data_9FGI
# 
_entry.id   9FGI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9FGI         pdb_00009fgi 10.2210/pdb9fgi/pdb 
WWPDB D_1292133404 ?            ?                   
# 
_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       2025-06-11 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9FGI 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 8Q6W unspecified 
PDB . 9FEO unspecified 
PDB . 9FEL unspecified 
PDB . 9FEM unspecified 
PDB . 9FEN unspecified 
PDB . 9FEQ unspecified 
PDB . 9FER unspecified 
PDB . 9FFI unspecified 
PDB . 9FES unspecified 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              brynda@uochb.cas.cz 
_pdbx_contact_author.name_first         Jiri 
_pdbx_contact_author.name_last          Brynda 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3675-6769 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Myskova, J.' 1 ? 
'Brynda, J.'  2 ? 
'Lazar, J.'   3 ? 
# 
loop_
_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 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? ? ? ? primary 'To Be Published' ? 0353 ? ? ? ? ? ? ? 'Directionality of Optical Properties of Fluorescent Proteins' 
? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? 1       'To Be Published' ? 0353 ? ? ? ? ? ? ? 'Directional optical properties of fluorescent proteins'       
? ? ? ? ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Myskova, J.'   1 ? 
primary 'Brynda, J.'    2 ? 
primary 'Khoroshyy, P.' 3 ? 
primary 'Lazar, J.'     4 ? 
1       'Myskova, J.'   5 ? 
1       'Lazar, J.'     6 ? 
# 
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 nowGFP 27537.072 2   ? ? ? ? 
2 water   nat water  18.015    171 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MVSKGEKLFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKMSLKFICTTGKLPVPWPTLKTTL(CRF)MQCFARYPDH
MKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGVDFKEDGNILGHKLEYNAISGNANITADKQ
KNGIKAYFTIRHDVEDGSVLLADHYQQNTPIGDGPVLLPDNHYLSTQSKQSKDPNEKRDHMVLLEFVTAAGIPLGADELY
KHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVSKGEKLFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKMSLKFICTTGKLPVPWPTLKTTLTWGMQCFARYPDHMK
QHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGVDFKEDGNILGHKLEYNAISGNANITADKQKN
GIKAYFTIRHDVEDGSVLLADHYQQNTPIGDGPVLLPDNHYLSTQSKQSKDPNEKRDHMVLLEFVTAAGIPLGADELYKH
HHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   VAL n 
1 3   SER n 
1 4   LYS n 
1 5   GLY n 
1 6   GLU n 
1 7   LYS n 
1 8   LEU n 
1 9   PHE n 
1 10  THR n 
1 11  GLY n 
1 12  VAL n 
1 13  VAL n 
1 14  PRO n 
1 15  ILE n 
1 16  LEU n 
1 17  VAL n 
1 18  GLU n 
1 19  LEU n 
1 20  ASP n 
1 21  GLY n 
1 22  ASP n 
1 23  VAL n 
1 24  ASN n 
1 25  GLY n 
1 26  HIS n 
1 27  LYS n 
1 28  PHE n 
1 29  SER n 
1 30  VAL n 
1 31  SER n 
1 32  GLY n 
1 33  GLU n 
1 34  GLY n 
1 35  GLU n 
1 36  GLY n 
1 37  ASP n 
1 38  ALA n 
1 39  THR n 
1 40  TYR n 
1 41  GLY n 
1 42  LYS n 
1 43  MET n 
1 44  SER n 
1 45  LEU n 
1 46  LYS n 
1 47  PHE n 
1 48  ILE n 
1 49  CYS n 
1 50  THR n 
1 51  THR n 
1 52  GLY n 
1 53  LYS n 
1 54  LEU n 
1 55  PRO n 
1 56  VAL n 
1 57  PRO n 
1 58  TRP n 
1 59  PRO n 
1 60  THR n 
1 61  LEU n 
1 62  LYS n 
1 63  THR n 
1 64  THR n 
1 65  LEU n 
1 66  CRF n 
1 67  MET n 
1 68  GLN n 
1 69  CYS n 
1 70  PHE n 
1 71  ALA n 
1 72  ARG n 
1 73  TYR n 
1 74  PRO n 
1 75  ASP n 
1 76  HIS n 
1 77  MET n 
1 78  LYS n 
1 79  GLN n 
1 80  HIS n 
1 81  ASP n 
1 82  PHE n 
1 83  PHE n 
1 84  LYS n 
1 85  SER n 
1 86  ALA n 
1 87  MET n 
1 88  PRO n 
1 89  GLU n 
1 90  GLY n 
1 91  TYR n 
1 92  VAL n 
1 93  GLN n 
1 94  GLU n 
1 95  ARG n 
1 96  THR n 
1 97  ILE n 
1 98  PHE n 
1 99  PHE n 
1 100 LYS n 
1 101 ASP n 
1 102 ASP n 
1 103 GLY n 
1 104 ASN n 
1 105 TYR n 
1 106 LYS n 
1 107 THR n 
1 108 ARG n 
1 109 ALA n 
1 110 GLU n 
1 111 VAL n 
1 112 LYS n 
1 113 PHE n 
1 114 GLU n 
1 115 GLY n 
1 116 ASP n 
1 117 THR n 
1 118 LEU n 
1 119 VAL n 
1 120 ASN n 
1 121 ARG n 
1 122 ILE n 
1 123 GLU n 
1 124 LEU n 
1 125 LYS n 
1 126 GLY n 
1 127 VAL n 
1 128 ASP n 
1 129 PHE n 
1 130 LYS n 
1 131 GLU n 
1 132 ASP n 
1 133 GLY n 
1 134 ASN n 
1 135 ILE n 
1 136 LEU n 
1 137 GLY n 
1 138 HIS n 
1 139 LYS n 
1 140 LEU n 
1 141 GLU n 
1 142 TYR n 
1 143 ASN n 
1 144 ALA n 
1 145 ILE n 
1 146 SER n 
1 147 GLY n 
1 148 ASN n 
1 149 ALA n 
1 150 ASN n 
1 151 ILE n 
1 152 THR n 
1 153 ALA n 
1 154 ASP n 
1 155 LYS n 
1 156 GLN n 
1 157 LYS n 
1 158 ASN n 
1 159 GLY n 
1 160 ILE n 
1 161 LYS n 
1 162 ALA n 
1 163 TYR n 
1 164 PHE n 
1 165 THR n 
1 166 ILE n 
1 167 ARG n 
1 168 HIS n 
1 169 ASP n 
1 170 VAL n 
1 171 GLU n 
1 172 ASP n 
1 173 GLY n 
1 174 SER n 
1 175 VAL n 
1 176 LEU n 
1 177 LEU n 
1 178 ALA n 
1 179 ASP n 
1 180 HIS n 
1 181 TYR n 
1 182 GLN n 
1 183 GLN n 
1 184 ASN n 
1 185 THR n 
1 186 PRO n 
1 187 ILE n 
1 188 GLY n 
1 189 ASP n 
1 190 GLY n 
1 191 PRO n 
1 192 VAL n 
1 193 LEU n 
1 194 LEU n 
1 195 PRO n 
1 196 ASP n 
1 197 ASN n 
1 198 HIS n 
1 199 TYR n 
1 200 LEU n 
1 201 SER n 
1 202 THR n 
1 203 GLN n 
1 204 SER n 
1 205 LYS n 
1 206 GLN n 
1 207 SER n 
1 208 LYS n 
1 209 ASP n 
1 210 PRO n 
1 211 ASN n 
1 212 GLU n 
1 213 LYS n 
1 214 ARG n 
1 215 ASP n 
1 216 HIS n 
1 217 MET n 
1 218 VAL n 
1 219 LEU n 
1 220 LEU n 
1 221 GLU n 
1 222 PHE n 
1 223 VAL n 
1 224 THR n 
1 225 ALA n 
1 226 ALA n 
1 227 GLY n 
1 228 ILE n 
1 229 PRO n 
1 230 LEU n 
1 231 GLY n 
1 232 ALA n 
1 233 ASP n 
1 234 GLU n 
1 235 LEU n 
1 236 TYR n 
1 237 LYS n 
1 238 HIS n 
1 239 HIS n 
1 240 HIS n 
1 241 HIS n 
1 242 HIS n 
1 243 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   243 
_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      'Aequorea victoria' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     6100 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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                   ? 
# 
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 
CRF 'L-peptide linking' n 
'[(4Z)-2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(1H-indol-3-ylmethylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid' ? 
'C17 H18 N4 O4'  342.349 
CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   A . n 
A 1 2   VAL 2   1   ?   ?   ?   A . n 
A 1 3   SER 3   2   2   SER SER A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   GLY 5   4   4   GLY GLY A . n 
A 1 6   GLU 6   5   5   GLU GLU A . n 
A 1 7   LYS 7   6   6   LYS LYS A . n 
A 1 8   LEU 8   7   7   LEU LEU A . n 
A 1 9   PHE 9   8   8   PHE PHE A . n 
A 1 10  THR 10  9   9   THR THR A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  VAL 12  11  11  VAL VAL A . n 
A 1 13  VAL 13  12  12  VAL VAL A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  ILE 15  14  14  ILE ILE A . n 
A 1 16  LEU 16  15  15  LEU LEU A . n 
A 1 17  VAL 17  16  16  VAL VAL A . n 
A 1 18  GLU 18  17  17  GLU GLU A . n 
A 1 19  LEU 19  18  18  LEU LEU A . n 
A 1 20  ASP 20  19  19  ASP ASP A . n 
A 1 21  GLY 21  20  20  GLY GLY A . n 
A 1 22  ASP 22  21  21  ASP ASP A . n 
A 1 23  VAL 23  22  22  VAL VAL A . n 
A 1 24  ASN 24  23  23  ASN ASN A . n 
A 1 25  GLY 25  24  24  GLY GLY A . n 
A 1 26  HIS 26  25  25  HIS HIS A . n 
A 1 27  LYS 27  26  26  LYS LYS A . n 
A 1 28  PHE 28  27  27  PHE PHE A . n 
A 1 29  SER 29  28  28  SER SER A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  SER 31  30  30  SER SER A . n 
A 1 32  GLY 32  31  31  GLY GLY A . n 
A 1 33  GLU 33  32  32  GLU GLU A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  GLU 35  34  34  GLU GLU A . n 
A 1 36  GLY 36  35  35  GLY GLY A . n 
A 1 37  ASP 37  36  36  ASP ASP A . n 
A 1 38  ALA 38  37  37  ALA ALA A . n 
A 1 39  THR 39  38  38  THR THR A . n 
A 1 40  TYR 40  39  39  TYR TYR A . n 
A 1 41  GLY 41  40  40  GLY GLY A . n 
A 1 42  LYS 42  41  41  LYS LYS A . n 
A 1 43  MET 43  42  42  MET MET A . n 
A 1 44  SER 44  43  43  SER SER A . n 
A 1 45  LEU 45  44  44  LEU LEU A . n 
A 1 46  LYS 46  45  45  LYS LYS A . n 
A 1 47  PHE 47  46  46  PHE PHE A . n 
A 1 48  ILE 48  47  47  ILE ILE A . n 
A 1 49  CYS 49  48  48  CYS CYS A . n 
A 1 50  THR 50  49  49  THR THR A . n 
A 1 51  THR 51  50  50  THR THR A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  LYS 53  52  52  LYS LYS A . n 
A 1 54  LEU 54  53  53  LEU LEU A . n 
A 1 55  PRO 55  54  54  PRO PRO A . n 
A 1 56  VAL 56  55  55  VAL VAL A . n 
A 1 57  PRO 57  56  56  PRO PRO A . n 
A 1 58  TRP 58  57  57  TRP TRP A . n 
A 1 59  PRO 59  58  58  PRO PRO A . n 
A 1 60  THR 60  59  59  THR THR A . n 
A 1 61  LEU 61  60  60  LEU LEU A . n 
A 1 62  LYS 62  61  61  LYS LYS A . n 
A 1 63  THR 63  62  62  THR THR A . n 
A 1 64  THR 64  63  63  THR THR A . n 
A 1 65  LEU 65  64  64  LEU LEU A . n 
A 1 66  CRF 66  65  65  CRF CRF A . n 
A 1 67  MET 67  68  68  MET MET A . n 
A 1 68  GLN 68  69  69  GLN GLN A . n 
A 1 69  CYS 69  70  70  CYS CYS A . n 
A 1 70  PHE 70  71  71  PHE PHE A . n 
A 1 71  ALA 71  72  72  ALA ALA A . n 
A 1 72  ARG 72  73  73  ARG ARG A . n 
A 1 73  TYR 73  74  74  TYR TYR A . n 
A 1 74  PRO 74  75  75  PRO PRO A . n 
A 1 75  ASP 75  76  76  ASP ASP A . n 
A 1 76  HIS 76  77  77  HIS HIS A . n 
A 1 77  MET 77  78  78  MET MET A . n 
A 1 78  LYS 78  79  79  LYS LYS A . n 
A 1 79  GLN 79  80  80  GLN GLN A . n 
A 1 80  HIS 80  81  81  HIS HIS A . n 
A 1 81  ASP 81  82  82  ASP ASP A . n 
A 1 82  PHE 82  83  83  PHE PHE A . n 
A 1 83  PHE 83  84  84  PHE PHE A . n 
A 1 84  LYS 84  85  85  LYS LYS A . n 
A 1 85  SER 85  86  86  SER SER A . n 
A 1 86  ALA 86  87  87  ALA ALA A . n 
A 1 87  MET 87  88  88  MET MET A . n 
A 1 88  PRO 88  89  89  PRO PRO A . n 
A 1 89  GLU 89  90  90  GLU GLU A . n 
A 1 90  GLY 90  91  91  GLY GLY A . n 
A 1 91  TYR 91  92  92  TYR TYR A . n 
A 1 92  VAL 92  93  93  VAL VAL A . n 
A 1 93  GLN 93  94  94  GLN GLN A . n 
A 1 94  GLU 94  95  95  GLU GLU A . n 
A 1 95  ARG 95  96  96  ARG ARG A . n 
A 1 96  THR 96  97  97  THR THR A . n 
A 1 97  ILE 97  98  98  ILE ILE A . n 
A 1 98  PHE 98  99  99  PHE PHE A . n 
A 1 99  PHE 99  100 100 PHE PHE A . n 
A 1 100 LYS 100 101 101 LYS LYS A . n 
A 1 101 ASP 101 102 102 ASP ASP A . n 
A 1 102 ASP 102 103 103 ASP ASP A . n 
A 1 103 GLY 103 104 104 GLY GLY A . n 
A 1 104 ASN 104 105 105 ASN ASN A . n 
A 1 105 TYR 105 106 106 TYR TYR A . n 
A 1 106 LYS 106 107 107 LYS LYS A . n 
A 1 107 THR 107 108 108 THR THR A . n 
A 1 108 ARG 108 109 109 ARG ARG A . n 
A 1 109 ALA 109 110 110 ALA ALA A . n 
A 1 110 GLU 110 111 111 GLU GLU A . n 
A 1 111 VAL 111 112 112 VAL VAL A . n 
A 1 112 LYS 112 113 113 LYS LYS A . n 
A 1 113 PHE 113 114 114 PHE PHE A . n 
A 1 114 GLU 114 115 115 GLU GLU A . n 
A 1 115 GLY 115 116 116 GLY GLY A . n 
A 1 116 ASP 116 117 117 ASP ASP A . n 
A 1 117 THR 117 118 118 THR THR A . n 
A 1 118 LEU 118 119 119 LEU LEU A . n 
A 1 119 VAL 119 120 120 VAL VAL A . n 
A 1 120 ASN 120 121 121 ASN ASN A . n 
A 1 121 ARG 121 122 122 ARG ARG A . n 
A 1 122 ILE 122 123 123 ILE ILE A . n 
A 1 123 GLU 123 124 124 GLU GLU A . n 
A 1 124 LEU 124 125 125 LEU LEU A . n 
A 1 125 LYS 125 126 126 LYS LYS A . n 
A 1 126 GLY 126 127 127 GLY GLY A . n 
A 1 127 VAL 127 128 128 VAL VAL A . n 
A 1 128 ASP 128 129 129 ASP ASP A . n 
A 1 129 PHE 129 130 130 PHE PHE A . n 
A 1 130 LYS 130 131 131 LYS LYS A . n 
A 1 131 GLU 131 132 132 GLU GLU A . n 
A 1 132 ASP 132 133 133 ASP ASP A . n 
A 1 133 GLY 133 134 134 GLY GLY A . n 
A 1 134 ASN 134 135 135 ASN ASN A . n 
A 1 135 ILE 135 136 136 ILE ILE A . n 
A 1 136 LEU 136 137 137 LEU LEU A . n 
A 1 137 GLY 137 138 138 GLY GLY A . n 
A 1 138 HIS 138 139 139 HIS HIS A . n 
A 1 139 LYS 139 140 140 LYS LYS A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 GLU 141 142 142 GLU GLU A . n 
A 1 142 TYR 142 143 143 TYR TYR A . n 
A 1 143 ASN 143 144 144 ASN ASN A . n 
A 1 144 ALA 144 145 145 ALA ALA A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 SER 146 147 147 SER SER A . n 
A 1 147 GLY 147 148 148 GLY GLY A . n 
A 1 148 ASN 148 149 149 ASN ASN A . n 
A 1 149 ALA 149 150 150 ALA ALA A . n 
A 1 150 ASN 150 151 151 ASN ASN A . n 
A 1 151 ILE 151 152 152 ILE ILE A . n 
A 1 152 THR 152 153 153 THR THR A . n 
A 1 153 ALA 153 154 154 ALA ALA A . n 
A 1 154 ASP 154 155 155 ASP ASP A . n 
A 1 155 LYS 155 156 156 LYS LYS A . n 
A 1 156 GLN 156 157 157 GLN GLN A . n 
A 1 157 LYS 157 158 158 LYS LYS A . n 
A 1 158 ASN 158 159 159 ASN ASN A . n 
A 1 159 GLY 159 160 160 GLY GLY A . n 
A 1 160 ILE 160 161 161 ILE ILE A . n 
A 1 161 LYS 161 162 162 LYS LYS A . n 
A 1 162 ALA 162 163 163 ALA ALA A . n 
A 1 163 TYR 163 164 164 TYR TYR A . n 
A 1 164 PHE 164 165 165 PHE PHE A . n 
A 1 165 THR 165 166 166 THR THR A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 ARG 167 168 168 ARG ARG A . n 
A 1 168 HIS 168 169 169 HIS HIS A . n 
A 1 169 ASP 169 170 170 ASP ASP A . n 
A 1 170 VAL 170 171 171 VAL VAL A . n 
A 1 171 GLU 171 172 172 GLU GLU A . n 
A 1 172 ASP 172 173 173 ASP ASP A . n 
A 1 173 GLY 173 174 174 GLY GLY A . n 
A 1 174 SER 174 175 175 SER SER A . n 
A 1 175 VAL 175 176 176 VAL VAL A . n 
A 1 176 LEU 176 177 177 LEU LEU A . n 
A 1 177 LEU 177 178 178 LEU LEU A . n 
A 1 178 ALA 178 179 179 ALA ALA A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 HIS 180 181 181 HIS HIS A . n 
A 1 181 TYR 181 182 182 TYR TYR A . n 
A 1 182 GLN 182 183 183 GLN GLN A . n 
A 1 183 GLN 183 184 184 GLN GLN A . n 
A 1 184 ASN 184 185 185 ASN ASN A . n 
A 1 185 THR 185 186 186 THR THR A . n 
A 1 186 PRO 186 187 187 PRO PRO A . n 
A 1 187 ILE 187 188 188 ILE ILE A . n 
A 1 188 GLY 188 189 189 GLY GLY A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 GLY 190 191 191 GLY GLY A . n 
A 1 191 PRO 191 192 192 PRO PRO A . n 
A 1 192 VAL 192 193 193 VAL VAL A . n 
A 1 193 LEU 193 194 194 LEU LEU A . n 
A 1 194 LEU 194 195 195 LEU LEU A . n 
A 1 195 PRO 195 196 196 PRO PRO A . n 
A 1 196 ASP 196 197 197 ASP ASP A . n 
A 1 197 ASN 197 198 198 ASN ASN A . n 
A 1 198 HIS 198 199 199 HIS HIS A . n 
A 1 199 TYR 199 200 200 TYR TYR A . n 
A 1 200 LEU 200 201 201 LEU LEU A . n 
A 1 201 SER 201 202 202 SER SER A . n 
A 1 202 THR 202 203 203 THR THR A . n 
A 1 203 GLN 203 204 204 GLN GLN A . n 
A 1 204 SER 204 205 205 SER SER A . n 
A 1 205 LYS 205 206 206 LYS LYS A . n 
A 1 206 GLN 206 207 207 GLN GLN A . n 
A 1 207 SER 207 208 208 SER SER A . n 
A 1 208 LYS 208 209 209 LYS LYS A . n 
A 1 209 ASP 209 210 210 ASP ASP A . n 
A 1 210 PRO 210 211 211 PRO PRO A . n 
A 1 211 ASN 211 212 212 ASN ASN A . n 
A 1 212 GLU 212 213 213 GLU GLU A . n 
A 1 213 LYS 213 214 214 LYS LYS A . n 
A 1 214 ARG 214 215 215 ARG ARG A . n 
A 1 215 ASP 215 216 216 ASP ASP A . n 
A 1 216 HIS 216 217 217 HIS HIS A . n 
A 1 217 MET 217 218 218 MET MET A . n 
A 1 218 VAL 218 219 219 VAL VAL A . n 
A 1 219 LEU 219 220 220 LEU LEU A . n 
A 1 220 LEU 220 221 221 LEU LEU A . n 
A 1 221 GLU 221 222 222 GLU GLU A . n 
A 1 222 PHE 222 223 223 PHE PHE A . n 
A 1 223 VAL 223 224 224 VAL VAL A . n 
A 1 224 THR 224 225 225 THR THR A . n 
A 1 225 ALA 225 226 226 ALA ALA A . n 
A 1 226 ALA 226 227 227 ALA ALA A . n 
A 1 227 GLY 227 228 228 GLY GLY A . n 
A 1 228 ILE 228 229 229 ILE ILE A . n 
A 1 229 PRO 229 230 230 PRO PRO A . n 
A 1 230 LEU 230 231 231 LEU LEU A . n 
A 1 231 GLY 231 232 ?   ?   ?   A . n 
A 1 232 ALA 232 233 ?   ?   ?   A . n 
A 1 233 ASP 233 234 ?   ?   ?   A . n 
A 1 234 GLU 234 235 ?   ?   ?   A . n 
A 1 235 LEU 235 236 ?   ?   ?   A . n 
A 1 236 TYR 236 237 ?   ?   ?   A . n 
A 1 237 LYS 237 238 ?   ?   ?   A . n 
A 1 238 HIS 238 239 ?   ?   ?   A . n 
A 1 239 HIS 239 240 ?   ?   ?   A . n 
A 1 240 HIS 240 241 ?   ?   ?   A . n 
A 1 241 HIS 241 242 ?   ?   ?   A . n 
A 1 242 HIS 242 243 ?   ?   ?   A . n 
A 1 243 HIS 243 244 ?   ?   ?   A . n 
B 1 1   MET 1   0   0   MET MET B . n 
B 1 2   VAL 2   1   1   VAL VAL B . n 
B 1 3   SER 3   2   2   SER SER B . n 
B 1 4   LYS 4   3   3   LYS LYS B . n 
B 1 5   GLY 5   4   4   GLY GLY B . n 
B 1 6   GLU 6   5   5   GLU GLU B . n 
B 1 7   LYS 7   6   6   LYS LYS B . n 
B 1 8   LEU 8   7   7   LEU LEU B . n 
B 1 9   PHE 9   8   8   PHE PHE B . n 
B 1 10  THR 10  9   9   THR THR B . n 
B 1 11  GLY 11  10  10  GLY GLY B . n 
B 1 12  VAL 12  11  11  VAL VAL B . n 
B 1 13  VAL 13  12  12  VAL VAL B . n 
B 1 14  PRO 14  13  13  PRO PRO B . n 
B 1 15  ILE 15  14  14  ILE ILE B . n 
B 1 16  LEU 16  15  15  LEU LEU B . n 
B 1 17  VAL 17  16  16  VAL VAL B . n 
B 1 18  GLU 18  17  17  GLU GLU B . n 
B 1 19  LEU 19  18  18  LEU LEU B . n 
B 1 20  ASP 20  19  19  ASP ASP B . n 
B 1 21  GLY 21  20  20  GLY GLY B . n 
B 1 22  ASP 22  21  21  ASP ASP B . n 
B 1 23  VAL 23  22  22  VAL VAL B . n 
B 1 24  ASN 24  23  23  ASN ASN B . n 
B 1 25  GLY 25  24  24  GLY GLY B . n 
B 1 26  HIS 26  25  25  HIS HIS B . n 
B 1 27  LYS 27  26  26  LYS LYS B . n 
B 1 28  PHE 28  27  27  PHE PHE B . n 
B 1 29  SER 29  28  28  SER SER B . n 
B 1 30  VAL 30  29  29  VAL VAL B . n 
B 1 31  SER 31  30  30  SER SER B . n 
B 1 32  GLY 32  31  31  GLY GLY B . n 
B 1 33  GLU 33  32  32  GLU GLU B . n 
B 1 34  GLY 34  33  33  GLY GLY B . n 
B 1 35  GLU 35  34  34  GLU GLU B . n 
B 1 36  GLY 36  35  35  GLY GLY B . n 
B 1 37  ASP 37  36  36  ASP ASP B . n 
B 1 38  ALA 38  37  37  ALA ALA B . n 
B 1 39  THR 39  38  38  THR THR B . n 
B 1 40  TYR 40  39  39  TYR TYR B . n 
B 1 41  GLY 41  40  40  GLY GLY B . n 
B 1 42  LYS 42  41  41  LYS LYS B . n 
B 1 43  MET 43  42  42  MET MET B . n 
B 1 44  SER 44  43  43  SER SER B . n 
B 1 45  LEU 45  44  44  LEU LEU B . n 
B 1 46  LYS 46  45  45  LYS LYS B . n 
B 1 47  PHE 47  46  46  PHE PHE B . n 
B 1 48  ILE 48  47  47  ILE ILE B . n 
B 1 49  CYS 49  48  48  CYS CYS B . n 
B 1 50  THR 50  49  49  THR THR B . n 
B 1 51  THR 51  50  50  THR THR B . n 
B 1 52  GLY 52  51  51  GLY GLY B . n 
B 1 53  LYS 53  52  52  LYS LYS B . n 
B 1 54  LEU 54  53  53  LEU LEU B . n 
B 1 55  PRO 55  54  54  PRO PRO B . n 
B 1 56  VAL 56  55  55  VAL VAL B . n 
B 1 57  PRO 57  56  56  PRO PRO B . n 
B 1 58  TRP 58  57  57  TRP TRP B . n 
B 1 59  PRO 59  58  58  PRO PRO B . n 
B 1 60  THR 60  59  59  THR THR B . n 
B 1 61  LEU 61  60  60  LEU LEU B . n 
B 1 62  LYS 62  61  61  LYS LYS B . n 
B 1 63  THR 63  62  62  THR THR B . n 
B 1 64  THR 64  63  63  THR THR B . n 
B 1 65  LEU 65  64  64  LEU LEU B . n 
B 1 66  CRF 66  65  65  CRF CRF B . n 
B 1 67  MET 67  68  68  MET MET B . n 
B 1 68  GLN 68  69  69  GLN GLN B . n 
B 1 69  CYS 69  70  70  CYS CYS B . n 
B 1 70  PHE 70  71  71  PHE PHE B . n 
B 1 71  ALA 71  72  72  ALA ALA B . n 
B 1 72  ARG 72  73  73  ARG ARG B . n 
B 1 73  TYR 73  74  74  TYR TYR B . n 
B 1 74  PRO 74  75  75  PRO PRO B . n 
B 1 75  ASP 75  76  76  ASP ASP B . n 
B 1 76  HIS 76  77  77  HIS HIS B . n 
B 1 77  MET 77  78  78  MET MET B . n 
B 1 78  LYS 78  79  79  LYS LYS B . n 
B 1 79  GLN 79  80  80  GLN GLN B . n 
B 1 80  HIS 80  81  81  HIS HIS B . n 
B 1 81  ASP 81  82  82  ASP ASP B . n 
B 1 82  PHE 82  83  83  PHE PHE B . n 
B 1 83  PHE 83  84  84  PHE PHE B . n 
B 1 84  LYS 84  85  85  LYS LYS B . n 
B 1 85  SER 85  86  86  SER SER B . n 
B 1 86  ALA 86  87  87  ALA ALA B . n 
B 1 87  MET 87  88  88  MET MET B . n 
B 1 88  PRO 88  89  89  PRO PRO B . n 
B 1 89  GLU 89  90  90  GLU GLU B . n 
B 1 90  GLY 90  91  91  GLY GLY B . n 
B 1 91  TYR 91  92  92  TYR TYR B . n 
B 1 92  VAL 92  93  93  VAL VAL B . n 
B 1 93  GLN 93  94  94  GLN GLN B . n 
B 1 94  GLU 94  95  95  GLU GLU B . n 
B 1 95  ARG 95  96  96  ARG ARG B . n 
B 1 96  THR 96  97  97  THR THR B . n 
B 1 97  ILE 97  98  98  ILE ILE B . n 
B 1 98  PHE 98  99  99  PHE PHE B . n 
B 1 99  PHE 99  100 100 PHE PHE B . n 
B 1 100 LYS 100 101 101 LYS LYS B . n 
B 1 101 ASP 101 102 102 ASP ASP B . n 
B 1 102 ASP 102 103 103 ASP ASP B . n 
B 1 103 GLY 103 104 104 GLY GLY B . n 
B 1 104 ASN 104 105 105 ASN ASN B . n 
B 1 105 TYR 105 106 106 TYR TYR B . n 
B 1 106 LYS 106 107 107 LYS LYS B . n 
B 1 107 THR 107 108 108 THR THR B . n 
B 1 108 ARG 108 109 109 ARG ARG B . n 
B 1 109 ALA 109 110 110 ALA ALA B . n 
B 1 110 GLU 110 111 111 GLU GLU B . n 
B 1 111 VAL 111 112 112 VAL VAL B . n 
B 1 112 LYS 112 113 113 LYS LYS B . n 
B 1 113 PHE 113 114 114 PHE PHE B . n 
B 1 114 GLU 114 115 115 GLU GLU B . n 
B 1 115 GLY 115 116 116 GLY GLY B . n 
B 1 116 ASP 116 117 117 ASP ASP B . n 
B 1 117 THR 117 118 118 THR THR B . n 
B 1 118 LEU 118 119 119 LEU LEU B . n 
B 1 119 VAL 119 120 120 VAL VAL B . n 
B 1 120 ASN 120 121 121 ASN ASN B . n 
B 1 121 ARG 121 122 122 ARG ARG B . n 
B 1 122 ILE 122 123 123 ILE ILE B . n 
B 1 123 GLU 123 124 124 GLU GLU B . n 
B 1 124 LEU 124 125 125 LEU LEU B . n 
B 1 125 LYS 125 126 126 LYS LYS B . n 
B 1 126 GLY 126 127 127 GLY GLY B . n 
B 1 127 VAL 127 128 128 VAL VAL B . n 
B 1 128 ASP 128 129 129 ASP ASP B . n 
B 1 129 PHE 129 130 130 PHE PHE B . n 
B 1 130 LYS 130 131 131 LYS LYS B . n 
B 1 131 GLU 131 132 132 GLU GLU B . n 
B 1 132 ASP 132 133 133 ASP ASP B . n 
B 1 133 GLY 133 134 134 GLY GLY B . n 
B 1 134 ASN 134 135 135 ASN ASN B . n 
B 1 135 ILE 135 136 136 ILE ILE B . n 
B 1 136 LEU 136 137 137 LEU LEU B . n 
B 1 137 GLY 137 138 138 GLY GLY B . n 
B 1 138 HIS 138 139 139 HIS HIS B . n 
B 1 139 LYS 139 140 140 LYS LYS B . n 
B 1 140 LEU 140 141 141 LEU LEU B . n 
B 1 141 GLU 141 142 142 GLU GLU B . n 
B 1 142 TYR 142 143 143 TYR TYR B . n 
B 1 143 ASN 143 144 144 ASN ASN B . n 
B 1 144 ALA 144 145 145 ALA ALA B . n 
B 1 145 ILE 145 146 146 ILE ILE B . n 
B 1 146 SER 146 147 147 SER SER B . n 
B 1 147 GLY 147 148 148 GLY GLY B . n 
B 1 148 ASN 148 149 149 ASN ASN B . n 
B 1 149 ALA 149 150 150 ALA ALA B . n 
B 1 150 ASN 150 151 151 ASN ASN B . n 
B 1 151 ILE 151 152 152 ILE ILE B . n 
B 1 152 THR 152 153 153 THR THR B . n 
B 1 153 ALA 153 154 154 ALA ALA B . n 
B 1 154 ASP 154 155 155 ASP ASP B . n 
B 1 155 LYS 155 156 156 LYS LYS B . n 
B 1 156 GLN 156 157 157 GLN GLN B . n 
B 1 157 LYS 157 158 158 LYS LYS B . n 
B 1 158 ASN 158 159 159 ASN ASN B . n 
B 1 159 GLY 159 160 160 GLY GLY B . n 
B 1 160 ILE 160 161 161 ILE ILE B . n 
B 1 161 LYS 161 162 162 LYS LYS B . n 
B 1 162 ALA 162 163 163 ALA ALA B . n 
B 1 163 TYR 163 164 164 TYR TYR B . n 
B 1 164 PHE 164 165 165 PHE PHE B . n 
B 1 165 THR 165 166 166 THR THR B . n 
B 1 166 ILE 166 167 167 ILE ILE B . n 
B 1 167 ARG 167 168 168 ARG ARG B . n 
B 1 168 HIS 168 169 169 HIS HIS B . n 
B 1 169 ASP 169 170 170 ASP ASP B . n 
B 1 170 VAL 170 171 171 VAL VAL B . n 
B 1 171 GLU 171 172 172 GLU GLU B . n 
B 1 172 ASP 172 173 173 ASP ASP B . n 
B 1 173 GLY 173 174 174 GLY GLY B . n 
B 1 174 SER 174 175 175 SER SER B . n 
B 1 175 VAL 175 176 176 VAL VAL B . n 
B 1 176 LEU 176 177 177 LEU LEU B . n 
B 1 177 LEU 177 178 178 LEU LEU B . n 
B 1 178 ALA 178 179 179 ALA ALA B . n 
B 1 179 ASP 179 180 180 ASP ASP B . n 
B 1 180 HIS 180 181 181 HIS HIS B . n 
B 1 181 TYR 181 182 182 TYR TYR B . n 
B 1 182 GLN 182 183 183 GLN GLN B . n 
B 1 183 GLN 183 184 184 GLN GLN B . n 
B 1 184 ASN 184 185 185 ASN ASN B . n 
B 1 185 THR 185 186 186 THR THR B . n 
B 1 186 PRO 186 187 187 PRO PRO B . n 
B 1 187 ILE 187 188 188 ILE ILE B . n 
B 1 188 GLY 188 189 189 GLY GLY B . n 
B 1 189 ASP 189 190 190 ASP ASP B . n 
B 1 190 GLY 190 191 191 GLY GLY B . n 
B 1 191 PRO 191 192 192 PRO PRO B . n 
B 1 192 VAL 192 193 193 VAL VAL B . n 
B 1 193 LEU 193 194 194 LEU LEU B . n 
B 1 194 LEU 194 195 195 LEU LEU B . n 
B 1 195 PRO 195 196 196 PRO PRO B . n 
B 1 196 ASP 196 197 197 ASP ASP B . n 
B 1 197 ASN 197 198 198 ASN ASN B . n 
B 1 198 HIS 198 199 199 HIS HIS B . n 
B 1 199 TYR 199 200 200 TYR TYR B . n 
B 1 200 LEU 200 201 201 LEU LEU B . n 
B 1 201 SER 201 202 202 SER SER B . n 
B 1 202 THR 202 203 203 THR THR B . n 
B 1 203 GLN 203 204 204 GLN GLN B . n 
B 1 204 SER 204 205 205 SER SER B . n 
B 1 205 LYS 205 206 206 LYS LYS B . n 
B 1 206 GLN 206 207 207 GLN GLN B . n 
B 1 207 SER 207 208 208 SER SER B . n 
B 1 208 LYS 208 209 209 LYS LYS B . n 
B 1 209 ASP 209 210 210 ASP ASP B . n 
B 1 210 PRO 210 211 211 PRO PRO B . n 
B 1 211 ASN 211 212 212 ASN ASN B . n 
B 1 212 GLU 212 213 213 GLU GLU B . n 
B 1 213 LYS 213 214 214 LYS LYS B . n 
B 1 214 ARG 214 215 215 ARG ARG B . n 
B 1 215 ASP 215 216 216 ASP ASP B . n 
B 1 216 HIS 216 217 217 HIS HIS B . n 
B 1 217 MET 217 218 218 MET MET B . n 
B 1 218 VAL 218 219 219 VAL VAL B . n 
B 1 219 LEU 219 220 220 LEU LEU B . n 
B 1 220 LEU 220 221 221 LEU LEU B . n 
B 1 221 GLU 221 222 222 GLU GLU B . n 
B 1 222 PHE 222 223 223 PHE PHE B . n 
B 1 223 VAL 223 224 224 VAL VAL B . n 
B 1 224 THR 224 225 225 THR THR B . n 
B 1 225 ALA 225 226 226 ALA ALA B . n 
B 1 226 ALA 226 227 227 ALA ALA B . n 
B 1 227 GLY 227 228 228 GLY GLY B . n 
B 1 228 ILE 228 229 229 ILE ILE B . n 
B 1 229 PRO 229 230 230 PRO PRO B . n 
B 1 230 LEU 230 231 231 LEU LEU B . n 
B 1 231 GLY 231 232 ?   ?   ?   B . n 
B 1 232 ALA 232 233 ?   ?   ?   B . n 
B 1 233 ASP 233 234 ?   ?   ?   B . n 
B 1 234 GLU 234 235 ?   ?   ?   B . n 
B 1 235 LEU 235 236 ?   ?   ?   B . n 
B 1 236 TYR 236 237 ?   ?   ?   B . n 
B 1 237 LYS 237 238 ?   ?   ?   B . n 
B 1 238 HIS 238 239 ?   ?   ?   B . n 
B 1 239 HIS 239 240 ?   ?   ?   B . n 
B 1 240 HIS 240 241 ?   ?   ?   B . n 
B 1 241 HIS 241 242 ?   ?   ?   B . n 
B 1 242 HIS 242 243 ?   ?   ?   B . n 
B 1 243 HIS 243 244 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        CRF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   CRF 
_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 HOH 1  301 72  HOH HOH A . 
C 2 HOH 2  302 111 HOH HOH A . 
C 2 HOH 3  303 29  HOH HOH A . 
C 2 HOH 4  304 99  HOH HOH A . 
C 2 HOH 5  305 150 HOH HOH A . 
C 2 HOH 6  306 2   HOH HOH A . 
C 2 HOH 7  307 57  HOH HOH A . 
C 2 HOH 8  308 30  HOH HOH A . 
C 2 HOH 9  309 129 HOH HOH A . 
C 2 HOH 10 310 54  HOH HOH A . 
C 2 HOH 11 311 156 HOH HOH A . 
C 2 HOH 12 312 6   HOH HOH A . 
C 2 HOH 13 313 42  HOH HOH A . 
C 2 HOH 14 314 105 HOH HOH A . 
C 2 HOH 15 315 75  HOH HOH A . 
C 2 HOH 16 316 109 HOH HOH A . 
C 2 HOH 17 317 1   HOH HOH A . 
C 2 HOH 18 318 62  HOH HOH A . 
C 2 HOH 19 319 5   HOH HOH A . 
C 2 HOH 20 320 45  HOH HOH A . 
C 2 HOH 21 321 43  HOH HOH A . 
C 2 HOH 22 322 88  HOH HOH A . 
C 2 HOH 23 323 121 HOH HOH A . 
C 2 HOH 24 324 40  HOH HOH A . 
C 2 HOH 25 325 35  HOH HOH A . 
C 2 HOH 26 326 18  HOH HOH A . 
C 2 HOH 27 327 96  HOH HOH A . 
C 2 HOH 28 328 4   HOH HOH A . 
C 2 HOH 29 329 37  HOH HOH A . 
C 2 HOH 30 330 117 HOH HOH A . 
C 2 HOH 31 331 16  HOH HOH A . 
C 2 HOH 32 332 119 HOH HOH A . 
C 2 HOH 33 333 118 HOH HOH A . 
C 2 HOH 34 334 71  HOH HOH A . 
C 2 HOH 35 335 108 HOH HOH A . 
C 2 HOH 36 336 79  HOH HOH A . 
C 2 HOH 37 337 73  HOH HOH A . 
C 2 HOH 38 338 168 HOH HOH A . 
C 2 HOH 39 339 81  HOH HOH A . 
C 2 HOH 40 340 125 HOH HOH A . 
C 2 HOH 41 341 110 HOH HOH A . 
C 2 HOH 42 342 15  HOH HOH A . 
C 2 HOH 43 343 27  HOH HOH A . 
C 2 HOH 44 344 61  HOH HOH A . 
C 2 HOH 45 345 122 HOH HOH A . 
C 2 HOH 46 346 63  HOH HOH A . 
C 2 HOH 47 347 13  HOH HOH A . 
C 2 HOH 48 348 93  HOH HOH A . 
C 2 HOH 49 349 24  HOH HOH A . 
C 2 HOH 50 350 142 HOH HOH A . 
C 2 HOH 51 351 101 HOH HOH A . 
C 2 HOH 52 352 68  HOH HOH A . 
C 2 HOH 53 353 115 HOH HOH A . 
C 2 HOH 54 354 149 HOH HOH A . 
C 2 HOH 55 355 83  HOH HOH A . 
C 2 HOH 56 356 69  HOH HOH A . 
C 2 HOH 57 357 80  HOH HOH A . 
C 2 HOH 58 358 17  HOH HOH A . 
C 2 HOH 59 359 103 HOH HOH A . 
C 2 HOH 60 360 147 HOH HOH A . 
C 2 HOH 61 361 12  HOH HOH A . 
C 2 HOH 62 362 21  HOH HOH A . 
C 2 HOH 63 363 8   HOH HOH A . 
C 2 HOH 64 364 148 HOH HOH A . 
C 2 HOH 65 365 66  HOH HOH A . 
C 2 HOH 66 366 87  HOH HOH A . 
C 2 HOH 67 367 67  HOH HOH A . 
C 2 HOH 68 368 160 HOH HOH A . 
C 2 HOH 69 369 120 HOH HOH A . 
C 2 HOH 70 370 32  HOH HOH A . 
C 2 HOH 71 371 104 HOH HOH A . 
C 2 HOH 72 372 162 HOH HOH A . 
C 2 HOH 73 373 130 HOH HOH A . 
C 2 HOH 74 374 65  HOH HOH A . 
C 2 HOH 75 375 91  HOH HOH A . 
C 2 HOH 76 376 23  HOH HOH A . 
C 2 HOH 77 377 127 HOH HOH A . 
C 2 HOH 78 378 161 HOH HOH A . 
C 2 HOH 79 379 141 HOH HOH A . 
C 2 HOH 80 380 74  HOH HOH A . 
C 2 HOH 81 381 14  HOH HOH A . 
C 2 HOH 82 382 106 HOH HOH A . 
C 2 HOH 83 383 56  HOH HOH A . 
C 2 HOH 84 384 50  HOH HOH A . 
C 2 HOH 85 385 135 HOH HOH A . 
C 2 HOH 86 386 25  HOH HOH A . 
C 2 HOH 87 387 157 HOH HOH A . 
C 2 HOH 88 388 165 HOH HOH A . 
C 2 HOH 89 389 172 HOH HOH A . 
C 2 HOH 90 390 146 HOH HOH A . 
C 2 HOH 91 391 26  HOH HOH A . 
C 2 HOH 92 392 154 HOH HOH A . 
C 2 HOH 93 393 124 HOH HOH A . 
C 2 HOH 94 394 152 HOH HOH A . 
C 2 HOH 95 395 155 HOH HOH A . 
C 2 HOH 96 396 144 HOH HOH A . 
C 2 HOH 97 397 167 HOH HOH A . 
C 2 HOH 98 398 176 HOH HOH A . 
C 2 HOH 99 399 95  HOH HOH A . 
D 2 HOH 1  301 10  HOH HOH B . 
D 2 HOH 2  302 136 HOH HOH B . 
D 2 HOH 3  303 97  HOH HOH B . 
D 2 HOH 4  304 169 HOH HOH B . 
D 2 HOH 5  305 92  HOH HOH B . 
D 2 HOH 6  306 49  HOH HOH B . 
D 2 HOH 7  307 3   HOH HOH B . 
D 2 HOH 8  308 143 HOH HOH B . 
D 2 HOH 9  309 140 HOH HOH B . 
D 2 HOH 10 310 11  HOH HOH B . 
D 2 HOH 11 311 175 HOH HOH B . 
D 2 HOH 12 312 174 HOH HOH B . 
D 2 HOH 13 313 38  HOH HOH B . 
D 2 HOH 14 314 85  HOH HOH B . 
D 2 HOH 15 315 7   HOH HOH B . 
D 2 HOH 16 316 166 HOH HOH B . 
D 2 HOH 17 317 153 HOH HOH B . 
D 2 HOH 18 318 171 HOH HOH B . 
D 2 HOH 19 319 159 HOH HOH B . 
D 2 HOH 20 320 77  HOH HOH B . 
D 2 HOH 21 321 100 HOH HOH B . 
D 2 HOH 22 322 22  HOH HOH B . 
D 2 HOH 23 323 151 HOH HOH B . 
D 2 HOH 24 324 19  HOH HOH B . 
D 2 HOH 25 325 78  HOH HOH B . 
D 2 HOH 26 326 64  HOH HOH B . 
D 2 HOH 27 327 76  HOH HOH B . 
D 2 HOH 28 328 134 HOH HOH B . 
D 2 HOH 29 329 36  HOH HOH B . 
D 2 HOH 30 330 53  HOH HOH B . 
D 2 HOH 31 331 59  HOH HOH B . 
D 2 HOH 32 332 123 HOH HOH B . 
D 2 HOH 33 333 126 HOH HOH B . 
D 2 HOH 34 334 44  HOH HOH B . 
D 2 HOH 35 335 89  HOH HOH B . 
D 2 HOH 36 336 137 HOH HOH B . 
D 2 HOH 37 337 41  HOH HOH B . 
D 2 HOH 38 338 82  HOH HOH B . 
D 2 HOH 39 339 34  HOH HOH B . 
D 2 HOH 40 340 39  HOH HOH B . 
D 2 HOH 41 341 128 HOH HOH B . 
D 2 HOH 42 342 52  HOH HOH B . 
D 2 HOH 43 343 20  HOH HOH B . 
D 2 HOH 44 344 158 HOH HOH B . 
D 2 HOH 45 345 177 HOH HOH B . 
D 2 HOH 46 346 33  HOH HOH B . 
D 2 HOH 47 347 51  HOH HOH B . 
D 2 HOH 48 348 55  HOH HOH B . 
D 2 HOH 49 349 102 HOH HOH B . 
D 2 HOH 50 350 163 HOH HOH B . 
D 2 HOH 51 351 60  HOH HOH B . 
D 2 HOH 52 352 31  HOH HOH B . 
D 2 HOH 53 353 86  HOH HOH B . 
D 2 HOH 54 354 164 HOH HOH B . 
D 2 HOH 55 355 70  HOH HOH B . 
D 2 HOH 56 356 98  HOH HOH B . 
D 2 HOH 57 357 46  HOH HOH B . 
D 2 HOH 58 358 116 HOH HOH B . 
D 2 HOH 59 359 145 HOH HOH B . 
D 2 HOH 60 360 58  HOH HOH B . 
D 2 HOH 61 361 47  HOH HOH B . 
D 2 HOH 62 362 107 HOH HOH B . 
D 2 HOH 63 363 173 HOH HOH B . 
D 2 HOH 64 364 131 HOH HOH B . 
D 2 HOH 65 365 178 HOH HOH B . 
D 2 HOH 66 366 170 HOH HOH B . 
D 2 HOH 67 367 90  HOH HOH B . 
D 2 HOH 68 368 138 HOH HOH B . 
D 2 HOH 69 369 112 HOH HOH B . 
D 2 HOH 70 370 48  HOH HOH B . 
D 2 HOH 71 371 139 HOH HOH B . 
D 2 HOH 72 372 113 HOH HOH B . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0267 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        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                     9FGI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.260 
_cell.length_a_esd                 ? 
_cell.length_b                     51.390 
_cell.length_b_esd                 ? 
_cell.length_c                     195.740 
_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                         9FGI 
_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                   9FGI 
_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             2.31 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.79 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5 
_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    
;20 % w/v Polyethylene glycol 6,000
100 mM tri-Sodium citrate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-07-23 
_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   0.9184 
_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                        'BESSY BEAMLINE 14.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9184 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   14.1 
_diffrn_source.pdbx_synchrotron_site       BESSY 
# 
_reflns.B_iso_Wilson_estimate                          38.9 
_reflns.entry_id                                       9FGI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.77 
_reflns.d_resolution_low                               50.0 
_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                                     51138 
_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                           99.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.108 
_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                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.093 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.77 1.88 ? ? ? ? ? ? 7970 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2.33  ? ? 1 1 0.497 ? ? ? ? 2.74  ? ? ? ? ? ? ? ? ? 
1.88 2.0  ? ? ? ? ? ? 3808 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.67  ? ? 2 1 0.405 ? ? ? ? 1.545 ? ? ? ? ? ? ? ? ? 
2.00 2.16 ? ? ? ? ? ? 3484 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.38  ? ? 3 1 0.681 ? ? ? ? 0.865 ? ? ? ? ? ? ? ? ? 
2.16 2.37 ? ? ? ? ? ? 3149 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.22  ? ? 4 1 0.86  ? ? ? ? 0.464 ? ? ? ? ? ? ? ? ? 
2.37 2.65 ? ? ? ? ? ? 2772 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.284 ? ? 5 1 0.945 ? ? ? ? 0.243 ? ? ? ? ? ? ? ? ? 
2.65 3.06 ? ? ? ? ? ? 2403 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.143 ? ? 6 1 0.987 ? ? ? ? 0.123 ? ? ? ? ? ? ? ? ? 
3.06 3.74 ? ? ? ? ? ? 1954 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.062 ? ? 7 1 0.997 ? ? ? ? 0.054 ? ? ? ? ? ? ? ? ? 
3.74 5.28 ? ? ? ? ? ? 1446 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.039 ? ? 8 1 0.999 ? ? ? ? 0.034 ? ? ? ? ? ? ? ? ? 
5.28 50.0 ? ? ? ? ? ? 2131 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.036 ? ? 9 1 0.999 ? ? ? ? 0.032 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            2.33 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -0.63 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.70 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               41.139 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.949 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9FGI 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.77 
_refine.ls_d_res_low                             49.59 
_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                     49037 
_refine.ls_number_reflns_R_free                  2101 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.09 
_refine.ls_percent_reflns_R_free                 4.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20041 
_refine.ls_R_factor_R_free                       0.23958 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19874 
_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                    'BABINET MODEL WITH MASK' 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.120 
_refine.pdbx_overall_ESU_R_Free                  0.120 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             4.080 
_refine.overall_SU_ML                            0.118 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.77 
_refine_hist.d_res_low                        49.59 
_refine_hist.number_atoms_solvent             171 
_refine_hist.number_atoms_total               3804 
_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        3633 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.014  0.013  3721 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.017  3481 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.128  1.668  5023 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.403  1.604  8064 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 8.220  5.000  454  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 30.636 24.239 184  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.160 15.000 647  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.775 15.000 12   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.087  0.200  471  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  4193 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  815  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 4.141  4.011  1822 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.127  4.009  1821 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.003  6.004  2271 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.008  6.007  2272 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.900  4.560  1899 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.899  4.562  1900 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 8.552  6.594  2752 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 9.965  46.149 3857 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 9.980  46.076 3837 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.77 
_refine_ls_shell.d_res_low                        1.814 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             148 
_refine_ls_shell.number_reflns_R_work             3446 
_refine_ls_shell.percent_reflns_obs               96.33 
_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                  0.364 
_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                  0.342 
# 
_struct.entry_id                     9FGI 
_struct.title                        'LSSmOrange (P1) - Directionality of Optical Properties of Fluorescent Proteins' 
_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        9FGI 
_struct_keywords.text            'FLUORESCENT PROTEIN' 
_struct_keywords.pdbx_keywords   'FLUORESCENT 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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9FGI 
_struct_ref.pdbx_db_accession          9FGI 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           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 9FGI A 1 ? 243 ? 9FGI 0 ? 244 ? 0 244 
2 1 9FGI B 1 ? 243 ? 9FGI 0 ? 244 ? 0 244 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C 
2 1 B,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LYS A 4   ? THR A 10  ? LYS A 3   THR A 9   5 ? 7 
HELX_P HELX_P2  AA2 ALA A 38  ? TYR A 40  ? ALA A 37  TYR A 39  5 ? 3 
HELX_P HELX_P3  AA3 PRO A 57  ? LYS A 62  ? PRO A 56  LYS A 61  5 ? 6 
HELX_P HELX_P4  AA4 MET A 67  ? ALA A 71  ? MET A 68  ALA A 72  5 ? 5 
HELX_P HELX_P5  AA5 PRO A 74  ? HIS A 80  ? PRO A 75  HIS A 81  5 ? 7 
HELX_P HELX_P6  AA6 ASP A 81  ? ALA A 86  ? ASP A 82  ALA A 87  1 ? 6 
HELX_P HELX_P7  AA7 SER B 3   ? LEU B 8   ? SER B 2   LEU B 7   1 ? 6 
HELX_P HELX_P8  AA8 ALA B 38  ? TYR B 40  ? ALA B 37  TYR B 39  5 ? 3 
HELX_P HELX_P9  AA9 PRO B 57  ? LYS B 62  ? PRO B 56  LYS B 61  5 ? 6 
HELX_P HELX_P10 AB1 MET B 67  ? ALA B 71  ? MET B 68  ALA B 72  5 ? 5 
HELX_P HELX_P11 AB2 PRO B 74  ? HIS B 80  ? PRO B 75  HIS B 81  5 ? 7 
HELX_P HELX_P12 AB3 ASP B 81  ? ALA B 86  ? ASP B 82  ALA B 87  1 ? 6 
HELX_P HELX_P13 AB4 LYS B 155 ? ASN B 158 ? LYS B 156 ASN B 159 5 ? 4 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A LEU 65 C  ? ? ? 1_555 A CRF 66 N1 ? ? A LEU 64 A CRF 65 1_555 ? ? ? ? ? ? ? 1.539 ? ? 
covale2 covale both ? A CRF 66 C3 ? ? ? 1_555 A MET 67 N  ? ? A CRF 65 A MET 68 1_555 ? ? ? ? ? ? ? 1.336 ? ? 
covale3 covale both ? B CRF 66 C3 ? ? ? 1_555 B MET 67 N  ? ? B CRF 65 B MET 68 1_555 ? ? ? ? ? ? ? 1.344 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CRF A 66 ? . . . . CRF A 65 ? 1_555 . . . . . . . 'THR, TRP, GLY' 1 CRF None Chromophore/chromophore-like 
2 CRF B 66 ? . . . . CRF B 65 ? 1_555 . . . . . . . 'THR, TRP, GLY' 1 CRF None Chromophore/chromophore-like 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 MET 87 A . ? MET 88 A PRO 88 A ? PRO 89 A 1 12.47 
2 MET 87 B . ? MET 88 B PRO 88 B ? PRO 89 B 1 2.52  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 12 ? 
AA2 ? 12 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA1 4  5  ? anti-parallel 
AA1 5  6  ? anti-parallel 
AA1 6  7  ? anti-parallel 
AA1 7  8  ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 11 ? anti-parallel 
AA1 11 12 ? parallel      
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 4  5  ? anti-parallel 
AA2 5  6  ? anti-parallel 
AA2 6  7  ? anti-parallel 
AA2 7  8  ? anti-parallel 
AA2 8  9  ? anti-parallel 
AA2 9  10 ? anti-parallel 
AA2 10 11 ? anti-parallel 
AA2 11 12 ? 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  VAL A 13  ? VAL A 23  ? VAL A 12  VAL A 22  
AA1 2  HIS A 26  ? ASP A 37  ? HIS A 25  ASP A 36  
AA1 3  LYS A 42  ? CYS A 49  ? LYS A 41  CYS A 48  
AA1 4  HIS A 216 ? ALA A 226 ? HIS A 217 ALA A 227 
AA1 5  HIS A 198 ? SER A 207 ? HIS A 199 SER A 208 
AA1 6  GLY A 147 ? ASP A 154 ? GLY A 148 ASP A 155 
AA1 7  GLY A 159 ? ASP A 169 ? GLY A 160 ASP A 170 
AA1 8  VAL A 175 ? PRO A 186 ? VAL A 176 PRO A 187 
AA1 9  TYR A 91  ? PHE A 99  ? TYR A 92  PHE A 100 
AA1 10 ASN A 104 ? GLU A 114 ? ASN A 105 GLU A 115 
AA1 11 THR A 117 ? VAL A 127 ? THR A 118 VAL A 128 
AA1 12 VAL A 13  ? VAL A 23  ? VAL A 12  VAL A 22  
AA2 1  VAL B 13  ? VAL B 23  ? VAL B 12  VAL B 22  
AA2 2  HIS B 26  ? ASP B 37  ? HIS B 25  ASP B 36  
AA2 3  LYS B 42  ? CYS B 49  ? LYS B 41  CYS B 48  
AA2 4  HIS B 216 ? ALA B 226 ? HIS B 217 ALA B 227 
AA2 5  HIS B 198 ? SER B 207 ? HIS B 199 SER B 208 
AA2 6  GLY B 147 ? ASP B 154 ? GLY B 148 ASP B 155 
AA2 7  GLY B 159 ? ASP B 169 ? GLY B 160 ASP B 170 
AA2 8  VAL B 175 ? PRO B 186 ? VAL B 176 PRO B 187 
AA2 9  TYR B 91  ? PHE B 99  ? TYR B 92  PHE B 100 
AA2 10 ASN B 104 ? GLU B 114 ? ASN B 105 GLU B 115 
AA2 11 THR B 117 ? VAL B 127 ? THR B 118 VAL B 128 
AA2 12 VAL B 13  ? VAL B 23  ? VAL B 12  VAL B 22  
# 
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 GLY A 21  ? N GLY A 20  O PHE A 28  ? O PHE A 27  
AA1 2  3  N ASP A 37  ? N ASP A 36  O LYS A 42  ? O LYS A 41  
AA1 3  4  N PHE A 47  ? N PHE A 46  O MET A 217 ? O MET A 218 
AA1 4  5  O PHE A 222 ? O PHE A 223 N GLN A 203 ? N GLN A 204 
AA1 5  6  O THR A 202 ? O THR A 203 N GLY A 147 ? N GLY A 148 
AA1 6  7  N ASP A 154 ? N ASP A 155 O GLY A 159 ? O GLY A 160 
AA1 7  8  N PHE A 164 ? N PHE A 165 O HIS A 180 ? O HIS A 181 
AA1 8  9  O THR A 185 ? O THR A 186 N VAL A 92  ? N VAL A 93  
AA1 9  10 N ILE A 97  ? N ILE A 98  O TYR A 105 ? O TYR A 106 
AA1 10 11 N LYS A 112 ? N LYS A 113 O VAL A 119 ? O VAL A 120 
AA1 11 12 O ILE A 122 ? O ILE A 123 N GLU A 18  ? N GLU A 17  
AA2 1  2  N VAL B 13  ? N VAL B 12  O GLY B 36  ? O GLY B 35  
AA2 2  3  N ASP B 37  ? N ASP B 36  O LYS B 42  ? O LYS B 41  
AA2 3  4  N PHE B 47  ? N PHE B 46  O MET B 217 ? O MET B 218 
AA2 4  5  O THR B 224 ? O THR B 225 N SER B 201 ? N SER B 202 
AA2 5  6  O HIS B 198 ? O HIS B 199 N ILE B 151 ? N ILE B 152 
AA2 6  7  N THR B 152 ? N THR B 153 O LYS B 161 ? O LYS B 162 
AA2 7  8  N PHE B 164 ? N PHE B 165 O HIS B 180 ? O HIS B 181 
AA2 8  9  O GLN B 183 ? O GLN B 184 N GLU B 94  ? N GLU B 95  
AA2 9  10 N TYR B 91  ? N TYR B 92  O VAL B 111 ? O VAL B 112 
AA2 10 11 N LYS B 112 ? N LYS B 113 O VAL B 119 ? O VAL B 120 
AA2 11 12 O GLY B 126 ? O GLY B 127 N ASP B 22  ? N ASP B 21  
# 
_pdbx_entry_details.entry_id                   9FGI 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 C  B LEU 64 ? ? N1  B CRF 65  ? ? 1.66 
2 1 CE A LYS 61 ? ? OE1 A GLN 207 ? ? 2.09 
3 1 CE B LYS 61 ? ? OE1 B GLN 207 ? ? 2.15 
4 1 NZ B LYS 61 ? ? OE1 B GLN 207 ? ? 2.15 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              231 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             C 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_2              231 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             O 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              231 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                99.43 
_pdbx_validate_rmsd_angle.angle_target_value         120.10 
_pdbx_validate_rmsd_angle.angle_deviation            -20.67 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.10 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ILE A 136 ? ? -92.99  -64.39 
2 1 ASP A 155 ? ? -119.52 74.63  
3 1 ILE B 136 ? ? -90.27  -62.20 
4 1 ASP B 155 ? ? -109.85 74.81  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 ARG A 96 ? ? THR A 97 ? ? 147.32 
2 1 ARG B 96 ? ? THR B 97 ? ? 148.01 
# 
_pdbx_validate_polymer_linkage.id               1 
_pdbx_validate_polymer_linkage.PDB_model_num    1 
_pdbx_validate_polymer_linkage.auth_atom_id_1   C 
_pdbx_validate_polymer_linkage.auth_asym_id_1   B 
_pdbx_validate_polymer_linkage.auth_comp_id_1   LEU 
_pdbx_validate_polymer_linkage.auth_seq_id_1    64 
_pdbx_validate_polymer_linkage.PDB_ins_code_1   ? 
_pdbx_validate_polymer_linkage.label_alt_id_1   ? 
_pdbx_validate_polymer_linkage.auth_atom_id_2   N1 
_pdbx_validate_polymer_linkage.auth_asym_id_2   B 
_pdbx_validate_polymer_linkage.auth_comp_id_2   CRF 
_pdbx_validate_polymer_linkage.auth_seq_id_2    65 
_pdbx_validate_polymer_linkage.PDB_ins_code_2   ? 
_pdbx_validate_polymer_linkage.label_alt_id_2   ? 
_pdbx_validate_polymer_linkage.dist             1.66 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 0   ? A MET 1   
2  1 Y 1 A VAL 1   ? A VAL 2   
3  1 Y 1 A GLY 232 ? A GLY 231 
4  1 Y 1 A ALA 233 ? A ALA 232 
5  1 Y 1 A ASP 234 ? A ASP 233 
6  1 Y 1 A GLU 235 ? A GLU 234 
7  1 Y 1 A LEU 236 ? A LEU 235 
8  1 Y 1 A TYR 237 ? A TYR 236 
9  1 Y 1 A LYS 238 ? A LYS 237 
10 1 Y 1 A HIS 239 ? A HIS 238 
11 1 Y 1 A HIS 240 ? A HIS 239 
12 1 Y 1 A HIS 241 ? A HIS 240 
13 1 Y 1 A HIS 242 ? A HIS 241 
14 1 Y 1 A HIS 243 ? A HIS 242 
15 1 Y 1 A HIS 244 ? A HIS 243 
16 1 Y 1 B GLY 232 ? B GLY 231 
17 1 Y 1 B ALA 233 ? B ALA 232 
18 1 Y 1 B ASP 234 ? B ASP 233 
19 1 Y 1 B GLU 235 ? B GLU 234 
20 1 Y 1 B LEU 236 ? B LEU 235 
21 1 Y 1 B TYR 237 ? B TYR 236 
22 1 Y 1 B LYS 238 ? B LYS 237 
23 1 Y 1 B HIS 239 ? B HIS 238 
24 1 Y 1 B HIS 240 ? B HIS 239 
25 1 Y 1 B HIS 241 ? B HIS 240 
26 1 Y 1 B HIS 242 ? B HIS 241 
27 1 Y 1 B HIS 243 ? B HIS 242 
28 1 Y 1 B HIS 244 ? B HIS 243 
# 
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  
CRF N1   N N N 74  
CRF CA1  C N R 75  
CRF CB1  C N R 76  
CRF CG1  C N N 77  
CRF OG1  O N N 78  
CRF C1   C N N 79  
CRF N2   N N N 80  
CRF N3   N N N 81  
CRF C2   C N N 82  
CRF O2   O N N 83  
CRF CA2  C N N 84  
CRF CA3  C N N 85  
CRF C3   C N N 86  
CRF O3   O N N 87  
CRF CB2  C N N 88  
CRF CG2  C Y N 89  
CRF CD1  C Y N 90  
CRF CD2  C Y N 91  
CRF CE2  C Y N 92  
CRF NE1  N Y N 93  
CRF CE3  C Y N 94  
CRF CZ2  C Y N 95  
CRF CZ3  C Y N 96  
CRF CH2  C Y N 97  
CRF H    H N N 98  
CRF H2   H N N 99  
CRF HA1  H N N 100 
CRF HB1  H N N 101 
CRF HG11 H N N 102 
CRF HG12 H N N 103 
CRF HG13 H N N 104 
CRF HOG  H N N 105 
CRF HA31 H N N 106 
CRF HA32 H N N 107 
CRF OXT  O N N 108 
CRF HB2  H N N 109 
CRF HD1  H N N 110 
CRF HE1  H N N 111 
CRF HE3  H N N 112 
CRF HZ2  H N N 113 
CRF HZ3  H N N 114 
CRF HH2  H N N 115 
CRF HXT  H N N 116 
CYS N    N N N 117 
CYS CA   C N R 118 
CYS C    C N N 119 
CYS O    O N N 120 
CYS CB   C N N 121 
CYS SG   S N N 122 
CYS OXT  O N N 123 
CYS H    H N N 124 
CYS H2   H N N 125 
CYS HA   H N N 126 
CYS HB2  H N N 127 
CYS HB3  H N N 128 
CYS HG   H N N 129 
CYS HXT  H N N 130 
GLN N    N N N 131 
GLN CA   C N S 132 
GLN C    C N N 133 
GLN O    O N N 134 
GLN CB   C N N 135 
GLN CG   C N N 136 
GLN CD   C N N 137 
GLN OE1  O N N 138 
GLN NE2  N N N 139 
GLN OXT  O N N 140 
GLN H    H N N 141 
GLN H2   H N N 142 
GLN HA   H N N 143 
GLN HB2  H N N 144 
GLN HB3  H N N 145 
GLN HG2  H N N 146 
GLN HG3  H N N 147 
GLN HE21 H N N 148 
GLN HE22 H N N 149 
GLN HXT  H N N 150 
GLU N    N N N 151 
GLU CA   C N S 152 
GLU C    C N N 153 
GLU O    O N N 154 
GLU CB   C N N 155 
GLU CG   C N N 156 
GLU CD   C N N 157 
GLU OE1  O N N 158 
GLU OE2  O N N 159 
GLU OXT  O N N 160 
GLU H    H N N 161 
GLU H2   H N N 162 
GLU HA   H N N 163 
GLU HB2  H N N 164 
GLU HB3  H N N 165 
GLU HG2  H N N 166 
GLU HG3  H N N 167 
GLU HE2  H N N 168 
GLU HXT  H N N 169 
GLY N    N N N 170 
GLY CA   C N N 171 
GLY C    C N N 172 
GLY O    O N N 173 
GLY OXT  O N N 174 
GLY H    H N N 175 
GLY H2   H N N 176 
GLY HA2  H N N 177 
GLY HA3  H N N 178 
GLY HXT  H N N 179 
HIS N    N N N 180 
HIS CA   C N S 181 
HIS C    C N N 182 
HIS O    O N N 183 
HIS CB   C N N 184 
HIS CG   C Y N 185 
HIS ND1  N Y N 186 
HIS CD2  C Y N 187 
HIS CE1  C Y N 188 
HIS NE2  N Y N 189 
HIS OXT  O N N 190 
HIS H    H N N 191 
HIS H2   H N N 192 
HIS HA   H N N 193 
HIS HB2  H N N 194 
HIS HB3  H N N 195 
HIS HD1  H N N 196 
HIS HD2  H N N 197 
HIS HE1  H N N 198 
HIS HE2  H N N 199 
HIS HXT  H N N 200 
HOH O    O N N 201 
HOH H1   H N N 202 
HOH H2   H N N 203 
ILE N    N N N 204 
ILE CA   C N S 205 
ILE C    C N N 206 
ILE O    O N N 207 
ILE CB   C N S 208 
ILE CG1  C N N 209 
ILE CG2  C N N 210 
ILE CD1  C N N 211 
ILE OXT  O N N 212 
ILE H    H N N 213 
ILE H2   H N N 214 
ILE HA   H N N 215 
ILE HB   H N N 216 
ILE HG12 H N N 217 
ILE HG13 H N N 218 
ILE HG21 H N N 219 
ILE HG22 H N N 220 
ILE HG23 H N N 221 
ILE HD11 H N N 222 
ILE HD12 H N N 223 
ILE HD13 H N N 224 
ILE HXT  H N N 225 
LEU N    N N N 226 
LEU CA   C N S 227 
LEU C    C N N 228 
LEU O    O N N 229 
LEU CB   C N N 230 
LEU CG   C N N 231 
LEU CD1  C N N 232 
LEU CD2  C N N 233 
LEU OXT  O N N 234 
LEU H    H N N 235 
LEU H2   H N N 236 
LEU HA   H N N 237 
LEU HB2  H N N 238 
LEU HB3  H N N 239 
LEU HG   H N N 240 
LEU HD11 H N N 241 
LEU HD12 H N N 242 
LEU HD13 H N N 243 
LEU HD21 H N N 244 
LEU HD22 H N N 245 
LEU HD23 H N N 246 
LEU HXT  H N N 247 
LYS N    N N N 248 
LYS CA   C N S 249 
LYS C    C N N 250 
LYS O    O N N 251 
LYS CB   C N N 252 
LYS CG   C N N 253 
LYS CD   C N N 254 
LYS CE   C N N 255 
LYS NZ   N N N 256 
LYS OXT  O N N 257 
LYS H    H N N 258 
LYS H2   H N N 259 
LYS HA   H N N 260 
LYS HB2  H N N 261 
LYS HB3  H N N 262 
LYS HG2  H N N 263 
LYS HG3  H N N 264 
LYS HD2  H N N 265 
LYS HD3  H N N 266 
LYS HE2  H N N 267 
LYS HE3  H N N 268 
LYS HZ1  H N N 269 
LYS HZ2  H N N 270 
LYS HZ3  H N N 271 
LYS HXT  H N N 272 
MET N    N N N 273 
MET CA   C N S 274 
MET C    C N N 275 
MET O    O N N 276 
MET CB   C N N 277 
MET CG   C N N 278 
MET SD   S N N 279 
MET CE   C N N 280 
MET OXT  O N N 281 
MET H    H N N 282 
MET H2   H N N 283 
MET HA   H N N 284 
MET HB2  H N N 285 
MET HB3  H N N 286 
MET HG2  H N N 287 
MET HG3  H N N 288 
MET HE1  H N N 289 
MET HE2  H N N 290 
MET HE3  H N N 291 
MET HXT  H N N 292 
PHE N    N N N 293 
PHE CA   C N S 294 
PHE C    C N N 295 
PHE O    O N N 296 
PHE CB   C N N 297 
PHE CG   C Y N 298 
PHE CD1  C Y N 299 
PHE CD2  C Y N 300 
PHE CE1  C Y N 301 
PHE CE2  C Y N 302 
PHE CZ   C Y N 303 
PHE OXT  O N N 304 
PHE H    H N N 305 
PHE H2   H N N 306 
PHE HA   H N N 307 
PHE HB2  H N N 308 
PHE HB3  H N N 309 
PHE HD1  H N N 310 
PHE HD2  H N N 311 
PHE HE1  H N N 312 
PHE HE2  H N N 313 
PHE HZ   H N N 314 
PHE HXT  H N N 315 
PRO N    N N N 316 
PRO CA   C N S 317 
PRO C    C N N 318 
PRO O    O N N 319 
PRO CB   C N N 320 
PRO CG   C N N 321 
PRO CD   C N N 322 
PRO OXT  O N N 323 
PRO H    H N N 324 
PRO HA   H N N 325 
PRO HB2  H N N 326 
PRO HB3  H N N 327 
PRO HG2  H N N 328 
PRO HG3  H N N 329 
PRO HD2  H N N 330 
PRO HD3  H N N 331 
PRO HXT  H N N 332 
SER N    N N N 333 
SER CA   C N S 334 
SER C    C N N 335 
SER O    O N N 336 
SER CB   C N N 337 
SER OG   O N N 338 
SER OXT  O N N 339 
SER H    H N N 340 
SER H2   H N N 341 
SER HA   H N N 342 
SER HB2  H N N 343 
SER HB3  H N N 344 
SER HG   H N N 345 
SER HXT  H N N 346 
THR N    N N N 347 
THR CA   C N S 348 
THR C    C N N 349 
THR O    O N N 350 
THR CB   C N R 351 
THR OG1  O N N 352 
THR CG2  C N N 353 
THR OXT  O N N 354 
THR H    H N N 355 
THR H2   H N N 356 
THR HA   H N N 357 
THR HB   H N N 358 
THR HG1  H N N 359 
THR HG21 H N N 360 
THR HG22 H N N 361 
THR HG23 H N N 362 
THR HXT  H N N 363 
TRP N    N N N 364 
TRP CA   C N S 365 
TRP C    C N N 366 
TRP O    O N N 367 
TRP CB   C N N 368 
TRP CG   C Y N 369 
TRP CD1  C Y N 370 
TRP CD2  C Y N 371 
TRP NE1  N Y N 372 
TRP CE2  C Y N 373 
TRP CE3  C Y N 374 
TRP CZ2  C Y N 375 
TRP CZ3  C Y N 376 
TRP CH2  C Y N 377 
TRP OXT  O N N 378 
TRP H    H N N 379 
TRP H2   H N N 380 
TRP HA   H N N 381 
TRP HB2  H N N 382 
TRP HB3  H N N 383 
TRP HD1  H N N 384 
TRP HE1  H N N 385 
TRP HE3  H N N 386 
TRP HZ2  H N N 387 
TRP HZ3  H N N 388 
TRP HH2  H N N 389 
TRP HXT  H N N 390 
TYR N    N N N 391 
TYR CA   C N S 392 
TYR C    C N N 393 
TYR O    O N N 394 
TYR CB   C N N 395 
TYR CG   C Y N 396 
TYR CD1  C Y N 397 
TYR CD2  C Y N 398 
TYR CE1  C Y N 399 
TYR CE2  C Y N 400 
TYR CZ   C Y N 401 
TYR OH   O N N 402 
TYR OXT  O N N 403 
TYR H    H N N 404 
TYR H2   H N N 405 
TYR HA   H N N 406 
TYR HB2  H N N 407 
TYR HB3  H N N 408 
TYR HD1  H N N 409 
TYR HD2  H N N 410 
TYR HE1  H N N 411 
TYR HE2  H N N 412 
TYR HH   H N N 413 
TYR HXT  H N N 414 
VAL N    N N N 415 
VAL CA   C N S 416 
VAL C    C N N 417 
VAL O    O N N 418 
VAL CB   C N N 419 
VAL CG1  C N N 420 
VAL CG2  C N N 421 
VAL OXT  O N N 422 
VAL H    H N N 423 
VAL H2   H N N 424 
VAL HA   H N N 425 
VAL HB   H N N 426 
VAL HG11 H N N 427 
VAL HG12 H N N 428 
VAL HG13 H N N 429 
VAL HG21 H N N 430 
VAL HG22 H N N 431 
VAL HG23 H N N 432 
VAL HXT  H N N 433 
# 
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  
CRF N1  CA1  sing N N 70  
CRF N1  H    sing N N 71  
CRF N1  H2   sing N N 72  
CRF CA1 CB1  sing N N 73  
CRF CA1 C1   sing N N 74  
CRF CA1 HA1  sing N N 75  
CRF CB1 CG1  sing N N 76  
CRF CB1 OG1  sing N N 77  
CRF CB1 HB1  sing N N 78  
CRF CG1 HG11 sing N N 79  
CRF CG1 HG12 sing N N 80  
CRF CG1 HG13 sing N N 81  
CRF OG1 HOG  sing N N 82  
CRF C1  N2   doub N N 83  
CRF C1  N3   sing N N 84  
CRF N2  CA2  sing N N 85  
CRF N3  C2   sing N N 86  
CRF N3  CA3  sing N N 87  
CRF C2  O2   doub N N 88  
CRF C2  CA2  sing N N 89  
CRF CA2 CB2  doub N Z 90  
CRF CA3 C3   sing N N 91  
CRF CA3 HA31 sing N N 92  
CRF CA3 HA32 sing N N 93  
CRF C3  O3   doub N N 94  
CRF C3  OXT  sing N N 95  
CRF CB2 CG2  sing N N 96  
CRF CB2 HB2  sing N N 97  
CRF CG2 CD1  doub Y N 98  
CRF CG2 CD2  sing Y N 99  
CRF CD1 NE1  sing Y N 100 
CRF CD1 HD1  sing N N 101 
CRF CD2 CE2  doub Y N 102 
CRF CD2 CE3  sing Y N 103 
CRF CE2 NE1  sing Y N 104 
CRF CE2 CZ2  sing Y N 105 
CRF NE1 HE1  sing N N 106 
CRF CE3 CZ3  doub Y N 107 
CRF CE3 HE3  sing N N 108 
CRF CZ2 CH2  doub Y N 109 
CRF CZ2 HZ2  sing N N 110 
CRF CZ3 CH2  sing Y N 111 
CRF CZ3 HZ3  sing N N 112 
CRF CH2 HH2  sing N N 113 
CRF OXT HXT  sing N N 114 
CYS N   CA   sing N N 115 
CYS N   H    sing N N 116 
CYS N   H2   sing N N 117 
CYS CA  C    sing N N 118 
CYS CA  CB   sing N N 119 
CYS CA  HA   sing N N 120 
CYS C   O    doub N N 121 
CYS C   OXT  sing N N 122 
CYS CB  SG   sing N N 123 
CYS CB  HB2  sing N N 124 
CYS CB  HB3  sing N N 125 
CYS SG  HG   sing N N 126 
CYS OXT HXT  sing N N 127 
GLN N   CA   sing N N 128 
GLN N   H    sing N N 129 
GLN N   H2   sing N N 130 
GLN CA  C    sing N N 131 
GLN CA  CB   sing N N 132 
GLN CA  HA   sing N N 133 
GLN C   O    doub N N 134 
GLN C   OXT  sing N N 135 
GLN CB  CG   sing N N 136 
GLN CB  HB2  sing N N 137 
GLN CB  HB3  sing N N 138 
GLN CG  CD   sing N N 139 
GLN CG  HG2  sing N N 140 
GLN CG  HG3  sing N N 141 
GLN CD  OE1  doub N N 142 
GLN CD  NE2  sing N N 143 
GLN NE2 HE21 sing N N 144 
GLN NE2 HE22 sing N N 145 
GLN OXT HXT  sing N N 146 
GLU N   CA   sing N N 147 
GLU N   H    sing N N 148 
GLU N   H2   sing N N 149 
GLU CA  C    sing N N 150 
GLU CA  CB   sing N N 151 
GLU CA  HA   sing N N 152 
GLU C   O    doub N N 153 
GLU C   OXT  sing N N 154 
GLU CB  CG   sing N N 155 
GLU CB  HB2  sing N N 156 
GLU CB  HB3  sing N N 157 
GLU CG  CD   sing N N 158 
GLU CG  HG2  sing N N 159 
GLU CG  HG3  sing N N 160 
GLU CD  OE1  doub N N 161 
GLU CD  OE2  sing N N 162 
GLU OE2 HE2  sing N N 163 
GLU OXT HXT  sing N N 164 
GLY N   CA   sing N N 165 
GLY N   H    sing N N 166 
GLY N   H2   sing N N 167 
GLY CA  C    sing N N 168 
GLY CA  HA2  sing N N 169 
GLY CA  HA3  sing N N 170 
GLY C   O    doub N N 171 
GLY C   OXT  sing N N 172 
GLY OXT HXT  sing N N 173 
HIS N   CA   sing N N 174 
HIS N   H    sing N N 175 
HIS N   H2   sing N N 176 
HIS CA  C    sing N N 177 
HIS CA  CB   sing N N 178 
HIS CA  HA   sing N N 179 
HIS C   O    doub N N 180 
HIS C   OXT  sing N N 181 
HIS CB  CG   sing N N 182 
HIS CB  HB2  sing N N 183 
HIS CB  HB3  sing N N 184 
HIS CG  ND1  sing Y N 185 
HIS CG  CD2  doub Y N 186 
HIS ND1 CE1  doub Y N 187 
HIS ND1 HD1  sing N N 188 
HIS CD2 NE2  sing Y N 189 
HIS CD2 HD2  sing N N 190 
HIS CE1 NE2  sing Y N 191 
HIS CE1 HE1  sing N N 192 
HIS NE2 HE2  sing N N 193 
HIS OXT HXT  sing N N 194 
HOH O   H1   sing N N 195 
HOH O   H2   sing N N 196 
ILE N   CA   sing N N 197 
ILE N   H    sing N N 198 
ILE N   H2   sing N N 199 
ILE CA  C    sing N N 200 
ILE CA  CB   sing N N 201 
ILE CA  HA   sing N N 202 
ILE C   O    doub N N 203 
ILE C   OXT  sing N N 204 
ILE CB  CG1  sing N N 205 
ILE CB  CG2  sing N N 206 
ILE CB  HB   sing N N 207 
ILE CG1 CD1  sing N N 208 
ILE CG1 HG12 sing N N 209 
ILE CG1 HG13 sing N N 210 
ILE CG2 HG21 sing N N 211 
ILE CG2 HG22 sing N N 212 
ILE CG2 HG23 sing N N 213 
ILE CD1 HD11 sing N N 214 
ILE CD1 HD12 sing N N 215 
ILE CD1 HD13 sing N N 216 
ILE OXT HXT  sing N N 217 
LEU N   CA   sing N N 218 
LEU N   H    sing N N 219 
LEU N   H2   sing N N 220 
LEU CA  C    sing N N 221 
LEU CA  CB   sing N N 222 
LEU CA  HA   sing N N 223 
LEU C   O    doub N N 224 
LEU C   OXT  sing N N 225 
LEU CB  CG   sing N N 226 
LEU CB  HB2  sing N N 227 
LEU CB  HB3  sing N N 228 
LEU CG  CD1  sing N N 229 
LEU CG  CD2  sing N N 230 
LEU CG  HG   sing N N 231 
LEU CD1 HD11 sing N N 232 
LEU CD1 HD12 sing N N 233 
LEU CD1 HD13 sing N N 234 
LEU CD2 HD21 sing N N 235 
LEU CD2 HD22 sing N N 236 
LEU CD2 HD23 sing N N 237 
LEU OXT HXT  sing N N 238 
LYS N   CA   sing N N 239 
LYS N   H    sing N N 240 
LYS N   H2   sing N N 241 
LYS CA  C    sing N N 242 
LYS CA  CB   sing N N 243 
LYS CA  HA   sing N N 244 
LYS C   O    doub N N 245 
LYS C   OXT  sing N N 246 
LYS CB  CG   sing N N 247 
LYS CB  HB2  sing N N 248 
LYS CB  HB3  sing N N 249 
LYS CG  CD   sing N N 250 
LYS CG  HG2  sing N N 251 
LYS CG  HG3  sing N N 252 
LYS CD  CE   sing N N 253 
LYS CD  HD2  sing N N 254 
LYS CD  HD3  sing N N 255 
LYS CE  NZ   sing N N 256 
LYS CE  HE2  sing N N 257 
LYS CE  HE3  sing N N 258 
LYS NZ  HZ1  sing N N 259 
LYS NZ  HZ2  sing N N 260 
LYS NZ  HZ3  sing N N 261 
LYS OXT HXT  sing N N 262 
MET N   CA   sing N N 263 
MET N   H    sing N N 264 
MET N   H2   sing N N 265 
MET CA  C    sing N N 266 
MET CA  CB   sing N N 267 
MET CA  HA   sing N N 268 
MET C   O    doub N N 269 
MET C   OXT  sing N N 270 
MET CB  CG   sing N N 271 
MET CB  HB2  sing N N 272 
MET CB  HB3  sing N N 273 
MET CG  SD   sing N N 274 
MET CG  HG2  sing N N 275 
MET CG  HG3  sing N N 276 
MET SD  CE   sing N N 277 
MET CE  HE1  sing N N 278 
MET CE  HE2  sing N N 279 
MET CE  HE3  sing N N 280 
MET OXT HXT  sing N N 281 
PHE N   CA   sing N N 282 
PHE N   H    sing N N 283 
PHE N   H2   sing N N 284 
PHE CA  C    sing N N 285 
PHE CA  CB   sing N N 286 
PHE CA  HA   sing N N 287 
PHE C   O    doub N N 288 
PHE C   OXT  sing N N 289 
PHE CB  CG   sing N N 290 
PHE CB  HB2  sing N N 291 
PHE CB  HB3  sing N N 292 
PHE CG  CD1  doub Y N 293 
PHE CG  CD2  sing Y N 294 
PHE CD1 CE1  sing Y N 295 
PHE CD1 HD1  sing N N 296 
PHE CD2 CE2  doub Y N 297 
PHE CD2 HD2  sing N N 298 
PHE CE1 CZ   doub Y N 299 
PHE CE1 HE1  sing N N 300 
PHE CE2 CZ   sing Y N 301 
PHE CE2 HE2  sing N N 302 
PHE CZ  HZ   sing N N 303 
PHE OXT HXT  sing N N 304 
PRO N   CA   sing N N 305 
PRO N   CD   sing N N 306 
PRO N   H    sing N N 307 
PRO CA  C    sing N N 308 
PRO CA  CB   sing N N 309 
PRO CA  HA   sing N N 310 
PRO C   O    doub N N 311 
PRO C   OXT  sing N N 312 
PRO CB  CG   sing N N 313 
PRO CB  HB2  sing N N 314 
PRO CB  HB3  sing N N 315 
PRO CG  CD   sing N N 316 
PRO CG  HG2  sing N N 317 
PRO CG  HG3  sing N N 318 
PRO CD  HD2  sing N N 319 
PRO CD  HD3  sing N N 320 
PRO OXT HXT  sing N N 321 
SER N   CA   sing N N 322 
SER N   H    sing N N 323 
SER N   H2   sing N N 324 
SER CA  C    sing N N 325 
SER CA  CB   sing N N 326 
SER CA  HA   sing N N 327 
SER C   O    doub N N 328 
SER C   OXT  sing N N 329 
SER CB  OG   sing N N 330 
SER CB  HB2  sing N N 331 
SER CB  HB3  sing N N 332 
SER OG  HG   sing N N 333 
SER OXT HXT  sing N N 334 
THR N   CA   sing N N 335 
THR N   H    sing N N 336 
THR N   H2   sing N N 337 
THR CA  C    sing N N 338 
THR CA  CB   sing N N 339 
THR CA  HA   sing N N 340 
THR C   O    doub N N 341 
THR C   OXT  sing N N 342 
THR CB  OG1  sing N N 343 
THR CB  CG2  sing N N 344 
THR CB  HB   sing N N 345 
THR OG1 HG1  sing N N 346 
THR CG2 HG21 sing N N 347 
THR CG2 HG22 sing N N 348 
THR CG2 HG23 sing N N 349 
THR OXT HXT  sing N N 350 
TRP N   CA   sing N N 351 
TRP N   H    sing N N 352 
TRP N   H2   sing N N 353 
TRP CA  C    sing N N 354 
TRP CA  CB   sing N N 355 
TRP CA  HA   sing N N 356 
TRP C   O    doub N N 357 
TRP C   OXT  sing N N 358 
TRP CB  CG   sing N N 359 
TRP CB  HB2  sing N N 360 
TRP CB  HB3  sing N N 361 
TRP CG  CD1  doub Y N 362 
TRP CG  CD2  sing Y N 363 
TRP CD1 NE1  sing Y N 364 
TRP CD1 HD1  sing N N 365 
TRP CD2 CE2  doub Y N 366 
TRP CD2 CE3  sing Y N 367 
TRP NE1 CE2  sing Y N 368 
TRP NE1 HE1  sing N N 369 
TRP CE2 CZ2  sing Y N 370 
TRP CE3 CZ3  doub Y N 371 
TRP CE3 HE3  sing N N 372 
TRP CZ2 CH2  doub Y N 373 
TRP CZ2 HZ2  sing N N 374 
TRP CZ3 CH2  sing Y N 375 
TRP CZ3 HZ3  sing N N 376 
TRP CH2 HH2  sing N N 377 
TRP OXT HXT  sing N N 378 
TYR N   CA   sing N N 379 
TYR N   H    sing N N 380 
TYR N   H2   sing N N 381 
TYR CA  C    sing N N 382 
TYR CA  CB   sing N N 383 
TYR CA  HA   sing N N 384 
TYR C   O    doub N N 385 
TYR C   OXT  sing N N 386 
TYR CB  CG   sing N N 387 
TYR CB  HB2  sing N N 388 
TYR CB  HB3  sing N N 389 
TYR CG  CD1  doub Y N 390 
TYR CG  CD2  sing Y N 391 
TYR CD1 CE1  sing Y N 392 
TYR CD1 HD1  sing N N 393 
TYR CD2 CE2  doub Y N 394 
TYR CD2 HD2  sing N N 395 
TYR CE1 CZ   doub Y N 396 
TYR CE1 HE1  sing N N 397 
TYR CE2 CZ   sing Y N 398 
TYR CE2 HE2  sing N N 399 
TYR CZ  OH   sing N N 400 
TYR OH  HH   sing N N 401 
TYR OXT HXT  sing N N 402 
VAL N   CA   sing N N 403 
VAL N   H    sing N N 404 
VAL N   H2   sing N N 405 
VAL CA  C    sing N N 406 
VAL CA  CB   sing N N 407 
VAL CA  HA   sing N N 408 
VAL C   O    doub N N 409 
VAL C   OXT  sing N N 410 
VAL CB  CG1  sing N N 411 
VAL CB  CG2  sing N N 412 
VAL CB  HB   sing N N 413 
VAL CG1 HG11 sing N N 414 
VAL CG1 HG12 sing N N 415 
VAL CG1 HG13 sing N N 416 
VAL CG2 HG21 sing N N 417 
VAL CG2 HG22 sing N N 418 
VAL CG2 HG23 sing N N 419 
VAL OXT HXT  sing N N 420 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Ministry of Education, Youth and Sports of the Czech Republic' 'Czech Republic' CZ.02.1.01/0.0/0.0/16_019/0000729 1 
'Czech Science Foundation'                                      'Czech Republic' 23-05983S                         2 
# 
_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   4rys 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9FGI 
_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]   0.019508 
_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]   0.019459 
_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]   0.005109 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
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   . SER A 1 3   ? 16.914  9.718   60.010  1.00 63.20  ? 2   SER A N   1 
ATOM   2    C CA  . SER A 1 3   ? 15.736  10.480  59.435  1.00 60.92  ? 2   SER A CA  1 
ATOM   3    C C   . SER A 1 3   ? 14.397  9.805   59.800  1.00 64.12  ? 2   SER A C   1 
ATOM   4    O O   . SER A 1 3   ? 14.340  8.537   59.891  1.00 59.69  ? 2   SER A O   1 
ATOM   5    C CB  . SER A 1 3   ? 15.864  10.677  57.902  1.00 69.45  ? 2   SER A CB  1 
ATOM   6    O OG  . SER A 1 3   ? 14.651  11.184  57.311  1.00 53.85  ? 2   SER A OG  1 
ATOM   7    N N   . LYS A 1 4   ? 13.355  10.642  59.940  1.00 61.47  ? 3   LYS A N   1 
ATOM   8    C CA  . LYS A 1 4   ? 11.973  10.276  60.353  1.00 59.64  ? 3   LYS A CA  1 
ATOM   9    C C   . LYS A 1 4   ? 10.987  10.735  59.253  1.00 49.15  ? 3   LYS A C   1 
ATOM   10   O O   . LYS A 1 4   ? 9.802   10.883  59.509  1.00 43.50  ? 3   LYS A O   1 
ATOM   11   C CB  . LYS A 1 4   ? 11.707  10.903  61.724  1.00 84.21  ? 3   LYS A CB  1 
ATOM   12   C CG  . LYS A 1 4   ? 12.323  12.285  61.946  1.00 98.79  ? 3   LYS A CG  1 
ATOM   13   C CD  . LYS A 1 4   ? 12.487  12.686  63.419  1.00 107.81 ? 3   LYS A CD  1 
ATOM   14   C CE  . LYS A 1 4   ? 11.454  13.683  63.915  1.00 110.65 ? 3   LYS A CE  1 
ATOM   15   N NZ  . LYS A 1 4   ? 10.090  13.099  63.948  1.00 120.65 ? 3   LYS A NZ  1 
ATOM   16   N N   . GLY A 1 5   ? 11.475  10.882  58.015  1.00 44.12  ? 4   GLY A N   1 
ATOM   17   C CA  . GLY A 1 5   ? 10.637  11.155  56.821  1.00 42.60  ? 4   GLY A CA  1 
ATOM   18   C C   . GLY A 1 5   ? 9.503   10.161  56.653  1.00 40.75  ? 4   GLY A C   1 
ATOM   19   O O   . GLY A 1 5   ? 8.421   10.570  56.202  1.00 39.36  ? 4   GLY A O   1 
ATOM   20   N N   . GLU A 1 6   ? 9.713   8.904   57.051  1.00 43.37  ? 5   GLU A N   1 
ATOM   21   C CA  . GLU A 1 6   ? 8.740   7.792   56.905  1.00 43.25  ? 5   GLU A CA  1 
ATOM   22   C C   . GLU A 1 6   ? 7.443   8.165   57.627  1.00 40.36  ? 5   GLU A C   1 
ATOM   23   O O   . GLU A 1 6   ? 6.357   7.803   57.126  1.00 35.76  ? 5   GLU A O   1 
ATOM   24   C CB  . GLU A 1 6   ? 9.380   6.458   57.339  1.00 52.21  ? 5   GLU A CB  1 
ATOM   25   C CG  . GLU A 1 6   ? 9.584   6.276   58.851  1.00 67.04  ? 5   GLU A CG  1 
ATOM   26   C CD  . GLU A 1 6   ? 10.699  7.056   59.574  1.00 76.16  ? 5   GLU A CD  1 
ATOM   27   O OE1 . GLU A 1 6   ? 11.746  7.341   58.965  1.00 64.22  ? 5   GLU A OE1 1 
ATOM   28   O OE2 . GLU A 1 6   ? 10.516  7.406   60.769  1.00 87.29  ? 5   GLU A OE2 1 
ATOM   29   N N   . LYS A 1 7   ? 7.527   8.867   58.768  1.00 42.10  ? 6   LYS A N   1 
ATOM   30   C CA  . LYS A 1 7   ? 6.317   9.153   59.603  1.00 43.24  ? 6   LYS A CA  1 
ATOM   31   C C   . LYS A 1 7   ? 5.379   10.092  58.862  1.00 40.62  ? 6   LYS A C   1 
ATOM   32   O O   . LYS A 1 7   ? 4.176   10.073  59.164  1.00 40.62  ? 6   LYS A O   1 
ATOM   33   C CB  . LYS A 1 7   ? 6.667   9.778   60.960  1.00 43.46  ? 6   LYS A CB  1 
ATOM   34   C CG  . LYS A 1 7   ? 7.470   8.862   61.862  1.00 51.60  ? 6   LYS A CG  1 
ATOM   35   C CD  . LYS A 1 7   ? 8.014   9.615   63.097  1.00 62.51  ? 6   LYS A CD  1 
ATOM   36   C CE  . LYS A 1 7   ? 9.281   8.989   63.636  1.00 65.28  ? 6   LYS A CE  1 
ATOM   37   N NZ  . LYS A 1 7   ? 9.042   7.564   63.935  1.00 67.84  ? 6   LYS A NZ  1 
ATOM   38   N N   . LEU A 1 8   ? 5.893   10.847  57.897  1.00 36.11  ? 7   LEU A N   1 
ATOM   39   C CA  . LEU A 1 8   ? 5.110   11.826  57.117  1.00 37.53  ? 7   LEU A CA  1 
ATOM   40   C C   . LEU A 1 8   ? 4.139   11.093  56.192  1.00 35.80  ? 7   LEU A C   1 
ATOM   41   O O   . LEU A 1 8   ? 3.275   11.811  55.641  1.00 34.73  ? 7   LEU A O   1 
ATOM   42   C CB  . LEU A 1 8   ? 6.042   12.729  56.291  1.00 33.18  ? 7   LEU A CB  1 
ATOM   43   C CG  . LEU A 1 8   ? 6.991   13.590  57.115  1.00 41.46  ? 7   LEU A CG  1 
ATOM   44   C CD1 . LEU A 1 8   ? 7.935   14.350  56.205  1.00 39.30  ? 7   LEU A CD1 1 
ATOM   45   C CD2 . LEU A 1 8   ? 6.245   14.561  58.022  1.00 45.68  ? 7   LEU A CD2 1 
ATOM   46   N N   . PHE A 1 9   ? 4.310   9.769   55.988  1.00 32.63  ? 8   PHE A N   1 
ATOM   47   C CA  . PHE A 1 9   ? 3.533   8.998   54.976  1.00 30.24  ? 8   PHE A CA  1 
ATOM   48   C C   . PHE A 1 9   ? 2.571   7.975   55.570  1.00 30.65  ? 8   PHE A C   1 
ATOM   49   O O   . PHE A 1 9   ? 2.031   7.217   54.765  1.00 34.49  ? 8   PHE A O   1 
ATOM   50   C CB  . PHE A 1 9   ? 4.455   8.321   53.942  1.00 31.81  ? 8   PHE A CB  1 
ATOM   51   C CG  . PHE A 1 9   ? 5.210   9.318   53.097  1.00 32.46  ? 8   PHE A CG  1 
ATOM   52   C CD1 . PHE A 1 9   ? 6.411   9.849   53.533  1.00 34.30  ? 8   PHE A CD1 1 
ATOM   53   C CD2 . PHE A 1 9   ? 4.697   9.737   51.889  1.00 31.28  ? 8   PHE A CD2 1 
ATOM   54   C CE1 . PHE A 1 9   ? 7.088   10.798  52.776  1.00 30.49  ? 8   PHE A CE1 1 
ATOM   55   C CE2 . PHE A 1 9   ? 5.404   10.634  51.104  1.00 34.50  ? 8   PHE A CE2 1 
ATOM   56   C CZ  . PHE A 1 9   ? 6.588   11.150  51.535  1.00 30.28  ? 8   PHE A CZ  1 
ATOM   57   N N   . THR A 1 10  ? 2.302   7.955   56.893  1.00 35.94  ? 9   THR A N   1 
ATOM   58   C CA  . THR A 1 10  ? 1.466   6.878   57.509  1.00 34.64  ? 9   THR A CA  1 
ATOM   59   C C   . THR A 1 10  ? 0.009   7.124   57.198  1.00 34.25  ? 9   THR A C   1 
ATOM   60   O O   . THR A 1 10  ? -0.801  6.139   57.263  1.00 37.50  ? 9   THR A O   1 
ATOM   61   C CB  . THR A 1 10  ? 1.724   6.777   59.018  1.00 41.20  ? 9   THR A CB  1 
ATOM   62   O OG1 . THR A 1 10  ? 1.549   8.101   59.483  1.00 36.93  ? 9   THR A OG1 1 
ATOM   63   C CG2 . THR A 1 10  ? 3.136   6.347   59.364  1.00 42.46  ? 9   THR A CG2 1 
ATOM   64   N N   . GLY A 1 11  ? -0.329  8.358   56.869  1.00 36.39  ? 10  GLY A N   1 
ATOM   65   C CA  . GLY A 1 11  ? -1.713  8.745   56.562  1.00 38.89  ? 10  GLY A CA  1 
ATOM   66   C C   . GLY A 1 11  ? -1.904  9.002   55.077  1.00 39.12  ? 10  GLY A C   1 
ATOM   67   O O   . GLY A 1 11  ? -1.028  8.674   54.258  1.00 36.65  ? 10  GLY A O   1 
ATOM   68   N N   . VAL A 1 12  ? -3.034  9.575   54.732  1.00 37.96  ? 11  VAL A N   1 
ATOM   69   C CA  . VAL A 1 12  ? -3.332  10.013  53.336  1.00 35.52  ? 11  VAL A CA  1 
ATOM   70   C C   . VAL A 1 12  ? -2.717  11.418  53.148  1.00 36.17  ? 11  VAL A C   1 
ATOM   71   O O   . VAL A 1 12  ? -2.991  12.316  53.919  1.00 33.71  ? 11  VAL A O   1 
ATOM   72   C CB  . VAL A 1 12  ? -4.847  10.006  53.155  1.00 36.50  ? 11  VAL A CB  1 
ATOM   73   C CG1 . VAL A 1 12  ? -5.224  10.489  51.747  1.00 43.19  ? 11  VAL A CG1 1 
ATOM   74   C CG2 . VAL A 1 12  ? -5.436  8.623   53.479  1.00 39.90  ? 11  VAL A CG2 1 
ATOM   75   N N   . VAL A 1 13  ? -1.914  11.600  52.126  1.00 32.90  ? 12  VAL A N   1 
ATOM   76   C CA  . VAL A 1 13  ? -1.153  12.843  51.803  1.00 31.11  ? 12  VAL A CA  1 
ATOM   77   C C   . VAL A 1 13  ? -1.654  13.456  50.509  1.00 30.58  ? 12  VAL A C   1 
ATOM   78   O O   . VAL A 1 13  ? -1.727  12.770  49.460  1.00 29.64  ? 12  VAL A O   1 
ATOM   79   C CB  . VAL A 1 13  ? 0.329   12.507  51.719  1.00 31.82  ? 12  VAL A CB  1 
ATOM   80   C CG1 . VAL A 1 13  ? 1.176   13.722  51.375  1.00 34.86  ? 12  VAL A CG1 1 
ATOM   81   C CG2 . VAL A 1 13  ? 0.758   11.861  53.015  1.00 36.34  ? 12  VAL A CG2 1 
ATOM   82   N N   . PRO A 1 14  ? -2.091  14.730  50.539  1.00 29.46  ? 13  PRO A N   1 
ATOM   83   C CA  . PRO A 1 14  ? -2.465  15.427  49.313  1.00 29.90  ? 13  PRO A CA  1 
ATOM   84   C C   . PRO A 1 14  ? -1.216  15.586  48.436  1.00 28.51  ? 13  PRO A C   1 
ATOM   85   O O   . PRO A 1 14  ? -0.133  15.763  48.914  1.00 29.02  ? 13  PRO A O   1 
ATOM   86   C CB  . PRO A 1 14  ? -3.023  16.787  49.764  1.00 31.04  ? 13  PRO A CB  1 
ATOM   87   C CG  . PRO A 1 14  ? -3.401  16.548  51.200  1.00 37.81  ? 13  PRO A CG  1 
ATOM   88   C CD  . PRO A 1 14  ? -2.354  15.579  51.724  1.00 33.33  ? 13  PRO A CD  1 
ATOM   89   N N   . ILE A 1 15  ? -1.464  15.488  47.139  1.00 27.51  ? 14  ILE A N   1 
ATOM   90   C CA  . ILE A 1 15  ? -0.445  15.563  46.069  1.00 31.34  ? 14  ILE A CA  1 
ATOM   91   C C   . ILE A 1 15  ? -0.786  16.733  45.148  1.00 26.23  ? 14  ILE A C   1 
ATOM   92   O O   . ILE A 1 15  ? -1.963  16.824  44.716  1.00 29.65  ? 14  ILE A O   1 
ATOM   93   C CB  . ILE A 1 15  ? -0.402  14.258  45.284  1.00 28.45  ? 14  ILE A CB  1 
ATOM   94   C CG1 . ILE A 1 15  ? 0.042   13.121  46.198  1.00 28.69  ? 14  ILE A CG1 1 
ATOM   95   C CG2 . ILE A 1 15  ? 0.479   14.421  44.070  1.00 29.63  ? 14  ILE A CG2 1 
ATOM   96   C CD1 . ILE A 1 15  ? -0.075  11.766  45.569  1.00 27.70  ? 14  ILE A CD1 1 
ATOM   97   N N   . LEU A 1 16  ? 0.263   17.450  44.747  1.00 30.93  ? 15  LEU A N   1 
ATOM   98   C CA  . LEU A 1 16  ? 0.227   18.491  43.683  1.00 28.64  ? 15  LEU A CA  1 
ATOM   99   C C   . LEU A 1 16  ? 1.362   18.273  42.697  1.00 26.23  ? 15  LEU A C   1 
ATOM   100  O O   . LEU A 1 16  ? 2.517   18.072  43.104  1.00 28.92  ? 15  LEU A O   1 
ATOM   101  C CB  . LEU A 1 16  ? 0.348   19.867  44.330  1.00 28.46  ? 15  LEU A CB  1 
ATOM   102  C CG  . LEU A 1 16  ? 0.280   21.045  43.359  1.00 32.86  ? 15  LEU A CG  1 
ATOM   103  C CD1 . LEU A 1 16  ? -1.102  21.142  42.722  1.00 36.24  ? 15  LEU A CD1 1 
ATOM   104  C CD2 . LEU A 1 16  ? 0.624   22.379  44.074  1.00 33.96  ? 15  LEU A CD2 1 
ATOM   105  N N   . VAL A 1 17  ? 1.027   18.201  41.413  1.00 28.57  ? 16  VAL A N   1 
ATOM   106  C CA  . VAL A 1 17  ? 2.056   17.988  40.372  1.00 27.34  ? 16  VAL A CA  1 
ATOM   107  C C   . VAL A 1 17  ? 1.949   19.147  39.361  1.00 27.80  ? 16  VAL A C   1 
ATOM   108  O O   . VAL A 1 17  ? 0.861   19.542  39.056  1.00 28.17  ? 16  VAL A O   1 
ATOM   109  C CB  . VAL A 1 17  ? 1.890   16.618  39.668  1.00 30.20  ? 16  VAL A CB  1 
ATOM   110  C CG1 . VAL A 1 17  ? 3.045   16.355  38.738  1.00 32.01  ? 16  VAL A CG1 1 
ATOM   111  C CG2 . VAL A 1 17  ? 1.758   15.476  40.680  1.00 30.19  ? 16  VAL A CG2 1 
ATOM   112  N N   . GLU A 1 18  ? 3.098   19.633  38.914  1.00 32.16  ? 17  GLU A N   1 
ATOM   113  C CA  . GLU A 1 18  ? 3.266   20.709  37.922  1.00 32.49  ? 17  GLU A CA  1 
ATOM   114  C C   . GLU A 1 18  ? 4.369   20.239  36.992  1.00 31.97  ? 17  GLU A C   1 
ATOM   115  O O   . GLU A 1 18  ? 5.482   20.019  37.479  1.00 32.34  ? 17  GLU A O   1 
ATOM   116  C CB  . GLU A 1 18  ? 3.671   22.015  38.612  1.00 33.97  ? 17  GLU A CB  1 
ATOM   117  C CG  . GLU A 1 18  ? 2.479   22.559  39.373  1.00 41.35  ? 17  GLU A CG  1 
ATOM   118  C CD  . GLU A 1 18  ? 2.751   23.875  40.066  1.00 49.51  ? 17  GLU A CD  1 
ATOM   119  O OE1 . GLU A 1 18  ? 3.933   24.099  40.426  1.00 42.51  ? 17  GLU A OE1 1 
ATOM   120  O OE2 . GLU A 1 18  ? 1.755   24.630  40.301  1.00 48.67  ? 17  GLU A OE2 1 
ATOM   121  N N   . LEU A 1 19  ? 4.067   20.216  35.695  1.00 32.05  ? 18  LEU A N   1 
ATOM   122  C CA  . LEU A 1 19  ? 5.031   19.886  34.646  1.00 30.29  ? 18  LEU A CA  1 
ATOM   123  C C   . LEU A 1 19  ? 5.021   20.985  33.556  1.00 32.60  ? 18  LEU A C   1 
ATOM   124  O O   . LEU A 1 19  ? 3.917   21.338  33.080  1.00 36.16  ? 18  LEU A O   1 
ATOM   125  C CB  . LEU A 1 19  ? 4.679   18.542  34.044  1.00 31.28  ? 18  LEU A CB  1 
ATOM   126  C CG  . LEU A 1 19  ? 5.742   18.120  33.033  1.00 34.57  ? 18  LEU A CG  1 
ATOM   127  C CD1 . LEU A 1 19  ? 5.967   16.620  33.065  1.00 35.60  ? 18  LEU A CD1 1 
ATOM   128  C CD2 . LEU A 1 19  ? 5.290   18.588  31.682  1.00 35.62  ? 18  LEU A CD2 1 
ATOM   129  N N   . ASP A 1 20  ? 6.188   21.522  33.234  1.00 34.64  ? 19  ASP A N   1 
ATOM   130  C CA  . ASP A 1 20  ? 6.363   22.399  32.039  1.00 39.21  ? 19  ASP A CA  1 
ATOM   131  C C   . ASP A 1 20  ? 7.207   21.615  31.052  1.00 33.33  ? 19  ASP A C   1 
ATOM   132  O O   . ASP A 1 20  ? 8.313   21.189  31.423  1.00 34.51  ? 19  ASP A O   1 
ATOM   133  C CB  . ASP A 1 20  ? 7.043   23.735  32.346  1.00 42.24  ? 19  ASP A CB  1 
ATOM   134  C CG  . ASP A 1 20  ? 6.120   24.688  33.091  1.00 53.47  ? 19  ASP A CG  1 
ATOM   135  O OD1 . ASP A 1 20  ? 4.870   24.693  32.835  1.00 43.35  ? 19  ASP A OD1 1 
ATOM   136  O OD2 . ASP A 1 20  ? 6.643   25.439  33.910  1.00 64.51  ? 19  ASP A OD2 1 
ATOM   137  N N   . GLY A 1 21  ? 6.696   21.454  29.843  1.00 34.18  ? 20  GLY A N   1 
ATOM   138  C CA  . GLY A 1 21  ? 7.312   20.597  28.820  1.00 32.89  ? 20  GLY A CA  1 
ATOM   139  C C   . GLY A 1 21  ? 7.562   21.355  27.522  1.00 38.68  ? 20  GLY A C   1 
ATOM   140  O O   . GLY A 1 21  ? 6.812   22.314  27.171  1.00 37.49  ? 20  GLY A O   1 
ATOM   141  N N   . ASP A 1 22  ? 8.640   20.984  26.879  1.00 35.22  ? 21  ASP A N   1 
ATOM   142  C CA  . ASP A 1 22  ? 8.960   21.428  25.503  1.00 34.91  ? 21  ASP A CA  1 
ATOM   143  C C   . ASP A 1 22  ? 9.450   20.218  24.756  1.00 31.91  ? 21  ASP A C   1 
ATOM   144  O O   . ASP A 1 22  ? 10.543  19.721  25.096  1.00 42.06  ? 21  ASP A O   1 
ATOM   145  C CB  . ASP A 1 22  ? 10.000  22.548  25.561  1.00 39.83  ? 21  ASP A CB  1 
ATOM   146  C CG  . ASP A 1 22  ? 10.378  23.112  24.190  1.00 42.64  ? 21  ASP A CG  1 
ATOM   147  O OD1 . ASP A 1 22  ? 10.194  22.400  23.186  1.00 42.97  ? 21  ASP A OD1 1 
ATOM   148  O OD2 . ASP A 1 22  ? 10.871  24.231  24.176  1.00 48.77  ? 21  ASP A OD2 1 
ATOM   149  N N   . VAL A 1 23  ? 8.678   19.749  23.796  1.00 32.38  ? 22  VAL A N   1 
ATOM   150  C CA  . VAL A 1 23  ? 9.057   18.598  22.956  1.00 33.35  ? 22  VAL A CA  1 
ATOM   151  C C   . VAL A 1 23  ? 9.109   19.086  21.497  1.00 36.17  ? 22  VAL A C   1 
ATOM   152  O O   . VAL A 1 23  ? 8.015   19.359  20.929  1.00 39.45  ? 22  VAL A O   1 
ATOM   153  C CB  . VAL A 1 23  ? 8.090   17.438  23.157  1.00 34.68  ? 22  VAL A CB  1 
ATOM   154  C CG1 . VAL A 1 23  ? 8.384   16.358  22.163  1.00 34.07  ? 22  VAL A CG1 1 
ATOM   155  C CG2 . VAL A 1 23  ? 8.148   16.908  24.616  1.00 34.82  ? 22  VAL A CG2 1 
ATOM   156  N N   . ASN A 1 24  ? 10.323  19.206  20.948  1.00 42.05  ? 23  ASN A N   1 
ATOM   157  C CA  . ASN A 1 24  ? 10.557  19.709  19.555  1.00 39.23  ? 23  ASN A CA  1 
ATOM   158  C C   . ASN A 1 24  ? 9.883   21.079  19.374  1.00 38.13  ? 23  ASN A C   1 
ATOM   159  O O   . ASN A 1 24  ? 9.337   21.309  18.274  1.00 45.58  ? 23  ASN A O   1 
ATOM   160  C CB  . ASN A 1 24  ? 9.953   18.781  18.503  1.00 40.53  ? 23  ASN A CB  1 
ATOM   161  C CG  . ASN A 1 24  ? 10.757  17.549  18.139  1.00 39.62  ? 23  ASN A CG  1 
ATOM   162  O OD1 . ASN A 1 24  ? 11.529  17.007  18.942  1.00 40.74  ? 23  ASN A OD1 1 
ATOM   163  N ND2 . ASN A 1 24  ? 10.522  17.050  16.926  1.00 39.22  ? 23  ASN A ND2 1 
ATOM   164  N N   . GLY A 1 25  ? 9.885   21.924  20.389  1.00 38.98  ? 24  GLY A N   1 
ATOM   165  C CA  . GLY A 1 25  ? 9.349   23.297  20.409  1.00 41.32  ? 24  GLY A CA  1 
ATOM   166  C C   . GLY A 1 25  ? 7.849   23.329  20.570  1.00 44.18  ? 24  GLY A C   1 
ATOM   167  O O   . GLY A 1 25  ? 7.262   24.447  20.600  1.00 44.73  ? 24  GLY A O   1 
ATOM   168  N N   . HIS A 1 26  ? 7.180   22.187  20.742  1.00 42.66  ? 25  HIS A N   1 
ATOM   169  C CA  . HIS A 1 26  ? 5.762   22.220  21.202  1.00 40.71  ? 25  HIS A CA  1 
ATOM   170  C C   . HIS A 1 26  ? 5.816   22.399  22.729  1.00 39.83  ? 25  HIS A C   1 
ATOM   171  O O   . HIS A 1 26  ? 6.229   21.469  23.407  1.00 38.45  ? 25  HIS A O   1 
ATOM   172  C CB  . HIS A 1 26  ? 4.964   20.968  20.803  1.00 40.65  ? 25  HIS A CB  1 
ATOM   173  C CG  . HIS A 1 26  ? 5.092   20.520  19.384  1.00 47.74  ? 25  HIS A CG  1 
ATOM   174  N ND1 . HIS A 1 26  ? 4.108   20.787  18.424  1.00 51.84  ? 25  HIS A ND1 1 
ATOM   175  C CD2 . HIS A 1 26  ? 5.992   19.726  18.774  1.00 47.17  ? 25  HIS A CD2 1 
ATOM   176  C CE1 . HIS A 1 26  ? 4.424   20.185  17.300  1.00 49.62  ? 25  HIS A CE1 1 
ATOM   177  N NE2 . HIS A 1 26  ? 5.575   19.548  17.470  1.00 52.68  ? 25  HIS A NE2 1 
ATOM   178  N N   . LYS A 1 27  ? 5.445   23.562  23.231  1.00 37.34  ? 26  LYS A N   1 
ATOM   179  C CA  . LYS A 1 27  ? 5.450   23.944  24.656  1.00 42.85  ? 26  LYS A CA  1 
ATOM   180  C C   . LYS A 1 27  ? 4.110   23.545  25.253  1.00 40.28  ? 26  LYS A C   1 
ATOM   181  O O   . LYS A 1 27  ? 3.094   23.680  24.586  1.00 41.33  ? 26  LYS A O   1 
ATOM   182  C CB  . LYS A 1 27  ? 5.764   25.428  24.743  1.00 51.98  ? 26  LYS A CB  1 
ATOM   183  C CG  . LYS A 1 27  ? 7.070   25.785  24.078  1.00 55.61  ? 26  LYS A CG  1 
ATOM   184  C CD  . LYS A 1 27  ? 7.690   27.046  24.612  1.00 65.28  ? 26  LYS A CD  1 
ATOM   185  C CE  . LYS A 1 27  ? 9.187   27.038  24.441  1.00 77.02  ? 26  LYS A CE  1 
ATOM   186  N NZ  . LYS A 1 27  ? 9.871   27.609  25.627  1.00 88.36  ? 26  LYS A NZ  1 
ATOM   187  N N   . PHE A 1 28  ? 4.097   22.949  26.451  1.00 37.37  ? 27  PHE A N   1 
ATOM   188  C CA  . PHE A 1 28  ? 2.805   22.565  27.074  1.00 32.75  ? 27  PHE A CA  1 
ATOM   189  C C   . PHE A 1 28  ? 3.014   22.495  28.570  1.00 32.31  ? 27  PHE A C   1 
ATOM   190  O O   . PHE A 1 28  ? 4.197   22.449  28.960  1.00 35.20  ? 27  PHE A O   1 
ATOM   191  C CB  . PHE A 1 28  ? 2.327   21.236  26.493  1.00 36.76  ? 27  PHE A CB  1 
ATOM   192  C CG  . PHE A 1 28  ? 3.274   20.108  26.811  1.00 38.11  ? 27  PHE A CG  1 
ATOM   193  C CD1 . PHE A 1 28  ? 3.139   19.411  28.000  1.00 35.25  ? 27  PHE A CD1 1 
ATOM   194  C CD2 . PHE A 1 28  ? 4.306   19.760  25.946  1.00 42.25  ? 27  PHE A CD2 1 
ATOM   195  C CE1 . PHE A 1 28  ? 3.990   18.351  28.275  1.00 33.81  ? 27  PHE A CE1 1 
ATOM   196  C CE2 . PHE A 1 28  ? 5.150   18.707  26.231  1.00 43.13  ? 27  PHE A CE2 1 
ATOM   197  C CZ  . PHE A 1 28  ? 5.000   18.028  27.407  1.00 37.14  ? 27  PHE A CZ  1 
ATOM   198  N N   . SER A 1 29  ? 1.944   22.557  29.331  1.00 35.26  ? 28  SER A N   1 
ATOM   199  C CA  . SER A 1 29  ? 1.977   22.398  30.807  1.00 34.36  ? 28  SER A CA  1 
ATOM   200  C C   . SER A 1 29  ? 0.940   21.369  31.243  1.00 36.09  ? 28  SER A C   1 
ATOM   201  O O   . SER A 1 29  ? -0.124  21.310  30.650  1.00 32.10  ? 28  SER A O   1 
ATOM   202  C CB  . SER A 1 29  ? 1.725   23.708  31.519  1.00 43.70  ? 28  SER A CB  1 
ATOM   203  O OG  . SER A 1 29  ? 2.727   24.629  31.157  1.00 40.73  ? 28  SER A OG  1 
ATOM   204  N N   . VAL A 1 30  ? 1.210   20.695  32.367  1.00 32.81  ? 29  VAL A N   1 
ATOM   205  C CA  . VAL A 1 30  ? 0.320   19.651  32.919  1.00 30.52  ? 29  VAL A CA  1 
ATOM   206  C C   . VAL A 1 30  ? 0.288   19.974  34.395  1.00 32.83  ? 29  VAL A C   1 
ATOM   207  O O   . VAL A 1 30  ? 1.355   20.296  34.965  1.00 33.73  ? 29  VAL A O   1 
ATOM   208  C CB  . VAL A 1 30  ? 0.823   18.216  32.661  1.00 32.50  ? 29  VAL A CB  1 
ATOM   209  C CG1 . VAL A 1 30  ? 0.070   17.204  33.549  1.00 30.48  ? 29  VAL A CG1 1 
ATOM   210  C CG2 . VAL A 1 30  ? 0.606   17.839  31.197  1.00 33.61  ? 29  VAL A CG2 1 
ATOM   211  N N   . SER A 1 31  ? -0.896  19.984  34.974  1.00 30.25  ? 30  SER A N   1 
ATOM   212  C CA  . SER A 1 31  ? -1.004  19.958  36.446  1.00 33.87  ? 30  SER A CA  1 
ATOM   213  C C   . SER A 1 31  ? -1.737  18.682  36.886  1.00 32.90  ? 30  SER A C   1 
ATOM   214  O O   . SER A 1 31  ? -2.549  18.112  36.132  1.00 37.29  ? 30  SER A O   1 
ATOM   215  C CB  . SER A 1 31  ? -1.733  21.176  36.973  1.00 35.93  ? 30  SER A CB  1 
ATOM   216  O OG  . SER A 1 31  ? -3.021  21.129  36.435  1.00 37.55  ? 30  SER A OG  1 
ATOM   217  N N   . GLY A 1 32  ? -1.488  18.295  38.121  1.00 34.05  ? 31  GLY A N   1 
ATOM   218  C CA  . GLY A 1 32  ? -2.097  17.084  38.653  1.00 31.76  ? 31  GLY A CA  1 
ATOM   219  C C   . GLY A 1 32  ? -2.446  17.289  40.084  1.00 30.72  ? 31  GLY A C   1 
ATOM   220  O O   . GLY A 1 32  ? -1.754  18.100  40.772  1.00 30.38  ? 31  GLY A O   1 
ATOM   221  N N   . GLU A 1 33  ? -3.448  16.552  40.527  1.00 29.48  ? 32  GLU A N   1 
ATOM   222  C CA  . GLU A 1 33  ? -3.805  16.518  41.956  1.00 31.30  ? 32  GLU A CA  1 
ATOM   223  C C   . GLU A 1 33  ? -4.190  15.108  42.358  1.00 31.17  ? 32  GLU A C   1 
ATOM   224  O O   . GLU A 1 33  ? -4.651  14.350  41.491  1.00 32.54  ? 32  GLU A O   1 
ATOM   225  C CB  . GLU A 1 33  ? -4.964  17.469  42.241  1.00 29.11  ? 32  GLU A CB  1 
ATOM   226  C CG  . GLU A 1 33  ? -6.192  17.247  41.360  1.00 35.20  ? 32  GLU A CG  1 
ATOM   227  C CD  . GLU A 1 33  ? -7.490  17.739  41.976  1.00 39.99  ? 32  GLU A CD  1 
ATOM   228  O OE1 . GLU A 1 33  ? -7.667  17.569  43.194  1.00 43.36  ? 32  GLU A OE1 1 
ATOM   229  O OE2 . GLU A 1 33  ? -8.334  18.256  41.238  1.00 38.48  ? 32  GLU A OE2 1 
ATOM   230  N N   . GLY A 1 34  ? -4.138  14.864  43.640  1.00 30.27  ? 33  GLY A N   1 
ATOM   231  C CA  . GLY A 1 34  ? -4.759  13.667  44.227  1.00 36.50  ? 33  GLY A CA  1 
ATOM   232  C C   . GLY A 1 34  ? -4.172  13.369  45.582  1.00 34.62  ? 33  GLY A C   1 
ATOM   233  O O   . GLY A 1 34  ? -3.922  14.309  46.319  1.00 31.90  ? 33  GLY A O   1 
ATOM   234  N N   . GLU A 1 35  ? -4.092  12.075  45.947  1.00 32.08  ? 34  GLU A N   1 
ATOM   235  C CA  . GLU A 1 35  ? -3.856  11.630  47.331  1.00 39.42  ? 34  GLU A CA  1 
ATOM   236  C C   . GLU A 1 35  ? -2.927  10.423  47.292  1.00 32.50  ? 34  GLU A C   1 
ATOM   237  O O   . GLU A 1 35  ? -3.156  9.562   46.443  1.00 30.34  ? 34  GLU A O   1 
ATOM   238  C CB  . GLU A 1 35  ? -5.189  11.184  47.945  1.00 40.81  ? 34  GLU A CB  1 
ATOM   239  C CG  . GLU A 1 35  ? -6.188  12.303  47.967  1.00 51.59  ? 34  GLU A CG  1 
ATOM   240  C CD  . GLU A 1 35  ? -7.224  12.165  49.064  1.00 54.46  ? 34  GLU A CD  1 
ATOM   241  O OE1 . GLU A 1 35  ? -7.855  11.071  49.141  1.00 67.72  ? 34  GLU A OE1 1 
ATOM   242  O OE2 . GLU A 1 35  ? -7.305  13.111  49.878  1.00 73.21  ? 34  GLU A OE2 1 
ATOM   243  N N   . GLY A 1 36  ? -1.948  10.363  48.182  1.00 30.35  ? 35  GLY A N   1 
ATOM   244  C CA  . GLY A 1 36  ? -1.056  9.199   48.315  1.00 32.99  ? 35  GLY A CA  1 
ATOM   245  C C   . GLY A 1 36  ? -1.288  8.527   49.650  1.00 32.98  ? 35  GLY A C   1 
ATOM   246  O O   . GLY A 1 36  ? -1.489  9.250   50.669  1.00 32.76  ? 35  GLY A O   1 
ATOM   247  N N   . ASP A 1 37  ? -1.291  7.207   49.679  1.00 32.66  ? 36  ASP A N   1 
ATOM   248  C CA  . ASP A 1 37  ? -1.504  6.448   50.910  1.00 29.72  ? 36  ASP A CA  1 
ATOM   249  C C   . ASP A 1 37  ? -0.474  5.358   50.881  1.00 29.46  ? 36  ASP A C   1 
ATOM   250  O O   . ASP A 1 37  ? -0.814  4.245   50.384  1.00 30.99  ? 36  ASP A O   1 
ATOM   251  C CB  . ASP A 1 37  ? -2.935  5.935   50.930  1.00 33.07  ? 36  ASP A CB  1 
ATOM   252  C CG  . ASP A 1 37  ? -3.459  5.388   52.237  1.00 37.49  ? 36  ASP A CG  1 
ATOM   253  O OD1 . ASP A 1 37  ? -2.732  5.390   53.234  1.00 39.48  ? 36  ASP A OD1 1 
ATOM   254  O OD2 . ASP A 1 37  ? -4.642  4.986   52.200  1.00 42.85  ? 36  ASP A OD2 1 
ATOM   255  N N   . ALA A 1 38  ? 0.739   5.697   51.298  1.00 30.67  ? 37  ALA A N   1 
ATOM   256  C CA  . ALA A 1 38  ? 1.920   4.828   51.109  1.00 31.76  ? 37  ALA A CA  1 
ATOM   257  C C   . ALA A 1 38  ? 1.791   3.533   51.927  1.00 36.40  ? 37  ALA A C   1 
ATOM   258  O O   . ALA A 1 38  ? 2.443   2.544   51.574  1.00 30.85  ? 37  ALA A O   1 
ATOM   259  C CB  . ALA A 1 38  ? 3.152   5.572   51.514  1.00 31.42  ? 37  ALA A CB  1 
ATOM   260  N N   . THR A 1 39  ? 1.011   3.566   53.012  1.00 33.65  ? 38  THR A N   1 
ATOM   261  C CA  . THR A 1 39  ? 0.691   2.349   53.800  1.00 35.81  ? 38  THR A CA  1 
ATOM   262  C C   . THR A 1 39  ? 0.290   1.213   52.865  1.00 31.80  ? 38  THR A C   1 
ATOM   263  O O   . THR A 1 39  ? 0.743   0.029   53.148  1.00 39.78  ? 38  THR A O   1 
ATOM   264  C CB  . THR A 1 39  ? -0.373  2.600   54.875  1.00 35.43  ? 38  THR A CB  1 
ATOM   265  O OG1 . THR A 1 39  ? 0.153   3.676   55.652  1.00 34.41  ? 38  THR A OG1 1 
ATOM   266  C CG2 . THR A 1 39  ? -0.580  1.358   55.737  1.00 31.13  ? 38  THR A CG2 1 
ATOM   267  N N   . TYR A 1 40  ? -0.518  1.502   51.848  1.00 28.45  ? 39  TYR A N   1 
ATOM   268  C CA  . TYR A 1 40  ? -1.047  0.559   50.822  1.00 30.50  ? 39  TYR A CA  1 
ATOM   269  C C   . TYR A 1 40  ? -0.383  0.735   49.454  1.00 29.80  ? 39  TYR A C   1 
ATOM   270  O O   . TYR A 1 40  ? -0.945  0.217   48.449  1.00 34.06  ? 39  TYR A O   1 
ATOM   271  C CB  . TYR A 1 40  ? -2.569  0.684   50.697  1.00 31.92  ? 39  TYR A CB  1 
ATOM   272  C CG  . TYR A 1 40  ? -3.155  0.549   52.069  1.00 35.90  ? 39  TYR A CG  1 
ATOM   273  C CD1 . TYR A 1 40  ? -3.208  -0.699  52.677  1.00 35.78  ? 39  TYR A CD1 1 
ATOM   274  C CD2 . TYR A 1 40  ? -3.525  1.663   52.798  1.00 37.12  ? 39  TYR A CD2 1 
ATOM   275  C CE1 . TYR A 1 40  ? -3.651  -0.837  53.983  1.00 34.21  ? 39  TYR A CE1 1 
ATOM   276  C CE2 . TYR A 1 40  ? -3.990  1.559   54.097  1.00 37.97  ? 39  TYR A CE2 1 
ATOM   277  C CZ  . TYR A 1 40  ? -4.069  0.294   54.677  1.00 38.76  ? 39  TYR A CZ  1 
ATOM   278  O OH  . TYR A 1 40  ? -4.470  0.185   55.959  1.00 40.56  ? 39  TYR A OH  1 
ATOM   279  N N   . GLY A 1 41  ? 0.700   1.532   49.394  1.00 33.78  ? 40  GLY A N   1 
ATOM   280  C CA  . GLY A 1 41  ? 1.439   1.826   48.141  1.00 31.61  ? 40  GLY A CA  1 
ATOM   281  C C   . GLY A 1 41  ? 0.559   2.516   47.101  1.00 33.00  ? 40  GLY A C   1 
ATOM   282  O O   . GLY A 1 41  ? 0.869   2.439   45.874  1.00 31.86  ? 40  GLY A O   1 
ATOM   283  N N   . LYS A 1 42  ? -0.439  3.276   47.541  1.00 30.14  ? 41  LYS A N   1 
ATOM   284  C CA  . LYS A 1 42  ? -1.489  3.735   46.627  1.00 29.94  ? 41  LYS A CA  1 
ATOM   285  C C   . LYS A 1 42  ? -1.365  5.226   46.279  1.00 33.33  ? 41  LYS A C   1 
ATOM   286  O O   . LYS A 1 42  ? -1.053  6.054   47.206  1.00 32.50  ? 41  LYS A O   1 
ATOM   287  C CB  . LYS A 1 42  ? -2.856  3.448   47.245  1.00 31.46  ? 41  LYS A CB  1 
ATOM   288  C CG  . LYS A 1 42  ? -4.024  3.893   46.387  1.00 38.64  ? 41  LYS A CG  1 
ATOM   289  C CD  . LYS A 1 42  ? -5.353  3.604   47.111  1.00 47.45  ? 41  LYS A CD  1 
ATOM   290  C CE  . LYS A 1 42  ? -6.519  4.424   46.602  1.00 51.15  ? 41  LYS A CE  1 
ATOM   291  N NZ  . LYS A 1 42  ? -7.453  4.760   47.709  1.00 64.82  ? 41  LYS A NZ  1 
ATOM   292  N N   . MET A 1 43  ? -1.582  5.541   44.998  1.00 30.72  ? 42  MET A N   1 
ATOM   293  C CA  . MET A 1 43  ? -1.861  6.932   44.560  1.00 30.44  ? 42  MET A CA  1 
ATOM   294  C C   . MET A 1 43  ? -3.108  6.968   43.706  1.00 29.85  ? 42  MET A C   1 
ATOM   295  O O   . MET A 1 43  ? -3.271  6.125   42.811  1.00 30.97  ? 42  MET A O   1 
ATOM   296  C CB  . MET A 1 43  ? -0.688  7.542   43.790  1.00 29.20  ? 42  MET A CB  1 
ATOM   297  C CG  . MET A 1 43  ? 0.543   7.650   44.634  1.00 27.10  ? 42  MET A CG  1 
ATOM   298  S SD  . MET A 1 43  ? 2.001   8.260   43.741  1.00 34.23  ? 42  MET A SD  1 
ATOM   299  C CE  . MET A 1 43  ? 2.351   6.904   42.633  1.00 34.09  ? 42  MET A CE  1 
ATOM   300  N N   . SER A 1 44  ? -3.975  7.930   43.974  1.00 28.52  ? 43  SER A N   1 
ATOM   301  C CA  A SER A 1 44  ? -5.086  8.241   43.059  0.50 30.62  ? 43  SER A CA  1 
ATOM   302  C CA  B SER A 1 44  ? -5.150  8.273   43.150  0.50 30.71  ? 43  SER A CA  1 
ATOM   303  C C   . SER A 1 44  ? -4.926  9.686   42.580  1.00 33.05  ? 43  SER A C   1 
ATOM   304  O O   . SER A 1 44  ? -4.780  10.603  43.398  1.00 29.95  ? 43  SER A O   1 
ATOM   305  C CB  A SER A 1 44  ? -6.449  7.945   43.606  0.50 33.24  ? 43  SER A CB  1 
ATOM   306  C CB  B SER A 1 44  ? -6.414  8.159   43.970  0.50 35.00  ? 43  SER A CB  1 
ATOM   307  O OG  A SER A 1 44  ? -6.652  8.572   44.846  0.50 35.19  ? 43  SER A OG  1 
ATOM   308  O OG  B SER A 1 44  ? -7.570  8.496   43.218  0.50 38.01  ? 43  SER A OG  1 
ATOM   309  N N   . LEU A 1 45  ? -4.898  9.826   41.255  1.00 28.57  ? 44  LEU A N   1 
ATOM   310  C CA  . LEU A 1 45  ? -4.470  11.089  40.607  1.00 28.95  ? 44  LEU A CA  1 
ATOM   311  C C   . LEU A 1 45  ? -5.310  11.409  39.411  1.00 31.12  ? 44  LEU A C   1 
ATOM   312  O O   . LEU A 1 45  ? -5.767  10.481  38.705  1.00 31.05  ? 44  LEU A O   1 
ATOM   313  C CB  . LEU A 1 45  ? -3.015  10.961  40.167  1.00 32.09  ? 44  LEU A CB  1 
ATOM   314  C CG  . LEU A 1 45  ? -2.037  10.639  41.281  1.00 33.98  ? 44  LEU A CG  1 
ATOM   315  C CD1 . LEU A 1 45  ? -0.811  10.015  40.691  1.00 36.37  ? 44  LEU A CD1 1 
ATOM   316  C CD2 . LEU A 1 45  ? -1.705  11.899  42.050  1.00 33.72  ? 44  LEU A CD2 1 
ATOM   317  N N   . LYS A 1 46  ? -5.476  12.727  39.200  1.00 31.89  ? 45  LYS A N   1 
ATOM   318  C CA  . LYS A 1 46  ? -6.008  13.233  37.939  1.00 32.19  ? 45  LYS A CA  1 
ATOM   319  C C   . LYS A 1 46  ? -5.064  14.309  37.407  1.00 35.35  ? 45  LYS A C   1 
ATOM   320  O O   . LYS A 1 46  ? -4.677  15.212  38.164  1.00 31.73  ? 45  LYS A O   1 
ATOM   321  C CB  . LYS A 1 46  ? -7.441  13.690  38.177  1.00 32.67  ? 45  LYS A CB  1 
ATOM   322  C CG  . LYS A 1 46  ? -8.025  14.304  36.938  1.00 34.54  ? 45  LYS A CG  1 
ATOM   323  C CD  . LYS A 1 46  ? -9.394  14.851  37.175  1.00 32.37  ? 45  LYS A CD  1 
ATOM   324  C CE  . LYS A 1 46  ? -9.933  15.419  35.871  1.00 35.11  ? 45  LYS A CE  1 
ATOM   325  N NZ  . LYS A 1 46  ? -11.249 16.055  36.060  1.00 39.24  ? 45  LYS A NZ  1 
ATOM   326  N N   . PHE A 1 47  ? -4.669  14.187  36.148  1.00 32.86  ? 46  PHE A N   1 
ATOM   327  C CA  . PHE A 1 47  ? -3.812  15.175  35.467  1.00 33.40  ? 46  PHE A CA  1 
ATOM   328  C C   . PHE A 1 47  ? -4.603  15.875  34.351  1.00 36.24  ? 46  PHE A C   1 
ATOM   329  O O   . PHE A 1 47  ? -5.414  15.198  33.663  1.00 30.39  ? 46  PHE A O   1 
ATOM   330  C CB  . PHE A 1 47  ? -2.582  14.481  34.875  1.00 30.99  ? 46  PHE A CB  1 
ATOM   331  C CG  . PHE A 1 47  ? -1.698  13.824  35.890  1.00 31.69  ? 46  PHE A CG  1 
ATOM   332  C CD1 . PHE A 1 47  ? -0.719  14.558  36.537  1.00 29.46  ? 46  PHE A CD1 1 
ATOM   333  C CD2 . PHE A 1 47  ? -1.863  12.475  36.216  1.00 31.67  ? 46  PHE A CD2 1 
ATOM   334  C CE1 . PHE A 1 47  ? 0.102   13.966  37.483  1.00 32.26  ? 46  PHE A CE1 1 
ATOM   335  C CE2 . PHE A 1 47  ? -1.045  11.875  37.154  1.00 33.51  ? 46  PHE A CE2 1 
ATOM   336  C CZ  . PHE A 1 47  ? -0.062  12.625  37.802  1.00 36.40  ? 46  PHE A CZ  1 
ATOM   337  N N   . ILE A 1 48  ? -4.304  17.158  34.111  1.00 33.26  ? 47  ILE A N   1 
ATOM   338  C CA  . ILE A 1 48  ? -4.940  17.971  33.025  1.00 35.98  ? 47  ILE A CA  1 
ATOM   339  C C   . ILE A 1 48  ? -3.846  18.671  32.225  1.00 33.46  ? 47  ILE A C   1 
ATOM   340  O O   . ILE A 1 48  ? -2.809  19.033  32.800  1.00 32.82  ? 47  ILE A O   1 
ATOM   341  C CB  . ILE A 1 48  ? -5.961  18.975  33.574  1.00 35.51  ? 47  ILE A CB  1 
ATOM   342  C CG1 . ILE A 1 48  ? -5.327  19.897  34.607  1.00 40.06  ? 47  ILE A CG1 1 
ATOM   343  C CG2 . ILE A 1 48  ? -7.157  18.253  34.142  1.00 39.76  ? 47  ILE A CG2 1 
ATOM   344  C CD1 . ILE A 1 48  ? -6.226  21.048  34.967  1.00 49.05  ? 47  ILE A CD1 1 
ATOM   345  N N   . CYS A 1 49  ? -4.061  18.801  30.917  1.00 30.99  ? 48  CYS A N   1 
ATOM   346  C CA  . CYS A 1 49  ? -3.219  19.684  30.092  1.00 32.62  ? 48  CYS A CA  1 
ATOM   347  C C   . CYS A 1 49  ? -3.834  21.082  30.228  1.00 32.66  ? 48  CYS A C   1 
ATOM   348  O O   . CYS A 1 49  ? -5.001  21.230  29.907  1.00 36.08  ? 48  CYS A O   1 
ATOM   349  C CB  . CYS A 1 49  ? -3.147  19.236  28.646  1.00 35.33  ? 48  CYS A CB  1 
ATOM   350  S SG  . CYS A 1 49  ? -1.995  20.320  27.761  1.00 37.38  ? 48  CYS A SG  1 
ATOM   351  N N   . THR A 1 50  ? -3.091  22.014  30.799  1.00 33.84  ? 49  THR A N   1 
ATOM   352  C CA  . THR A 1 50  ? -3.576  23.380  31.090  1.00 40.39  ? 49  THR A CA  1 
ATOM   353  C C   . THR A 1 50  ? -3.356  24.289  29.879  1.00 44.79  ? 49  THR A C   1 
ATOM   354  O O   . THR A 1 50  ? -3.764  25.444  29.935  1.00 41.26  ? 49  THR A O   1 
ATOM   355  C CB  . THR A 1 50  ? -2.886  23.936  32.325  1.00 38.23  ? 49  THR A CB  1 
ATOM   356  O OG1 . THR A 1 50  ? -1.486  24.059  32.106  1.00 38.22  ? 49  THR A OG1 1 
ATOM   357  C CG2 . THR A 1 50  ? -3.185  23.085  33.544  1.00 42.80  ? 49  THR A CG2 1 
ATOM   358  N N   . THR A 1 51  ? -2.680  23.806  28.839  1.00 39.85  ? 50  THR A N   1 
ATOM   359  C CA  . THR A 1 51  ? -2.311  24.660  27.683  1.00 42.58  ? 50  THR A CA  1 
ATOM   360  C C   . THR A 1 51  ? -3.081  24.202  26.440  1.00 46.74  ? 50  THR A C   1 
ATOM   361  O O   . THR A 1 51  ? -2.738  24.676  25.378  1.00 45.83  ? 50  THR A O   1 
ATOM   362  C CB  . THR A 1 51  ? -0.799  24.641  27.441  1.00 43.87  ? 50  THR A CB  1 
ATOM   363  O OG1 . THR A 1 51  ? -0.460  23.246  27.417  1.00 39.39  ? 50  THR A OG1 1 
ATOM   364  C CG2 . THR A 1 51  ? -0.029  25.451  28.459  1.00 44.06  ? 50  THR A CG2 1 
ATOM   365  N N   . GLY A 1 52  ? -4.077  23.323  26.559  1.00 41.35  ? 51  GLY A N   1 
ATOM   366  C CA  . GLY A 1 52  ? -4.890  22.844  25.414  1.00 44.58  ? 51  GLY A CA  1 
ATOM   367  C C   . GLY A 1 52  ? -4.694  21.366  25.141  1.00 45.49  ? 51  GLY A C   1 
ATOM   368  O O   . GLY A 1 52  ? -4.816  20.574  26.087  1.00 44.19  ? 51  GLY A O   1 
ATOM   369  N N   . LYS A 1 53  ? -4.337  20.990  23.912  1.00 40.00  ? 52  LYS A N   1 
ATOM   370  C CA  . LYS A 1 53  ? -4.102  19.575  23.529  1.00 48.33  ? 52  LYS A CA  1 
ATOM   371  C C   . LYS A 1 53  ? -2.672  19.203  23.935  1.00 40.31  ? 52  LYS A C   1 
ATOM   372  O O   . LYS A 1 53  ? -1.696  19.939  23.624  1.00 36.58  ? 52  LYS A O   1 
ATOM   373  C CB  . LYS A 1 53  ? -4.413  19.323  22.047  1.00 64.20  ? 52  LYS A CB  1 
ATOM   374  C CG  . LYS A 1 53  ? -5.905  19.313  21.716  1.00 79.80  ? 52  LYS A CG  1 
ATOM   375  C CD  . LYS A 1 53  ? -6.698  18.134  22.333  1.00 96.30  ? 52  LYS A CD  1 
ATOM   376  C CE  . LYS A 1 53  ? -7.923  18.563  23.131  1.00 98.07  ? 52  LYS A CE  1 
ATOM   377  N NZ  . LYS A 1 53  ? -8.512  17.445  23.912  1.00 101.23 ? 52  LYS A NZ  1 
ATOM   378  N N   . LEU A 1 54  ? -2.536  18.059  24.588  1.00 40.51  ? 53  LEU A N   1 
ATOM   379  C CA  . LEU A 1 54  ? -1.196  17.517  24.870  1.00 36.41  ? 53  LEU A CA  1 
ATOM   380  C C   . LEU A 1 54  ? -0.569  17.120  23.538  1.00 33.75  ? 53  LEU A C   1 
ATOM   381  O O   . LEU A 1 54  ? -1.171  16.379  22.791  1.00 41.26  ? 53  LEU A O   1 
ATOM   382  C CB  . LEU A 1 54  ? -1.319  16.324  25.806  1.00 40.64  ? 53  LEU A CB  1 
ATOM   383  C CG  . LEU A 1 54  ? -0.010  15.979  26.519  1.00 39.73  ? 53  LEU A CG  1 
ATOM   384  C CD1 . LEU A 1 54  ? 0.389   17.107  27.481  1.00 43.46  ? 53  LEU A CD1 1 
ATOM   385  C CD2 . LEU A 1 54  ? -0.162  14.660  27.245  1.00 36.89  ? 53  LEU A CD2 1 
ATOM   386  N N   . PRO A 1 55  ? 0.634   17.622  23.209  1.00 37.80  ? 54  PRO A N   1 
ATOM   387  C CA  . PRO A 1 55  ? 1.300   17.310  21.928  1.00 36.50  ? 54  PRO A CA  1 
ATOM   388  C C   . PRO A 1 55  ? 2.068   15.990  21.861  1.00 41.88  ? 54  PRO A C   1 
ATOM   389  O O   . PRO A 1 55  ? 2.663   15.679  20.802  1.00 43.24  ? 54  PRO A O   1 
ATOM   390  C CB  . PRO A 1 55  ? 2.308   18.477  21.806  1.00 37.53  ? 54  PRO A CB  1 
ATOM   391  C CG  . PRO A 1 55  ? 2.651   18.807  23.239  1.00 40.70  ? 54  PRO A CG  1 
ATOM   392  C CD  . PRO A 1 55  ? 1.341   18.656  23.982  1.00 40.62  ? 54  PRO A CD  1 
ATOM   393  N N   . VAL A 1 56  ? 2.101   15.252  22.984  1.00 36.44  ? 55  VAL A N   1 
ATOM   394  C CA  . VAL A 1 56  ? 2.680   13.898  23.043  1.00 35.86  ? 55  VAL A CA  1 
ATOM   395  C C   . VAL A 1 56  ? 1.603   13.040  23.708  1.00 36.80  ? 55  VAL A C   1 
ATOM   396  O O   . VAL A 1 56  ? 0.735   13.586  24.377  1.00 39.02  ? 55  VAL A O   1 
ATOM   397  C CB  . VAL A 1 56  ? 4.013   13.851  23.819  1.00 37.61  ? 55  VAL A CB  1 
ATOM   398  C CG1 . VAL A 1 56  ? 5.114   14.707  23.177  1.00 39.15  ? 55  VAL A CG1 1 
ATOM   399  C CG2 . VAL A 1 56  ? 3.812   14.307  25.258  1.00 37.45  ? 55  VAL A CG2 1 
ATOM   400  N N   . PRO A 1 57  ? 1.648   11.706  23.552  1.00 39.47  ? 56  PRO A N   1 
ATOM   401  C CA  . PRO A 1 57  ? 0.687   10.802  24.196  1.00 37.05  ? 56  PRO A CA  1 
ATOM   402  C C   . PRO A 1 57  ? 0.891   10.778  25.726  1.00 30.21  ? 56  PRO A C   1 
ATOM   403  O O   . PRO A 1 57  ? 2.062   10.883  26.230  1.00 35.55  ? 56  PRO A O   1 
ATOM   404  C CB  . PRO A 1 57  ? 0.999   9.433   23.590  1.00 40.51  ? 56  PRO A CB  1 
ATOM   405  C CG  . PRO A 1 57  ? 1.833   9.747   22.350  1.00 38.48  ? 56  PRO A CG  1 
ATOM   406  C CD  . PRO A 1 57  ? 2.620   10.984  22.710  1.00 35.88  ? 56  PRO A CD  1 
ATOM   407  N N   . TRP A 1 58  ? -0.233  10.795  26.455  1.00 34.00  ? 57  TRP A N   1 
ATOM   408  C CA  . TRP A 1 58  ? -0.243  10.725  27.949  1.00 34.63  ? 57  TRP A CA  1 
ATOM   409  C C   . TRP A 1 58  ? 0.621   9.574   28.434  1.00 31.92  ? 57  TRP A C   1 
ATOM   410  O O   . TRP A 1 58  ? 1.449   9.770   29.325  1.00 37.33  ? 57  TRP A O   1 
ATOM   411  C CB  . TRP A 1 58  ? -1.668  10.587  28.512  1.00 33.74  ? 57  TRP A CB  1 
ATOM   412  C CG  . TRP A 1 58  ? -2.433  11.863  28.597  1.00 37.95  ? 57  TRP A CG  1 
ATOM   413  C CD1 . TRP A 1 58  ? -3.508  12.233  27.828  1.00 41.79  ? 57  TRP A CD1 1 
ATOM   414  C CD2 . TRP A 1 58  ? -2.188  12.944  29.512  1.00 34.37  ? 57  TRP A CD2 1 
ATOM   415  N NE1 . TRP A 1 58  ? -3.937  13.474  28.197  1.00 37.04  ? 57  TRP A NE1 1 
ATOM   416  C CE2 . TRP A 1 58  ? -3.168  13.925  29.238  1.00 34.35  ? 57  TRP A CE2 1 
ATOM   417  C CE3 . TRP A 1 58  ? -1.306  13.117  30.593  1.00 32.99  ? 57  TRP A CE3 1 
ATOM   418  C CZ2 . TRP A 1 58  ? -3.248  15.102  29.962  1.00 34.72  ? 57  TRP A CZ2 1 
ATOM   419  C CZ3 . TRP A 1 58  ? -1.351  14.303  31.276  1.00 33.24  ? 57  TRP A CZ3 1 
ATOM   420  C CH2 . TRP A 1 58  ? -2.324  15.275  30.981  1.00 36.02  ? 57  TRP A CH2 1 
ATOM   421  N N   . PRO A 1 59  ? 0.571   8.368   27.808  1.00 35.42  ? 58  PRO A N   1 
ATOM   422  C CA  . PRO A 1 59  ? 1.439   7.265   28.256  1.00 29.20  ? 58  PRO A CA  1 
ATOM   423  C C   . PRO A 1 59  ? 2.935   7.557   28.338  1.00 32.90  ? 58  PRO A C   1 
ATOM   424  O O   . PRO A 1 59  ? 3.558   7.035   29.260  1.00 32.60  ? 58  PRO A O   1 
ATOM   425  C CB  . PRO A 1 59  ? 1.137   6.126   27.290  1.00 38.81  ? 58  PRO A CB  1 
ATOM   426  C CG  . PRO A 1 59  ? -0.323  6.437   26.889  1.00 37.57  ? 58  PRO A CG  1 
ATOM   427  C CD  . PRO A 1 59  ? -0.404  7.946   26.767  1.00 34.73  ? 58  PRO A CD  1 
ATOM   428  N N   . THR A 1 60  ? 3.475   8.439   27.479  1.00 31.85  ? 59  THR A N   1 
ATOM   429  C CA  . THR A 1 60  ? 4.920   8.808   27.484  1.00 30.82  ? 59  THR A CA  1 
ATOM   430  C C   . THR A 1 60  ? 5.256   9.687   28.683  1.00 29.22  ? 59  THR A C   1 
ATOM   431  O O   . THR A 1 60  ? 6.469   9.798   28.976  1.00 32.39  ? 59  THR A O   1 
ATOM   432  C CB  . THR A 1 60  ? 5.359   9.563   26.210  1.00 32.65  ? 59  THR A CB  1 
ATOM   433  O OG1 . THR A 1 60  ? 4.850   10.895  26.089  1.00 33.08  ? 59  THR A OG1 1 
ATOM   434  C CG2 . THR A 1 60  ? 4.935   8.739   24.998  1.00 36.00  ? 59  THR A CG2 1 
ATOM   435  N N   . LEU A 1 61  ? 4.257   10.319  29.323  1.00 31.67  ? 60  LEU A N   1 
ATOM   436  C CA  . LEU A 1 61  ? 4.524   11.232  30.462  1.00 31.83  ? 60  LEU A CA  1 
ATOM   437  C C   . LEU A 1 61  ? 4.333   10.480  31.783  1.00 36.57  ? 60  LEU A C   1 
ATOM   438  O O   . LEU A 1 61  ? 4.623   11.053  32.779  1.00 28.09  ? 60  LEU A O   1 
ATOM   439  C CB  . LEU A 1 61  ? 3.586   12.436  30.372  1.00 33.34  ? 60  LEU A CB  1 
ATOM   440  C CG  . LEU A 1 61  ? 3.828   13.399  29.195  1.00 35.77  ? 60  LEU A CG  1 
ATOM   441  C CD1 . LEU A 1 61  ? 2.952   14.644  29.321  1.00 37.75  ? 60  LEU A CD1 1 
ATOM   442  C CD2 . LEU A 1 61  ? 5.270   13.842  29.083  1.00 32.81  ? 60  LEU A CD2 1 
ATOM   443  N N   . LYS A 1 62  ? 3.775   9.262   31.803  1.00 32.36  ? 61  LYS A N   1 
ATOM   444  C CA  . LYS A 1 62  ? 3.349   8.650   33.103  1.00 32.34  ? 61  LYS A CA  1 
ATOM   445  C C   . LYS A 1 62  ? 4.515   8.527   34.053  1.00 30.53  ? 61  LYS A C   1 
ATOM   446  O O   . LYS A 1 62  ? 4.359   8.910   35.255  1.00 30.61  ? 61  LYS A O   1 
ATOM   447  C CB  . LYS A 1 62  ? 2.741   7.257   33.007  1.00 35.97  ? 61  LYS A CB  1 
ATOM   448  C CG  . LYS A 1 62  ? 1.377   7.208   32.371  1.00 46.14  ? 61  LYS A CG  1 
ATOM   449  C CD  . LYS A 1 62  ? 0.951   5.809   32.007  1.00 58.91  ? 61  LYS A CD  1 
ATOM   450  C CE  . LYS A 1 62  ? -0.282  5.781   31.133  1.00 70.86  ? 61  LYS A CE  1 
ATOM   451  N NZ  . LYS A 1 62  ? -0.677  4.395   30.781  1.00 84.76  ? 61  LYS A NZ  1 
ATOM   452  N N   . THR A 1 63  ? 5.592   7.896   33.635  1.00 34.31  ? 62  THR A N   1 
ATOM   453  C CA  . THR A 1 63  ? 6.753   7.716   34.546  1.00 29.06  ? 62  THR A CA  1 
ATOM   454  C C   . THR A 1 63  ? 7.308   9.048   35.080  1.00 32.35  ? 62  THR A C   1 
ATOM   455  O O   . THR A 1 63  ? 7.876   9.040   36.219  1.00 29.81  ? 62  THR A O   1 
ATOM   456  C CB  . THR A 1 63  ? 7.895   6.934   33.885  1.00 35.30  ? 62  THR A CB  1 
ATOM   457  O OG1 . THR A 1 63  ? 8.384   7.625   32.715  1.00 31.56  ? 62  THR A OG1 1 
ATOM   458  C CG2 . THR A 1 63  ? 7.451   5.521   33.566  1.00 32.51  ? 62  THR A CG2 1 
ATOM   459  N N   . THR A 1 64  ? 7.251   10.140  34.297  1.00 31.41  ? 63  THR A N   1 
ATOM   460  C CA  . THR A 1 64  ? 7.776   11.470  34.710  1.00 29.17  ? 63  THR A CA  1 
ATOM   461  C C   . THR A 1 64  ? 6.876   12.096  35.781  1.00 31.99  ? 63  THR A C   1 
ATOM   462  O O   . THR A 1 64  ? 7.366   12.688  36.786  1.00 31.31  ? 63  THR A O   1 
ATOM   463  C CB  . THR A 1 64  ? 7.899   12.391  33.481  1.00 31.74  ? 63  THR A CB  1 
ATOM   464  O OG1 . THR A 1 64  ? 8.902   11.852  32.625  1.00 31.84  ? 63  THR A OG1 1 
ATOM   465  C CG2 . THR A 1 64  ? 8.393   13.749  33.882  1.00 30.63  ? 63  THR A CG2 1 
ATOM   466  N N   . LEU A 1 65  ? 5.597   12.017  35.546  1.00 27.89  ? 64  LEU A N   1 
ATOM   467  C CA  . LEU A 1 65  ? 4.563   12.632  36.408  1.00 29.77  ? 64  LEU A CA  1 
ATOM   468  C C   . LEU A 1 65  ? 4.497   11.871  37.746  1.00 28.31  ? 64  LEU A C   1 
ATOM   469  O O   . LEU A 1 65  ? 4.270   12.464  38.840  1.00 32.37  ? 64  LEU A O   1 
ATOM   470  C CB  . LEU A 1 65  ? 3.218   12.553  35.668  1.00 29.39  ? 64  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 65  ? 3.034   13.527  34.491  1.00 31.01  ? 64  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 65  ? 1.734   13.193  33.767  1.00 31.51  ? 64  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 65  ? 3.014   14.972  34.975  1.00 30.86  ? 64  LEU A CD2 1 
HETATM 474  N N1  . CRF A 1 66  ? 4.461   10.334  37.676  1.00 28.94  ? 65  CRF A N1  1 
HETATM 475  C CA1 . CRF A 1 66  ? 4.473   9.525   38.886  1.00 28.06  ? 65  CRF A CA1 1 
HETATM 476  C CB1 . CRF A 1 66  ? 3.171   8.727   39.008  1.00 37.06  ? 65  CRF A CB1 1 
HETATM 477  C CG1 . CRF A 1 66  ? 1.977   9.616   38.853  1.00 41.77  ? 65  CRF A CG1 1 
HETATM 478  O OG1 . CRF A 1 66  ? 3.053   7.916   37.800  1.00 43.68  ? 65  CRF A OG1 1 
HETATM 479  C C1  . CRF A 1 66  ? 5.639   8.630   38.777  1.00 30.81  ? 65  CRF A C1  1 
HETATM 480  N N2  . CRF A 1 66  ? 5.592   7.353   38.299  1.00 32.44  ? 65  CRF A N2  1 
HETATM 481  N N3  . CRF A 1 66  ? 6.904   8.993   39.113  1.00 31.66  ? 65  CRF A N3  1 
HETATM 482  C C2  . CRF A 1 66  ? 7.728   7.957   38.819  1.00 32.10  ? 65  CRF A C2  1 
HETATM 483  O O2  . CRF A 1 66  ? 9.029   8.013   39.088  1.00 34.79  ? 65  CRF A O2  1 
HETATM 484  C CA2 . CRF A 1 66  ? 6.902   6.914   38.334  1.00 33.22  ? 65  CRF A CA2 1 
HETATM 485  C CA3 . CRF A 1 66  ? 7.277   10.309  39.610  1.00 30.29  ? 65  CRF A CA3 1 
HETATM 486  C C3  . CRF A 1 66  ? 7.449   10.502  41.052  1.00 32.35  ? 65  CRF A C3  1 
HETATM 487  O O3  . CRF A 1 66  ? 8.046   11.548  41.314  1.00 34.97  ? 65  CRF A O3  1 
HETATM 488  C CB2 . CRF A 1 66  ? 7.308   5.534   37.803  1.00 40.21  ? 65  CRF A CB2 1 
HETATM 489  C CG2 . CRF A 1 66  ? 6.405   4.561   37.164  1.00 34.92  ? 65  CRF A CG2 1 
HETATM 490  C CD1 . CRF A 1 66  ? 5.107   4.686   36.712  1.00 38.50  ? 65  CRF A CD1 1 
HETATM 491  C CD2 . CRF A 1 66  ? 6.988   3.295   36.720  1.00 32.46  ? 65  CRF A CD2 1 
HETATM 492  C CE2 . CRF A 1 66  ? 5.879   2.633   36.092  1.00 40.20  ? 65  CRF A CE2 1 
HETATM 493  N NE1 . CRF A 1 66  ? 4.797   3.493   36.100  1.00 42.19  ? 65  CRF A NE1 1 
HETATM 494  C CE3 . CRF A 1 66  ? 8.294   2.835   36.815  1.00 34.04  ? 65  CRF A CE3 1 
HETATM 495  C CZ2 . CRF A 1 66  ? 6.108   1.361   35.552  1.00 47.10  ? 65  CRF A CZ2 1 
HETATM 496  C CZ3 . CRF A 1 66  ? 8.471   1.516   36.283  1.00 43.18  ? 65  CRF A CZ3 1 
HETATM 497  C CH2 . CRF A 1 66  ? 7.411   0.797   35.702  1.00 43.91  ? 65  CRF A CH2 1 
ATOM   498  N N   . MET A 1 67  ? 6.625   9.727   41.763  1.00 31.41  ? 68  MET A N   1 
ATOM   499  C CA  . MET A 1 67  ? 6.564   10.057  43.195  1.00 29.47  ? 68  MET A CA  1 
ATOM   500  C C   . MET A 1 67  ? 6.731   8.723   43.980  1.00 32.52  ? 68  MET A C   1 
ATOM   501  O O   . MET A 1 67  ? 5.802   8.281   44.664  1.00 29.57  ? 68  MET A O   1 
ATOM   502  C CB  . MET A 1 67  ? 5.231   10.737  43.509  1.00 30.91  ? 68  MET A CB  1 
ATOM   503  C CG  . MET A 1 67  ? 5.181   12.155  42.945  1.00 32.27  ? 68  MET A CG  1 
ATOM   504  S SD  . MET A 1 67  ? 3.541   12.901  43.063  1.00 33.62  ? 68  MET A SD  1 
ATOM   505  C CE  . MET A 1 67  ? 2.609   11.950  41.873  1.00 33.74  ? 68  MET A CE  1 
ATOM   506  N N   . GLN A 1 68  ? 7.924   8.155   43.869  1.00 31.69  ? 69  GLN A N   1 
ATOM   507  C CA  . GLN A 1 68  ? 8.274   6.816   44.387  1.00 31.18  ? 69  GLN A CA  1 
ATOM   508  C C   . GLN A 1 68  ? 8.338   6.864   45.900  1.00 31.65  ? 69  GLN A C   1 
ATOM   509  O O   . GLN A 1 68  ? 8.381   5.741   46.517  1.00 30.42  ? 69  GLN A O   1 
ATOM   510  C CB  . GLN A 1 68  ? 9.597   6.365   43.785  1.00 29.67  ? 69  GLN A CB  1 
ATOM   511  C CG  . GLN A 1 68  ? 9.437   6.132   42.283  1.00 31.48  ? 69  GLN A CG  1 
ATOM   512  C CD  . GLN A 1 68  ? 10.748  5.907   41.578  1.00 31.41  ? 69  GLN A CD  1 
ATOM   513  O OE1 . GLN A 1 68  ? 11.711  6.652   41.756  1.00 33.00  ? 69  GLN A OE1 1 
ATOM   514  N NE2 . GLN A 1 68  ? 10.720  4.992   40.633  1.00 36.81  ? 69  GLN A NE2 1 
ATOM   515  N N   . CYS A 1 69  ? 8.287   8.068   46.491  1.00 29.34  ? 70  CYS A N   1 
ATOM   516  C CA  . CYS A 1 69  ? 8.043   8.201   47.962  1.00 26.62  ? 70  CYS A CA  1 
ATOM   517  C C   . CYS A 1 69  ? 6.721   7.574   48.407  1.00 26.84  ? 70  CYS A C   1 
ATOM   518  O O   . CYS A 1 69  ? 6.597   7.273   49.622  1.00 28.05  ? 70  CYS A O   1 
ATOM   519  C CB  . CYS A 1 69  ? 8.151   9.670   48.410  1.00 31.76  ? 70  CYS A CB  1 
ATOM   520  S SG  . CYS A 1 69  ? 7.078   10.759  47.446  1.00 31.51  ? 70  CYS A SG  1 
ATOM   521  N N   . PHE A 1 70  ? 5.735   7.302   47.557  1.00 26.10  ? 71  PHE A N   1 
ATOM   522  C CA  . PHE A 1 70  ? 4.489   6.650   48.030  1.00 28.40  ? 71  PHE A CA  1 
ATOM   523  C C   . PHE A 1 70  ? 4.502   5.118   47.867  1.00 26.51  ? 71  PHE A C   1 
ATOM   524  O O   . PHE A 1 70  ? 3.451   4.455   48.034  1.00 31.11  ? 71  PHE A O   1 
ATOM   525  C CB  . PHE A 1 70  ? 3.301   7.232   47.302  1.00 25.25  ? 71  PHE A CB  1 
ATOM   526  C CG  . PHE A 1 70  ? 3.031   8.657   47.675  1.00 28.31  ? 71  PHE A CG  1 
ATOM   527  C CD1 . PHE A 1 70  ? 2.516   8.961   48.928  1.00 29.56  ? 71  PHE A CD1 1 
ATOM   528  C CD2 . PHE A 1 70  ? 3.223   9.700   46.783  1.00 26.91  ? 71  PHE A CD2 1 
ATOM   529  C CE1 . PHE A 1 70  ? 2.258   10.263  49.287  1.00 34.13  ? 71  PHE A CE1 1 
ATOM   530  C CE2 . PHE A 1 70  ? 3.015   11.005  47.193  1.00 27.86  ? 71  PHE A CE2 1 
ATOM   531  C CZ  . PHE A 1 70  ? 2.528   11.289  48.422  1.00 29.20  ? 71  PHE A CZ  1 
ATOM   532  N N   . ALA A 1 71  ? 5.633   4.551   47.515  1.00 27.30  ? 72  ALA A N   1 
ATOM   533  C CA  . ALA A 1 71  ? 5.738   3.077   47.453  1.00 28.10  ? 72  ALA A CA  1 
ATOM   534  C C   . ALA A 1 71  ? 5.500   2.489   48.860  1.00 27.42  ? 72  ALA A C   1 
ATOM   535  O O   . ALA A 1 71  ? 5.836   3.113   49.907  1.00 29.36  ? 72  ALA A O   1 
ATOM   536  C CB  . ALA A 1 71  ? 7.079   2.671   46.937  1.00 28.92  ? 72  ALA A CB  1 
ATOM   537  N N   . ARG A 1 72  ? 4.943   1.299   48.891  1.00 32.38  ? 73  ARG A N   1 
ATOM   538  C CA  . ARG A 1 72  ? 4.856   0.526   50.146  1.00 31.36  ? 73  ARG A CA  1 
ATOM   539  C C   . ARG A 1 72  ? 6.151   -0.257  50.265  1.00 29.74  ? 73  ARG A C   1 
ATOM   540  O O   . ARG A 1 72  ? 6.331   -1.200  49.466  1.00 32.85  ? 73  ARG A O   1 
ATOM   541  C CB  . ARG A 1 72  ? 3.665   -0.428  50.159  1.00 32.05  ? 73  ARG A CB  1 
ATOM   542  C CG  . ARG A 1 72  ? 3.658   -1.301  51.406  1.00 30.15  ? 73  ARG A CG  1 
ATOM   543  C CD  . ARG A 1 72  ? 2.370   -2.090  51.490  1.00 31.79  ? 73  ARG A CD  1 
ATOM   544  N NE  . ARG A 1 72  ? 2.347   -3.226  50.579  1.00 38.25  ? 73  ARG A NE  1 
ATOM   545  C CZ  . ARG A 1 72  ? 2.920   -4.432  50.845  1.00 33.65  ? 73  ARG A CZ  1 
ATOM   546  N NH1 . ARG A 1 72  ? 3.561   -4.662  51.978  1.00 33.44  ? 73  ARG A NH1 1 
ATOM   547  N NH2 . ARG A 1 72  ? 2.845   -5.392  49.948  1.00 36.85  ? 73  ARG A NH2 1 
ATOM   548  N N   . TYR A 1 73  ? 6.992   0.079   51.236  1.00 34.09  ? 74  TYR A N   1 
ATOM   549  C CA  . TYR A 1 73  ? 8.156   -0.774  51.576  1.00 31.82  ? 74  TYR A CA  1 
ATOM   550  C C   . TYR A 1 73  ? 7.663   -1.732  52.652  1.00 37.37  ? 74  TYR A C   1 
ATOM   551  O O   . TYR A 1 73  ? 7.302   -1.304  53.748  1.00 33.36  ? 74  TYR A O   1 
ATOM   552  C CB  . TYR A 1 73  ? 9.376   0.014   52.024  1.00 32.43  ? 74  TYR A CB  1 
ATOM   553  C CG  . TYR A 1 73  ? 10.225  0.517   50.880  1.00 32.82  ? 74  TYR A CG  1 
ATOM   554  C CD1 . TYR A 1 73  ? 9.752   1.535   50.049  1.00 33.51  ? 74  TYR A CD1 1 
ATOM   555  C CD2 . TYR A 1 73  ? 11.492  0.012   50.617  1.00 32.41  ? 74  TYR A CD2 1 
ATOM   556  C CE1 . TYR A 1 73  ? 10.508  1.986   48.981  1.00 30.89  ? 74  TYR A CE1 1 
ATOM   557  C CE2 . TYR A 1 73  ? 12.281  0.479   49.571  1.00 32.87  ? 74  TYR A CE2 1 
ATOM   558  C CZ  . TYR A 1 73  ? 11.776  1.467   48.720  1.00 31.19  ? 74  TYR A CZ  1 
ATOM   559  O OH  . TYR A 1 73  ? 12.563  1.895   47.686  1.00 32.44  ? 74  TYR A OH  1 
ATOM   560  N N   . PRO A 1 74  ? 7.679   -3.052  52.406  1.00 35.07  ? 75  PRO A N   1 
ATOM   561  C CA  . PRO A 1 74  ? 7.402   -3.982  53.498  1.00 39.95  ? 75  PRO A CA  1 
ATOM   562  C C   . PRO A 1 74  ? 8.298   -3.711  54.697  1.00 32.83  ? 75  PRO A C   1 
ATOM   563  O O   . PRO A 1 74  ? 9.444   -3.275  54.551  1.00 35.19  ? 75  PRO A O   1 
ATOM   564  C CB  . PRO A 1 74  ? 7.744   -5.357  52.891  1.00 43.10  ? 75  PRO A CB  1 
ATOM   565  C CG  . PRO A 1 74  ? 7.531   -5.149  51.382  1.00 41.33  ? 75  PRO A CG  1 
ATOM   566  C CD  . PRO A 1 74  ? 8.024   -3.740  51.149  1.00 36.23  ? 75  PRO A CD  1 
ATOM   567  N N   . ASP A 1 75  ? 7.843   -4.140  55.885  1.00 34.93  ? 76  ASP A N   1 
ATOM   568  C CA  . ASP A 1 75  ? 8.573   -3.827  57.146  1.00 35.65  ? 76  ASP A CA  1 
ATOM   569  C C   . ASP A 1 75  ? 10.047  -4.267  57.036  1.00 31.48  ? 76  ASP A C   1 
ATOM   570  O O   . ASP A 1 75  ? 10.968  -3.518  57.460  1.00 30.84  ? 76  ASP A O   1 
ATOM   571  C CB  . ASP A 1 75  ? 7.841   -4.483  58.330  1.00 35.57  ? 76  ASP A CB  1 
ATOM   572  C CG  . ASP A 1 75  ? 8.653   -4.312  59.575  1.00 38.30  ? 76  ASP A CG  1 
ATOM   573  O OD1 . ASP A 1 75  ? 8.682   -3.238  60.055  1.00 37.25  ? 76  ASP A OD1 1 
ATOM   574  O OD2 . ASP A 1 75  ? 9.336   -5.233  59.948  1.00 38.42  ? 76  ASP A OD2 1 
ATOM   575  N N   . HIS A 1 76  ? 10.302  -5.462  56.518  1.00 33.90  ? 77  HIS A N   1 
ATOM   576  C CA  . HIS A 1 76  ? 11.683  -6.006  56.490  1.00 37.36  ? 77  HIS A CA  1 
ATOM   577  C C   . HIS A 1 76  ? 12.566  -5.196  55.529  1.00 38.12  ? 77  HIS A C   1 
ATOM   578  O O   . HIS A 1 76  ? 13.769  -5.413  55.535  1.00 33.55  ? 77  HIS A O   1 
ATOM   579  C CB  . HIS A 1 76  ? 11.670  -7.502  56.144  1.00 32.70  ? 77  HIS A CB  1 
ATOM   580  C CG  . HIS A 1 76  ? 11.504  -7.815  54.689  1.00 36.30  ? 77  HIS A CG  1 
ATOM   581  N ND1 . HIS A 1 76  ? 10.242  -7.907  54.102  1.00 32.55  ? 77  HIS A ND1 1 
ATOM   582  C CD2 . HIS A 1 76  ? 12.415  -8.072  53.712  1.00 31.90  ? 77  HIS A CD2 1 
ATOM   583  C CE1 . HIS A 1 76  ? 10.384  -8.280  52.845  1.00 38.73  ? 77  HIS A CE1 1 
ATOM   584  N NE2 . HIS A 1 76  ? 11.692  -8.351  52.559  1.00 34.45  ? 77  HIS A NE2 1 
ATOM   585  N N   . MET A 1 77  ? 11.996  -4.362  54.660  1.00 36.38  ? 78  MET A N   1 
ATOM   586  C CA  . MET A 1 77  ? 12.807  -3.564  53.684  1.00 34.45  ? 78  MET A CA  1 
ATOM   587  C C   . MET A 1 77  ? 12.807  -2.068  53.998  1.00 35.34  ? 78  MET A C   1 
ATOM   588  O O   . MET A 1 77  ? 13.384  -1.333  53.194  1.00 34.47  ? 78  MET A O   1 
ATOM   589  C CB  . MET A 1 77  ? 12.242  -3.760  52.273  1.00 33.50  ? 78  MET A CB  1 
ATOM   590  C CG  . MET A 1 77  ? 12.425  -5.118  51.700  1.00 36.51  ? 78  MET A CG  1 
ATOM   591  S SD  . MET A 1 77  ? 11.694  -5.249  50.054  1.00 37.91  ? 78  MET A SD  1 
ATOM   592  C CE  . MET A 1 77  ? 12.840  -4.159  49.180  1.00 36.80  ? 78  MET A CE  1 
ATOM   593  N N   . LYS A 1 78  ? 12.332  -1.619  55.155  1.00 35.71  ? 79  LYS A N   1 
ATOM   594  C CA  . LYS A 1 78  ? 12.180  -0.165  55.465  1.00 38.00  ? 79  LYS A CA  1 
ATOM   595  C C   . LYS A 1 78  ? 13.515  0.570   55.446  1.00 34.64  ? 79  LYS A C   1 
ATOM   596  O O   . LYS A 1 78  ? 13.540  1.759   55.109  1.00 37.47  ? 79  LYS A O   1 
ATOM   597  C CB  . LYS A 1 78  ? 11.632  0.028   56.884  1.00 42.32  ? 79  LYS A CB  1 
ATOM   598  C CG  . LYS A 1 78  ? 10.218  -0.439  57.090  1.00 54.79  ? 79  LYS A CG  1 
ATOM   599  C CD  . LYS A 1 78  ? 9.202   0.386   56.320  1.00 59.01  ? 79  LYS A CD  1 
ATOM   600  C CE  . LYS A 1 78  ? 7.768   0.207   56.811  1.00 57.63  ? 79  LYS A CE  1 
ATOM   601  N NZ  . LYS A 1 78  ? 6.795   0.695   55.804  1.00 52.55  ? 79  LYS A NZ  1 
ATOM   602  N N   . GLN A 1 79  ? 14.608  -0.122  55.731  1.00 37.80  ? 80  GLN A N   1 
ATOM   603  C CA  . GLN A 1 79  ? 15.942  0.497   55.830  1.00 37.42  ? 80  GLN A CA  1 
ATOM   604  C C   . GLN A 1 79  ? 16.450  0.835   54.417  1.00 36.03  ? 80  GLN A C   1 
ATOM   605  O O   . GLN A 1 79  ? 17.471  1.524   54.323  1.00 38.78  ? 80  GLN A O   1 
ATOM   606  C CB  . GLN A 1 79  ? 16.874  -0.388  56.664  1.00 43.10  ? 80  GLN A CB  1 
ATOM   607  C CG  . GLN A 1 79  ? 17.282  -1.676  55.967  1.00 52.03  ? 80  GLN A CG  1 
ATOM   608  C CD  . GLN A 1 79  ? 16.393  -2.859  56.269  1.00 55.21  ? 80  GLN A CD  1 
ATOM   609  O OE1 . GLN A 1 79  ? 15.171  -2.758  56.436  1.00 43.55  ? 80  GLN A OE1 1 
ATOM   610  N NE2 . GLN A 1 79  ? 17.026  -4.021  56.319  1.00 60.21  ? 80  GLN A NE2 1 
ATOM   611  N N   . HIS A 1 80  ? 15.744  0.403   53.367  1.00 33.20  ? 81  HIS A N   1 
ATOM   612  C CA  . HIS A 1 80  ? 16.092  0.644   51.954  1.00 35.68  ? 81  HIS A CA  1 
ATOM   613  C C   . HIS A 1 80  ? 15.256  1.769   51.315  1.00 33.27  ? 81  HIS A C   1 
ATOM   614  O O   . HIS A 1 80  ? 15.395  1.970   50.099  1.00 34.05  ? 81  HIS A O   1 
ATOM   615  C CB  . HIS A 1 80  ? 15.995  -0.667  51.186  1.00 36.81  ? 81  HIS A CB  1 
ATOM   616  C CG  . HIS A 1 80  ? 16.848  -1.738  51.780  1.00 40.82  ? 81  HIS A CG  1 
ATOM   617  N ND1 . HIS A 1 80  ? 16.306  -2.894  52.349  1.00 48.69  ? 81  HIS A ND1 1 
ATOM   618  C CD2 . HIS A 1 80  ? 18.177  -1.808  51.959  1.00 40.60  ? 81  HIS A CD2 1 
ATOM   619  C CE1 . HIS A 1 80  ? 17.297  -3.648  52.843  1.00 44.42  ? 81  HIS A CE1 1 
ATOM   620  N NE2 . HIS A 1 80  ? 18.472  -2.995  52.631  1.00 43.31  ? 81  HIS A NE2 1 
ATOM   621  N N   . ASP A 1 81  ? 14.390  2.465   52.044  1.00 32.63  ? 82  ASP A N   1 
ATOM   622  C CA  . ASP A 1 81  ? 13.478  3.497   51.495  1.00 33.24  ? 82  ASP A CA  1 
ATOM   623  C C   . ASP A 1 81  ? 14.186  4.870   51.518  1.00 34.90  ? 82  ASP A C   1 
ATOM   624  O O   . ASP A 1 81  ? 13.972  5.684   52.449  1.00 32.82  ? 82  ASP A O   1 
ATOM   625  C CB  . ASP A 1 81  ? 12.144  3.465   52.216  1.00 34.92  ? 82  ASP A CB  1 
ATOM   626  C CG  . ASP A 1 81  ? 11.079  4.356   51.599  1.00 34.25  ? 82  ASP A CG  1 
ATOM   627  O OD1 . ASP A 1 81  ? 11.407  5.100   50.658  1.00 30.25  ? 82  ASP A OD1 1 
ATOM   628  O OD2 . ASP A 1 81  ? 9.941   4.271   52.061  1.00 31.38  ? 82  ASP A OD2 1 
ATOM   629  N N   . PHE A 1 82  ? 15.039  5.113   50.520  1.00 33.93  ? 83  PHE A N   1 
ATOM   630  C CA  . PHE A 1 82  ? 15.696  6.431   50.284  1.00 31.86  ? 83  PHE A CA  1 
ATOM   631  C C   . PHE A 1 82  ? 14.630  7.540   50.217  1.00 29.47  ? 83  PHE A C   1 
ATOM   632  O O   . PHE A 1 82  ? 14.827  8.627   50.805  1.00 31.34  ? 83  PHE A O   1 
ATOM   633  C CB  . PHE A 1 82  ? 16.561  6.397   49.019  1.00 33.89  ? 83  PHE A CB  1 
ATOM   634  C CG  . PHE A 1 82  ? 16.980  7.767   48.538  1.00 32.67  ? 83  PHE A CG  1 
ATOM   635  C CD1 . PHE A 1 82  ? 18.018  8.463   49.156  1.00 35.04  ? 83  PHE A CD1 1 
ATOM   636  C CD2 . PHE A 1 82  ? 16.231  8.419   47.575  1.00 33.10  ? 83  PHE A CD2 1 
ATOM   637  C CE1 . PHE A 1 82  ? 18.373  9.732   48.728  1.00 37.90  ? 83  PHE A CE1 1 
ATOM   638  C CE2 . PHE A 1 82  ? 16.581  9.706   47.161  1.00 32.01  ? 83  PHE A CE2 1 
ATOM   639  C CZ  . PHE A 1 82  ? 17.633  10.361  47.750  1.00 34.22  ? 83  PHE A CZ  1 
ATOM   640  N N   . PHE A 1 83  ? 13.583  7.306   49.455  1.00 29.51  ? 84  PHE A N   1 
ATOM   641  C CA  . PHE A 1 83  ? 12.607  8.310   48.979  1.00 33.14  ? 84  PHE A CA  1 
ATOM   642  C C   . PHE A 1 83  ? 11.927  9.005   50.155  1.00 33.65  ? 84  PHE A C   1 
ATOM   643  O O   . PHE A 1 83  ? 12.010  10.221  50.220  1.00 31.14  ? 84  PHE A O   1 
ATOM   644  C CB  . PHE A 1 83  ? 11.578  7.672   48.084  1.00 30.97  ? 84  PHE A CB  1 
ATOM   645  C CG  . PHE A 1 83  ? 12.170  6.975   46.889  1.00 30.69  ? 84  PHE A CG  1 
ATOM   646  C CD1 . PHE A 1 83  ? 12.656  7.682   45.799  1.00 33.65  ? 84  PHE A CD1 1 
ATOM   647  C CD2 . PHE A 1 83  ? 12.288  5.590   46.890  1.00 30.32  ? 84  PHE A CD2 1 
ATOM   648  C CE1 . PHE A 1 83  ? 13.196  7.012   44.710  1.00 34.21  ? 84  PHE A CE1 1 
ATOM   649  C CE2 . PHE A 1 83  ? 12.824  4.920   45.807  1.00 31.55  ? 84  PHE A CE2 1 
ATOM   650  C CZ  . PHE A 1 83  ? 13.273  5.634   44.719  1.00 34.42  ? 84  PHE A CZ  1 
ATOM   651  N N   . LYS A 1 84  ? 11.438  8.244   51.117  1.00 30.91  ? 85  LYS A N   1 
ATOM   652  C CA  . LYS A 1 84  ? 10.895  8.841   52.359  1.00 34.20  ? 85  LYS A CA  1 
ATOM   653  C C   . LYS A 1 84  ? 12.017  9.419   53.238  1.00 34.79  ? 85  LYS A C   1 
ATOM   654  O O   . LYS A 1 84  ? 11.759  10.464  53.854  1.00 36.38  ? 85  LYS A O   1 
ATOM   655  C CB  . LYS A 1 84  ? 10.050  7.839   53.121  1.00 31.70  ? 85  LYS A CB  1 
ATOM   656  C CG  . LYS A 1 84  ? 8.811   7.360   52.374  1.00 32.50  ? 85  LYS A CG  1 
ATOM   657  C CD  . LYS A 1 84  ? 7.905   6.492   53.196  1.00 28.55  ? 85  LYS A CD  1 
ATOM   658  C CE  . LYS A 1 84  ? 6.829   5.804   52.391  1.00 31.05  ? 85  LYS A CE  1 
ATOM   659  N NZ  . LYS A 1 84  ? 7.477   5.009   51.331  1.00 32.52  ? 85  LYS A NZ  1 
ATOM   660  N N   . SER A 1 85  ? 13.217  8.832   53.250  1.00 32.72  ? 86  SER A N   1 
ATOM   661  C CA  . SER A 1 85  ? 14.291  9.243   54.175  1.00 37.97  ? 86  SER A CA  1 
ATOM   662  C C   . SER A 1 85  ? 14.662  10.689  53.865  1.00 35.23  ? 86  SER A C   1 
ATOM   663  O O   . SER A 1 85  ? 15.138  11.370  54.775  1.00 35.67  ? 86  SER A O   1 
ATOM   664  C CB  . SER A 1 85  ? 15.495  8.318   54.106  1.00 37.09  ? 86  SER A CB  1 
ATOM   665  O OG  . SER A 1 85  ? 16.438  8.732   53.123  1.00 36.52  ? 86  SER A OG  1 
ATOM   666  N N   . ALA A 1 86  ? 14.515  11.108  52.613  1.00 33.59  ? 87  ALA A N   1 
ATOM   667  C CA  . ALA A 1 86  ? 14.868  12.473  52.111  1.00 34.72  ? 87  ALA A CA  1 
ATOM   668  C C   . ALA A 1 86  ? 13.865  13.567  52.516  1.00 38.25  ? 87  ALA A C   1 
ATOM   669  O O   . ALA A 1 86  ? 14.144  14.782  52.320  1.00 36.54  ? 87  ALA A O   1 
ATOM   670  C CB  . ALA A 1 86  ? 15.004  12.437  50.607  1.00 36.07  ? 87  ALA A CB  1 
ATOM   671  N N   . MET A 1 87  ? 12.709  13.180  53.015  1.00 35.41  ? 88  MET A N   1 
ATOM   672  C CA  . MET A 1 87  ? 11.615  14.147  53.291  1.00 33.02  ? 88  MET A CA  1 
ATOM   673  C C   . MET A 1 87  ? 11.812  14.686  54.721  1.00 34.93  ? 88  MET A C   1 
ATOM   674  O O   . MET A 1 87  ? 12.221  13.957  55.609  1.00 33.99  ? 88  MET A O   1 
ATOM   675  C CB  . MET A 1 87  ? 10.269  13.431  53.116  1.00 33.10  ? 88  MET A CB  1 
ATOM   676  C CG  . MET A 1 87  ? 10.073  12.909  51.678  1.00 34.95  ? 88  MET A CG  1 
ATOM   677  S SD  . MET A 1 87  ? 9.914   14.273  50.591  1.00 33.12  ? 88  MET A SD  1 
ATOM   678  C CE  . MET A 1 87  ? 9.951   13.403  49.030  1.00 34.52  ? 88  MET A CE  1 
ATOM   679  N N   . PRO A 1 88  ? 11.356  15.903  55.056  1.00 36.08  ? 89  PRO A N   1 
ATOM   680  C CA  . PRO A 1 88  ? 10.435  16.655  54.196  1.00 36.58  ? 89  PRO A CA  1 
ATOM   681  C C   . PRO A 1 88  ? 11.143  17.552  53.164  1.00 35.59  ? 89  PRO A C   1 
ATOM   682  O O   . PRO A 1 88  ? 10.492  17.995  52.218  1.00 35.46  ? 89  PRO A O   1 
ATOM   683  C CB  . PRO A 1 88  ? 9.630   17.407  55.275  1.00 36.81  ? 89  PRO A CB  1 
ATOM   684  C CG  . PRO A 1 88  ? 10.710  17.732  56.305  1.00 40.91  ? 89  PRO A CG  1 
ATOM   685  C CD  . PRO A 1 88  ? 11.499  16.467  56.410  1.00 36.03  ? 89  PRO A CD  1 
ATOM   686  N N   . GLU A 1 89  ? 12.460  17.749  53.282  1.00 35.16  ? 90  GLU A N   1 
ATOM   687  C CA  . GLU A 1 89  ? 13.252  18.680  52.419  1.00 35.23  ? 90  GLU A CA  1 
ATOM   688  C C   . GLU A 1 89  ? 13.217  18.201  50.952  1.00 35.16  ? 90  GLU A C   1 
ATOM   689  O O   . GLU A 1 89  ? 13.283  19.030  50.021  1.00 32.87  ? 90  GLU A O   1 
ATOM   690  C CB  . GLU A 1 89  ? 14.714  18.781  52.883  1.00 42.25  ? 90  GLU A CB  1 
ATOM   691  C CG  . GLU A 1 89  ? 14.933  19.233  54.324  1.00 45.89  ? 90  GLU A CG  1 
ATOM   692  C CD  . GLU A 1 89  ? 14.848  18.159  55.415  1.00 64.28  ? 90  GLU A CD  1 
ATOM   693  O OE1 . GLU A 1 89  ? 14.505  16.960  55.141  1.00 46.64  ? 90  GLU A OE1 1 
ATOM   694  O OE2 . GLU A 1 89  ? 15.069  18.530  56.589  1.00 81.65  ? 90  GLU A OE2 1 
ATOM   695  N N   . GLY A 1 90  ? 13.185  16.894  50.739  1.00 31.65  ? 91  GLY A N   1 
ATOM   696  C CA  . GLY A 1 90  ? 12.867  16.348  49.411  1.00 34.02  ? 91  GLY A CA  1 
ATOM   697  C C   . GLY A 1 90  ? 14.079  15.879  48.650  1.00 35.32  ? 91  GLY A C   1 
ATOM   698  O O   . GLY A 1 90  ? 15.217  15.815  49.238  1.00 36.35  ? 91  GLY A O   1 
ATOM   699  N N   . TYR A 1 91  ? 13.852  15.521  47.389  1.00 36.76  ? 92  TYR A N   1 
ATOM   700  C CA  . TYR A 1 91  ? 14.905  15.027  46.470  1.00 36.26  ? 92  TYR A CA  1 
ATOM   701  C C   . TYR A 1 91  ? 14.727  15.607  45.088  1.00 34.22  ? 92  TYR A C   1 
ATOM   702  O O   . TYR A 1 91  ? 13.583  15.942  44.665  1.00 31.30  ? 92  TYR A O   1 
ATOM   703  C CB  . TYR A 1 91  ? 14.953  13.504  46.419  1.00 35.98  ? 92  TYR A CB  1 
ATOM   704  C CG  . TYR A 1 91  ? 13.669  12.762  46.118  1.00 30.28  ? 92  TYR A CG  1 
ATOM   705  C CD1 . TYR A 1 91  ? 13.224  12.607  44.809  1.00 31.57  ? 92  TYR A CD1 1 
ATOM   706  C CD2 . TYR A 1 91  ? 12.947  12.129  47.130  1.00 34.49  ? 92  TYR A CD2 1 
ATOM   707  C CE1 . TYR A 1 91  ? 12.100  11.832  44.519  1.00 28.39  ? 92  TYR A CE1 1 
ATOM   708  C CE2 . TYR A 1 91  ? 11.781  11.417  46.848  1.00 31.43  ? 92  TYR A CE2 1 
ATOM   709  C CZ  . TYR A 1 91  ? 11.394  11.238  45.547  1.00 28.86  ? 92  TYR A CZ  1 
ATOM   710  O OH  . TYR A 1 91  ? 10.254  10.533  45.241  1.00 32.09  ? 92  TYR A OH  1 
ATOM   711  N N   . VAL A 1 92  ? 15.856  15.655  44.375  1.00 31.84  ? 93  VAL A N   1 
ATOM   712  C CA  . VAL A 1 92  ? 15.882  15.879  42.920  1.00 35.26  ? 93  VAL A CA  1 
ATOM   713  C C   . VAL A 1 92  ? 15.812  14.540  42.213  1.00 33.17  ? 93  VAL A C   1 
ATOM   714  O O   . VAL A 1 92  ? 16.585  13.595  42.567  1.00 40.17  ? 93  VAL A O   1 
ATOM   715  C CB  . VAL A 1 92  ? 17.130  16.669  42.525  1.00 37.22  ? 93  VAL A CB  1 
ATOM   716  C CG1 . VAL A 1 92  ? 17.191  16.885  41.026  1.00 41.07  ? 93  VAL A CG1 1 
ATOM   717  C CG2 . VAL A 1 92  ? 17.144  18.008  43.262  1.00 38.63  ? 93  VAL A CG2 1 
ATOM   718  N N   . GLN A 1 93  ? 14.944  14.482  41.211  1.00 32.95  ? 94  GLN A N   1 
ATOM   719  C CA  . GLN A 1 93  ? 14.815  13.305  40.349  1.00 31.92  ? 94  GLN A CA  1 
ATOM   720  C C   . GLN A 1 93  ? 15.094  13.741  38.911  1.00 34.14  ? 94  GLN A C   1 
ATOM   721  O O   . GLN A 1 93  ? 14.373  14.595  38.377  1.00 35.24  ? 94  GLN A O   1 
ATOM   722  C CB  . GLN A 1 93  ? 13.433  12.697  40.513  1.00 30.35  ? 94  GLN A CB  1 
ATOM   723  C CG  . GLN A 1 93  ? 13.196  11.530  39.599  1.00 31.58  ? 94  GLN A CG  1 
ATOM   724  C CD  . GLN A 1 93  ? 12.122  10.563  40.087  1.00 31.40  ? 94  GLN A CD  1 
ATOM   725  O OE1 . GLN A 1 93  ? 12.110  10.052  41.218  1.00 32.80  ? 94  GLN A OE1 1 
ATOM   726  N NE2 . GLN A 1 93  ? 11.216  10.294  39.197  1.00 29.12  ? 94  GLN A NE2 1 
ATOM   727  N N   . GLU A 1 94  ? 16.133  13.170  38.329  1.00 32.37  ? 95  GLU A N   1 
ATOM   728  C CA  . GLU A 1 94  ? 16.554  13.468  36.952  1.00 34.43  ? 95  GLU A CA  1 
ATOM   729  C C   . GLU A 1 94  ? 16.475  12.178  36.149  1.00 33.69  ? 95  GLU A C   1 
ATOM   730  O O   . GLU A 1 94  ? 16.887  11.111  36.693  1.00 33.49  ? 95  GLU A O   1 
ATOM   731  C CB  . GLU A 1 94  ? 17.979  14.018  36.981  1.00 38.80  ? 95  GLU A CB  1 
ATOM   732  C CG  . GLU A 1 94  ? 18.040  15.493  37.242  1.00 47.97  ? 95  GLU A CG  1 
ATOM   733  C CD  . GLU A 1 94  ? 19.419  16.034  37.562  1.00 56.75  ? 95  GLU A CD  1 
ATOM   734  O OE1 . GLU A 1 94  ? 20.258  15.258  38.116  1.00 63.22  ? 95  GLU A OE1 1 
ATOM   735  O OE2 . GLU A 1 94  ? 19.621  17.248  37.305  1.00 62.43  ? 95  GLU A OE2 1 
ATOM   736  N N   . ARG A 1 95  ? 15.902  12.256  34.940  1.00 32.44  ? 96  ARG A N   1 
ATOM   737  C CA  . ARG A 1 95  ? 15.948  11.130  33.988  1.00 33.39  ? 96  ARG A CA  1 
ATOM   738  C C   . ARG A 1 95  ? 16.475  11.592  32.621  1.00 34.06  ? 96  ARG A C   1 
ATOM   739  O O   . ARG A 1 95  ? 16.184  12.698  32.227  1.00 33.38  ? 96  ARG A O   1 
ATOM   740  C CB  . ARG A 1 95  ? 14.552  10.528  33.865  1.00 31.24  ? 96  ARG A CB  1 
ATOM   741  C CG  . ARG A 1 95  ? 14.076  9.813   35.140  1.00 31.45  ? 96  ARG A CG  1 
ATOM   742  C CD  . ARG A 1 95  ? 13.225  8.621   34.835  1.00 32.88  ? 96  ARG A CD  1 
ATOM   743  N NE  . ARG A 1 95  ? 12.688  7.949   36.045  1.00 30.95  ? 96  ARG A NE  1 
ATOM   744  C CZ  . ARG A 1 95  ? 11.431  8.058   36.487  1.00 38.10  ? 96  ARG A CZ  1 
ATOM   745  N NH1 . ARG A 1 95  ? 10.572  8.871   35.889  1.00 33.61  ? 96  ARG A NH1 1 
ATOM   746  N NH2 . ARG A 1 95  ? 11.028  7.341   37.536  1.00 34.67  ? 96  ARG A NH2 1 
ATOM   747  N N   . THR A 1 96  ? 17.001  10.640  31.880  1.00 36.26  ? 97  THR A N   1 
ATOM   748  C CA  . THR A 1 96  ? 16.935  10.614  30.388  1.00 33.58  ? 97  THR A CA  1 
ATOM   749  C C   . THR A 1 96  ? 16.098  9.404   30.021  1.00 33.38  ? 97  THR A C   1 
ATOM   750  O O   . THR A 1 96  ? 16.351  8.323   30.585  1.00 35.03  ? 97  THR A O   1 
ATOM   751  C CB  . THR A 1 96  ? 18.348  10.663  29.777  1.00 36.59  ? 97  THR A CB  1 
ATOM   752  O OG1 . THR A 1 96  ? 19.017  11.794  30.355  1.00 39.69  ? 97  THR A OG1 1 
ATOM   753  C CG2 . THR A 1 96  ? 18.327  10.882  28.277  1.00 44.72  ? 97  THR A CG2 1 
ATOM   754  N N   . ILE A 1 97  ? 15.130  9.617   29.130  1.00 31.70  ? 98  ILE A N   1 
ATOM   755  C CA  . ILE A 1 97  ? 14.298  8.578   28.526  1.00 32.13  ? 98  ILE A CA  1 
ATOM   756  C C   . ILE A 1 97  ? 14.604  8.559   27.039  1.00 37.40  ? 98  ILE A C   1 
ATOM   757  O O   . ILE A 1 97  ? 14.273  9.544   26.357  1.00 36.58  ? 98  ILE A O   1 
ATOM   758  C CB  . ILE A 1 97  ? 12.801  8.816   28.833  1.00 32.73  ? 98  ILE A CB  1 
ATOM   759  C CG1 . ILE A 1 97  ? 12.582  9.006   30.347  1.00 32.26  ? 98  ILE A CG1 1 
ATOM   760  C CG2 . ILE A 1 97  ? 11.995  7.706   28.285  1.00 32.36  ? 98  ILE A CG2 1 
ATOM   761  C CD1 . ILE A 1 97  ? 11.172  9.422   30.719  1.00 33.87  ? 98  ILE A CD1 1 
ATOM   762  N N   . PHE A 1 98  ? 15.165  7.445   26.578  1.00 39.70  ? 99  PHE A N   1 
ATOM   763  C CA  . PHE A 1 98  ? 15.462  7.187   25.135  1.00 35.53  ? 99  PHE A CA  1 
ATOM   764  C C   . PHE A 1 98  ? 14.356  6.327   24.513  1.00 32.45  ? 99  PHE A C   1 
ATOM   765  O O   . PHE A 1 98  ? 14.195  5.104   24.839  1.00 35.95  ? 99  PHE A O   1 
ATOM   766  C CB  . PHE A 1 98  ? 16.832  6.530   25.048  1.00 35.79  ? 99  PHE A CB  1 
ATOM   767  C CG  . PHE A 1 98  ? 17.962  7.423   25.463  1.00 40.93  ? 99  PHE A CG  1 
ATOM   768  C CD1 . PHE A 1 98  ? 18.563  8.277   24.553  1.00 41.56  ? 99  PHE A CD1 1 
ATOM   769  C CD2 . PHE A 1 98  ? 18.453  7.386   26.759  1.00 36.33  ? 99  PHE A CD2 1 
ATOM   770  C CE1 . PHE A 1 98  ? 19.638  9.065   24.937  1.00 43.86  ? 99  PHE A CE1 1 
ATOM   771  C CE2 . PHE A 1 98  ? 19.489  8.221   27.155  1.00 41.32  ? 99  PHE A CE2 1 
ATOM   772  C CZ  . PHE A 1 98  ? 20.096  9.051   26.239  1.00 39.30  ? 99  PHE A CZ  1 
ATOM   773  N N   . PHE A 1 99  ? 13.580  6.937   23.610  1.00 33.15  ? 100 PHE A N   1 
ATOM   774  C CA  . PHE A 1 99  ? 12.539  6.230   22.866  1.00 32.67  ? 100 PHE A CA  1 
ATOM   775  C C   . PHE A 1 99  ? 13.177  5.605   21.624  1.00 37.19  ? 100 PHE A C   1 
ATOM   776  O O   . PHE A 1 99  ? 13.865  6.360   20.868  1.00 37.25  ? 100 PHE A O   1 
ATOM   777  C CB  . PHE A 1 99  ? 11.417  7.167   22.488  1.00 34.45  ? 100 PHE A CB  1 
ATOM   778  C CG  . PHE A 1 99  ? 10.634  7.658   23.679  1.00 36.43  ? 100 PHE A CG  1 
ATOM   779  C CD1 . PHE A 1 99  ? 9.634   6.889   24.241  1.00 40.00  ? 100 PHE A CD1 1 
ATOM   780  C CD2 . PHE A 1 99  ? 10.925  8.874   24.238  1.00 38.94  ? 100 PHE A CD2 1 
ATOM   781  C CE1 . PHE A 1 99  ? 8.891   7.376   25.306  1.00 38.67  ? 100 PHE A CE1 1 
ATOM   782  C CE2 . PHE A 1 99  ? 10.181  9.374   25.299  1.00 38.05  ? 100 PHE A CE2 1 
ATOM   783  C CZ  . PHE A 1 99  ? 9.183   8.609   25.840  1.00 42.74  ? 100 PHE A CZ  1 
ATOM   784  N N   . LYS A 1 100 ? 13.015  4.294   21.468  1.00 35.74  ? 101 LYS A N   1 
ATOM   785  C CA  . LYS A 1 100 ? 13.750  3.536   20.421  1.00 36.70  ? 101 LYS A CA  1 
ATOM   786  C C   . LYS A 1 100 ? 13.362  4.064   19.031  1.00 38.25  ? 101 LYS A C   1 
ATOM   787  O O   . LYS A 1 100 ? 12.159  4.158   18.731  1.00 34.69  ? 101 LYS A O   1 
ATOM   788  C CB  . LYS A 1 100 ? 13.519  2.032   20.552  1.00 40.88  ? 101 LYS A CB  1 
ATOM   789  C CG  . LYS A 1 100 ? 14.059  1.250   19.359  1.00 44.90  ? 101 LYS A CG  1 
ATOM   790  C CD  . LYS A 1 100 ? 14.558  -0.107  19.710  1.00 45.64  ? 101 LYS A CD  1 
ATOM   791  C CE  . LYS A 1 100 ? 14.713  -1.049  18.545  1.00 50.33  ? 101 LYS A CE  1 
ATOM   792  N NZ  . LYS A 1 100 ? 16.037  -0.851  17.910  1.00 54.93  ? 101 LYS A NZ  1 
ATOM   793  N N   . ASP A 1 101 ? 14.363  4.462   18.241  1.00 40.19  ? 102 ASP A N   1 
ATOM   794  C CA  . ASP A 1 101 ? 14.183  4.972   16.857  1.00 41.10  ? 102 ASP A CA  1 
ATOM   795  C C   . ASP A 1 101 ? 13.372  6.259   16.875  1.00 45.36  ? 102 ASP A C   1 
ATOM   796  O O   . ASP A 1 101 ? 12.807  6.594   15.842  1.00 40.84  ? 102 ASP A O   1 
ATOM   797  C CB  . ASP A 1 101 ? 13.573  3.926   15.917  1.00 43.26  ? 102 ASP A CB  1 
ATOM   798  C CG  . ASP A 1 101 ? 14.520  2.760   15.727  1.00 45.41  ? 102 ASP A CG  1 
ATOM   799  O OD1 . ASP A 1 101 ? 15.710  2.984   15.940  1.00 50.13  ? 102 ASP A OD1 1 
ATOM   800  O OD2 . ASP A 1 101 ? 14.052  1.623   15.537  1.00 42.13  ? 102 ASP A OD2 1 
ATOM   801  N N   . ASP A 1 102 ? 13.395  7.005   17.971  1.00 41.91  ? 103 ASP A N   1 
ATOM   802  C CA  . ASP A 1 102 ? 12.672  8.294   18.034  1.00 36.31  ? 103 ASP A CA  1 
ATOM   803  C C   . ASP A 1 102 ? 13.477  9.187   18.976  1.00 38.14  ? 103 ASP A C   1 
ATOM   804  O O   . ASP A 1 102 ? 14.642  8.863   19.186  1.00 32.43  ? 103 ASP A O   1 
ATOM   805  C CB  . ASP A 1 102 ? 11.196  8.026   18.364  1.00 38.82  ? 103 ASP A CB  1 
ATOM   806  C CG  . ASP A 1 102 ? 10.232  9.134   17.939  1.00 40.16  ? 103 ASP A CG  1 
ATOM   807  O OD1 . ASP A 1 102 ? 10.694  10.253  17.650  1.00 43.07  ? 103 ASP A OD1 1 
ATOM   808  O OD2 . ASP A 1 102 ? 9.010   8.872   17.891  1.00 47.55  ? 103 ASP A OD2 1 
ATOM   809  N N   . GLY A 1 103 ? 12.898  10.272  19.534  1.00 36.03  ? 104 GLY A N   1 
ATOM   810  C CA  . GLY A 1 103 ? 13.622  11.219  20.385  1.00 37.50  ? 104 GLY A CA  1 
ATOM   811  C C   . GLY A 1 103 ? 13.817  10.783  21.824  1.00 35.42  ? 104 GLY A C   1 
ATOM   812  O O   . GLY A 1 103 ? 13.552  9.616   22.189  1.00 36.18  ? 104 GLY A O   1 
ATOM   813  N N   . ASN A 1 104 ? 14.293  11.700  22.617  1.00 34.69  ? 105 ASN A N   1 
ATOM   814  C CA  . ASN A 1 104 ? 14.551  11.452  24.058  1.00 34.49  ? 105 ASN A CA  1 
ATOM   815  C C   . ASN A 1 104 ? 13.950  12.604  24.868  1.00 39.78  ? 105 ASN A C   1 
ATOM   816  O O   . ASN A 1 104 ? 13.868  13.735  24.399  1.00 37.87  ? 105 ASN A O   1 
ATOM   817  C CB  . ASN A 1 104 ? 16.036  11.227  24.357  1.00 36.78  ? 105 ASN A CB  1 
ATOM   818  C CG  . ASN A 1 104 ? 16.900  12.386  23.913  1.00 41.38  ? 105 ASN A CG  1 
ATOM   819  O OD1 . ASN A 1 104 ? 17.275  12.490  22.746  1.00 47.09  ? 105 ASN A OD1 1 
ATOM   820  N ND2 . ASN A 1 104 ? 17.083  13.318  24.778  1.00 33.01  ? 105 ASN A ND2 1 
ATOM   821  N N   . TYR A 1 105 ? 13.502  12.285  26.068  1.00 36.63  ? 106 TYR A N   1 
ATOM   822  C CA  . TYR A 1 105 ? 13.143  13.264  27.099  1.00 34.93  ? 106 TYR A CA  1 
ATOM   823  C C   . TYR A 1 105 ? 14.293  13.310  28.121  1.00 34.32  ? 106 TYR A C   1 
ATOM   824  O O   . TYR A 1 105 ? 14.906  12.285  28.520  1.00 33.72  ? 106 TYR A O   1 
ATOM   825  C CB  . TYR A 1 105 ? 11.869  12.919  27.869  1.00 33.64  ? 106 TYR A CB  1 
ATOM   826  C CG  . TYR A 1 105 ? 10.581  12.762  27.106  1.00 33.48  ? 106 TYR A CG  1 
ATOM   827  C CD1 . TYR A 1 105 ? 10.361  13.375  25.890  1.00 34.08  ? 106 TYR A CD1 1 
ATOM   828  C CD2 . TYR A 1 105 ? 9.521   12.086  27.687  1.00 32.36  ? 106 TYR A CD2 1 
ATOM   829  C CE1 . TYR A 1 105 ? 9.148   13.264  25.251  1.00 35.54  ? 106 TYR A CE1 1 
ATOM   830  C CE2 . TYR A 1 105 ? 8.285   12.010  27.085  1.00 33.18  ? 106 TYR A CE2 1 
ATOM   831  C CZ  . TYR A 1 105 ? 8.097   12.581  25.834  1.00 39.65  ? 106 TYR A CZ  1 
ATOM   832  O OH  . TYR A 1 105 ? 6.884   12.527  25.195  1.00 35.80  ? 106 TYR A OH  1 
ATOM   833  N N   . LYS A 1 106 ? 14.570  14.523  28.544  1.00 34.61  ? 107 LYS A N   1 
ATOM   834  C CA  . LYS A 1 106 ? 15.383  14.890  29.727  1.00 33.22  ? 107 LYS A CA  1 
ATOM   835  C C   . LYS A 1 106 ? 14.448  15.528  30.745  1.00 34.99  ? 107 LYS A C   1 
ATOM   836  O O   . LYS A 1 106 ? 13.769  16.507  30.396  1.00 33.46  ? 107 LYS A O   1 
ATOM   837  C CB  . LYS A 1 106 ? 16.552  15.791  29.359  1.00 38.82  ? 107 LYS A CB  1 
ATOM   838  C CG  . LYS A 1 106 ? 17.655  15.019  28.641  1.00 49.44  ? 107 LYS A CG  1 
ATOM   839  C CD  . LYS A 1 106 ? 18.993  15.737  28.481  1.00 58.48  ? 107 LYS A CD  1 
ATOM   840  C CE  . LYS A 1 106 ? 20.110  14.796  28.050  1.00 57.77  ? 107 LYS A CE  1 
ATOM   841  N NZ  . LYS A 1 106 ? 19.836  14.148  26.729  1.00 64.37  ? 107 LYS A NZ  1 
ATOM   842  N N   . THR A 1 107 ? 14.384  14.977  31.966  1.00 34.36  ? 108 THR A N   1 
ATOM   843  C CA  . THR A 1 107 ? 13.470  15.543  32.986  1.00 35.46  ? 108 THR A CA  1 
ATOM   844  C C   . THR A 1 107 ? 14.277  15.877  34.233  1.00 38.17  ? 108 THR A C   1 
ATOM   845  O O   . THR A 1 107 ? 15.220  15.150  34.562  1.00 32.69  ? 108 THR A O   1 
ATOM   846  C CB  . THR A 1 107 ? 12.315  14.595  33.312  1.00 36.90  ? 108 THR A CB  1 
ATOM   847  O OG1 . THR A 1 107 ? 12.810  13.428  33.970  1.00 30.26  ? 108 THR A OG1 1 
ATOM   848  C CG2 . THR A 1 107 ? 11.579  14.180  32.076  1.00 34.90  ? 108 THR A CG2 1 
ATOM   849  N N   . ARG A 1 108 ? 13.895  16.954  34.911  1.00 33.44  ? 109 ARG A N   1 
ATOM   850  C CA  . ARG A 1 108 ? 14.418  17.312  36.248  1.00 34.66  ? 109 ARG A CA  1 
ATOM   851  C C   . ARG A 1 108 ? 13.212  17.699  37.097  1.00 38.44  ? 109 ARG A C   1 
ATOM   852  O O   . ARG A 1 108 ? 12.390  18.525  36.626  1.00 36.42  ? 109 ARG A O   1 
ATOM   853  C CB  . ARG A 1 108 ? 15.393  18.487  36.161  1.00 40.70  ? 109 ARG A CB  1 
ATOM   854  C CG  . ARG A 1 108 ? 15.966  18.901  37.512  1.00 41.44  ? 109 ARG A CG  1 
ATOM   855  C CD  . ARG A 1 108 ? 16.932  20.090  37.416  1.00 45.34  ? 109 ARG A CD  1 
ATOM   856  N NE  . ARG A 1 108 ? 17.621  20.221  38.691  1.00 45.20  ? 109 ARG A NE  1 
ATOM   857  C CZ  . ARG A 1 108 ? 17.091  20.761  39.779  1.00 46.20  ? 109 ARG A CZ  1 
ATOM   858  N NH1 . ARG A 1 108 ? 15.857  21.259  39.767  1.00 53.11  ? 109 ARG A NH1 1 
ATOM   859  N NH2 . ARG A 1 108 ? 17.826  20.853  40.866  1.00 47.88  ? 109 ARG A NH2 1 
ATOM   860  N N   . ALA A 1 109 ? 13.080  17.083  38.264  1.00 34.91  ? 110 ALA A N   1 
ATOM   861  C CA  . ALA A 1 109 ? 11.922  17.294  39.150  1.00 35.50  ? 110 ALA A CA  1 
ATOM   862  C C   . ALA A 1 109 ? 12.455  17.557  40.542  1.00 36.03  ? 110 ALA A C   1 
ATOM   863  O O   . ALA A 1 109 ? 13.532  17.021  40.896  1.00 33.18  ? 110 ALA A O   1 
ATOM   864  C CB  . ALA A 1 109 ? 11.017  16.104  39.166  1.00 36.19  ? 110 ALA A CB  1 
ATOM   865  N N   . GLU A 1 110 ? 11.725  18.373  41.286  1.00 34.51  ? 111 GLU A N   1 
ATOM   866  C CA  . GLU A 1 110 ? 11.934  18.460  42.737  1.00 30.45  ? 111 GLU A CA  1 
ATOM   867  C C   . GLU A 1 110 ? 10.675  17.918  43.400  1.00 31.57  ? 111 GLU A C   1 
ATOM   868  O O   . GLU A 1 110 ? 9.553   18.407  43.095  1.00 29.69  ? 111 GLU A O   1 
ATOM   869  C CB  . GLU A 1 110 ? 12.221  19.890  43.231  1.00 36.39  ? 111 GLU A CB  1 
ATOM   870  C CG  . GLU A 1 110 ? 13.650  20.287  42.903  1.00 41.85  ? 111 GLU A CG  1 
ATOM   871  C CD  . GLU A 1 110 ? 14.020  21.690  43.363  1.00 51.68  ? 111 GLU A CD  1 
ATOM   872  O OE1 . GLU A 1 110 ? 13.315  22.218  44.325  1.00 49.67  ? 111 GLU A OE1 1 
ATOM   873  O OE2 . GLU A 1 110 ? 14.943  22.263  42.701  1.00 53.23  ? 111 GLU A OE2 1 
ATOM   874  N N   . VAL A 1 111 ? 10.905  16.991  44.314  1.00 29.71  ? 112 VAL A N   1 
ATOM   875  C CA  . VAL A 1 111 ? 9.811   16.316  45.033  1.00 29.84  ? 112 VAL A CA  1 
ATOM   876  C C   . VAL A 1 111 ? 9.977   16.644  46.492  1.00 30.10  ? 112 VAL A C   1 
ATOM   877  O O   . VAL A 1 111 ? 11.006  16.269  47.089  1.00 30.80  ? 112 VAL A O   1 
ATOM   878  C CB  . VAL A 1 111 ? 9.797   14.811  44.759  1.00 31.26  ? 112 VAL A CB  1 
ATOM   879  C CG1 . VAL A 1 111 ? 8.549   14.218  45.371  1.00 30.75  ? 112 VAL A CG1 1 
ATOM   880  C CG2 . VAL A 1 111 ? 9.863   14.516  43.286  1.00 31.30  ? 112 VAL A CG2 1 
ATOM   881  N N   . LYS A 1 112 ? 9.007   17.366  47.085  1.00 30.74  ? 113 LYS A N   1 
ATOM   882  C CA  . LYS A 1 112 ? 9.182   17.764  48.504  1.00 31.87  ? 113 LYS A CA  1 
ATOM   883  C C   . LYS A 1 112 ? 7.839   18.143  49.123  1.00 29.46  ? 113 LYS A C   1 
ATOM   884  O O   . LYS A 1 112 ? 6.904   18.422  48.385  1.00 32.23  ? 113 LYS A O   1 
ATOM   885  C CB  . LYS A 1 112 ? 10.161  18.956  48.624  1.00 36.20  ? 113 LYS A CB  1 
ATOM   886  C CG  . LYS A 1 112 ? 9.623   20.263  48.037  1.00 43.80  ? 113 LYS A CG  1 
ATOM   887  C CD  . LYS A 1 112 ? 10.488  21.538  48.264  1.00 51.18  ? 113 LYS A CD  1 
ATOM   888  C CE  . LYS A 1 112 ? 11.636  21.677  47.280  1.00 62.19  ? 113 LYS A CE  1 
ATOM   889  N NZ  . LYS A 1 112 ? 11.327  22.558  46.124  1.00 72.27  ? 113 LYS A NZ  1 
ATOM   890  N N   . PHE A 1 113 ? 7.825   18.315  50.448  1.00 32.09  ? 114 PHE A N   1 
ATOM   891  C CA  . PHE A 1 113 ? 6.618   18.790  51.166  1.00 32.92  ? 114 PHE A CA  1 
ATOM   892  C C   . PHE A 1 113 ? 6.600   20.327  51.120  1.00 34.35  ? 114 PHE A C   1 
ATOM   893  O O   . PHE A 1 113 ? 7.665   20.934  51.290  1.00 37.35  ? 114 PHE A O   1 
ATOM   894  C CB  . PHE A 1 113 ? 6.607   18.263  52.605  1.00 32.08  ? 114 PHE A CB  1 
ATOM   895  C CG  . PHE A 1 113 ? 6.000   16.874  52.740  1.00 31.23  ? 114 PHE A CG  1 
ATOM   896  C CD1 . PHE A 1 113 ? 4.628   16.692  52.863  1.00 33.39  ? 114 PHE A CD1 1 
ATOM   897  C CD2 . PHE A 1 113 ? 6.805   15.754  52.617  1.00 32.58  ? 114 PHE A CD2 1 
ATOM   898  C CE1 . PHE A 1 113 ? 4.079   15.417  52.959  1.00 35.90  ? 114 PHE A CE1 1 
ATOM   899  C CE2 . PHE A 1 113 ? 6.265   14.472  52.703  1.00 31.37  ? 114 PHE A CE2 1 
ATOM   900  C CZ  . PHE A 1 113 ? 4.910   14.304  52.905  1.00 33.57  ? 114 PHE A CZ  1 
ATOM   901  N N   . GLU A 1 114 ? 5.431   20.880  50.868  1.00 33.34  ? 115 GLU A N   1 
ATOM   902  C CA  . GLU A 1 114 ? 5.050   22.280  51.124  1.00 36.76  ? 115 GLU A CA  1 
ATOM   903  C C   . GLU A 1 114 ? 3.898   22.167  52.087  1.00 35.44  ? 115 GLU A C   1 
ATOM   904  O O   . GLU A 1 114 ? 2.792   21.833  51.697  1.00 32.89  ? 115 GLU A O   1 
ATOM   905  C CB  . GLU A 1 114 ? 4.639   22.996  49.836  1.00 37.33  ? 115 GLU A CB  1 
ATOM   906  C CG  . GLU A 1 114 ? 5.739   23.069  48.794  1.00 45.98  ? 115 GLU A CG  1 
ATOM   907  C CD  . GLU A 1 114 ? 6.818   24.115  49.034  1.00 59.73  ? 115 GLU A CD  1 
ATOM   908  O OE1 . GLU A 1 114 ? 6.613   25.000  49.919  1.00 53.40  ? 115 GLU A OE1 1 
ATOM   909  O OE2 . GLU A 1 114 ? 7.867   24.050  48.337  1.00 59.40  ? 115 GLU A OE2 1 
ATOM   910  N N   . GLY A 1 115 ? 4.191   22.374  53.351  1.00 33.55  ? 116 GLY A N   1 
ATOM   911  C CA  . GLY A 1 115 ? 3.218   22.070  54.395  1.00 34.66  ? 116 GLY A CA  1 
ATOM   912  C C   . GLY A 1 115 ? 2.867   20.597  54.345  1.00 35.10  ? 116 GLY A C   1 
ATOM   913  O O   . GLY A 1 115 ? 3.797   19.770  54.354  1.00 37.00  ? 116 GLY A O   1 
ATOM   914  N N   . ASP A 1 116 ? 1.586   20.289  54.352  1.00 31.22  ? 117 ASP A N   1 
ATOM   915  C CA  . ASP A 1 116 ? 1.102   18.887  54.340  1.00 37.05  ? 117 ASP A CA  1 
ATOM   916  C C   . ASP A 1 116 ? 1.019   18.327  52.916  1.00 33.33  ? 117 ASP A C   1 
ATOM   917  O O   . ASP A 1 116 ? 0.706   17.186  52.799  1.00 32.62  ? 117 ASP A O   1 
ATOM   918  C CB  . ASP A 1 116 ? -0.260  18.769  54.992  1.00 38.78  ? 117 ASP A CB  1 
ATOM   919  C CG  . ASP A 1 116 ? -0.144  18.948  56.518  1.00 52.43  ? 117 ASP A CG  1 
ATOM   920  O OD1 . ASP A 1 116 ? 0.974   18.726  57.098  1.00 43.25  ? 117 ASP A OD1 1 
ATOM   921  O OD2 . ASP A 1 116 ? -1.125  19.361  57.098  1.00 58.46  ? 117 ASP A OD2 1 
ATOM   922  N N   . THR A 1 117 ? 1.292   19.103  51.888  1.00 32.41  ? 118 THR A N   1 
ATOM   923  C CA  . THR A 1 117 ? 1.136   18.624  50.492  1.00 27.72  ? 118 THR A CA  1 
ATOM   924  C C   . THR A 1 117 ? 2.465   18.099  49.985  1.00 29.81  ? 118 THR A C   1 
ATOM   925  O O   . THR A 1 117 ? 3.497   18.797  50.102  1.00 30.90  ? 118 THR A O   1 
ATOM   926  C CB  . THR A 1 117 ? 0.539   19.722  49.605  1.00 31.09  ? 118 THR A CB  1 
ATOM   927  O OG1 . THR A 1 117 ? -0.742  19.981  50.153  1.00 34.14  ? 118 THR A OG1 1 
ATOM   928  C CG2 . THR A 1 117 ? 0.381   19.339  48.148  1.00 30.82  ? 118 THR A CG2 1 
ATOM   929  N N   . LEU A 1 118 ? 2.408   16.978  49.259  1.00 31.80  ? 119 LEU A N   1 
ATOM   930  C CA  . LEU A 1 118 ? 3.617   16.471  48.552  1.00 28.13  ? 119 LEU A CA  1 
ATOM   931  C C   . LEU A 1 118 ? 3.576   17.036  47.151  1.00 27.90  ? 119 LEU A C   1 
ATOM   932  O O   . LEU A 1 118 ? 2.581   16.785  46.445  1.00 32.01  ? 119 LEU A O   1 
ATOM   933  C CB  . LEU A 1 118 ? 3.615   14.934  48.551  1.00 29.52  ? 119 LEU A CB  1 
ATOM   934  C CG  . LEU A 1 118 ? 4.869   14.260  48.009  1.00 26.30  ? 119 LEU A CG  1 
ATOM   935  C CD1 . LEU A 1 118 ? 4.925   14.289  46.472  1.00 28.85  ? 119 LEU A CD1 1 
ATOM   936  C CD2 . LEU A 1 118 ? 6.181   14.678  48.716  1.00 29.86  ? 119 LEU A CD2 1 
ATOM   937  N N   . VAL A 1 119 ? 4.602   17.818  46.813  1.00 30.15  ? 120 VAL A N   1 
ATOM   938  C CA  . VAL A 1 119 ? 4.684   18.604  45.562  1.00 29.08  ? 120 VAL A CA  1 
ATOM   939  C C   . VAL A 1 119 ? 5.791   18.082  44.664  1.00 25.94  ? 120 VAL A C   1 
ATOM   940  O O   . VAL A 1 119 ? 6.918   17.869  45.122  1.00 32.96  ? 120 VAL A O   1 
ATOM   941  C CB  . VAL A 1 119 ? 4.921   20.097  45.850  1.00 31.28  ? 120 VAL A CB  1 
ATOM   942  C CG1 . VAL A 1 119 ? 4.942   20.883  44.550  1.00 35.14  ? 120 VAL A CG1 1 
ATOM   943  C CG2 . VAL A 1 119 ? 3.876   20.652  46.804  1.00 31.88  ? 120 VAL A CG2 1 
ATOM   944  N N   . ASN A 1 120 ? 5.417   17.786  43.431  1.00 29.97  ? 121 ASN A N   1 
ATOM   945  C CA  . ASN A 1 120 ? 6.291   17.256  42.385  1.00 29.27  ? 121 ASN A CA  1 
ATOM   946  C C   . ASN A 1 120 ? 6.349   18.306  41.276  1.00 29.00  ? 121 ASN A C   1 
ATOM   947  O O   . ASN A 1 120 ? 5.422   18.375  40.539  1.00 32.86  ? 121 ASN A O   1 
ATOM   948  C CB  . ASN A 1 120 ? 5.716   15.954  41.829  1.00 32.06  ? 121 ASN A CB  1 
ATOM   949  C CG  . ASN A 1 120 ? 6.661   15.283  40.863  1.00 35.26  ? 121 ASN A CG  1 
ATOM   950  O OD1 . ASN A 1 120 ? 7.811   15.704  40.696  1.00 30.66  ? 121 ASN A OD1 1 
ATOM   951  N ND2 . ASN A 1 120 ? 6.114   14.267  40.193  1.00 35.72  ? 121 ASN A ND2 1 
ATOM   952  N N   . ARG A 1 121 ? 7.421   19.092  41.220  1.00 29.42  ? 122 ARG A N   1 
ATOM   953  C CA  . ARG A 1 121 ? 7.605   20.128  40.183  1.00 32.22  ? 122 ARG A CA  1 
ATOM   954  C C   . ARG A 1 121 ? 8.613   19.672  39.146  1.00 28.94  ? 122 ARG A C   1 
ATOM   955  O O   . ARG A 1 121 ? 9.753   19.344  39.512  1.00 32.60  ? 122 ARG A O   1 
ATOM   956  C CB  . ARG A 1 121 ? 8.117   21.413  40.838  1.00 33.92  ? 122 ARG A CB  1 
ATOM   957  C CG  . ARG A 1 121 ? 7.014   22.219  41.483  1.00 41.57  ? 122 ARG A CG  1 
ATOM   958  C CD  . ARG A 1 121 ? 7.604   23.577  41.925  1.00 55.91  ? 122 ARG A CD  1 
ATOM   959  N NE  . ARG A 1 121 ? 7.130   23.901  43.258  1.00 68.99  ? 122 ARG A NE  1 
ATOM   960  C CZ  . ARG A 1 121 ? 7.270   25.060  43.899  1.00 83.13  ? 122 ARG A CZ  1 
ATOM   961  N NH1 . ARG A 1 121 ? 6.708   25.222  45.096  1.00 58.10  ? 122 ARG A NH1 1 
ATOM   962  N NH2 . ARG A 1 121 ? 7.909   26.064  43.315  1.00 98.63  ? 122 ARG A NH2 1 
ATOM   963  N N   . ILE A 1 122 ? 8.205   19.646  37.891  1.00 31.55  ? 123 ILE A N   1 
ATOM   964  C CA  . ILE A 1 122 ? 8.960   18.967  36.809  1.00 31.84  ? 123 ILE A CA  1 
ATOM   965  C C   . ILE A 1 122 ? 9.211   19.919  35.624  1.00 32.67  ? 123 ILE A C   1 
ATOM   966  O O   . ILE A 1 122 ? 8.231   20.547  35.187  1.00 31.22  ? 123 ILE A O   1 
ATOM   967  C CB  . ILE A 1 122 ? 8.153   17.782  36.292  1.00 30.69  ? 123 ILE A CB  1 
ATOM   968  C CG1 . ILE A 1 122 ? 7.681   16.890  37.446  1.00 33.55  ? 123 ILE A CG1 1 
ATOM   969  C CG2 . ILE A 1 122 ? 9.005   16.988  35.314  1.00 34.16  ? 123 ILE A CG2 1 
ATOM   970  C CD1 . ILE A 1 122 ? 6.436   16.106  37.110  1.00 35.20  ? 123 ILE A CD1 1 
ATOM   971  N N   . GLU A 1 123 ? 10.423  19.892  35.079  1.00 32.99  ? 124 GLU A N   1 
ATOM   972  C CA  . GLU A 1 123 ? 10.731  20.459  33.727  1.00 36.93  ? 124 GLU A CA  1 
ATOM   973  C C   . GLU A 1 123 ? 11.122  19.322  32.784  1.00 34.63  ? 124 GLU A C   1 
ATOM   974  O O   . GLU A 1 123 ? 11.977  18.470  33.180  1.00 35.30  ? 124 GLU A O   1 
ATOM   975  C CB  . GLU A 1 123 ? 11.931  21.379  33.708  1.00 38.38  ? 124 GLU A CB  1 
ATOM   976  C CG  . GLU A 1 123 ? 12.178  22.232  34.911  1.00 61.16  ? 124 GLU A CG  1 
ATOM   977  C CD  . GLU A 1 123 ? 13.515  22.951  34.737  1.00 76.26  ? 124 GLU A CD  1 
ATOM   978  O OE1 . GLU A 1 123 ? 14.364  22.901  35.691  1.00 78.96  ? 124 GLU A OE1 1 
ATOM   979  O OE2 . GLU A 1 123 ? 13.736  23.488  33.604  1.00 82.98  ? 124 GLU A OE2 1 
ATOM   980  N N   . LEU A 1 124 ? 10.477  19.224  31.629  1.00 35.78  ? 125 LEU A N   1 
ATOM   981  C CA  . LEU A 1 124 ? 10.766  18.176  30.622  1.00 31.17  ? 125 LEU A CA  1 
ATOM   982  C C   . LEU A 1 124 ? 11.185  18.833  29.289  1.00 36.35  ? 125 LEU A C   1 
ATOM   983  O O   . LEU A 1 124 ? 10.517  19.801  28.883  1.00 35.00  ? 125 LEU A O   1 
ATOM   984  C CB  . LEU A 1 124 ? 9.504   17.348  30.441  1.00 32.82  ? 125 LEU A CB  1 
ATOM   985  C CG  . LEU A 1 124 ? 9.598   16.232  29.410  1.00 32.24  ? 125 LEU A CG  1 
ATOM   986  C CD1 . LEU A 1 124 ? 8.706   15.093  29.823  1.00 36.55  ? 125 LEU A CD1 1 
ATOM   987  C CD2 . LEU A 1 124 ? 9.188   16.722  28.014  1.00 34.56  ? 125 LEU A CD2 1 
ATOM   988  N N   . LYS A 1 125 ? 12.286  18.363  28.706  1.00 38.46  ? 126 LYS A N   1 
ATOM   989  C CA  . LYS A 1 125 ? 12.783  18.791  27.377  1.00 36.76  ? 126 LYS A CA  1 
ATOM   990  C C   . LYS A 1 125 ? 12.922  17.548  26.532  1.00 36.95  ? 126 LYS A C   1 
ATOM   991  O O   . LYS A 1 125 ? 13.710  16.632  26.935  1.00 37.00  ? 126 LYS A O   1 
ATOM   992  C CB  . LYS A 1 125 ? 14.117  19.530  27.467  1.00 48.58  ? 126 LYS A CB  1 
ATOM   993  C CG  . LYS A 1 125 ? 14.672  19.996  26.108  1.00 55.50  ? 126 LYS A CG  1 
ATOM   994  C CD  . LYS A 1 125 ? 14.019  21.306  25.597  1.00 69.53  ? 126 LYS A CD  1 
ATOM   995  C CE  . LYS A 1 125 ? 14.577  21.855  24.293  1.00 62.62  ? 126 LYS A CE  1 
ATOM   996  N NZ  . LYS A 1 125 ? 16.000  22.214  24.462  1.00 71.64  ? 126 LYS A NZ  1 
ATOM   997  N N   . GLY A 1 126 ? 12.209  17.540  25.413  1.00 34.83  ? 127 GLY A N   1 
ATOM   998  C CA  . GLY A 1 126 ? 12.289  16.474  24.409  1.00 34.18  ? 127 GLY A CA  1 
ATOM   999  C C   . GLY A 1 126 ? 12.884  16.992  23.109  1.00 38.35  ? 127 GLY A C   1 
ATOM   1000 O O   . GLY A 1 126 ? 12.440  18.099  22.677  1.00 36.92  ? 127 GLY A O   1 
ATOM   1001 N N   . VAL A 1 127 ? 13.765  16.203  22.492  1.00 41.12  ? 128 VAL A N   1 
ATOM   1002 C CA  . VAL A 1 127 ? 14.496  16.612  21.245  1.00 40.80  ? 128 VAL A CA  1 
ATOM   1003 C C   . VAL A 1 127 ? 14.538  15.430  20.300  1.00 39.97  ? 128 VAL A C   1 
ATOM   1004 O O   . VAL A 1 127 ? 14.474  14.299  20.779  1.00 36.70  ? 128 VAL A O   1 
ATOM   1005 C CB  . VAL A 1 127 ? 15.907  17.118  21.526  1.00 41.59  ? 128 VAL A CB  1 
ATOM   1006 C CG1 . VAL A 1 127 ? 15.860  18.421  22.315  1.00 49.20  ? 128 VAL A CG1 1 
ATOM   1007 C CG2 . VAL A 1 127 ? 16.809  16.056  22.165  1.00 46.28  ? 128 VAL A CG2 1 
ATOM   1008 N N   . ASP A 1 128 ? 14.569  15.708  18.999  1.00 39.23  ? 129 ASP A N   1 
ATOM   1009 C CA  . ASP A 1 128 ? 14.860  14.694  17.949  1.00 39.45  ? 129 ASP A CA  1 
ATOM   1010 C C   . ASP A 1 128 ? 13.724  13.694  17.811  1.00 38.85  ? 129 ASP A C   1 
ATOM   1011 O O   . ASP A 1 128 ? 13.977  12.532  17.521  1.00 39.83  ? 129 ASP A O   1 
ATOM   1012 C CB  . ASP A 1 128 ? 16.164  13.957  18.229  1.00 44.84  ? 129 ASP A CB  1 
ATOM   1013 C CG  . ASP A 1 128 ? 17.321  14.931  18.164  1.00 51.85  ? 129 ASP A CG  1 
ATOM   1014 O OD1 . ASP A 1 128 ? 17.155  15.954  17.477  1.00 53.35  ? 129 ASP A OD1 1 
ATOM   1015 O OD2 . ASP A 1 128 ? 18.364  14.642  18.736  1.00 66.10  ? 129 ASP A OD2 1 
ATOM   1016 N N   . PHE A 1 129 ? 12.501  14.162  18.005  1.00 36.74  ? 130 PHE A N   1 
ATOM   1017 C CA  . PHE A 1 129 ? 11.303  13.354  17.755  1.00 44.27  ? 130 PHE A CA  1 
ATOM   1018 C C   . PHE A 1 129 ? 10.968  13.502  16.278  1.00 46.55  ? 130 PHE A C   1 
ATOM   1019 O O   . PHE A 1 129 ? 11.198  14.616  15.720  1.00 41.30  ? 130 PHE A O   1 
ATOM   1020 C CB  . PHE A 1 129 ? 10.193  13.776  18.710  1.00 42.60  ? 130 PHE A CB  1 
ATOM   1021 C CG  . PHE A 1 129 ? 10.418  13.239  20.102  1.00 37.56  ? 130 PHE A CG  1 
ATOM   1022 C CD1 . PHE A 1 129 ? 10.030  11.930  20.422  1.00 43.36  ? 130 PHE A CD1 1 
ATOM   1023 C CD2 . PHE A 1 129 ? 11.034  14.001  21.075  1.00 39.82  ? 130 PHE A CD2 1 
ATOM   1024 C CE1 . PHE A 1 129 ? 10.244  11.415  21.702  1.00 34.68  ? 130 PHE A CE1 1 
ATOM   1025 C CE2 . PHE A 1 129 ? 11.310  13.466  22.328  1.00 38.83  ? 130 PHE A CE2 1 
ATOM   1026 C CZ  . PHE A 1 129 ? 10.908  12.188  22.641  1.00 33.73  ? 130 PHE A CZ  1 
ATOM   1027 N N   . LYS A 1 130 ? 10.400  12.438  15.720  1.00 42.77  ? 131 LYS A N   1 
ATOM   1028 C CA  . LYS A 1 130 ? 9.819   12.399  14.345  1.00 48.04  ? 131 LYS A CA  1 
ATOM   1029 C C   . LYS A 1 130 ? 8.412   12.985  14.373  1.00 49.51  ? 131 LYS A C   1 
ATOM   1030 O O   . LYS A 1 130 ? 7.535   12.401  15.078  1.00 44.80  ? 131 LYS A O   1 
ATOM   1031 C CB  . LYS A 1 130 ? 9.772   10.973  13.833  1.00 51.95  ? 131 LYS A CB  1 
ATOM   1032 C CG  . LYS A 1 130 ? 11.143  10.342  13.709  1.00 64.58  ? 131 LYS A CG  1 
ATOM   1033 C CD  . LYS A 1 130 ? 11.141  8.892   13.315  1.00 67.97  ? 131 LYS A CD  1 
ATOM   1034 C CE  . LYS A 1 130 ? 12.566  8.380   13.335  1.00 72.71  ? 131 LYS A CE  1 
ATOM   1035 N NZ  . LYS A 1 130 ? 12.644  6.927   13.068  1.00 83.03  ? 131 LYS A NZ  1 
ATOM   1036 N N   . GLU A 1 131 ? 8.183   14.071  13.625  1.00 50.39  ? 132 GLU A N   1 
ATOM   1037 C CA  . GLU A 1 131 ? 6.926   14.849  13.741  1.00 54.43  ? 132 GLU A CA  1 
ATOM   1038 C C   . GLU A 1 131 ? 5.808   13.947  13.239  1.00 61.73  ? 132 GLU A C   1 
ATOM   1039 O O   . GLU A 1 131 ? 4.651   14.185  13.657  1.00 61.77  ? 132 GLU A O   1 
ATOM   1040 C CB  . GLU A 1 131 ? 6.940   16.209  13.047  1.00 47.89  ? 132 GLU A CB  1 
ATOM   1041 C CG  . GLU A 1 131 ? 7.779   17.247  13.764  1.00 47.82  ? 132 GLU A CG  1 
ATOM   1042 C CD  . GLU A 1 131 ? 7.135   18.042  14.907  1.00 47.71  ? 132 GLU A CD  1 
ATOM   1043 O OE1 . GLU A 1 131 ? 7.887   18.844  15.531  1.00 56.67  ? 132 GLU A OE1 1 
ATOM   1044 O OE2 . GLU A 1 131 ? 5.869   17.932  15.126  1.00 47.57  ? 132 GLU A OE2 1 
ATOM   1045 N N   . ASP A 1 132 ? 6.148   12.895  12.490  1.00 56.71  ? 133 ASP A N   1 
ATOM   1046 C CA  . ASP A 1 132 ? 5.130   11.911  12.032  1.00 68.08  ? 133 ASP A CA  1 
ATOM   1047 C C   . ASP A 1 132 ? 5.378   10.502  12.614  1.00 62.41  ? 133 ASP A C   1 
ATOM   1048 O O   . ASP A 1 132 ? 4.681   9.587   12.160  1.00 76.99  ? 133 ASP A O   1 
ATOM   1049 C CB  . ASP A 1 132 ? 5.072   11.903  10.502  1.00 79.25  ? 133 ASP A CB  1 
ATOM   1050 C CG  . ASP A 1 132 ? 6.388   11.530  9.833   1.00 91.52  ? 133 ASP A CG  1 
ATOM   1051 O OD1 . ASP A 1 132 ? 7.404   11.311  10.569  1.00 90.44  ? 133 ASP A OD1 1 
ATOM   1052 O OD2 . ASP A 1 132 ? 6.397   11.463  8.574   1.00 94.29  ? 133 ASP A OD2 1 
ATOM   1053 N N   . GLY A 1 133 ? 6.252   10.319  13.620  1.00 59.66  ? 134 GLY A N   1 
ATOM   1054 C CA  . GLY A 1 133 ? 6.472   9.024   14.315  1.00 51.25  ? 134 GLY A CA  1 
ATOM   1055 C C   . GLY A 1 133 ? 5.345   8.690   15.305  1.00 43.10  ? 134 GLY A C   1 
ATOM   1056 O O   . GLY A 1 133 ? 4.293   9.361   15.308  1.00 51.46  ? 134 GLY A O   1 
ATOM   1057 N N   . ASN A 1 134 ? 5.533   7.653   16.101  1.00 46.63  ? 135 ASN A N   1 
ATOM   1058 C CA  . ASN A 1 134 ? 4.482   7.124   17.009  1.00 47.02  ? 135 ASN A CA  1 
ATOM   1059 C C   . ASN A 1 134 ? 4.186   8.074   18.188  1.00 47.58  ? 135 ASN A C   1 
ATOM   1060 O O   . ASN A 1 134 ? 3.082   7.918   18.799  1.00 42.67  ? 135 ASN A O   1 
ATOM   1061 C CB  . ASN A 1 134 ? 4.835   5.728   17.467  1.00 51.16  ? 135 ASN A CB  1 
ATOM   1062 C CG  . ASN A 1 134 ? 4.948   4.771   16.303  1.00 48.70  ? 135 ASN A CG  1 
ATOM   1063 O OD1 . ASN A 1 134 ? 5.803   3.906   16.323  1.00 49.89  ? 135 ASN A OD1 1 
ATOM   1064 N ND2 . ASN A 1 134 ? 4.135   4.951   15.279  1.00 50.78  ? 135 ASN A ND2 1 
ATOM   1065 N N   . ILE A 1 135 ? 5.071   9.025   18.488  1.00 41.56  ? 136 ILE A N   1 
ATOM   1066 C CA  . ILE A 1 135 ? 4.890   9.953   19.644  1.00 42.72  ? 136 ILE A CA  1 
ATOM   1067 C C   . ILE A 1 135 ? 4.190   11.221  19.160  1.00 44.96  ? 136 ILE A C   1 
ATOM   1068 O O   . ILE A 1 135 ? 3.009   11.458  19.539  1.00 40.02  ? 136 ILE A O   1 
ATOM   1069 C CB  . ILE A 1 135 ? 6.232   10.125  20.392  1.00 41.26  ? 136 ILE A CB  1 
ATOM   1070 C CG1 . ILE A 1 135 ? 6.622   8.799   21.034  1.00 44.90  ? 136 ILE A CG1 1 
ATOM   1071 C CG2 . ILE A 1 135 ? 6.195   11.229  21.421  1.00 36.26  ? 136 ILE A CG2 1 
ATOM   1072 C CD1 . ILE A 1 135 ? 8.104   8.679   21.356  1.00 48.42  ? 136 ILE A CD1 1 
ATOM   1073 N N   . LEU A 1 136 ? 4.812   11.999  18.289  1.00 45.75  ? 137 LEU A N   1 
ATOM   1074 C CA  . LEU A 1 136 ? 4.205   13.288  17.882  1.00 44.55  ? 137 LEU A CA  1 
ATOM   1075 C C   . LEU A 1 136 ? 3.008   13.006  16.975  1.00 46.11  ? 137 LEU A C   1 
ATOM   1076 O O   . LEU A 1 136 ? 2.153   13.901  16.827  1.00 48.91  ? 137 LEU A O   1 
ATOM   1077 C CB  . LEU A 1 136 ? 5.274   14.159  17.228  1.00 46.66  ? 137 LEU A CB  1 
ATOM   1078 C CG  . LEU A 1 136 ? 6.330   14.710  18.178  1.00 46.52  ? 137 LEU A CG  1 
ATOM   1079 C CD1 . LEU A 1 136 ? 7.313   15.598  17.428  1.00 48.60  ? 137 LEU A CD1 1 
ATOM   1080 C CD2 . LEU A 1 136 ? 5.714   15.522  19.326  1.00 48.40  ? 137 LEU A CD2 1 
ATOM   1081 N N   . GLY A 1 137 ? 2.930   11.798  16.438  1.00 42.75  ? 138 GLY A N   1 
ATOM   1082 C CA  . GLY A 1 137 ? 1.813   11.354  15.592  1.00 49.95  ? 138 GLY A CA  1 
ATOM   1083 C C   . GLY A 1 137 ? 0.667   10.790  16.410  1.00 53.91  ? 138 GLY A C   1 
ATOM   1084 O O   . GLY A 1 137 ? -0.328  10.488  15.801  1.00 42.50  ? 138 GLY A O   1 
ATOM   1085 N N   . HIS A 1 138 ? 0.805   10.590  17.732  1.00 45.70  ? 139 HIS A N   1 
ATOM   1086 C CA  . HIS A 1 138 ? -0.326  10.137  18.597  1.00 50.18  ? 139 HIS A CA  1 
ATOM   1087 C C   . HIS A 1 138 ? -0.822  8.766   18.105  1.00 53.64  ? 139 HIS A C   1 
ATOM   1088 O O   . HIS A 1 138 ? -2.019  8.636   17.775  1.00 53.75  ? 139 HIS A O   1 
ATOM   1089 C CB  . HIS A 1 138 ? -1.453  11.212  18.640  1.00 50.11  ? 139 HIS A CB  1 
ATOM   1090 C CG  . HIS A 1 138 ? -1.154  12.490  19.373  1.00 51.89  ? 139 HIS A CG  1 
ATOM   1091 N ND1 . HIS A 1 138 ? -1.377  12.633  20.760  1.00 50.17  ? 139 HIS A ND1 1 
ATOM   1092 C CD2 . HIS A 1 138 ? -0.708  13.706  18.943  1.00 53.07  ? 139 HIS A CD2 1 
ATOM   1093 C CE1 . HIS A 1 138 ? -1.061  13.861  21.131  1.00 45.62  ? 139 HIS A CE1 1 
ATOM   1094 N NE2 . HIS A 1 138 ? -0.666  14.547  20.047  1.00 49.62  ? 139 HIS A NE2 1 
ATOM   1095 N N   . LYS A 1 139 ? 0.058   7.762   18.102  1.00 53.26  ? 140 LYS A N   1 
ATOM   1096 C CA  . LYS A 1 139 ? -0.242  6.407   17.590  1.00 53.56  ? 140 LYS A CA  1 
ATOM   1097 C C   . LYS A 1 139 ? -0.034  5.362   18.701  1.00 49.48  ? 140 LYS A C   1 
ATOM   1098 O O   . LYS A 1 139 ? 0.101   4.162   18.373  1.00 51.40  ? 140 LYS A O   1 
ATOM   1099 C CB  . LYS A 1 139 ? 0.620   6.142   16.340  1.00 58.59  ? 140 LYS A CB  1 
ATOM   1100 C CG  . LYS A 1 139 ? 0.433   7.165   15.228  1.00 65.18  ? 140 LYS A CG  1 
ATOM   1101 C CD  . LYS A 1 139 ? 1.105   6.889   13.887  1.00 66.34  ? 140 LYS A CD  1 
ATOM   1102 C CE  . LYS A 1 139 ? 0.885   8.049   12.929  1.00 70.29  ? 140 LYS A CE  1 
ATOM   1103 N NZ  . LYS A 1 139 ? 1.910   8.112   11.858  1.00 73.03  ? 140 LYS A NZ  1 
ATOM   1104 N N   . LEU A 1 140 ? 0.018   5.765   19.978  1.00 49.40  ? 141 LEU A N   1 
ATOM   1105 C CA  . LEU A 1 140 ? 0.290   4.843   21.117  1.00 43.55  ? 141 LEU A CA  1 
ATOM   1106 C C   . LEU A 1 140 ? -1.024  4.516   21.818  1.00 46.97  ? 141 LEU A C   1 
ATOM   1107 O O   . LEU A 1 140 ? -1.836  5.440   21.967  1.00 49.87  ? 141 LEU A O   1 
ATOM   1108 C CB  . LEU A 1 140 ? 1.265   5.472   22.123  1.00 42.24  ? 141 LEU A CB  1 
ATOM   1109 C CG  . LEU A 1 140 ? 2.663   5.807   21.620  1.00 41.42  ? 141 LEU A CG  1 
ATOM   1110 C CD1 . LEU A 1 140 ? 3.479   6.383   22.783  1.00 39.41  ? 141 LEU A CD1 1 
ATOM   1111 C CD2 . LEU A 1 140 ? 3.368   4.583   20.999  1.00 39.36  ? 141 LEU A CD2 1 
ATOM   1112 N N   . GLU A 1 141 ? -1.192  3.263   22.231  1.00 46.79  ? 142 GLU A N   1 
ATOM   1113 C CA  . GLU A 1 141 ? -2.311  2.770   23.081  1.00 49.39  ? 142 GLU A CA  1 
ATOM   1114 C C   . GLU A 1 141 ? -2.393  3.577   24.381  1.00 61.58  ? 142 GLU A C   1 
ATOM   1115 O O   . GLU A 1 141 ? -1.344  3.835   25.028  1.00 49.35  ? 142 GLU A O   1 
ATOM   1116 C CB  . GLU A 1 141 ? -2.095  1.311   23.443  1.00 52.31  ? 142 GLU A CB  1 
ATOM   1117 C CG  . GLU A 1 141 ? -2.055  0.386   22.235  1.00 55.95  ? 142 GLU A CG  1 
ATOM   1118 C CD  . GLU A 1 141 ? -3.341  0.366   21.415  1.00 56.11  ? 142 GLU A CD  1 
ATOM   1119 O OE1 . GLU A 1 141 ? -4.409  0.689   21.990  1.00 55.19  ? 142 GLU A OE1 1 
ATOM   1120 O OE2 . GLU A 1 141 ? -3.258  0.006   20.225  1.00 57.53  ? 142 GLU A OE2 1 
ATOM   1121 N N   . TYR A 1 142 ? -3.607  3.933   24.776  1.00 66.44  ? 143 TYR A N   1 
ATOM   1122 C CA  . TYR A 1 142 ? -3.929  4.528   26.099  1.00 61.46  ? 143 TYR A CA  1 
ATOM   1123 C C   . TYR A 1 142 ? -4.360  3.365   26.996  1.00 62.66  ? 143 TYR A C   1 
ATOM   1124 O O   . TYR A 1 142 ? -5.554  3.008   27.053  1.00 55.22  ? 143 TYR A O   1 
ATOM   1125 C CB  . TYR A 1 142 ? -4.943  5.660   25.924  1.00 57.58  ? 143 TYR A CB  1 
ATOM   1126 C CG  . TYR A 1 142 ? -5.255  6.385   27.199  1.00 56.64  ? 143 TYR A CG  1 
ATOM   1127 C CD1 . TYR A 1 142 ? -4.429  7.415   27.626  1.00 66.15  ? 143 TYR A CD1 1 
ATOM   1128 C CD2 . TYR A 1 142 ? -6.369  6.056   27.980  1.00 63.85  ? 143 TYR A CD2 1 
ATOM   1129 C CE1 . TYR A 1 142 ? -4.674  8.091   28.814  1.00 62.06  ? 143 TYR A CE1 1 
ATOM   1130 C CE2 . TYR A 1 142 ? -6.646  6.737   29.161  1.00 63.38  ? 143 TYR A CE2 1 
ATOM   1131 C CZ  . TYR A 1 142 ? -5.798  7.766   29.570  1.00 66.18  ? 143 TYR A CZ  1 
ATOM   1132 O OH  . TYR A 1 142 ? -6.038  8.498   30.693  1.00 50.60  ? 143 TYR A OH  1 
ATOM   1133 N N   . ASN A 1 143 ? -3.365  2.692   27.566  1.00 63.73  ? 144 ASN A N   1 
ATOM   1134 C CA  . ASN A 1 143 ? -3.559  1.517   28.448  1.00 69.43  ? 144 ASN A CA  1 
ATOM   1135 C C   . ASN A 1 143 ? -2.401  1.484   29.448  1.00 74.23  ? 144 ASN A C   1 
ATOM   1136 O O   . ASN A 1 143 ? -1.412  2.274   29.283  1.00 62.53  ? 144 ASN A O   1 
ATOM   1137 C CB  . ASN A 1 143 ? -3.640  0.213   27.652  1.00 74.99  ? 144 ASN A CB  1 
ATOM   1138 C CG  . ASN A 1 143 ? -2.343  -0.053  26.925  1.00 65.17  ? 144 ASN A CG  1 
ATOM   1139 O OD1 . ASN A 1 143 ? -1.670  0.874   26.550  1.00 67.14  ? 144 ASN A OD1 1 
ATOM   1140 N ND2 . ASN A 1 143 ? -1.974  -1.297  26.731  1.00 59.73  ? 144 ASN A ND2 1 
ATOM   1141 N N   . ALA A 1 144 ? -2.505  0.572   30.409  1.00 76.28  ? 145 ALA A N   1 
ATOM   1142 C CA  . ALA A 1 144 ? -1.827  0.664   31.717  1.00 79.96  ? 145 ALA A CA  1 
ATOM   1143 C C   . ALA A 1 144 ? -0.340  0.342   31.547  1.00 65.89  ? 145 ALA A C   1 
ATOM   1144 O O   . ALA A 1 144 ? -0.055  -0.643  30.896  1.00 47.56  ? 145 ALA A O   1 
ATOM   1145 C CB  . ALA A 1 144 ? -2.490  -0.275  32.687  1.00 78.21  ? 145 ALA A CB  1 
ATOM   1146 N N   . ILE A 1 145 ? 0.562   1.146   32.121  1.00 67.28  ? 146 ILE A N   1 
ATOM   1147 C CA  . ILE A 1 145 ? 2.006   0.773   32.208  1.00 60.20  ? 146 ILE A CA  1 
ATOM   1148 C C   . ILE A 1 145 ? 2.270   0.273   33.639  1.00 54.25  ? 146 ILE A C   1 
ATOM   1149 O O   . ILE A 1 145 ? 2.125   1.054   34.661  1.00 56.65  ? 146 ILE A O   1 
ATOM   1150 C CB  . ILE A 1 145 ? 2.925   1.897   31.685  1.00 63.31  ? 146 ILE A CB  1 
ATOM   1151 C CG1 . ILE A 1 145 ? 3.112   3.020   32.697  1.00 75.91  ? 146 ILE A CG1 1 
ATOM   1152 C CG2 . ILE A 1 145 ? 2.423   2.431   30.330  1.00 57.85  ? 146 ILE A CG2 1 
ATOM   1153 C CD1 . ILE A 1 145 ? 4.280   3.912   32.377  1.00 96.68  ? 146 ILE A CD1 1 
ATOM   1154 N N   . SER A 1 146 ? 2.515   -1.022  33.698  1.00 43.93  ? 147 SER A N   1 
ATOM   1155 C CA  . SER A 1 146 ? 2.890   -1.786  34.907  1.00 47.29  ? 147 SER A CA  1 
ATOM   1156 C C   . SER A 1 146 ? 4.330   -2.240  34.754  1.00 46.52  ? 147 SER A C   1 
ATOM   1157 O O   . SER A 1 146 ? 4.791   -2.322  33.626  1.00 55.04  ? 147 SER A O   1 
ATOM   1158 C CB  . SER A 1 146 ? 1.927   -2.910  35.109  1.00 48.73  ? 147 SER A CB  1 
ATOM   1159 O OG  . SER A 1 146 ? 0.610   -2.343  35.275  1.00 45.05  ? 147 SER A OG  1 
ATOM   1160 N N   . GLY A 1 147 ? 5.046   -2.493  35.840  1.00 41.66  ? 148 GLY A N   1 
ATOM   1161 C CA  . GLY A 1 147 ? 6.375   -3.138  35.765  1.00 37.14  ? 148 GLY A CA  1 
ATOM   1162 C C   . GLY A 1 147 ? 7.339   -2.666  36.822  1.00 39.32  ? 148 GLY A C   1 
ATOM   1163 O O   . GLY A 1 147 ? 6.921   -2.027  37.794  1.00 37.49  ? 148 GLY A O   1 
ATOM   1164 N N   . ASN A 1 148 ? 8.603   -3.031  36.659  1.00 37.26  ? 149 ASN A N   1 
ATOM   1165 C CA  . ASN A 1 148 ? 9.613   -2.896  37.716  1.00 43.15  ? 149 ASN A CA  1 
ATOM   1166 C C   . ASN A 1 148 ? 10.555  -1.723  37.442  1.00 41.35  ? 149 ASN A C   1 
ATOM   1167 O O   . ASN A 1 148 ? 11.057  -1.576  36.304  1.00 39.21  ? 149 ASN A O   1 
ATOM   1168 C CB  . ASN A 1 148 ? 10.327  -4.245  37.818  1.00 42.51  ? 149 ASN A CB  1 
ATOM   1169 C CG  . ASN A 1 148 ? 9.356   -5.312  38.280  1.00 41.61  ? 149 ASN A CG  1 
ATOM   1170 O OD1 . ASN A 1 148 ? 8.371   -5.014  38.936  1.00 40.58  ? 149 ASN A OD1 1 
ATOM   1171 N ND2 . ASN A 1 148 ? 9.584   -6.543  37.880  1.00 49.32  ? 149 ASN A ND2 1 
ATOM   1172 N N   . ALA A 1 149 ? 10.880  -0.968  38.472  1.00 34.75  ? 150 ALA A N   1 
ATOM   1173 C CA  . ALA A 1 149 ? 11.977  0.013   38.465  1.00 32.16  ? 150 ALA A CA  1 
ATOM   1174 C C   . ALA A 1 149 ? 13.094  -0.524  39.331  1.00 35.65  ? 150 ALA A C   1 
ATOM   1175 O O   . ALA A 1 149 ? 12.851  -0.765  40.537  1.00 37.89  ? 150 ALA A O   1 
ATOM   1176 C CB  . ALA A 1 149 ? 11.478  1.368   38.968  1.00 31.99  ? 150 ALA A CB  1 
ATOM   1177 N N   . ASN A 1 150 ? 14.268  -0.743  38.753  1.00 32.75  ? 151 ASN A N   1 
ATOM   1178 C CA  . ASN A 1 150 ? 15.451  -1.271  39.457  1.00 36.87  ? 151 ASN A CA  1 
ATOM   1179 C C   . ASN A 1 150 ? 16.164  -0.109  40.149  1.00 42.24  ? 151 ASN A C   1 
ATOM   1180 O O   . ASN A 1 150 ? 16.566  0.821   39.446  1.00 39.72  ? 151 ASN A O   1 
ATOM   1181 C CB  . ASN A 1 150 ? 16.419  -1.958  38.476  1.00 41.30  ? 151 ASN A CB  1 
ATOM   1182 C CG  . ASN A 1 150 ? 15.737  -3.101  37.777  1.00 42.89  ? 151 ASN A CG  1 
ATOM   1183 O OD1 . ASN A 1 150 ? 15.377  -3.044  36.589  1.00 42.59  ? 151 ASN A OD1 1 
ATOM   1184 N ND2 . ASN A 1 150 ? 15.483  -4.113  38.553  1.00 35.79  ? 151 ASN A ND2 1 
ATOM   1185 N N   . ILE A 1 151 ? 16.360  -0.197  41.468  1.00 34.02  ? 152 ILE A N   1 
ATOM   1186 C CA  . ILE A 1 151 ? 16.999  0.836   42.324  1.00 33.83  ? 152 ILE A CA  1 
ATOM   1187 C C   . ILE A 1 151 ? 18.366  0.340   42.789  1.00 37.29  ? 152 ILE A C   1 
ATOM   1188 O O   . ILE A 1 151 ? 18.409  -0.762  43.337  1.00 41.35  ? 152 ILE A O   1 
ATOM   1189 C CB  . ILE A 1 151 ? 16.131  1.106   43.569  1.00 34.14  ? 152 ILE A CB  1 
ATOM   1190 C CG1 . ILE A 1 151 ? 14.645  1.378   43.264  1.00 40.24  ? 152 ILE A CG1 1 
ATOM   1191 C CG2 . ILE A 1 151 ? 16.791  2.173   44.418  1.00 35.37  ? 152 ILE A CG2 1 
ATOM   1192 C CD1 . ILE A 1 151 ? 14.358  2.319   42.145  1.00 44.57  ? 152 ILE A CD1 1 
ATOM   1193 N N   . THR A 1 152 ? 19.399  1.187   42.764  1.00 39.76  ? 153 THR A N   1 
ATOM   1194 C CA  . THR A 1 152 ? 20.725  0.904   43.394  1.00 38.73  ? 153 THR A CA  1 
ATOM   1195 C C   . THR A 1 152 ? 21.275  2.145   44.079  1.00 36.62  ? 153 THR A C   1 
ATOM   1196 O O   . THR A 1 152 ? 20.891  3.276   43.696  1.00 39.04  ? 153 THR A O   1 
ATOM   1197 C CB  . THR A 1 152 ? 21.778  0.448   42.372  1.00 45.92  ? 153 THR A CB  1 
ATOM   1198 O OG1 . THR A 1 152 ? 21.915  1.555   41.464  1.00 43.99  ? 153 THR A OG1 1 
ATOM   1199 C CG2 . THR A 1 152 ? 21.328  -0.783  41.631  1.00 52.82  ? 153 THR A CG2 1 
ATOM   1200 N N   . ALA A 1 153 ? 22.132  1.944   45.077  1.00 40.85  ? 154 ALA A N   1 
ATOM   1201 C CA  . ALA A 1 153 ? 22.739  3.044   45.855  1.00 42.12  ? 154 ALA A CA  1 
ATOM   1202 C C   . ALA A 1 153 ? 23.655  3.825   44.896  1.00 45.95  ? 154 ALA A C   1 
ATOM   1203 O O   . ALA A 1 153 ? 24.236  3.223   43.984  1.00 42.43  ? 154 ALA A O   1 
ATOM   1204 C CB  . ALA A 1 153 ? 23.478  2.512   47.062  1.00 44.98  ? 154 ALA A CB  1 
ATOM   1205 N N   . ASP A 1 154 ? 23.724  5.129   45.062  1.00 42.54  ? 155 ASP A N   1 
ATOM   1206 C CA  . ASP A 1 154 ? 24.766  5.995   44.453  1.00 44.04  ? 155 ASP A CA  1 
ATOM   1207 C C   . ASP A 1 154 ? 25.514  6.659   45.593  1.00 50.85  ? 155 ASP A C   1 
ATOM   1208 O O   . ASP A 1 154 ? 25.205  7.867   45.920  1.00 52.14  ? 155 ASP A O   1 
ATOM   1209 C CB  . ASP A 1 154 ? 24.142  7.007   43.505  1.00 49.78  ? 155 ASP A CB  1 
ATOM   1210 C CG  . ASP A 1 154 ? 25.149  7.753   42.660  1.00 48.12  ? 155 ASP A CG  1 
ATOM   1211 O OD1 . ASP A 1 154 ? 26.368  7.527   42.834  1.00 51.79  ? 155 ASP A OD1 1 
ATOM   1212 O OD2 . ASP A 1 154 ? 24.699  8.523   41.823  1.00 56.61  ? 155 ASP A OD2 1 
ATOM   1213 N N   . LYS A 1 155 ? 26.364  5.873   46.262  1.00 49.25  ? 156 LYS A N   1 
ATOM   1214 C CA  . LYS A 1 155 ? 26.998  6.335   47.520  1.00 59.83  ? 156 LYS A CA  1 
ATOM   1215 C C   . LYS A 1 155 ? 27.803  7.603   47.217  1.00 48.97  ? 156 LYS A C   1 
ATOM   1216 O O   . LYS A 1 155 ? 27.851  8.484   48.080  1.00 52.99  ? 156 LYS A O   1 
ATOM   1217 C CB  . LYS A 1 155 ? 27.829  5.227   48.175  1.00 75.72  ? 156 LYS A CB  1 
ATOM   1218 C CG  . LYS A 1 155 ? 28.122  5.492   49.645  1.00 82.31  ? 156 LYS A CG  1 
ATOM   1219 C CD  . LYS A 1 155 ? 29.427  4.906   50.151  1.00 89.46  ? 156 LYS A CD  1 
ATOM   1220 C CE  . LYS A 1 155 ? 30.149  5.860   51.084  1.00 95.56  ? 156 LYS A CE  1 
ATOM   1221 N NZ  . LYS A 1 155 ? 30.524  5.209   52.357  1.00 103.08 ? 156 LYS A NZ  1 
ATOM   1222 N N   . GLN A 1 156 ? 28.319  7.756   46.003  1.00 52.55  ? 157 GLN A N   1 
ATOM   1223 C CA  . GLN A 1 156 ? 29.079  8.976   45.610  1.00 66.33  ? 157 GLN A CA  1 
ATOM   1224 C C   . GLN A 1 156 ? 28.214  10.235  45.792  1.00 68.25  ? 157 GLN A C   1 
ATOM   1225 O O   . GLN A 1 156 ? 28.738  11.240  46.299  1.00 74.88  ? 157 GLN A O   1 
ATOM   1226 C CB  . GLN A 1 156 ? 29.563  8.837   44.169  1.00 79.08  ? 157 GLN A CB  1 
ATOM   1227 C CG  . GLN A 1 156 ? 30.355  10.036  43.684  1.00 86.98  ? 157 GLN A CG  1 
ATOM   1228 C CD  . GLN A 1 156 ? 31.092  9.698   42.414  1.00 98.20  ? 157 GLN A CD  1 
ATOM   1229 O OE1 . GLN A 1 156 ? 31.428  8.542   42.165  1.00 104.82 ? 157 GLN A OE1 1 
ATOM   1230 N NE2 . GLN A 1 156 ? 31.346  10.711  41.602  1.00 98.46  ? 157 GLN A NE2 1 
ATOM   1231 N N   . LYS A 1 157 ? 26.958  10.208  45.343  1.00 55.36  ? 158 LYS A N   1 
ATOM   1232 C CA  . LYS A 1 157 ? 26.055  11.383  45.309  1.00 60.29  ? 158 LYS A CA  1 
ATOM   1233 C C   . LYS A 1 157 ? 25.169  11.340  46.555  1.00 62.41  ? 158 LYS A C   1 
ATOM   1234 O O   . LYS A 1 157 ? 24.309  12.266  46.728  1.00 53.95  ? 158 LYS A O   1 
ATOM   1235 C CB  . LYS A 1 157 ? 25.190  11.379  44.040  1.00 63.84  ? 158 LYS A CB  1 
ATOM   1236 C CG  . LYS A 1 157 ? 25.936  11.427  42.707  1.00 71.44  ? 158 LYS A CG  1 
ATOM   1237 C CD  . LYS A 1 157 ? 26.503  12.785  42.327  1.00 91.10  ? 158 LYS A CD  1 
ATOM   1238 C CE  . LYS A 1 157 ? 27.024  12.854  40.899  1.00 98.17  ? 158 LYS A CE  1 
ATOM   1239 N NZ  . LYS A 1 157 ? 28.162  11.930  40.671  1.00 106.21 ? 158 LYS A NZ  1 
ATOM   1240 N N   . ASN A 1 158 ? 25.314  10.281  47.360  1.00 55.60  ? 159 ASN A N   1 
ATOM   1241 C CA  . ASN A 1 158 ? 24.483  10.093  48.569  1.00 51.92  ? 159 ASN A CA  1 
ATOM   1242 C C   . ASN A 1 158 ? 23.006  9.987   48.130  1.00 53.01  ? 159 ASN A C   1 
ATOM   1243 O O   . ASN A 1 158 ? 22.137  10.519  48.801  1.00 45.91  ? 159 ASN A O   1 
ATOM   1244 C CB  . ASN A 1 158 ? 24.721  11.280  49.499  1.00 58.50  ? 159 ASN A CB  1 
ATOM   1245 C CG  . ASN A 1 158 ? 24.167  11.078  50.881  1.00 50.34  ? 159 ASN A CG  1 
ATOM   1246 O OD1 . ASN A 1 158 ? 24.323  10.010  51.441  1.00 55.02  ? 159 ASN A OD1 1 
ATOM   1247 N ND2 . ASN A 1 158 ? 23.542  12.105  51.432  1.00 53.07  ? 159 ASN A ND2 1 
ATOM   1248 N N   . GLY A 1 159 ? 22.734  9.307   47.030  1.00 48.50  ? 160 GLY A N   1 
ATOM   1249 C CA  . GLY A 1 159 ? 21.351  9.047   46.615  1.00 46.04  ? 160 GLY A CA  1 
ATOM   1250 C C   . GLY A 1 159 ? 21.234  7.703   45.938  1.00 45.39  ? 160 GLY A C   1 
ATOM   1251 O O   . GLY A 1 159 ? 21.860  6.743   46.398  1.00 42.01  ? 160 GLY A O   1 
ATOM   1252 N N   . ILE A 1 160 ? 20.467  7.643   44.864  1.00 40.28  ? 161 ILE A N   1 
ATOM   1253 C CA  . ILE A 1 160 ? 20.150  6.373   44.174  1.00 38.48  ? 161 ILE A CA  1 
ATOM   1254 C C   . ILE A 1 160 ? 20.254  6.613   42.661  1.00 39.98  ? 161 ILE A C   1 
ATOM   1255 O O   . ILE A 1 160 ? 20.155  7.763   42.225  1.00 38.64  ? 161 ILE A O   1 
ATOM   1256 C CB  . ILE A 1 160 ? 18.803  5.778   44.632  1.00 34.30  ? 161 ILE A CB  1 
ATOM   1257 C CG1 . ILE A 1 160 ? 17.595  6.698   44.420  1.00 33.22  ? 161 ILE A CG1 1 
ATOM   1258 C CG2 . ILE A 1 160 ? 18.832  5.368   46.112  1.00 34.23  ? 161 ILE A CG2 1 
ATOM   1259 C CD1 . ILE A 1 160 ? 16.839  6.498   43.129  1.00 42.73  ? 161 ILE A CD1 1 
ATOM   1260 N N   . LYS A 1 161 ? 20.413  5.531   41.915  1.00 38.16  ? 162 LYS A N   1 
ATOM   1261 C CA  . LYS A 1 161 ? 20.191  5.486   40.455  1.00 44.27  ? 162 LYS A CA  1 
ATOM   1262 C C   . LYS A 1 161 ? 19.081  4.473   40.286  1.00 41.66  ? 162 LYS A C   1 
ATOM   1263 O O   . LYS A 1 161 ? 18.929  3.637   41.178  1.00 38.52  ? 162 LYS A O   1 
ATOM   1264 C CB  . LYS A 1 161 ? 21.488  5.108   39.723  1.00 45.23  ? 162 LYS A CB  1 
ATOM   1265 C CG  . LYS A 1 161 ? 22.609  6.123   39.955  1.00 58.90  ? 162 LYS A CG  1 
ATOM   1266 C CD  . LYS A 1 161 ? 23.897  5.983   39.135  1.00 72.63  ? 162 LYS A CD  1 
ATOM   1267 C CE  . LYS A 1 161 ? 23.670  6.072   37.641  1.00 88.05  ? 162 LYS A CE  1 
ATOM   1268 N NZ  . LYS A 1 161 ? 23.507  4.724   37.041  1.00 104.81 ? 162 LYS A NZ  1 
ATOM   1269 N N   . ALA A 1 162 ? 18.357  4.540   39.189  1.00 32.94  ? 163 ALA A N   1 
ATOM   1270 C CA  . ALA A 1 162 ? 17.351  3.548   38.822  1.00 33.43  ? 163 ALA A CA  1 
ATOM   1271 C C   . ALA A 1 162 ? 17.471  3.304   37.338  1.00 33.85  ? 163 ALA A C   1 
ATOM   1272 O O   . ALA A 1 162 ? 18.000  4.165   36.642  1.00 35.15  ? 163 ALA A O   1 
ATOM   1273 C CB  . ALA A 1 162 ? 15.963  4.044   39.176  1.00 33.79  ? 163 ALA A CB  1 
ATOM   1274 N N   . TYR A 1 163 ? 16.934  2.192   36.867  1.00 34.94  ? 164 TYR A N   1 
ATOM   1275 C CA  . TYR A 1 163 ? 16.909  1.922   35.412  1.00 40.02  ? 164 TYR A CA  1 
ATOM   1276 C C   . TYR A 1 163 ? 15.820  0.909   35.177  1.00 35.64  ? 164 TYR A C   1 
ATOM   1277 O O   . TYR A 1 163 ? 15.518  0.055   36.059  1.00 41.32  ? 164 TYR A O   1 
ATOM   1278 C CB  . TYR A 1 163 ? 18.277  1.443   34.910  1.00 37.09  ? 164 TYR A CB  1 
ATOM   1279 C CG  . TYR A 1 163 ? 18.708  0.154   35.547  1.00 40.34  ? 164 TYR A CG  1 
ATOM   1280 C CD1 . TYR A 1 163 ? 18.190  -1.051  35.106  1.00 41.54  ? 164 TYR A CD1 1 
ATOM   1281 C CD2 . TYR A 1 163 ? 19.603  0.149   36.601  1.00 45.45  ? 164 TYR A CD2 1 
ATOM   1282 C CE1 . TYR A 1 163 ? 18.513  -2.232  35.744  1.00 45.76  ? 164 TYR A CE1 1 
ATOM   1283 C CE2 . TYR A 1 163 ? 19.960  -1.029  37.231  1.00 44.73  ? 164 TYR A CE2 1 
ATOM   1284 C CZ  . TYR A 1 163 ? 19.402  -2.214  36.804  1.00 46.84  ? 164 TYR A CZ  1 
ATOM   1285 O OH  . TYR A 1 163 ? 19.804  -3.369  37.394  1.00 50.29  ? 164 TYR A OH  1 
ATOM   1286 N N   . PHE A 1 164 ? 15.187  1.047   34.037  1.00 33.50  ? 165 PHE A N   1 
ATOM   1287 C CA  . PHE A 1 164 ? 14.094  0.165   33.571  1.00 33.92  ? 165 PHE A CA  1 
ATOM   1288 C C   . PHE A 1 164 ? 13.794  0.543   32.139  1.00 35.19  ? 165 PHE A C   1 
ATOM   1289 O O   . PHE A 1 164 ? 14.220  1.660   31.721  1.00 35.32  ? 165 PHE A O   1 
ATOM   1290 C CB  . PHE A 1 164 ? 12.828  0.302   34.456  1.00 39.52  ? 165 PHE A CB  1 
ATOM   1291 C CG  . PHE A 1 164 ? 12.341  1.695   34.758  1.00 32.73  ? 165 PHE A CG  1 
ATOM   1292 C CD1 . PHE A 1 164 ? 12.898  2.447   35.741  1.00 33.67  ? 165 PHE A CD1 1 
ATOM   1293 C CD2 . PHE A 1 164 ? 11.252  2.203   34.093  1.00 36.13  ? 165 PHE A CD2 1 
ATOM   1294 C CE1 . PHE A 1 164 ? 12.399  3.706   36.058  1.00 34.20  ? 165 PHE A CE1 1 
ATOM   1295 C CE2 . PHE A 1 164 ? 10.794  3.493   34.340  1.00 34.73  ? 165 PHE A CE2 1 
ATOM   1296 C CZ  . PHE A 1 164 ? 11.363  4.236   35.333  1.00 34.58  ? 165 PHE A CZ  1 
ATOM   1297 N N   . THR A 1 165 ? 13.076  -0.329  31.464  1.00 34.54  ? 166 THR A N   1 
ATOM   1298 C CA  . THR A 1 165 ? 12.574  -0.188  30.092  1.00 36.97  ? 166 THR A CA  1 
ATOM   1299 C C   . THR A 1 165 ? 11.048  -0.259  30.202  1.00 35.71  ? 166 THR A C   1 
ATOM   1300 O O   . THR A 1 165 ? 10.517  -1.275  30.721  1.00 37.35  ? 166 THR A O   1 
ATOM   1301 C CB  . THR A 1 165 ? 13.247  -1.221  29.169  1.00 33.44  ? 166 THR A CB  1 
ATOM   1302 O OG1 . THR A 1 165 ? 14.677  -1.037  29.129  1.00 35.18  ? 166 THR A OG1 1 
ATOM   1303 C CG2 . THR A 1 165 ? 12.689  -1.173  27.780  1.00 37.38  ? 166 THR A CG2 1 
ATOM   1304 N N   . ILE A 1 166 ? 10.364  0.771   29.723  1.00 34.43  ? 167 ILE A N   1 
ATOM   1305 C CA  . ILE A 1 166 ? 8.899   0.742   29.475  1.00 35.47  ? 167 ILE A CA  1 
ATOM   1306 C C   . ILE A 1 166 ? 8.577   0.276   28.068  1.00 42.55  ? 167 ILE A C   1 
ATOM   1307 O O   . ILE A 1 166 ? 9.225   0.732   27.089  1.00 38.27  ? 167 ILE A O   1 
ATOM   1308 C CB  . ILE A 1 166 ? 8.274   2.102   29.766  1.00 35.10  ? 167 ILE A CB  1 
ATOM   1309 C CG1 . ILE A 1 166 ? 8.491   2.499   31.227  1.00 36.72  ? 167 ILE A CG1 1 
ATOM   1310 C CG2 . ILE A 1 166 ? 6.809   2.072   29.364  1.00 37.30  ? 167 ILE A CG2 1 
ATOM   1311 C CD1 . ILE A 1 166 ? 7.973   1.555   32.279  1.00 38.54  ? 167 ILE A CD1 1 
ATOM   1312 N N   . ARG A 1 167 ? 7.540   -0.552  27.975  1.00 36.89  ? 168 ARG A N   1 
ATOM   1313 C CA  . ARG A 1 167 ? 7.091   -1.173  26.713  1.00 46.22  ? 168 ARG A CA  1 
ATOM   1314 C C   . ARG A 1 167 ? 5.746   -0.547  26.361  1.00 41.99  ? 168 ARG A C   1 
ATOM   1315 O O   . ARG A 1 167 ? 4.769   -0.988  26.886  1.00 45.97  ? 168 ARG A O   1 
ATOM   1316 C CB  . ARG A 1 167 ? 7.006   -2.709  26.850  1.00 49.04  ? 168 ARG A CB  1 
ATOM   1317 C CG  . ARG A 1 167 ? 8.338   -3.396  27.144  1.00 59.70  ? 168 ARG A CG  1 
ATOM   1318 C CD  . ARG A 1 167 ? 8.258   -4.918  27.274  1.00 62.47  ? 168 ARG A CD  1 
ATOM   1319 N NE  . ARG A 1 167 ? 7.651   -5.562  26.100  1.00 75.60  ? 168 ARG A NE  1 
ATOM   1320 C CZ  . ARG A 1 167 ? 8.321   -6.016  25.038  1.00 77.62  ? 168 ARG A CZ  1 
ATOM   1321 N NH1 . ARG A 1 167 ? 9.642   -5.893  24.974  1.00 69.95  ? 168 ARG A NH1 1 
ATOM   1322 N NH2 . ARG A 1 167 ? 7.656   -6.565  24.028  1.00 74.11  ? 168 ARG A NH2 1 
ATOM   1323 N N   . HIS A 1 168 ? 5.715   0.482   25.525  1.00 37.68  ? 169 HIS A N   1 
ATOM   1324 C CA  . HIS A 1 168 ? 4.473   1.153   25.069  1.00 44.34  ? 169 HIS A CA  1 
ATOM   1325 C C   . HIS A 1 168 ? 3.925   0.413   23.840  1.00 49.84  ? 169 HIS A C   1 
ATOM   1326 O O   . HIS A 1 168 ? 4.602   0.367   22.758  1.00 41.72  ? 169 HIS A O   1 
ATOM   1327 C CB  . HIS A 1 168 ? 4.673   2.642   24.726  1.00 41.85  ? 169 HIS A CB  1 
ATOM   1328 C CG  . HIS A 1 168 ? 5.172   3.525   25.828  1.00 46.31  ? 169 HIS A CG  1 
ATOM   1329 N ND1 . HIS A 1 168 ? 4.383   3.913   26.905  1.00 39.61  ? 169 HIS A ND1 1 
ATOM   1330 C CD2 . HIS A 1 168 ? 6.352   4.185   25.965  1.00 40.75  ? 169 HIS A CD2 1 
ATOM   1331 C CE1 . HIS A 1 168 ? 5.090   4.720   27.686  1.00 44.49  ? 169 HIS A CE1 1 
ATOM   1332 N NE2 . HIS A 1 168 ? 6.308   4.900   27.146  1.00 42.28  ? 169 HIS A NE2 1 
ATOM   1333 N N   . ASP A 1 169 ? 2.679   -0.039  23.913  1.00 51.90  ? 170 ASP A N   1 
ATOM   1334 C CA  . ASP A 1 169 ? 1.973   -0.573  22.716  1.00 48.50  ? 170 ASP A CA  1 
ATOM   1335 C C   . ASP A 1 169 ? 1.628   0.542   21.759  1.00 47.34  ? 170 ASP A C   1 
ATOM   1336 O O   . ASP A 1 169 ? 1.151   1.619   22.189  1.00 47.83  ? 170 ASP A O   1 
ATOM   1337 C CB  . ASP A 1 169 ? 0.706   -1.355  23.077  1.00 58.92  ? 170 ASP A CB  1 
ATOM   1338 C CG  . ASP A 1 169 ? 1.076   -2.584  23.878  1.00 67.32  ? 170 ASP A CG  1 
ATOM   1339 O OD1 . ASP A 1 169 ? 2.112   -3.213  23.538  1.00 59.93  ? 170 ASP A OD1 1 
ATOM   1340 O OD2 . ASP A 1 169 ? 0.412   -2.825  24.898  1.00 75.44  ? 170 ASP A OD2 1 
ATOM   1341 N N   . VAL A 1 170 ? 1.873   0.246   20.486  1.00 47.05  ? 171 VAL A N   1 
ATOM   1342 C CA  . VAL A 1 170 ? 1.580   1.110   19.324  1.00 47.53  ? 171 VAL A CA  1 
ATOM   1343 C C   . VAL A 1 170 ? 0.328   0.513   18.725  1.00 48.67  ? 171 VAL A C   1 
ATOM   1344 O O   . VAL A 1 170 ? 0.107   -0.713  18.953  1.00 50.56  ? 171 VAL A O   1 
ATOM   1345 C CB  . VAL A 1 170 ? 2.743   1.122   18.318  1.00 47.34  ? 171 VAL A CB  1 
ATOM   1346 C CG1 . VAL A 1 170 ? 2.490   2.040   17.139  1.00 48.81  ? 171 VAL A CG1 1 
ATOM   1347 C CG2 . VAL A 1 170 ? 4.060   1.466   19.002  1.00 52.24  ? 171 VAL A CG2 1 
ATOM   1348 N N   . GLU A 1 171 ? -0.435  1.363   18.050  1.00 54.10  ? 172 GLU A N   1 
ATOM   1349 C CA  . GLU A 1 171 ? -1.756  1.032   17.489  1.00 67.58  ? 172 GLU A CA  1 
ATOM   1350 C C   . GLU A 1 171 ? -1.592  0.194   16.216  1.00 70.13  ? 172 GLU A C   1 
ATOM   1351 O O   . GLU A 1 171 ? -2.616  -0.077  15.608  1.00 71.43  ? 172 GLU A O   1 
ATOM   1352 C CB  . GLU A 1 171 ? -2.543  2.313   17.233  1.00 67.79  ? 172 GLU A CB  1 
ATOM   1353 C CG  . GLU A 1 171 ? -2.332  2.866   15.841  1.00 80.85  ? 172 GLU A CG  1 
ATOM   1354 C CD  . GLU A 1 171 ? -2.816  4.289   15.693  1.00 87.72  ? 172 GLU A CD  1 
ATOM   1355 O OE1 . GLU A 1 171 ? -3.441  4.802   16.679  1.00 84.89  ? 172 GLU A OE1 1 
ATOM   1356 O OE2 . GLU A 1 171 ? -2.541  4.877   14.613  1.00 84.75  ? 172 GLU A OE2 1 
ATOM   1357 N N   . ASP A 1 172 ? -0.377  -0.180  15.794  1.00 68.61  ? 173 ASP A N   1 
ATOM   1358 C CA  . ASP A 1 172 ? -0.214  -1.132  14.656  1.00 60.20  ? 173 ASP A CA  1 
ATOM   1359 C C   . ASP A 1 172 ? 0.184   -2.515  15.192  1.00 52.59  ? 173 ASP A C   1 
ATOM   1360 O O   . ASP A 1 172 ? 0.474   -3.368  14.382  1.00 62.26  ? 173 ASP A O   1 
ATOM   1361 C CB  . ASP A 1 172 ? 0.731   -0.604  13.563  1.00 60.17  ? 173 ASP A CB  1 
ATOM   1362 C CG  . ASP A 1 172 ? 2.142   -0.262  14.009  1.00 55.00  ? 173 ASP A CG  1 
ATOM   1363 O OD1 . ASP A 1 172 ? 2.533   -0.705  15.074  1.00 47.94  ? 173 ASP A OD1 1 
ATOM   1364 O OD2 . ASP A 1 172 ? 2.830   0.462   13.265  1.00 56.09  ? 173 ASP A OD2 1 
ATOM   1365 N N   . GLY A 1 173 ? 0.196   -2.748  16.503  1.00 55.03  ? 174 GLY A N   1 
ATOM   1366 C CA  . GLY A 1 173 ? 0.633   -4.037  17.091  1.00 55.85  ? 174 GLY A CA  1 
ATOM   1367 C C   . GLY A 1 173 ? 2.113   -4.086  17.431  1.00 53.65  ? 174 GLY A C   1 
ATOM   1368 O O   . GLY A 1 173 ? 2.519   -5.055  18.119  1.00 53.30  ? 174 GLY A O   1 
ATOM   1369 N N   . SER A 1 174 ? 2.899   -3.067  17.051  1.00 53.30  ? 175 SER A N   1 
ATOM   1370 C CA  . SER A 1 174 ? 4.347   -3.026  17.408  1.00 50.59  ? 175 SER A CA  1 
ATOM   1371 C C   . SER A 1 174 ? 4.494   -2.470  18.822  1.00 53.48  ? 175 SER A C   1 
ATOM   1372 O O   . SER A 1 174 ? 3.479   -2.110  19.414  1.00 51.04  ? 175 SER A O   1 
ATOM   1373 C CB  . SER A 1 174 ? 5.174   -2.275  16.414  1.00 50.98  ? 175 SER A CB  1 
ATOM   1374 O OG  . SER A 1 174 ? 4.688   -0.962  16.218  1.00 47.97  ? 175 SER A OG  1 
ATOM   1375 N N   . VAL A 1 175 ? 5.712   -2.453  19.361  1.00 45.61  ? 176 VAL A N   1 
ATOM   1376 C CA  . VAL A 1 175 ? 6.015   -1.995  20.742  1.00 50.38  ? 176 VAL A CA  1 
ATOM   1377 C C   . VAL A 1 175 ? 7.104   -0.907  20.646  1.00 53.10  ? 176 VAL A C   1 
ATOM   1378 O O   . VAL A 1 175 ? 8.033   -1.105  19.863  1.00 45.16  ? 176 VAL A O   1 
ATOM   1379 C CB  . VAL A 1 175 ? 6.403   -3.222  21.583  1.00 56.30  ? 176 VAL A CB  1 
ATOM   1380 C CG1 . VAL A 1 175 ? 6.855   -2.847  22.969  1.00 55.10  ? 176 VAL A CG1 1 
ATOM   1381 C CG2 . VAL A 1 175 ? 5.267   -4.243  21.654  1.00 60.38  ? 176 VAL A CG2 1 
ATOM   1382 N N   . LEU A 1 176 ? 6.922   0.241   21.310  1.00 48.02  ? 177 LEU A N   1 
ATOM   1383 C CA  . LEU A 1 176 ? 7.888   1.371   21.432  1.00 38.63  ? 177 LEU A CA  1 
ATOM   1384 C C   . LEU A 1 176 ? 8.601   1.215   22.784  1.00 45.65  ? 177 LEU A C   1 
ATOM   1385 O O   . LEU A 1 176 ? 7.943   1.309   23.860  1.00 43.95  ? 177 LEU A O   1 
ATOM   1386 C CB  . LEU A 1 176 ? 7.129   2.696   21.298  1.00 40.97  ? 177 LEU A CB  1 
ATOM   1387 C CG  . LEU A 1 176 ? 7.921   3.955   21.616  1.00 44.63  ? 177 LEU A CG  1 
ATOM   1388 C CD1 . LEU A 1 176 ? 9.152   4.072   20.740  1.00 42.96  ? 177 LEU A CD1 1 
ATOM   1389 C CD2 . LEU A 1 176 ? 7.066   5.173   21.407  1.00 49.57  ? 177 LEU A CD2 1 
ATOM   1390 N N   . LEU A 1 177 ? 9.877   0.854   22.755  1.00 38.69  ? 178 LEU A N   1 
ATOM   1391 C CA  . LEU A 1 177 ? 10.726  0.679   23.958  1.00 38.58  ? 178 LEU A CA  1 
ATOM   1392 C C   . LEU A 1 177 ? 11.227  2.051   24.400  1.00 38.28  ? 178 LEU A C   1 
ATOM   1393 O O   . LEU A 1 177 ? 11.620  2.850   23.551  1.00 35.68  ? 178 LEU A O   1 
ATOM   1394 C CB  . LEU A 1 177 ? 11.871  -0.288  23.667  1.00 39.50  ? 178 LEU A CB  1 
ATOM   1395 C CG  . LEU A 1 177 ? 11.436  -1.668  23.169  1.00 44.50  ? 178 LEU A CG  1 
ATOM   1396 C CD1 . LEU A 1 177 ? 12.631  -2.532  22.829  1.00 48.22  ? 178 LEU A CD1 1 
ATOM   1397 C CD2 . LEU A 1 177 ? 10.540  -2.379  24.165  1.00 46.90  ? 178 LEU A CD2 1 
ATOM   1398 N N   . ALA A 1 178 ? 11.097  2.357   25.680  1.00 39.35  ? 179 ALA A N   1 
ATOM   1399 C CA  . ALA A 1 178 ? 11.617  3.580   26.319  1.00 33.51  ? 179 ALA A CA  1 
ATOM   1400 C C   . ALA A 1 178 ? 12.532  3.208   27.466  1.00 38.40  ? 179 ALA A C   1 
ATOM   1401 O O   . ALA A 1 178 ? 12.026  2.762   28.567  1.00 35.35  ? 179 ALA A O   1 
ATOM   1402 C CB  . ALA A 1 178 ? 10.453  4.437   26.802  1.00 40.56  ? 179 ALA A CB  1 
ATOM   1403 N N   . ASP A 1 179 ? 13.840  3.356   27.238  1.00 34.88  ? 180 ASP A N   1 
ATOM   1404 C CA  . ASP A 1 179 ? 14.880  3.058   28.241  1.00 36.25  ? 180 ASP A CA  1 
ATOM   1405 C C   . ASP A 1 179 ? 15.076  4.268   29.142  1.00 35.32  ? 180 ASP A C   1 
ATOM   1406 O O   . ASP A 1 179 ? 15.420  5.388   28.658  1.00 32.05  ? 180 ASP A O   1 
ATOM   1407 C CB  . ASP A 1 179 ? 16.177  2.598   27.553  1.00 32.95  ? 180 ASP A CB  1 
ATOM   1408 C CG  . ASP A 1 179 ? 15.967  1.395   26.659  1.00 40.73  ? 180 ASP A CG  1 
ATOM   1409 O OD1 . ASP A 1 179 ? 15.411  0.340   27.166  1.00 34.46  ? 180 ASP A OD1 1 
ATOM   1410 O OD2 . ASP A 1 179 ? 16.374  1.488   25.457  1.00 35.22  ? 180 ASP A OD2 1 
ATOM   1411 N N   . HIS A 1 180 ? 14.898  4.040   30.441  1.00 33.40  ? 181 HIS A N   1 
ATOM   1412 C CA  . HIS A 1 180 ? 14.898  5.081   31.494  1.00 33.54  ? 181 HIS A CA  1 
ATOM   1413 C C   . HIS A 1 180 ? 16.201  4.971   32.275  1.00 32.97  ? 181 HIS A C   1 
ATOM   1414 O O   . HIS A 1 180 ? 16.578  3.841   32.728  1.00 39.92  ? 181 HIS A O   1 
ATOM   1415 C CB  . HIS A 1 180 ? 13.656  4.874   32.398  1.00 33.82  ? 181 HIS A CB  1 
ATOM   1416 C CG  . HIS A 1 180 ? 12.320  5.253   31.846  1.00 29.47  ? 181 HIS A CG  1 
ATOM   1417 N ND1 . HIS A 1 180 ? 11.697  4.660   30.781  1.00 33.11  ? 181 HIS A ND1 1 
ATOM   1418 C CD2 . HIS A 1 180 ? 11.442  6.185   32.321  1.00 32.44  ? 181 HIS A CD2 1 
ATOM   1419 C CE1 . HIS A 1 180 ? 10.505  5.218   30.577  1.00 31.94  ? 181 HIS A CE1 1 
ATOM   1420 N NE2 . HIS A 1 180 ? 10.321  6.147   31.541  1.00 31.45  ? 181 HIS A NE2 1 
ATOM   1421 N N   . TYR A 1 181 ? 16.856  6.106   32.493  1.00 31.70  ? 182 TYR A N   1 
ATOM   1422 C CA  . TYR A 1 181 ? 18.086  6.256   33.302  1.00 36.69  ? 182 TYR A CA  1 
ATOM   1423 C C   . TYR A 1 181 ? 17.779  7.336   34.338  1.00 38.05  ? 182 TYR A C   1 
ATOM   1424 O O   . TYR A 1 181 ? 17.439  8.449   33.952  1.00 34.20  ? 182 TYR A O   1 
ATOM   1425 C CB  . TYR A 1 181 ? 19.305  6.603   32.435  1.00 35.54  ? 182 TYR A CB  1 
ATOM   1426 C CG  . TYR A 1 181 ? 19.532  5.576   31.368  1.00 33.45  ? 182 TYR A CG  1 
ATOM   1427 C CD1 . TYR A 1 181 ? 18.780  5.602   30.208  1.00 36.05  ? 182 TYR A CD1 1 
ATOM   1428 C CD2 . TYR A 1 181 ? 20.469  4.561   31.522  1.00 35.33  ? 182 TYR A CD2 1 
ATOM   1429 C CE1 . TYR A 1 181 ? 18.979  4.678   29.204  1.00 33.56  ? 182 TYR A CE1 1 
ATOM   1430 C CE2 . TYR A 1 181 ? 20.642  3.594   30.535  1.00 38.57  ? 182 TYR A CE2 1 
ATOM   1431 C CZ  . TYR A 1 181 ? 19.871  3.633   29.385  1.00 41.11  ? 182 TYR A CZ  1 
ATOM   1432 O OH  . TYR A 1 181 ? 19.985  2.672   28.417  1.00 40.61  ? 182 TYR A OH  1 
ATOM   1433 N N   . GLN A 1 182 ? 17.958  7.024   35.609  1.00 34.22  ? 183 GLN A N   1 
ATOM   1434 C CA  . GLN A 1 182 ? 17.390  7.850   36.695  1.00 31.97  ? 183 GLN A CA  1 
ATOM   1435 C C   . GLN A 1 182 ? 18.475  8.045   37.738  1.00 31.21  ? 183 GLN A C   1 
ATOM   1436 O O   . GLN A 1 182 ? 19.180  7.073   38.032  1.00 36.52  ? 183 GLN A O   1 
ATOM   1437 C CB  . GLN A 1 182 ? 16.068  7.215   37.183  1.00 33.49  ? 183 GLN A CB  1 
ATOM   1438 C CG  . GLN A 1 182 ? 15.504  7.890   38.433  1.00 36.81  ? 183 GLN A CG  1 
ATOM   1439 C CD  . GLN A 1 182 ? 14.252  7.232   38.969  1.00 35.93  ? 183 GLN A CD  1 
ATOM   1440 O OE1 . GLN A 1 182 ? 13.574  6.485   38.285  1.00 31.13  ? 183 GLN A OE1 1 
ATOM   1441 N NE2 . GLN A 1 182 ? 13.983  7.456   40.249  1.00 34.16  ? 183 GLN A NE2 1 
ATOM   1442 N N   . GLN A 1 183 ? 18.551  9.259   38.250  1.00 35.50  ? 184 GLN A N   1 
ATOM   1443 C CA  . GLN A 1 183 ? 19.428  9.723   39.326  1.00 40.68  ? 184 GLN A CA  1 
ATOM   1444 C C   . GLN A 1 183 ? 18.558  10.509  40.309  1.00 38.10  ? 184 GLN A C   1 
ATOM   1445 O O   . GLN A 1 183 ? 17.861  11.446  39.866  1.00 37.53  ? 184 GLN A O   1 
ATOM   1446 C CB  . GLN A 1 183 ? 20.544  10.562  38.692  1.00 45.85  ? 184 GLN A CB  1 
ATOM   1447 C CG  . GLN A 1 183 ? 21.537  11.126  39.699  1.00 69.95  ? 184 GLN A CG  1 
ATOM   1448 C CD  . GLN A 1 183 ? 22.282  10.036  40.434  1.00 86.66  ? 184 GLN A CD  1 
ATOM   1449 O OE1 . GLN A 1 183 ? 22.745  9.081   39.806  1.00 106.48 ? 184 GLN A OE1 1 
ATOM   1450 N NE2 . GLN A 1 183 ? 22.390  10.152  41.761  1.00 83.99  ? 184 GLN A NE2 1 
ATOM   1451 N N   . ASN A 1 184 ? 18.667  10.206  41.597  1.00 35.96  ? 185 ASN A N   1 
ATOM   1452 C CA  . ASN A 1 184 ? 18.020  11.008  42.668  1.00 36.79  ? 185 ASN A CA  1 
ATOM   1453 C C   . ASN A 1 184 ? 19.053  11.419  43.718  1.00 42.03  ? 185 ASN A C   1 
ATOM   1454 O O   . ASN A 1 184 ? 19.949  10.607  44.143  1.00 40.47  ? 185 ASN A O   1 
ATOM   1455 C CB  . ASN A 1 184 ? 16.874  10.286  43.354  1.00 36.68  ? 185 ASN A CB  1 
ATOM   1456 C CG  . ASN A 1 184 ? 15.733  9.926   42.444  1.00 35.47  ? 185 ASN A CG  1 
ATOM   1457 O OD1 . ASN A 1 184 ? 15.936  9.378   41.377  1.00 42.03  ? 185 ASN A OD1 1 
ATOM   1458 N ND2 . ASN A 1 184 ? 14.522  10.095  42.907  1.00 36.27  ? 185 ASN A ND2 1 
ATOM   1459 N N   . THR A 1 185 ? 18.909  12.644  44.187  1.00 36.58  ? 186 THR A N   1 
ATOM   1460 C CA  . THR A 1 185 ? 19.807  13.170  45.237  1.00 38.83  ? 186 THR A CA  1 
ATOM   1461 C C   . THR A 1 185 ? 18.986  13.997  46.214  1.00 41.87  ? 186 THR A C   1 
ATOM   1462 O O   . THR A 1 185 ? 18.038  14.695  45.857  1.00 39.60  ? 186 THR A O   1 
ATOM   1463 C CB  . THR A 1 185 ? 20.952  13.957  44.587  1.00 41.74  ? 186 THR A CB  1 
ATOM   1464 O OG1 . THR A 1 185 ? 20.272  14.938  43.838  1.00 43.50  ? 186 THR A OG1 1 
ATOM   1465 C CG2 . THR A 1 185 ? 21.821  13.191  43.617  1.00 45.39  ? 186 THR A CG2 1 
ATOM   1466 N N   . PRO A 1 186 ? 19.364  13.949  47.501  1.00 40.88  ? 187 PRO A N   1 
ATOM   1467 C CA  . PRO A 1 186 ? 18.585  14.633  48.522  1.00 38.99  ? 187 PRO A CA  1 
ATOM   1468 C C   . PRO A 1 186 ? 18.797  16.147  48.315  1.00 38.48  ? 187 PRO A C   1 
ATOM   1469 O O   . PRO A 1 186 ? 19.817  16.541  47.811  1.00 38.27  ? 187 PRO A O   1 
ATOM   1470 C CB  . PRO A 1 186 ? 19.174  14.088  49.811  1.00 39.63  ? 187 PRO A CB  1 
ATOM   1471 C CG  . PRO A 1 186 ? 20.579  13.654  49.439  1.00 42.40  ? 187 PRO A CG  1 
ATOM   1472 C CD  . PRO A 1 186 ? 20.550  13.228  47.993  1.00 37.91  ? 187 PRO A CD  1 
ATOM   1473 N N   . ILE A 1 187 ? 17.793  16.950  48.617  1.00 40.91  ? 188 ILE A N   1 
ATOM   1474 C CA  . ILE A 1 187 ? 17.900  18.439  48.643  1.00 38.29  ? 188 ILE A CA  1 
ATOM   1475 C C   . ILE A 1 187 ? 18.553  18.898  49.960  1.00 43.00  ? 188 ILE A C   1 
ATOM   1476 O O   . ILE A 1 187 ? 19.273  19.877  49.918  1.00 42.00  ? 188 ILE A O   1 
ATOM   1477 C CB  . ILE A 1 187 ? 16.520  19.086  48.398  1.00 43.33  ? 188 ILE A CB  1 
ATOM   1478 C CG1 . ILE A 1 187 ? 16.007  18.688  47.006  1.00 42.67  ? 188 ILE A CG1 1 
ATOM   1479 C CG2 . ILE A 1 187 ? 16.599  20.613  48.554  1.00 45.18  ? 188 ILE A CG2 1 
ATOM   1480 C CD1 . ILE A 1 187 ? 14.620  19.097  46.659  1.00 40.42  ? 188 ILE A CD1 1 
ATOM   1481 N N   . GLY A 1 188 ? 18.244  18.262  51.093  1.00 42.85  ? 189 GLY A N   1 
ATOM   1482 C CA  . GLY A 1 188 ? 18.718  18.675  52.424  1.00 50.62  ? 189 GLY A CA  1 
ATOM   1483 C C   . GLY A 1 188 ? 20.059  18.006  52.709  1.00 57.30  ? 189 GLY A C   1 
ATOM   1484 O O   . GLY A 1 188 ? 20.490  17.146  51.874  1.00 53.44  ? 189 GLY A O   1 
ATOM   1485 N N   . ASP A 1 189 ? 20.728  18.322  53.823  1.00 50.39  ? 190 ASP A N   1 
ATOM   1486 C CA  . ASP A 1 189 ? 22.053  17.674  54.065  1.00 66.35  ? 190 ASP A CA  1 
ATOM   1487 C C   . ASP A 1 189 ? 21.946  16.680  55.230  1.00 63.28  ? 190 ASP A C   1 
ATOM   1488 O O   . ASP A 1 189 ? 22.967  16.019  55.546  1.00 67.37  ? 190 ASP A O   1 
ATOM   1489 C CB  . ASP A 1 189 ? 23.152  18.726  54.215  1.00 72.63  ? 190 ASP A CB  1 
ATOM   1490 C CG  . ASP A 1 189 ? 22.670  19.906  55.023  1.00 79.93  ? 190 ASP A CG  1 
ATOM   1491 O OD1 . ASP A 1 189 ? 22.077  19.660  56.115  1.00 73.36  ? 190 ASP A OD1 1 
ATOM   1492 O OD2 . ASP A 1 189 ? 22.827  21.042  54.523  1.00 93.15  ? 190 ASP A OD2 1 
ATOM   1493 N N   . GLY A 1 190 ? 20.753  16.549  55.813  1.00 55.23  ? 191 GLY A N   1 
ATOM   1494 C CA  . GLY A 1 190 ? 20.455  15.560  56.854  1.00 54.14  ? 191 GLY A CA  1 
ATOM   1495 C C   . GLY A 1 190 ? 20.683  14.175  56.289  1.00 49.12  ? 191 GLY A C   1 
ATOM   1496 O O   . GLY A 1 190 ? 20.709  14.022  55.082  1.00 49.10  ? 191 GLY A O   1 
ATOM   1497 N N   . PRO A 1 191 ? 20.781  13.133  57.136  1.00 54.71  ? 192 PRO A N   1 
ATOM   1498 C CA  . PRO A 1 191 ? 21.063  11.779  56.664  1.00 57.79  ? 192 PRO A CA  1 
ATOM   1499 C C   . PRO A 1 191 ? 19.878  11.138  55.921  1.00 43.85  ? 192 PRO A C   1 
ATOM   1500 O O   . PRO A 1 191 ? 18.742  11.440  56.160  1.00 52.02  ? 192 PRO A O   1 
ATOM   1501 C CB  . PRO A 1 191 ? 21.354  11.009  57.957  1.00 55.81  ? 192 PRO A CB  1 
ATOM   1502 C CG  . PRO A 1 191 ? 20.489  11.725  58.976  1.00 59.53  ? 192 PRO A CG  1 
ATOM   1503 C CD  . PRO A 1 191 ? 20.550  13.192  58.584  1.00 60.09  ? 192 PRO A CD  1 
ATOM   1504 N N   . VAL A 1 192 ? 20.217  10.249  55.007  1.00 46.48  ? 193 VAL A N   1 
ATOM   1505 C CA  . VAL A 1 192 ? 19.260  9.494   54.169  1.00 45.56  ? 193 VAL A CA  1 
ATOM   1506 C C   . VAL A 1 192 ? 19.674  8.031   54.251  1.00 49.52  ? 193 VAL A C   1 
ATOM   1507 O O   . VAL A 1 192 ? 20.779  7.747   54.772  1.00 46.93  ? 193 VAL A O   1 
ATOM   1508 C CB  . VAL A 1 192 ? 19.271  10.046  52.730  1.00 45.51  ? 193 VAL A CB  1 
ATOM   1509 C CG1 . VAL A 1 192 ? 18.914  11.542  52.715  1.00 41.68  ? 193 VAL A CG1 1 
ATOM   1510 C CG2 . VAL A 1 192 ? 20.592  9.800   52.017  1.00 50.68  ? 193 VAL A CG2 1 
ATOM   1511 N N   . LEU A 1 193 ? 18.809  7.157   53.751  1.00 44.12  ? 194 LEU A N   1 
ATOM   1512 C CA  . LEU A 1 193 ? 19.015  5.701   53.729  1.00 41.72  ? 194 LEU A CA  1 
ATOM   1513 C C   . LEU A 1 193 ? 19.490  5.334   52.341  1.00 40.96  ? 194 LEU A C   1 
ATOM   1514 O O   . LEU A 1 193 ? 18.751  5.620   51.334  1.00 39.27  ? 194 LEU A O   1 
ATOM   1515 C CB  . LEU A 1 193 ? 17.692  4.998   54.025  1.00 37.62  ? 194 LEU A CB  1 
ATOM   1516 C CG  . LEU A 1 193 ? 17.168  5.170   55.442  1.00 40.75  ? 194 LEU A CG  1 
ATOM   1517 C CD1 . LEU A 1 193 ? 15.772  4.614   55.494  1.00 37.14  ? 194 LEU A CD1 1 
ATOM   1518 C CD2 . LEU A 1 193 ? 18.076  4.498   56.496  1.00 42.23  ? 194 LEU A CD2 1 
ATOM   1519 N N   . LEU A 1 194 ? 20.674  4.769   52.264  1.00 39.39  ? 195 LEU A N   1 
ATOM   1520 C CA  . LEU A 1 194 ? 21.230  4.273   50.991  1.00 41.77  ? 195 LEU A CA  1 
ATOM   1521 C C   . LEU A 1 194 ? 20.899  2.790   50.925  1.00 43.79  ? 195 LEU A C   1 
ATOM   1522 O O   . LEU A 1 194 ? 21.303  2.012   51.783  1.00 43.16  ? 195 LEU A O   1 
ATOM   1523 C CB  . LEU A 1 194 ? 22.727  4.561   50.925  1.00 45.17  ? 195 LEU A CB  1 
ATOM   1524 C CG  . LEU A 1 194 ? 23.089  6.044   50.904  1.00 55.48  ? 195 LEU A CG  1 
ATOM   1525 C CD1 . LEU A 1 194 ? 24.595  6.275   50.946  1.00 57.43  ? 195 LEU A CD1 1 
ATOM   1526 C CD2 . LEU A 1 194 ? 22.477  6.733   49.699  1.00 55.29  ? 195 LEU A CD2 1 
ATOM   1527 N N   . PRO A 1 195 ? 20.119  2.353   49.927  1.00 36.72  ? 196 PRO A N   1 
ATOM   1528 C CA  . PRO A 1 195 ? 19.582  0.993   49.900  1.00 38.97  ? 196 PRO A CA  1 
ATOM   1529 C C   . PRO A 1 195 ? 20.526  -0.046  49.290  1.00 37.41  ? 196 PRO A C   1 
ATOM   1530 O O   . PRO A 1 195 ? 21.390  0.341   48.547  1.00 42.51  ? 196 PRO A O   1 
ATOM   1531 C CB  . PRO A 1 195 ? 18.416  1.116   48.931  1.00 34.26  ? 196 PRO A CB  1 
ATOM   1532 C CG  . PRO A 1 195 ? 18.924  2.136   47.932  1.00 33.11  ? 196 PRO A CG  1 
ATOM   1533 C CD  . PRO A 1 195 ? 19.641  3.150   48.795  1.00 39.88  ? 196 PRO A CD  1 
ATOM   1534 N N   . ASP A 1 196 ? 20.362  -1.308  49.680  1.00 40.24  ? 197 ASP A N   1 
ATOM   1535 C CA  . ASP A 1 196 ? 20.792  -2.465  48.867  1.00 40.34  ? 197 ASP A CA  1 
ATOM   1536 C C   . ASP A 1 196 ? 19.927  -2.537  47.618  1.00 44.30  ? 197 ASP A C   1 
ATOM   1537 O O   . ASP A 1 196 ? 18.812  -1.986  47.620  1.00 38.12  ? 197 ASP A O   1 
ATOM   1538 C CB  . ASP A 1 196 ? 20.604  -3.766  49.637  1.00 44.56  ? 197 ASP A CB  1 
ATOM   1539 C CG  . ASP A 1 196 ? 21.498  -3.908  50.842  1.00 44.48  ? 197 ASP A CG  1 
ATOM   1540 O OD1 . ASP A 1 196 ? 22.500  -3.188  50.919  1.00 46.88  ? 197 ASP A OD1 1 
ATOM   1541 O OD2 . ASP A 1 196 ? 21.188  -4.781  51.653  1.00 50.32  ? 197 ASP A OD2 1 
ATOM   1542 N N   . ASN A 1 197 ? 20.391  -3.262  46.608  1.00 38.08  ? 198 ASN A N   1 
ATOM   1543 C CA  . ASN A 1 197 ? 19.663  -3.417  45.340  1.00 38.80  ? 198 ASN A CA  1 
ATOM   1544 C C   . ASN A 1 197 ? 18.280  -3.981  45.614  1.00 40.23  ? 198 ASN A C   1 
ATOM   1545 O O   . ASN A 1 197 ? 18.115  -5.017  46.372  1.00 36.19  ? 198 ASN A O   1 
ATOM   1546 C CB  . ASN A 1 197 ? 20.412  -4.279  44.318  1.00 42.44  ? 198 ASN A CB  1 
ATOM   1547 C CG  . ASN A 1 197 ? 21.739  -3.684  43.896  1.00 44.45  ? 198 ASN A CG  1 
ATOM   1548 O OD1 . ASN A 1 197 ? 22.050  -2.551  44.208  1.00 42.91  ? 198 ASN A OD1 1 
ATOM   1549 N ND2 . ASN A 1 197 ? 22.523  -4.449  43.145  1.00 45.03  ? 198 ASN A ND2 1 
ATOM   1550 N N   . HIS A 1 198 ? 17.285  -3.379  44.964  1.00 36.67  ? 199 HIS A N   1 
ATOM   1551 C CA  . HIS A 1 198 ? 15.905  -3.897  44.996  1.00 37.95  ? 199 HIS A CA  1 
ATOM   1552 C C   . HIS A 1 198 ? 15.149  -3.325  43.811  1.00 34.83  ? 199 HIS A C   1 
ATOM   1553 O O   . HIS A 1 198 ? 15.724  -2.558  43.054  1.00 37.96  ? 199 HIS A O   1 
ATOM   1554 C CB  . HIS A 1 198 ? 15.265  -3.538  46.379  1.00 33.66  ? 199 HIS A CB  1 
ATOM   1555 C CG  . HIS A 1 198 ? 15.019  -2.076  46.562  1.00 30.54  ? 199 HIS A CG  1 
ATOM   1556 N ND1 . HIS A 1 198 ? 16.022  -1.187  46.944  1.00 34.54  ? 199 HIS A ND1 1 
ATOM   1557 C CD2 . HIS A 1 198 ? 13.886  -1.335  46.491  1.00 32.91  ? 199 HIS A CD2 1 
ATOM   1558 C CE1 . HIS A 1 198 ? 15.493  0.022   47.140  1.00 33.34  ? 199 HIS A CE1 1 
ATOM   1559 N NE2 . HIS A 1 198 ? 14.212  -0.024  46.789  1.00 31.23  ? 199 HIS A NE2 1 
ATOM   1560 N N   . TYR A 1 199 ? 13.856  -3.547  43.748  1.00 35.43  ? 200 TYR A N   1 
ATOM   1561 C CA  . TYR A 1 199 ? 13.016  -2.903  42.735  1.00 38.34  ? 200 TYR A CA  1 
ATOM   1562 C C   . TYR A 1 199 ? 11.672  -2.486  43.324  1.00 35.80  ? 200 TYR A C   1 
ATOM   1563 O O   . TYR A 1 199 ? 11.224  -2.994  44.383  1.00 34.66  ? 200 TYR A O   1 
ATOM   1564 C CB  . TYR A 1 199 ? 12.875  -3.806  41.517  1.00 35.89  ? 200 TYR A CB  1 
ATOM   1565 C CG  . TYR A 1 199 ? 12.094  -5.065  41.759  1.00 37.62  ? 200 TYR A CG  1 
ATOM   1566 C CD1 . TYR A 1 199 ? 10.728  -5.112  41.505  1.00 37.91  ? 200 TYR A CD1 1 
ATOM   1567 C CD2 . TYR A 1 199 ? 12.723  -6.229  42.173  1.00 43.44  ? 200 TYR A CD2 1 
ATOM   1568 C CE1 . TYR A 1 199 ? 9.998   -6.282  41.673  1.00 42.26  ? 200 TYR A CE1 1 
ATOM   1569 C CE2 . TYR A 1 199 ? 11.999  -7.411  42.343  1.00 39.07  ? 200 TYR A CE2 1 
ATOM   1570 C CZ  . TYR A 1 199 ? 10.645  -7.434  42.079  1.00 39.85  ? 200 TYR A CZ  1 
ATOM   1571 O OH  . TYR A 1 199 ? 9.929   -8.574  42.255  1.00 46.10  ? 200 TYR A OH  1 
ATOM   1572 N N   . LEU A 1 200 ? 11.059  -1.561  42.596  1.00 33.09  ? 201 LEU A N   1 
ATOM   1573 C CA  . LEU A 1 200 ? 9.654   -1.144  42.801  1.00 32.20  ? 201 LEU A CA  1 
ATOM   1574 C C   . LEU A 1 200 ? 8.800   -1.732  41.724  1.00 31.45  ? 201 LEU A C   1 
ATOM   1575 O O   . LEU A 1 200 ? 9.052   -1.482  40.518  1.00 32.56  ? 201 LEU A O   1 
ATOM   1576 C CB  . LEU A 1 200 ? 9.476   0.371   42.835  1.00 29.41  ? 201 LEU A CB  1 
ATOM   1577 C CG  . LEU A 1 200 ? 10.430  1.084   43.801  1.00 30.37  ? 201 LEU A CG  1 
ATOM   1578 C CD1 . LEU A 1 200 ? 10.255  2.600   43.778  1.00 32.31  ? 201 LEU A CD1 1 
ATOM   1579 C CD2 . LEU A 1 200 ? 10.225  0.540   45.218  1.00 33.02  ? 201 LEU A CD2 1 
ATOM   1580 N N   . SER A 1 201 ? 7.744   -2.376  42.174  1.00 29.82  ? 202 SER A N   1 
ATOM   1581 C CA  . SER A 1 201 ? 6.787   -3.005  41.267  1.00 32.64  ? 202 SER A CA  1 
ATOM   1582 C C   . SER A 1 201 ? 5.579   -2.103  41.230  1.00 32.62  ? 202 SER A C   1 
ATOM   1583 O O   . SER A 1 201 ? 4.974   -1.901  42.287  1.00 34.69  ? 202 SER A O   1 
ATOM   1584 C CB  . SER A 1 201 ? 6.468   -4.440  41.674  1.00 38.09  ? 202 SER A CB  1 
ATOM   1585 O OG  . SER A 1 201 ? 5.267   -4.874  41.035  1.00 37.42  ? 202 SER A OG  1 
ATOM   1586 N N   . THR A 1 202 ? 5.201   -1.630  40.036  1.00 31.86  ? 203 THR A N   1 
ATOM   1587 C CA  . THR A 1 202 ? 4.020   -0.762  39.860  1.00 35.22  ? 203 THR A CA  1 
ATOM   1588 C C   . THR A 1 202 ? 2.883   -1.472  39.131  1.00 37.40  ? 203 THR A C   1 
ATOM   1589 O O   . THR A 1 202 ? 3.115   -1.980  38.032  1.00 40.79  ? 203 THR A O   1 
ATOM   1590 C CB  . THR A 1 202 ? 4.382   0.503   39.072  1.00 38.86  ? 203 THR A CB  1 
ATOM   1591 O OG1 . THR A 1 202 ? 5.360   1.249   39.780  1.00 32.70  ? 203 THR A OG1 1 
ATOM   1592 C CG2 . THR A 1 202 ? 3.197   1.397   38.849  1.00 35.50  ? 203 THR A CG2 1 
ATOM   1593 N N   . GLN A 1 203 ? 1.677   -1.452  39.690  1.00 36.94  ? 204 GLN A N   1 
ATOM   1594 C CA  . GLN A 1 203 ? 0.441   -1.868  38.987  1.00 41.90  ? 204 GLN A CA  1 
ATOM   1595 C C   . GLN A 1 203 ? -0.329  -0.560  38.724  1.00 44.77  ? 204 GLN A C   1 
ATOM   1596 O O   . GLN A 1 203 ? -0.445  0.232   39.622  1.00 40.77  ? 204 GLN A O   1 
ATOM   1597 C CB  . GLN A 1 203 ? -0.230  -2.936  39.864  1.00 52.72  ? 204 GLN A CB  1 
ATOM   1598 C CG  . GLN A 1 203 ? -1.499  -3.552  39.293  1.00 59.10  ? 204 GLN A CG  1 
ATOM   1599 C CD  . GLN A 1 203 ? -2.729  -2.691  39.505  1.00 62.97  ? 204 GLN A CD  1 
ATOM   1600 O OE1 . GLN A 1 203 ? -3.041  -2.277  40.613  1.00 80.49  ? 204 GLN A OE1 1 
ATOM   1601 N NE2 . GLN A 1 203 ? -3.439  -2.360  38.440  1.00 68.76  ? 204 GLN A NE2 1 
ATOM   1602 N N   . SER A 1 204 ? -0.727  -0.283  37.489  1.00 44.45  ? 205 SER A N   1 
ATOM   1603 C CA  . SER A 1 204 ? -1.437  0.959   37.121  1.00 47.84  ? 205 SER A CA  1 
ATOM   1604 C C   . SER A 1 204 ? -2.796  0.688   36.470  1.00 56.97  ? 205 SER A C   1 
ATOM   1605 O O   . SER A 1 204 ? -2.848  -0.161  35.620  1.00 49.19  ? 205 SER A O   1 
ATOM   1606 C CB  . SER A 1 204 ? -0.561  1.803   36.267  1.00 41.96  ? 205 SER A CB  1 
ATOM   1607 O OG  . SER A 1 204 ? -1.321  2.898   35.802  1.00 44.60  ? 205 SER A OG  1 
ATOM   1608 N N   . LYS A 1 205 ? -3.854  1.386   36.881  1.00 51.91  ? 206 LYS A N   1 
ATOM   1609 C CA  . LYS A 1 205 ? -5.104  1.462   36.087  1.00 52.99  ? 206 LYS A CA  1 
ATOM   1610 C C   . LYS A 1 205 ? -5.273  2.920   35.624  1.00 55.58  ? 206 LYS A C   1 
ATOM   1611 O O   . LYS A 1 205 ? -5.235  3.867   36.453  1.00 43.70  ? 206 LYS A O   1 
ATOM   1612 C CB  . LYS A 1 205 ? -6.258  0.912   36.927  1.00 70.98  ? 206 LYS A CB  1 
ATOM   1613 C CG  . LYS A 1 205 ? -7.504  0.511   36.142  1.00 79.44  ? 206 LYS A CG  1 
ATOM   1614 C CD  . LYS A 1 205 ? -8.731  0.329   37.000  1.00 83.91  ? 206 LYS A CD  1 
ATOM   1615 C CE  . LYS A 1 205 ? -9.555  1.592   37.102  1.00 82.02  ? 206 LYS A CE  1 
ATOM   1616 N NZ  . LYS A 1 205 ? -10.363 1.575   38.334  1.00 87.46  ? 206 LYS A NZ  1 
ATOM   1617 N N   . GLN A 1 206 ? -5.439  3.109   34.330  1.00 42.80  ? 207 GLN A N   1 
ATOM   1618 C CA  . GLN A 1 206 ? -5.606  4.411   33.668  1.00 42.90  ? 207 GLN A CA  1 
ATOM   1619 C C   . GLN A 1 206 ? -7.026  4.558   33.158  1.00 41.08  ? 207 GLN A C   1 
ATOM   1620 O O   . GLN A 1 206 ? -7.573  3.579   32.583  1.00 45.00  ? 207 GLN A O   1 
ATOM   1621 C CB  . GLN A 1 206 ? -4.616  4.437   32.531  1.00 50.20  ? 207 GLN A CB  1 
ATOM   1622 C CG  . GLN A 1 206 ? -4.696  5.658   31.642  1.00 58.78  ? 207 GLN A CG  1 
ATOM   1623 C CD  . GLN A 1 206 ? -3.357  5.754   30.941  1.00 72.54  ? 207 GLN A CD  1 
ATOM   1624 O OE1 . GLN A 1 206 ? -2.319  5.723   31.595  1.00 71.07  ? 207 GLN A OE1 1 
ATOM   1625 N NE2 . GLN A 1 206 ? -3.330  5.768   29.616  1.00 63.30  ? 207 GLN A NE2 1 
ATOM   1626 N N   . SER A 1 207 ? -7.589  5.746   33.245  1.00 38.42  ? 208 SER A N   1 
ATOM   1627 C CA  . SER A 1 207 ? -8.994  5.991   32.836  1.00 40.22  ? 208 SER A CA  1 
ATOM   1628 C C   . SER A 1 207 ? -9.245  7.455   32.491  1.00 41.17  ? 208 SER A C   1 
ATOM   1629 O O   . SER A 1 207 ? -8.287  8.252   32.535  1.00 39.45  ? 208 SER A O   1 
ATOM   1630 C CB  . SER A 1 207 ? -9.943  5.494   33.863  1.00 37.92  ? 208 SER A CB  1 
ATOM   1631 O OG  . SER A 1 207 ? -9.806  6.193   35.067  1.00 43.07  ? 208 SER A OG  1 
ATOM   1632 N N   . LYS A 1 208 ? -10.444 7.743   31.989  1.00 40.92  ? 209 LYS A N   1 
ATOM   1633 C CA  . LYS A 1 208 ? -10.895 9.115   31.608  1.00 45.18  ? 209 LYS A CA  1 
ATOM   1634 C C   . LYS A 1 208 ? -12.085 9.485   32.463  1.00 45.16  ? 209 LYS A C   1 
ATOM   1635 O O   . LYS A 1 208 ? -12.804 8.577   32.862  1.00 48.11  ? 209 LYS A O   1 
ATOM   1636 C CB  . LYS A 1 208 ? -11.343 9.158   30.148  1.00 45.18  ? 209 LYS A CB  1 
ATOM   1637 C CG  . LYS A 1 208 ? -10.231 8.896   29.152  1.00 52.81  ? 209 LYS A CG  1 
ATOM   1638 C CD  . LYS A 1 208 ? -9.183  9.954   29.139  1.00 46.42  ? 209 LYS A CD  1 
ATOM   1639 C CE  . LYS A 1 208 ? -8.382  9.911   27.861  1.00 51.57  ? 209 LYS A CE  1 
ATOM   1640 N NZ  . LYS A 1 208 ? -7.200  10.799  27.949  1.00 54.00  ? 209 LYS A NZ  1 
ATOM   1641 N N   . ASP A 1 209 ? -12.260 10.759  32.740  1.00 41.10  ? 210 ASP A N   1 
ATOM   1642 C CA  . ASP A 1 209 ? -13.417 11.269  33.511  1.00 39.80  ? 210 ASP A CA  1 
ATOM   1643 C C   . ASP A 1 209 ? -14.431 11.755  32.481  1.00 45.32  ? 210 ASP A C   1 
ATOM   1644 O O   . ASP A 1 209 ? -14.153 12.685  31.729  1.00 38.96  ? 210 ASP A O   1 
ATOM   1645 C CB  . ASP A 1 209 ? -12.947 12.358  34.474  1.00 39.08  ? 210 ASP A CB  1 
ATOM   1646 C CG  . ASP A 1 209 ? -13.989 13.266  35.082  1.00 44.94  ? 210 ASP A CG  1 
ATOM   1647 O OD1 . ASP A 1 209 ? -15.243 13.081  34.843  1.00 51.93  ? 210 ASP A OD1 1 
ATOM   1648 O OD2 . ASP A 1 209 ? -13.522 14.194  35.776  1.00 39.34  ? 210 ASP A OD2 1 
ATOM   1649 N N   . PRO A 1 210 ? -15.617 11.117  32.365  1.00 50.09  ? 211 PRO A N   1 
ATOM   1650 C CA  . PRO A 1 210 ? -16.549 11.456  31.286  1.00 49.19  ? 211 PRO A CA  1 
ATOM   1651 C C   . PRO A 1 210 ? -17.098 12.898  31.343  1.00 52.65  ? 211 PRO A C   1 
ATOM   1652 O O   . PRO A 1 210 ? -17.479 13.360  30.305  1.00 58.35  ? 211 PRO A O   1 
ATOM   1653 C CB  . PRO A 1 210 ? -17.637 10.365  31.378  1.00 51.37  ? 211 PRO A CB  1 
ATOM   1654 C CG  . PRO A 1 210 ? -17.563 9.879   32.814  1.00 53.33  ? 211 PRO A CG  1 
ATOM   1655 C CD  . PRO A 1 210 ? -16.087 9.985   33.187  1.00 57.61  ? 211 PRO A CD  1 
ATOM   1656 N N   . ASN A 1 211 ? -17.032 13.582  32.494  1.00 52.34  ? 212 ASN A N   1 
ATOM   1657 C CA  . ASN A 1 211 ? -17.437 15.006  32.673  1.00 62.37  ? 212 ASN A CA  1 
ATOM   1658 C C   . ASN A 1 211 ? -16.290 15.991  32.421  1.00 55.58  ? 212 ASN A C   1 
ATOM   1659 O O   . ASN A 1 211 ? -16.479 17.200  32.686  1.00 45.81  ? 212 ASN A O   1 
ATOM   1660 C CB  . ASN A 1 211 ? -17.911 15.307  34.101  1.00 61.02  ? 212 ASN A CB  1 
ATOM   1661 C CG  . ASN A 1 211 ? -19.134 14.505  34.466  1.00 67.05  ? 212 ASN A CG  1 
ATOM   1662 O OD1 . ASN A 1 211 ? -19.146 13.857  35.499  1.00 59.58  ? 212 ASN A OD1 1 
ATOM   1663 N ND2 . ASN A 1 211 ? -20.129 14.495  33.596  1.00 60.51  ? 212 ASN A ND2 1 
ATOM   1664 N N   . GLU A 1 212 ? -15.111 15.526  32.023  1.00 49.69  ? 213 GLU A N   1 
ATOM   1665 C CA  . GLU A 1 212 ? -13.944 16.427  31.887  1.00 40.32  ? 213 GLU A CA  1 
ATOM   1666 C C   . GLU A 1 212 ? -13.749 16.755  30.407  1.00 44.02  ? 213 GLU A C   1 
ATOM   1667 O O   . GLU A 1 212 ? -13.442 15.824  29.652  1.00 40.06  ? 213 GLU A O   1 
ATOM   1668 C CB  . GLU A 1 212 ? -12.705 15.759  32.499  1.00 40.99  ? 213 GLU A CB  1 
ATOM   1669 C CG  . GLU A 1 212 ? -11.465 16.616  32.379  1.00 34.77  ? 213 GLU A CG  1 
ATOM   1670 C CD  . GLU A 1 212 ? -11.645 17.999  32.997  1.00 40.31  ? 213 GLU A CD  1 
ATOM   1671 O OE1 . GLU A 1 212 ? -11.671 18.099  34.225  1.00 36.58  ? 213 GLU A OE1 1 
ATOM   1672 O OE2 . GLU A 1 212 ? -11.690 18.968  32.265  1.00 42.12  ? 213 GLU A OE2 1 
ATOM   1673 N N   . LYS A 1 213 ? -13.837 18.034  30.024  1.00 42.75  ? 214 LYS A N   1 
ATOM   1674 C CA  . LYS A 1 213 ? -13.623 18.517  28.628  1.00 42.77  ? 214 LYS A CA  1 
ATOM   1675 C C   . LYS A 1 213 ? -12.142 18.714  28.337  1.00 43.72  ? 214 LYS A C   1 
ATOM   1676 O O   . LYS A 1 213 ? -11.794 18.762  27.183  1.00 40.00  ? 214 LYS A O   1 
ATOM   1677 C CB  . LYS A 1 213 ? -14.354 19.849  28.401  1.00 49.07  ? 214 LYS A CB  1 
ATOM   1678 C CG  . LYS A 1 213 ? -15.877 19.826  28.606  1.00 67.46  ? 214 LYS A CG  1 
ATOM   1679 C CD  . LYS A 1 213 ? -16.640 18.611  28.000  1.00 83.49  ? 214 LYS A CD  1 
ATOM   1680 C CE  . LYS A 1 213 ? -17.634 17.960  28.958  1.00 97.41  ? 214 LYS A CE  1 
ATOM   1681 N NZ  . LYS A 1 213 ? -17.651 16.479  28.829  1.00 103.72 ? 214 LYS A NZ  1 
ATOM   1682 N N   . ARG A 1 214 ? -11.318 19.039  29.335  1.00 36.89  ? 215 ARG A N   1 
ATOM   1683 C CA  . ARG A 1 214 ? -9.864  19.237  29.138  1.00 37.26  ? 215 ARG A CA  1 
ATOM   1684 C C   . ARG A 1 214 ? -9.194  17.908  28.786  1.00 35.02  ? 215 ARG A C   1 
ATOM   1685 O O   . ARG A 1 214 ? -9.640  16.843  29.203  1.00 39.92  ? 215 ARG A O   1 
ATOM   1686 C CB  . ARG A 1 214 ? -9.245  19.936  30.350  1.00 41.62  ? 215 ARG A CB  1 
ATOM   1687 C CG  . ARG A 1 214 ? -9.805  21.344  30.552  1.00 38.68  ? 215 ARG A CG  1 
ATOM   1688 C CD  . ARG A 1 214 ? -9.411  21.948  31.898  1.00 43.53  ? 215 ARG A CD  1 
ATOM   1689 N NE  . ARG A 1 214 ? -10.029 21.176  32.971  1.00 44.56  ? 215 ARG A NE  1 
ATOM   1690 C CZ  . ARG A 1 214 ? -9.860  21.389  34.245  1.00 40.01  ? 215 ARG A CZ  1 
ATOM   1691 N NH1 . ARG A 1 214 ? -9.057  22.357  34.651  1.00 38.56  ? 215 ARG A NH1 1 
ATOM   1692 N NH2 . ARG A 1 214 ? -10.439 20.579  35.115  1.00 38.12  ? 215 ARG A NH2 1 
ATOM   1693 N N   . ASP A 1 215 ? -8.121  17.975  28.021  1.00 37.28  ? 216 ASP A N   1 
ATOM   1694 C CA  . ASP A 1 215 ? -7.274  16.802  27.758  1.00 36.22  ? 216 ASP A CA  1 
ATOM   1695 C C   . ASP A 1 215 ? -6.706  16.380  29.126  1.00 37.65  ? 216 ASP A C   1 
ATOM   1696 O O   . ASP A 1 215 ? -6.211  17.274  29.820  1.00 34.36  ? 216 ASP A O   1 
ATOM   1697 C CB  . ASP A 1 215 ? -6.106  17.175  26.865  1.00 38.16  ? 216 ASP A CB  1 
ATOM   1698 C CG  . ASP A 1 215 ? -5.428  16.021  26.157  1.00 40.09  ? 216 ASP A CG  1 
ATOM   1699 O OD1 . ASP A 1 215 ? -5.733  14.848  26.482  1.00 37.99  ? 216 ASP A OD1 1 
ATOM   1700 O OD2 . ASP A 1 215 ? -4.636  16.323  25.289  1.00 42.18  ? 216 ASP A OD2 1 
ATOM   1701 N N   . HIS A 1 216 ? -6.890  15.131  29.543  1.00 35.80  ? 217 HIS A N   1 
ATOM   1702 C CA  . HIS A 1 216 ? -6.655  14.716  30.958  1.00 34.77  ? 217 HIS A CA  1 
ATOM   1703 C C   . HIS A 1 216 ? -6.386  13.213  31.036  1.00 38.70  ? 217 HIS A C   1 
ATOM   1704 O O   . HIS A 1 216 ? -6.593  12.503  30.045  1.00 35.97  ? 217 HIS A O   1 
ATOM   1705 C CB  . HIS A 1 216 ? -7.857  15.087  31.836  1.00 37.03  ? 217 HIS A CB  1 
ATOM   1706 C CG  . HIS A 1 216 ? -9.027  14.225  31.574  1.00 38.91  ? 217 HIS A CG  1 
ATOM   1707 N ND1 . HIS A 1 216 ? -9.805  14.406  30.457  1.00 37.87  ? 217 HIS A ND1 1 
ATOM   1708 C CD2 . HIS A 1 216 ? -9.505  13.145  32.243  1.00 41.67  ? 217 HIS A CD2 1 
ATOM   1709 C CE1 . HIS A 1 216 ? -10.738 13.469  30.446  1.00 43.72  ? 217 HIS A CE1 1 
ATOM   1710 N NE2 . HIS A 1 216 ? -10.584 12.694  31.544  1.00 45.79  ? 217 HIS A NE2 1 
ATOM   1711 N N   . MET A 1 217 ? -5.937  12.743  32.185  1.00 33.64  ? 218 MET A N   1 
ATOM   1712 C CA  . MET A 1 217 ? -5.650  11.297  32.463  1.00 32.85  ? 218 MET A CA  1 
ATOM   1713 C C   . MET A 1 217 ? -5.979  11.058  33.941  1.00 37.11  ? 218 MET A C   1 
ATOM   1714 O O   . MET A 1 217 ? -5.518  11.872  34.762  1.00 33.15  ? 218 MET A O   1 
ATOM   1715 C CB  . MET A 1 217 ? -4.151  11.020  32.220  1.00 34.05  ? 218 MET A CB  1 
ATOM   1716 C CG  . MET A 1 217 ? -3.627  9.682   32.718  1.00 37.92  ? 218 MET A CG  1 
ATOM   1717 S SD  . MET A 1 217 ? -1.955  9.359   32.162  1.00 38.04  ? 218 MET A SD  1 
ATOM   1718 C CE  . MET A 1 217 ? -0.977  10.424  33.234  1.00 37.88  ? 218 MET A CE  1 
ATOM   1719 N N   . VAL A 1 218 ? -6.764  10.033  34.254  1.00 36.46  ? 219 VAL A N   1 
ATOM   1720 C CA  . VAL A 1 218 ? -7.012  9.557   35.643  1.00 34.33  ? 219 VAL A CA  1 
ATOM   1721 C C   . VAL A 1 218 ? -6.182  8.310   35.873  1.00 36.35  ? 219 VAL A C   1 
ATOM   1722 O O   . VAL A 1 218 ? -6.208  7.458   34.967  1.00 36.06  ? 219 VAL A O   1 
ATOM   1723 C CB  . VAL A 1 218 ? -8.507  9.316   35.856  1.00 38.53  ? 219 VAL A CB  1 
ATOM   1724 C CG1 . VAL A 1 218 ? -8.768  8.827   37.280  1.00 37.46  ? 219 VAL A CG1 1 
ATOM   1725 C CG2 . VAL A 1 218 ? -9.272  10.597  35.579  1.00 37.53  ? 219 VAL A CG2 1 
ATOM   1726 N N   . LEU A 1 219 ? -5.485  8.225   37.007  1.00 33.03  ? 220 LEU A N   1 
ATOM   1727 C CA  . LEU A 1 219 ? -4.556  7.113   37.329  1.00 32.89  ? 220 LEU A CA  1 
ATOM   1728 C C   . LEU A 1 219 ? -4.871  6.591   38.721  1.00 39.75  ? 220 LEU A C   1 
ATOM   1729 O O   . LEU A 1 219 ? -5.009  7.411   39.707  1.00 32.62  ? 220 LEU A O   1 
ATOM   1730 C CB  . LEU A 1 219 ? -3.087  7.565   37.324  1.00 39.63  ? 220 LEU A CB  1 
ATOM   1731 C CG  . LEU A 1 219 ? -2.319  7.706   36.034  1.00 40.29  ? 220 LEU A CG  1 
ATOM   1732 C CD1 . LEU A 1 219 ? -0.835  8.003   36.334  1.00 41.78  ? 220 LEU A CD1 1 
ATOM   1733 C CD2 . LEU A 1 219 ? -2.433  6.461   35.178  1.00 39.03  ? 220 LEU A CD2 1 
ATOM   1734 N N   . LEU A 1 220 ? -4.859  5.274   38.854  1.00 34.32  ? 221 LEU A N   1 
ATOM   1735 C CA  . LEU A 1 220 ? -4.811  4.582   40.170  1.00 36.38  ? 221 LEU A CA  1 
ATOM   1736 C C   . LEU A 1 220 ? -3.572  3.702   40.108  1.00 39.61  ? 221 LEU A C   1 
ATOM   1737 O O   . LEU A 1 220 ? -3.539  2.789   39.284  1.00 37.92  ? 221 LEU A O   1 
ATOM   1738 C CB  . LEU A 1 220 ? -6.077  3.738   40.348  1.00 40.62  ? 221 LEU A CB  1 
ATOM   1739 C CG  . LEU A 1 220 ? -6.185  2.925   41.633  1.00 40.00  ? 221 LEU A CG  1 
ATOM   1740 C CD1 . LEU A 1 220 ? -6.192  3.830   42.882  1.00 45.80  ? 221 LEU A CD1 1 
ATOM   1741 C CD2 . LEU A 1 220 ? -7.443  2.078   41.605  1.00 40.71  ? 221 LEU A CD2 1 
ATOM   1742 N N   . GLU A 1 221 ? -2.639  3.963   40.998  1.00 31.19  ? 222 GLU A N   1 
ATOM   1743 C CA  . GLU A 1 221 ? -1.301  3.320   41.034  1.00 37.74  ? 222 GLU A CA  1 
ATOM   1744 C C   . GLU A 1 221 ? -1.114  2.618   42.380  1.00 36.45  ? 222 GLU A C   1 
ATOM   1745 O O   . GLU A 1 221 ? -1.478  3.156   43.470  1.00 37.73  ? 222 GLU A O   1 
ATOM   1746 C CB  . GLU A 1 221 ? -0.184  4.331   40.893  1.00 40.28  ? 222 GLU A CB  1 
ATOM   1747 C CG  . GLU A 1 221 ? -0.460  5.319   39.826  1.00 45.26  ? 222 GLU A CG  1 
ATOM   1748 C CD  . GLU A 1 221 ? -0.164  4.648   38.539  1.00 52.32  ? 222 GLU A CD  1 
ATOM   1749 O OE1 . GLU A 1 221 ? 1.024   4.312   38.403  1.00 57.25  ? 222 GLU A OE1 1 
ATOM   1750 O OE2 . GLU A 1 221 ? -1.154  4.406   37.739  1.00 49.73  ? 222 GLU A OE2 1 
ATOM   1751 N N   . PHE A 1 222 ? -0.576  1.414   42.313  1.00 34.88  ? 223 PHE A N   1 
ATOM   1752 C CA  . PHE A 1 222 ? -0.085  0.693   43.487  1.00 33.21  ? 223 PHE A CA  1 
ATOM   1753 C C   . PHE A 1 222 ? 1.361   0.335   43.241  1.00 31.32  ? 223 PHE A C   1 
ATOM   1754 O O   . PHE A 1 222 ? 1.699   -0.209  42.188  1.00 40.08  ? 223 PHE A O   1 
ATOM   1755 C CB  . PHE A 1 222 ? -0.928  -0.550  43.716  1.00 39.27  ? 223 PHE A CB  1 
ATOM   1756 C CG  . PHE A 1 222 ? -2.332  -0.228  44.133  1.00 32.14  ? 223 PHE A CG  1 
ATOM   1757 C CD1 . PHE A 1 222 ? -2.625  0.046   45.445  1.00 34.37  ? 223 PHE A CD1 1 
ATOM   1758 C CD2 . PHE A 1 222 ? -3.350  -0.215  43.191  1.00 38.60  ? 223 PHE A CD2 1 
ATOM   1759 C CE1 . PHE A 1 222 ? -3.932  0.328   45.842  1.00 40.34  ? 223 PHE A CE1 1 
ATOM   1760 C CE2 . PHE A 1 222 ? -4.648  0.045   43.584  1.00 37.82  ? 223 PHE A CE2 1 
ATOM   1761 C CZ  . PHE A 1 222 ? -4.941  0.317   44.897  1.00 36.75  ? 223 PHE A CZ  1 
ATOM   1762 N N   . VAL A 1 223 ? 2.209   0.666   44.172  1.00 30.43  ? 224 VAL A N   1 
ATOM   1763 C CA  . VAL A 1 223 ? 3.674   0.525   44.002  1.00 32.69  ? 224 VAL A CA  1 
ATOM   1764 C C   . VAL A 1 223 ? 4.207   -0.177  45.255  1.00 30.27  ? 224 VAL A C   1 
ATOM   1765 O O   . VAL A 1 223 ? 3.972   0.327   46.360  1.00 30.45  ? 224 VAL A O   1 
ATOM   1766 C CB  . VAL A 1 223 ? 4.358   1.895   43.761  1.00 31.86  ? 224 VAL A CB  1 
ATOM   1767 C CG1 . VAL A 1 223 ? 5.854   1.732   43.509  1.00 33.42  ? 224 VAL A CG1 1 
ATOM   1768 C CG2 . VAL A 1 223 ? 3.752   2.660   42.595  1.00 35.50  ? 224 VAL A CG2 1 
ATOM   1769 N N   . THR A 1 224 ? 5.017   -1.235  45.086  1.00 32.53  ? 225 THR A N   1 
ATOM   1770 C CA  . THR A 1 224 ? 5.435   -2.145  46.185  1.00 34.98  ? 225 THR A CA  1 
ATOM   1771 C C   . THR A 1 224 ? 6.939   -2.398  46.049  1.00 32.15  ? 225 THR A C   1 
ATOM   1772 O O   . THR A 1 224 ? 7.388   -2.749  44.965  1.00 36.25  ? 225 THR A O   1 
ATOM   1773 C CB  . THR A 1 224 ? 4.613   -3.443  46.148  1.00 35.52  ? 225 THR A CB  1 
ATOM   1774 O OG1 . THR A 1 224 ? 3.191   -3.258  45.999  1.00 35.78  ? 225 THR A OG1 1 
ATOM   1775 C CG2 . THR A 1 224 ? 4.863   -4.251  47.398  1.00 37.59  ? 225 THR A CG2 1 
ATOM   1776 N N   . ALA A 1 225 ? 7.705   -2.208  47.100  1.00 31.31  ? 226 ALA A N   1 
ATOM   1777 C CA  . ALA A 1 225 ? 9.154   -2.495  47.088  1.00 29.25  ? 226 ALA A CA  1 
ATOM   1778 C C   . ALA A 1 225 ? 9.311   -4.021  47.202  1.00 35.33  ? 226 ALA A C   1 
ATOM   1779 O O   . ALA A 1 225 ? 8.437   -4.676  47.923  1.00 30.16  ? 226 ALA A O   1 
ATOM   1780 C CB  . ALA A 1 225 ? 9.904   -1.788  48.192  1.00 30.92  ? 226 ALA A CB  1 
ATOM   1781 N N   . ALA A 1 226 ? 10.260  -4.593  46.454  1.00 36.91  ? 227 ALA A N   1 
ATOM   1782 C CA  . ALA A 1 226 ? 10.419  -6.073  46.419  1.00 37.89  ? 227 ALA A CA  1 
ATOM   1783 C C   . ALA A 1 226 ? 11.839  -6.399  46.012  1.00 43.02  ? 227 ALA A C   1 
ATOM   1784 O O   . ALA A 1 226 ? 12.593  -5.449  45.761  1.00 33.27  ? 227 ALA A O   1 
ATOM   1785 C CB  . ALA A 1 226 ? 9.391   -6.688  45.514  1.00 39.23  ? 227 ALA A CB  1 
ATOM   1786 N N   . GLY A 1 227 ? 12.213  -7.680  46.070  1.00 39.73  ? 228 GLY A N   1 
ATOM   1787 C CA  . GLY A 1 227 ? 13.515  -8.139  45.569  1.00 35.93  ? 228 GLY A CA  1 
ATOM   1788 C C   . GLY A 1 227 ? 14.496  -8.468  46.663  1.00 44.64  ? 228 GLY A C   1 
ATOM   1789 O O   . GLY A 1 227 ? 15.611  -8.876  46.345  1.00 38.05  ? 228 GLY A O   1 
ATOM   1790 N N   . ILE A 1 228 ? 14.109  -8.299  47.922  1.00 43.08  ? 229 ILE A N   1 
ATOM   1791 C CA  . ILE A 1 228 ? 14.964  -8.708  49.053  1.00 44.81  ? 229 ILE A CA  1 
ATOM   1792 C C   . ILE A 1 228 ? 14.071  -9.608  49.869  1.00 49.60  ? 229 ILE A C   1 
ATOM   1793 O O   . ILE A 1 228 ? 12.992  -9.171  50.244  1.00 41.56  ? 229 ILE A O   1 
ATOM   1794 C CB  . ILE A 1 228 ? 15.540  -7.520  49.858  1.00 45.93  ? 229 ILE A CB  1 
ATOM   1795 C CG1 . ILE A 1 228 ? 16.470  -6.650  49.003  1.00 44.44  ? 229 ILE A CG1 1 
ATOM   1796 C CG2 . ILE A 1 228 ? 16.266  -8.072  51.071  1.00 51.11  ? 229 ILE A CG2 1 
ATOM   1797 C CD1 . ILE A 1 228 ? 16.919  -5.385  49.648  1.00 43.87  ? 229 ILE A CD1 1 
ATOM   1798 N N   . PRO A 1 229 ? 14.420  -10.904 50.044  1.00 46.60  ? 230 PRO A N   1 
ATOM   1799 C CA  . PRO A 1 229 ? 13.509  -11.820 50.725  1.00 46.69  ? 230 PRO A CA  1 
ATOM   1800 C C   . PRO A 1 229 ? 13.381  -11.535 52.237  1.00 41.04  ? 230 PRO A C   1 
ATOM   1801 O O   . PRO A 1 229 ? 14.255  -10.949 52.914  1.00 44.51  ? 230 PRO A O   1 
ATOM   1802 C CB  . PRO A 1 229 ? 14.111  -13.210 50.451  1.00 52.43  ? 230 PRO A CB  1 
ATOM   1803 C CG  . PRO A 1 229 ? 15.591  -12.942 50.209  1.00 55.21  ? 230 PRO A CG  1 
ATOM   1804 C CD  . PRO A 1 229 ? 15.668  -11.555 49.596  1.00 55.77  ? 230 PRO A CD  1 
ATOM   1805 N N   . LEU A 1 230 ? 12.214  -11.893 52.734  1.00 46.55  ? 231 LEU A N   1 
ATOM   1806 C CA  . LEU A 1 230 ? 11.978  -12.109 54.168  1.00 48.52  ? 231 LEU A CA  1 
ATOM   1807 C C   . LEU A 1 230 ? 12.770  -13.356 54.563  1.00 41.99  ? 231 LEU A C   1 
ATOM   1808 O O   . LEU A 1 230 ? 13.278  -12.950 55.605  1.00 53.70  ? 231 LEU A O   1 
ATOM   1809 C CB  . LEU A 1 230 ? 10.471  -12.276 54.307  1.00 52.16  ? 231 LEU A CB  1 
ATOM   1810 C CG  . LEU A 1 230 ? 9.912   -12.287 55.726  1.00 53.21  ? 231 LEU A CG  1 
ATOM   1811 C CD1 . LEU A 1 230 ? 10.055  -10.929 56.402  1.00 51.23  ? 231 LEU A CD1 1 
ATOM   1812 C CD2 . LEU A 1 230 ? 8.453   -12.686 55.687  1.00 50.52  ? 231 LEU A CD2 1 
ATOM   1813 N N   . MET B 1 1   ? 30.209  1.632   -16.593 1.00 48.73  ? 0   MET B N   1 
ATOM   1814 C CA  . MET B 1 1   ? 28.777  1.775   -16.267 1.00 51.49  ? 0   MET B CA  1 
ATOM   1815 C C   . MET B 1 1   ? 28.594  1.767   -14.746 1.00 50.78  ? 0   MET B C   1 
ATOM   1816 O O   . MET B 1 1   ? 29.261  0.964   -14.079 1.00 48.44  ? 0   MET B O   1 
ATOM   1817 C CB  . MET B 1 1   ? 27.929  0.638   -16.857 1.00 43.99  ? 0   MET B CB  1 
ATOM   1818 C CG  . MET B 1 1   ? 26.408  0.984   -16.915 1.00 40.47  ? 0   MET B CG  1 
ATOM   1819 S SD  . MET B 1 1   ? 25.932  1.888   -18.447 1.00 47.38  ? 0   MET B SD  1 
ATOM   1820 C CE  . MET B 1 1   ? 24.183  2.192   -18.174 1.00 41.83  ? 0   MET B CE  1 
ATOM   1821 N N   . VAL B 1 2   ? 27.694  2.608   -14.248 1.00 53.33  ? 1   VAL B N   1 
ATOM   1822 C CA  . VAL B 1 2   ? 27.278  2.602   -12.813 1.00 54.68  ? 1   VAL B CA  1 
ATOM   1823 C C   . VAL B 1 2   ? 26.553  1.276   -12.462 1.00 60.80  ? 1   VAL B C   1 
ATOM   1824 O O   . VAL B 1 2   ? 26.468  0.917   -11.260 1.00 57.11  ? 1   VAL B O   1 
ATOM   1825 C CB  . VAL B 1 2   ? 26.398  3.834   -12.502 1.00 55.21  ? 1   VAL B CB  1 
ATOM   1826 C CG1 . VAL B 1 2   ? 24.956  3.633   -12.960 1.00 51.72  ? 1   VAL B CG1 1 
ATOM   1827 C CG2 . VAL B 1 2   ? 26.472  4.218   -11.021 1.00 55.09  ? 1   VAL B CG2 1 
ATOM   1828 N N   . SER B 1 3   ? 26.002  0.576   -13.451 1.00 57.06  ? 2   SER B N   1 
ATOM   1829 C CA  . SER B 1 3   ? 25.260  -0.714  -13.300 1.00 65.51  ? 2   SER B CA  1 
ATOM   1830 C C   . SER B 1 3   ? 26.205  -1.909  -13.055 1.00 57.92  ? 2   SER B C   1 
ATOM   1831 O O   . SER B 1 3   ? 25.680  -3.022  -12.769 1.00 54.87  ? 2   SER B O   1 
ATOM   1832 C CB  . SER B 1 3   ? 24.392  -0.975  -14.541 1.00 58.06  ? 2   SER B CB  1 
ATOM   1833 O OG  . SER B 1 3   ? 23.475  0.080   -14.722 1.00 71.03  ? 2   SER B OG  1 
ATOM   1834 N N   . LYS B 1 4   ? 27.522  -1.722  -13.227 1.00 49.27  ? 3   LYS B N   1 
ATOM   1835 C CA  . LYS B 1 4   ? 28.499  -2.839  -13.253 1.00 54.58  ? 3   LYS B CA  1 
ATOM   1836 C C   . LYS B 1 4   ? 28.515  -3.502  -11.858 1.00 42.90  ? 3   LYS B C   1 
ATOM   1837 O O   . LYS B 1 4   ? 28.369  -4.722  -11.782 1.00 42.43  ? 3   LYS B O   1 
ATOM   1838 C CB  . LYS B 1 4   ? 29.862  -2.352  -13.738 1.00 52.92  ? 3   LYS B CB  1 
ATOM   1839 C CG  . LYS B 1 4   ? 31.027  -3.251  -13.369 1.00 67.81  ? 3   LYS B CG  1 
ATOM   1840 C CD  . LYS B 1 4   ? 32.206  -3.123  -14.298 1.00 80.52  ? 3   LYS B CD  1 
ATOM   1841 C CE  . LYS B 1 4   ? 33.519  -3.011  -13.549 1.00 85.26  ? 3   LYS B CE  1 
ATOM   1842 N NZ  . LYS B 1 4   ? 34.629  -2.726  -14.484 1.00 93.09  ? 3   LYS B NZ  1 
ATOM   1843 N N   . GLY B 1 5   ? 28.595  -2.703  -10.797 1.00 41.16  ? 4   GLY B N   1 
ATOM   1844 C CA  . GLY B 1 5   ? 28.698  -3.214  -9.423  1.00 41.63  ? 4   GLY B CA  1 
ATOM   1845 C C   . GLY B 1 5   ? 27.559  -4.151  -9.048  1.00 35.54  ? 4   GLY B C   1 
ATOM   1846 O O   . GLY B 1 5   ? 27.826  -5.230  -8.515  1.00 38.74  ? 4   GLY B O   1 
ATOM   1847 N N   . GLU B 1 6   ? 26.319  -3.751  -9.306  1.00 39.49  ? 5   GLU B N   1 
ATOM   1848 C CA  . GLU B 1 6   ? 25.109  -4.539  -8.977  1.00 35.15  ? 5   GLU B CA  1 
ATOM   1849 C C   . GLU B 1 6   ? 25.207  -5.918  -9.631  1.00 36.91  ? 5   GLU B C   1 
ATOM   1850 O O   . GLU B 1 6   ? 24.815  -6.889  -8.977  1.00 36.47  ? 5   GLU B O   1 
ATOM   1851 C CB  . GLU B 1 6   ? 23.832  -3.743  -9.331  1.00 46.09  ? 5   GLU B CB  1 
ATOM   1852 C CG  . GLU B 1 6   ? 23.162  -4.067  -10.667 1.00 64.33  ? 5   GLU B CG  1 
ATOM   1853 C CD  . GLU B 1 6   ? 22.107  -5.170  -10.616 1.00 74.82  ? 5   GLU B CD  1 
ATOM   1854 O OE1 . GLU B 1 6   ? 21.203  -5.079  -9.750  1.00 90.52  ? 5   GLU B OE1 1 
ATOM   1855 O OE2 . GLU B 1 6   ? 22.182  -6.119  -11.454 1.00 89.57  ? 5   GLU B OE2 1 
ATOM   1856 N N   . LYS B 1 7   ? 25.656  -6.021  -10.888 1.00 38.42  ? 6   LYS B N   1 
ATOM   1857 C CA  . LYS B 1 7   ? 25.742  -7.331  -11.595 1.00 44.36  ? 6   LYS B CA  1 
ATOM   1858 C C   . LYS B 1 7   ? 26.687  -8.310  -10.878 1.00 40.09  ? 6   LYS B C   1 
ATOM   1859 O O   . LYS B 1 7   ? 26.492  -9.502  -11.056 1.00 42.45  ? 6   LYS B O   1 
ATOM   1860 C CB  . LYS B 1 7   ? 26.219  -7.164  -13.038 1.00 53.37  ? 6   LYS B CB  1 
ATOM   1861 C CG  . LYS B 1 7   ? 25.363  -6.281  -13.939 1.00 58.79  ? 6   LYS B CG  1 
ATOM   1862 C CD  . LYS B 1 7   ? 26.187  -5.823  -15.183 1.00 66.52  ? 6   LYS B CD  1 
ATOM   1863 C CE  . LYS B 1 7   ? 25.687  -4.595  -15.927 1.00 68.25  ? 6   LYS B CE  1 
ATOM   1864 N NZ  . LYS B 1 7   ? 24.486  -4.909  -16.736 1.00 72.17  ? 6   LYS B NZ  1 
ATOM   1865 N N   . LEU B 1 8   ? 27.617  -7.856  -10.040 1.00 36.79  ? 7   LEU B N   1 
ATOM   1866 C CA  . LEU B 1 8   ? 28.544  -8.747  -9.267  1.00 35.99  ? 7   LEU B CA  1 
ATOM   1867 C C   . LEU B 1 8   ? 27.806  -9.486  -8.138  1.00 37.57  ? 7   LEU B C   1 
ATOM   1868 O O   . LEU B 1 8   ? 28.347  -10.421 -7.622  1.00 35.40  ? 7   LEU B O   1 
ATOM   1869 C CB  . LEU B 1 8   ? 29.710  -7.926  -8.715  1.00 38.50  ? 7   LEU B CB  1 
ATOM   1870 C CG  . LEU B 1 8   ? 30.603  -7.226  -9.736  1.00 39.88  ? 7   LEU B CG  1 
ATOM   1871 C CD1 . LEU B 1 8   ? 31.641  -6.315  -9.080  1.00 37.41  ? 7   LEU B CD1 1 
ATOM   1872 C CD2 . LEU B 1 8   ? 31.269  -8.258  -10.644 1.00 49.05  ? 7   LEU B CD2 1 
ATOM   1873 N N   . PHE B 1 9   ? 26.557  -9.137  -7.827  1.00 38.40  ? 8   PHE B N   1 
ATOM   1874 C CA  . PHE B 1 9   ? 25.853  -9.631  -6.623  1.00 37.43  ? 8   PHE B CA  1 
ATOM   1875 C C   . PHE B 1 9   ? 24.633  -10.496 -7.000  1.00 42.36  ? 8   PHE B C   1 
ATOM   1876 O O   . PHE B 1 9   ? 23.897  -10.876 -6.050  1.00 39.34  ? 8   PHE B O   1 
ATOM   1877 C CB  . PHE B 1 9   ? 25.419  -8.455  -5.740  1.00 34.90  ? 8   PHE B CB  1 
ATOM   1878 C CG  . PHE B 1 9   ? 26.556  -7.804  -5.018  1.00 34.50  ? 8   PHE B CG  1 
ATOM   1879 C CD1 . PHE B 1 9   ? 27.010  -8.269  -3.791  1.00 32.63  ? 8   PHE B CD1 1 
ATOM   1880 C CD2 . PHE B 1 9   ? 27.241  -6.747  -5.621  1.00 32.47  ? 8   PHE B CD2 1 
ATOM   1881 C CE1 . PHE B 1 9   ? 28.117  -7.667  -3.190  1.00 31.20  ? 8   PHE B CE1 1 
ATOM   1882 C CE2 . PHE B 1 9   ? 28.342  -6.163  -5.025  1.00 31.93  ? 8   PHE B CE2 1 
ATOM   1883 C CZ  . PHE B 1 9   ? 28.734  -6.577  -3.792  1.00 34.29  ? 8   PHE B CZ  1 
ATOM   1884 N N   . THR B 1 10  ? 24.400  -10.821 -8.284  1.00 37.63  ? 9   THR B N   1 
ATOM   1885 C CA  . THR B 1 10  ? 23.187  -11.602 -8.693  1.00 43.47  ? 9   THR B CA  1 
ATOM   1886 C C   . THR B 1 10  ? 23.325  -13.071 -8.259  1.00 43.46  ? 9   THR B C   1 
ATOM   1887 O O   . THR B 1 10  ? 22.338  -13.736 -8.162  1.00 44.33  ? 9   THR B O   1 
ATOM   1888 C CB  . THR B 1 10  ? 22.896  -11.496 -10.205 1.00 46.85  ? 9   THR B CB  1 
ATOM   1889 O OG1 . THR B 1 10  ? 24.023  -11.932 -10.944 1.00 41.19  ? 9   THR B OG1 1 
ATOM   1890 C CG2 . THR B 1 10  ? 22.588  -10.088 -10.657 1.00 49.74  ? 9   THR B CG2 1 
ATOM   1891 N N   . GLY B 1 11  ? 24.526  -13.546 -7.965  1.00 43.36  ? 10  GLY B N   1 
ATOM   1892 C CA  . GLY B 1 11  ? 24.767  -14.938 -7.552  1.00 44.03  ? 10  GLY B CA  1 
ATOM   1893 C C   . GLY B 1 11  ? 25.179  -14.955 -6.098  1.00 48.25  ? 10  GLY B C   1 
ATOM   1894 O O   . GLY B 1 11  ? 25.103  -13.894 -5.429  1.00 41.30  ? 10  GLY B O   1 
ATOM   1895 N N   . VAL B 1 12  ? 25.602  -16.118 -5.648  1.00 42.79  ? 11  VAL B N   1 
ATOM   1896 C CA  . VAL B 1 12  ? 26.182  -16.346 -4.304  1.00 43.13  ? 11  VAL B CA  1 
ATOM   1897 C C   . VAL B 1 12  ? 27.621  -15.867 -4.365  1.00 44.14  ? 11  VAL B C   1 
ATOM   1898 O O   . VAL B 1 12  ? 28.351  -16.245 -5.300  1.00 37.30  ? 11  VAL B O   1 
ATOM   1899 C CB  . VAL B 1 12  ? 26.102  -17.822 -3.897  1.00 46.16  ? 11  VAL B CB  1 
ATOM   1900 C CG1 . VAL B 1 12  ? 26.791  -18.040 -2.566  1.00 50.33  ? 11  VAL B CG1 1 
ATOM   1901 C CG2 . VAL B 1 12  ? 24.656  -18.285 -3.855  1.00 42.14  ? 11  VAL B CG2 1 
ATOM   1902 N N   . VAL B 1 13  ? 27.980  -14.977 -3.442  1.00 39.03  ? 12  VAL B N   1 
ATOM   1903 C CA  . VAL B 1 13  ? 29.329  -14.356 -3.413  1.00 37.01  ? 12  VAL B CA  1 
ATOM   1904 C C   . VAL B 1 13  ? 30.035  -14.805 -2.137  1.00 37.07  ? 12  VAL B C   1 
ATOM   1905 O O   . VAL B 1 13  ? 29.505  -14.649 -1.037  1.00 36.51  ? 12  VAL B O   1 
ATOM   1906 C CB  . VAL B 1 13  ? 29.275  -12.826 -3.510  1.00 36.77  ? 12  VAL B CB  1 
ATOM   1907 C CG1 . VAL B 1 13  ? 30.668  -12.241 -3.413  1.00 35.00  ? 12  VAL B CG1 1 
ATOM   1908 C CG2 . VAL B 1 13  ? 28.636  -12.373 -4.815  1.00 40.65  ? 12  VAL B CG2 1 
ATOM   1909 N N   . PRO B 1 14  ? 31.243  -15.396 -2.264  1.00 37.77  ? 13  PRO B N   1 
ATOM   1910 C CA  . PRO B 1 14  ? 32.061  -15.741 -1.096  1.00 36.60  ? 13  PRO B CA  1 
ATOM   1911 C C   . PRO B 1 14  ? 32.529  -14.465 -0.369  1.00 32.43  ? 13  PRO B C   1 
ATOM   1912 O O   . PRO B 1 14  ? 32.717  -13.434 -0.977  1.00 32.50  ? 13  PRO B O   1 
ATOM   1913 C CB  . PRO B 1 14  ? 33.263  -16.552 -1.650  1.00 37.01  ? 13  PRO B CB  1 
ATOM   1914 C CG  . PRO B 1 14  ? 33.061  -16.664 -3.131  1.00 39.29  ? 13  PRO B CG  1 
ATOM   1915 C CD  . PRO B 1 14  ? 31.874  -15.787 -3.532  1.00 40.81  ? 13  PRO B CD  1 
ATOM   1916 N N   . ILE B 1 15  ? 32.556  -14.553 0.952   1.00 32.34  ? 14  ILE B N   1 
ATOM   1917 C CA  . ILE B 1 15  ? 32.781  -13.424 1.859   1.00 28.23  ? 14  ILE B CA  1 
ATOM   1918 C C   . ILE B 1 15  ? 33.987  -13.844 2.704   1.00 33.29  ? 14  ILE B C   1 
ATOM   1919 O O   . ILE B 1 15  ? 33.988  -14.967 3.262   1.00 33.98  ? 14  ILE B O   1 
ATOM   1920 C CB  . ILE B 1 15  ? 31.543  -13.146 2.739   1.00 30.01  ? 14  ILE B CB  1 
ATOM   1921 C CG1 . ILE B 1 15  ? 30.344  -12.634 1.929   1.00 31.68  ? 14  ILE B CG1 1 
ATOM   1922 C CG2 . ILE B 1 15  ? 31.983  -12.175 3.800   1.00 30.82  ? 14  ILE B CG2 1 
ATOM   1923 C CD1 . ILE B 1 15  ? 29.160  -12.331 2.790   1.00 35.76  ? 14  ILE B CD1 1 
ATOM   1924 N N   . LEU B 1 16  ? 34.773  -12.854 3.040   1.00 32.58  ? 15  LEU B N   1 
ATOM   1925 C CA  . LEU B 1 16  ? 35.901  -12.963 3.965   1.00 35.58  ? 15  LEU B CA  1 
ATOM   1926 C C   . LEU B 1 16  ? 35.945  -11.682 4.756   1.00 34.69  ? 15  LEU B C   1 
ATOM   1927 O O   . LEU B 1 16  ? 35.869  -10.595 4.158   1.00 36.30  ? 15  LEU B O   1 
ATOM   1928 C CB  . LEU B 1 16  ? 37.126  -13.103 3.058   1.00 37.49  ? 15  LEU B CB  1 
ATOM   1929 C CG  . LEU B 1 16  ? 38.332  -13.813 3.589   1.00 53.27  ? 15  LEU B CG  1 
ATOM   1930 C CD1 . LEU B 1 16  ? 37.949  -15.220 4.024   1.00 49.86  ? 15  LEU B CD1 1 
ATOM   1931 C CD2 . LEU B 1 16  ? 39.366  -13.831 2.457   1.00 47.50  ? 15  LEU B CD2 1 
ATOM   1932 N N   . VAL B 1 17  ? 35.966  -11.796 6.067   1.00 35.24  ? 16  VAL B N   1 
ATOM   1933 C CA  . VAL B 1 17  ? 36.010  -10.640 6.978   1.00 37.07  ? 16  VAL B CA  1 
ATOM   1934 C C   . VAL B 1 17  ? 37.302  -10.792 7.780   1.00 34.05  ? 16  VAL B C   1 
ATOM   1935 O O   . VAL B 1 17  ? 37.538  -11.901 8.284   1.00 36.65  ? 16  VAL B O   1 
ATOM   1936 C CB  . VAL B 1 17  ? 34.772  -10.579 7.882   1.00 35.07  ? 16  VAL B CB  1 
ATOM   1937 C CG1 . VAL B 1 17  ? 34.815  -9.337  8.758   1.00 34.77  ? 16  VAL B CG1 1 
ATOM   1938 C CG2 . VAL B 1 17  ? 33.490  -10.541 7.073   1.00 34.68  ? 16  VAL B CG2 1 
ATOM   1939 N N   . GLU B 1 18  ? 38.063  -9.729  7.949   1.00 34.37  ? 17  GLU B N   1 
ATOM   1940 C CA  . GLU B 1 18  ? 39.236  -9.725  8.867   1.00 37.21  ? 17  GLU B CA  1 
ATOM   1941 C C   . GLU B 1 18  ? 39.159  -8.452  9.669   1.00 34.00  ? 17  GLU B C   1 
ATOM   1942 O O   . GLU B 1 18  ? 39.004  -7.392  9.046   1.00 41.21  ? 17  GLU B O   1 
ATOM   1943 C CB  . GLU B 1 18  ? 40.590  -9.780  8.147   1.00 36.43  ? 17  GLU B CB  1 
ATOM   1944 C CG  . GLU B 1 18  ? 40.621  -10.879 7.153   1.00 40.85  ? 17  GLU B CG  1 
ATOM   1945 C CD  . GLU B 1 18  ? 40.647  -12.278 7.747   1.00 41.63  ? 17  GLU B CD  1 
ATOM   1946 O OE1 . GLU B 1 18  ? 41.102  -12.418 8.895   1.00 41.14  ? 17  GLU B OE1 1 
ATOM   1947 O OE2 . GLU B 1 18  ? 40.189  -13.223 7.046   1.00 47.90  ? 17  GLU B OE2 1 
ATOM   1948 N N   . LEU B 1 19  ? 39.246  -8.593  10.987  1.00 35.91  ? 18  LEU B N   1 
ATOM   1949 C CA  . LEU B 1 19  ? 39.164  -7.497  11.959  1.00 37.14  ? 18  LEU B CA  1 
ATOM   1950 C C   . LEU B 1 19  ? 40.402  -7.589  12.850  1.00 35.43  ? 18  LEU B C   1 
ATOM   1951 O O   . LEU B 1 19  ? 40.660  -8.649  13.458  1.00 36.18  ? 18  LEU B O   1 
ATOM   1952 C CB  . LEU B 1 19  ? 37.882  -7.576  12.788  1.00 38.85  ? 18  LEU B CB  1 
ATOM   1953 C CG  . LEU B 1 19  ? 37.696  -6.421  13.760  1.00 39.27  ? 18  LEU B CG  1 
ATOM   1954 C CD1 . LEU B 1 19  ? 36.260  -6.321  14.235  1.00 48.78  ? 18  LEU B CD1 1 
ATOM   1955 C CD2 . LEU B 1 19  ? 38.569  -6.609  14.965  1.00 44.78  ? 18  LEU B CD2 1 
ATOM   1956 N N   . ASP B 1 20  ? 41.171  -6.511  12.846  1.00 42.66  ? 19  ASP B N   1 
ATOM   1957 C CA  . ASP B 1 20  ? 42.328  -6.294  13.759  1.00 43.37  ? 19  ASP B CA  1 
ATOM   1958 C C   . ASP B 1 20  ? 41.857  -5.263  14.783  1.00 38.72  ? 19  ASP B C   1 
ATOM   1959 O O   . ASP B 1 20  ? 41.470  -4.145  14.386  1.00 38.31  ? 19  ASP B O   1 
ATOM   1960 C CB  . ASP B 1 20  ? 43.588  -5.845  12.994  1.00 49.08  ? 19  ASP B CB  1 
ATOM   1961 C CG  . ASP B 1 20  ? 44.653  -6.939  12.891  1.00 75.57  ? 19  ASP B CG  1 
ATOM   1962 O OD1 . ASP B 1 20  ? 44.296  -8.212  12.914  1.00 58.77  ? 19  ASP B OD1 1 
ATOM   1963 O OD2 . ASP B 1 20  ? 45.841  -6.543  12.781  1.00 90.93  ? 19  ASP B OD2 1 
ATOM   1964 N N   . GLY B 1 21  ? 41.756  -5.678  16.030  1.00 41.69  ? 20  GLY B N   1 
ATOM   1965 C CA  . GLY B 1 21  ? 41.126  -4.873  17.075  1.00 38.90  ? 20  GLY B CA  1 
ATOM   1966 C C   . GLY B 1 21  ? 42.149  -4.476  18.119  1.00 41.08  ? 20  GLY B C   1 
ATOM   1967 O O   . GLY B 1 21  ? 42.982  -5.291  18.436  1.00 40.33  ? 20  GLY B O   1 
ATOM   1968 N N   . ASP B 1 22  ? 41.950  -3.329  18.747  1.00 46.17  ? 21  ASP B N   1 
ATOM   1969 C CA  . ASP B 1 22  ? 42.707  -2.937  19.966  1.00 52.94  ? 21  ASP B CA  1 
ATOM   1970 C C   . ASP B 1 22  ? 41.779  -2.120  20.851  1.00 38.35  ? 21  ASP B C   1 
ATOM   1971 O O   . ASP B 1 22  ? 41.464  -0.998  20.462  1.00 45.90  ? 21  ASP B O   1 
ATOM   1972 C CB  . ASP B 1 22  ? 43.985  -2.133  19.670  1.00 62.60  ? 21  ASP B CB  1 
ATOM   1973 C CG  . ASP B 1 22  ? 44.797  -1.877  20.937  1.00 60.34  ? 21  ASP B CG  1 
ATOM   1974 O OD1 . ASP B 1 22  ? 44.211  -1.371  21.907  1.00 74.05  ? 21  ASP B OD1 1 
ATOM   1975 O OD2 . ASP B 1 22  ? 45.977  -2.253  20.971  1.00 65.60  ? 21  ASP B OD2 1 
ATOM   1976 N N   . VAL B 1 23  ? 41.370  -2.706  21.970  1.00 44.66  ? 22  VAL B N   1 
ATOM   1977 C CA  . VAL B 1 23  ? 40.469  -2.099  22.962  1.00 40.12  ? 22  VAL B CA  1 
ATOM   1978 C C   . VAL B 1 23  ? 41.242  -1.975  24.284  1.00 41.64  ? 22  VAL B C   1 
ATOM   1979 O O   . VAL B 1 23  ? 41.586  -2.984  24.884  1.00 40.18  ? 22  VAL B O   1 
ATOM   1980 C CB  . VAL B 1 23  ? 39.189  -2.923  23.110  1.00 44.11  ? 22  VAL B CB  1 
ATOM   1981 C CG1 . VAL B 1 23  ? 38.271  -2.314  24.152  1.00 42.03  ? 22  VAL B CG1 1 
ATOM   1982 C CG2 . VAL B 1 23  ? 38.465  -3.045  21.767  1.00 48.53  ? 22  VAL B CG2 1 
ATOM   1983 N N   . ASN B 1 24  ? 41.551  -0.750  24.671  1.00 47.07  ? 23  ASN B N   1 
ATOM   1984 C CA  . ASN B 1 24  ? 42.355  -0.480  25.882  1.00 43.92  ? 23  ASN B CA  1 
ATOM   1985 C C   . ASN B 1 24  ? 43.663  -1.256  25.837  1.00 48.39  ? 23  ASN B C   1 
ATOM   1986 O O   . ASN B 1 24  ? 43.964  -1.924  26.825  1.00 51.37  ? 23  ASN B O   1 
ATOM   1987 C CB  . ASN B 1 24  ? 41.578  -0.900  27.104  1.00 47.45  ? 23  ASN B CB  1 
ATOM   1988 C CG  . ASN B 1 24  ? 40.582  0.175   27.454  1.00 51.24  ? 23  ASN B CG  1 
ATOM   1989 O OD1 . ASN B 1 24  ? 40.133  0.917   26.574  1.00 47.81  ? 23  ASN B OD1 1 
ATOM   1990 N ND2 . ASN B 1 24  ? 40.280  0.279   28.731  1.00 48.29  ? 23  ASN B ND2 1 
ATOM   1991 N N   . GLY B 1 25  ? 44.336  -1.251  24.691  1.00 56.31  ? 24  GLY B N   1 
ATOM   1992 C CA  . GLY B 1 25  ? 45.576  -2.041  24.516  1.00 67.26  ? 24  GLY B CA  1 
ATOM   1993 C C   . GLY B 1 25  ? 45.371  -3.556  24.376  1.00 72.63  ? 24  GLY B C   1 
ATOM   1994 O O   . GLY B 1 25  ? 46.377  -4.230  24.037  1.00 61.17  ? 24  GLY B O   1 
ATOM   1995 N N   . HIS B 1 26  ? 44.174  -4.122  24.617  1.00 53.20  ? 25  HIS B N   1 
ATOM   1996 C CA  . HIS B 1 26  ? 43.936  -5.577  24.422  1.00 52.02  ? 25  HIS B CA  1 
ATOM   1997 C C   . HIS B 1 26  ? 43.796  -5.825  22.920  1.00 58.22  ? 25  HIS B C   1 
ATOM   1998 O O   . HIS B 1 26  ? 42.804  -5.330  22.325  1.00 53.65  ? 25  HIS B O   1 
ATOM   1999 C CB  . HIS B 1 26  ? 42.751  -6.080  25.268  1.00 55.94  ? 25  HIS B CB  1 
ATOM   2000 C CG  . HIS B 1 26  ? 42.866  -5.684  26.703  1.00 64.61  ? 25  HIS B CG  1 
ATOM   2001 N ND1 . HIS B 1 26  ? 43.976  -6.011  27.473  1.00 70.03  ? 25  HIS B ND1 1 
ATOM   2002 C CD2 . HIS B 1 26  ? 42.068  -4.934  27.495  1.00 60.87  ? 25  HIS B CD2 1 
ATOM   2003 C CE1 . HIS B 1 26  ? 43.831  -5.511  28.684  1.00 67.60  ? 25  HIS B CE1 1 
ATOM   2004 N NE2 . HIS B 1 26  ? 42.668  -4.839  28.719  1.00 63.56  ? 25  HIS B NE2 1 
ATOM   2005 N N   . LYS B 1 27  ? 44.776  -6.514  22.320  1.00 58.20  ? 26  LYS B N   1 
ATOM   2006 C CA  . LYS B 1 27  ? 44.827  -6.819  20.868  1.00 57.89  ? 26  LYS B CA  1 
ATOM   2007 C C   . LYS B 1 27  ? 44.067  -8.125  20.614  1.00 49.62  ? 26  LYS B C   1 
ATOM   2008 O O   . LYS B 1 27  ? 44.094  -9.019  21.435  1.00 46.35  ? 26  LYS B O   1 
ATOM   2009 C CB  . LYS B 1 27  ? 46.275  -6.861  20.369  1.00 63.95  ? 26  LYS B CB  1 
ATOM   2010 C CG  . LYS B 1 27  ? 47.094  -5.639  20.768  1.00 68.36  ? 26  LYS B CG  1 
ATOM   2011 C CD  . LYS B 1 27  ? 47.931  -5.034  19.664  1.00 79.77  ? 26  LYS B CD  1 
ATOM   2012 C CE  . LYS B 1 27  ? 48.429  -3.655  20.048  1.00 96.97  ? 26  LYS B CE  1 
ATOM   2013 N NZ  . LYS B 1 27  ? 49.533  -3.174  19.189  1.00 101.03 ? 26  LYS B NZ  1 
ATOM   2014 N N   . PHE B 1 28  ? 43.365  -8.218  19.499  1.00 47.98  ? 27  PHE B N   1 
ATOM   2015 C CA  . PHE B 1 28  ? 42.625  -9.443  19.139  1.00 39.73  ? 27  PHE B CA  1 
ATOM   2016 C C   . PHE B 1 28  ? 42.425  -9.364  17.648  1.00 35.09  ? 27  PHE B C   1 
ATOM   2017 O O   . PHE B 1 28  ? 42.430  -8.216  17.112  1.00 39.65  ? 27  PHE B O   1 
ATOM   2018 C CB  . PHE B 1 28  ? 41.303  -9.549  19.902  1.00 37.72  ? 27  PHE B CB  1 
ATOM   2019 C CG  . PHE B 1 28  ? 40.325  -8.412  19.680  1.00 38.37  ? 27  PHE B CG  1 
ATOM   2020 C CD1 . PHE B 1 28  ? 40.409  -7.262  20.424  1.00 34.90  ? 27  PHE B CD1 1 
ATOM   2021 C CD2 . PHE B 1 28  ? 39.275  -8.505  18.765  1.00 40.66  ? 27  PHE B CD2 1 
ATOM   2022 C CE1 . PHE B 1 28  ? 39.496  -6.233  20.272  1.00 42.33  ? 27  PHE B CE1 1 
ATOM   2023 C CE2 . PHE B 1 28  ? 38.345  -7.472  18.631  1.00 39.47  ? 27  PHE B CE2 1 
ATOM   2024 C CZ  . PHE B 1 28  ? 38.466  -6.333  19.372  1.00 39.21  ? 27  PHE B CZ  1 
ATOM   2025 N N   . SER B 1 29  ? 42.299  -10.530 17.013  1.00 38.58  ? 28  SER B N   1 
ATOM   2026 C CA  . SER B 1 29  ? 41.899  -10.657 15.609  1.00 40.85  ? 28  SER B CA  1 
ATOM   2027 C C   . SER B 1 29  ? 40.643  -11.551 15.499  1.00 40.39  ? 28  SER B C   1 
ATOM   2028 O O   . SER B 1 29  ? 40.476  -12.488 16.263  1.00 41.43  ? 28  SER B O   1 
ATOM   2029 C CB  . SER B 1 29  ? 43.057  -11.176 14.789  1.00 48.29  ? 28  SER B CB  1 
ATOM   2030 O OG  . SER B 1 29  ? 44.178  -10.352 15.036  1.00 43.76  ? 28  SER B OG  1 
ATOM   2031 N N   . VAL B 1 30  ? 39.799  -11.241 14.528  1.00 40.25  ? 29  VAL B N   1 
ATOM   2032 C CA  . VAL B 1 30  ? 38.592  -12.039 14.202  1.00 34.53  ? 29  VAL B CA  1 
ATOM   2033 C C   . VAL B 1 30  ? 38.653  -12.305 12.702  1.00 34.00  ? 29  VAL B C   1 
ATOM   2034 O O   . VAL B 1 30  ? 38.835  -11.351 11.960  1.00 35.57  ? 29  VAL B O   1 
ATOM   2035 C CB  . VAL B 1 30  ? 37.309  -11.282 14.595  1.00 36.69  ? 29  VAL B CB  1 
ATOM   2036 C CG1 . VAL B 1 30  ? 36.066  -11.997 14.061  1.00 34.91  ? 29  VAL B CG1 1 
ATOM   2037 C CG2 . VAL B 1 30  ? 37.227  -11.071 16.086  1.00 35.27  ? 29  VAL B CG2 1 
ATOM   2038 N N   . SER B 1 31  ? 38.450  -13.544 12.277  1.00 35.95  ? 30  SER B N   1 
ATOM   2039 C CA  . SER B 1 31  ? 38.268  -13.859 10.856  1.00 37.35  ? 30  SER B CA  1 
ATOM   2040 C C   . SER B 1 31  ? 36.868  -14.423 10.663  1.00 36.88  ? 30  SER B C   1 
ATOM   2041 O O   . SER B 1 31  ? 36.356  -15.158 11.560  1.00 37.18  ? 30  SER B O   1 
ATOM   2042 C CB  . SER B 1 31  ? 39.346  -14.810 10.346  1.00 41.17  ? 30  SER B CB  1 
ATOM   2043 O OG  . SER B 1 31  ? 39.189  -15.985 11.058  1.00 47.55  ? 30  SER B OG  1 
ATOM   2044 N N   . GLY B 1 32  ? 36.241  -14.003 9.584   1.00 36.27  ? 31  GLY B N   1 
ATOM   2045 C CA  . GLY B 1 32  ? 34.896  -14.457 9.180   1.00 36.72  ? 31  GLY B CA  1 
ATOM   2046 C C   . GLY B 1 32  ? 34.954  -15.065 7.823   1.00 35.99  ? 31  GLY B C   1 
ATOM   2047 O O   . GLY B 1 32  ? 35.786  -14.583 6.948   1.00 32.69  ? 31  GLY B O   1 
ATOM   2048 N N   . GLU B 1 33  ? 34.193  -16.129 7.627   1.00 34.48  ? 32  GLU B N   1 
ATOM   2049 C CA  . GLU B 1 33  ? 33.978  -16.696 6.277   1.00 35.57  ? 32  GLU B CA  1 
ATOM   2050 C C   . GLU B 1 33  ? 32.477  -16.977 6.106   1.00 35.27  ? 32  GLU B C   1 
ATOM   2051 O O   . GLU B 1 33  ? 31.784  -17.272 7.103   1.00 37.45  ? 32  GLU B O   1 
ATOM   2052 C CB  . GLU B 1 33  ? 34.793  -17.971 6.043   1.00 37.66  ? 32  GLU B CB  1 
ATOM   2053 C CG  . GLU B 1 33  ? 36.270  -17.907 6.368   1.00 40.22  ? 32  GLU B CG  1 
ATOM   2054 C CD  . GLU B 1 33  ? 37.031  -19.209 6.086   1.00 40.99  ? 32  GLU B CD  1 
ATOM   2055 O OE1 . GLU B 1 33  ? 36.485  -20.121 5.475   1.00 37.89  ? 32  GLU B OE1 1 
ATOM   2056 O OE2 . GLU B 1 33  ? 38.164  -19.317 6.493   1.00 40.20  ? 32  GLU B OE2 1 
ATOM   2057 N N   . GLY B 1 34  ? 31.997  -16.880 4.890   1.00 36.60  ? 33  GLY B N   1 
ATOM   2058 C CA  . GLY B 1 34  ? 30.650  -17.341 4.524   1.00 38.75  ? 33  GLY B CA  1 
ATOM   2059 C C   . GLY B 1 34  ? 30.312  -16.912 3.120   1.00 37.43  ? 33  GLY B C   1 
ATOM   2060 O O   . GLY B 1 34  ? 31.219  -16.773 2.291   1.00 32.97  ? 33  GLY B O   1 
ATOM   2061 N N   . GLU B 1 35  ? 29.033  -16.637 2.894   1.00 34.65  ? 34  GLU B N   1 
ATOM   2062 C CA  . GLU B 1 35  ? 28.458  -16.395 1.578   1.00 36.07  ? 34  GLU B CA  1 
ATOM   2063 C C   . GLU B 1 35  ? 27.407  -15.305 1.720   1.00 29.47  ? 34  GLU B C   1 
ATOM   2064 O O   . GLU B 1 35  ? 26.680  -15.324 2.732   1.00 33.51  ? 34  GLU B O   1 
ATOM   2065 C CB  . GLU B 1 35  ? 27.701  -17.650 1.118   1.00 44.88  ? 34  GLU B CB  1 
ATOM   2066 C CG  . GLU B 1 35  ? 28.526  -18.894 1.056   1.00 54.66  ? 34  GLU B CG  1 
ATOM   2067 C CD  . GLU B 1 35  ? 27.795  -19.974 0.276   1.00 53.72  ? 34  GLU B CD  1 
ATOM   2068 O OE1 . GLU B 1 35  ? 26.546  -20.112 0.438   1.00 56.94  ? 34  GLU B OE1 1 
ATOM   2069 O OE2 . GLU B 1 35  ? 28.458  -20.607 -0.542  1.00 75.59  ? 34  GLU B OE2 1 
ATOM   2070 N N   . GLY B 1 36  ? 27.321  -14.480 0.689   1.00 33.93  ? 35  GLY B N   1 
ATOM   2071 C CA  . GLY B 1 36  ? 26.319  -13.399 0.549   1.00 35.56  ? 35  GLY B CA  1 
ATOM   2072 C C   . GLY B 1 36  ? 25.480  -13.663 -0.694  1.00 34.03  ? 35  GLY B C   1 
ATOM   2073 O O   . GLY B 1 36  ? 26.053  -14.068 -1.743  1.00 34.46  ? 35  GLY B O   1 
ATOM   2074 N N   . ASP B 1 37  ? 24.158  -13.511 -0.552  1.00 36.30  ? 36  ASP B N   1 
ATOM   2075 C CA  . ASP B 1 37  ? 23.191  -13.694 -1.664  1.00 38.67  ? 36  ASP B CA  1 
ATOM   2076 C C   . ASP B 1 37  ? 22.255  -12.479 -1.646  1.00 32.82  ? 36  ASP B C   1 
ATOM   2077 O O   . ASP B 1 37  ? 21.169  -12.533 -1.022  1.00 33.15  ? 36  ASP B O   1 
ATOM   2078 C CB  . ASP B 1 37  ? 22.462  -15.030 -1.466  1.00 41.76  ? 36  ASP B CB  1 
ATOM   2079 C CG  . ASP B 1 37  ? 21.901  -15.688 -2.717  1.00 45.63  ? 36  ASP B CG  1 
ATOM   2080 O OD1 . ASP B 1 37  ? 22.031  -15.120 -3.787  1.00 39.70  ? 36  ASP B OD1 1 
ATOM   2081 O OD2 . ASP B 1 37  ? 21.360  -16.795 -2.573  1.00 45.86  ? 36  ASP B OD2 1 
ATOM   2082 N N   . ALA B 1 38  ? 22.693  -11.385 -2.248  1.00 34.21  ? 37  ALA B N   1 
ATOM   2083 C CA  . ALA B 1 38  ? 22.011  -10.067 -2.140  1.00 37.01  ? 37  ALA B CA  1 
ATOM   2084 C C   . ALA B 1 38  ? 20.607  -10.126 -2.762  1.00 34.07  ? 37  ALA B C   1 
ATOM   2085 O O   . ALA B 1 38  ? 19.763  -9.327  -2.384  1.00 34.28  ? 37  ALA B O   1 
ATOM   2086 C CB  . ALA B 1 38  ? 22.810  -9.011  -2.883  1.00 32.37  ? 37  ALA B CB  1 
ATOM   2087 N N   . THR B 1 39  ? 20.411  -11.019 -3.725  1.00 36.85  ? 38  THR B N   1 
ATOM   2088 C CA  . THR B 1 39  ? 19.079  -11.276 -4.335  1.00 37.59  ? 38  THR B CA  1 
ATOM   2089 C C   . THR B 1 39  ? 18.063  -11.461 -3.199  1.00 42.90  ? 38  THR B C   1 
ATOM   2090 O O   . THR B 1 39  ? 16.946  -10.979 -3.324  1.00 36.69  ? 38  THR B O   1 
ATOM   2091 C CB  . THR B 1 39  ? 19.100  -12.481 -5.272  1.00 38.03  ? 38  THR B CB  1 
ATOM   2092 O OG1 . THR B 1 39  ? 20.120  -12.293 -6.257  1.00 36.78  ? 38  THR B OG1 1 
ATOM   2093 C CG2 . THR B 1 39  ? 17.754  -12.666 -5.945  1.00 47.64  ? 38  THR B CG2 1 
ATOM   2094 N N   . TYR B 1 40  ? 18.457  -12.045 -2.073  1.00 38.87  ? 39  TYR B N   1 
ATOM   2095 C CA  . TYR B 1 40  ? 17.565  -12.364 -0.937  1.00 38.65  ? 39  TYR B CA  1 
ATOM   2096 C C   . TYR B 1 40  ? 17.958  -11.537 0.289   1.00 35.27  ? 39  TYR B C   1 
ATOM   2097 O O   . TYR B 1 40  ? 17.420  -11.750 1.385   1.00 38.18  ? 39  TYR B O   1 
ATOM   2098 C CB  . TYR B 1 40  ? 17.577  -13.881 -0.673  1.00 39.67  ? 39  TYR B CB  1 
ATOM   2099 C CG  . TYR B 1 40  ? 17.366  -14.690 -1.925  1.00 43.33  ? 39  TYR B CG  1 
ATOM   2100 C CD1 . TYR B 1 40  ? 16.095  -14.896 -2.450  1.00 43.03  ? 39  TYR B CD1 1 
ATOM   2101 C CD2 . TYR B 1 40  ? 18.442  -15.192 -2.646  1.00 44.36  ? 39  TYR B CD2 1 
ATOM   2102 C CE1 . TYR B 1 40  ? 15.914  -15.615 -3.622  1.00 42.31  ? 39  TYR B CE1 1 
ATOM   2103 C CE2 . TYR B 1 40  ? 18.279  -15.886 -3.837  1.00 43.82  ? 39  TYR B CE2 1 
ATOM   2104 C CZ  . TYR B 1 40  ? 16.999  -16.137 -4.314  1.00 47.28  ? 39  TYR B CZ  1 
ATOM   2105 O OH  . TYR B 1 40  ? 16.824  -16.809 -5.506  1.00 42.87  ? 39  TYR B OH  1 
ATOM   2106 N N   . GLY B 1 41  ? 18.872  -10.582 0.112   1.00 36.42  ? 40  GLY B N   1 
ATOM   2107 C CA  . GLY B 1 41  ? 19.488  -9.823  1.220   1.00 34.02  ? 40  GLY B CA  1 
ATOM   2108 C C   . GLY B 1 41  ? 20.175  -10.697 2.277   1.00 32.21  ? 40  GLY B C   1 
ATOM   2109 O O   . GLY B 1 41  ? 20.231  -10.290 3.465   1.00 35.54  ? 40  GLY B O   1 
ATOM   2110 N N   . LYS B 1 42  ? 20.730  -11.824 1.855   1.00 35.68  ? 41  LYS B N   1 
ATOM   2111 C CA  . LYS B 1 42  ? 21.086  -12.883 2.813   1.00 38.49  ? 41  LYS B CA  1 
ATOM   2112 C C   . LYS B 1 42  ? 22.607  -12.959 2.992   1.00 33.30  ? 41  LYS B C   1 
ATOM   2113 O O   . LYS B 1 42  ? 23.356  -13.021 2.031   1.00 37.53  ? 41  LYS B O   1 
ATOM   2114 C CB  . LYS B 1 42  ? 20.567  -14.231 2.324   1.00 37.85  ? 41  LYS B CB  1 
ATOM   2115 C CG  . LYS B 1 42  ? 20.886  -15.399 3.247   1.00 36.37  ? 41  LYS B CG  1 
ATOM   2116 C CD  . LYS B 1 42  ? 20.658  -16.730 2.564   1.00 46.40  ? 41  LYS B CD  1 
ATOM   2117 C CE  . LYS B 1 42  ? 20.586  -17.896 3.530   1.00 47.94  ? 41  LYS B CE  1 
ATOM   2118 N NZ  . LYS B 1 42  ? 19.694  -18.956 2.992   1.00 54.55  ? 41  LYS B NZ  1 
ATOM   2119 N N   . MET B 1 43  ? 23.024  -13.038 4.231   1.00 32.84  ? 42  MET B N   1 
ATOM   2120 C CA  . MET B 1 43  ? 24.417  -13.438 4.566   1.00 32.49  ? 42  MET B CA  1 
ATOM   2121 C C   . MET B 1 43  ? 24.411  -14.587 5.555   1.00 29.08  ? 42  MET B C   1 
ATOM   2122 O O   . MET B 1 43  ? 23.721  -14.509 6.571   1.00 33.35  ? 42  MET B O   1 
ATOM   2123 C CB  . MET B 1 43  ? 25.195  -12.255 5.162   1.00 30.71  ? 42  MET B CB  1 
ATOM   2124 C CG  . MET B 1 43  ? 25.463  -11.176 4.118   1.00 37.33  ? 42  MET B CG  1 
ATOM   2125 S SD  . MET B 1 43  ? 26.213  -9.708  4.788   1.00 35.75  ? 42  MET B SD  1 
ATOM   2126 C CE  . MET B 1 43  ? 24.944  -9.109  5.888   1.00 42.67  ? 42  MET B CE  1 
ATOM   2127 N N   . SER B 1 44  ? 25.291  -15.544 5.344   1.00 34.02  ? 43  SER B N   1 
ATOM   2128 C CA  . SER B 1 44  ? 25.580  -16.547 6.390   1.00 34.93  ? 43  SER B CA  1 
ATOM   2129 C C   . SER B 1 44  ? 27.086  -16.622 6.622   1.00 32.12  ? 43  SER B C   1 
ATOM   2130 O O   . SER B 1 44  ? 27.802  -16.847 5.652   1.00 36.87  ? 43  SER B O   1 
ATOM   2131 C CB  . SER B 1 44  ? 24.970  -17.883 6.062   1.00 42.90  ? 43  SER B CB  1 
ATOM   2132 O OG  . SER B 1 44  ? 25.448  -18.364 4.867   1.00 58.02  ? 43  SER B OG  1 
ATOM   2133 N N   . LEU B 1 45  ? 27.476  -16.469 7.890   1.00 36.09  ? 44  LEU B N   1 
ATOM   2134 C CA  . LEU B 1 45  ? 28.837  -16.107 8.323   1.00 36.83  ? 44  LEU B CA  1 
ATOM   2135 C C   . LEU B 1 45  ? 29.179  -16.878 9.572   1.00 37.76  ? 44  LEU B C   1 
ATOM   2136 O O   . LEU B 1 45  ? 28.304  -16.995 10.467  1.00 33.58  ? 44  LEU B O   1 
ATOM   2137 C CB  . LEU B 1 45  ? 28.877  -14.619 8.622   1.00 34.54  ? 44  LEU B CB  1 
ATOM   2138 C CG  . LEU B 1 45  ? 28.609  -13.744 7.412   1.00 38.28  ? 44  LEU B CG  1 
ATOM   2139 C CD1 . LEU B 1 45  ? 28.154  -12.368 7.817   1.00 37.81  ? 44  LEU B CD1 1 
ATOM   2140 C CD2 . LEU B 1 45  ? 29.835  -13.740 6.540   1.00 43.98  ? 44  LEU B CD2 1 
ATOM   2141 N N   . LYS B 1 46  ? 30.426  -17.327 9.660   1.00 32.52  ? 45  LYS B N   1 
ATOM   2142 C CA  . LYS B 1 46  ? 30.976  -17.811 10.961  1.00 30.14  ? 45  LYS B CA  1 
ATOM   2143 C C   . LYS B 1 46  ? 32.238  -17.001 11.266  1.00 29.37  ? 45  LYS B C   1 
ATOM   2144 O O   . LYS B 1 46  ? 33.121  -16.945 10.358  1.00 37.16  ? 45  LYS B O   1 
ATOM   2145 C CB  . LYS B 1 46  ? 31.421  -19.272 10.857  1.00 34.50  ? 45  LYS B CB  1 
ATOM   2146 C CG  . LYS B 1 46  ? 32.131  -19.808 12.103  1.00 35.59  ? 45  LYS B CG  1 
ATOM   2147 C CD  . LYS B 1 46  ? 32.423  -21.315 11.999  1.00 38.90  ? 45  LYS B CD  1 
ATOM   2148 C CE  . LYS B 1 46  ? 33.185  -21.775 13.212  1.00 38.23  ? 45  LYS B CE  1 
ATOM   2149 N NZ  . LYS B 1 46  ? 33.517  -23.199 13.097  1.00 42.20  ? 45  LYS B NZ  1 
ATOM   2150 N N   . PHE B 1 47  ? 32.285  -16.424 12.443  1.00 30.14  ? 46  PHE B N   1 
ATOM   2151 C CA  . PHE B 1 47  ? 33.363  -15.553 12.935  1.00 31.52  ? 46  PHE B CA  1 
ATOM   2152 C C   . PHE B 1 47  ? 34.126  -16.323 14.002  1.00 40.48  ? 46  PHE B C   1 
ATOM   2153 O O   . PHE B 1 47  ? 33.513  -16.998 14.813  1.00 35.13  ? 46  PHE B O   1 
ATOM   2154 C CB  . PHE B 1 47  ? 32.806  -14.246 13.439  1.00 34.47  ? 46  PHE B CB  1 
ATOM   2155 C CG  . PHE B 1 47  ? 32.189  -13.385 12.366  1.00 35.35  ? 46  PHE B CG  1 
ATOM   2156 C CD1 . PHE B 1 47  ? 32.994  -12.614 11.540  1.00 35.97  ? 46  PHE B CD1 1 
ATOM   2157 C CD2 . PHE B 1 47  ? 30.819  -13.380 12.153  1.00 33.12  ? 46  PHE B CD2 1 
ATOM   2158 C CE1 . PHE B 1 47  ? 32.431  -11.843 10.534  1.00 33.15  ? 46  PHE B CE1 1 
ATOM   2159 C CE2 . PHE B 1 47  ? 30.262  -12.587 11.160  1.00 34.97  ? 46  PHE B CE2 1 
ATOM   2160 C CZ  . PHE B 1 47  ? 31.057  -11.829 10.355  1.00 34.18  ? 46  PHE B CZ  1 
ATOM   2161 N N   . ILE B 1 48  ? 35.448  -16.218 13.975  1.00 36.78  ? 47  ILE B N   1 
ATOM   2162 C CA  . ILE B 1 48  ? 36.346  -16.945 14.912  1.00 35.56  ? 47  ILE B CA  1 
ATOM   2163 C C   . ILE B 1 48  ? 37.298  -15.916 15.476  1.00 37.31  ? 47  ILE B C   1 
ATOM   2164 O O   . ILE B 1 48  ? 37.831  -15.139 14.673  1.00 37.30  ? 47  ILE B O   1 
ATOM   2165 C CB  . ILE B 1 48  ? 37.126  -18.064 14.211  1.00 39.89  ? 47  ILE B CB  1 
ATOM   2166 C CG1 . ILE B 1 48  ? 36.208  -19.068 13.523  1.00 44.45  ? 47  ILE B CG1 1 
ATOM   2167 C CG2 . ILE B 1 48  ? 38.074  -18.732 15.199  1.00 43.66  ? 47  ILE B CG2 1 
ATOM   2168 C CD1 . ILE B 1 48  ? 36.917  -20.003 12.564  1.00 46.67  ? 47  ILE B CD1 1 
ATOM   2169 N N   . CYS B 1 49  ? 37.442  -15.850 16.789  1.00 36.74  ? 48  CYS B N   1 
ATOM   2170 C CA  . CYS B 1 49  ? 38.562  -15.090 17.406  1.00 44.03  ? 48  CYS B CA  1 
ATOM   2171 C C   . CYS B 1 49  ? 39.836  -15.951 17.312  1.00 42.06  ? 48  CYS B C   1 
ATOM   2172 O O   . CYS B 1 49  ? 39.896  -17.004 17.928  1.00 42.61  ? 48  CYS B O   1 
ATOM   2173 C CB  . CYS B 1 49  ? 38.274  -14.686 18.836  1.00 43.44  ? 48  CYS B CB  1 
ATOM   2174 S SG  . CYS B 1 49  ? 39.666  -13.806 19.571  1.00 40.90  ? 48  CYS B SG  1 
ATOM   2175 N N   . THR B 1 50  ? 40.763  -15.535 16.464  1.00 40.67  ? 49  THR B N   1 
ATOM   2176 C CA  . THR B 1 50  ? 41.961  -16.341 16.081  1.00 43.93  ? 49  THR B CA  1 
ATOM   2177 C C   . THR B 1 50  ? 43.050  -16.150 17.147  1.00 48.71  ? 49  THR B C   1 
ATOM   2178 O O   . THR B 1 50  ? 43.984  -16.914 17.136  1.00 53.62  ? 49  THR B O   1 
ATOM   2179 C CB  . THR B 1 50  ? 42.506  -15.980 14.677  1.00 44.29  ? 49  THR B CB  1 
ATOM   2180 O OG1 . THR B 1 50  ? 42.887  -14.609 14.747  1.00 44.83  ? 49  THR B OG1 1 
ATOM   2181 C CG2 . THR B 1 50  ? 41.532  -16.126 13.537  1.00 51.29  ? 49  THR B CG2 1 
ATOM   2182 N N   . THR B 1 51  ? 42.941  -15.170 18.052  1.00 46.55  ? 50  THR B N   1 
ATOM   2183 C CA  . THR B 1 51  ? 44.009  -14.851 19.018  1.00 52.18  ? 50  THR B CA  1 
ATOM   2184 C C   . THR B 1 51  ? 43.698  -15.376 20.413  1.00 45.17  ? 50  THR B C   1 
ATOM   2185 O O   . THR B 1 51  ? 44.301  -14.816 21.328  1.00 44.69  ? 50  THR B O   1 
ATOM   2186 C CB  . THR B 1 51  ? 44.211  -13.342 19.104  1.00 50.44  ? 50  THR B CB  1 
ATOM   2187 O OG1 . THR B 1 51  ? 42.930  -12.725 19.362  1.00 47.30  ? 50  THR B OG1 1 
ATOM   2188 C CG2 . THR B 1 51  ? 44.854  -12.875 17.825  1.00 45.89  ? 50  THR B CG2 1 
ATOM   2189 N N   . GLY B 1 52  ? 42.742  -16.301 20.585  1.00 47.53  ? 51  GLY B N   1 
ATOM   2190 C CA  . GLY B 1 52  ? 42.278  -16.742 21.919  1.00 50.32  ? 51  GLY B CA  1 
ATOM   2191 C C   . GLY B 1 52  ? 40.881  -16.235 22.299  1.00 60.26  ? 51  GLY B C   1 
ATOM   2192 O O   . GLY B 1 52  ? 39.921  -16.378 21.498  1.00 50.02  ? 51  GLY B O   1 
ATOM   2193 N N   . LYS B 1 53  ? 40.738  -15.751 23.534  1.00 51.08  ? 52  LYS B N   1 
ATOM   2194 C CA  . LYS B 1 53  ? 39.453  -15.301 24.113  1.00 56.26  ? 52  LYS B CA  1 
ATOM   2195 C C   . LYS B 1 53  ? 39.185  -13.903 23.562  1.00 46.75  ? 52  LYS B C   1 
ATOM   2196 O O   . LYS B 1 53  ? 40.109  -13.085 23.492  1.00 48.61  ? 52  LYS B O   1 
ATOM   2197 C CB  . LYS B 1 53  ? 39.485  -15.339 25.646  1.00 60.50  ? 52  LYS B CB  1 
ATOM   2198 C CG  . LYS B 1 53  ? 39.230  -16.703 26.283  1.00 79.53  ? 52  LYS B CG  1 
ATOM   2199 C CD  . LYS B 1 53  ? 37.861  -17.315 25.993  1.00 88.72  ? 52  LYS B CD  1 
ATOM   2200 C CE  . LYS B 1 53  ? 37.912  -18.452 24.991  1.00 91.40  ? 52  LYS B CE  1 
ATOM   2201 N NZ  . LYS B 1 53  ? 36.552  -18.957 24.686  1.00 106.90 ? 52  LYS B NZ  1 
ATOM   2202 N N   . LEU B 1 54  ? 37.989  -13.658 23.054  1.00 44.32  ? 53  LEU B N   1 
ATOM   2203 C CA  . LEU B 1 54  ? 37.607  -12.292 22.627  1.00 42.55  ? 53  LEU B CA  1 
ATOM   2204 C C   . LEU B 1 54  ? 37.485  -11.418 23.858  1.00 42.68  ? 53  LEU B C   1 
ATOM   2205 O O   . LEU B 1 54  ? 36.756  -11.803 24.769  1.00 45.13  ? 53  LEU B O   1 
ATOM   2206 C CB  . LEU B 1 54  ? 36.278  -12.376 21.897  1.00 44.71  ? 53  LEU B CB  1 
ATOM   2207 C CG  . LEU B 1 54  ? 35.906  -11.123 21.139  1.00 42.41  ? 53  LEU B CG  1 
ATOM   2208 C CD1 . LEU B 1 54  ? 36.894  -10.869 20.032  1.00 40.62  ? 53  LEU B CD1 1 
ATOM   2209 C CD2 . LEU B 1 54  ? 34.481  -11.265 20.596  1.00 42.79  ? 53  LEU B CD2 1 
ATOM   2210 N N   . PRO B 1 55  ? 38.216  -10.281 23.974  1.00 45.69  ? 54  PRO B N   1 
ATOM   2211 C CA  . PRO B 1 55  ? 38.207  -9.486  25.204  1.00 45.82  ? 54  PRO B CA  1 
ATOM   2212 C C   . PRO B 1 55  ? 37.047  -8.498  25.310  1.00 48.69  ? 54  PRO B C   1 
ATOM   2213 O O   . PRO B 1 55  ? 36.969  -7.804  26.280  1.00 43.57  ? 54  PRO B O   1 
ATOM   2214 C CB  . PRO B 1 55  ? 39.568  -8.765  25.156  1.00 51.69  ? 54  PRO B CB  1 
ATOM   2215 C CG  . PRO B 1 55  ? 39.807  -8.539  23.679  1.00 50.90  ? 54  PRO B CG  1 
ATOM   2216 C CD  . PRO B 1 55  ? 39.198  -9.765  23.016  1.00 52.61  ? 54  PRO B CD  1 
ATOM   2217 N N   . VAL B 1 56  ? 36.176  -8.449  24.303  1.00 43.68  ? 55  VAL B N   1 
ATOM   2218 C CA  . VAL B 1 56  ? 34.893  -7.700  24.359  1.00 36.80  ? 55  VAL B CA  1 
ATOM   2219 C C   . VAL B 1 56  ? 33.781  -8.705  24.016  1.00 39.08  ? 55  VAL B C   1 
ATOM   2220 O O   . VAL B 1 56  ? 34.002  -9.782  23.453  1.00 37.67  ? 55  VAL B O   1 
ATOM   2221 C CB  . VAL B 1 56  ? 34.897  -6.483  23.413  1.00 39.23  ? 55  VAL B CB  1 
ATOM   2222 C CG1 . VAL B 1 56  ? 35.938  -5.409  23.722  1.00 45.86  ? 55  VAL B CG1 1 
ATOM   2223 C CG2 . VAL B 1 56  ? 35.059  -6.862  21.936  1.00 42.57  ? 55  VAL B CG2 1 
ATOM   2224 N N   . PRO B 1 57  ? 32.514  -8.365  24.268  1.00 37.68  ? 56  PRO B N   1 
ATOM   2225 C CA  . PRO B 1 57  ? 31.402  -9.240  23.891  1.00 35.04  ? 56  PRO B CA  1 
ATOM   2226 C C   . PRO B 1 57  ? 31.144  -9.246  22.374  1.00 30.19  ? 56  PRO B C   1 
ATOM   2227 O O   . PRO B 1 57  ? 31.159  -8.170  21.739  1.00 32.62  ? 56  PRO B O   1 
ATOM   2228 C CB  . PRO B 1 57  ? 30.223  -8.571  24.638  1.00 37.29  ? 56  PRO B CB  1 
ATOM   2229 C CG  . PRO B 1 57  ? 30.905  -7.753  25.707  1.00 39.00  ? 56  PRO B CG  1 
ATOM   2230 C CD  . PRO B 1 57  ? 32.064  -7.139  24.921  1.00 36.02  ? 56  PRO B CD  1 
ATOM   2231 N N   . TRP B 1 58  ? 30.892  -10.422 21.837  1.00 33.82  ? 57  TRP B N   1 
ATOM   2232 C CA  . TRP B 1 58  ? 30.563  -10.590 20.396  1.00 34.67  ? 57  TRP B CA  1 
ATOM   2233 C C   . TRP B 1 58  ? 29.502  -9.590  19.980  1.00 38.69  ? 57  TRP B C   1 
ATOM   2234 O O   . TRP B 1 58  ? 29.590  -8.974  18.890  1.00 35.95  ? 57  TRP B O   1 
ATOM   2235 C CB  . TRP B 1 58  ? 30.126  -12.010 20.103  1.00 35.58  ? 57  TRP B CB  1 
ATOM   2236 C CG  . TRP B 1 58  ? 31.258  -12.972 19.945  1.00 39.10  ? 57  TRP B CG  1 
ATOM   2237 C CD1 . TRP B 1 58  ? 31.593  -13.954 20.825  1.00 38.59  ? 57  TRP B CD1 1 
ATOM   2238 C CD2 . TRP B 1 58  ? 32.197  -13.061 18.851  1.00 38.96  ? 57  TRP B CD2 1 
ATOM   2239 N NE1 . TRP B 1 58  ? 32.669  -14.663 20.351  1.00 42.50  ? 57  TRP B NE1 1 
ATOM   2240 C CE2 . TRP B 1 58  ? 33.059  -14.136 19.144  1.00 39.44  ? 57  TRP B CE2 1 
ATOM   2241 C CE3 . TRP B 1 58  ? 32.435  -12.309 17.694  1.00 35.07  ? 57  TRP B CE3 1 
ATOM   2242 C CZ2 . TRP B 1 58  ? 34.112  -14.494 18.313  1.00 39.46  ? 57  TRP B CZ2 1 
ATOM   2243 C CZ3 . TRP B 1 58  ? 33.471  -12.668 16.864  1.00 38.27  ? 57  TRP B CZ3 1 
ATOM   2244 C CH2 . TRP B 1 58  ? 34.294  -13.757 17.162  1.00 41.02  ? 57  TRP B CH2 1 
ATOM   2245 N N   . PRO B 1 59  ? 28.409  -9.420  20.769  1.00 36.53  ? 58  PRO B N   1 
ATOM   2246 C CA  . PRO B 1 59  ? 27.359  -8.519  20.313  1.00 36.41  ? 58  PRO B CA  1 
ATOM   2247 C C   . PRO B 1 59  ? 27.844  -7.119  19.948  1.00 35.21  ? 58  PRO B C   1 
ATOM   2248 O O   . PRO B 1 59  ? 27.201  -6.503  19.154  1.00 34.02  ? 58  PRO B O   1 
ATOM   2249 C CB  . PRO B 1 59  ? 26.342  -8.538  21.480  1.00 39.39  ? 58  PRO B CB  1 
ATOM   2250 C CG  . PRO B 1 59  ? 26.524  -9.920  22.054  1.00 39.33  ? 58  PRO B CG  1 
ATOM   2251 C CD  . PRO B 1 59  ? 28.015  -10.210 21.957  1.00 35.19  ? 58  PRO B CD  1 
ATOM   2252 N N   . THR B 1 60  ? 28.897  -6.627  20.592  1.00 33.73  ? 59  THR B N   1 
ATOM   2253 C CA  . THR B 1 60  ? 29.375  -5.250  20.381  1.00 36.06  ? 59  THR B CA  1 
ATOM   2254 C C   . THR B 1 60  ? 30.118  -5.113  19.041  1.00 30.07  ? 59  THR B C   1 
ATOM   2255 O O   . THR B 1 60  ? 30.285  -3.939  18.620  1.00 32.70  ? 59  THR B O   1 
ATOM   2256 C CB  . THR B 1 60  ? 30.280  -4.723  21.500  1.00 34.40  ? 59  THR B CB  1 
ATOM   2257 O OG1 . THR B 1 60  ? 31.492  -5.471  21.518  1.00 35.64  ? 59  THR B OG1 1 
ATOM   2258 C CG2 . THR B 1 60  ? 29.575  -4.758  22.840  1.00 38.31  ? 59  THR B CG2 1 
ATOM   2259 N N   . LEU B 1 61  ? 30.489  -6.225  18.433  1.00 34.01  ? 60  LEU B N   1 
ATOM   2260 C CA  . LEU B 1 61  ? 31.233  -6.252  17.154  1.00 34.15  ? 60  LEU B CA  1 
ATOM   2261 C C   . LEU B 1 61  ? 30.304  -6.516  15.978  1.00 38.86  ? 60  LEU B C   1 
ATOM   2262 O O   . LEU B 1 61  ? 30.843  -6.517  14.867  1.00 32.35  ? 60  LEU B O   1 
ATOM   2263 C CB  . LEU B 1 61  ? 32.309  -7.357  17.211  1.00 34.55  ? 60  LEU B CB  1 
ATOM   2264 C CG  . LEU B 1 61  ? 33.443  -7.165  18.212  1.00 34.29  ? 60  LEU B CG  1 
ATOM   2265 C CD1 . LEU B 1 61  ? 34.445  -8.284  18.071  1.00 35.13  ? 60  LEU B CD1 1 
ATOM   2266 C CD2 . LEU B 1 61  ? 34.119  -5.830  18.056  1.00 34.27  ? 60  LEU B CD2 1 
ATOM   2267 N N   . LYS B 1 62  ? 29.036  -6.875  16.180  1.00 34.36  ? 61  LYS B N   1 
ATOM   2268 C CA  . LYS B 1 62  ? 28.197  -7.379  15.063  1.00 35.11  ? 61  LYS B CA  1 
ATOM   2269 C C   . LYS B 1 62  ? 28.039  -6.308  13.977  1.00 30.53  ? 61  LYS B C   1 
ATOM   2270 O O   . LYS B 1 62  ? 28.179  -6.687  12.795  1.00 30.47  ? 61  LYS B O   1 
ATOM   2271 C CB  . LYS B 1 62  ? 26.808  -7.814  15.525  1.00 35.28  ? 61  LYS B CB  1 
ATOM   2272 C CG  . LYS B 1 62  ? 26.810  -9.181  16.201  1.00 41.65  ? 61  LYS B CG  1 
ATOM   2273 C CD  . LYS B 1 62  ? 25.463  -9.422  16.844  1.00 56.46  ? 61  LYS B CD  1 
ATOM   2274 C CE  . LYS B 1 62  ? 25.457  -10.509 17.896  1.00 68.27  ? 61  LYS B CE  1 
ATOM   2275 N NZ  . LYS B 1 62  ? 24.242  -10.369 18.750  1.00 80.43  ? 61  LYS B NZ  1 
ATOM   2276 N N   . THR B 1 63  ? 27.734  -5.056  14.320  1.00 31.47  ? 62  THR B N   1 
ATOM   2277 C CA  . THR B 1 63  ? 27.554  -4.012  13.287  1.00 30.42  ? 62  THR B CA  1 
ATOM   2278 C C   . THR B 1 63  ? 28.877  -3.709  12.546  1.00 32.31  ? 62  THR B C   1 
ATOM   2279 O O   . THR B 1 63  ? 28.791  -3.327  11.375  1.00 29.73  ? 62  THR B O   1 
ATOM   2280 C CB  . THR B 1 63  ? 27.021  -2.702  13.878  1.00 28.98  ? 62  THR B CB  1 
ATOM   2281 O OG1 . THR B 1 63  ? 27.895  -2.328  14.946  1.00 32.87  ? 62  THR B OG1 1 
ATOM   2282 C CG2 . THR B 1 63  ? 25.586  -2.831  14.362  1.00 34.82  ? 62  THR B CG2 1 
ATOM   2283 N N   . THR B 1 64  ? 30.027  -3.875  13.191  1.00 30.63  ? 63  THR B N   1 
ATOM   2284 C CA  . THR B 1 64  ? 31.351  -3.653  12.547  1.00 34.62  ? 63  THR B CA  1 
ATOM   2285 C C   . THR B 1 64  ? 31.664  -4.808  11.580  1.00 31.77  ? 63  THR B C   1 
ATOM   2286 O O   . THR B 1 64  ? 32.154  -4.557  10.491  1.00 32.05  ? 63  THR B O   1 
ATOM   2287 C CB  . THR B 1 64  ? 32.442  -3.528  13.604  1.00 31.01  ? 63  THR B CB  1 
ATOM   2288 O OG1 . THR B 1 64  ? 32.075  -2.428  14.449  1.00 34.24  ? 63  THR B OG1 1 
ATOM   2289 C CG2 . THR B 1 64  ? 33.800  -3.336  12.970  1.00 36.19  ? 63  THR B CG2 1 
ATOM   2290 N N   . LEU B 1 65  ? 31.338  -6.028  11.931  1.00 31.52  ? 64  LEU B N   1 
ATOM   2291 C CA  . LEU B 1 65  ? 31.766  -7.228  11.185  1.00 32.97  ? 64  LEU B CA  1 
ATOM   2292 C C   . LEU B 1 65  ? 30.832  -7.469  10.016  1.00 32.22  ? 64  LEU B C   1 
ATOM   2293 O O   . LEU B 1 65  ? 31.118  -7.672  8.865   1.00 32.84  ? 64  LEU B O   1 
ATOM   2294 C CB  . LEU B 1 65  ? 31.676  -8.419  12.120  1.00 30.16  ? 64  LEU B CB  1 
ATOM   2295 C CG  . LEU B 1 65  ? 32.774  -8.591  13.126  1.00 30.21  ? 64  LEU B CG  1 
ATOM   2296 C CD1 . LEU B 1 65  ? 32.319  -9.695  14.092  1.00 30.55  ? 64  LEU B CD1 1 
ATOM   2297 C CD2 . LEU B 1 65  ? 34.073  -8.971  12.451  1.00 33.63  ? 64  LEU B CD2 1 
HETATM 2298 N N1  . CRF B 1 66  ? 29.290  -6.862  10.079  1.00 28.98  ? 65  CRF B N1  1 
HETATM 2299 C CA1 . CRF B 1 66  ? 28.273  -6.993  9.127   1.00 32.32  ? 65  CRF B CA1 1 
HETATM 2300 C CB1 . CRF B 1 66  ? 27.278  -8.156  9.379   1.00 35.75  ? 65  CRF B CB1 1 
HETATM 2301 C CG1 . CRF B 1 66  ? 28.108  -9.358  9.545   1.00 38.04  ? 65  CRF B CG1 1 
HETATM 2302 O OG1 . CRF B 1 66  ? 26.690  -8.155  10.676  1.00 44.01  ? 65  CRF B OG1 1 
HETATM 2303 C C1  . CRF B 1 66  ? 27.632  -5.676  9.226   1.00 31.47  ? 65  CRF B C1  1 
HETATM 2304 N N2  . CRF B 1 66  ? 26.464  -5.389  9.829   1.00 33.77  ? 65  CRF B N2  1 
HETATM 2305 N N3  . CRF B 1 66  ? 28.196  -4.581  8.614   1.00 33.57  ? 65  CRF B N3  1 
HETATM 2306 C C2  . CRF B 1 66  ? 27.384  -3.558  8.889   1.00 33.92  ? 65  CRF B C2  1 
HETATM 2307 O O2  . CRF B 1 66  ? 27.500  -2.372  8.522   1.00 36.95  ? 65  CRF B O2  1 
HETATM 2308 C CA2 . CRF B 1 66  ? 26.268  -4.051  9.679   1.00 33.11  ? 65  CRF B CA2 1 
HETATM 2309 C CA3 . CRF B 1 66  ? 29.501  -4.628  7.860   1.00 32.04  ? 65  CRF B CA3 1 
HETATM 2310 C C3  . CRF B 1 66  ? 29.644  -4.530  6.375   1.00 33.43  ? 65  CRF B C3  1 
HETATM 2311 O O3  . CRF B 1 66  ? 30.628  -3.856  5.941   1.00 39.45  ? 65  CRF B O3  1 
HETATM 2312 C CB2 . CRF B 1 66  ? 25.112  -3.273  10.192  1.00 37.78  ? 65  CRF B CB2 1 
HETATM 2313 C CG2 . CRF B 1 66  ? 24.092  -3.871  11.021  1.00 37.63  ? 65  CRF B CG2 1 
HETATM 2314 C CD1 . CRF B 1 66  ? 24.105  -5.170  11.582  1.00 45.65  ? 65  CRF B CD1 1 
HETATM 2315 C CD2 . CRF B 1 66  ? 23.007  -3.065  11.610  1.00 36.51  ? 65  CRF B CD2 1 
HETATM 2316 C CE2 . CRF B 1 66  ? 22.307  -4.062  12.453  1.00 42.87  ? 65  CRF B CE2 1 
HETATM 2317 N NE1 . CRF B 1 66  ? 22.993  -5.247  12.413  1.00 42.11  ? 65  CRF B NE1 1 
HETATM 2318 C CE3 . CRF B 1 66  ? 22.571  -1.808  11.461  1.00 36.87  ? 65  CRF B CE3 1 
HETATM 2319 C CZ2 . CRF B 1 66  ? 21.132  -3.639  13.097  1.00 43.53  ? 65  CRF B CZ2 1 
HETATM 2320 C CZ3 . CRF B 1 66  ? 21.406  -1.423  12.158  1.00 36.79  ? 65  CRF B CZ3 1 
HETATM 2321 C CH2 . CRF B 1 66  ? 20.683  -2.317  12.905  1.00 38.94  ? 65  CRF B CH2 1 
ATOM   2322 N N   . MET B 1 67  ? 28.571  -5.168  5.876   1.00 32.72  ? 68  MET B N   1 
ATOM   2323 C CA  . MET B 1 67  ? 28.651  -5.451  4.402   1.00 30.39  ? 68  MET B CA  1 
ATOM   2324 C C   . MET B 1 67  ? 27.263  -5.136  3.821   1.00 33.59  ? 68  MET B C   1 
ATOM   2325 O O   . MET B 1 67  ? 26.537  -6.033  3.425   1.00 31.56  ? 68  MET B O   1 
ATOM   2326 C CB  . MET B 1 67  ? 29.131  -6.876  4.155   1.00 34.15  ? 68  MET B CB  1 
ATOM   2327 C CG  . MET B 1 67  ? 30.525  -7.123  4.697   1.00 33.57  ? 68  MET B CG  1 
ATOM   2328 S SD  . MET B 1 67  ? 30.986  -8.794  4.558   1.00 34.85  ? 68  MET B SD  1 
ATOM   2329 C CE  . MET B 1 67  ? 30.237  -9.531  6.018   1.00 37.26  ? 68  MET B CE  1 
ATOM   2330 N N   . GLN B 1 68  ? 26.891  -3.858  3.837   1.00 35.23  ? 69  GLN B N   1 
ATOM   2331 C CA  . GLN B 1 68  ? 25.516  -3.413  3.463   1.00 30.46  ? 69  GLN B CA  1 
ATOM   2332 C C   . GLN B 1 68  ? 25.348  -3.558  1.947   1.00 32.07  ? 69  GLN B C   1 
ATOM   2333 O O   . GLN B 1 68  ? 24.204  -3.411  1.440   1.00 30.85  ? 69  GLN B O   1 
ATOM   2334 C CB  . GLN B 1 68  ? 25.306  -2.009  4.033   1.00 31.83  ? 69  GLN B CB  1 
ATOM   2335 C CG  . GLN B 1 68  ? 25.190  -1.980  5.567   1.00 32.51  ? 69  GLN B CG  1 
ATOM   2336 C CD  . GLN B 1 68  ? 25.334  -0.589  6.120   1.00 33.51  ? 69  GLN B CD  1 
ATOM   2337 O OE1 . GLN B 1 68  ? 26.119  0.212   5.621   1.00 37.19  ? 69  GLN B OE1 1 
ATOM   2338 N NE2 . GLN B 1 68  ? 24.562  -0.270  7.159   1.00 38.15  ? 69  GLN B NE2 1 
ATOM   2339 N N   . CYS B 1 69  ? 26.446  -3.838  1.208   1.00 30.17  ? 70  CYS B N   1 
ATOM   2340 C CA  . CYS B 1 69  ? 26.387  -4.226  -0.229  1.00 31.38  ? 70  CYS B CA  1 
ATOM   2341 C C   . CYS B 1 69  ? 25.566  -5.510  -0.413  1.00 29.13  ? 70  CYS B C   1 
ATOM   2342 O O   . CYS B 1 69  ? 25.129  -5.785  -1.569  1.00 30.77  ? 70  CYS B O   1 
ATOM   2343 C CB  . CYS B 1 69  ? 27.792  -4.372  -0.813  1.00 33.18  ? 70  CYS B CB  1 
ATOM   2344 S SG  . CYS B 1 69  ? 28.875  -5.463  0.162   1.00 34.16  ? 70  CYS B SG  1 
ATOM   2345 N N   . PHE B 1 70  ? 25.377  -6.323  0.640   1.00 30.88  ? 71  PHE B N   1 
ATOM   2346 C CA  . PHE B 1 70  ? 24.513  -7.545  0.551   1.00 30.99  ? 71  PHE B CA  1 
ATOM   2347 C C   . PHE B 1 70  ? 23.019  -7.268  0.877   1.00 33.03  ? 71  PHE B C   1 
ATOM   2348 O O   . PHE B 1 70  ? 22.213  -8.228  0.758   1.00 33.16  ? 71  PHE B O   1 
ATOM   2349 C CB  . PHE B 1 70  ? 25.061  -8.735  1.354   1.00 33.51  ? 71  PHE B CB  1 
ATOM   2350 C CG  . PHE B 1 70  ? 26.337  -9.301  0.749   1.00 30.34  ? 71  PHE B CG  1 
ATOM   2351 C CD1 . PHE B 1 70  ? 26.338  -9.955  -0.464  1.00 30.33  ? 71  PHE B CD1 1 
ATOM   2352 C CD2 . PHE B 1 70  ? 27.564  -9.146  1.395   1.00 31.07  ? 71  PHE B CD2 1 
ATOM   2353 C CE1 . PHE B 1 70  ? 27.521  -10.449 -1.012  1.00 32.31  ? 71  PHE B CE1 1 
ATOM   2354 C CE2 . PHE B 1 70  ? 28.753  -9.543  0.809   1.00 28.52  ? 71  PHE B CE2 1 
ATOM   2355 C CZ  . PHE B 1 70  ? 28.732  -10.215 -0.390  1.00 30.88  ? 71  PHE B CZ  1 
ATOM   2356 N N   . ALA B 1 71  ? 22.630  -6.022  1.105   1.00 34.88  ? 72  ALA B N   1 
ATOM   2357 C CA  . ALA B 1 71  ? 21.200  -5.642  1.266   1.00 33.35  ? 72  ALA B CA  1 
ATOM   2358 C C   . ALA B 1 71  ? 20.439  -5.983  -0.005  1.00 34.35  ? 72  ALA B C   1 
ATOM   2359 O O   . ALA B 1 71  ? 21.024  -5.860  -1.103  1.00 30.75  ? 72  ALA B O   1 
ATOM   2360 C CB  . ALA B 1 71  ? 21.025  -4.184  1.591   1.00 35.17  ? 72  ALA B CB  1 
ATOM   2361 N N   . ARG B 1 72  ? 19.183  -6.408  0.158   1.00 34.54  ? 73  ARG B N   1 
ATOM   2362 C CA  . ARG B 1 72  ? 18.227  -6.530  -0.966  1.00 36.48  ? 73  ARG B CA  1 
ATOM   2363 C C   . ARG B 1 72  ? 17.536  -5.188  -1.180  1.00 32.69  ? 73  ARG B C   1 
ATOM   2364 O O   . ARG B 1 72  ? 16.883  -4.739  -0.292  1.00 32.59  ? 73  ARG B O   1 
ATOM   2365 C CB  . ARG B 1 72  ? 17.163  -7.609  -0.757  1.00 38.57  ? 73  ARG B CB  1 
ATOM   2366 C CG  . ARG B 1 72  ? 16.247  -7.686  -1.975  1.00 39.13  ? 73  ARG B CG  1 
ATOM   2367 C CD  . ARG B 1 72  ? 15.243  -8.776  -1.906  1.00 39.11  ? 73  ARG B CD  1 
ATOM   2368 N NE  . ARG B 1 72  ? 14.228  -8.494  -0.923  1.00 38.54  ? 73  ARG B NE  1 
ATOM   2369 C CZ  . ARG B 1 72  ? 13.149  -7.737  -1.150  1.00 41.37  ? 73  ARG B CZ  1 
ATOM   2370 N NH1 . ARG B 1 72  ? 12.977  -7.092  -2.295  1.00 37.58  ? 73  ARG B NH1 1 
ATOM   2371 N NH2 . ARG B 1 72  ? 12.301  -7.532  -0.174  1.00 41.49  ? 73  ARG B NH2 1 
ATOM   2372 N N   . TYR B 1 73  ? 17.800  -4.530  -2.301  1.00 30.66  ? 74  TYR B N   1 
ATOM   2373 C CA  . TYR B 1 73  ? 17.112  -3.294  -2.761  1.00 30.67  ? 74  TYR B CA  1 
ATOM   2374 C C   . TYR B 1 73  ? 15.976  -3.746  -3.657  1.00 35.63  ? 74  TYR B C   1 
ATOM   2375 O O   . TYR B 1 73  ? 16.233  -4.425  -4.637  1.00 37.99  ? 74  TYR B O   1 
ATOM   2376 C CB  . TYR B 1 73  ? 18.093  -2.355  -3.450  1.00 30.64  ? 74  TYR B CB  1 
ATOM   2377 C CG  . TYR B 1 73  ? 18.812  -1.454  -2.488  1.00 32.56  ? 74  TYR B CG  1 
ATOM   2378 C CD1 . TYR B 1 73  ? 19.898  -1.912  -1.761  1.00 35.25  ? 74  TYR B CD1 1 
ATOM   2379 C CD2 . TYR B 1 73  ? 18.442  -0.131  -2.312  1.00 32.92  ? 74  TYR B CD2 1 
ATOM   2380 C CE1 . TYR B 1 73  ? 20.563  -1.107  -0.867  1.00 30.59  ? 74  TYR B CE1 1 
ATOM   2381 C CE2 . TYR B 1 73  ? 19.103  0.693   -1.437  1.00 32.13  ? 74  TYR B CE2 1 
ATOM   2382 C CZ  . TYR B 1 73  ? 20.175  0.212   -0.698  1.00 31.99  ? 74  TYR B CZ  1 
ATOM   2383 O OH  . TYR B 1 73  ? 20.825  0.997   0.221   1.00 32.54  ? 74  TYR B OH  1 
ATOM   2384 N N   . PRO B 1 74  ? 14.705  -3.481  -3.299  1.00 36.47  ? 75  PRO B N   1 
ATOM   2385 C CA  . PRO B 1 74  ? 13.587  -3.754  -4.199  1.00 37.04  ? 75  PRO B CA  1 
ATOM   2386 C C   . PRO B 1 74  ? 13.921  -3.105  -5.541  1.00 34.12  ? 75  PRO B C   1 
ATOM   2387 O O   . PRO B 1 74  ? 14.551  -2.079  -5.517  1.00 33.67  ? 75  PRO B O   1 
ATOM   2388 C CB  . PRO B 1 74  ? 12.407  -3.073  -3.490  1.00 39.07  ? 75  PRO B CB  1 
ATOM   2389 C CG  . PRO B 1 74  ? 12.787  -3.132  -2.042  1.00 36.48  ? 75  PRO B CG  1 
ATOM   2390 C CD  . PRO B 1 74  ? 14.275  -2.853  -2.045  1.00 37.50  ? 75  PRO B CD  1 
ATOM   2391 N N   . ASP B 1 75  ? 13.524  -3.711  -6.642  1.00 35.16  ? 76  ASP B N   1 
ATOM   2392 C CA  . ASP B 1 75  ? 13.780  -3.200  -8.023  1.00 35.29  ? 76  ASP B CA  1 
ATOM   2393 C C   . ASP B 1 75  ? 13.460  -1.717  -8.122  1.00 43.67  ? 76  ASP B C   1 
ATOM   2394 O O   . ASP B 1 75  ? 14.273  -0.944  -8.742  1.00 36.20  ? 76  ASP B O   1 
ATOM   2395 C CB  . ASP B 1 75  ? 12.964  -4.003  -9.000  1.00 40.82  ? 76  ASP B CB  1 
ATOM   2396 C CG  . ASP B 1 75  ? 13.187  -3.539  -10.405 1.00 44.92  ? 76  ASP B CG  1 
ATOM   2397 O OD1 . ASP B 1 75  ? 14.178  -3.999  -11.020 1.00 42.91  ? 76  ASP B OD1 1 
ATOM   2398 O OD2 . ASP B 1 75  ? 12.413  -2.676  -10.822 1.00 41.94  ? 76  ASP B OD2 1 
ATOM   2399 N N   . HIS B 1 76  ? 12.390  -1.274  -7.453  1.00 41.69  ? 77  HIS B N   1 
ATOM   2400 C CA  . HIS B 1 76  ? 11.868  0.108   -7.637  1.00 42.26  ? 77  HIS B CA  1 
ATOM   2401 C C   . HIS B 1 76  ? 12.822  1.049   -6.917  1.00 41.44  ? 77  HIS B C   1 
ATOM   2402 O O   . HIS B 1 76  ? 12.732  2.244   -7.139  1.00 42.62  ? 77  HIS B O   1 
ATOM   2403 C CB  . HIS B 1 76  ? 10.378  0.211   -7.198  1.00 47.68  ? 77  HIS B CB  1 
ATOM   2404 C CG  . HIS B 1 76  ? 10.186  0.386   -5.735  1.00 48.17  ? 77  HIS B CG  1 
ATOM   2405 N ND1 . HIS B 1 76  ? 9.878   -0.686  -4.920  1.00 52.32  ? 77  HIS B ND1 1 
ATOM   2406 C CD2 . HIS B 1 76  ? 10.245  1.481   -4.928  1.00 52.31  ? 77  HIS B CD2 1 
ATOM   2407 C CE1 . HIS B 1 76  ? 9.800   -0.266  -3.660  1.00 48.17  ? 77  HIS B CE1 1 
ATOM   2408 N NE2 . HIS B 1 76  ? 10.008  1.063   -3.632  1.00 49.21  ? 77  HIS B NE2 1 
ATOM   2409 N N   . MET B 1 77  ? 13.701  0.535   -6.059  1.00 37.16  ? 78  MET B N   1 
ATOM   2410 C CA  . MET B 1 77  ? 14.643  1.370   -5.274  1.00 40.45  ? 78  MET B CA  1 
ATOM   2411 C C   . MET B 1 77  ? 16.087  1.182   -5.777  1.00 35.84  ? 78  MET B C   1 
ATOM   2412 O O   . MET B 1 77  ? 16.996  1.696   -5.137  1.00 37.18  ? 78  MET B O   1 
ATOM   2413 C CB  . MET B 1 77  ? 14.620  0.985   -3.782  1.00 38.93  ? 78  MET B CB  1 
ATOM   2414 C CG  . MET B 1 77  ? 13.423  1.476   -3.034  1.00 43.13  ? 78  MET B CG  1 
ATOM   2415 S SD  . MET B 1 77  ? 13.397  0.916   -1.352  1.00 41.33  ? 78  MET B SD  1 
ATOM   2416 C CE  . MET B 1 77  ? 14.711  1.878   -0.635  1.00 34.51  ? 78  MET B CE  1 
ATOM   2417 N N   . LYS B 1 78  ? 16.321  0.455   -6.849  1.00 37.21  ? 79  LYS B N   1 
ATOM   2418 C CA  . LYS B 1 78  ? 17.714  0.038   -7.222  1.00 41.69  ? 79  LYS B CA  1 
ATOM   2419 C C   . LYS B 1 78  ? 18.587  1.255   -7.575  1.00 43.79  ? 79  LYS B C   1 
ATOM   2420 O O   . LYS B 1 78  ? 19.816  1.191   -7.352  1.00 34.62  ? 79  LYS B O   1 
ATOM   2421 C CB  . LYS B 1 78  ? 17.715  -1.116  -8.235  1.00 52.20  ? 79  LYS B CB  1 
ATOM   2422 C CG  . LYS B 1 78  ? 17.673  -2.492  -7.523  1.00 57.79  ? 79  LYS B CG  1 
ATOM   2423 C CD  . LYS B 1 78  ? 17.667  -3.782  -8.347  1.00 64.15  ? 79  LYS B CD  1 
ATOM   2424 C CE  . LYS B 1 78  ? 17.805  -5.004  -7.452  1.00 67.93  ? 79  LYS B CE  1 
ATOM   2425 N NZ  . LYS B 1 78  ? 18.129  -6.211  -8.245  1.00 69.36  ? 79  LYS B NZ  1 
ATOM   2426 N N   . GLN B 1 79  ? 18.016  2.390   -7.980  1.00 39.15  ? 80  GLN B N   1 
ATOM   2427 C CA  . GLN B 1 79  ? 18.830  3.605   -8.281  1.00 41.05  ? 80  GLN B CA  1 
ATOM   2428 C C   . GLN B 1 79  ? 19.365  4.210   -6.961  1.00 39.90  ? 80  GLN B C   1 
ATOM   2429 O O   . GLN B 1 79  ? 20.226  5.133   -6.993  1.00 38.63  ? 80  GLN B O   1 
ATOM   2430 C CB  . GLN B 1 79  ? 17.991  4.515   -9.204  1.00 45.98  ? 80  GLN B CB  1 
ATOM   2431 C CG  . GLN B 1 79  ? 16.846  5.207   -8.482  1.00 55.19  ? 80  GLN B CG  1 
ATOM   2432 C CD  . GLN B 1 79  ? 15.508  4.499   -8.326  1.00 59.67  ? 80  GLN B CD  1 
ATOM   2433 O OE1 . GLN B 1 79  ? 15.364  3.262   -8.306  1.00 47.33  ? 80  GLN B OE1 1 
ATOM   2434 N NE2 . GLN B 1 79  ? 14.474  5.317   -8.165  1.00 63.65  ? 80  GLN B NE2 1 
ATOM   2435 N N   . HIS B 1 80  ? 18.995  3.696   -5.788  1.00 32.08  ? 81  HIS B N   1 
ATOM   2436 C CA  . HIS B 1 80  ? 19.499  4.248   -4.500  1.00 33.10  ? 81  HIS B CA  1 
ATOM   2437 C C   . HIS B 1 80  ? 20.529  3.339   -3.842  1.00 34.97  ? 81  HIS B C   1 
ATOM   2438 O O   . HIS B 1 80  ? 20.854  3.586   -2.657  1.00 35.28  ? 81  HIS B O   1 
ATOM   2439 C CB  . HIS B 1 80  ? 18.334  4.470   -3.509  1.00 38.62  ? 81  HIS B CB  1 
ATOM   2440 C CG  . HIS B 1 80  ? 17.374  5.453   -4.038  1.00 43.89  ? 81  HIS B CG  1 
ATOM   2441 N ND1 . HIS B 1 80  ? 16.179  5.086   -4.664  1.00 51.25  ? 81  HIS B ND1 1 
ATOM   2442 C CD2 . HIS B 1 80  ? 17.470  6.793   -4.101  1.00 45.36  ? 81  HIS B CD2 1 
ATOM   2443 C CE1 . HIS B 1 80  ? 15.575  6.183   -5.109  1.00 41.64  ? 81  HIS B CE1 1 
ATOM   2444 N NE2 . HIS B 1 80  ? 16.354  7.245   -4.748  1.00 46.40  ? 81  HIS B NE2 1 
ATOM   2445 N N   . ASP B 1 81  ? 20.993  2.286   -4.519  1.00 36.12  ? 82  ASP B N   1 
ATOM   2446 C CA  . ASP B 1 81  ? 21.998  1.368   -3.914  1.00 36.48  ? 82  ASP B CA  1 
ATOM   2447 C C   . ASP B 1 81  ? 23.410  1.892   -4.191  1.00 32.01  ? 82  ASP B C   1 
ATOM   2448 O O   . ASP B 1 81  ? 24.061  1.350   -5.129  1.00 34.19  ? 82  ASP B O   1 
ATOM   2449 C CB  . ASP B 1 81  ? 21.810  -0.071  -4.419  1.00 35.41  ? 82  ASP B CB  1 
ATOM   2450 C CG  . ASP B 1 81  ? 22.627  -1.177  -3.733  1.00 32.53  ? 82  ASP B CG  1 
ATOM   2451 O OD1 . ASP B 1 81  ? 23.525  -0.866  -2.887  1.00 30.77  ? 82  ASP B OD1 1 
ATOM   2452 O OD2 . ASP B 1 81  ? 22.290  -2.373  -4.038  1.00 33.92  ? 82  ASP B OD2 1 
ATOM   2453 N N   . PHE B 1 82  ? 23.914  2.710   -3.281  1.00 32.92  ? 83  PHE B N   1 
ATOM   2454 C CA  . PHE B 1 82  ? 25.297  3.218   -3.273  1.00 32.75  ? 83  PHE B CA  1 
ATOM   2455 C C   . PHE B 1 82  ? 26.321  2.081   -3.158  1.00 33.65  ? 83  PHE B C   1 
ATOM   2456 O O   . PHE B 1 82  ? 27.403  2.094   -3.802  1.00 32.60  ? 83  PHE B O   1 
ATOM   2457 C CB  . PHE B 1 82  ? 25.509  4.149   -2.094  1.00 31.72  ? 83  PHE B CB  1 
ATOM   2458 C CG  . PHE B 1 82  ? 26.955  4.477   -1.895  1.00 33.96  ? 83  PHE B CG  1 
ATOM   2459 C CD1 . PHE B 1 82  ? 27.615  5.395   -2.714  1.00 34.52  ? 83  PHE B CD1 1 
ATOM   2460 C CD2 . PHE B 1 82  ? 27.684  3.829   -0.920  1.00 35.16  ? 83  PHE B CD2 1 
ATOM   2461 C CE1 . PHE B 1 82  ? 28.957  5.643   -2.492  1.00 34.54  ? 83  PHE B CE1 1 
ATOM   2462 C CE2 . PHE B 1 82  ? 29.027  4.076   -0.729  1.00 33.26  ? 83  PHE B CE2 1 
ATOM   2463 C CZ  . PHE B 1 82  ? 29.653  5.014   -1.502  1.00 35.18  ? 83  PHE B CZ  1 
ATOM   2464 N N   . PHE B 1 83  ? 25.993  1.118   -2.304  1.00 32.97  ? 84  PHE B N   1 
ATOM   2465 C CA  . PHE B 1 83  ? 26.961  0.125   -1.792  1.00 30.65  ? 84  PHE B CA  1 
ATOM   2466 C C   . PHE B 1 83  ? 27.390  -0.738  -2.973  1.00 31.00  ? 84  PHE B C   1 
ATOM   2467 O O   . PHE B 1 83  ? 28.566  -0.944  -3.147  1.00 31.51  ? 84  PHE B O   1 
ATOM   2468 C CB  . PHE B 1 83  ? 26.360  -0.670  -0.641  1.00 29.75  ? 84  PHE B CB  1 
ATOM   2469 C CG  . PHE B 1 83  ? 25.832  0.163   0.507   1.00 29.92  ? 84  PHE B CG  1 
ATOM   2470 C CD1 . PHE B 1 83  ? 26.685  0.660   1.487   1.00 30.11  ? 84  PHE B CD1 1 
ATOM   2471 C CD2 . PHE B 1 83  ? 24.470  0.409   0.644   1.00 32.33  ? 84  PHE B CD2 1 
ATOM   2472 C CE1 . PHE B 1 83  ? 26.210  1.380   2.564   1.00 33.81  ? 84  PHE B CE1 1 
ATOM   2473 C CE2 . PHE B 1 83  ? 24.005  1.170   1.715   1.00 31.27  ? 84  PHE B CE2 1 
ATOM   2474 C CZ  . PHE B 1 83  ? 24.860  1.597   2.691   1.00 32.54  ? 84  PHE B CZ  1 
ATOM   2475 N N   . LYS B 1 84  ? 26.468  -1.289  -3.752  1.00 30.63  ? 85  LYS B N   1 
ATOM   2476 C CA  . LYS B 1 84  ? 26.924  -2.135  -4.872  1.00 31.61  ? 85  LYS B CA  1 
ATOM   2477 C C   . LYS B 1 84  ? 27.580  -1.261  -5.960  1.00 32.72  ? 85  LYS B C   1 
ATOM   2478 O O   . LYS B 1 84  ? 28.390  -1.790  -6.735  1.00 32.06  ? 85  LYS B O   1 
ATOM   2479 C CB  . LYS B 1 84  ? 25.739  -2.902  -5.430  1.00 38.70  ? 85  LYS B CB  1 
ATOM   2480 C CG  . LYS B 1 84  ? 25.188  -3.965  -4.508  1.00 33.95  ? 85  LYS B CG  1 
ATOM   2481 C CD  . LYS B 1 84  ? 24.043  -4.745  -5.130  1.00 33.76  ? 85  LYS B CD  1 
ATOM   2482 C CE  . LYS B 1 84  ? 23.259  -5.575  -4.134  1.00 33.31  ? 85  LYS B CE  1 
ATOM   2483 N NZ  . LYS B 1 84  ? 22.802  -4.732  -2.997  1.00 35.54  ? 85  LYS B NZ  1 
ATOM   2484 N N   . SER B 1 85  ? 27.113  -0.026  -6.139  1.00 32.56  ? 86  SER B N   1 
ATOM   2485 C CA  . SER B 1 85  ? 27.524  0.870   -7.255  1.00 35.94  ? 86  SER B CA  1 
ATOM   2486 C C   . SER B 1 85  ? 29.036  1.129   -7.122  1.00 39.07  ? 86  SER B C   1 
ATOM   2487 O O   . SER B 1 85  ? 29.656  1.311   -8.135  1.00 37.82  ? 86  SER B O   1 
ATOM   2488 C CB  . SER B 1 85  ? 26.703  2.162   -7.353  1.00 33.96  ? 86  SER B CB  1 
ATOM   2489 O OG  . SER B 1 85  ? 27.115  3.143   -6.412  1.00 32.62  ? 86  SER B OG  1 
ATOM   2490 N N   . ALA B 1 86  ? 29.586  1.076   -5.919  1.00 33.74  ? 87  ALA B N   1 
ATOM   2491 C CA  . ALA B 1 86  ? 31.007  1.393   -5.623  1.00 34.02  ? 87  ALA B CA  1 
ATOM   2492 C C   . ALA B 1 86  ? 31.919  0.219   -5.991  1.00 33.58  ? 87  ALA B C   1 
ATOM   2493 O O   . ALA B 1 86  ? 33.177  0.395   -6.011  1.00 36.16  ? 87  ALA B O   1 
ATOM   2494 C CB  . ALA B 1 86  ? 31.150  1.776   -4.171  1.00 34.32  ? 87  ALA B CB  1 
ATOM   2495 N N   . MET B 1 87  ? 31.344  -0.949  -6.231  1.00 35.22  ? 88  MET B N   1 
ATOM   2496 C CA  . MET B 1 87  ? 32.102  -2.199  -6.475  1.00 36.16  ? 88  MET B CA  1 
ATOM   2497 C C   . MET B 1 87  ? 32.470  -2.247  -7.964  1.00 42.52  ? 88  MET B C   1 
ATOM   2498 O O   . MET B 1 87  ? 31.767  -1.683  -8.802  1.00 38.35  ? 88  MET B O   1 
ATOM   2499 C CB  . MET B 1 87  ? 31.223  -3.391  -6.118  1.00 36.98  ? 88  MET B CB  1 
ATOM   2500 C CG  . MET B 1 87  ? 30.900  -3.475  -4.622  1.00 38.80  ? 88  MET B CG  1 
ATOM   2501 S SD  . MET B 1 87  ? 32.335  -3.589  -3.600  1.00 34.88  ? 88  MET B SD  1 
ATOM   2502 C CE  . MET B 1 87  ? 31.739  -2.966  -2.031  1.00 35.95  ? 88  MET B CE  1 
ATOM   2503 N N   . PRO B 1 88  ? 33.543  -2.941  -8.377  1.00 39.75  ? 89  PRO B N   1 
ATOM   2504 C CA  . PRO B 1 88  ? 34.380  -3.724  -7.460  1.00 39.04  ? 89  PRO B CA  1 
ATOM   2505 C C   . PRO B 1 88  ? 35.500  -3.068  -6.641  1.00 34.50  ? 89  PRO B C   1 
ATOM   2506 O O   . PRO B 1 88  ? 35.910  -3.691  -5.699  1.00 36.09  ? 89  PRO B O   1 
ATOM   2507 C CB  . PRO B 1 88  ? 34.974  -4.776  -8.441  1.00 46.66  ? 89  PRO B CB  1 
ATOM   2508 C CG  . PRO B 1 88  ? 35.095  -4.042  -9.783  1.00 46.82  ? 89  PRO B CG  1 
ATOM   2509 C CD  . PRO B 1 88  ? 33.938  -3.063  -9.803  1.00 41.26  ? 89  PRO B CD  1 
ATOM   2510 N N   . GLU B 1 89  ? 35.810  -1.808  -6.896  1.00 36.88  ? 90  GLU B N   1 
ATOM   2511 C CA  . GLU B 1 89  ? 36.883  -1.043  -6.252  1.00 37.79  ? 90  GLU B CA  1 
ATOM   2512 C C   . GLU B 1 89  ? 36.560  -0.897  -4.763  1.00 35.95  ? 90  GLU B C   1 
ATOM   2513 O O   . GLU B 1 89  ? 37.444  -0.955  -3.940  1.00 35.89  ? 90  GLU B O   1 
ATOM   2514 C CB  . GLU B 1 89  ? 37.024  0.310   -6.963  1.00 47.76  ? 90  GLU B CB  1 
ATOM   2515 C CG  . GLU B 1 89  ? 37.368  0.273   -8.446  1.00 48.46  ? 90  GLU B CG  1 
ATOM   2516 C CD  . GLU B 1 89  ? 36.240  0.100   -9.449  1.00 55.10  ? 90  GLU B CD  1 
ATOM   2517 O OE1 . GLU B 1 89  ? 35.051  0.049   -9.099  1.00 47.17  ? 90  GLU B OE1 1 
ATOM   2518 O OE2 . GLU B 1 89  ? 36.570  -0.032  -10.605 1.00 65.56  ? 90  GLU B OE2 1 
ATOM   2519 N N   . GLY B 1 90  ? 35.276  -0.747  -4.402  1.00 37.28  ? 91  GLY B N   1 
ATOM   2520 C CA  . GLY B 1 90  ? 34.881  -0.785  -2.987  1.00 31.23  ? 91  GLY B CA  1 
ATOM   2521 C C   . GLY B 1 90  ? 34.554  0.561   -2.415  1.00 33.93  ? 91  GLY B C   1 
ATOM   2522 O O   . GLY B 1 90  ? 34.599  1.604   -3.113  1.00 39.04  ? 91  GLY B O   1 
ATOM   2523 N N   . TYR B 1 91  ? 34.218  0.540   -1.138  1.00 33.62  ? 92  TYR B N   1 
ATOM   2524 C CA  . TYR B 1 91  ? 34.044  1.732   -0.306  1.00 34.88  ? 92  TYR B CA  1 
ATOM   2525 C C   . TYR B 1 91  ? 34.824  1.551   0.993   1.00 35.24  ? 92  TYR B C   1 
ATOM   2526 O O   . TYR B 1 91  ? 35.123  0.409   1.518   1.00 33.97  ? 92  TYR B O   1 
ATOM   2527 C CB  . TYR B 1 91  ? 32.552  2.036   -0.160  1.00 39.23  ? 92  TYR B CB  1 
ATOM   2528 C CG  . TYR B 1 91  ? 31.709  0.919   0.413   1.00 33.27  ? 92  TYR B CG  1 
ATOM   2529 C CD1 . TYR B 1 91  ? 31.766  0.576   1.741   1.00 36.41  ? 92  TYR B CD1 1 
ATOM   2530 C CD2 . TYR B 1 91  ? 30.828  0.220   -0.382  1.00 35.05  ? 92  TYR B CD2 1 
ATOM   2531 C CE1 . TYR B 1 91  ? 30.974  -0.444  2.273   1.00 34.63  ? 92  TYR B CE1 1 
ATOM   2532 C CE2 . TYR B 1 91  ? 30.030  -0.806  0.126   1.00 32.90  ? 92  TYR B CE2 1 
ATOM   2533 C CZ  . TYR B 1 91  ? 30.079  -1.114  1.474   1.00 33.03  ? 92  TYR B CZ  1 
ATOM   2534 O OH  . TYR B 1 91  ? 29.291  -2.130  1.993   1.00 33.79  ? 92  TYR B OH  1 
ATOM   2535 N N   . VAL B 1 92  ? 35.222  2.692   1.524   1.00 33.55  ? 93  VAL B N   1 
ATOM   2536 C CA  . VAL B 1 92  ? 35.674  2.830   2.936   1.00 35.15  ? 93  VAL B CA  1 
ATOM   2537 C C   . VAL B 1 92  ? 34.405  3.080   3.782   1.00 33.98  ? 93  VAL B C   1 
ATOM   2538 O O   . VAL B 1 92  ? 33.510  3.871   3.370   1.00 36.01  ? 93  VAL B O   1 
ATOM   2539 C CB  . VAL B 1 92  ? 36.722  3.944   3.110   1.00 40.26  ? 93  VAL B CB  1 
ATOM   2540 C CG1 . VAL B 1 92  ? 37.070  4.201   4.553   1.00 40.04  ? 93  VAL B CG1 1 
ATOM   2541 C CG2 . VAL B 1 92  ? 37.995  3.689   2.269   1.00 45.99  ? 93  VAL B CG2 1 
ATOM   2542 N N   . GLN B 1 93  ? 34.313  2.360   4.888   1.00 35.85  ? 94  GLN B N   1 
ATOM   2543 C CA  . GLN B 1 93  ? 33.210  2.456   5.890   1.00 34.28  ? 94  GLN B CA  1 
ATOM   2544 C C   . GLN B 1 93  ? 33.872  2.814   7.213   1.00 30.77  ? 94  GLN B C   1 
ATOM   2545 O O   . GLN B 1 93  ? 34.757  2.024   7.707   1.00 36.44  ? 94  GLN B O   1 
ATOM   2546 C CB  . GLN B 1 93  ? 32.453  1.117   5.961   1.00 31.70  ? 94  GLN B CB  1 
ATOM   2547 C CG  . GLN B 1 93  ? 31.433  1.124   7.094   1.00 33.36  ? 94  GLN B CG  1 
ATOM   2548 C CD  . GLN B 1 93  ? 30.258  0.202   6.835   1.00 35.25  ? 94  GLN B CD  1 
ATOM   2549 O OE1 . GLN B 1 93  ? 29.645  0.186   5.769   1.00 36.50  ? 94  GLN B OE1 1 
ATOM   2550 N NE2 . GLN B 1 93  ? 29.873  -0.542  7.845   1.00 36.08  ? 94  GLN B NE2 1 
ATOM   2551 N N   . GLU B 1 94  ? 33.561  4.006   7.708   1.00 35.08  ? 95  GLU B N   1 
ATOM   2552 C CA  . GLU B 1 94  ? 34.106  4.533   8.982   1.00 33.59  ? 95  GLU B CA  1 
ATOM   2553 C C   . GLU B 1 94  ? 32.959  4.706   9.964   1.00 31.34  ? 95  GLU B C   1 
ATOM   2554 O O   . GLU B 1 94  ? 31.923  5.307   9.565   1.00 33.52  ? 95  GLU B O   1 
ATOM   2555 C CB  . GLU B 1 94  ? 34.827  5.884   8.736   1.00 37.05  ? 95  GLU B CB  1 
ATOM   2556 C CG  . GLU B 1 94  ? 36.200  5.683   8.064   1.00 44.85  ? 95  GLU B CG  1 
ATOM   2557 C CD  . GLU B 1 94  ? 36.919  6.972   7.667   1.00 55.67  ? 95  GLU B CD  1 
ATOM   2558 O OE1 . GLU B 1 94  ? 36.360  7.713   6.835   1.00 51.49  ? 95  GLU B OE1 1 
ATOM   2559 O OE2 . GLU B 1 94  ? 37.993  7.247   8.237   1.00 51.97  ? 95  GLU B OE2 1 
ATOM   2560 N N   . ARG B 1 95  ? 33.184  4.338   11.222  1.00 34.66  ? 96  ARG B N   1 
ATOM   2561 C CA  . ARG B 1 95  ? 32.205  4.633   12.281  1.00 39.58  ? 96  ARG B CA  1 
ATOM   2562 C C   . ARG B 1 95  ? 32.934  5.200   13.491  1.00 35.31  ? 96  ARG B C   1 
ATOM   2563 O O   . ARG B 1 95  ? 34.029  4.703   13.817  1.00 34.43  ? 96  ARG B O   1 
ATOM   2564 C CB  . ARG B 1 95  ? 31.429  3.373   12.694  1.00 32.45  ? 96  ARG B CB  1 
ATOM   2565 C CG  . ARG B 1 95  ? 30.580  2.800   11.570  1.00 35.69  ? 96  ARG B CG  1 
ATOM   2566 C CD  . ARG B 1 95  ? 29.313  2.208   12.149  1.00 33.39  ? 96  ARG B CD  1 
ATOM   2567 N NE  . ARG B 1 95  ? 28.363  1.602   11.236  1.00 32.73  ? 96  ARG B NE  1 
ATOM   2568 C CZ  . ARG B 1 95  ? 28.332  0.314   10.887  1.00 28.67  ? 96  ARG B CZ  1 
ATOM   2569 N NH1 . ARG B 1 95  ? 29.188  -0.554  11.374  1.00 33.30  ? 96  ARG B NH1 1 
ATOM   2570 N NH2 . ARG B 1 95  ? 27.398  -0.092  10.050  1.00 34.63  ? 96  ARG B NH2 1 
ATOM   2571 N N   . THR B 1 96  ? 32.199  5.993   14.248  1.00 35.92  ? 97  THR B N   1 
ATOM   2572 C CA  . THR B 1 96  ? 32.406  6.080   15.717  1.00 38.73  ? 97  THR B CA  1 
ATOM   2573 C C   . THR B 1 96  ? 31.189  5.469   16.431  1.00 33.77  ? 97  THR B C   1 
ATOM   2574 O O   . THR B 1 96  ? 30.004  5.718   15.996  1.00 39.29  ? 97  THR B O   1 
ATOM   2575 C CB  . THR B 1 96  ? 32.756  7.514   16.158  1.00 42.89  ? 97  THR B CB  1 
ATOM   2576 O OG1 . THR B 1 96  ? 33.960  7.957   15.538  1.00 41.57  ? 97  THR B OG1 1 
ATOM   2577 C CG2 . THR B 1 96  ? 32.993  7.572   17.651  1.00 45.15  ? 97  THR B CG2 1 
ATOM   2578 N N   . ILE B 1 97  ? 31.468  4.605   17.399  1.00 35.20  ? 98  ILE B N   1 
ATOM   2579 C CA  . ILE B 1 97  ? 30.402  3.946   18.230  1.00 36.14  ? 98  ILE B CA  1 
ATOM   2580 C C   . ILE B 1 97  ? 30.635  4.331   19.687  1.00 34.16  ? 98  ILE B C   1 
ATOM   2581 O O   . ILE B 1 97  ? 31.633  3.834   20.269  1.00 33.29  ? 98  ILE B O   1 
ATOM   2582 C CB  . ILE B 1 97  ? 30.411  2.415   18.096  1.00 33.62  ? 98  ILE B CB  1 
ATOM   2583 C CG1 . ILE B 1 97  ? 30.301  2.014   16.612  1.00 37.61  ? 98  ILE B CG1 1 
ATOM   2584 C CG2 . ILE B 1 97  ? 29.326  1.742   18.966  1.00 33.77  ? 98  ILE B CG2 1 
ATOM   2585 C CD1 . ILE B 1 97  ? 30.533  0.511   16.368  1.00 34.35  ? 98  ILE B CD1 1 
ATOM   2586 N N   . PHE B 1 98  ? 29.671  5.073   20.228  1.00 33.22  ? 99  PHE B N   1 
ATOM   2587 C CA  . PHE B 1 98  ? 29.691  5.596   21.608  1.00 40.03  ? 99  PHE B CA  1 
ATOM   2588 C C   . PHE B 1 98  ? 28.830  4.680   22.499  1.00 37.68  ? 99  PHE B C   1 
ATOM   2589 O O   . PHE B 1 98  ? 27.604  4.603   22.281  1.00 38.55  ? 99  PHE B O   1 
ATOM   2590 C CB  . PHE B 1 98  ? 29.162  7.026   21.581  1.00 43.53  ? 99  PHE B CB  1 
ATOM   2591 C CG  . PHE B 1 98  ? 30.053  8.025   20.912  1.00 45.69  ? 99  PHE B CG  1 
ATOM   2592 C CD1 . PHE B 1 98  ? 31.249  8.403   21.515  1.00 46.51  ? 99  PHE B CD1 1 
ATOM   2593 C CD2 . PHE B 1 98  ? 29.660  8.639   19.724  1.00 46.62  ? 99  PHE B CD2 1 
ATOM   2594 C CE1 . PHE B 1 98  ? 32.037  9.369   20.925  1.00 49.19  ? 99  PHE B CE1 1 
ATOM   2595 C CE2 . PHE B 1 98  ? 30.467  9.596   19.137  1.00 55.71  ? 99  PHE B CE2 1 
ATOM   2596 C CZ  . PHE B 1 98  ? 31.647  9.965   19.744  1.00 47.22  ? 99  PHE B CZ  1 
ATOM   2597 N N   . PHE B 1 99  ? 29.464  3.918   23.385  1.00 33.76  ? 100 PHE B N   1 
ATOM   2598 C CA  . PHE B 1 99  ? 28.769  3.053   24.348  1.00 36.02  ? 100 PHE B CA  1 
ATOM   2599 C C   . PHE B 1 99  ? 28.452  3.937   25.552  1.00 46.00  ? 100 PHE B C   1 
ATOM   2600 O O   . PHE B 1 99  ? 29.393  4.499   26.114  1.00 41.11  ? 100 PHE B O   1 
ATOM   2601 C CB  . PHE B 1 99  ? 29.632  1.859   24.726  1.00 36.41  ? 100 PHE B CB  1 
ATOM   2602 C CG  . PHE B 1 99  ? 29.840  0.900   23.574  1.00 40.34  ? 100 PHE B CG  1 
ATOM   2603 C CD1 . PHE B 1 99  ? 28.866  -0.027  23.255  1.00 42.25  ? 100 PHE B CD1 1 
ATOM   2604 C CD2 . PHE B 1 99  ? 30.993  0.943   22.796  1.00 41.83  ? 100 PHE B CD2 1 
ATOM   2605 C CE1 . PHE B 1 99  ? 29.029  -0.909  22.196  1.00 38.69  ? 100 PHE B CE1 1 
ATOM   2606 C CE2 . PHE B 1 99  ? 31.148  0.073   21.725  1.00 43.28  ? 100 PHE B CE2 1 
ATOM   2607 C CZ  . PHE B 1 99  ? 30.181  -0.868  21.447  1.00 43.03  ? 100 PHE B CZ  1 
ATOM   2608 N N   . LYS B 1 100 ? 27.193  4.016   25.957  1.00 42.92  ? 101 LYS B N   1 
ATOM   2609 C CA  . LYS B 1 100 ? 26.773  4.972   27.030  1.00 48.38  ? 101 LYS B CA  1 
ATOM   2610 C C   . LYS B 1 100 ? 27.500  4.663   28.363  1.00 36.71  ? 101 LYS B C   1 
ATOM   2611 O O   . LYS B 1 100 ? 27.583  3.518   28.776  1.00 41.00  ? 101 LYS B O   1 
ATOM   2612 C CB  . LYS B 1 100 ? 25.251  4.969   27.153  1.00 48.12  ? 101 LYS B CB  1 
ATOM   2613 C CG  . LYS B 1 100 ? 24.715  5.902   28.230  1.00 57.67  ? 101 LYS B CG  1 
ATOM   2614 C CD  . LYS B 1 100 ? 23.225  5.709   28.562  1.00 57.23  ? 101 LYS B CD  1 
ATOM   2615 C CE  . LYS B 1 100 ? 22.790  6.473   29.803  1.00 49.55  ? 101 LYS B CE  1 
ATOM   2616 N NZ  . LYS B 1 100 ? 22.337  7.832   29.447  1.00 67.99  ? 101 LYS B NZ  1 
ATOM   2617 N N   . ASP B 1 101 ? 28.103  5.699   28.954  1.00 51.30  ? 102 ASP B N   1 
ATOM   2618 C CA  . ASP B 1 101 ? 28.876  5.703   30.230  1.00 49.26  ? 102 ASP B CA  1 
ATOM   2619 C C   . ASP B 1 101 ? 30.026  4.716   30.097  1.00 53.28  ? 102 ASP B C   1 
ATOM   2620 O O   . ASP B 1 101 ? 30.441  4.103   31.111  1.00 41.80  ? 102 ASP B O   1 
ATOM   2621 C CB  . ASP B 1 101 ? 27.984  5.441   31.444  1.00 56.35  ? 102 ASP B CB  1 
ATOM   2622 C CG  . ASP B 1 101 ? 26.878  6.478   31.556  1.00 62.23  ? 102 ASP B CG  1 
ATOM   2623 O OD1 . ASP B 1 101 ? 27.180  7.695   31.352  1.00 57.32  ? 102 ASP B OD1 1 
ATOM   2624 O OD2 . ASP B 1 101 ? 25.706  6.070   31.780  1.00 67.66  ? 102 ASP B OD2 1 
ATOM   2625 N N   . ASP B 1 102 ? 30.559  4.563   28.896  1.00 41.54  ? 103 ASP B N   1 
ATOM   2626 C CA  . ASP B 1 102 ? 31.737  3.690   28.722  1.00 42.51  ? 103 ASP B CA  1 
ATOM   2627 C C   . ASP B 1 102 ? 32.519  4.228   27.528  1.00 38.51  ? 103 ASP B C   1 
ATOM   2628 O O   . ASP B 1 102 ? 32.295  5.369   27.127  1.00 41.92  ? 103 ASP B O   1 
ATOM   2629 C CB  . ASP B 1 102 ? 31.274  2.224   28.689  1.00 45.86  ? 103 ASP B CB  1 
ATOM   2630 C CG  . ASP B 1 102 ? 32.299  1.209   29.177  1.00 41.94  ? 103 ASP B CG  1 
ATOM   2631 O OD1 . ASP B 1 102 ? 33.512  1.566   29.220  1.00 51.89  ? 103 ASP B OD1 1 
ATOM   2632 O OD2 . ASP B 1 102 ? 31.930  0.019   29.374  1.00 43.66  ? 103 ASP B OD2 1 
ATOM   2633 N N   . GLY B 1 103 ? 33.389  3.403   26.972  1.00 41.12  ? 104 GLY B N   1 
ATOM   2634 C CA  . GLY B 1 103 ? 34.308  3.802   25.896  1.00 44.83  ? 104 GLY B CA  1 
ATOM   2635 C C   . GLY B 1 103 ? 33.643  3.895   24.533  1.00 48.45  ? 104 GLY B C   1 
ATOM   2636 O O   . GLY B 1 103 ? 32.391  3.903   24.420  1.00 41.44  ? 104 GLY B O   1 
ATOM   2637 N N   . ASN B 1 104 ? 34.472  4.034   23.505  1.00 45.54  ? 105 ASN B N   1 
ATOM   2638 C CA  . ASN B 1 104 ? 33.972  4.206   22.116  1.00 48.22  ? 105 ASN B CA  1 
ATOM   2639 C C   . ASN B 1 104 ? 34.832  3.318   21.234  1.00 46.16  ? 105 ASN B C   1 
ATOM   2640 O O   . ASN B 1 104 ? 36.022  3.117   21.574  1.00 40.90  ? 105 ASN B O   1 
ATOM   2641 C CB  . ASN B 1 104 ? 33.877  5.679   21.679  1.00 48.88  ? 105 ASN B CB  1 
ATOM   2642 C CG  . ASN B 1 104 ? 35.205  6.410   21.701  1.00 54.78  ? 105 ASN B CG  1 
ATOM   2643 O OD1 . ASN B 1 104 ? 35.458  7.192   22.610  1.00 47.99  ? 105 ASN B OD1 1 
ATOM   2644 N ND2 . ASN B 1 104 ? 36.059  6.132   20.733  1.00 41.71  ? 105 ASN B ND2 1 
ATOM   2645 N N   . TYR B 1 105 ? 34.234  2.771   20.174  1.00 37.79  ? 106 TYR B N   1 
ATOM   2646 C CA  . TYR B 1 105 ? 35.016  2.166   19.075  1.00 37.29  ? 106 TYR B CA  1 
ATOM   2647 C C   . TYR B 1 105 ? 35.138  3.197   17.968  1.00 36.71  ? 106 TYR B C   1 
ATOM   2648 O O   . TYR B 1 105 ? 34.158  3.923   17.665  1.00 38.82  ? 106 TYR B O   1 
ATOM   2649 C CB  . TYR B 1 105 ? 34.344  0.889   18.559  1.00 35.99  ? 106 TYR B CB  1 
ATOM   2650 C CG  . TYR B 1 105 ? 34.182  -0.296  19.471  1.00 33.70  ? 106 TYR B CG  1 
ATOM   2651 C CD1 . TYR B 1 105 ? 34.983  -0.518  20.565  1.00 34.75  ? 106 TYR B CD1 1 
ATOM   2652 C CD2 . TYR B 1 105 ? 33.229  -1.272  19.166  1.00 32.82  ? 106 TYR B CD2 1 
ATOM   2653 C CE1 . TYR B 1 105 ? 34.836  -1.658  21.344  1.00 36.15  ? 106 TYR B CE1 1 
ATOM   2654 C CE2 . TYR B 1 105 ? 33.088  -2.412  19.920  1.00 35.41  ? 106 TYR B CE2 1 
ATOM   2655 C CZ  . TYR B 1 105 ? 33.865  -2.594  21.044  1.00 36.36  ? 106 TYR B CZ  1 
ATOM   2656 O OH  . TYR B 1 105 ? 33.704  -3.725  21.768  1.00 38.22  ? 106 TYR B OH  1 
ATOM   2657 N N   . LYS B 1 106 ? 36.286  3.177   17.294  1.00 40.29  ? 107 LYS B N   1 
ATOM   2658 C CA  . LYS B 1 106 ? 36.481  3.905   16.028  1.00 39.51  ? 107 LYS B CA  1 
ATOM   2659 C C   . LYS B 1 106 ? 36.907  2.861   15.002  1.00 39.26  ? 107 LYS B C   1 
ATOM   2660 O O   . LYS B 1 106 ? 37.848  2.110   15.264  1.00 40.78  ? 107 LYS B O   1 
ATOM   2661 C CB  . LYS B 1 106 ? 37.477  5.055   16.186  1.00 49.27  ? 107 LYS B CB  1 
ATOM   2662 C CG  . LYS B 1 106 ? 36.870  6.333   16.752  1.00 55.90  ? 107 LYS B CG  1 
ATOM   2663 C CD  . LYS B 1 106 ? 37.878  7.478   16.850  1.00 66.52  ? 107 LYS B CD  1 
ATOM   2664 C CE  . LYS B 1 106 ? 37.241  8.806   17.215  1.00 74.75  ? 107 LYS B CE  1 
ATOM   2665 N NZ  . LYS B 1 106 ? 36.961  8.889   18.669  1.00 80.93  ? 107 LYS B NZ  1 
ATOM   2666 N N   . THR B 1 107 ? 36.168  2.752   13.903  1.00 41.04  ? 108 THR B N   1 
ATOM   2667 C CA  . THR B 1 107 ? 36.422  1.677   12.941  1.00 41.08  ? 108 THR B CA  1 
ATOM   2668 C C   . THR B 1 107 ? 36.698  2.299   11.568  1.00 36.73  ? 108 THR B C   1 
ATOM   2669 O O   . THR B 1 107 ? 36.001  3.234   11.115  1.00 37.80  ? 108 THR B O   1 
ATOM   2670 C CB  . THR B 1 107 ? 35.289  0.632   12.973  1.00 32.83  ? 108 THR B CB  1 
ATOM   2671 O OG1 . THR B 1 107 ? 34.094  1.252   12.475  1.00 30.67  ? 108 THR B OG1 1 
ATOM   2672 C CG2 . THR B 1 107 ? 35.108  0.049   14.353  1.00 36.14  ? 108 THR B CG2 1 
ATOM   2673 N N   . ARG B 1 108 ? 37.560  1.620   10.834  1.00 40.07  ? 109 ARG B N   1 
ATOM   2674 C CA  . ARG B 1 108 ? 37.805  1.945   9.415   1.00 38.81  ? 109 ARG B CA  1 
ATOM   2675 C C   . ARG B 1 108 ? 37.901  0.628   8.682   1.00 32.03  ? 109 ARG B C   1 
ATOM   2676 O O   . ARG B 1 108 ? 38.747  -0.179  9.004   1.00 35.60  ? 109 ARG B O   1 
ATOM   2677 C CB  . ARG B 1 108 ? 39.072  2.814   9.278   1.00 42.06  ? 109 ARG B CB  1 
ATOM   2678 C CG  . ARG B 1 108 ? 39.365  3.196   7.829   1.00 44.91  ? 109 ARG B CG  1 
ATOM   2679 C CD  . ARG B 1 108 ? 40.624  4.062   7.578   1.00 44.26  ? 109 ARG B CD  1 
ATOM   2680 N NE  . ARG B 1 108 ? 40.779  4.359   6.157   1.00 47.53  ? 109 ARG B NE  1 
ATOM   2681 C CZ  . ARG B 1 108 ? 41.183  3.501   5.223   1.00 50.91  ? 109 ARG B CZ  1 
ATOM   2682 N NH1 . ARG B 1 108 ? 41.498  2.253   5.498   1.00 51.03  ? 109 ARG B NH1 1 
ATOM   2683 N NH2 . ARG B 1 108 ? 41.247  3.886   3.965   1.00 69.83  ? 109 ARG B NH2 1 
ATOM   2684 N N   . ALA B 1 109 ? 37.009  0.430   7.747   1.00 34.36  ? 110 ALA B N   1 
ATOM   2685 C CA  . ALA B 1 109 ? 36.965  -0.800  6.972   1.00 38.25  ? 110 ALA B CA  1 
ATOM   2686 C C   . ALA B 1 109 ? 37.110  -0.434  5.504   1.00 34.17  ? 110 ALA B C   1 
ATOM   2687 O O   . ALA B 1 109 ? 36.577  0.603   5.077   1.00 37.61  ? 110 ALA B O   1 
ATOM   2688 C CB  . ALA B 1 109 ? 35.683  -1.543  7.272   1.00 35.12  ? 110 ALA B CB  1 
ATOM   2689 N N   . GLU B 1 110 ? 37.709  -1.348  4.782   1.00 33.94  ? 111 GLU B N   1 
ATOM   2690 C CA  . GLU B 1 110 ? 37.638  -1.395  3.315   1.00 35.99  ? 111 GLU B CA  1 
ATOM   2691 C C   . GLU B 1 110 ? 36.768  -2.574  2.891   1.00 32.86  ? 111 GLU B C   1 
ATOM   2692 O O   . GLU B 1 110 ? 37.074  -3.713  3.284   1.00 33.86  ? 111 GLU B O   1 
ATOM   2693 C CB  . GLU B 1 110 ? 39.069  -1.448  2.777   1.00 38.76  ? 111 GLU B CB  1 
ATOM   2694 C CG  . GLU B 1 110 ? 39.721  -0.080  2.879   1.00 44.99  ? 111 GLU B CG  1 
ATOM   2695 C CD  . GLU B 1 110 ? 41.071  0.041   2.184   1.00 49.03  ? 111 GLU B CD  1 
ATOM   2696 O OE1 . GLU B 1 110 ? 41.354  -0.783  1.287   1.00 51.26  ? 111 GLU B OE1 1 
ATOM   2697 O OE2 . GLU B 1 110 ? 41.822  0.923   2.588   1.00 53.20  ? 111 GLU B OE2 1 
ATOM   2698 N N   . VAL B 1 111 ? 35.667  -2.275  2.196   1.00 32.40  ? 112 VAL B N   1 
ATOM   2699 C CA  . VAL B 1 111 ? 34.777  -3.323  1.638   1.00 31.52  ? 112 VAL B CA  1 
ATOM   2700 C C   . VAL B 1 111 ? 34.968  -3.365  0.138   1.00 33.37  ? 112 VAL B C   1 
ATOM   2701 O O   . VAL B 1 111 ? 34.670  -2.359  -0.494  1.00 36.12  ? 112 VAL B O   1 
ATOM   2702 C CB  . VAL B 1 111 ? 33.346  -3.058  2.081   1.00 29.99  ? 112 VAL B CB  1 
ATOM   2703 C CG1 . VAL B 1 111 ? 32.467  -4.190  1.647   1.00 33.73  ? 112 VAL B CG1 1 
ATOM   2704 C CG2 . VAL B 1 111 ? 33.288  -2.828  3.585   1.00 33.56  ? 112 VAL B CG2 1 
ATOM   2705 N N   . LYS B 1 112 ? 35.504  -4.458  -0.404  1.00 32.21  ? 113 LYS B N   1 
ATOM   2706 C CA  . LYS B 1 112 ? 35.836  -4.482  -1.848  1.00 38.59  ? 113 LYS B CA  1 
ATOM   2707 C C   . LYS B 1 112 ? 35.999  -5.926  -2.303  1.00 33.60  ? 113 LYS B C   1 
ATOM   2708 O O   . LYS B 1 112 ? 36.221  -6.794  -1.475  1.00 33.54  ? 113 LYS B O   1 
ATOM   2709 C CB  . LYS B 1 112 ? 37.134  -3.693  -2.065  1.00 36.50  ? 113 LYS B CB  1 
ATOM   2710 C CG  . LYS B 1 112 ? 38.385  -4.406  -1.560  1.00 49.75  ? 113 LYS B CG  1 
ATOM   2711 C CD  . LYS B 1 112 ? 39.733  -3.807  -2.080  1.00 53.02  ? 113 LYS B CD  1 
ATOM   2712 C CE  . LYS B 1 112 ? 40.351  -2.813  -1.133  1.00 59.84  ? 113 LYS B CE  1 
ATOM   2713 N NZ  . LYS B 1 112 ? 41.222  -3.474  -0.133  1.00 60.90  ? 113 LYS B NZ  1 
ATOM   2714 N N   . PHE B 1 113 ? 35.994  -6.133  -3.603  1.00 31.92  ? 114 PHE B N   1 
ATOM   2715 C CA  . PHE B 1 113 ? 36.358  -7.418  -4.224  1.00 35.43  ? 114 PHE B CA  1 
ATOM   2716 C C   . PHE B 1 113 ? 37.885  -7.548  -4.261  1.00 36.29  ? 114 PHE B C   1 
ATOM   2717 O O   . PHE B 1 113 ? 38.592  -6.557  -4.578  1.00 37.54  ? 114 PHE B O   1 
ATOM   2718 C CB  . PHE B 1 113 ? 35.690  -7.598  -5.582  1.00 40.34  ? 114 PHE B CB  1 
ATOM   2719 C CG  . PHE B 1 113 ? 34.244  -7.996  -5.508  1.00 34.82  ? 114 PHE B CG  1 
ATOM   2720 C CD1 . PHE B 1 113 ? 33.266  -7.013  -5.483  1.00 38.65  ? 114 PHE B CD1 1 
ATOM   2721 C CD2 . PHE B 1 113 ? 33.852  -9.328  -5.485  1.00 36.28  ? 114 PHE B CD2 1 
ATOM   2722 C CE1 . PHE B 1 113 ? 31.919  -7.347  -5.403  1.00 36.33  ? 114 PHE B CE1 1 
ATOM   2723 C CE2 . PHE B 1 113 ? 32.509  -9.661  -5.367  1.00 38.09  ? 114 PHE B CE2 1 
ATOM   2724 C CZ  . PHE B 1 113 ? 31.541  -8.660  -5.348  1.00 35.06  ? 114 PHE B CZ  1 
ATOM   2725 N N   . GLU B 1 114 ? 38.351  -8.684  -3.754  1.00 43.19  ? 115 GLU B N   1 
ATOM   2726 C CA  . GLU B 1 114 ? 39.684  -9.268  -4.013  1.00 42.48  ? 115 GLU B CA  1 
ATOM   2727 C C   . GLU B 1 114 ? 39.384  -10.467 -4.899  1.00 41.32  ? 115 GLU B C   1 
ATOM   2728 O O   . GLU B 1 114 ? 38.919  -11.502 -4.362  1.00 42.73  ? 115 GLU B O   1 
ATOM   2729 C CB  . GLU B 1 114 ? 40.406  -9.744  -2.769  1.00 43.13  ? 115 GLU B CB  1 
ATOM   2730 C CG  . GLU B 1 114 ? 40.778  -8.660  -1.766  1.00 45.16  ? 115 GLU B CG  1 
ATOM   2731 C CD  . GLU B 1 114 ? 41.941  -7.753  -2.089  1.00 53.44  ? 115 GLU B CD  1 
ATOM   2732 O OE1 . GLU B 1 114 ? 42.499  -7.822  -3.223  1.00 47.50  ? 115 GLU B OE1 1 
ATOM   2733 O OE2 . GLU B 1 114 ? 42.266  -6.956  -1.214  1.00 61.57  ? 115 GLU B OE2 1 
ATOM   2734 N N   . GLY B 1 115 ? 39.609  -10.324 -6.201  1.00 38.03  ? 116 GLY B N   1 
ATOM   2735 C CA  . GLY B 1 115 ? 39.155  -11.349 -7.144  1.00 45.12  ? 116 GLY B CA  1 
ATOM   2736 C C   . GLY B 1 115 ? 37.639  -11.485 -7.085  1.00 45.89  ? 116 GLY B C   1 
ATOM   2737 O O   . GLY B 1 115 ? 36.967  -10.439 -7.183  1.00 45.33  ? 116 GLY B O   1 
ATOM   2738 N N   . ASP B 1 116 ? 37.113  -12.705 -6.918  1.00 48.16  ? 117 ASP B N   1 
ATOM   2739 C CA  . ASP B 1 116 ? 35.636  -12.994 -6.887  1.00 46.96  ? 117 ASP B CA  1 
ATOM   2740 C C   . ASP B 1 116 ? 35.118  -12.992 -5.442  1.00 38.92  ? 117 ASP B C   1 
ATOM   2741 O O   . ASP B 1 116 ? 33.966  -13.369 -5.242  1.00 37.05  ? 117 ASP B O   1 
ATOM   2742 C CB  . ASP B 1 116 ? 35.231  -14.357 -7.463  1.00 50.40  ? 117 ASP B CB  1 
ATOM   2743 C CG  . ASP B 1 116 ? 35.562  -14.602 -8.936  1.00 81.40  ? 117 ASP B CG  1 
ATOM   2744 O OD1 . ASP B 1 116 ? 35.697  -13.603 -9.704  1.00 91.56  ? 117 ASP B OD1 1 
ATOM   2745 O OD2 . ASP B 1 116 ? 35.659  -15.799 -9.324  1.00 89.55  ? 117 ASP B OD2 1 
ATOM   2746 N N   . THR B 1 117 ? 35.926  -12.573 -4.474  1.00 38.09  ? 118 THR B N   1 
ATOM   2747 C CA  . THR B 1 117 ? 35.525  -12.610 -3.050  1.00 43.35  ? 118 THR B CA  1 
ATOM   2748 C C   . THR B 1 117 ? 35.234  -11.183 -2.558  1.00 38.33  ? 118 THR B C   1 
ATOM   2749 O O   . THR B 1 117 ? 36.110  -10.261 -2.747  1.00 32.72  ? 118 THR B O   1 
ATOM   2750 C CB  . THR B 1 117 ? 36.610  -13.309 -2.219  1.00 43.36  ? 118 THR B CB  1 
ATOM   2751 O OG1 . THR B 1 117 ? 36.784  -14.599 -2.804  1.00 42.73  ? 118 THR B OG1 1 
ATOM   2752 C CG2 . THR B 1 117 ? 36.215  -13.443 -0.768  1.00 43.28  ? 118 THR B CG2 1 
ATOM   2753 N N   . LEU B 1 118 ? 34.094  -10.998 -1.890  1.00 34.85  ? 119 LEU B N   1 
ATOM   2754 C CA  . LEU B 1 118 ? 33.808  -9.746  -1.144  1.00 34.05  ? 119 LEU B CA  1 
ATOM   2755 C C   . LEU B 1 118 ? 34.585  -9.763  0.170   1.00 34.66  ? 119 LEU B C   1 
ATOM   2756 O O   . LEU B 1 118 ? 34.410  -10.668 0.979   1.00 32.27  ? 119 LEU B O   1 
ATOM   2757 C CB  . LEU B 1 118 ? 32.294  -9.600  -0.960  1.00 34.58  ? 119 LEU B CB  1 
ATOM   2758 C CG  . LEU B 1 118 ? 31.790  -8.231  -0.532  1.00 33.55  ? 119 LEU B CG  1 
ATOM   2759 C CD1 . LEU B 1 118 ? 32.062  -7.946  0.924   1.00 30.49  ? 119 LEU B CD1 1 
ATOM   2760 C CD2 . LEU B 1 118 ? 32.297  -7.079  -1.407  1.00 32.13  ? 119 LEU B CD2 1 
ATOM   2761 N N   . VAL B 1 119 ? 35.520  -8.826  0.328   1.00 32.86  ? 120 VAL B N   1 
ATOM   2762 C CA  . VAL B 1 119 ? 36.350  -8.730  1.537   1.00 36.26  ? 120 VAL B CA  1 
ATOM   2763 C C   . VAL B 1 119 ? 35.973  -7.499  2.347   1.00 35.67  ? 120 VAL B C   1 
ATOM   2764 O O   . VAL B 1 119 ? 35.783  -6.463  1.773   1.00 37.83  ? 120 VAL B O   1 
ATOM   2765 C CB  . VAL B 1 119 ? 37.838  -8.693  1.168   1.00 38.41  ? 120 VAL B CB  1 
ATOM   2766 C CG1 . VAL B 1 119 ? 38.673  -8.401  2.404   1.00 40.14  ? 120 VAL B CG1 1 
ATOM   2767 C CG2 . VAL B 1 119 ? 38.231  -9.994  0.489   1.00 37.71  ? 120 VAL B CG2 1 
ATOM   2768 N N   . ASN B 1 120 ? 35.884  -7.677  3.653   1.00 34.68  ? 121 ASN B N   1 
ATOM   2769 C CA  . ASN B 1 120 ? 35.632  -6.638  4.658   1.00 33.59  ? 121 ASN B CA  1 
ATOM   2770 C C   . ASN B 1 120 ? 36.851  -6.637  5.585   1.00 36.04  ? 121 ASN B C   1 
ATOM   2771 O O   . ASN B 1 120 ? 36.923  -7.481  6.480   1.00 36.01  ? 121 ASN B O   1 
ATOM   2772 C CB  . ASN B 1 120 ? 34.278  -6.836  5.368   1.00 32.81  ? 121 ASN B CB  1 
ATOM   2773 C CG  . ASN B 1 120 ? 33.956  -5.700  6.289   1.00 35.32  ? 121 ASN B CG  1 
ATOM   2774 O OD1 . ASN B 1 120 ? 34.565  -4.638  6.190   1.00 35.15  ? 121 ASN B OD1 1 
ATOM   2775 N ND2 . ASN B 1 120 ? 33.134  -5.964  7.313   1.00 31.80  ? 121 ASN B ND2 1 
ATOM   2776 N N   . ARG B 1 121 ? 37.765  -5.688  5.381   1.00 37.32  ? 122 ARG B N   1 
ATOM   2777 C CA  . ARG B 1 121 ? 39.033  -5.562  6.117   1.00 36.08  ? 122 ARG B CA  1 
ATOM   2778 C C   . ARG B 1 121 ? 38.875  -4.387  7.060   1.00 32.96  ? 122 ARG B C   1 
ATOM   2779 O O   . ARG B 1 121 ? 38.691  -3.273  6.559   1.00 34.07  ? 122 ARG B O   1 
ATOM   2780 C CB  . ARG B 1 121 ? 40.235  -5.146  5.254   1.00 46.97  ? 122 ARG B CB  1 
ATOM   2781 C CG  . ARG B 1 121 ? 41.274  -6.219  4.986   1.00 60.66  ? 122 ARG B CG  1 
ATOM   2782 C CD  . ARG B 1 121 ? 42.538  -5.697  4.286   1.00 65.65  ? 122 ARG B CD  1 
ATOM   2783 N NE  . ARG B 1 121 ? 42.606  -6.230  2.910   1.00 86.18  ? 122 ARG B NE  1 
ATOM   2784 C CZ  . ARG B 1 121 ? 43.704  -6.631  2.264   1.00 93.09  ? 122 ARG B CZ  1 
ATOM   2785 N NH1 . ARG B 1 121 ? 43.597  -7.132  1.040   1.00 79.96  ? 122 ARG B NH1 1 
ATOM   2786 N NH2 . ARG B 1 121 ? 44.894  -6.556  2.853   1.00 106.84 ? 122 ARG B NH2 1 
ATOM   2787 N N   . ILE B 1 122 ? 38.943  -4.644  8.344   1.00 31.48  ? 123 ILE B N   1 
ATOM   2788 C CA  . ILE B 1 122 ? 38.532  -3.726  9.441   1.00 35.53  ? 123 ILE B CA  1 
ATOM   2789 C C   . ILE B 1 122 ? 39.723  -3.530  10.376  1.00 34.21  ? 123 ILE B C   1 
ATOM   2790 O O   . ILE B 1 122 ? 40.310  -4.536  10.831  1.00 34.72  ? 123 ILE B O   1 
ATOM   2791 C CB  . ILE B 1 122 ? 37.320  -4.274  10.249  1.00 36.09  ? 123 ILE B CB  1 
ATOM   2792 C CG1 . ILE B 1 122 ? 36.195  -4.804  9.367   1.00 34.63  ? 123 ILE B CG1 1 
ATOM   2793 C CG2 . ILE B 1 122 ? 36.806  -3.196  11.197  1.00 39.26  ? 123 ILE B CG2 1 
ATOM   2794 C CD1 . ILE B 1 122 ? 35.481  -5.968  9.907   1.00 43.63  ? 123 ILE B CD1 1 
ATOM   2795 N N   . GLU B 1 123 ? 39.951  -2.277  10.727  1.00 38.05  ? 124 GLU B N   1 
ATOM   2796 C CA  . GLU B 1 123 ? 40.773  -1.843  11.876  1.00 41.32  ? 124 GLU B CA  1 
ATOM   2797 C C   . GLU B 1 123 ? 39.809  -1.242  12.896  1.00 33.54  ? 124 GLU B C   1 
ATOM   2798 O O   . GLU B 1 123 ? 39.009  -0.365  12.544  1.00 37.57  ? 124 GLU B O   1 
ATOM   2799 C CB  . GLU B 1 123 ? 41.796  -0.776  11.464  1.00 47.86  ? 124 GLU B CB  1 
ATOM   2800 C CG  . GLU B 1 123 ? 42.873  -1.249  10.491  1.00 69.81  ? 124 GLU B CG  1 
ATOM   2801 C CD  . GLU B 1 123 ? 43.808  -0.137  9.998   1.00 88.76  ? 124 GLU B CD  1 
ATOM   2802 O OE1 . GLU B 1 123 ? 43.378  0.726   9.155   1.00 73.93  ? 124 GLU B OE1 1 
ATOM   2803 O OE2 . GLU B 1 123 ? 44.969  -0.112  10.474  1.00 103.39 ? 124 GLU B OE2 1 
ATOM   2804 N N   . LEU B 1 124 ? 39.851  -1.732  14.112  1.00 38.10  ? 125 LEU B N   1 
ATOM   2805 C CA  . LEU B 1 124 ? 39.001  -1.223  15.196  1.00 38.95  ? 125 LEU B CA  1 
ATOM   2806 C C   . LEU B 1 124 ? 39.914  -0.737  16.325  1.00 35.79  ? 125 LEU B C   1 
ATOM   2807 O O   . LEU B 1 124 ? 40.696  -1.544  16.838  1.00 35.99  ? 125 LEU B O   1 
ATOM   2808 C CB  . LEU B 1 124 ? 38.115  -2.367  15.672  1.00 36.06  ? 125 LEU B CB  1 
ATOM   2809 C CG  . LEU B 1 124 ? 37.163  -2.036  16.825  1.00 38.14  ? 125 LEU B CG  1 
ATOM   2810 C CD1 . LEU B 1 124 ? 35.939  -2.922  16.744  1.00 35.49  ? 125 LEU B CD1 1 
ATOM   2811 C CD2 . LEU B 1 124 ? 37.809  -2.153  18.194  1.00 40.66  ? 125 LEU B CD2 1 
ATOM   2812 N N   . LYS B 1 125 ? 39.679  0.483   16.790  1.00 42.26  ? 126 LYS B N   1 
ATOM   2813 C CA  . LYS B 1 125 ? 40.377  0.998   18.002  1.00 45.36  ? 126 LYS B CA  1 
ATOM   2814 C C   . LYS B 1 125 ? 39.348  1.400   19.068  1.00 37.28  ? 126 LYS B C   1 
ATOM   2815 O O   . LYS B 1 125 ? 38.478  2.298   18.791  1.00 39.59  ? 126 LYS B O   1 
ATOM   2816 C CB  . LYS B 1 125 ? 41.288  2.170   17.604  1.00 46.82  ? 126 LYS B CB  1 
ATOM   2817 C CG  . LYS B 1 125 ? 42.193  2.667   18.719  1.00 62.74  ? 126 LYS B CG  1 
ATOM   2818 C CD  . LYS B 1 125 ? 43.471  1.836   18.878  1.00 74.09  ? 126 LYS B CD  1 
ATOM   2819 C CE  . LYS B 1 125 ? 44.221  2.052   20.188  1.00 77.51  ? 126 LYS B CE  1 
ATOM   2820 N NZ  . LYS B 1 125 ? 44.202  3.474   20.597  1.00 72.28  ? 126 LYS B NZ  1 
ATOM   2821 N N   . GLY B 1 126 ? 39.437  0.758   20.231  1.00 40.53  ? 127 GLY B N   1 
ATOM   2822 C CA  . GLY B 1 126 ? 38.593  1.080   21.388  1.00 43.18  ? 127 GLY B CA  1 
ATOM   2823 C C   . GLY B 1 126 ? 39.393  1.807   22.473  1.00 45.84  ? 127 GLY B C   1 
ATOM   2824 O O   . GLY B 1 126 ? 40.416  1.236   22.926  1.00 40.03  ? 127 GLY B O   1 
ATOM   2825 N N   . VAL B 1 127 ? 38.879  2.949   22.949  1.00 40.86  ? 128 VAL B N   1 
ATOM   2826 C CA  . VAL B 1 127 ? 39.500  3.717   24.080  1.00 50.32  ? 128 VAL B CA  1 
ATOM   2827 C C   . VAL B 1 127 ? 38.471  4.001   25.180  1.00 48.19  ? 128 VAL B C   1 
ATOM   2828 O O   . VAL B 1 127 ? 37.235  4.096   24.880  1.00 42.92  ? 128 VAL B O   1 
ATOM   2829 C CB  . VAL B 1 127 ? 40.144  5.023   23.570  1.00 42.65  ? 128 VAL B CB  1 
ATOM   2830 C CG1 . VAL B 1 127 ? 41.179  4.707   22.493  1.00 45.05  ? 128 VAL B CG1 1 
ATOM   2831 C CG2 . VAL B 1 127 ? 39.098  6.021   23.062  1.00 45.04  ? 128 VAL B CG2 1 
ATOM   2832 N N   . ASP B 1 128 ? 38.981  4.191   26.402  1.00 47.19  ? 129 ASP B N   1 
ATOM   2833 C CA  . ASP B 1 128 ? 38.240  4.830   27.521  1.00 46.73  ? 129 ASP B CA  1 
ATOM   2834 C C   . ASP B 1 128 ? 37.184  3.850   28.033  1.00 45.12  ? 129 ASP B C   1 
ATOM   2835 O O   . ASP B 1 128 ? 36.191  4.313   28.570  1.00 49.60  ? 129 ASP B O   1 
ATOM   2836 C CB  . ASP B 1 128 ? 37.645  6.168   27.072  1.00 45.46  ? 129 ASP B CB  1 
ATOM   2837 C CG  . ASP B 1 128 ? 38.725  7.213   26.743  1.00 55.19  ? 129 ASP B CG  1 
ATOM   2838 O OD1 . ASP B 1 128 ? 39.967  6.906   26.905  1.00 55.41  ? 129 ASP B OD1 1 
ATOM   2839 O OD2 . ASP B 1 128 ? 38.359  8.299   26.315  1.00 53.53  ? 129 ASP B OD2 1 
ATOM   2840 N N   . PHE B 1 129 ? 37.432  2.548   27.891  1.00 46.16  ? 130 PHE B N   1 
ATOM   2841 C CA  . PHE B 1 129 ? 36.539  1.480   28.419  1.00 48.43  ? 130 PHE B CA  1 
ATOM   2842 C C   . PHE B 1 129 ? 36.900  1.272   29.878  1.00 48.74  ? 130 PHE B C   1 
ATOM   2843 O O   . PHE B 1 129 ? 38.064  1.395   30.160  1.00 44.44  ? 130 PHE B O   1 
ATOM   2844 C CB  . PHE B 1 129 ? 36.630  0.186   27.607  1.00 46.72  ? 130 PHE B CB  1 
ATOM   2845 C CG  . PHE B 1 129 ? 35.918  0.310   26.284  1.00 44.24  ? 130 PHE B CG  1 
ATOM   2846 C CD1 . PHE B 1 129 ? 34.534  0.243   26.218  1.00 53.94  ? 130 PHE B CD1 1 
ATOM   2847 C CD2 . PHE B 1 129 ? 36.613  0.629   25.131  1.00 43.65  ? 130 PHE B CD2 1 
ATOM   2848 C CE1 . PHE B 1 129 ? 33.864  0.422   25.016  1.00 45.16  ? 130 PHE B CE1 1 
ATOM   2849 C CE2 . PHE B 1 129 ? 35.937  0.813   23.927  1.00 47.34  ? 130 PHE B CE2 1 
ATOM   2850 C CZ  . PHE B 1 129 ? 34.568  0.723   23.876  1.00 51.19  ? 130 PHE B CZ  1 
ATOM   2851 N N   . LYS B 1 130 ? 35.923  0.947   30.713  1.00 48.55  ? 131 LYS B N   1 
ATOM   2852 C CA  . LYS B 1 130 ? 36.077  0.582   32.144  1.00 53.26  ? 131 LYS B CA  1 
ATOM   2853 C C   . LYS B 1 130 ? 36.440  -0.898  32.251  1.00 55.20  ? 131 LYS B C   1 
ATOM   2854 O O   . LYS B 1 130 ? 35.732  -1.737  31.644  1.00 50.64  ? 131 LYS B O   1 
ATOM   2855 C CB  . LYS B 1 130 ? 34.771  0.832   32.900  1.00 57.67  ? 131 LYS B CB  1 
ATOM   2856 C CG  . LYS B 1 130 ? 34.228  2.255   32.828  1.00 61.34  ? 131 LYS B CG  1 
ATOM   2857 C CD  . LYS B 1 130 ? 32.869  2.426   33.500  1.00 63.56  ? 131 LYS B CD  1 
ATOM   2858 C CE  . LYS B 1 130 ? 32.384  3.863   33.466  1.00 69.86  ? 131 LYS B CE  1 
ATOM   2859 N NZ  . LYS B 1 130 ? 30.946  3.958   33.838  1.00 68.86  ? 131 LYS B NZ  1 
ATOM   2860 N N   . GLU B 1 131 ? 37.493  -1.227  33.002  1.00 50.79  ? 132 GLU B N   1 
ATOM   2861 C CA  . GLU B 1 131 ? 38.013  -2.627  33.062  1.00 61.05  ? 132 GLU B CA  1 
ATOM   2862 C C   . GLU B 1 131 ? 36.982  -3.535  33.756  1.00 56.06  ? 132 GLU B C   1 
ATOM   2863 O O   . GLU B 1 131 ? 36.990  -4.742  33.495  1.00 63.88  ? 132 GLU B O   1 
ATOM   2864 C CB  . GLU B 1 131 ? 39.408  -2.719  33.710  1.00 68.22  ? 132 GLU B CB  1 
ATOM   2865 C CG  . GLU B 1 131 ? 40.599  -2.526  32.736  1.00 71.90  ? 132 GLU B CG  1 
ATOM   2866 C CD  . GLU B 1 131 ? 40.923  -3.542  31.605  1.00 77.05  ? 132 GLU B CD  1 
ATOM   2867 O OE1 . GLU B 1 131 ? 41.588  -3.120  30.582  1.00 68.08  ? 132 GLU B OE1 1 
ATOM   2868 O OE2 . GLU B 1 131 ? 40.563  -4.764  31.704  1.00 59.05  ? 132 GLU B OE2 1 
ATOM   2869 N N   . ASP B 1 132 ? 36.103  -2.986  34.589  1.00 65.16  ? 133 ASP B N   1 
ATOM   2870 C CA  . ASP B 1 132 ? 35.110  -3.793  35.356  1.00 71.63  ? 133 ASP B CA  1 
ATOM   2871 C C   . ASP B 1 132 ? 33.749  -3.731  34.657  1.00 71.54  ? 133 ASP B C   1 
ATOM   2872 O O   . ASP B 1 132 ? 32.926  -4.620  34.948  1.00 70.62  ? 133 ASP B O   1 
ATOM   2873 C CB  . ASP B 1 132 ? 34.980  -3.288  36.796  1.00 77.73  ? 133 ASP B CB  1 
ATOM   2874 C CG  . ASP B 1 132 ? 34.332  -1.902  36.910  1.00 92.09  ? 133 ASP B CG  1 
ATOM   2875 O OD1 . ASP B 1 132 ? 34.650  -1.007  36.074  1.00 86.27  ? 133 ASP B OD1 1 
ATOM   2876 O OD2 . ASP B 1 132 ? 33.487  -1.716  37.825  1.00 111.82 ? 133 ASP B OD2 1 
ATOM   2877 N N   . GLY B 1 133 ? 33.538  -2.733  33.776  1.00 63.22  ? 134 GLY B N   1 
ATOM   2878 C CA  . GLY B 1 133 ? 32.232  -2.365  33.189  1.00 55.56  ? 134 GLY B CA  1 
ATOM   2879 C C   . GLY B 1 133 ? 31.612  -3.487  32.363  1.00 50.27  ? 134 GLY B C   1 
ATOM   2880 O O   . GLY B 1 133 ? 32.088  -4.663  32.399  1.00 46.08  ? 134 GLY B O   1 
ATOM   2881 N N   . ASN B 1 134 ? 30.570  -3.169  31.614  1.00 48.20  ? 135 ASN B N   1 
ATOM   2882 C CA  . ASN B 1 134 ? 29.750  -4.238  30.995  1.00 48.07  ? 135 ASN B CA  1 
ATOM   2883 C C   . ASN B 1 134 ? 30.424  -4.837  29.773  1.00 41.19  ? 135 ASN B C   1 
ATOM   2884 O O   . ASN B 1 134 ? 30.025  -5.935  29.393  1.00 40.79  ? 135 ASN B O   1 
ATOM   2885 C CB  . ASN B 1 134 ? 28.401  -3.735  30.537  1.00 45.55  ? 135 ASN B CB  1 
ATOM   2886 C CG  . ASN B 1 134 ? 27.649  -3.111  31.671  1.00 46.80  ? 135 ASN B CG  1 
ATOM   2887 O OD1 . ASN B 1 134 ? 27.075  -2.053  31.494  1.00 54.17  ? 135 ASN B OD1 1 
ATOM   2888 N ND2 . ASN B 1 134 ? 27.619  -3.795  32.800  1.00 52.20  ? 135 ASN B ND2 1 
ATOM   2889 N N   . ILE B 1 135 ? 31.353  -4.105  29.155  1.00 42.38  ? 136 ILE B N   1 
ATOM   2890 C CA  . ILE B 1 135 ? 31.968  -4.563  27.890  1.00 44.33  ? 136 ILE B CA  1 
ATOM   2891 C C   . ILE B 1 135 ? 33.213  -5.391  28.231  1.00 42.11  ? 136 ILE B C   1 
ATOM   2892 O O   . ILE B 1 135 ? 33.206  -6.604  27.960  1.00 44.30  ? 136 ILE B O   1 
ATOM   2893 C CB  . ILE B 1 135 ? 32.213  -3.350  26.990  1.00 46.09  ? 136 ILE B CB  1 
ATOM   2894 C CG1 . ILE B 1 135 ? 30.889  -2.833  26.435  1.00 48.00  ? 136 ILE B CG1 1 
ATOM   2895 C CG2 . ILE B 1 135 ? 33.208  -3.676  25.869  1.00 49.38  ? 136 ILE B CG2 1 
ATOM   2896 C CD1 . ILE B 1 135 ? 30.965  -1.417  26.025  1.00 46.88  ? 136 ILE B CD1 1 
ATOM   2897 N N   . LEU B 1 136 ? 34.226  -4.802  28.878  1.00 45.64  ? 137 LEU B N   1 
ATOM   2898 C CA  . LEU B 1 136 ? 35.453  -5.558  29.266  1.00 41.82  ? 137 LEU B CA  1 
ATOM   2899 C C   . LEU B 1 136 ? 35.147  -6.594  30.347  1.00 46.13  ? 137 LEU B C   1 
ATOM   2900 O O   . LEU B 1 136 ? 35.836  -7.636  30.390  1.00 49.51  ? 137 LEU B O   1 
ATOM   2901 C CB  . LEU B 1 136 ? 36.491  -4.556  29.727  1.00 44.60  ? 137 LEU B CB  1 
ATOM   2902 C CG  . LEU B 1 136 ? 37.131  -3.769  28.600  1.00 42.92  ? 137 LEU B CG  1 
ATOM   2903 C CD1 . LEU B 1 136 ? 38.128  -2.777  29.147  1.00 52.39  ? 137 LEU B CD1 1 
ATOM   2904 C CD2 . LEU B 1 136 ? 37.795  -4.707  27.594  1.00 48.26  ? 137 LEU B CD2 1 
ATOM   2905 N N   . GLY B 1 137 ? 34.085  -6.359  31.119  1.00 46.15  ? 138 GLY B N   1 
ATOM   2906 C CA  . GLY B 1 137 ? 33.595  -7.278  32.151  1.00 45.49  ? 138 GLY B CA  1 
ATOM   2907 C C   . GLY B 1 137 ? 32.737  -8.378  31.564  1.00 46.46  ? 138 GLY B C   1 
ATOM   2908 O O   . GLY B 1 137 ? 32.340  -9.260  32.316  1.00 45.21  ? 138 GLY B O   1 
ATOM   2909 N N   . HIS B 1 138 ? 32.437  -8.368  30.264  1.00 43.91  ? 139 HIS B N   1 
ATOM   2910 C CA  . HIS B 1 138 ? 31.563  -9.408  29.639  1.00 41.68  ? 139 HIS B CA  1 
ATOM   2911 C C   . HIS B 1 138 ? 30.200  -9.549  30.365  1.00 42.76  ? 139 HIS B C   1 
ATOM   2912 O O   . HIS B 1 138 ? 29.842  -10.652 30.743  1.00 41.84  ? 139 HIS B O   1 
ATOM   2913 C CB  . HIS B 1 138 ? 32.289  -10.743 29.626  1.00 44.93  ? 139 HIS B CB  1 
ATOM   2914 C CG  . HIS B 1 138 ? 33.469  -10.720 28.728  1.00 49.67  ? 139 HIS B CG  1 
ATOM   2915 N ND1 . HIS B 1 138 ? 33.334  -10.871 27.371  1.00 50.60  ? 139 HIS B ND1 1 
ATOM   2916 C CD2 . HIS B 1 138 ? 34.789  -10.568 28.988  1.00 50.30  ? 139 HIS B CD2 1 
ATOM   2917 C CE1 . HIS B 1 138 ? 34.526  -10.806 26.811  1.00 52.75  ? 139 HIS B CE1 1 
ATOM   2918 N NE2 . HIS B 1 138 ? 35.439  -10.612 27.775  1.00 53.12  ? 139 HIS B NE2 1 
ATOM   2919 N N   . LYS B 1 139 ? 29.424  -8.476  30.492  1.00 40.64  ? 140 LYS B N   1 
ATOM   2920 C CA  . LYS B 1 139 ? 28.110  -8.505  31.190  1.00 47.44  ? 140 LYS B CA  1 
ATOM   2921 C C   . LYS B 1 139 ? 26.941  -8.321  30.230  1.00 43.56  ? 140 LYS B C   1 
ATOM   2922 O O   . LYS B 1 139 ? 25.815  -8.113  30.731  1.00 46.07  ? 140 LYS B O   1 
ATOM   2923 C CB  . LYS B 1 139 ? 28.106  -7.445  32.304  1.00 53.96  ? 140 LYS B CB  1 
ATOM   2924 C CG  . LYS B 1 139 ? 29.260  -7.645  33.277  1.00 55.37  ? 140 LYS B CG  1 
ATOM   2925 C CD  . LYS B 1 139 ? 29.195  -6.905  34.576  1.00 61.44  ? 140 LYS B CD  1 
ATOM   2926 C CE  . LYS B 1 139 ? 30.569  -6.825  35.215  1.00 63.50  ? 140 LYS B CE  1 
ATOM   2927 N NZ  . LYS B 1 139 ? 30.678  -5.644  36.098  1.00 65.35  ? 140 LYS B NZ  1 
ATOM   2928 N N   . LEU B 1 140 ? 27.128  -8.464  28.919  1.00 43.81  ? 141 LEU B N   1 
ATOM   2929 C CA  . LEU B 1 140 ? 26.013  -8.268  27.959  1.00 41.45  ? 141 LEU B CA  1 
ATOM   2930 C C   . LEU B 1 140 ? 25.356  -9.612  27.651  1.00 41.49  ? 141 LEU B C   1 
ATOM   2931 O O   . LEU B 1 140 ? 26.072  -10.639 27.603  1.00 43.66  ? 141 LEU B O   1 
ATOM   2932 C CB  . LEU B 1 140 ? 26.549  -7.576  26.705  1.00 44.09  ? 141 LEU B CB  1 
ATOM   2933 C CG  . LEU B 1 140 ? 27.208  -6.213  26.942  1.00 37.89  ? 141 LEU B CG  1 
ATOM   2934 C CD1 . LEU B 1 140 ? 27.711  -5.627  25.618  1.00 40.86  ? 141 LEU B CD1 1 
ATOM   2935 C CD2 . LEU B 1 140 ? 26.240  -5.224  27.576  1.00 38.30  ? 141 LEU B CD2 1 
ATOM   2936 N N   . GLU B 1 141 ? 24.037  -9.607  27.455  1.00 43.39  ? 142 GLU B N   1 
ATOM   2937 C CA  . GLU B 1 141 ? 23.270  -10.782 26.957  1.00 42.42  ? 142 GLU B CA  1 
ATOM   2938 C C   . GLU B 1 141 ? 23.628  -11.016 25.491  1.00 51.14  ? 142 GLU B C   1 
ATOM   2939 O O   . GLU B 1 141 ? 23.978  -10.041 24.828  1.00 46.54  ? 142 GLU B O   1 
ATOM   2940 C CB  . GLU B 1 141 ? 21.772  -10.582 27.141  1.00 43.83  ? 142 GLU B CB  1 
ATOM   2941 C CG  . GLU B 1 141 ? 21.357  -10.431 28.605  1.00 50.01  ? 142 GLU B CG  1 
ATOM   2942 C CD  . GLU B 1 141 ? 21.498  -11.666 29.475  1.00 61.00  ? 142 GLU B CD  1 
ATOM   2943 O OE1 . GLU B 1 141 ? 21.604  -12.783 28.919  1.00 60.19  ? 142 GLU B OE1 1 
ATOM   2944 O OE2 . GLU B 1 141 ? 21.554  -11.502 30.705  1.00 67.37  ? 142 GLU B OE2 1 
ATOM   2945 N N   . TYR B 1 142 ? 23.688  -12.284 25.097  1.00 58.30  ? 143 TYR B N   1 
ATOM   2946 C CA  . TYR B 1 142 ? 24.262  -12.771 23.816  1.00 67.86  ? 143 TYR B CA  1 
ATOM   2947 C C   . TYR B 1 142 ? 23.026  -12.973 22.951  1.00 66.65  ? 143 TYR B C   1 
ATOM   2948 O O   . TYR B 1 142 ? 22.588  -14.102 22.800  1.00 68.16  ? 143 TYR B O   1 
ATOM   2949 C CB  . TYR B 1 142 ? 25.163  -14.010 23.985  1.00 69.21  ? 143 TYR B CB  1 
ATOM   2950 C CG  . TYR B 1 142 ? 25.657  -14.604 22.680  1.00 81.59  ? 143 TYR B CG  1 
ATOM   2951 C CD1 . TYR B 1 142 ? 26.710  -14.016 21.987  1.00 82.02  ? 143 TYR B CD1 1 
ATOM   2952 C CD2 . TYR B 1 142 ? 25.073  -15.741 22.106  1.00 88.18  ? 143 TYR B CD2 1 
ATOM   2953 C CE1 . TYR B 1 142 ? 27.145  -14.514 20.758  1.00 84.39  ? 143 TYR B CE1 1 
ATOM   2954 C CE2 . TYR B 1 142 ? 25.505  -16.259 20.881  1.00 86.57  ? 143 TYR B CE2 1 
ATOM   2955 C CZ  . TYR B 1 142 ? 26.545  -15.635 20.190  1.00 86.05  ? 143 TYR B CZ  1 
ATOM   2956 O OH  . TYR B 1 142 ? 26.988  -16.068 18.960  1.00 61.32  ? 143 TYR B OH  1 
ATOM   2957 N N   . ASN B 1 143 ? 22.434  -11.876 22.489  1.00 60.64  ? 144 ASN B N   1 
ATOM   2958 C CA  . ASN B 1 143 ? 21.180  -11.937 21.710  1.00 71.66  ? 144 ASN B CA  1 
ATOM   2959 C C   . ASN B 1 143 ? 21.253  -11.016 20.472  1.00 84.26  ? 144 ASN B C   1 
ATOM   2960 O O   . ASN B 1 143 ? 22.196  -10.147 20.341  1.00 60.94  ? 144 ASN B O   1 
ATOM   2961 C CB  . ASN B 1 143 ? 20.000  -11.623 22.612  1.00 73.99  ? 144 ASN B CB  1 
ATOM   2962 C CG  . ASN B 1 143 ? 20.179  -10.254 23.203  1.00 74.02  ? 144 ASN B CG  1 
ATOM   2963 O OD1 . ASN B 1 143 ? 20.988  -9.468  22.715  1.00 85.87  ? 144 ASN B OD1 1 
ATOM   2964 N ND2 . ASN B 1 143 ? 19.473  -9.988  24.276  1.00 74.09  ? 144 ASN B ND2 1 
ATOM   2965 N N   . ALA B 1 144 ? 20.270  -11.222 19.592  1.00 92.57  ? 145 ALA B N   1 
ATOM   2966 C CA  . ALA B 1 144 ? 20.328  -10.878 18.159  1.00 86.30  ? 145 ALA B CA  1 
ATOM   2967 C C   . ALA B 1 144 ? 20.100  -9.378  18.025  1.00 66.12  ? 145 ALA B C   1 
ATOM   2968 O O   . ALA B 1 144 ? 19.200  -8.855  18.671  1.00 65.28  ? 145 ALA B O   1 
ATOM   2969 C CB  . ALA B 1 144 ? 19.330  -11.687 17.365  1.00 95.54  ? 145 ALA B CB  1 
ATOM   2970 N N   . ILE B 1 145 ? 20.935  -8.705  17.241  1.00 49.60  ? 146 ILE B N   1 
ATOM   2971 C CA  . ILE B 1 145 ? 20.804  -7.238  17.134  1.00 45.35  ? 146 ILE B CA  1 
ATOM   2972 C C   . ILE B 1 145 ? 20.315  -6.935  15.716  1.00 46.38  ? 146 ILE B C   1 
ATOM   2973 O O   . ILE B 1 145 ? 21.041  -7.178  14.681  1.00 42.96  ? 146 ILE B O   1 
ATOM   2974 C CB  . ILE B 1 145 ? 22.058  -6.507  17.630  1.00 54.26  ? 146 ILE B CB  1 
ATOM   2975 C CG1 . ILE B 1 145 ? 23.155  -6.562  16.602  1.00 48.69  ? 146 ILE B CG1 1 
ATOM   2976 C CG2 . ILE B 1 145 ? 22.572  -6.958  19.005  1.00 48.90  ? 146 ILE B CG2 1 
ATOM   2977 C CD1 . ILE B 1 145 ? 23.200  -5.299  15.864  1.00 52.44  ? 146 ILE B CD1 1 
ATOM   2978 N N   . SER B 1 146 ? 19.028  -6.603  15.684  1.00 46.33  ? 147 SER B N   1 
ATOM   2979 C CA  . SER B 1 146 ? 18.176  -6.440  14.485  1.00 41.06  ? 147 SER B CA  1 
ATOM   2980 C C   . SER B 1 146 ? 17.720  -4.987  14.472  1.00 43.48  ? 147 SER B C   1 
ATOM   2981 O O   . SER B 1 146 ? 17.842  -4.361  15.475  1.00 42.76  ? 147 SER B O   1 
ATOM   2982 C CB  . SER B 1 146 ? 16.969  -7.371  14.500  1.00 44.75  ? 147 SER B CB  1 
ATOM   2983 O OG  . SER B 1 146 ? 17.388  -8.716  14.372  1.00 41.47  ? 147 SER B OG  1 
ATOM   2984 N N   . GLY B 1 147 ? 17.185  -4.487  13.368  1.00 35.42  ? 148 GLY B N   1 
ATOM   2985 C CA  . GLY B 1 147 ? 16.659  -3.110  13.354  1.00 40.15  ? 148 GLY B CA  1 
ATOM   2986 C C   . GLY B 1 147 ? 17.198  -2.334  12.150  1.00 35.70  ? 148 GLY B C   1 
ATOM   2987 O O   . GLY B 1 147 ? 17.756  -2.942  11.180  1.00 36.96  ? 148 GLY B O   1 
ATOM   2988 N N   . ASN B 1 148 ? 17.059  -1.029  12.233  1.00 37.19  ? 149 ASN B N   1 
ATOM   2989 C CA  . ASN B 1 148 ? 17.013  -0.111  11.066  1.00 39.54  ? 149 ASN B CA  1 
ATOM   2990 C C   . ASN B 1 148 ? 18.250  0.787   11.085  1.00 40.28  ? 149 ASN B C   1 
ATOM   2991 O O   . ASN B 1 148 ? 18.566  1.288   12.125  1.00 40.57  ? 149 ASN B O   1 
ATOM   2992 C CB  . ASN B 1 148 ? 15.737  0.716   11.086  1.00 40.55  ? 149 ASN B CB  1 
ATOM   2993 C CG  . ASN B 1 148 ? 14.538  -0.163  10.848  1.00 38.44  ? 149 ASN B CG  1 
ATOM   2994 O OD1 . ASN B 1 148 ? 14.635  -1.222  10.230  1.00 38.41  ? 149 ASN B OD1 1 
ATOM   2995 N ND2 . ASN B 1 148 ? 13.403  0.297   11.306  1.00 45.62  ? 149 ASN B ND2 1 
ATOM   2996 N N   . ALA B 1 149 ? 18.960  0.886   9.958   1.00 41.68  ? 150 ALA B N   1 
ATOM   2997 C CA  . ALA B 1 149 ? 20.056  1.853   9.754   1.00 42.78  ? 150 ALA B CA  1 
ATOM   2998 C C   . ALA B 1 149 ? 19.516  2.905   8.780   1.00 40.66  ? 150 ALA B C   1 
ATOM   2999 O O   . ALA B 1 149 ? 19.038  2.536   7.691   1.00 41.27  ? 150 ALA B O   1 
ATOM   3000 C CB  . ALA B 1 149 ? 21.281  1.131   9.231   1.00 44.95  ? 150 ALA B CB  1 
ATOM   3001 N N   . ASN B 1 150 ? 19.518  4.173   9.192   1.00 38.54  ? 151 ASN B N   1 
ATOM   3002 C CA  . ASN B 1 150 ? 19.028  5.321   8.382   1.00 44.42  ? 151 ASN B CA  1 
ATOM   3003 C C   . ASN B 1 150 ? 20.174  5.802   7.489   1.00 36.76  ? 151 ASN B C   1 
ATOM   3004 O O   . ASN B 1 150 ? 21.246  6.170   8.042   1.00 39.78  ? 151 ASN B O   1 
ATOM   3005 C CB  . ASN B 1 150 ? 18.540  6.460   9.272   1.00 46.85  ? 151 ASN B CB  1 
ATOM   3006 C CG  . ASN B 1 150 ? 17.662  5.874   10.364  1.00 52.80  ? 151 ASN B CG  1 
ATOM   3007 O OD1 . ASN B 1 150 ? 18.148  5.553   11.487  1.00 46.82  ? 151 ASN B OD1 1 
ATOM   3008 N ND2 . ASN B 1 150 ? 16.414  5.630   9.965   1.00 50.84  ? 151 ASN B ND2 1 
ATOM   3009 N N   . ILE B 1 151 ? 19.925  5.777   6.192   1.00 40.04  ? 152 ILE B N   1 
ATOM   3010 C CA  . ILE B 1 151 ? 20.927  6.100   5.145   1.00 37.52  ? 152 ILE B CA  1 
ATOM   3011 C C   . ILE B 1 151 ? 20.562  7.475   4.572   1.00 33.54  ? 152 ILE B C   1 
ATOM   3012 O O   . ILE B 1 151 ? 19.446  7.616   4.106   1.00 38.06  ? 152 ILE B O   1 
ATOM   3013 C CB  . ILE B 1 151 ? 20.946  5.026   4.038   1.00 38.46  ? 152 ILE B CB  1 
ATOM   3014 C CG1 . ILE B 1 151 ? 21.048  3.603   4.598   1.00 38.24  ? 152 ILE B CG1 1 
ATOM   3015 C CG2 . ILE B 1 151 ? 22.072  5.331   3.050   1.00 36.75  ? 152 ILE B CG2 1 
ATOM   3016 C CD1 . ILE B 1 151 ? 22.303  3.309   5.374   1.00 38.76  ? 152 ILE B CD1 1 
ATOM   3017 N N   . THR B 1 152 ? 21.529  8.388   4.484   1.00 41.52  ? 153 THR B N   1 
ATOM   3018 C CA  . THR B 1 152 ? 21.356  9.665   3.740   1.00 47.41  ? 153 THR B CA  1 
ATOM   3019 C C   . THR B 1 152 ? 22.543  9.897   2.817   1.00 45.84  ? 153 THR B C   1 
ATOM   3020 O O   . THR B 1 152 ? 23.617  9.314   3.045   1.00 37.74  ? 153 THR B O   1 
ATOM   3021 C CB  . THR B 1 152 ? 21.182  10.868  4.671   1.00 49.76  ? 153 THR B CB  1 
ATOM   3022 O OG1 . THR B 1 152 ? 22.418  10.992  5.365   1.00 45.92  ? 153 THR B OG1 1 
ATOM   3023 C CG2 . THR B 1 152 ? 20.004  10.688  5.608   1.00 57.54  ? 153 THR B CG2 1 
ATOM   3024 N N   . ALA B 1 153 ? 22.341  10.657  1.748   1.00 40.41  ? 154 ALA B N   1 
ATOM   3025 C CA  . ALA B 1 153 ? 23.478  10.973  0.852   1.00 40.47  ? 154 ALA B CA  1 
ATOM   3026 C C   . ALA B 1 153 ? 24.391  11.957  1.583   1.00 43.15  ? 154 ALA B C   1 
ATOM   3027 O O   . ALA B 1 153 ? 23.879  12.786  2.367   1.00 46.24  ? 154 ALA B O   1 
ATOM   3028 C CB  . ALA B 1 153 ? 23.019  11.475  -0.490  1.00 43.94  ? 154 ALA B CB  1 
ATOM   3029 N N   . ASP B 1 154 ? 25.692  11.754  1.396   1.00 39.79  ? 155 ASP B N   1 
ATOM   3030 C CA  . ASP B 1 154 ? 26.800  12.685  1.703   1.00 43.53  ? 155 ASP B CA  1 
ATOM   3031 C C   . ASP B 1 154 ? 27.371  13.172  0.356   1.00 45.78  ? 155 ASP B C   1 
ATOM   3032 O O   . ASP B 1 154 ? 28.414  12.628  -0.070  1.00 46.66  ? 155 ASP B O   1 
ATOM   3033 C CB  . ASP B 1 154 ? 27.861  11.994  2.562   1.00 44.10  ? 155 ASP B CB  1 
ATOM   3034 C CG  . ASP B 1 154 ? 28.786  12.976  3.295   1.00 57.14  ? 155 ASP B CG  1 
ATOM   3035 O OD1 . ASP B 1 154 ? 28.921  14.135  2.855   1.00 54.39  ? 155 ASP B OD1 1 
ATOM   3036 O OD2 . ASP B 1 154 ? 29.382  12.573  4.287   1.00 60.07  ? 155 ASP B OD2 1 
ATOM   3037 N N   . LYS B 1 155 ? 26.661  14.066  -0.333  1.00 44.92  ? 156 LYS B N   1 
ATOM   3038 C CA  . LYS B 1 155 ? 27.031  14.575  -1.679  1.00 56.83  ? 156 LYS B CA  1 
ATOM   3039 C C   . LYS B 1 155 ? 28.488  15.081  -1.653  1.00 60.89  ? 156 LYS B C   1 
ATOM   3040 O O   . LYS B 1 155 ? 29.219  14.760  -2.589  1.00 56.22  ? 156 LYS B O   1 
ATOM   3041 C CB  . LYS B 1 155 ? 26.091  15.686  -2.149  1.00 63.94  ? 156 LYS B CB  1 
ATOM   3042 C CG  . LYS B 1 155 ? 26.740  16.536  -3.237  1.00 87.39  ? 156 LYS B CG  1 
ATOM   3043 C CD  . LYS B 1 155 ? 25.851  17.077  -4.324  1.00 95.10  ? 156 LYS B CD  1 
ATOM   3044 C CE  . LYS B 1 155 ? 26.639  17.215  -5.609  1.00 94.68  ? 156 LYS B CE  1 
ATOM   3045 N NZ  . LYS B 1 155 ? 25.814  17.773  -6.698  1.00 97.96  ? 156 LYS B NZ  1 
ATOM   3046 N N   . GLN B 1 156 ? 28.864  15.827  -0.613  1.00 58.94  ? 157 GLN B N   1 
ATOM   3047 C CA  . GLN B 1 156 ? 30.223  16.337  -0.294  1.00 72.56  ? 157 GLN B CA  1 
ATOM   3048 C C   . GLN B 1 156 ? 31.304  15.286  -0.556  1.00 68.12  ? 157 GLN B C   1 
ATOM   3049 O O   . GLN B 1 156 ? 32.307  15.631  -1.162  1.00 73.60  ? 157 GLN B O   1 
ATOM   3050 C CB  . GLN B 1 156 ? 30.259  16.773  1.174   1.00 88.14  ? 157 GLN B CB  1 
ATOM   3051 C CG  . GLN B 1 156 ? 31.665  16.927  1.756   1.00 116.27 ? 157 GLN B CG  1 
ATOM   3052 C CD  . GLN B 1 156 ? 31.707  17.741  3.035   1.00 135.47 ? 157 GLN B CD  1 
ATOM   3053 O OE1 . GLN B 1 156 ? 30.674  18.112  3.602   1.00 159.12 ? 157 GLN B OE1 1 
ATOM   3054 N NE2 . GLN B 1 156 ? 32.915  18.037  3.501   1.00 120.66 ? 157 GLN B NE2 1 
ATOM   3055 N N   . LYS B 1 157 ? 31.148  14.073  -0.035  1.00 64.54  ? 158 LYS B N   1 
ATOM   3056 C CA  . LYS B 1 157 ? 32.194  13.007  -0.047  1.00 60.94  ? 158 LYS B CA  1 
ATOM   3057 C C   . LYS B 1 157 ? 31.865  11.981  -1.154  1.00 47.47  ? 158 LYS B C   1 
ATOM   3058 O O   . LYS B 1 157 ? 32.523  10.952  -1.249  1.00 45.20  ? 158 LYS B O   1 
ATOM   3059 C CB  . LYS B 1 157 ? 32.263  12.338  1.335   1.00 65.71  ? 158 LYS B CB  1 
ATOM   3060 C CG  . LYS B 1 157 ? 32.821  13.192  2.466   1.00 72.51  ? 158 LYS B CG  1 
ATOM   3061 C CD  . LYS B 1 157 ? 34.351  13.271  2.501   1.00 79.96  ? 158 LYS B CD  1 
ATOM   3062 C CE  . LYS B 1 157 ? 34.891  13.724  3.848   1.00 90.56  ? 158 LYS B CE  1 
ATOM   3063 N NZ  . LYS B 1 157 ? 34.091  14.836  4.429   1.00 96.26  ? 158 LYS B NZ  1 
ATOM   3064 N N   . ASN B 1 158 ? 30.796  12.221  -1.906  1.00 46.66  ? 159 ASN B N   1 
ATOM   3065 C CA  . ASN B 1 158 ? 30.374  11.344  -3.018  1.00 47.29  ? 159 ASN B CA  1 
ATOM   3066 C C   . ASN B 1 158 ? 29.966  9.978   -2.427  1.00 45.79  ? 159 ASN B C   1 
ATOM   3067 O O   . ASN B 1 158 ? 30.185  8.933   -3.055  1.00 44.53  ? 159 ASN B O   1 
ATOM   3068 C CB  . ASN B 1 158 ? 31.500  11.277  -4.047  1.00 47.18  ? 159 ASN B CB  1 
ATOM   3069 C CG  . ASN B 1 158 ? 30.949  10.885  -5.381  1.00 45.86  ? 159 ASN B CG  1 
ATOM   3070 O OD1 . ASN B 1 158 ? 29.801  11.192  -5.693  1.00 46.62  ? 159 ASN B OD1 1 
ATOM   3071 N ND2 . ASN B 1 158 ? 31.733  10.128  -6.121  1.00 49.89  ? 159 ASN B ND2 1 
ATOM   3072 N N   . GLY B 1 159 ? 29.345  9.987   -1.248  1.00 45.71  ? 160 GLY B N   1 
ATOM   3073 C CA  . GLY B 1 159 ? 29.129  8.740   -0.488  1.00 42.59  ? 160 GLY B CA  1 
ATOM   3074 C C   . GLY B 1 159 ? 27.835  8.820   0.257   1.00 39.24  ? 160 GLY B C   1 
ATOM   3075 O O   . GLY B 1 159 ? 26.885  9.489   -0.234  1.00 38.52  ? 160 GLY B O   1 
ATOM   3076 N N   . ILE B 1 160 ? 27.818  8.186   1.421   1.00 39.43  ? 161 ILE B N   1 
ATOM   3077 C CA  . ILE B 1 160 ? 26.599  8.088   2.255   1.00 40.03  ? 161 ILE B CA  1 
ATOM   3078 C C   . ILE B 1 160 ? 26.979  8.306   3.720   1.00 37.68  ? 161 ILE B C   1 
ATOM   3079 O O   . ILE B 1 160 ? 28.146  8.161   4.100   1.00 39.44  ? 161 ILE B O   1 
ATOM   3080 C CB  . ILE B 1 160 ? 25.799  6.791   2.030   1.00 38.91  ? 161 ILE B CB  1 
ATOM   3081 C CG1 . ILE B 1 160 ? 26.542  5.511   2.445   1.00 38.46  ? 161 ILE B CG1 1 
ATOM   3082 C CG2 . ILE B 1 160 ? 25.293  6.719   0.595   1.00 41.79  ? 161 ILE B CG2 1 
ATOM   3083 C CD1 . ILE B 1 160 ? 26.518  5.158   3.963   1.00 39.08  ? 161 ILE B CD1 1 
ATOM   3084 N N   . LYS B 1 161 ? 25.977  8.673   4.520   1.00 35.20  ? 162 LYS B N   1 
ATOM   3085 C CA  . LYS B 1 161 ? 26.160  8.703   5.983   1.00 39.24  ? 162 LYS B CA  1 
ATOM   3086 C C   . LYS B 1 161 ? 25.057  7.813   6.533   1.00 35.29  ? 162 LYS B C   1 
ATOM   3087 O O   . LYS B 1 161 ? 24.000  7.699   5.853   1.00 40.93  ? 162 LYS B O   1 
ATOM   3088 C CB  . LYS B 1 161 ? 26.073  10.134  6.522   1.00 43.56  ? 162 LYS B CB  1 
ATOM   3089 C CG  . LYS B 1 161 ? 27.285  11.004  6.260   1.00 57.63  ? 162 LYS B CG  1 
ATOM   3090 C CD  . LYS B 1 161 ? 27.363  12.296  7.102   1.00 79.17  ? 162 LYS B CD  1 
ATOM   3091 C CE  . LYS B 1 161 ? 27.869  12.095  8.526   1.00 87.21  ? 162 LYS B CE  1 
ATOM   3092 N NZ  . LYS B 1 161 ? 26.840  12.432  9.545   1.00 108.51 ? 162 LYS B NZ  1 
ATOM   3093 N N   . ALA B 1 162 ? 25.267  7.293   7.746   1.00 47.63  ? 163 ALA B N   1 
ATOM   3094 C CA  . ALA B 1 162 ? 24.212  6.603   8.537   1.00 43.83  ? 163 ALA B CA  1 
ATOM   3095 C C   . ALA B 1 162 ? 24.387  6.925   10.024  1.00 43.43  ? 163 ALA B C   1 
ATOM   3096 O O   . ALA B 1 162 ? 25.484  7.342   10.490  1.00 39.63  ? 163 ALA B O   1 
ATOM   3097 C CB  . ALA B 1 162 ? 24.230  5.100   8.279   1.00 39.78  ? 163 ALA B CB  1 
ATOM   3098 N N   . TYR B 1 163 ? 23.294  6.757   10.744  1.00 51.35  ? 164 TYR B N   1 
ATOM   3099 C CA  . TYR B 1 163 ? 23.203  6.972   12.210  1.00 50.11  ? 164 TYR B CA  1 
ATOM   3100 C C   . TYR B 1 163 ? 22.099  6.018   12.707  1.00 53.35  ? 164 TYR B C   1 
ATOM   3101 O O   . TYR B 1 163 ? 21.127  5.582   11.977  1.00 45.33  ? 164 TYR B O   1 
ATOM   3102 C CB  . TYR B 1 163 ? 22.997  8.448   12.535  1.00 52.16  ? 164 TYR B CB  1 
ATOM   3103 C CG  . TYR B 1 163 ? 21.651  8.893   12.055  1.00 76.02  ? 164 TYR B CG  1 
ATOM   3104 C CD1 . TYR B 1 163 ? 21.514  9.398   10.764  1.00 83.40  ? 164 TYR B CD1 1 
ATOM   3105 C CD2 . TYR B 1 163 ? 20.498  8.687   12.826  1.00 78.73  ? 164 TYR B CD2 1 
ATOM   3106 C CE1 . TYR B 1 163 ? 20.265  9.755   10.268  1.00 85.93  ? 164 TYR B CE1 1 
ATOM   3107 C CE2 . TYR B 1 163 ? 19.240  9.035   12.343  1.00 66.11  ? 164 TYR B CE2 1 
ATOM   3108 C CZ  . TYR B 1 163 ? 19.134  9.575   11.060  1.00 83.89  ? 164 TYR B CZ  1 
ATOM   3109 O OH  . TYR B 1 163 ? 17.931  9.914   10.510  1.00 79.47  ? 164 TYR B OH  1 
ATOM   3110 N N   . PHE B 1 164 ? 22.330  5.492   13.879  1.00 42.66  ? 165 PHE B N   1 
ATOM   3111 C CA  . PHE B 1 164 ? 21.406  4.507   14.442  1.00 41.97  ? 165 PHE B CA  1 
ATOM   3112 C C   . PHE B 1 164 ? 22.007  4.160   15.787  1.00 37.48  ? 165 PHE B C   1 
ATOM   3113 O O   . PHE B 1 164 ? 23.224  4.384   16.058  1.00 37.81  ? 165 PHE B O   1 
ATOM   3114 C CB  . PHE B 1 164 ? 21.174  3.311   13.508  1.00 40.70  ? 165 PHE B CB  1 
ATOM   3115 C CG  . PHE B 1 164 ? 22.404  2.494   13.190  1.00 37.28  ? 165 PHE B CG  1 
ATOM   3116 C CD1 . PHE B 1 164 ? 22.823  1.471   14.017  1.00 39.28  ? 165 PHE B CD1 1 
ATOM   3117 C CD2 . PHE B 1 164 ? 23.148  2.748   12.028  1.00 38.78  ? 165 PHE B CD2 1 
ATOM   3118 C CE1 . PHE B 1 164 ? 23.938  0.702   13.702  1.00 35.84  ? 165 PHE B CE1 1 
ATOM   3119 C CE2 . PHE B 1 164 ? 24.283  2.005   11.737  1.00 37.02  ? 165 PHE B CE2 1 
ATOM   3120 C CZ  . PHE B 1 164 ? 24.689  1.000   12.594  1.00 38.32  ? 165 PHE B CZ  1 
ATOM   3121 N N   . THR B 1 165 ? 21.127  3.716   16.673  1.00 43.38  ? 166 THR B N   1 
ATOM   3122 C CA  . THR B 1 165 ? 21.488  3.256   18.021  1.00 35.22  ? 166 THR B CA  1 
ATOM   3123 C C   . THR B 1 165 ? 21.197  1.778   18.136  1.00 34.39  ? 166 THR B C   1 
ATOM   3124 O O   . THR B 1 165 ? 20.096  1.355   17.746  1.00 34.58  ? 166 THR B O   1 
ATOM   3125 C CB  . THR B 1 165 ? 20.676  3.988   19.090  1.00 40.38  ? 166 THR B CB  1 
ATOM   3126 O OG1 . THR B 1 165 ? 20.908  5.360   18.765  1.00 38.53  ? 166 THR B OG1 1 
ATOM   3127 C CG2 . THR B 1 165 ? 21.169  3.543   20.451  1.00 37.59  ? 166 THR B CG2 1 
ATOM   3128 N N   . ILE B 1 166 ? 22.149  1.030   18.699  1.00 35.82  ? 167 ILE B N   1 
ATOM   3129 C CA  . ILE B 1 166 ? 21.921  -0.370  19.092  1.00 34.47  ? 167 ILE B CA  1 
ATOM   3130 C C   . ILE B 1 166 ? 21.682  -0.415  20.596  1.00 32.02  ? 167 ILE B C   1 
ATOM   3131 O O   . ILE B 1 166 ? 22.521  0.153   21.316  1.00 36.22  ? 167 ILE B O   1 
ATOM   3132 C CB  . ILE B 1 166 ? 23.098  -1.249  18.692  1.00 31.07  ? 167 ILE B CB  1 
ATOM   3133 C CG1 . ILE B 1 166 ? 23.298  -1.147  17.161  1.00 30.74  ? 167 ILE B CG1 1 
ATOM   3134 C CG2 . ILE B 1 166 ? 22.920  -2.641  19.165  1.00 32.54  ? 167 ILE B CG2 1 
ATOM   3135 C CD1 . ILE B 1 166 ? 22.121  -1.697  16.326  1.00 34.35  ? 167 ILE B CD1 1 
ATOM   3136 N N   . ARG B 1 167 ? 20.682  -1.232  20.990  1.00 30.92  ? 168 ARG B N   1 
ATOM   3137 C CA  . ARG B 1 167 ? 20.323  -1.508  22.395  1.00 32.10  ? 168 ARG B CA  1 
ATOM   3138 C C   . ARG B 1 167 ? 20.975  -2.828  22.806  1.00 32.82  ? 168 ARG B C   1 
ATOM   3139 O O   . ARG B 1 167 ? 20.661  -3.809  22.179  1.00 32.78  ? 168 ARG B O   1 
ATOM   3140 C CB  . ARG B 1 167 ? 18.797  -1.554  22.500  1.00 34.97  ? 168 ARG B CB  1 
ATOM   3141 C CG  . ARG B 1 167 ? 18.096  -0.232  22.231  1.00 35.91  ? 168 ARG B CG  1 
ATOM   3142 C CD  . ARG B 1 167 ? 16.570  -0.329  22.364  1.00 40.23  ? 168 ARG B CD  1 
ATOM   3143 N NE  . ARG B 1 167 ? 16.162  -0.595  23.738  1.00 37.09  ? 168 ARG B NE  1 
ATOM   3144 C CZ  . ARG B 1 167 ? 15.924  -1.789  24.273  1.00 40.08  ? 168 ARG B CZ  1 
ATOM   3145 N NH1 . ARG B 1 167 ? 16.053  -2.913  23.568  1.00 35.98  ? 168 ARG B NH1 1 
ATOM   3146 N NH2 . ARG B 1 167 ? 15.599  -1.855  25.558  1.00 36.20  ? 168 ARG B NH2 1 
ATOM   3147 N N   . HIS B 1 168 ? 21.934  -2.852  23.721  1.00 31.75  ? 169 HIS B N   1 
ATOM   3148 C CA  . HIS B 1 168 ? 22.529  -4.111  24.231  1.00 33.77  ? 169 HIS B CA  1 
ATOM   3149 C C   . HIS B 1 168 ? 21.923  -4.393  25.625  1.00 37.54  ? 169 HIS B C   1 
ATOM   3150 O O   . HIS B 1 168 ? 22.166  -3.581  26.569  1.00 38.10  ? 169 HIS B O   1 
ATOM   3151 C CB  . HIS B 1 168 ? 24.052  -4.063  24.295  1.00 40.26  ? 169 HIS B CB  1 
ATOM   3152 C CG  . HIS B 1 168 ? 24.740  -3.888  22.987  1.00 42.94  ? 169 HIS B CG  1 
ATOM   3153 N ND1 . HIS B 1 168 ? 24.754  -4.898  22.026  1.00 39.86  ? 169 HIS B ND1 1 
ATOM   3154 C CD2 . HIS B 1 168 ? 25.519  -2.877  22.516  1.00 39.42  ? 169 HIS B CD2 1 
ATOM   3155 C CE1 . HIS B 1 168 ? 25.470  -4.469  20.993  1.00 44.05  ? 169 HIS B CE1 1 
ATOM   3156 N NE2 . HIS B 1 168 ? 25.977  -3.251  21.277  1.00 38.03  ? 169 HIS B NE2 1 
ATOM   3157 N N   . ASP B 1 169 ? 21.138  -5.467  25.762  1.00 35.59  ? 170 ASP B N   1 
ATOM   3158 C CA  . ASP B 1 169 ? 20.643  -5.880  27.097  1.00 34.32  ? 170 ASP B CA  1 
ATOM   3159 C C   . ASP B 1 169 ? 21.839  -6.267  27.963  1.00 45.18  ? 170 ASP B C   1 
ATOM   3160 O O   . ASP B 1 169 ? 22.705  -7.014  27.449  1.00 41.83  ? 170 ASP B O   1 
ATOM   3161 C CB  . ASP B 1 169 ? 19.645  -7.014  27.012  1.00 38.34  ? 170 ASP B CB  1 
ATOM   3162 C CG  . ASP B 1 169 ? 18.363  -6.572  26.374  1.00 38.51  ? 170 ASP B CG  1 
ATOM   3163 O OD1 . ASP B 1 169 ? 17.955  -5.409  26.648  1.00 44.51  ? 170 ASP B OD1 1 
ATOM   3164 O OD2 . ASP B 1 169 ? 17.777  -7.399  25.664  1.00 41.88  ? 170 ASP B OD2 1 
ATOM   3165 N N   . VAL B 1 170 ? 21.819  -5.854  29.237  1.00 39.68  ? 171 VAL B N   1 
ATOM   3166 C CA  . VAL B 1 170 ? 22.870  -6.179  30.247  1.00 39.99  ? 171 VAL B CA  1 
ATOM   3167 C C   . VAL B 1 170 ? 22.262  -7.200  31.190  1.00 40.83  ? 171 VAL B C   1 
ATOM   3168 O O   . VAL B 1 170 ? 21.054  -7.137  31.369  1.00 41.32  ? 171 VAL B O   1 
ATOM   3169 C CB  . VAL B 1 170 ? 23.343  -4.918  30.972  1.00 38.28  ? 171 VAL B CB  1 
ATOM   3170 C CG1 . VAL B 1 170 ? 24.524  -5.213  31.870  1.00 40.96  ? 171 VAL B CG1 1 
ATOM   3171 C CG2 . VAL B 1 170 ? 23.670  -3.816  29.973  1.00 39.44  ? 171 VAL B CG2 1 
ATOM   3172 N N   . GLU B 1 171 ? 23.076  -8.082  31.765  1.00 45.53  ? 172 GLU B N   1 
ATOM   3173 C CA  . GLU B 1 171 ? 22.568  -9.235  32.550  1.00 47.77  ? 172 GLU B CA  1 
ATOM   3174 C C   . GLU B 1 171 ? 21.795  -8.740  33.788  1.00 43.79  ? 172 GLU B C   1 
ATOM   3175 O O   . GLU B 1 171 ? 20.891  -9.412  34.198  1.00 46.22  ? 172 GLU B O   1 
ATOM   3176 C CB  . GLU B 1 171 ? 23.715  -10.191 32.844  1.00 51.63  ? 172 GLU B CB  1 
ATOM   3177 C CG  . GLU B 1 171 ? 24.685  -9.645  33.840  1.00 50.77  ? 172 GLU B CG  1 
ATOM   3178 C CD  . GLU B 1 171 ? 26.038  -10.365 33.843  1.00 51.60  ? 172 GLU B CD  1 
ATOM   3179 O OE1 . GLU B 1 171 ? 26.313  -11.283 32.976  1.00 50.74  ? 172 GLU B OE1 1 
ATOM   3180 O OE2 . GLU B 1 171 ? 26.841  -9.965  34.695  1.00 54.59  ? 172 GLU B OE2 1 
ATOM   3181 N N   . ASP B 1 172 ? 22.050  -7.546  34.273  1.00 48.45  ? 173 ASP B N   1 
ATOM   3182 C CA  . ASP B 1 172 ? 21.317  -6.971  35.423  1.00 49.78  ? 173 ASP B CA  1 
ATOM   3183 C C   . ASP B 1 172 ? 20.012  -6.246  35.018  1.00 46.58  ? 173 ASP B C   1 
ATOM   3184 O O   . ASP B 1 172 ? 19.435  -5.604  35.914  1.00 46.63  ? 173 ASP B O   1 
ATOM   3185 C CB  . ASP B 1 172 ? 22.281  -6.076  36.188  1.00 49.56  ? 173 ASP B CB  1 
ATOM   3186 C CG  . ASP B 1 172 ? 22.645  -4.798  35.472  1.00 50.32  ? 173 ASP B CG  1 
ATOM   3187 O OD1 . ASP B 1 172 ? 22.191  -4.612  34.335  1.00 45.66  ? 173 ASP B OD1 1 
ATOM   3188 O OD2 . ASP B 1 172 ? 23.377  -4.018  36.060  1.00 50.79  ? 173 ASP B OD2 1 
ATOM   3189 N N   . GLY B 1 173 ? 19.552  -6.327  33.755  1.00 43.95  ? 174 GLY B N   1 
ATOM   3190 C CA  . GLY B 1 173 ? 18.301  -5.717  33.249  1.00 41.67  ? 174 GLY B CA  1 
ATOM   3191 C C   . GLY B 1 173 ? 18.461  -4.230  32.874  1.00 39.41  ? 174 GLY B C   1 
ATOM   3192 O O   . GLY B 1 173 ? 17.464  -3.620  32.426  1.00 43.58  ? 174 GLY B O   1 
ATOM   3193 N N   . SER B 1 174 ? 19.665  -3.636  33.019  1.00 40.89  ? 175 SER B N   1 
ATOM   3194 C CA  . SER B 1 174 ? 20.016  -2.338  32.360  1.00 39.29  ? 175 SER B CA  1 
ATOM   3195 C C   . SER B 1 174 ? 20.153  -2.499  30.818  1.00 40.26  ? 175 SER B C   1 
ATOM   3196 O O   . SER B 1 174 ? 20.106  -3.619  30.285  1.00 39.20  ? 175 SER B O   1 
ATOM   3197 C CB  . SER B 1 174 ? 21.225  -1.662  32.976  1.00 38.92  ? 175 SER B CB  1 
ATOM   3198 O OG  . SER B 1 174 ? 22.392  -2.453  32.883  1.00 40.00  ? 175 SER B OG  1 
ATOM   3199 N N   . VAL B 1 175 ? 20.278  -1.371  30.141  1.00 36.85  ? 176 VAL B N   1 
ATOM   3200 C CA  . VAL B 1 175 ? 20.435  -1.308  28.679  1.00 38.39  ? 176 VAL B CA  1 
ATOM   3201 C C   . VAL B 1 175 ? 21.662  -0.455  28.361  1.00 40.90  ? 176 VAL B C   1 
ATOM   3202 O O   . VAL B 1 175 ? 21.715  0.705   28.811  1.00 38.37  ? 176 VAL B O   1 
ATOM   3203 C CB  . VAL B 1 175 ? 19.139  -0.824  28.023  1.00 35.57  ? 176 VAL B CB  1 
ATOM   3204 C CG1 . VAL B 1 175 ? 19.291  -0.740  26.503  1.00 37.22  ? 176 VAL B CG1 1 
ATOM   3205 C CG2 . VAL B 1 175 ? 17.973  -1.743  28.408  1.00 36.58  ? 176 VAL B CG2 1 
ATOM   3206 N N   . LEU B 1 176 ? 22.615  -1.041  27.600  1.00 36.88  ? 177 LEU B N   1 
ATOM   3207 C CA  . LEU B 1 176 ? 23.773  -0.274  27.103  1.00 39.24  ? 177 LEU B CA  1 
ATOM   3208 C C   . LEU B 1 176 ? 23.408  0.232   25.712  1.00 33.50  ? 177 LEU B C   1 
ATOM   3209 O O   . LEU B 1 176 ? 23.066  -0.602  24.857  1.00 36.60  ? 177 LEU B O   1 
ATOM   3210 C CB  . LEU B 1 176 ? 24.993  -1.188  27.111  1.00 37.02  ? 177 LEU B CB  1 
ATOM   3211 C CG  . LEU B 1 176 ? 26.247  -0.562  26.513  1.00 43.89  ? 177 LEU B CG  1 
ATOM   3212 C CD1 . LEU B 1 176 ? 26.639  0.678   27.258  1.00 46.14  ? 177 LEU B CD1 1 
ATOM   3213 C CD2 . LEU B 1 176 ? 27.376  -1.576  26.480  1.00 43.36  ? 177 LEU B CD2 1 
ATOM   3214 N N   . LEU B 1 177 ? 23.354  1.535   25.533  1.00 34.94  ? 178 LEU B N   1 
ATOM   3215 C CA  . LEU B 1 177 ? 23.096  2.129   24.207  1.00 34.40  ? 178 LEU B CA  1 
ATOM   3216 C C   . LEU B 1 177 ? 24.425  2.356   23.506  1.00 34.90  ? 178 LEU B C   1 
ATOM   3217 O O   . LEU B 1 177 ? 25.387  2.913   24.117  1.00 34.35  ? 178 LEU B O   1 
ATOM   3218 C CB  . LEU B 1 177 ? 22.237  3.380   24.333  1.00 38.59  ? 178 LEU B CB  1 
ATOM   3219 C CG  . LEU B 1 177 ? 20.853  3.167   24.986  1.00 36.93  ? 178 LEU B CG  1 
ATOM   3220 C CD1 . LEU B 1 177 ? 20.171  4.518   25.178  1.00 41.50  ? 178 LEU B CD1 1 
ATOM   3221 C CD2 . LEU B 1 177 ? 19.973  2.289   24.152  1.00 38.81  ? 178 LEU B CD2 1 
ATOM   3222 N N   . ALA B 1 178 ? 24.451  1.922   22.242  1.00 35.96  ? 179 ALA B N   1 
ATOM   3223 C CA  . ALA B 1 178 ? 25.604  2.058   21.331  1.00 37.70  ? 179 ALA B CA  1 
ATOM   3224 C C   . ALA B 1 178 ? 25.167  2.961   20.184  1.00 34.71  ? 179 ALA B C   1 
ATOM   3225 O O   . ALA B 1 178 ? 24.456  2.494   19.279  1.00 36.05  ? 179 ALA B O   1 
ATOM   3226 C CB  . ALA B 1 178 ? 26.040  0.690   20.871  1.00 38.09  ? 179 ALA B CB  1 
ATOM   3227 N N   . ASP B 1 179 ? 25.607  4.220   20.230  1.00 32.84  ? 180 ASP B N   1 
ATOM   3228 C CA  . ASP B 1 179 ? 25.241  5.277   19.262  1.00 38.46  ? 180 ASP B CA  1 
ATOM   3229 C C   . ASP B 1 179 ? 26.261  5.181   18.131  1.00 32.85  ? 180 ASP B C   1 
ATOM   3230 O O   . ASP B 1 179 ? 27.507  5.385   18.416  1.00 35.78  ? 180 ASP B O   1 
ATOM   3231 C CB  . ASP B 1 179 ? 25.243  6.686   19.878  1.00 41.24  ? 180 ASP B CB  1 
ATOM   3232 C CG  . ASP B 1 179 ? 24.190  6.916   20.959  1.00 50.40  ? 180 ASP B CG  1 
ATOM   3233 O OD1 . ASP B 1 179 ? 23.094  6.317   20.858  1.00 43.52  ? 180 ASP B OD1 1 
ATOM   3234 O OD2 . ASP B 1 179 ? 24.449  7.767   21.837  1.00 50.49  ? 180 ASP B OD2 1 
ATOM   3235 N N   . HIS B 1 180 ? 25.749  4.914   16.936  1.00 34.99  ? 181 HIS B N   1 
ATOM   3236 C CA  . HIS B 1 180 ? 26.564  4.678   15.722  1.00 36.99  ? 181 HIS B CA  1 
ATOM   3237 C C   . HIS B 1 180 ? 26.505  5.929   14.849  1.00 37.62  ? 181 HIS B C   1 
ATOM   3238 O O   . HIS B 1 180 ? 25.401  6.332   14.448  1.00 38.67  ? 181 HIS B O   1 
ATOM   3239 C CB  . HIS B 1 180 ? 26.095  3.468   14.906  1.00 31.85  ? 181 HIS B CB  1 
ATOM   3240 C CG  . HIS B 1 180 ? 26.392  2.150   15.502  1.00 28.49  ? 181 HIS B CG  1 
ATOM   3241 N ND1 . HIS B 1 180 ? 26.006  1.805   16.800  1.00 31.05  ? 181 HIS B ND1 1 
ATOM   3242 C CD2 . HIS B 1 180 ? 27.127  1.113   15.063  1.00 31.39  ? 181 HIS B CD2 1 
ATOM   3243 C CE1 . HIS B 1 180 ? 26.403  0.574   17.077  1.00 31.24  ? 181 HIS B CE1 1 
ATOM   3244 N NE2 . HIS B 1 180 ? 27.066  0.095   16.029  1.00 33.87  ? 181 HIS B NE2 1 
ATOM   3245 N N   . TYR B 1 181 ? 27.679  6.419   14.464  1.00 37.65  ? 182 TYR B N   1 
ATOM   3246 C CA  . TYR B 1 181 ? 27.881  7.465   13.425  1.00 35.20  ? 182 TYR B CA  1 
ATOM   3247 C C   . TYR B 1 181 ? 28.689  6.862   12.276  1.00 32.82  ? 182 TYR B C   1 
ATOM   3248 O O   . TYR B 1 181 ? 29.754  6.333   12.553  1.00 38.95  ? 182 TYR B O   1 
ATOM   3249 C CB  . TYR B 1 181 ? 28.635  8.637   14.072  1.00 39.32  ? 182 TYR B CB  1 
ATOM   3250 C CG  . TYR B 1 181 ? 27.768  9.346   15.077  1.00 49.36  ? 182 TYR B CG  1 
ATOM   3251 C CD1 . TYR B 1 181 ? 26.802  10.243  14.652  1.00 57.10  ? 182 TYR B CD1 1 
ATOM   3252 C CD2 . TYR B 1 181 ? 27.814  9.030   16.425  1.00 45.01  ? 182 TYR B CD2 1 
ATOM   3253 C CE1 . TYR B 1 181 ? 25.956  10.878  15.545  1.00 64.98  ? 182 TYR B CE1 1 
ATOM   3254 C CE2 . TYR B 1 181 ? 26.965  9.644   17.328  1.00 57.97  ? 182 TYR B CE2 1 
ATOM   3255 C CZ  . TYR B 1 181 ? 26.044  10.578  16.890  1.00 67.43  ? 182 TYR B CZ  1 
ATOM   3256 O OH  . TYR B 1 181 ? 25.217  11.200  17.773  1.00 76.87  ? 182 TYR B OH  1 
ATOM   3257 N N   . GLN B 1 182 ? 28.197  6.925   11.059  1.00 36.20  ? 183 GLN B N   1 
ATOM   3258 C CA  . GLN B 1 182 ? 28.799  6.156   9.927   1.00 35.24  ? 183 GLN B CA  1 
ATOM   3259 C C   . GLN B 1 182 ? 28.960  7.074   8.710   1.00 34.06  ? 183 GLN B C   1 
ATOM   3260 O O   . GLN B 1 182 ? 28.020  7.833   8.364   1.00 36.96  ? 183 GLN B O   1 
ATOM   3261 C CB  . GLN B 1 182 ? 27.891  4.989   9.531   1.00 32.99  ? 183 GLN B CB  1 
ATOM   3262 C CG  . GLN B 1 182 ? 28.489  3.964   8.574   1.00 33.62  ? 183 GLN B CG  1 
ATOM   3263 C CD  . GLN B 1 182 ? 27.442  2.966   8.145   1.00 37.47  ? 183 GLN B CD  1 
ATOM   3264 O OE1 . GLN B 1 182 ? 26.642  2.498   8.969   1.00 34.24  ? 183 GLN B OE1 1 
ATOM   3265 N NE2 . GLN B 1 182 ? 27.424  2.647   6.860   1.00 32.73  ? 183 GLN B NE2 1 
ATOM   3266 N N   . GLN B 1 183 ? 30.088  6.929   8.047   1.00 36.29  ? 184 GLN B N   1 
ATOM   3267 C CA  . GLN B 1 183 ? 30.449  7.642   6.802   1.00 40.88  ? 184 GLN B CA  1 
ATOM   3268 C C   . GLN B 1 183 ? 31.006  6.595   5.828   1.00 34.13  ? 184 GLN B C   1 
ATOM   3269 O O   . GLN B 1 183 ? 31.922  5.842   6.230   1.00 35.18  ? 184 GLN B O   1 
ATOM   3270 C CB  . GLN B 1 183 ? 31.477  8.707   7.223   1.00 48.92  ? 184 GLN B CB  1 
ATOM   3271 C CG  . GLN B 1 183 ? 32.303  9.294   6.086   1.00 80.13  ? 184 GLN B CG  1 
ATOM   3272 C CD  . GLN B 1 183 ? 31.677  10.539  5.501   1.00 95.89  ? 184 GLN B CD  1 
ATOM   3273 O OE1 . GLN B 1 183 ? 31.388  11.501  6.219   1.00 99.70  ? 184 GLN B OE1 1 
ATOM   3274 N NE2 . GLN B 1 183 ? 31.447  10.519  4.191   1.00 95.16  ? 184 GLN B NE2 1 
ATOM   3275 N N   . ASN B 1 184 ? 30.553  6.608   4.580   1.00 38.74  ? 185 ASN B N   1 
ATOM   3276 C CA  . ASN B 1 184 ? 31.129  5.670   3.596   1.00 38.84  ? 185 ASN B CA  1 
ATOM   3277 C C   . ASN B 1 184 ? 31.527  6.507   2.381   1.00 34.66  ? 185 ASN B C   1 
ATOM   3278 O O   . ASN B 1 184 ? 30.661  7.346   1.931   1.00 39.67  ? 185 ASN B O   1 
ATOM   3279 C CB  . ASN B 1 184 ? 30.178  4.562   3.139   1.00 37.60  ? 185 ASN B CB  1 
ATOM   3280 C CG  . ASN B 1 184 ? 29.828  3.554   4.220   1.00 40.99  ? 185 ASN B CG  1 
ATOM   3281 O OD1 . ASN B 1 184 ? 29.665  3.934   5.377   1.00 39.26  ? 185 ASN B OD1 1 
ATOM   3282 N ND2 . ASN B 1 184 ? 29.675  2.283   3.841   1.00 35.69  ? 185 ASN B ND2 1 
ATOM   3283 N N   . THR B 1 185 ? 32.691  6.203   1.811   1.00 38.18  ? 186 THR B N   1 
ATOM   3284 C CA  . THR B 1 185 ? 33.222  6.938   0.603   1.00 38.06  ? 186 THR B CA  1 
ATOM   3285 C C   . THR B 1 185 ? 33.736  5.939   -0.421  1.00 36.03  ? 186 THR B C   1 
ATOM   3286 O O   . THR B 1 185 ? 34.307  4.940   -0.056  1.00 36.67  ? 186 THR B O   1 
ATOM   3287 C CB  . THR B 1 185 ? 34.304  7.921   1.084   1.00 37.38  ? 186 THR B CB  1 
ATOM   3288 O OG1 . THR B 1 185 ? 35.290  7.166   1.746   1.00 47.26  ? 186 THR B OG1 1 
ATOM   3289 C CG2 . THR B 1 185 ? 33.887  8.889   2.160   1.00 44.66  ? 186 THR B CG2 1 
ATOM   3290 N N   . PRO B 1 186 ? 33.546  6.161   -1.732  1.00 35.70  ? 187 PRO B N   1 
ATOM   3291 C CA  . PRO B 1 186 ? 34.039  5.237   -2.728  1.00 41.12  ? 187 PRO B CA  1 
ATOM   3292 C C   . PRO B 1 186 ? 35.573  5.158   -2.674  1.00 36.95  ? 187 PRO B C   1 
ATOM   3293 O O   . PRO B 1 186 ? 36.147  6.132   -2.428  1.00 40.97  ? 187 PRO B O   1 
ATOM   3294 C CB  . PRO B 1 186 ? 33.581  5.849   -4.064  1.00 36.92  ? 187 PRO B CB  1 
ATOM   3295 C CG  . PRO B 1 186 ? 32.581  6.902   -3.730  1.00 41.78  ? 187 PRO B CG  1 
ATOM   3296 C CD  . PRO B 1 186 ? 32.873  7.324   -2.316  1.00 41.87  ? 187 PRO B CD  1 
ATOM   3297 N N   . ILE B 1 187 ? 36.141  4.008   -2.959  1.00 37.88  ? 188 ILE B N   1 
ATOM   3298 C CA  . ILE B 1 187 ? 37.614  3.787   -3.103  1.00 40.70  ? 188 ILE B CA  1 
ATOM   3299 C C   . ILE B 1 187 ? 38.034  4.156   -4.536  1.00 43.84  ? 188 ILE B C   1 
ATOM   3300 O O   . ILE B 1 187 ? 39.025  4.839   -4.683  1.00 44.79  ? 188 ILE B O   1 
ATOM   3301 C CB  . ILE B 1 187 ? 38.024  2.362   -2.719  1.00 45.16  ? 188 ILE B CB  1 
ATOM   3302 C CG1 . ILE B 1 187 ? 37.887  2.215   -1.200  1.00 42.81  ? 188 ILE B CG1 1 
ATOM   3303 C CG2 . ILE B 1 187 ? 39.446  2.019   -3.243  1.00 44.17  ? 188 ILE B CG2 1 
ATOM   3304 C CD1 . ILE B 1 187 ? 37.997  0.807   -0.686  1.00 46.40  ? 188 ILE B CD1 1 
ATOM   3305 N N   . GLY B 1 188 ? 37.273  3.733   -5.527  1.00 45.66  ? 189 GLY B N   1 
ATOM   3306 C CA  . GLY B 1 188 ? 37.525  4.056   -6.948  1.00 50.64  ? 189 GLY B CA  1 
ATOM   3307 C C   . GLY B 1 188 ? 37.022  5.455   -7.310  1.00 47.17  ? 189 GLY B C   1 
ATOM   3308 O O   . GLY B 1 188 ? 36.495  6.210   -6.450  1.00 49.77  ? 189 GLY B O   1 
ATOM   3309 N N   . ASP B 1 189 ? 37.173  5.841   -8.562  1.00 49.66  ? 190 ASP B N   1 
ATOM   3310 C CA  . ASP B 1 189 ? 36.677  7.155   -9.060  1.00 52.89  ? 190 ASP B CA  1 
ATOM   3311 C C   . ASP B 1 189 ? 35.640  6.837   -10.142 1.00 51.21  ? 190 ASP B C   1 
ATOM   3312 O O   . ASP B 1 189 ? 35.378  7.672   -10.996 1.00 51.67  ? 190 ASP B O   1 
ATOM   3313 C CB  . ASP B 1 189 ? 37.869  8.074   -9.413  1.00 64.05  ? 190 ASP B CB  1 
ATOM   3314 C CG  . ASP B 1 189 ? 38.974  7.446   -10.255 1.00 69.83  ? 190 ASP B CG  1 
ATOM   3315 O OD1 . ASP B 1 189 ? 38.675  6.521   -11.059 1.00 66.85  ? 190 ASP B OD1 1 
ATOM   3316 O OD2 . ASP B 1 189 ? 40.124  7.903   -10.115 1.00 87.05  ? 190 ASP B OD2 1 
ATOM   3317 N N   . GLY B 1 190 ? 35.082  5.621   -10.106 1.00 50.97  ? 191 GLY B N   1 
ATOM   3318 C CA  . GLY B 1 190 ? 33.976  5.232   -10.985 1.00 40.66  ? 191 GLY B CA  1 
ATOM   3319 C C   . GLY B 1 190 ? 32.747  6.019   -10.586 1.00 42.76  ? 191 GLY B C   1 
ATOM   3320 O O   . GLY B 1 190 ? 32.779  6.722   -9.586  1.00 44.37  ? 191 GLY B O   1 
ATOM   3321 N N   . PRO B 1 191 ? 31.652  5.931   -11.364 1.00 43.59  ? 192 PRO B N   1 
ATOM   3322 C CA  . PRO B 1 191 ? 30.412  6.620   -11.019 1.00 45.89  ? 192 PRO B CA  1 
ATOM   3323 C C   . PRO B 1 191 ? 29.745  5.845   -9.873  1.00 41.41  ? 192 PRO B C   1 
ATOM   3324 O O   . PRO B 1 191 ? 29.917  4.651   -9.888  1.00 40.04  ? 192 PRO B O   1 
ATOM   3325 C CB  . PRO B 1 191 ? 29.569  6.508   -12.279 1.00 44.01  ? 192 PRO B CB  1 
ATOM   3326 C CG  . PRO B 1 191 ? 30.036  5.190   -12.887 1.00 49.01  ? 192 PRO B CG  1 
ATOM   3327 C CD  . PRO B 1 191 ? 31.516  5.100   -12.566 1.00 46.40  ? 192 PRO B CD  1 
ATOM   3328 N N   . VAL B 1 192 ? 28.961  6.525   -9.038  1.00 41.80  ? 193 VAL B N   1 
ATOM   3329 C CA  . VAL B 1 192 ? 28.237  5.945   -7.856  1.00 42.61  ? 193 VAL B CA  1 
ATOM   3330 C C   . VAL B 1 192 ? 26.794  6.440   -7.813  1.00 41.47  ? 193 VAL B C   1 
ATOM   3331 O O   . VAL B 1 192 ? 26.470  7.395   -8.482  1.00 37.06  ? 193 VAL B O   1 
ATOM   3332 C CB  . VAL B 1 192 ? 28.994  6.262   -6.566  1.00 40.53  ? 193 VAL B CB  1 
ATOM   3333 C CG1 . VAL B 1 192 ? 30.375  5.645   -6.621  1.00 43.59  ? 193 VAL B CG1 1 
ATOM   3334 C CG2 . VAL B 1 192 ? 29.050  7.747   -6.276  1.00 39.42  ? 193 VAL B CG2 1 
ATOM   3335 N N   . LEU B 1 193 ? 25.919  5.746   -7.095  1.00 37.91  ? 194 LEU B N   1 
ATOM   3336 C CA  . LEU B 1 193 ? 24.498  6.132   -6.952  1.00 38.47  ? 194 LEU B CA  1 
ATOM   3337 C C   . LEU B 1 193 ? 24.396  6.806   -5.591  1.00 44.57  ? 194 LEU B C   1 
ATOM   3338 O O   . LEU B 1 193 ? 24.883  6.209   -4.591  1.00 42.37  ? 194 LEU B O   1 
ATOM   3339 C CB  . LEU B 1 193 ? 23.603  4.899   -7.098  1.00 36.05  ? 194 LEU B CB  1 
ATOM   3340 C CG  . LEU B 1 193 ? 23.589  4.237   -8.474  1.00 37.42  ? 194 LEU B CG  1 
ATOM   3341 C CD1 . LEU B 1 193 ? 22.832  2.913   -8.374  1.00 38.23  ? 194 LEU B CD1 1 
ATOM   3342 C CD2 . LEU B 1 193 ? 22.941  5.143   -9.535  1.00 40.63  ? 194 LEU B CD2 1 
ATOM   3343 N N   . LEU B 1 194 ? 23.963  8.065   -5.567  1.00 37.84  ? 195 LEU B N   1 
ATOM   3344 C CA  . LEU B 1 194 ? 23.766  8.839   -4.321  1.00 43.78  ? 195 LEU B CA  1 
ATOM   3345 C C   . LEU B 1 194 ? 22.287  8.700   -4.023  1.00 42.66  ? 195 LEU B C   1 
ATOM   3346 O O   . LEU B 1 194 ? 21.469  8.995   -4.881  1.00 43.83  ? 195 LEU B O   1 
ATOM   3347 C CB  . LEU B 1 194 ? 24.193  10.300  -4.496  1.00 44.42  ? 195 LEU B CB  1 
ATOM   3348 C CG  . LEU B 1 194 ? 25.677  10.499  -4.771  1.00 58.43  ? 195 LEU B CG  1 
ATOM   3349 C CD1 . LEU B 1 194 ? 26.051  11.991  -4.762  1.00 57.34  ? 195 LEU B CD1 1 
ATOM   3350 C CD2 . LEU B 1 194 ? 26.518  9.704   -3.765  1.00 57.01  ? 195 LEU B CD2 1 
ATOM   3351 N N   . PRO B 1 195 ? 21.909  8.115   -2.867  1.00 37.69  ? 196 PRO B N   1 
ATOM   3352 C CA  . PRO B 1 195 ? 20.527  7.742   -2.642  1.00 42.05  ? 196 PRO B CA  1 
ATOM   3353 C C   . PRO B 1 195 ? 19.715  8.915   -2.071  1.00 37.71  ? 196 PRO B C   1 
ATOM   3354 O O   . PRO B 1 195 ? 20.276  9.711   -1.367  1.00 40.58  ? 196 PRO B O   1 
ATOM   3355 C CB  . PRO B 1 195 ? 20.657  6.677   -1.530  1.00 38.57  ? 196 PRO B CB  1 
ATOM   3356 C CG  . PRO B 1 195 ? 21.876  7.115   -0.725  1.00 35.46  ? 196 PRO B CG  1 
ATOM   3357 C CD  . PRO B 1 195 ? 22.781  7.783   -1.740  1.00 38.07  ? 196 PRO B CD  1 
ATOM   3358 N N   . ASP B 1 196 ? 18.424  8.910   -2.344  1.00 36.44  ? 197 ASP B N   1 
ATOM   3359 C CA  . ASP B 1 196 ? 17.400  9.572   -1.501  1.00 42.43  ? 197 ASP B CA  1 
ATOM   3360 C C   . ASP B 1 196 ? 17.374  8.865   -0.143  1.00 47.62  ? 197 ASP B C   1 
ATOM   3361 O O   . ASP B 1 196 ? 17.756  7.662   -0.049  1.00 43.29  ? 197 ASP B O   1 
ATOM   3362 C CB  . ASP B 1 196 ? 15.999  9.479   -2.113  1.00 44.38  ? 197 ASP B CB  1 
ATOM   3363 C CG  . ASP B 1 196 ? 15.771  10.384  -3.306  1.00 45.12  ? 197 ASP B CG  1 
ATOM   3364 O OD1 . ASP B 1 196 ? 16.568  11.274  -3.470  1.00 47.60  ? 197 ASP B OD1 1 
ATOM   3365 O OD2 . ASP B 1 196 ? 14.808  10.167  -4.052  1.00 50.40  ? 197 ASP B OD2 1 
ATOM   3366 N N   . ASN B 1 197 ? 16.856  9.560   0.857   1.00 42.79  ? 198 ASN B N   1 
ATOM   3367 C CA  . ASN B 1 197 ? 16.739  9.032   2.238   1.00 45.56  ? 198 ASN B CA  1 
ATOM   3368 C C   . ASN B 1 197 ? 15.960  7.724   2.193   1.00 37.33  ? 198 ASN B C   1 
ATOM   3369 O O   . ASN B 1 197 ? 14.917  7.597   1.466   1.00 42.72  ? 198 ASN B O   1 
ATOM   3370 C CB  . ASN B 1 197 ? 16.174  10.062  3.213   1.00 46.51  ? 198 ASN B CB  1 
ATOM   3371 C CG  . ASN B 1 197 ? 17.174  11.168  3.453   1.00 49.17  ? 198 ASN B CG  1 
ATOM   3372 O OD1 . ASN B 1 197 ? 18.201  11.244  2.787   1.00 52.38  ? 198 ASN B OD1 1 
ATOM   3373 N ND2 . ASN B 1 197 ? 16.915  12.008  4.440   1.00 52.51  ? 198 ASN B ND2 1 
ATOM   3374 N N   . HIS B 1 198 ? 16.514  6.744   2.900   1.00 41.41  ? 199 HIS B N   1 
ATOM   3375 C CA  . HIS B 1 198 ? 15.914  5.406   3.083   1.00 40.00  ? 199 HIS B CA  1 
ATOM   3376 C C   . HIS B 1 198 ? 16.595  4.731   4.273   1.00 35.95  ? 199 HIS B C   1 
ATOM   3377 O O   . HIS B 1 198 ? 17.448  5.347   5.006   1.00 43.01  ? 199 HIS B O   1 
ATOM   3378 C CB  . HIS B 1 198 ? 15.999  4.582   1.802   1.00 41.56  ? 199 HIS B CB  1 
ATOM   3379 C CG  . HIS B 1 198 ? 17.401  4.159   1.460   1.00 40.81  ? 199 HIS B CG  1 
ATOM   3380 N ND1 . HIS B 1 198 ? 18.306  5.041   0.888   1.00 40.99  ? 199 HIS B ND1 1 
ATOM   3381 C CD2 . HIS B 1 198 ? 18.064  2.990   1.617   1.00 43.60  ? 199 HIS B CD2 1 
ATOM   3382 C CE1 . HIS B 1 198 ? 19.466  4.424   0.700   1.00 43.50  ? 199 HIS B CE1 1 
ATOM   3383 N NE2 . HIS B 1 198 ? 19.358  3.177   1.160   1.00 40.68  ? 199 HIS B NE2 1 
ATOM   3384 N N   . TYR B 1 199 ? 16.182  3.506   4.521   1.00 39.64  ? 200 TYR B N   1 
ATOM   3385 C CA  . TYR B 1 199 ? 16.748  2.730   5.631   1.00 35.76  ? 200 TYR B CA  1 
ATOM   3386 C C   . TYR B 1 199 ? 16.942  1.275   5.185   1.00 33.17  ? 200 TYR B C   1 
ATOM   3387 O O   . TYR B 1 199 ? 16.304  0.767   4.229   1.00 37.45  ? 200 TYR B O   1 
ATOM   3388 C CB  . TYR B 1 199 ? 15.895  2.877   6.900   1.00 39.06  ? 200 TYR B CB  1 
ATOM   3389 C CG  . TYR B 1 199 ? 14.546  2.194   6.871   1.00 38.66  ? 200 TYR B CG  1 
ATOM   3390 C CD1 . TYR B 1 199 ? 13.401  2.870   6.441   1.00 42.73  ? 200 TYR B CD1 1 
ATOM   3391 C CD2 . TYR B 1 199 ? 14.399  0.899   7.350   1.00 42.70  ? 200 TYR B CD2 1 
ATOM   3392 C CE1 . TYR B 1 199 ? 12.148  2.277   6.479   1.00 45.85  ? 200 TYR B CE1 1 
ATOM   3393 C CE2 . TYR B 1 199 ? 13.159  0.276   7.352   1.00 43.79  ? 200 TYR B CE2 1 
ATOM   3394 C CZ  . TYR B 1 199 ? 12.030  0.983   6.966   1.00 48.06  ? 200 TYR B CZ  1 
ATOM   3395 O OH  . TYR B 1 199 ? 10.822  0.365   6.999   1.00 49.26  ? 200 TYR B OH  1 
ATOM   3396 N N   . LEU B 1 200 ? 17.834  0.609   5.919   1.00 34.04  ? 201 LEU B N   1 
ATOM   3397 C CA  . LEU B 1 200 ? 18.097  -0.837  5.756   1.00 34.47  ? 201 LEU B CA  1 
ATOM   3398 C C   . LEU B 1 200 ? 17.573  -1.518  7.023   1.00 33.23  ? 201 LEU B C   1 
ATOM   3399 O O   . LEU B 1 200 ? 17.902  -1.050  8.118   1.00 38.00  ? 201 LEU B O   1 
ATOM   3400 C CB  . LEU B 1 200 ? 19.599  -1.068  5.596   1.00 35.28  ? 201 LEU B CB  1 
ATOM   3401 C CG  . LEU B 1 200 ? 20.272  -0.445  4.371   1.00 29.28  ? 201 LEU B CG  1 
ATOM   3402 C CD1 . LEU B 1 200 ? 21.741  -0.885  4.354   1.00 37.32  ? 201 LEU B CD1 1 
ATOM   3403 C CD2 . LEU B 1 200 ? 19.590  -0.839  3.094   1.00 34.56  ? 201 LEU B CD2 1 
ATOM   3404 N N   . SER B 1 201 ? 16.774  -2.551  6.821   1.00 35.73  ? 202 SER B N   1 
ATOM   3405 C CA  . SER B 1 201 ? 16.142  -3.386  7.859   1.00 37.16  ? 202 SER B CA  1 
ATOM   3406 C C   . SER B 1 201 ? 16.915  -4.697  7.973   1.00 32.30  ? 202 SER B C   1 
ATOM   3407 O O   . SER B 1 201 ? 16.905  -5.492  7.024   1.00 37.88  ? 202 SER B O   1 
ATOM   3408 C CB  . SER B 1 201 ? 14.731  -3.633  7.491   1.00 39.73  ? 202 SER B CB  1 
ATOM   3409 O OG  . SER B 1 201 ? 14.107  -4.270  8.567   1.00 46.13  ? 202 SER B OG  1 
ATOM   3410 N N   . THR B 1 202 ? 17.559  -4.895  9.101   1.00 34.08  ? 203 THR B N   1 
ATOM   3411 C CA  . THR B 1 202 ? 18.340  -6.102  9.372   1.00 35.18  ? 203 THR B CA  1 
ATOM   3412 C C   . THR B 1 202 ? 17.558  -7.010  10.350  1.00 33.86  ? 203 THR B C   1 
ATOM   3413 O O   . THR B 1 202 ? 17.145  -6.535  11.460  1.00 37.98  ? 203 THR B O   1 
ATOM   3414 C CB  . THR B 1 202 ? 19.732  -5.799  9.933   1.00 37.73  ? 203 THR B CB  1 
ATOM   3415 O OG1 . THR B 1 202 ? 20.479  -5.142  8.923   1.00 38.26  ? 203 THR B OG1 1 
ATOM   3416 C CG2 . THR B 1 202 ? 20.488  -7.068  10.247  1.00 37.75  ? 203 THR B CG2 1 
ATOM   3417 N N   . GLN B 1 203 ? 17.347  -8.227  9.904   1.00 34.54  ? 204 GLN B N   1 
ATOM   3418 C CA  . GLN B 1 203 ? 16.861  -9.354  10.745  1.00 43.23  ? 204 GLN B CA  1 
ATOM   3419 C C   . GLN B 1 203 ? 18.066  -10.276 10.962  1.00 39.50  ? 204 GLN B C   1 
ATOM   3420 O O   . GLN B 1 203 ? 18.498  -10.856 9.959   1.00 44.32  ? 204 GLN B O   1 
ATOM   3421 C CB  . GLN B 1 203 ? 15.700  -10.046 10.005  1.00 52.23  ? 204 GLN B CB  1 
ATOM   3422 C CG  . GLN B 1 203 ? 14.724  -10.805 10.909  1.00 77.26  ? 204 GLN B CG  1 
ATOM   3423 C CD  . GLN B 1 203 ? 14.783  -12.319 10.800  1.00 88.73  ? 204 GLN B CD  1 
ATOM   3424 O OE1 . GLN B 1 203 ? 15.777  -12.963 11.168  1.00 104.44 ? 204 GLN B OE1 1 
ATOM   3425 N NE2 . GLN B 1 203 ? 13.690  -12.917 10.335  1.00 73.83  ? 204 GLN B NE2 1 
ATOM   3426 N N   . SER B 1 204 ? 18.530  -10.420 12.210  1.00 39.64  ? 205 SER B N   1 
ATOM   3427 C CA  . SER B 1 204 ? 19.749  -11.188 12.585  1.00 43.23  ? 205 SER B CA  1 
ATOM   3428 C C   . SER B 1 204 ? 19.427  -12.367 13.514  1.00 47.92  ? 205 SER B C   1 
ATOM   3429 O O   . SER B 1 204 ? 18.666  -12.202 14.445  1.00 41.43  ? 205 SER B O   1 
ATOM   3430 C CB  . SER B 1 204 ? 20.755  -10.285 13.214  1.00 43.37  ? 205 SER B CB  1 
ATOM   3431 O OG  . SER B 1 204 ? 21.943  -11.002 13.514  1.00 44.83  ? 205 SER B OG  1 
ATOM   3432 N N   . LYS B 1 205 ? 19.971  -13.537 13.225  1.00 47.45  ? 206 LYS B N   1 
ATOM   3433 C CA  . LYS B 1 205 ? 19.847  -14.709 14.109  1.00 47.45  ? 206 LYS B CA  1 
ATOM   3434 C C   . LYS B 1 205 ? 21.260  -15.222 14.362  1.00 48.87  ? 206 LYS B C   1 
ATOM   3435 O O   . LYS B 1 205 ? 21.969  -15.477 13.403  1.00 43.90  ? 206 LYS B O   1 
ATOM   3436 C CB  . LYS B 1 205 ? 18.948  -15.763 13.468  1.00 53.21  ? 206 LYS B CB  1 
ATOM   3437 C CG  . LYS B 1 205 ? 18.466  -16.855 14.414  1.00 65.23  ? 206 LYS B CG  1 
ATOM   3438 C CD  . LYS B 1 205 ? 17.892  -18.056 13.692  1.00 78.06  ? 206 LYS B CD  1 
ATOM   3439 C CE  . LYS B 1 205 ? 18.995  -18.963 13.177  1.00 90.45  ? 206 LYS B CE  1 
ATOM   3440 N NZ  . LYS B 1 205 ? 18.501  -19.958 12.195  1.00 88.06  ? 206 LYS B NZ  1 
ATOM   3441 N N   . GLN B 1 206 ? 21.613  -15.344 15.622  1.00 43.84  ? 207 GLN B N   1 
ATOM   3442 C CA  . GLN B 1 206 ? 22.955  -15.686 16.137  1.00 46.66  ? 207 GLN B CA  1 
ATOM   3443 C C   . GLN B 1 206 ? 22.928  -17.063 16.770  1.00 52.01  ? 207 GLN B C   1 
ATOM   3444 O O   . GLN B 1 206 ? 21.906  -17.396 17.372  1.00 45.06  ? 207 GLN B O   1 
ATOM   3445 C CB  . GLN B 1 206 ? 23.228  -14.602 17.156  1.00 55.98  ? 207 GLN B CB  1 
ATOM   3446 C CG  . GLN B 1 206 ? 24.545  -14.646 17.892  1.00 60.21  ? 207 GLN B CG  1 
ATOM   3447 C CD  . GLN B 1 206 ? 24.687  -13.222 18.385  1.00 72.39  ? 207 GLN B CD  1 
ATOM   3448 O OE1 . GLN B 1 206 ? 24.235  -12.265 17.727  1.00 59.81  ? 207 GLN B OE1 1 
ATOM   3449 N NE2 . GLN B 1 206 ? 25.232  -13.054 19.575  1.00 63.37  ? 207 GLN B NE2 1 
ATOM   3450 N N   . SER B 1 207 ? 24.008  -17.815 16.648  1.00 49.40  ? 208 SER B N   1 
ATOM   3451 C CA  . SER B 1 207 ? 24.128  -19.194 17.187  1.00 53.14  ? 208 SER B CA  1 
ATOM   3452 C C   . SER B 1 207 ? 25.600  -19.529 17.403  1.00 57.60  ? 208 SER B C   1 
ATOM   3453 O O   . SER B 1 207 ? 26.487  -18.622 17.214  1.00 50.89  ? 208 SER B O   1 
ATOM   3454 C CB  . SER B 1 207 ? 23.508  -20.176 16.263  1.00 42.60  ? 208 SER B CB  1 
ATOM   3455 O OG  . SER B 1 207 ? 23.843  -19.840 14.946  1.00 48.61  ? 208 SER B OG  1 
ATOM   3456 N N   . LYS B 1 208 ? 25.826  -20.754 17.855  1.00 56.70  ? 209 LYS B N   1 
ATOM   3457 C CA  . LYS B 1 208 ? 27.157  -21.333 18.150  1.00 61.16  ? 209 LYS B CA  1 
ATOM   3458 C C   . LYS B 1 208 ? 27.217  -22.626 17.349  1.00 54.31  ? 209 LYS B C   1 
ATOM   3459 O O   . LYS B 1 208 ? 26.144  -23.216 17.114  1.00 57.87  ? 209 LYS B O   1 
ATOM   3460 C CB  . LYS B 1 208 ? 27.380  -21.539 19.660  1.00 58.39  ? 209 LYS B CB  1 
ATOM   3461 C CG  . LYS B 1 208 ? 27.288  -20.276 20.516  1.00 54.83  ? 209 LYS B CG  1 
ATOM   3462 C CD  . LYS B 1 208 ? 28.456  -19.299 20.355  1.00 61.15  ? 209 LYS B CD  1 
ATOM   3463 C CE  . LYS B 1 208 ? 28.646  -18.386 21.550  1.00 67.24  ? 209 LYS B CE  1 
ATOM   3464 N NZ  . LYS B 1 208 ? 29.675  -17.332 21.327  1.00 57.45  ? 209 LYS B NZ  1 
ATOM   3465 N N   . ASP B 1 209 ? 28.397  -22.917 16.791  1.00 46.93  ? 210 ASP B N   1 
ATOM   3466 C CA  . ASP B 1 209 ? 28.782  -24.203 16.194  1.00 50.18  ? 210 ASP B CA  1 
ATOM   3467 C C   . ASP B 1 209 ? 28.996  -25.125 17.406  1.00 60.70  ? 210 ASP B C   1 
ATOM   3468 O O   . ASP B 1 209 ? 29.743  -24.782 18.316  1.00 48.42  ? 210 ASP B O   1 
ATOM   3469 C CB  . ASP B 1 209 ? 29.970  -23.928 15.273  1.00 54.35  ? 210 ASP B CB  1 
ATOM   3470 C CG  . ASP B 1 209 ? 30.561  -25.143 14.599  1.00 57.94  ? 210 ASP B CG  1 
ATOM   3471 O OD1 . ASP B 1 209 ? 30.157  -26.252 14.936  1.00 55.71  ? 210 ASP B OD1 1 
ATOM   3472 O OD2 . ASP B 1 209 ? 31.422  -24.952 13.741  1.00 54.67  ? 210 ASP B OD2 1 
ATOM   3473 N N   . PRO B 1 210 ? 28.278  -26.268 17.548  1.00 69.29  ? 211 PRO B N   1 
ATOM   3474 C CA  . PRO B 1 210 ? 28.432  -27.125 18.731  1.00 65.91  ? 211 PRO B CA  1 
ATOM   3475 C C   . PRO B 1 210 ? 29.837  -27.739 18.757  1.00 55.86  ? 211 PRO B C   1 
ATOM   3476 O O   . PRO B 1 210 ? 30.398  -27.853 19.800  1.00 58.44  ? 211 PRO B O   1 
ATOM   3477 C CB  . PRO B 1 210 ? 27.391  -28.238 18.525  1.00 72.04  ? 211 PRO B CB  1 
ATOM   3478 C CG  . PRO B 1 210 ? 27.182  -28.283 17.015  1.00 69.98  ? 211 PRO B CG  1 
ATOM   3479 C CD  . PRO B 1 210 ? 27.344  -26.842 16.562  1.00 69.69  ? 211 PRO B CD  1 
ATOM   3480 N N   . ASN B 1 211 ? 30.385  -28.017 17.571  1.00 61.88  ? 212 ASN B N   1 
ATOM   3481 C CA  . ASN B 1 211 ? 31.702  -28.674 17.374  1.00 64.52  ? 212 ASN B CA  1 
ATOM   3482 C C   . ASN B 1 211 ? 32.868  -27.683 17.369  1.00 61.42  ? 212 ASN B C   1 
ATOM   3483 O O   . ASN B 1 211 ? 33.964  -28.099 16.921  1.00 60.48  ? 212 ASN B O   1 
ATOM   3484 C CB  . ASN B 1 211 ? 31.760  -29.354 16.015  1.00 66.53  ? 212 ASN B CB  1 
ATOM   3485 C CG  . ASN B 1 211 ? 30.785  -30.494 15.897  1.00 77.01  ? 212 ASN B CG  1 
ATOM   3486 O OD1 . ASN B 1 211 ? 30.651  -31.026 14.808  1.00 76.85  ? 212 ASN B OD1 1 
ATOM   3487 N ND2 . ASN B 1 211 ? 30.125  -30.881 16.985  1.00 71.36  ? 212 ASN B ND2 1 
ATOM   3488 N N   . GLU B 1 212 ? 32.654  -26.425 17.762  1.00 55.47  ? 213 GLU B N   1 
ATOM   3489 C CA  . GLU B 1 212 ? 33.715  -25.408 17.634  1.00 47.51  ? 213 GLU B CA  1 
ATOM   3490 C C   . GLU B 1 212 ? 34.201  -25.010 19.020  1.00 48.48  ? 213 GLU B C   1 
ATOM   3491 O O   . GLU B 1 212 ? 33.431  -24.343 19.715  1.00 45.39  ? 213 GLU B O   1 
ATOM   3492 C CB  . GLU B 1 212 ? 33.231  -24.165 16.877  1.00 42.84  ? 213 GLU B CB  1 
ATOM   3493 C CG  . GLU B 1 212 ? 34.280  -23.060 16.826  1.00 44.41  ? 213 GLU B CG  1 
ATOM   3494 C CD  . GLU B 1 212 ? 35.614  -23.479 16.218  1.00 47.83  ? 213 GLU B CD  1 
ATOM   3495 O OE1 . GLU B 1 212 ? 35.640  -23.758 15.021  1.00 41.26  ? 213 GLU B OE1 1 
ATOM   3496 O OE2 . GLU B 1 212 ? 36.586  -23.558 16.932  1.00 44.63  ? 213 GLU B OE2 1 
ATOM   3497 N N   . LYS B 1 213 ? 35.477  -25.282 19.317  1.00 47.80  ? 214 LYS B N   1 
ATOM   3498 C CA  . LYS B 1 213 ? 36.096  -25.048 20.647  1.00 50.81  ? 214 LYS B CA  1 
ATOM   3499 C C   . LYS B 1 213 ? 36.600  -23.607 20.717  1.00 52.56  ? 214 LYS B C   1 
ATOM   3500 O O   . LYS B 1 213 ? 36.654  -23.079 21.819  1.00 45.92  ? 214 LYS B O   1 
ATOM   3501 C CB  . LYS B 1 213 ? 37.303  -25.968 20.888  1.00 65.32  ? 214 LYS B CB  1 
ATOM   3502 C CG  . LYS B 1 213 ? 37.086  -27.472 20.710  1.00 72.19  ? 214 LYS B CG  1 
ATOM   3503 C CD  . LYS B 1 213 ? 36.047  -28.089 21.638  1.00 82.12  ? 214 LYS B CD  1 
ATOM   3504 C CE  . LYS B 1 213 ? 34.861  -28.715 20.918  1.00 91.26  ? 214 LYS B CE  1 
ATOM   3505 N NZ  . LYS B 1 213 ? 33.579  -28.469 21.625  1.00 86.76  ? 214 LYS B NZ  1 
ATOM   3506 N N   . ARG B 1 214 ? 36.956  -22.960 19.593  1.00 43.67  ? 215 ARG B N   1 
ATOM   3507 C CA  . ARG B 1 214 ? 37.414  -21.557 19.663  1.00 39.69  ? 215 ARG B CA  1 
ATOM   3508 C C   . ARG B 1 214 ? 36.225  -20.650 19.957  1.00 36.87  ? 215 ARG B C   1 
ATOM   3509 O O   . ARG B 1 214 ? 35.078  -21.038 19.726  1.00 39.87  ? 215 ARG B O   1 
ATOM   3510 C CB  . ARG B 1 214 ? 38.109  -21.146 18.364  1.00 43.57  ? 215 ARG B CB  1 
ATOM   3511 C CG  . ARG B 1 214 ? 39.393  -21.906 18.105  1.00 41.69  ? 215 ARG B CG  1 
ATOM   3512 C CD  . ARG B 1 214 ? 39.754  -21.690 16.649  1.00 47.33  ? 215 ARG B CD  1 
ATOM   3513 N NE  . ARG B 1 214 ? 38.901  -22.473 15.756  1.00 45.19  ? 215 ARG B NE  1 
ATOM   3514 C CZ  . ARG B 1 214 ? 39.032  -22.497 14.440  1.00 42.51  ? 215 ARG B CZ  1 
ATOM   3515 N NH1 . ARG B 1 214 ? 39.993  -21.810 13.874  1.00 46.83  ? 215 ARG B NH1 1 
ATOM   3516 N NH2 . ARG B 1 214 ? 38.245  -23.222 13.675  1.00 37.91  ? 215 ARG B NH2 1 
ATOM   3517 N N   . ASP B 1 215 ? 36.534  -19.490 20.467  1.00 37.84  ? 216 ASP B N   1 
ATOM   3518 C CA  . ASP B 1 215 ? 35.589  -18.381 20.713  1.00 42.38  ? 216 ASP B CA  1 
ATOM   3519 C C   . ASP B 1 215 ? 35.027  -17.957 19.348  1.00 43.93  ? 216 ASP B C   1 
ATOM   3520 O O   . ASP B 1 215 ? 35.834  -17.754 18.452  1.00 41.11  ? 216 ASP B O   1 
ATOM   3521 C CB  . ASP B 1 215 ? 36.332  -17.267 21.425  1.00 40.95  ? 216 ASP B CB  1 
ATOM   3522 C CG  . ASP B 1 215 ? 35.418  -16.432 22.271  1.00 47.01  ? 216 ASP B CG  1 
ATOM   3523 O OD1 . ASP B 1 215 ? 34.147  -16.573 22.088  1.00 43.83  ? 216 ASP B OD1 1 
ATOM   3524 O OD2 . ASP B 1 215 ? 35.967  -15.637 23.073  1.00 45.98  ? 216 ASP B OD2 1 
ATOM   3525 N N   . HIS B 1 216 ? 33.711  -17.911 19.154  1.00 39.05  ? 217 HIS B N   1 
ATOM   3526 C CA  . HIS B 1 216 ? 33.129  -17.864 17.778  1.00 42.07  ? 217 HIS B CA  1 
ATOM   3527 C C   . HIS B 1 216 ? 31.681  -17.332 17.810  1.00 41.46  ? 217 HIS B C   1 
ATOM   3528 O O   . HIS B 1 216 ? 31.096  -17.219 18.905  1.00 37.31  ? 217 HIS B O   1 
ATOM   3529 C CB  . HIS B 1 216 ? 33.309  -19.238 17.102  1.00 38.09  ? 217 HIS B CB  1 
ATOM   3530 C CG  . HIS B 1 216 ? 32.307  -20.230 17.553  1.00 43.34  ? 217 HIS B CG  1 
ATOM   3531 N ND1 . HIS B 1 216 ? 32.360  -20.790 18.808  1.00 43.92  ? 217 HIS B ND1 1 
ATOM   3532 C CD2 . HIS B 1 216 ? 31.173  -20.674 16.960  1.00 48.42  ? 217 HIS B CD2 1 
ATOM   3533 C CE1 . HIS B 1 216 ? 31.332  -21.591 18.955  1.00 50.18  ? 217 HIS B CE1 1 
ATOM   3534 N NE2 . HIS B 1 216 ? 30.583  -21.540 17.827  1.00 47.14  ? 217 HIS B NE2 1 
ATOM   3535 N N   . MET B 1 217 ? 31.154  -16.916 16.655  1.00 36.43  ? 218 MET B N   1 
ATOM   3536 C CA  . MET B 1 217 ? 29.787  -16.360 16.537  1.00 43.33  ? 218 MET B CA  1 
ATOM   3537 C C   . MET B 1 217 ? 29.301  -16.834 15.186  1.00 46.17  ? 218 MET B C   1 
ATOM   3538 O O   . MET B 1 217 ? 30.086  -16.687 14.221  1.00 38.95  ? 218 MET B O   1 
ATOM   3539 C CB  . MET B 1 217 ? 29.800  -14.832 16.565  1.00 40.96  ? 218 MET B CB  1 
ATOM   3540 C CG  . MET B 1 217 ? 28.529  -14.223 16.110  1.00 43.33  ? 218 MET B CG  1 
ATOM   3541 S SD  . MET B 1 217 ? 28.452  -12.571 16.667  1.00 42.42  ? 218 MET B SD  1 
ATOM   3542 C CE  . MET B 1 217 ? 29.483  -11.745 15.451  1.00 42.39  ? 218 MET B CE  1 
ATOM   3543 N N   . VAL B 1 218 ? 28.116  -17.440 15.103  1.00 35.62  ? 219 VAL B N   1 
ATOM   3544 C CA  . VAL B 1 218 ? 27.528  -17.811 13.778  1.00 37.04  ? 219 VAL B CA  1 
ATOM   3545 C C   . VAL B 1 218 ? 26.345  -16.881 13.559  1.00 42.09  ? 219 VAL B C   1 
ATOM   3546 O O   . VAL B 1 218 ? 25.545  -16.692 14.532  1.00 39.21  ? 219 VAL B O   1 
ATOM   3547 C CB  . VAL B 1 218 ? 27.131  -19.298 13.707  1.00 40.92  ? 219 VAL B CB  1 
ATOM   3548 C CG1 . VAL B 1 218 ? 26.371  -19.596 12.458  1.00 39.73  ? 219 VAL B CG1 1 
ATOM   3549 C CG2 . VAL B 1 218 ? 28.320  -20.230 13.804  1.00 40.74  ? 219 VAL B CG2 1 
ATOM   3550 N N   . LEU B 1 219 ? 26.259  -16.250 12.388  1.00 40.50  ? 220 LEU B N   1 
ATOM   3551 C CA  . LEU B 1 219 ? 25.166  -15.314 12.065  1.00 37.73  ? 220 LEU B CA  1 
ATOM   3552 C C   . LEU B 1 219 ? 24.483  -15.757 10.802  1.00 33.11  ? 220 LEU B C   1 
ATOM   3553 O O   . LEU B 1 219 ? 25.144  -16.198 9.857   1.00 38.35  ? 220 LEU B O   1 
ATOM   3554 C CB  . LEU B 1 219 ? 25.664  -13.884 11.823  1.00 40.66  ? 220 LEU B CB  1 
ATOM   3555 C CG  . LEU B 1 219 ? 26.205  -13.118 13.010  1.00 38.89  ? 220 LEU B CG  1 
ATOM   3556 C CD1 . LEU B 1 219 ? 26.517  -11.668 12.577  1.00 38.05  ? 220 LEU B CD1 1 
ATOM   3557 C CD2 . LEU B 1 219 ? 25.214  -13.056 14.189  1.00 44.09  ? 220 LEU B CD2 1 
ATOM   3558 N N   . LEU B 1 220 ? 23.168  -15.524 10.766  1.00 37.81  ? 221 LEU B N   1 
ATOM   3559 C CA  . LEU B 1 220 ? 22.344  -15.582 9.548   1.00 38.13  ? 221 LEU B CA  1 
ATOM   3560 C C   . LEU B 1 220 ? 21.601  -14.255 9.528   1.00 38.51  ? 221 LEU B C   1 
ATOM   3561 O O   . LEU B 1 220 ? 20.885  -13.962 10.505  1.00 42.16  ? 221 LEU B O   1 
ATOM   3562 C CB  . LEU B 1 220 ? 21.375  -16.762 9.643   1.00 41.23  ? 221 LEU B CB  1 
ATOM   3563 C CG  . LEU B 1 220 ? 20.396  -16.908 8.479   1.00 43.47  ? 221 LEU B CG  1 
ATOM   3564 C CD1 . LEU B 1 220 ? 21.119  -17.111 7.164   1.00 46.49  ? 221 LEU B CD1 1 
ATOM   3565 C CD2 . LEU B 1 220 ? 19.428  -18.075 8.741   1.00 47.19  ? 221 LEU B CD2 1 
ATOM   3566 N N   . GLU B 1 221 ? 21.847  -13.447 8.508   1.00 38.29  ? 222 GLU B N   1 
ATOM   3567 C CA  . GLU B 1 221 ? 21.254  -12.104 8.401   1.00 35.64  ? 222 GLU B CA  1 
ATOM   3568 C C   . GLU B 1 221 ? 20.435  -11.995 7.135   1.00 35.26  ? 222 GLU B C   1 
ATOM   3569 O O   . GLU B 1 221 ? 20.842  -12.505 6.077   1.00 32.49  ? 222 GLU B O   1 
ATOM   3570 C CB  . GLU B 1 221 ? 22.287  -10.998 8.252   1.00 39.09  ? 222 GLU B CB  1 
ATOM   3571 C CG  . GLU B 1 221 ? 23.456  -11.211 9.118   1.00 40.25  ? 222 GLU B CG  1 
ATOM   3572 C CD  . GLU B 1 221 ? 23.328  -10.472 10.408  1.00 50.97  ? 222 GLU B CD  1 
ATOM   3573 O OE1 . GLU B 1 221 ? 23.526  -9.210  10.371  1.00 65.25  ? 222 GLU B OE1 1 
ATOM   3574 O OE2 . GLU B 1 221 ? 23.104  -11.200 11.428  1.00 57.90  ? 222 GLU B OE2 1 
ATOM   3575 N N   . PHE B 1 222 ? 19.329  -11.299 7.276   1.00 35.27  ? 223 PHE B N   1 
ATOM   3576 C CA  . PHE B 1 222 ? 18.511  -10.832 6.143   1.00 38.52  ? 223 PHE B CA  1 
ATOM   3577 C C   . PHE B 1 222 ? 18.400  -9.320  6.257   1.00 34.99  ? 223 PHE B C   1 
ATOM   3578 O O   . PHE B 1 222 ? 17.930  -8.808  7.259   1.00 36.13  ? 223 PHE B O   1 
ATOM   3579 C CB  . PHE B 1 222 ? 17.150  -11.531 6.129   1.00 41.48  ? 223 PHE B CB  1 
ATOM   3580 C CG  . PHE B 1 222 ? 17.268  -13.019 5.983   1.00 36.84  ? 223 PHE B CG  1 
ATOM   3581 C CD1 . PHE B 1 222 ? 17.549  -13.565 4.756   1.00 37.96  ? 223 PHE B CD1 1 
ATOM   3582 C CD2 . PHE B 1 222 ? 17.135  -13.835 7.090   1.00 39.56  ? 223 PHE B CD2 1 
ATOM   3583 C CE1 . PHE B 1 222 ? 17.677  -14.934 4.599   1.00 40.54  ? 223 PHE B CE1 1 
ATOM   3584 C CE2 . PHE B 1 222 ? 17.234  -15.205 6.941   1.00 41.10  ? 223 PHE B CE2 1 
ATOM   3585 C CZ  . PHE B 1 222 ? 17.512  -15.751 5.702   1.00 44.50  ? 223 PHE B CZ  1 
ATOM   3586 N N   . VAL B 1 223 ? 18.937  -8.633  5.255   1.00 35.75  ? 224 VAL B N   1 
ATOM   3587 C CA  . VAL B 1 223 ? 18.955  -7.139  5.199   1.00 37.42  ? 224 VAL B CA  1 
ATOM   3588 C C   . VAL B 1 223 ? 18.119  -6.659  3.992   1.00 34.54  ? 224 VAL B C   1 
ATOM   3589 O O   . VAL B 1 223 ? 18.392  -7.119  2.893   1.00 36.05  ? 224 VAL B O   1 
ATOM   3590 C CB  . VAL B 1 223 ? 20.400  -6.612  5.137   1.00 39.14  ? 224 VAL B CB  1 
ATOM   3591 C CG1 . VAL B 1 223 ? 20.407  -5.110  5.235   1.00 38.47  ? 224 VAL B CG1 1 
ATOM   3592 C CG2 . VAL B 1 223 ? 21.271  -7.226  6.236   1.00 34.69  ? 224 VAL B CG2 1 
ATOM   3593 N N   . THR B 1 224 ? 17.135  -5.785  4.220   1.00 35.58  ? 225 THR B N   1 
ATOM   3594 C CA  . THR B 1 224 ? 16.245  -5.273  3.156   1.00 37.24  ? 225 THR B CA  1 
ATOM   3595 C C   . THR B 1 224 ? 16.198  -3.745  3.149   1.00 32.60  ? 225 THR B C   1 
ATOM   3596 O O   . THR B 1 224 ? 16.087  -3.109  4.227   1.00 34.93  ? 225 THR B O   1 
ATOM   3597 C CB  . THR B 1 224 ? 14.849  -5.869  3.298   1.00 42.01  ? 225 THR B CB  1 
ATOM   3598 O OG1 . THR B 1 224 ? 15.052  -7.260  3.540   1.00 42.32  ? 225 THR B OG1 1 
ATOM   3599 C CG2 . THR B 1 224 ? 14.035  -5.627  2.042   1.00 44.50  ? 225 THR B CG2 1 
ATOM   3600 N N   . ALA B 1 225 ? 16.332  -3.140  1.970   1.00 33.75  ? 226 ALA B N   1 
ATOM   3601 C CA  . ALA B 1 225 ? 16.176  -1.679  1.892   1.00 31.64  ? 226 ALA B CA  1 
ATOM   3602 C C   . ALA B 1 225 ? 14.663  -1.381  1.889   1.00 32.24  ? 226 ALA B C   1 
ATOM   3603 O O   . ALA B 1 225 ? 13.920  -2.165  1.247   1.00 34.85  ? 226 ALA B O   1 
ATOM   3604 C CB  . ALA B 1 225 ? 16.796  -1.123  0.641   1.00 36.42  ? 226 ALA B CB  1 
ATOM   3605 N N   . ALA B 1 226 ? 14.269  -0.240  2.450   1.00 35.83  ? 227 ALA B N   1 
ATOM   3606 C CA  . ALA B 1 226 ? 12.844  0.183   2.457   1.00 42.60  ? 227 ALA B CA  1 
ATOM   3607 C C   . ALA B 1 226 ? 12.772  1.708   2.654   1.00 42.54  ? 227 ALA B C   1 
ATOM   3608 O O   . ALA B 1 226 ? 13.825  2.330   2.908   1.00 39.06  ? 227 ALA B O   1 
ATOM   3609 C CB  . ALA B 1 226 ? 12.120  -0.583  3.548   1.00 39.85  ? 227 ALA B CB  1 
ATOM   3610 N N   . GLY B 1 227 ? 11.559  2.269   2.569   1.00 49.06  ? 228 GLY B N   1 
ATOM   3611 C CA  . GLY B 1 227 ? 11.270  3.649   2.991   1.00 52.86  ? 228 GLY B CA  1 
ATOM   3612 C C   . GLY B 1 227 ? 10.902  4.526   1.806   1.00 58.60  ? 228 GLY B C   1 
ATOM   3613 O O   . GLY B 1 227 ? 10.438  5.638   2.040   1.00 68.25  ? 228 GLY B O   1 
ATOM   3614 N N   . ILE B 1 228 ? 11.130  4.063   0.578   1.00 59.12  ? 229 ILE B N   1 
ATOM   3615 C CA  . ILE B 1 228 ? 10.785  4.787   -0.682  1.00 64.91  ? 229 ILE B CA  1 
ATOM   3616 C C   . ILE B 1 228 ? 9.672   3.976   -1.327  1.00 64.71  ? 229 ILE B C   1 
ATOM   3617 O O   . ILE B 1 228 ? 9.915   2.931   -1.926  1.00 69.71  ? 229 ILE B O   1 
ATOM   3618 C CB  . ILE B 1 228 ? 12.001  4.985   -1.612  1.00 64.53  ? 229 ILE B CB  1 
ATOM   3619 C CG1 . ILE B 1 228 ? 13.112  5.775   -0.922  1.00 62.06  ? 229 ILE B CG1 1 
ATOM   3620 C CG2 . ILE B 1 228 ? 11.591  5.642   -2.914  1.00 58.24  ? 229 ILE B CG2 1 
ATOM   3621 C CD1 . ILE B 1 228 ? 14.316  6.052   -1.800  1.00 61.67  ? 229 ILE B CD1 1 
ATOM   3622 N N   . PRO B 1 229 ? 8.400   4.388   -1.141  1.00 86.88  ? 230 PRO B N   1 
ATOM   3623 C CA  . PRO B 1 229 ? 7.279   3.592   -1.635  1.00 85.87  ? 230 PRO B CA  1 
ATOM   3624 C C   . PRO B 1 229 ? 7.168   3.742   -3.163  1.00 93.26  ? 230 PRO B C   1 
ATOM   3625 O O   . PRO B 1 229 ? 7.887   4.573   -3.751  1.00 83.34  ? 230 PRO B O   1 
ATOM   3626 C CB  . PRO B 1 229 ? 6.068   4.115   -0.840  1.00 91.77  ? 230 PRO B CB  1 
ATOM   3627 C CG  . PRO B 1 229 ? 6.472   5.503   -0.323  1.00 93.77  ? 230 PRO B CG  1 
ATOM   3628 C CD  . PRO B 1 229 ? 7.983   5.610   -0.427  1.00 93.41  ? 230 PRO B CD  1 
ATOM   3629 N N   . LEU B 1 230 ? 6.312   2.919   -3.780  1.00 99.05  ? 231 LEU B N   1 
ATOM   3630 C CA  . LEU B 1 230 ? 5.983   2.982   -5.233  1.00 96.81  ? 231 LEU B CA  1 
ATOM   3631 C C   . LEU B 1 230 ? 5.061   4.187   -5.468  1.00 81.76  ? 231 LEU B C   1 
ATOM   3632 O O   . LEU B 1 230 ? 5.451   5.134   -6.137  1.00 79.90  ? 231 LEU B O   1 
ATOM   3633 C CB  . LEU B 1 230 ? 5.277   1.697   -5.682  1.00 94.27  ? 231 LEU B CB  1 
ATOM   3634 C CG  . LEU B 1 230 ? 6.031   0.379   -5.511  1.00 89.74  ? 231 LEU B CG  1 
ATOM   3635 C CD1 . LEU B 1 230 ? 5.788   -0.233  -4.123  1.00 88.20  ? 231 LEU B CD1 1 
ATOM   3636 C CD2 . LEU B 1 230 ? 5.609   -0.599  -6.598  1.00 81.61  ? 231 LEU B CD2 1 
HETATM 3637 O O   . HOH C 2 .   ? 7.500   0.704   39.254  1.00 40.36  ? 301 HOH A O   1 
HETATM 3638 O O   . HOH C 2 .   ? 7.735   27.076  50.261  1.00 54.18  ? 302 HOH A O   1 
HETATM 3639 O O   . HOH C 2 .   ? 2.900   5.281   39.513  1.00 37.78  ? 303 HOH A O   1 
HETATM 3640 O O   . HOH C 2 .   ? -2.704  20.892  56.156  1.00 49.75  ? 304 HOH A O   1 
HETATM 3641 O O   . HOH C 2 .   ? -1.455  3.154   33.309  1.00 47.50  ? 305 HOH A O   1 
HETATM 3642 O O   . HOH C 2 .   ? 10.052  9.822   42.647  1.00 33.83  ? 306 HOH A O   1 
HETATM 3643 O O   . HOH C 2 .   ? -0.454  5.801   54.228  1.00 39.23  ? 307 HOH A O   1 
HETATM 3644 O O   . HOH C 2 .   ? -6.794  20.613  27.651  1.00 40.11  ? 308 HOH A O   1 
HETATM 3645 O O   . HOH C 2 .   ? 19.700  -6.708  47.385  1.00 45.65  ? 309 HOH A O   1 
HETATM 3646 O O   . HOH C 2 .   ? 7.660   -7.053  48.486  1.00 38.16  ? 310 HOH A O   1 
HETATM 3647 O O   . HOH C 2 .   ? 2.299   -0.884  54.987  1.00 35.52  ? 311 HOH A O   1 
HETATM 3648 O O   . HOH C 2 .   ? 15.124  3.379   47.957  1.00 33.64  ? 312 HOH A O   1 
HETATM 3649 O O   . HOH C 2 .   ? 2.272   -3.028  43.597  1.00 38.73  ? 313 HOH A O   1 
HETATM 3650 O O   . HOH C 2 .   ? 8.786   12.859  60.825  1.00 47.79  ? 314 HOH A O   1 
HETATM 3651 O O   . HOH C 2 .   ? 13.647  21.550  50.527  1.00 41.85  ? 315 HOH A O   1 
HETATM 3652 O O   . HOH C 2 .   ? 1.957   11.422  59.202  1.00 46.92  ? 316 HOH A O   1 
HETATM 3653 O O   . HOH C 2 .   ? 7.601   9.902   31.456  1.00 29.87  ? 317 HOH A O   1 
HETATM 3654 O O   . HOH C 2 .   ? 0.987   23.173  50.314  1.00 44.62  ? 318 HOH A O   1 
HETATM 3655 O O   . HOH C 2 .   ? 7.312   10.763  17.163  1.00 35.88  ? 319 HOH A O   1 
HETATM 3656 O O   . HOH C 2 .   ? 12.460  13.714  36.576  1.00 36.20  ? 320 HOH A O   1 
HETATM 3657 O O   . HOH C 2 .   ? 1.430   -2.612  47.871  1.00 45.59  ? 321 HOH A O   1 
HETATM 3658 O O   . HOH C 2 .   ? 13.394  7.571   56.896  1.00 47.38  ? 322 HOH A O   1 
HETATM 3659 O O   . HOH C 2 .   ? 3.675   25.506  28.834  1.00 46.79  ? 323 HOH A O   1 
HETATM 3660 O O   . HOH C 2 .   ? 9.413   3.097   54.388  1.00 35.47  ? 324 HOH A O   1 
HETATM 3661 O O   . HOH C 2 .   ? 2.721   14.396  56.055  1.00 38.02  ? 325 HOH A O   1 
HETATM 3662 O O   . HOH C 2 .   ? 9.477   13.473  40.123  1.00 31.71  ? 326 HOH A O   1 
HETATM 3663 O O   . HOH C 2 .   ? 15.926  15.969  25.581  1.00 41.06  ? 327 HOH A O   1 
HETATM 3664 O O   . HOH C 2 .   ? 9.177   5.190   49.152  1.00 31.95  ? 328 HOH A O   1 
HETATM 3665 O O   . HOH C 2 .   ? -0.601  22.171  24.950  1.00 42.78  ? 329 HOH A O   1 
HETATM 3666 O O   . HOH C 2 .   ? -3.937  18.170  45.978  1.00 41.13  ? 330 HOH A O   1 
HETATM 3667 O O   . HOH C 2 .   ? 0.335   15.216  54.613  1.00 37.63  ? 331 HOH A O   1 
HETATM 3668 O O   . HOH C 2 .   ? -7.748  7.444   40.721  1.00 53.16  ? 332 HOH A O   1 
HETATM 3669 O O   . HOH C 2 .   ? -4.732  9.889   56.831  1.00 47.28  ? 333 HOH A O   1 
HETATM 3670 O O   . HOH C 2 .   ? 16.070  7.653   21.797  1.00 41.61  ? 334 HOH A O   1 
HETATM 3671 O O   . HOH C 2 .   ? 10.781  1.884   18.089  1.00 47.40  ? 335 HOH A O   1 
HETATM 3672 O O   . HOH C 2 .   ? -3.241  5.122   55.910  1.00 49.86  ? 336 HOH A O   1 
HETATM 3673 O O   . HOH C 2 .   ? 12.590  20.833  22.512  1.00 45.06  ? 337 HOH A O   1 
HETATM 3674 O O   . HOH C 2 .   ? 1.254   2.984   24.798  1.00 43.71  ? 338 HOH A O   1 
HETATM 3675 O O   . HOH C 2 .   ? 12.553  5.962   54.782  1.00 35.03  ? 339 HOH A O   1 
HETATM 3676 O O   . HOH C 2 .   ? 7.364   3.375   55.979  1.00 44.82  ? 340 HOH A O   1 
HETATM 3677 O O   . HOH C 2 .   ? 18.204  4.143   16.023  1.00 41.08  ? 341 HOH A O   1 
HETATM 3678 O O   . HOH C 2 .   ? 11.267  11.149  34.045  1.00 32.95  ? 342 HOH A O   1 
HETATM 3679 O O   . HOH C 2 .   ? 8.539   3.331   40.373  1.00 39.66  ? 343 HOH A O   1 
HETATM 3680 O O   . HOH C 2 .   ? 11.829  3.701   56.055  1.00 33.31  ? 344 HOH A O   1 
HETATM 3681 O O   . HOH C 2 .   ? 17.765  15.344  33.508  1.00 42.53  ? 345 HOH A O   1 
HETATM 3682 O O   . HOH C 2 .   ? -8.031  4.960   36.786  1.00 42.75  ? 346 HOH A O   1 
HETATM 3683 O O   . HOH C 2 .   ? 15.689  3.190   23.393  1.00 35.60  ? 347 HOH A O   1 
HETATM 3684 O O   . HOH C 2 .   ? 15.032  -3.778  29.095  1.00 42.30  ? 348 HOH A O   1 
HETATM 3685 O O   . HOH C 2 .   ? 18.731  -2.982  41.713  1.00 36.36  ? 349 HOH A O   1 
HETATM 3686 O O   . HOH C 2 .   ? 2.339   4.726   45.345  1.00 37.20  ? 350 HOH A O   1 
HETATM 3687 O O   . HOH C 2 .   ? 22.908  -4.386  46.898  1.00 41.97  ? 351 HOH A O   1 
HETATM 3688 O O   . HOH C 2 .   ? 5.434   7.240   41.474  1.00 38.51  ? 352 HOH A O   1 
HETATM 3689 O O   . HOH C 2 .   ? 7.719   6.464   28.965  1.00 39.78  ? 353 HOH A O   1 
HETATM 3690 O O   . HOH C 2 .   ? 20.586  4.079   35.602  1.00 54.90  ? 354 HOH A O   1 
HETATM 3691 O O   . HOH C 2 .   ? 16.855  15.889  51.608  1.00 40.87  ? 355 HOH A O   1 
HETATM 3692 O O   . HOH C 2 .   ? -6.077  17.600  37.714  1.00 36.68  ? 356 HOH A O   1 
HETATM 3693 O O   . HOH C 2 .   ? -11.410 17.467  38.479  1.00 41.48  ? 357 HOH A O   1 
HETATM 3694 O O   . HOH C 2 .   ? 0.711   11.059  56.503  1.00 34.73  ? 358 HOH A O   1 
HETATM 3695 O O   . HOH C 2 .   ? -8.084  13.535  27.282  1.00 46.12  ? 359 HOH A O   1 
HETATM 3696 O O   . HOH C 2 .   ? 5.470   5.417   55.932  1.00 44.33  ? 360 HOH A O   1 
HETATM 3697 O O   . HOH C 2 .   ? 6.564   2.328   52.875  1.00 35.86  ? 361 HOH A O   1 
HETATM 3698 O O   . HOH C 2 .   ? 22.671  -0.583  46.214  1.00 35.53  ? 362 HOH A O   1 
HETATM 3699 O O   . HOH C 2 .   ? 1.058   8.345   52.373  1.00 31.39  ? 363 HOH A O   1 
HETATM 3700 O O   . HOH C 2 .   ? 10.259  -8.904  49.586  1.00 45.59  ? 364 HOH A O   1 
HETATM 3701 O O   . HOH C 2 .   ? 10.094  12.822  37.538  1.00 34.57  ? 365 HOH A O   1 
HETATM 3702 O O   . HOH C 2 .   ? -12.205 5.675   31.181  1.00 44.45  ? 366 HOH A O   1 
HETATM 3703 O O   . HOH C 2 .   ? 5.896   6.921   30.861  1.00 30.29  ? 367 HOH A O   1 
HETATM 3704 O O   . HOH C 2 .   ? 2.083   4.284   35.765  1.00 52.95  ? 368 HOH A O   1 
HETATM 3705 O O   . HOH C 2 .   ? 4.873   5.610   44.319  1.00 42.00  ? 369 HOH A O   1 
HETATM 3706 O O   . HOH C 2 .   ? 20.848  7.217   57.572  1.00 54.76  ? 370 HOH A O   1 
HETATM 3707 O O   . HOH C 2 .   ? 17.020  10.183  21.074  1.00 43.08  ? 371 HOH A O   1 
HETATM 3708 O O   . HOH C 2 .   ? 5.023   -4.657  55.978  1.00 35.67  ? 372 HOH A O   1 
HETATM 3709 O O   . HOH C 2 .   ? 23.044  9.756   54.866  1.00 57.39  ? 373 HOH A O   1 
HETATM 3710 O O   . HOH C 2 .   ? 16.294  -1.001  31.504  1.00 33.25  ? 374 HOH A O   1 
HETATM 3711 O O   . HOH C 2 .   ? -6.630  5.966   50.361  1.00 48.90  ? 375 HOH A O   1 
HETATM 3712 O O   . HOH C 2 .   ? 8.827   20.820  44.533  1.00 39.89  ? 376 HOH A O   1 
HETATM 3713 O O   . HOH C 2 .   ? -0.166  3.453   58.543  1.00 46.65  ? 377 HOH A O   1 
HETATM 3714 O O   . HOH C 2 .   ? 6.478   -1.887  30.350  1.00 43.12  ? 378 HOH A O   1 
HETATM 3715 O O   . HOH C 2 .   ? 5.524   4.141   40.215  1.00 50.39  ? 379 HOH A O   1 
HETATM 3716 O O   . HOH C 2 .   ? -1.252  8.228   20.969  1.00 43.75  ? 380 HOH A O   1 
HETATM 3717 O O   . HOH C 2 .   ? 6.369   24.855  28.593  1.00 44.82  ? 381 HOH A O   1 
HETATM 3718 O O   . HOH C 2 .   ? 17.371  21.663  44.262  1.00 59.90  ? 382 HOH A O   1 
HETATM 3719 O O   . HOH C 2 .   ? 12.630  -2.986  32.662  1.00 34.58  ? 383 HOH A O   1 
HETATM 3720 O O   . HOH C 2 .   ? 1.254   -0.150  26.512  1.00 42.90  ? 384 HOH A O   1 
HETATM 3721 O O   . HOH C 2 .   ? 10.572  22.688  29.616  1.00 50.98  ? 385 HOH A O   1 
HETATM 3722 O O   . HOH C 2 .   ? 1.798   23.131  35.809  1.00 37.99  ? 386 HOH A O   1 
HETATM 3723 O O   . HOH C 2 .   ? 17.527  1.577   30.977  1.00 37.97  ? 387 HOH A O   1 
HETATM 3724 O O   . HOH C 2 .   ? -4.910  19.569  38.200  1.00 42.25  ? 388 HOH A O   1 
HETATM 3725 O O   . HOH C 2 .   ? -2.803  10.249  24.945  1.00 42.18  ? 389 HOH A O   1 
HETATM 3726 O O   . HOH C 2 .   ? 10.800  24.290  33.653  1.00 64.08  ? 390 HOH A O   1 
HETATM 3727 O O   . HOH C 2 .   ? 4.119   -2.728  54.313  1.00 38.49  ? 391 HOH A O   1 
HETATM 3728 O O   . HOH C 2 .   ? 3.306   4.048   55.731  1.00 43.91  ? 392 HOH A O   1 
HETATM 3729 O O   . HOH C 2 .   ? 10.616  -4.239  29.577  1.00 51.34  ? 393 HOH A O   1 
HETATM 3730 O O   . HOH C 2 .   ? 11.469  -5.002  27.488  1.00 51.37  ? 394 HOH A O   1 
HETATM 3731 O O   . HOH C 2 .   ? 17.764  15.212  53.969  1.00 65.22  ? 395 HOH A O   1 
HETATM 3732 O O   . HOH C 2 .   ? -4.527  11.294  20.749  1.00 60.92  ? 396 HOH A O   1 
HETATM 3733 O O   . HOH C 2 .   ? 14.152  16.346  14.678  1.00 56.06  ? 397 HOH A O   1 
HETATM 3734 O O   . HOH C 2 .   ? 3.517   -6.857  43.689  1.00 40.86  ? 398 HOH A O   1 
HETATM 3735 O O   . HOH C 2 .   ? -9.116  5.687   39.311  1.00 54.09  ? 399 HOH A O   1 
HETATM 3736 O O   . HOH D 2 .   ? 20.665  -7.427  23.513  1.00 38.90  ? 301 HOH B O   1 
HETATM 3737 O O   . HOH D 2 .   ? 42.453  -0.924  30.528  1.00 58.73  ? 302 HOH B O   1 
HETATM 3738 O O   . HOH D 2 .   ? 22.269  -12.978 -5.044  1.00 38.85  ? 303 HOH B O   1 
HETATM 3739 O O   . HOH D 2 .   ? 19.784  11.181  0.853   1.00 43.57  ? 304 HOH B O   1 
HETATM 3740 O O   . HOH D 2 .   ? 14.953  -9.214  1.870   1.00 44.09  ? 305 HOH B O   1 
HETATM 3741 O O   . HOH D 2 .   ? 30.195  -3.216  16.034  1.00 32.38  ? 306 HOH B O   1 
HETATM 3742 O O   . HOH D 2 .   ? 28.998  -2.017  4.582   1.00 34.05  ? 307 HOH B O   1 
HETATM 3743 O O   . HOH D 2 .   ? 13.281  9.456   0.694   1.00 45.50  ? 308 HOH B O   1 
HETATM 3744 O O   . HOH D 2 .   ? 22.629  -18.298 13.225  1.00 48.15  ? 309 HOH B O   1 
HETATM 3745 O O   . HOH D 2 .   ? 15.272  -7.949  6.050   1.00 40.50  ? 310 HOH B O   1 
HETATM 3746 O O   . HOH D 2 .   ? 18.076  -14.013 10.506  1.00 45.94  ? 311 HOH B O   1 
HETATM 3747 O O   . HOH D 2 .   ? 31.760  2.872   -9.279  1.00 39.63  ? 312 HOH B O   1 
HETATM 3748 O O   . HOH D 2 .   ? 20.175  -2.552  9.294   1.00 38.01  ? 313 HOH B O   1 
HETATM 3749 O O   . HOH D 2 .   ? 11.308  -2.650  1.206   1.00 41.95  ? 314 HOH B O   1 
HETATM 3750 O O   . HOH D 2 .   ? 23.464  -2.858  -1.122  1.00 33.55  ? 315 HOH B O   1 
HETATM 3751 O O   . HOH D 2 .   ? 18.027  -5.126  29.566  1.00 41.60  ? 316 HOH B O   1 
HETATM 3752 O O   . HOH D 2 .   ? 37.320  -8.263  -8.684  1.00 48.14  ? 317 HOH B O   1 
HETATM 3753 O O   . HOH D 2 .   ? 28.952  0.228   -10.570 1.00 45.35  ? 318 HOH B O   1 
HETATM 3754 O O   . HOH D 2 .   ? 22.438  3.263   -0.530  1.00 38.45  ? 319 HOH B O   1 
HETATM 3755 O O   . HOH D 2 .   ? 33.676  -1.939  29.894  1.00 41.95  ? 320 HOH B O   1 
HETATM 3756 O O   . HOH D 2 .   ? 25.629  -0.930  -9.512  1.00 34.77  ? 321 HOH B O   1 
HETATM 3757 O O   . HOH D 2 .   ? 32.798  -2.566  6.874   1.00 31.03  ? 322 HOH B O   1 
HETATM 3758 O O   . HOH D 2 .   ? 16.144  -9.328  -5.293  1.00 44.10  ? 323 HOH B O   1 
HETATM 3759 O O   . HOH D 2 .   ? 39.385  -18.846 20.541  1.00 49.58  ? 324 HOH B O   1 
HETATM 3760 O O   . HOH D 2 .   ? 21.499  -0.773  -8.137  1.00 40.01  ? 325 HOH B O   1 
HETATM 3761 O O   . HOH D 2 .   ? 35.752  -22.572 6.355   1.00 42.26  ? 326 HOH B O   1 
HETATM 3762 O O   . HOH D 2 .   ? 22.140  -10.984 16.349  1.00 46.32  ? 327 HOH B O   1 
HETATM 3763 O O   . HOH D 2 .   ? 33.771  0.387   9.902   1.00 41.49  ? 328 HOH B O   1 
HETATM 3764 O O   . HOH D 2 .   ? 14.472  -7.203  -4.581  1.00 39.22  ? 329 HOH B O   1 
HETATM 3765 O O   . HOH D 2 .   ? 20.657  -2.954  -6.155  1.00 35.88  ? 330 HOH B O   1 
HETATM 3766 O O   . HOH D 2 .   ? 31.537  -0.198  12.928  1.00 36.82  ? 331 HOH B O   1 
HETATM 3767 O O   . HOH D 2 .   ? 16.035  12.144  0.345   1.00 43.75  ? 332 HOH B O   1 
HETATM 3768 O O   . HOH D 2 .   ? 38.343  4.897   19.709  1.00 43.68  ? 333 HOH B O   1 
HETATM 3769 O O   . HOH D 2 .   ? 15.295  -4.681  26.447  1.00 47.59  ? 334 HOH B O   1 
HETATM 3770 O O   . HOH D 2 .   ? 27.169  -2.073  19.069  1.00 36.38  ? 335 HOH B O   1 
HETATM 3771 O O   . HOH D 2 .   ? 30.592  -24.075 20.863  1.00 61.35  ? 336 HOH B O   1 
HETATM 3772 O O   . HOH D 2 .   ? 34.622  2.928   -5.722  1.00 39.81  ? 337 HOH B O   1 
HETATM 3773 O O   . HOH D 2 .   ? 29.668  -6.364  -13.611 1.00 50.88  ? 338 HOH B O   1 
HETATM 3774 O O   . HOH D 2 .   ? 23.990  -0.370  -7.320  1.00 34.67  ? 339 HOH B O   1 
HETATM 3775 O O   . HOH D 2 .   ? 35.902  -19.629 2.790   1.00 38.71  ? 340 HOH B O   1 
HETATM 3776 O O   . HOH D 2 .   ? 34.527  7.008   4.836   1.00 51.97  ? 341 HOH B O   1 
HETATM 3777 O O   . HOH D 2 .   ? 25.167  -11.544 -3.638  1.00 34.58  ? 342 HOH B O   1 
HETATM 3778 O O   . HOH D 2 .   ? 35.002  -18.962 9.831   1.00 42.03  ? 343 HOH B O   1 
HETATM 3779 O O   . HOH D 2 .   ? 19.717  0.812   31.822  1.00 44.19  ? 344 HOH B O   1 
HETATM 3780 O O   . HOH D 2 .   ? 27.140  4.704   -16.047 1.00 52.44  ? 345 HOH B O   1 
HETATM 3781 O O   . HOH D 2 .   ? 27.108  -4.492  17.166  1.00 31.87  ? 346 HOH B O   1 
HETATM 3782 O O   . HOH D 2 .   ? 31.718  9.346   -9.104  1.00 44.76  ? 347 HOH B O   1 
HETATM 3783 O O   . HOH D 2 .   ? 20.492  7.023   21.905  1.00 41.52  ? 348 HOH B O   1 
HETATM 3784 O O   . HOH D 2 .   ? 29.303  9.322   -9.718  1.00 42.50  ? 349 HOH B O   1 
HETATM 3785 O O   . HOH D 2 .   ? 18.815  -2.360  19.064  1.00 37.70  ? 350 HOH B O   1 
HETATM 3786 O O   . HOH D 2 .   ? 24.750  -19.000 9.160   1.00 52.92  ? 351 HOH B O   1 
HETATM 3787 O O   . HOH D 2 .   ? 32.420  -1.819  9.499   1.00 37.39  ? 352 HOH B O   1 
HETATM 3788 O O   . HOH D 2 .   ? 22.623  -2.330  7.998   1.00 39.37  ? 353 HOH B O   1 
HETATM 3789 O O   . HOH D 2 .   ? 16.351  -3.441  20.650  1.00 36.97  ? 354 HOH B O   1 
HETATM 3790 O O   . HOH D 2 .   ? 31.019  6.598   24.728  1.00 43.35  ? 355 HOH B O   1 
HETATM 3791 O O   . HOH D 2 .   ? 19.043  0.257   15.178  1.00 42.98  ? 356 HOH B O   1 
HETATM 3792 O O   . HOH D 2 .   ? 25.776  -5.867  6.672   1.00 38.91  ? 357 HOH B O   1 
HETATM 3793 O O   . HOH D 2 .   ? 36.604  -15.432 -5.754  1.00 51.19  ? 358 HOH B O   1 
HETATM 3794 O O   . HOH D 2 .   ? 23.653  -7.458  23.196  1.00 56.07  ? 359 HOH B O   1 
HETATM 3795 O O   . HOH D 2 .   ? 34.248  3.083   -8.662  1.00 42.16  ? 360 HOH B O   1 
HETATM 3796 O O   . HOH D 2 .   ? 29.147  -10.289 27.557  1.00 40.10  ? 361 HOH B O   1 
HETATM 3797 O O   . HOH D 2 .   ? 23.576  -8.325  13.303  1.00 41.72  ? 362 HOH B O   1 
HETATM 3798 O O   . HOH D 2 .   ? 30.038  -12.513 23.925  1.00 44.92  ? 363 HOH B O   1 
HETATM 3799 O O   . HOH D 2 .   ? 39.978  -14.184 -3.264  1.00 53.38  ? 364 HOH B O   1 
HETATM 3800 O O   . HOH D 2 .   ? 30.348  -0.245  -19.113 1.00 52.15  ? 365 HOH B O   1 
HETATM 3801 O O   . HOH D 2 .   ? 40.696  2.495   13.796  1.00 54.33  ? 366 HOH B O   1 
HETATM 3802 O O   . HOH D 2 .   ? 7.380   7.594   -7.122  1.00 60.29  ? 367 HOH B O   1 
HETATM 3803 O O   . HOH D 2 .   ? 39.450  -14.979 -5.617  1.00 51.13  ? 368 HOH B O   1 
HETATM 3804 O O   . HOH D 2 .   ? 18.274  5.763   21.480  1.00 49.45  ? 369 HOH B O   1 
HETATM 3805 O O   . HOH D 2 .   ? 34.268  -21.429 8.714   1.00 39.69  ? 370 HOH B O   1 
HETATM 3806 O O   . HOH D 2 .   ? 40.471  6.251   19.100  1.00 46.23  ? 371 HOH B O   1 
HETATM 3807 O O   . HOH D 2 .   ? 23.022  -20.314 10.415  1.00 52.43  ? 372 HOH B O   1 
# 
