.00 22.63  ? 172 GLN B N     1 
ATOM   3290 C  CA    . GLN B 1 210 ? 11.629  22.119  32.819  1.00 28.42  ? 172 GLN B CA    1 
ATOM   3291 C  C     . GLN B 1 210 ? 11.893  22.008  31.326  1.00 24.80  ? 172 GLN B C     1 
ATOM   3292 O  O     . GLN B 1 210 ? 11.176  22.592  30.507  1.00 27.17  ? 172 GLN B O     1 
ATOM   3293 C  CB    . GLN B 1 210 ? 12.654  23.047  33.479  1.00 26.15  ? 172 GLN B CB    1 
ATOM   3294 C  CG    . GLN B 1 210 ? 12.173  23.693  34.754  1.00 28.03  ? 172 GLN B CG    1 
ATOM   3295 C  CD    . GLN B 1 210 ? 12.674  22.959  35.981  1.00 29.44  ? 172 GLN B CD    1 
ATOM   3296 O  OE1   . GLN B 1 210 ? 12.645  21.727  36.044  1.00 28.61  ? 172 GLN B OE1   1 
ATOM   3297 N  NE2   . GLN B 1 210 ? 13.165  23.712  36.953  1.00 34.41  ? 172 GLN B NE2   1 
ATOM   3298 N  N     . ALA B 1 211 ? 12.904  21.224  30.956  1.00 17.92  ? 173 ALA B N     1 
ATOM   3299 C  CA    . ALA B 1 211 ? 13.275  21.092  29.556  1.00 22.85  ? 173 ALA B CA    1 
ATOM   3300 C  C     . ALA B 1 211 ? 12.190  20.406  28.737  1.00 27.43  ? 173 ALA B C     1 
ATOM   3301 O  O     . ALA B 1 211 ? 12.030  20.706  27.549  1.00 29.35  ? 173 ALA B O     1 
ATOM   3302 C  CB    . ALA B 1 211 ? 14.587  20.325  29.456  1.00 29.54  ? 173 ALA B CB    1 
ATOM   3303 N  N     . ILE B 1 212 ? 11.436  19.498  29.356  1.00 21.85  ? 174 ILE B N     1 
ATOM   3304 C  CA    . ILE B 1 212 ? 10.439  18.694  28.666  1.00 19.17  ? 174 ILE B CA    1 
ATOM   3305 C  C     . ILE B 1 212 ? 9.115   19.423  28.569  1.00 22.94  ? 174 ILE B C     1 
ATOM   3306 O  O     . ILE B 1 212 ? 8.471   19.410  27.519  1.00 23.89  ? 174 ILE B O     1 
ATOM   3307 C  CB    . ILE B 1 212 ? 10.296  17.356  29.396  1.00 17.05  ? 174 ILE B CB    1 
ATOM   3308 C  CG1   . ILE B 1 212 ? 11.596  16.578  29.262  1.00 22.69  ? 174 ILE B CG1   1 
ATOM   3309 C  CG2   . ILE B 1 212 ? 9.150   16.558  28.834  1.00 19.89  ? 174 ILE B CG2   1 
ATOM   3310 C  CD1   . ILE B 1 212 ? 11.611  15.317  30.072  1.00 22.43  ? 174 ILE B CD1   1 
ATOM   3311 N  N     . GLU B 1 213 ? 8.692   20.040  29.672  1.00 28.07  ? 175 GLU B N     1 
ATOM   3312 C  CA    . GLU B 1 213 ? 7.595   20.995  29.622  1.00 21.91  ? 175 GLU B CA    1 
ATOM   3313 C  C     . GLU B 1 213 ? 7.848   22.061  28.569  1.00 21.58  ? 175 GLU B C     1 
ATOM   3314 O  O     . GLU B 1 213 ? 6.926   22.465  27.852  1.00 31.86  ? 175 GLU B O     1 
ATOM   3315 C  CB    . GLU B 1 213 ? 7.405   21.640  30.995  1.00 23.27  ? 175 GLU B CB    1 
ATOM   3316 C  CG    . GLU B 1 213 ? 6.422   20.921  31.875  1.00 25.63  ? 175 GLU B CG    1 
ATOM   3317 C  CD    . GLU B 1 213 ? 6.858   20.902  33.312  1.00 24.25  ? 175 GLU B CD    1 
ATOM   3318 O  OE1   . GLU B 1 213 ? 7.561   21.836  33.747  1.00 15.73  ? 175 GLU B OE1   1 
ATOM   3319 O  OE2   . GLU B 1 213 ? 6.520   19.924  33.999  1.00 33.01  ? 175 GLU B OE2   1 
ATOM   3320 N  N     . MET B 1 214 ? 9.087   22.545  28.475  1.00 22.14  ? 176 MET B N     1 
ATOM   3321 C  CA    . MET B 1 214 ? 9.432   23.491  27.417  1.00 23.88  ? 176 MET B CA    1 
ATOM   3322 C  C     . MET B 1 214 ? 9.173   22.886  26.049  1.00 23.32  ? 176 MET B C     1 
ATOM   3323 O  O     . MET B 1 214 ? 8.522   23.504  25.201  1.00 28.15  ? 176 MET B O     1 
ATOM   3324 C  CB    . MET B 1 214 ? 10.892  23.924  27.544  1.00 29.96  ? 176 MET B CB    1 
ATOM   3325 C  CG    . MET B 1 214 ? 11.335  24.943  26.518  1.00 20.28  ? 176 MET B CG    1 
ATOM   3326 S  SD    . MET B 1 214 ? 10.093  26.229  26.285  1.00 38.97  ? 176 MET B SD    1 
ATOM   3327 C  CE    . MET B 1 214 ? 11.036  27.716  26.574  1.00 26.10  ? 176 MET B CE    1 
ATOM   3328 N  N     . LEU B 1 215 ? 9.657   21.665  25.819  1.00 27.41  ? 177 LEU B N     1 
ATOM   3329 C  CA    . LEU B 1 215 ? 9.440   21.042  24.518  1.00 32.00  ? 177 LEU B CA    1 
ATOM   3330 C  C     . LEU B 1 215 ? 7.954   20.879  24.242  1.00 29.82  ? 177 LEU B C     1 
ATOM   3331 O  O     . LEU B 1 215 ? 7.471   21.205  23.149  1.00 29.50  ? 177 LEU B O     1 
ATOM   3332 C  CB    . LEU B 1 215 ? 10.161  19.691  24.435  1.00 35.31  ? 177 LEU B CB    1 
ATOM   3333 C  CG    . LEU B 1 215 ? 10.067  19.021  23.044  1.00 25.19  ? 177 LEU B CG    1 
ATOM   3334 C  CD1   . LEU B 1 215 ? 10.413  19.982  21.880  1.00 17.43  ? 177 LEU B CD1   1 
ATOM   3335 C  CD2   . LEU B 1 215 ? 10.909  17.773  22.988  1.00 14.64  ? 177 LEU B CD2   1 
ATOM   3336 N  N     . LEU B 1 216 ? 7.217   20.387  25.236  1.00 26.92  ? 178 LEU B N     1 
ATOM   3337 C  CA    . LEU B 1 216 ? 5.779   20.218  25.105  1.00 26.29  ? 178 LEU B CA    1 
ATOM   3338 C  C     . LEU B 1 216 ? 5.078   21.542  24.850  1.00 27.20  ? 178 LEU B C     1 
ATOM   3339 O  O     . LEU B 1 216 ? 4.089   21.595  24.107  1.00 32.46  ? 178 LEU B O     1 
ATOM   3340 C  CB    . LEU B 1 216 ? 5.236   19.553  26.365  1.00 43.74  ? 178 LEU B CB    1 
ATOM   3341 C  CG    . LEU B 1 216 ? 3.725   19.483  26.549  1.00 43.83  ? 178 LEU B CG    1 
ATOM   3342 C  CD1   . LEU B 1 216 ? 3.168   18.326  25.720  1.00 45.08  ? 178 LEU B CD1   1 
ATOM   3343 C  CD2   . LEU B 1 216 ? 3.426   19.272  28.027  1.00 19.51  ? 178 LEU B CD2   1 
ATOM   3344 N  N     . ASP B 1 217 ? 5.568   22.623  25.457  1.00 29.85  ? 179 ASP B N     1 
ATOM   3345 C  CA    . ASP B 1 217 ? 4.977   23.935  25.200  1.00 35.06  ? 179 ASP B CA    1 
ATOM   3346 C  C     . ASP B 1 217 ? 5.224   24.376  23.759  1.00 30.62  ? 179 ASP B C     1 
ATOM   3347 O  O     . ASP B 1 217 ? 4.377   25.035  23.146  1.00 32.95  ? 179 ASP B O     1 
ATOM   3348 C  CB    . ASP B 1 217 ? 5.538   24.963  26.182  1.00 23.09  ? 179 ASP B CB    1 
ATOM   3349 C  CG    . ASP B 1 217 ? 4.845   26.295  26.078  1.00 34.86  ? 179 ASP B CG    1 
ATOM   3350 O  OD1   . ASP B 1 217 ? 3.609   26.306  25.916  1.00 39.40  ? 179 ASP B OD1   1 
ATOM   3351 O  OD2   . ASP B 1 217 ? 5.531   27.335  26.161  1.00 42.00  ? 179 ASP B OD2   1 
ATOM   3352 N  N     . LEU B 1 218 ? 6.387   24.025  23.211  1.00 33.01  ? 180 LEU B N     1 
ATOM   3353 C  CA    . LEU B 1 218 ? 6.698   24.337  21.823  1.00 28.68  ? 180 LEU B CA    1 
ATOM   3354 C  C     . LEU B 1 218 ? 5.796   23.563  20.867  1.00 33.86  ? 180 LEU B C     1 
ATOM   3355 O  O     . LEU B 1 218 ? 5.278   24.123  19.890  1.00 32.60  ? 180 LEU B O     1 
ATOM   3356 C  CB    . LEU B 1 218 ? 8.162   24.014  21.549  1.00 21.34  ? 180 LEU B CB    1 
ATOM   3357 C  CG    . LEU B 1 218 ? 9.191   25.055  21.930  1.00 18.99  ? 180 LEU B CG    1 
ATOM   3358 C  CD1   . LEU B 1 218 ? 10.530  24.582  21.406  1.00 31.71  ? 180 LEU B CD1   1 
ATOM   3359 C  CD2   . LEU B 1 218 ? 8.822   26.383  21.338  1.00 27.26  ? 180 LEU B CD2   1 
ATOM   3360 N  N     . ILE B 1 219 ? 5.611   22.267  21.130  1.00 29.60  ? 181 ILE B N     1 
ATOM   3361 C  CA    . ILE B 1 219 ? 4.778   21.436  20.269  1.00 21.64  ? 181 ILE B CA    1 
ATOM   3362 C  C     . ILE B 1 219 ? 3.321   21.852  20.373  1.00 27.02  ? 181 ILE B C     1 
ATOM   3363 O  O     . ILE B 1 219 ? 2.580   21.809  19.383  1.00 28.97  ? 181 ILE B O     1 
ATOM   3364 C  CB    . ILE B 1 219 ? 4.964   19.952  20.622  1.00 27.11  ? 181 ILE B CB    1 
ATOM   3365 C  CG1   . ILE B 1 219 ? 6.439   19.587  20.640  1.00 23.05  ? 181 ILE B CG1   1 
ATOM   3366 C  CG2   . ILE B 1 219 ? 4.237   19.053  19.635  1.00 29.95  ? 181 ILE B CG2   1 
ATOM   3367 C  CD1   . ILE B 1 219 ? 6.712   18.248  21.267  1.00 14.74  ? 181 ILE B CD1   1 
ATOM   3368 N  N     . MET B 1 220 ? 2.884   22.259  21.574  1.00 36.74  ? 182 MET B N     1 
ATOM   3369 C  CA    . MET B 1 220 ? 1.478   22.606  21.784  1.00 32.34  ? 182 MET B CA    1 
ATOM   3370 C  C     . MET B 1 220 ? 1.132   23.944  21.152  1.00 26.64  ? 182 MET B C     1 
ATOM   3371 O  O     . MET B 1 220 ? 0.063   24.095  20.558  1.00 37.86  ? 182 MET B O     1 
ATOM   3372 C  CB    . MET B 1 220 ? 1.148   22.638  23.272  1.00 20.62  ? 182 MET B CB    1 
ATOM   3373 C  CG    . MET B 1 220 ? 0.952   21.276  23.895  1.00 31.56  ? 182 MET B CG    1 
ATOM   3374 S  SD    . MET B 1 220 ? -0.578  20.464  23.417  1.00 37.98  ? 182 MET B SD    1 
ATOM   3375 C  CE    . MET B 1 220 ? -1.696  21.862  23.332  1.00 41.13  ? 182 MET B CE    1 
ATOM   3376 N  N     . LYS B 1 221 ? 2.022   24.926  21.271  1.00 31.33  ? 183 LYS B N     1 
ATOM   3377 C  CA    . LYS B 1 221 ? 1.785   26.218  20.649  1.00 38.24  ? 183 LYS B CA    1 
ATOM   3378 C  C     . LYS B 1 221 ? 1.851   26.140  19.132  1.00 44.19  ? 183 LYS B C     1 
ATOM   3379 O  O     . LYS B 1 221 ? 1.353   27.044  18.456  1.00 49.10  ? 183 LYS B O     1 
ATOM   3380 C  CB    . LYS B 1 221 ? 2.787   27.242  21.181  1.00 37.51  ? 183 LYS B CB    1 
ATOM   3381 C  CG    . LYS B 1 221 ? 2.553   27.591  22.654  1.00 47.54  ? 183 LYS B CG    1 
ATOM   3382 C  CD    . LYS B 1 221 ? 3.337   28.815  23.106  1.00 32.56  ? 183 LYS B CD    1 
ATOM   3383 C  CE    . LYS B 1 221 ? 3.004   29.161  24.561  1.00 49.48  ? 183 LYS B CE    1 
ATOM   3384 N  NZ    . LYS B 1 221 ? 3.423   30.547  24.932  1.00 42.56  ? 183 LYS B NZ    1 
ATOM   3385 N  N     . ARG B 1 222 ? 2.438   25.078  18.583  1.00 50.26  ? 184 ARG B N     1 
ATOM   3386 C  CA    . ARG B 1 222 ? 2.496   24.929  17.133  1.00 46.94  ? 184 ARG B CA    1 
ATOM   3387 C  C     . ARG B 1 222 ? 1.148   24.492  16.575  1.00 50.89  ? 184 ARG B C     1 
ATOM   3388 O  O     . ARG B 1 222 ? 0.626   25.113  15.641  1.00 54.98  ? 184 ARG B O     1 
ATOM   3389 C  CB    . ARG B 1 222 ? 3.592   23.932  16.754  1.00 46.32  ? 184 ARG B CB    1 
ATOM   3390 C  CG    . ARG B 1 222 ? 4.039   23.993  15.299  1.00 34.92  ? 184 ARG B CG    1 
ATOM   3391 C  CD    . ARG B 1 222 ? 5.549   24.008  15.218  1.00 34.11  ? 184 ARG B CD    1 
ATOM   3392 N  NE    . ARG B 1 222 ? 6.055   23.428  13.979  1.00 48.45  ? 184 ARG B NE    1 
ATOM   3393 C  CZ    . ARG B 1 222 ? 7.341   23.422  13.629  1.00 46.43  ? 184 ARG B CZ    1 
ATOM   3394 N  NH1   . ARG B 1 222 ? 8.252   23.966  14.424  1.00 40.52  ? 184 ARG B NH1   1 
ATOM   3395 N  NH2   . ARG B 1 222 ? 7.719   22.875  12.484  1.00 46.53  ? 184 ARG B NH2   1 
ATOM   3396 N  N     . MET B 1 223 ? 0.565   23.433  17.150  1.00 45.37  ? 185 MET B N     1 
ATOM   3397 C  CA    . MET B 1 223 ? -0.749  22.966  16.708  1.00 60.12  ? 185 MET B CA    1 
ATOM   3398 C  C     . MET B 1 223 ? -1.806  24.056  16.853  1.00 60.14  ? 185 MET B C     1 
ATOM   3399 O  O     . MET B 1 223 ? -2.702  24.177  16.009  1.00 56.10  ? 185 MET B O     1 
ATOM   3400 C  CB    . MET B 1 223 ? -1.172  21.717  17.495  1.00 46.05  ? 185 MET B CB    1 
ATOM   3401 C  CG    . MET B 1 223 ? -0.179  20.573  17.448  1.00 35.67  ? 185 MET B CG    1 
ATOM   3402 S  SD    . MET B 1 223 ? -0.802  19.102  18.266  1.00 63.83  ? 185 MET B SD    1 
ATOM   3403 C  CE    . MET B 1 223 ? -1.017  17.997  16.870  1.00 53.69  ? 185 MET B CE    1 
ATOM   3404 N  N     . GLU B 1 224 ? -1.713  24.860  17.917  1.00 57.71  ? 186 GLU B N     1 
ATOM   3405 C  CA    . GLU B 1 224 ? -2.711  25.886  18.197  1.00 59.29  ? 186 GLU B CA    1 
ATOM   3406 C  C     . GLU B 1 224 ? -2.777  26.960  17.117  1.00 63.36  ? 186 GLU B C     1 
ATOM   3407 O  O     . GLU B 1 224 ? -3.718  27.766  17.123  1.00 62.29  ? 186 GLU B O     1 
ATOM   3408 C  CB    . GLU B 1 224 ? -2.423  26.526  19.558  1.00 53.89  ? 186 GLU B CB    1 
ATOM   3409 C  CG    . GLU B 1 224 ? -1.488  27.722  19.479  1.00 60.56  ? 186 GLU B CG    1 
ATOM   3410 C  CD    . GLU B 1 224 ? -1.143  28.299  20.838  1.00 68.88  ? 186 GLU B CD    1 
ATOM   3411 O  OE1   . GLU B 1 224 ? -1.602  27.742  21.864  1.00 78.58  ? 186 GLU B OE1   1 
ATOM   3412 O  OE2   . GLU B 1 224 ? -0.406  29.311  20.877  1.00 70.30  ? 186 GLU B OE2   1 
ATOM   3413 N  N     . ARG B 1 225 ? -1.809  26.997  16.198  1.00 66.97  ? 187 ARG B N     1 
ATOM   3414 C  CA    . ARG B 1 225 ? -1.878  27.925  15.076  1.00 63.93  ? 187 ARG B CA    1 
ATOM   3415 C  C     . ARG B 1 225 ? -2.802  27.392  13.987  1.00 65.20  ? 187 ARG B C     1 
ATOM   3416 O  O     . ARG B 1 225 ? -3.724  28.088  13.545  1.00 72.16  ? 187 ARG B O     1 
ATOM   3417 C  CB    . ARG B 1 225 ? -0.471  28.190  14.538  1.00 57.89  ? 187 ARG B CB    1 
ATOM   3418 C  CG    . ARG B 1 225 ? 0.519   28.562  15.638  1.00 54.24  ? 187 ARG B CG    1 
ATOM   3419 C  CD    . ARG B 1 225 ? 1.912   28.923  15.119  1.00 59.03  ? 187 ARG B CD    1 
ATOM   3420 N  NE    . ARG B 1 225 ? 2.815   29.189  16.239  1.00 67.39  ? 187 ARG B NE    1 
ATOM   3421 C  CZ    . ARG B 1 225 ? 3.859   28.431  16.570  1.00 62.46  ? 187 ARG B CZ    1 
ATOM   3422 N  NH1   . ARG B 1 225 ? 4.167   27.360  15.848  1.00 64.80  ? 187 ARG B NH1   1 
ATOM   3423 N  NH2   . ARG B 1 225 ? 4.606   28.751  17.621  1.00 43.67  ? 187 ARG B NH2   1 
ATOM   3424 N  N     . SER B 1 226 ? -2.585  26.151  13.564  1.00 59.55  ? 188 SER B N     1 
ATOM   3425 C  CA    . SER B 1 226 ? -3.436  25.518  12.566  1.00 58.98  ? 188 SER B CA    1 
ATOM   3426 C  C     . SER B 1 226 ? -4.731  24.986  13.184  1.00 62.49  ? 188 SER B C     1 
ATOM   3427 O  O     . SER B 1 226 ? -5.702  25.726  13.360  1.00 66.59  ? 188 SER B O     1 
ATOM   3428 C  CB    . SER B 1 226 ? -2.674  24.388  11.879  1.00 59.23  ? 188 SER B CB    1 
ATOM   3429 O  OG    . SER B 1 226 ? -1.827  23.728  12.804  1.00 56.26  ? 188 SER B OG    1 
HETATM 3430 C  C10   . WT6 C 2 .   ? -7.847  1.787   4.936   0.68 30.39  ? 201 WT6 A C10   1 
HETATM 3431 C  C16   . WT6 C 2 .   ? 0.309   10.058  8.775   0.68 43.67  ? 201 WT6 A C16   1 
HETATM 3432 C  C17   . WT6 C 2 .   ? 0.375   9.135   10.105  0.68 40.13  ? 201 WT6 A C17   1 
HETATM 3433 C  C03   . WT6 C 2 .   ? -1.997  5.396   7.767   0.68 44.40  ? 201 WT6 A C03   1 
HETATM 3434 C  C04   . WT6 C 2 .   ? -3.245  5.752   7.176   0.68 45.23  ? 201 WT6 A C04   1 
HETATM 3435 C  C05   . WT6 C 2 .   ? -4.296  4.841   7.149   0.68 37.86  ? 201 WT6 A C05   1 
HETATM 3436 C  C06   . WT6 C 2 .   ? -4.153  3.559   7.692   0.68 34.10  ? 201 WT6 A C06   1 
HETATM 3437 C  C08   . WT6 C 2 .   ? -6.012  2.498   6.316   0.68 41.73  ? 201 WT6 A C08   1 
HETATM 3438 C  C09   . WT6 C 2 .   ? -7.186  1.579   6.072   0.68 41.43  ? 201 WT6 A C09   1 
HETATM 3439 C  C12   . WT6 C 2 .   ? -2.887  3.190   8.289   0.68 43.62  ? 201 WT6 A C12   1 
HETATM 3440 C  C13   . WT6 C 2 .   ? -1.827  4.113   8.319   0.68 40.36  ? 201 WT6 A C13   1 
HETATM 3441 C  C15   . WT6 C 2 .   ? -0.620  9.519   7.947   0.68 48.69  ? 201 WT6 A C15   1 
HETATM 3442 C  C18   . WT6 C 2 .   ? -0.738  8.379   10.100  0.68 40.67  ? 201 WT6 A C18   1 
HETATM 3443 N  N07   . WT6 C 2 .   ? -5.286  2.622   7.615   0.68 32.37  ? 201 WT6 A N07   1 
HETATM 3444 N  N14   . WT6 C 2 .   ? -1.040  8.144   8.579   0.68 57.04  ? 201 WT6 A N14   1 
HETATM 3445 O  O01   . WT6 C 2 .   ? 0.498   6.038   8.367   0.68 57.36  ? 201 WT6 A O01   1 
HETATM 3446 O  O11   . WT6 C 2 .   ? -5.715  3.116   5.403   0.68 45.06  ? 201 WT6 A O11   1 
HETATM 3447 O  O19   . WT6 C 2 .   ? -0.128  6.900   6.420   0.68 52.92  ? 201 WT6 A O19   1 
HETATM 3448 S  S02   . WT6 C 2 .   ? -0.649  6.621   7.765   0.68 71.07  ? 201 WT6 A S02   1 
HETATM 3449 C  C10   . WT6 D 2 .   ? -8.136  -7.789  2.145   0.79 19.74  ? 202 WT6 A C10   1 
HETATM 3450 C  C16   . WT6 D 2 .   ? -14.781 -5.815  10.982  0.79 73.25  ? 202 WT6 A C16   1 
HETATM 3451 C  C17   . WT6 D 2 .   ? -16.007 -4.890  10.480  0.79 75.03  ? 202 WT6 A C17   1 
HETATM 3452 C  C03   . WT6 D 2 .   ? -11.907 -4.881  7.020   0.79 59.34  ? 202 WT6 A C03   1 
HETATM 3453 C  C04   . WT6 D 2 .   ? -10.740 -5.561  7.465   0.79 56.49  ? 202 WT6 A C04   1 
HETATM 3454 C  C05   . WT6 D 2 .   ? -9.916  -6.200  6.551   0.79 42.92  ? 202 WT6 A C05   1 
HETATM 3455 C  C06   . WT6 D 2 .   ? -10.249 -6.163  5.201   0.79 41.22  ? 202 WT6 A C06   1 
HETATM 3456 C  C08   . WT6 D 2 .   ? -8.239  -7.677  4.508   0.79 39.21  ? 202 WT6 A C08   1 
HETATM 3457 C  C09   . WT6 D 2 .   ? -7.552  -8.174  3.268   0.79 28.17  ? 202 WT6 A C09   1 
HETATM 3458 C  C12   . WT6 D 2 .   ? -11.420 -5.459  4.744   0.79 45.23  ? 202 WT6 A C12   1 
HETATM 3459 C  C13   . WT6 D 2 .   ? -12.242 -4.816  5.664   0.79 52.90  ? 202 WT6 A C13   1 
HETATM 3460 C  C15   . WT6 D 2 .   ? -14.137 -6.210  9.860   0.79 77.61  ? 202 WT6 A C15   1 
HETATM 3461 C  C18   . WT6 D 2 .   ? -15.651 -4.352  9.293   0.79 66.00  ? 202 WT6 A C18   1 
HETATM 3462 N  N07   . WT6 D 2 .   ? -9.395  -6.809  4.220   0.79 37.94  ? 202 WT6 A N07   1 
HETATM 3463 N  N14   . WT6 D 2 .   ? -14.286 -5.010  8.863   0.79 84.42  ? 202 WT6 A N14   1 
HETATM 3464 O  O01   . WT6 D 2 .   ? -12.079 -3.626  9.332   0.79 73.69  ? 202 WT6 A O01   1 
HETATM 3465 O  O11   . WT6 D 2 .   ? -7.871  -7.983  5.552   0.79 30.17  ? 202 WT6 A O11   1 
HETATM 3466 O  O19   . WT6 D 2 .   ? -13.358 -2.774  7.714   0.79 82.27  ? 202 WT6 A O19   1 
HETATM 3467 S  S02   . WT6 D 2 .   ? -12.921 -4.050  8.258   0.79 96.53  ? 202 WT6 A S02   1 
HETATM 3468 P  PG    . GNP E 3 .   ? 14.501  -9.325  -1.684  1.00 16.77  ? 203 GNP A PG    1 
HETATM 3469 O  O1G   . GNP E 3 .   ? 14.579  -7.921  -2.209  1.00 23.63  ? 203 GNP A O1G   1 
HETATM 3470 O  O2G   . GNP E 3 .   ? 15.896  -9.909  -1.420  1.00 21.71  ? 203 GNP A O2G   1 
HETATM 3471 O  O3G   . GNP E 3 .   ? 13.735  -9.270  -0.345  1.00 12.73  ? 203 GNP A O3G   1 
HETATM 3472 N  N3B   . GNP E 3 .   ? 13.708  -10.321 -2.833  1.00 19.95  ? 203 GNP A N3B   1 
HETATM 3473 P  PB    . GNP E 3 .   ? 12.593  -9.770  -3.907  1.00 17.51  ? 203 GNP A PB    1 
HETATM 3474 O  O1B   . GNP E 3 .   ? 11.238  -10.249 -3.498  1.00 15.33  ? 203 GNP A O1B   1 
HETATM 3475 O  O2B   . GNP E 3 .   ? 12.610  -8.267  -3.990  1.00 18.86  ? 203 GNP A O2B   1 
HETATM 3476 O  O3A   . GNP E 3 .   ? 12.841  -10.454 -5.382  1.00 21.37  ? 203 GNP A O3A   1 
HETATM 3477 P  PA    . GNP E 3 .   ? 13.352  -9.642  -6.635  1.00 17.01  ? 203 GNP A PA    1 
HETATM 3478 O  O1A   . GNP E 3 .   ? 14.464  -8.731  -6.122  1.00 25.70  ? 203 GNP A O1A   1 
HETATM 3479 O  O2A   . GNP E 3 .   ? 12.240  -8.983  -7.391  1.00 20.71  ? 203 GNP A O2A   1 
HETATM 3480 O  "O5'" . GNP E 3 .   ? 14.095  -10.722 -7.488  1.00 28.39  ? 203 GNP A "O5'" 1 
HETATM 3481 C  "C5'" . GNP E 3 .   ? 13.660  -12.094 -7.495  1.00 17.22  ? 203 GNP A "C5'" 1 
HETATM 3482 C  "C4'" . GNP E 3 .   ? 14.461  -12.865 -8.505  1.00 11.69  ? 203 GNP A "C4'" 1 
HETATM 3483 O  "O4'" . GNP E 3 .   ? 13.538  -13.642 -9.282  1.00 17.96  ? 203 GNP A "O4'" 1 
HETATM 3484 C  "C3'" . GNP E 3 .   ? 15.194  -12.025 -9.539  1.00 17.74  ? 203 GNP A "C3'" 1 
HETATM 3485 O  "O3'" . GNP E 3 .   ? 16.117  -12.801 -10.294 1.00 21.43  ? 203 GNP A "O3'" 1 
HETATM 3486 C  "C2'" . GNP E 3 .   ? 14.057  -11.648 -10.474 1.00 18.22  ? 203 GNP A "C2'" 1 
HETATM 3487 O  "O2'" . GNP E 3 .   ? 14.577  -11.335 -11.758 1.00 19.59  ? 203 GNP A "O2'" 1 
HETATM 3488 C  "C1'" . GNP E 3 .   ? 13.248  -12.950 -10.483 1.00 16.74  ? 203 GNP A "C1'" 1 
HETATM 3489 N  N9    . GNP E 3 .   ? 11.807  -12.717 -10.543 1.00 14.70  ? 203 GNP A N9    1 
HETATM 3490 C  C8    . GNP E 3 .   ? 11.047  -11.885 -9.775  1.00 13.90  ? 203 GNP A C8    1 
HETATM 3491 N  N7    . GNP E 3 .   ? 9.781   -11.888 -10.124 1.00 16.24  ? 203 GNP A N7    1 
HETATM 3492 C  C5    . GNP E 3 .   ? 9.727   -12.754 -11.195 1.00 8.67   ? 203 GNP A C5    1 
HETATM 3493 C  C6    . GNP E 3 .   ? 8.616   -13.182 -12.017 1.00 15.37  ? 203 GNP A C6    1 
HETATM 3494 O  O6    . GNP E 3 .   ? 7.444   -12.841 -11.902 1.00 15.89  ? 203 GNP A O6    1 
HETATM 3495 N  N1    . GNP E 3 .   ? 9.012   -14.074 -12.997 1.00 14.19  ? 203 GNP A N1    1 
HETATM 3496 C  C2    . GNP E 3 .   ? 10.297  -14.518 -13.190 1.00 19.23  ? 203 GNP A C2    1 
HETATM 3497 N  N2    . GNP E 3 .   ? 10.503  -15.387 -14.180 1.00 21.19  ? 203 GNP A N2    1 
HETATM 3498 N  N3    . GNP E 3 .   ? 11.316  -14.140 -12.427 1.00 19.35  ? 203 GNP A N3    1 
HETATM 3499 C  C4    . GNP E 3 .   ? 10.961  -13.280 -11.462 1.00 16.36  ? 203 GNP A C4    1 
HETATM 3500 C  C1    . GOL F 4 .   ? 14.803  -14.859 -15.670 1.00 28.07  ? 204 GOL A C1    1 
HETATM 3501 O  O1    . GOL F 4 .   ? 15.460  -16.090 -15.781 1.00 29.69  ? 204 GOL A O1    1 
HETATM 3502 C  C2    . GOL F 4 .   ? 14.114  -14.868 -14.293 1.00 29.13  ? 204 GOL A C2    1 
HETATM 3503 O  O2    . GOL F 4 .   ? 14.955  -14.457 -13.240 1.00 29.89  ? 204 GOL A O2    1 
HETATM 3504 C  C3    . GOL F 4 .   ? 13.671  -16.324 -14.175 1.00 27.20  ? 204 GOL A C3    1 
HETATM 3505 O  O3    . GOL F 4 .   ? 12.685  -16.430 -15.138 1.00 28.38  ? 204 GOL A O3    1 
HETATM 3506 MG MG    . MG  G 5 .   ? 13.641  -6.687  -3.324  1.00 21.11  ? 205 MG  A MG    1 
HETATM 3507 C  C10   . WT6 H 2 .   ? 7.655   16.953  12.985  1.00 29.92  ? 201 WT6 B C10   1 
HETATM 3508 C  C16   . WT6 H 2 .   ? -2.109  12.641  11.399  1.00 50.07  ? 201 WT6 B C16   1 
HETATM 3509 C  C17   . WT6 H 2 .   ? -3.002  11.891  12.522  0.98 59.56  ? 201 WT6 B C17   1 
HETATM 3510 C  C03   . WT6 H 2 .   ? 1.685   12.942  14.220  0.55 43.54  ? 201 WT6 B C03   1 
HETATM 3511 C  C04   . WT6 H 2 .   ? 1.593   14.366  14.222  0.70 41.16  ? 201 WT6 B C04   1 
HETATM 3512 C  C05   . WT6 H 2 .   ? 2.715   15.145  13.974  1.00 32.69  ? 201 WT6 B C05   1 
HETATM 3513 C  C06   . WT6 H 2 .   ? 3.954   14.548  13.739  0.93 30.94  ? 201 WT6 B C06   1 
HETATM 3514 C  C08   . WT6 H 2 .   ? 5.320   16.786  13.892  0.34 33.14  ? 201 WT6 B C08   1 
HETATM 3515 C  C09   . WT6 H 2 .   ? 6.597   17.540  13.543  0.86 29.74  ? 201 WT6 B C09   1 
HETATM 3516 C  C12   . WT6 H 2 .   ? 4.050   13.105  13.734  1.00 31.72  ? 201 WT6 B C12   1 
HETATM 3517 C  C13   . WT6 H 2 .   ? 2.922   12.319  13.975  1.00 35.80  ? 201 WT6 B C13   1 
HETATM 3518 C  C15   . WT6 H 2 .   ? -0.838  12.668  11.869  1.00 50.91  ? 201 WT6 B C15   1 
HETATM 3519 C  C18   . WT6 H 2 .   ? -2.182  10.995  13.111  1.00 42.34  ? 201 WT6 B C18   1 
HETATM 3520 N  N07   . WT6 H 2 .   ? 5.146   15.376  13.468  0.49 31.39  ? 201 WT6 B N07   1 
HETATM 3521 N  N14   . WT6 H 2 .   ? -0.768  11.680  13.089  0.65 46.41  ? 201 WT6 B N14   1 
HETATM 3522 O  O01   . WT6 H 2 .   ? -0.625  12.629  15.556  1.00 37.38  ? 201 WT6 B O01   1 
HETATM 3523 O  O11   . WT6 H 2 .   ? 4.508   17.344  14.488  0.62 35.54  ? 201 WT6 B O11   1 
HETATM 3524 O  O19   . WT6 H 2 .   ? 0.495   10.740  15.229  0.83 40.26  ? 201 WT6 B O19   1 
HETATM 3525 S  S02   . WT6 H 2 .   ? 0.175   11.983  14.558  0.10 40.28  ? 201 WT6 B S02   1 
HETATM 3526 P  PG    . GNP I 3 .   ? 22.902  5.300   24.302  1.00 18.81  ? 202 GNP B PG    1 
HETATM 3527 O  O1G   . GNP I 3 .   ? 21.767  4.430   24.749  1.00 15.61  ? 202 GNP B O1G   1 
HETATM 3528 O  O2G   . GNP I 3 .   ? 24.066  4.435   23.873  1.00 21.66  ? 202 GNP B O2G   1 
HETATM 3529 O  O3G   . GNP I 3 .   ? 22.420  6.212   23.130  1.00 20.22  ? 202 GNP B O3G   1 
HETATM 3530 N  N3B   . GNP I 3 .   ? 23.488  6.305   25.549  1.00 17.82  ? 202 GNP B N3B   1 
HETATM 3531 P  PB    . GNP I 3 .   ? 22.462  7.208   26.441  1.00 22.06  ? 202 GNP B PB    1 
HETATM 3532 O  O1B   . GNP I 3 .   ? 21.134  6.509   26.401  1.00 17.43  ? 202 GNP B O1B   1 
HETATM 3533 O  O2B   . GNP I 3 .   ? 22.339  8.601   25.912  1.00 19.69  ? 202 GNP B O2B   1 
HETATM 3534 O  O3A   . GNP I 3 .   ? 23.081  7.340   27.963  1.00 20.28  ? 202 GNP B O3A   1 
HETATM 3535 P  PA    . GNP I 3 .   ? 22.617  6.639   29.313  1.00 20.00  ? 202 GNP B PA    1 
HETATM 3536 O  O1A   . GNP I 3 .   ? 22.578  5.127   29.091  1.00 11.99  ? 202 GNP B O1A   1 
HETATM 3537 O  O2A   . GNP I 3 .   ? 21.394  7.240   29.859  1.00 17.31  ? 202 GNP B O2A   1 
HETATM 3538 O  "O5'" . GNP I 3 .   ? 23.754  7.076   30.305  1.00 17.43  ? 202 GNP B "O5'" 1 
HETATM 3539 C  "C5'" . GNP I 3 .   ? 25.152  6.917   29.983  1.00 22.68  ? 202 GNP B "C5'" 1 
HETATM 3540 C  "C4'" . GNP I 3 .   ? 25.965  6.861   31.267  1.00 14.59  ? 202 GNP B "C4'" 1 
HETATM 3541 O  "O4'" . GNP I 3 .   ? 26.043  8.176   31.866  1.00 10.41  ? 202 GNP B "O4'" 1 
HETATM 3542 C  "C3'" . GNP I 3 .   ? 25.428  5.942   32.362  1.00 20.68  ? 202 GNP B "C3'" 1 
HETATM 3543 O  "O3'" . GNP I 3 .   ? 26.524  5.339   33.037  1.00 20.79  ? 202 GNP B "O3'" 1 
HETATM 3544 C  "C2'" . GNP I 3 .   ? 24.622  6.908   33.237  1.00 16.42  ? 202 GNP B "C2'" 1 
HETATM 3545 O  "O2'" . GNP I 3 .   ? 24.462  6.520   34.594  1.00 17.61  ? 202 GNP B "O2'" 1 
HETATM 3546 C  "C1'" . GNP I 3 .   ? 25.503  8.152   33.173  1.00 17.28  ? 202 GNP B "C1'" 1 
HETATM 3547 N  N9    . GNP I 3 .   ? 24.746  9.394   33.369  1.00 16.32  ? 202 GNP B N9    1 
HETATM 3548 C  C8    . GNP I 3 .   ? 23.693  9.803   32.613  1.00 15.22  ? 202 GNP B C8    1 
HETATM 3549 N  N7    . GNP I 3 .   ? 23.215  10.965  32.992  1.00 18.79  ? 202 GNP B N7    1 
HETATM 3550 C  C5    . GNP I 3 .   ? 24.016  11.326  34.048  1.00 11.68  ? 202 GNP B C5    1 
HETATM 3551 C  C6    . GNP I 3 .   ? 23.985  12.511  34.891  1.00 17.46  ? 202 GNP B C6    1 
HETATM 3552 O  O6    . GNP I 3 .   ? 23.200  13.437  34.799  1.00 15.72  ? 202 GNP B O6    1 
HETATM 3553 N  N1    . GNP I 3 .   ? 24.964  12.482  35.855  1.00 15.96  ? 202 GNP B N1    1 
HETATM 3554 C  C2    . GNP I 3 .   ? 25.874  11.472  36.027  1.00 20.23  ? 202 GNP B C2    1 
HETATM 3555 N  N2    . GNP I 3 .   ? 26.763  11.610  37.008  1.00 30.03  ? 202 GNP B N2    1 
HETATM 3556 N  N3    . GNP I 3 .   ? 25.909  10.387  35.247  1.00 24.83  ? 202 GNP B N3    1 
HETATM 3557 C  C4    . GNP I 3 .   ? 24.961  10.384  34.312  1.00 17.61  ? 202 GNP B C4    1 
HETATM 3558 C  C10   . WT6 J 2 .   ? 14.330  24.584  15.927  0.87 38.68  ? 203 WT6 B C10   1 
HETATM 3559 C  C16   . WT6 J 2 .   ? 6.821   26.192  10.419  0.87 53.30  ? 203 WT6 B C16   1 
HETATM 3560 C  C17   . WT6 J 2 .   ? 6.231   27.699  10.376  0.87 59.39  ? 203 WT6 B C17   1 
HETATM 3561 C  C03   . WT6 J 2 .   ? 9.809   27.126  14.292  0.87 55.86  ? 203 WT6 B C03   1 
HETATM 3562 C  C04   . WT6 J 2 .   ? 11.183  26.738  13.910  0.87 63.41  ? 203 WT6 B C04   1 
HETATM 3563 C  C05   . WT6 J 2 .   ? 12.042  26.643  15.015  0.87 56.38  ? 203 WT6 B C05   1 
HETATM 3564 C  C06   . WT6 J 2 .   ? 11.575  26.904  16.320  0.87 58.46  ? 203 WT6 B C06   1 
HETATM 3565 C  C08   . WT6 J 2 .   ? 13.215  25.556  17.898  0.87 37.42  ? 203 WT6 B C08   1 
HETATM 3566 C  C09   . WT6 J 2 .   ? 13.376  24.470  16.859  0.87 42.78  ? 203 WT6 B C09   1 
HETATM 3567 C  C12   . WT6 J 2 .   ? 10.253  27.232  16.685  0.87 51.96  ? 203 WT6 B C12   1 
HETATM 3568 C  C13   . WT6 J 2 .   ? 9.385   27.345  15.644  0.87 52.80  ? 203 WT6 B C13   1 
HETATM 3569 C  C15   . WT6 J 2 .   ? 8.165   26.384  10.514  0.87 51.12  ? 203 WT6 B C15   1 
HETATM 3570 C  C18   . WT6 J 2 .   ? 7.208   28.486  10.902  0.87 62.08  ? 203 WT6 B C18   1 
HETATM 3571 N  N07   . WT6 J 2 .   ? 12.361  26.745  17.541  0.87 43.94  ? 203 WT6 B N07   1 
HETATM 3572 N  N14   . WT6 J 2 .   ? 8.273   27.554  11.539  0.87 71.70  ? 203 WT6 B N14   1 
HETATM 3573 O  O01   . WT6 J 2 .   ? 7.429   26.365  13.671  0.87 65.83  ? 203 WT6 B O01   1 
HETATM 3574 O  O11   . WT6 J 2 .   ? 13.792  25.452  18.904  0.87 40.64  ? 203 WT6 B O11   1 
HETATM 3575 O  O19   . WT6 J 2 .   ? 7.762   28.577  13.943  0.87 71.78  ? 203 WT6 B O19   1 
HETATM 3576 S  S02   . WT6 J 2 .   ? 8.319   27.402  13.298  0.87 82.77  ? 203 WT6 B S02   1 
HETATM 3577 C  C1    . GOL K 4 .   ? 31.520  15.914  41.480  1.00 30.46  ? 204 GOL B C1    1 
HETATM 3578 O  O1    . GOL K 4 .   ? 31.468  16.536  40.217  1.00 39.33  ? 204 GOL B O1    1 
HETATM 3579 C  C2    . GOL K 4 .   ? 30.686  16.770  42.501  1.00 24.69  ? 204 GOL B C2    1 
HETATM 3580 O  O2    . GOL K 4 .   ? 30.858  18.145  42.330  1.00 48.55  ? 204 GOL B O2    1 
HETATM 3581 C  C3    . GOL K 4 .   ? 29.221  16.382  42.297  1.00 27.63  ? 204 GOL B C3    1 
HETATM 3582 O  O3    . GOL K 4 .   ? 29.098  15.001  42.397  1.00 20.81  ? 204 GOL B O3    1 
HETATM 3583 C  C1    . GOL L 4 .   ? 29.693  2.258   16.625  1.00 28.51  ? 205 GOL B C1    1 
HETATM 3584 O  O1    . GOL L 4 .   ? 29.563  1.458   17.739  1.00 36.51  ? 205 GOL B O1    1 
HETATM 3585 C  C2    . GOL L 4 .   ? 28.961  1.465   15.617  1.00 26.34  ? 205 GOL B C2    1 
HETATM 3586 O  O2    . GOL L 4 .   ? 27.633  1.725   15.702  1.00 29.65  ? 205 GOL B O2    1 
HETATM 3587 C  C3    . GOL L 4 .   ? 29.605  1.812   14.255  1.00 35.23  ? 205 GOL B C3    1 
HETATM 3588 O  O3    . GOL L 4 .   ? 29.491  0.653   13.464  1.00 42.08  ? 205 GOL B O3    1 
HETATM 3589 MG MG    . MG  M 5 .   ? 20.283  4.759   26.097  1.00 8.29   ? 206 MG  B MG    1 
HETATM 3590 O  O     . HOH N 6 .   ? 3.198   15.171  4.751   1.00 23.38  ? 301 HOH A O     1 
HETATM 3591 O  O     . HOH N 6 .   ? -0.230  -14.939 -13.500 1.00 15.30  ? 302 HOH A O     1 
HETATM 3592 O  O     . HOH N 6 .   ? 15.365  -7.082  -4.904  1.00 15.28  ? 303 HOH A O     1 
HETATM 3593 O  O     . HOH N 6 .   ? -8.969  -8.965  8.331   1.00 32.19  ? 304 HOH A O     1 
HETATM 3594 O  O     . HOH N 6 .   ? -17.854 1.323   -10.846 1.00 42.87  ? 305 HOH A O     1 
HETATM 3595 O  O     . HOH N 6 .   ? -14.496 7.627   -7.310  1.00 25.82  ? 306 HOH A O     1 
HETATM 3596 O  O     . HOH N 6 .   ? 12.159  -6.204  -1.841  1.00 19.57  ? 307 HOH A O     1 
HETATM 3597 O  O     . HOH N 6 .   ? -8.148  0.926   -7.115  1.00 25.50  ? 308 HOH A O     1 
HETATM 3598 O  O     . HOH N 6 .   ? 18.349  -7.855  0.829   1.00 10.29  ? 309 HOH A O     1 
HETATM 3599 O  O     . HOH N 6 .   ? -3.093  -8.961  -16.578 1.00 15.36  ? 310 HOH A O     1 
HETATM 3600 O  O     . HOH N 6 .   ? 6.788   -15.061 0.899   1.00 15.77  ? 311 HOH A O     1 
HETATM 3601 O  O     . HOH N 6 .   ? -5.155  -22.981 7.008   1.00 16.96  ? 312 HOH A O     1 
HETATM 3602 O  O     . HOH N 6 .   ? -11.980 4.101   -15.744 1.00 24.64  ? 313 HOH A O     1 
HETATM 3603 O  O     . HOH N 6 .   ? 17.992  1.452   1.048   1.00 23.01  ? 314 HOH A O     1 
HETATM 3604 O  O     . HOH N 6 .   ? 4.658   -20.554 -11.848 1.00 15.45  ? 315 HOH A O     1 
HETATM 3605 O  O     . HOH N 6 .   ? 0.571   6.620   14.103  1.00 33.54  ? 316 HOH A O     1 
HETATM 3606 O  O     . HOH N 6 .   ? 1.189   -6.935  -18.867 1.00 25.44  ? 317 HOH A O     1 
HETATM 3607 O  O     . HOH N 6 .   ? -0.328  -0.052  9.535   1.00 26.38  ? 318 HOH A O     1 
HETATM 3608 O  O     . HOH N 6 .   ? -6.940  -11.884 -12.587 1.00 23.11  ? 319 HOH A O     1 
HETATM 3609 O  O     . HOH N 6 .   ? -12.295 0.934   -7.733  1.00 27.94  ? 320 HOH A O     1 
HETATM 3610 O  O     . HOH N 6 .   ? 16.432  -7.598  -8.598  1.00 18.74  ? 321 HOH A O     1 
HETATM 3611 O  O     . HOH N 6 .   ? -4.800  -1.631  6.416   1.00 32.00  ? 322 HOH A O     1 
HETATM 3612 O  O     . HOH N 6 .   ? 14.211  2.222   -16.195 1.00 30.95  ? 323 HOH A O     1 
HETATM 3613 O  O     . HOH N 6 .   ? -14.517 11.178  -13.585 1.00 30.62  ? 324 HOH A O     1 
HETATM 3614 O  O     . HOH N 6 .   ? -9.386  -17.319 -2.182  1.00 11.68  ? 325 HOH A O     1 
HETATM 3615 O  O     . HOH N 6 .   ? -12.203 -2.609  2.403   1.00 20.86  ? 326 HOH A O     1 
HETATM 3616 O  O     . HOH N 6 .   ? -9.915  -15.225 -1.122  1.00 18.90  ? 327 HOH A O     1 
HETATM 3617 O  O     . HOH N 6 .   ? -5.119  4.943   -13.008 1.00 12.65  ? 328 HOH A O     1 
HETATM 3618 O  O     . HOH N 6 .   ? 7.665   -13.988 9.361   1.00 22.68  ? 329 HOH A O     1 
HETATM 3619 O  O     . HOH N 6 .   ? -1.279  10.539  3.506   1.00 21.23  ? 330 HOH A O     1 
HETATM 3620 O  O     . HOH N 6 .   ? -9.818  2.951   -10.194 1.00 19.52  ? 331 HOH A O     1 
HETATM 3621 O  O     . HOH N 6 .   ? -9.511  -13.306 -6.350  1.00 29.64  ? 332 HOH A O     1 
HETATM 3622 O  O     . HOH N 6 .   ? 20.076  -11.852 -1.505  1.00 18.41  ? 333 HOH A O     1 
HETATM 3623 O  O     . HOH N 6 .   ? -5.045  -15.529 -10.513 1.00 25.26  ? 334 HOH A O     1 
HETATM 3624 O  O     . HOH N 6 .   ? 16.460  0.821   -18.617 1.00 14.16  ? 335 HOH A O     1 
HETATM 3625 O  O     . HOH N 6 .   ? -18.257 6.454   -17.197 1.00 24.49  ? 336 HOH A O     1 
HETATM 3626 O  O     . HOH N 6 .   ? -15.386 1.075   -11.444 1.00 33.27  ? 337 HOH A O     1 
HETATM 3627 O  O     . HOH N 6 .   ? -10.614 -22.944 -1.256  1.00 17.80  ? 338 HOH A O     1 
HETATM 3628 O  O     . HOH N 6 .   ? -2.031  -4.650  -16.382 1.00 26.19  ? 339 HOH A O     1 
HETATM 3629 O  O     . HOH N 6 .   ? -7.483  -9.652  -12.313 1.00 24.37  ? 340 HOH A O     1 
HETATM 3630 O  O     . HOH N 6 .   ? 2.166   -21.374 -12.980 1.00 24.00  ? 341 HOH A O     1 
HETATM 3631 O  O     . HOH N 6 .   ? 14.718  2.598   -12.036 1.00 25.23  ? 342 HOH A O     1 
HETATM 3632 O  O     . HOH N 6 .   ? 18.853  -2.556  12.771  1.00 17.08  ? 343 HOH A O     1 
HETATM 3633 O  O     . HOH N 6 .   ? -19.055 10.551  -7.825  1.00 26.84  ? 344 HOH A O     1 
HETATM 3634 O  O     . HOH N 6 .   ? 1.601   10.726  4.933   1.00 25.76  ? 345 HOH A O     1 
HETATM 3635 O  O     . HOH N 6 .   ? -8.839  -23.572 4.415   1.00 14.78  ? 346 HOH A O     1 
HETATM 3636 O  O     . HOH N 6 .   ? -12.563 -21.164 -2.242  1.00 16.66  ? 347 HOH A O     1 
HETATM 3637 O  O     . HOH N 6 .   ? -11.556 -3.540  -7.471  1.00 18.70  ? 348 HOH A O     1 
HETATM 3638 O  O     . HOH N 6 .   ? -15.217 -20.921 -0.671  1.00 16.81  ? 349 HOH A O     1 
HETATM 3639 O  O     . HOH N 6 .   ? -15.861 16.356  -5.027  1.00 30.07  ? 350 HOH A O     1 
HETATM 3640 O  O     . HOH N 6 .   ? 18.979  -14.470 -1.005  1.00 19.03  ? 351 HOH A O     1 
HETATM 3641 O  O     . HOH N 6 .   ? 7.838   5.735   -15.753 1.00 24.71  ? 352 HOH A O     1 
HETATM 3642 O  O     . HOH N 6 .   ? 7.950   -22.255 -18.461 1.00 27.71  ? 353 HOH A O     1 
HETATM 3643 O  O     . HOH N 6 .   ? -12.753 -14.741 6.960   1.00 23.42  ? 354 HOH A O     1 
HETATM 3644 O  O     . HOH N 6 .   ? -12.408 -21.285 4.678   1.00 17.78  ? 355 HOH A O     1 
HETATM 3645 O  O     . HOH N 6 .   ? -10.633 3.264   -12.802 1.00 18.64  ? 356 HOH A O     1 
HETATM 3646 O  O     . HOH N 6 .   ? 14.759  -1.402  -10.598 1.00 28.52  ? 357 HOH A O     1 
HETATM 3647 O  O     . HOH N 6 .   ? -6.245  2.972   -14.705 1.00 30.15  ? 358 HOH A O     1 
HETATM 3648 O  O     . HOH N 6 .   ? -6.626  -17.198 -8.432  1.00 34.00  ? 359 HOH A O     1 
HETATM 3649 O  O     . HOH N 6 .   ? 15.239  -5.167  -9.984  1.00 23.90  ? 360 HOH A O     1 
HETATM 3650 O  O     . HOH N 6 .   ? -7.194  -10.373 -17.897 1.00 15.80  ? 361 HOH A O     1 
HETATM 3651 O  O     . HOH N 6 .   ? -9.634  -16.513 -4.856  1.00 16.46  ? 362 HOH A O     1 
HETATM 3652 O  O     . HOH N 6 .   ? 16.888  1.040   -8.310  1.00 17.98  ? 363 HOH A O     1 
HETATM 3653 O  O     . HOH N 6 .   ? 18.814  19.802  3.189   1.00 24.28  ? 364 HOH A O     1 
HETATM 3654 O  O     . HOH N 6 .   ? 22.390  -11.568 -3.178  1.00 9.31   ? 365 HOH A O     1 
HETATM 3655 O  O     . HOH N 6 .   ? -6.311  -26.678 2.212   1.00 25.37  ? 366 HOH A O     1 
HETATM 3656 O  O     . HOH N 6 .   ? -10.800 -12.071 -9.390  1.00 15.83  ? 367 HOH A O     1 
HETATM 3657 O  O     . HOH N 6 .   ? -11.589 -11.632 -11.732 1.00 29.91  ? 368 HOH A O     1 
HETATM 3658 O  O     . HOH O 6 .   ? 15.182  27.492  15.770  1.00 27.29  ? 301 HOH B O     1 
HETATM 3659 O  O     . HOH O 6 .   ? 13.843  21.802  8.576   1.00 25.87  ? 302 HOH B O     1 
HETATM 3660 O  O     . HOH O 6 .   ? 19.346  5.679   24.437  1.00 18.49  ? 303 HOH B O     1 
HETATM 3661 O  O     . HOH O 6 .   ? 25.212  14.616  21.548  1.00 19.66  ? 304 HOH B O     1 
HETATM 3662 O  O     . HOH O 6 .   ? 35.426  15.647  31.209  1.00 11.12  ? 305 HOH B O     1 
HETATM 3663 O  O     . HOH O 6 .   ? 5.938   26.525  19.097  1.00 39.95  ? 306 HOH B O     1 
HETATM 3664 O  O     . HOH O 6 .   ? -0.048  8.654   16.727  1.00 20.48  ? 307 HOH B O     1 
HETATM 3665 O  O     . HOH O 6 .   ? 28.025  21.631  17.970  1.00 28.98  ? 308 HOH B O     1 
HETATM 3666 O  O     . HOH O 6 .   ? 31.498  22.014  15.115  1.00 34.03  ? 309 HOH B O     1 
HETATM 3667 O  O     . HOH O 6 .   ? 9.654   14.826  13.449  1.00 32.34  ? 310 HOH B O     1 
HETATM 3668 O  O     . HOH O 6 .   ? 5.776   20.365  16.491  1.00 33.54  ? 311 HOH B O     1 
HETATM 3669 O  O     . HOH O 6 .   ? 21.130  3.636   27.418  1.00 16.35  ? 312 HOH B O     1 
HETATM 3670 O  O     . HOH O 6 .   ? 5.963   15.629  10.888  1.00 33.42  ? 313 HOH B O     1 
HETATM 3671 O  O     . HOH O 6 .   ? 27.578  0.658   11.484  1.00 25.47  ? 314 HOH B O     1 
HETATM 3672 O  O     . HOH O 6 .   ? 22.038  3.429   31.191  1.00 20.90  ? 315 HOH B O     1 
HETATM 3673 O  O     . HOH O 6 .   ? 24.579  14.736  9.193   1.00 23.02  ? 316 HOH B O     1 
HETATM 3674 O  O     . HOH O 6 .   ? 6.184   20.531  13.739  1.00 31.48  ? 317 HOH B O     1 
HETATM 3675 O  O     . HOH O 6 .   ? 20.503  0.919   11.967  1.00 23.34  ? 318 HOH B O     1 
HETATM 3676 O  O     . HOH O 6 .   ? 21.450  11.553  6.012   1.00 26.86  ? 319 HOH B O     1 
HETATM 3677 O  O     . HOH O 6 .   ? 28.164  8.874   37.006  1.00 21.06  ? 320 HOH B O     1 
HETATM 3678 O  O     . HOH O 6 .   ? 23.136  20.119  39.075  1.00 18.72  ? 321 HOH B O     1 
HETATM 3679 O  O     . HOH O 6 .   ? 31.636  19.216  11.721  1.00 22.21  ? 322 HOH B O     1 
HETATM 3680 O  O     . HOH O 6 .   ? 15.581  23.895  13.263  1.00 34.19  ? 323 HOH B O     1 
HETATM 3681 O  O     . HOH O 6 .   ? 27.770  8.321   18.997  1.00 14.32  ? 324 HOH B O     1 
HETATM 3682 O  O     . HOH O 6 .   ? 24.712  12.701  13.927  1.00 17.05  ? 325 HOH B O     1 
HETATM 3683 O  O     . HOH O 6 .   ? 28.941  9.688   33.364  1.00 20.68  ? 326 HOH B O     1 
HETATM 3684 O  O     . HOH O 6 .   ? 34.203  17.725  15.538  1.00 23.84  ? 327 HOH B O     1 
HETATM 3685 O  O     . HOH O 6 .   ? 30.140  5.903   25.802  1.00 16.85  ? 328 HOH B O     1 
HETATM 3686 O  O     . HOH O 6 .   ? 12.738  -11.221 13.926  1.00 26.27  ? 329 HOH B O     1 
# 
